data_8R6E
# 
_entry.id   8R6E 
# 
_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   8R6E         pdb_00008r6e 10.2210/pdb8r6e/pdb 
WWPDB D_1292134556 ?            ?                   
# 
_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       2024-12-04 
# 
_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                        8R6E 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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                 5 
_pdbx_contact_author.email              reuvenw@ekmd.huji.ac.il 
_pdbx_contact_author.name_first         Reuven 
_pdbx_contact_author.name_last          Wiener 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4219-550X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fahoum, J.'    1 0000-0002-0631-6503 
'Wiener, R.'    2 0000-0002-4219-550X 
'Rouvinski, A.' 3 0000-0002-9917-7564 
'Isupov, M.N.'  4 0000-0001-6842-4289 
# 
_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                     'SARS-CoV-2 Nucleocapsid dimerization domain' 
_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 'Fahoum, J.'    1 0000-0002-0631-6503 
primary 'Wiener, R.'    2 0000-0002-4219-550X 
primary 'Rouvinski, A.' 3 0000-0002-9917-7564 
primary 'Isupov, M.N.'  4 0000-0001-6842-4289 
# 
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 Nucleoprotein           13259.933 2   ? ? ? ? 
2 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120   2   ? ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL          62.068    5   ? ? ? ? 
4 non-polymer syn GLYCEROL                92.094    1   ? ? ? ? 
5 non-polymer syn 'SODIUM ION'            22.990    3   ? ? ? ? 
6 water       nat water                   18.015    165 ? ? ? ? 
# 
_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       
;TKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTP
SGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTP
SGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DI(HYDROXYETHYL)ETHER' PEG 
3 1,2-ETHANEDIOL          EDO 
4 GLYCEROL                GOL 
5 'SODIUM ION'            NA  
6 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   LYS n 
1 3   LYS n 
1 4   SER n 
1 5   ALA n 
1 6   ALA n 
1 7   GLU n 
1 8   ALA n 
1 9   SER n 
1 10  LYS n 
1 11  LYS n 
1 12  PRO n 
1 13  ARG n 
1 14  GLN n 
1 15  LYS n 
1 16  ARG n 
1 17  THR n 
1 18  ALA n 
1 19  THR n 
1 20  LYS n 
1 21  ALA n 
1 22  TYR n 
1 23  ASN n 
1 24  VAL n 
1 25  THR n 
1 26  GLN n 
1 27  ALA n 
1 28  PHE n 
1 29  GLY n 
1 30  ARG n 
1 31  ARG n 
1 32  GLY n 
1 33  PRO n 
1 34  GLU n 
1 35  GLN n 
1 36  THR n 
1 37  GLN n 
1 38  GLY n 
1 39  ASN n 
1 40  PHE n 
1 41  GLY n 
1 42  ASP n 
1 43  GLN n 
1 44  GLU n 
1 45  LEU n 
1 46  ILE n 
1 47  ARG n 
1 48  GLN n 
1 49  GLY n 
1 50  THR n 
1 51  ASP n 
1 52  TYR n 
1 53  LYS n 
1 54  HIS n 
1 55  TRP n 
1 56  PRO n 
1 57  GLN n 
1 58  ILE n 
1 59  ALA n 
1 60  GLN n 
1 61  PHE n 
1 62  ALA n 
1 63  PRO n 
1 64  SER n 
1 65  ALA n 
1 66  SER n 
1 67  ALA n 
1 68  PHE n 
1 69  PHE n 
1 70  GLY n 
1 71  MET n 
1 72  SER n 
1 73  ARG n 
1 74  ILE n 
1 75  GLY n 
1 76  MET n 
1 77  GLU n 
1 78  VAL n 
1 79  THR n 
1 80  PRO n 
1 81  SER n 
1 82  GLY n 
1 83  THR n 
1 84  TRP n 
1 85  LEU n 
1 86  THR n 
1 87  TYR n 
1 88  THR n 
1 89  GLY n 
1 90  ALA n 
1 91  ILE n 
1 92  LYS n 
1 93  LEU n 
1 94  ASP n 
1 95  ASP n 
1 96  LYS n 
1 97  ASP n 
1 98  PRO n 
1 99  ASN n 
1 100 PHE n 
1 101 LYS n 
1 102 ASP n 
1 103 GLN n 
1 104 VAL n 
1 105 ILE n 
1 106 LEU n 
1 107 LEU n 
1 108 ASN n 
1 109 LYS n 
1 110 HIS n 
1 111 ILE n 
1 112 ASP n 
1 113 ALA n 
1 114 TYR n 
1 115 LYS n 
1 116 THR n 
1 117 PHE n 
1 118 PRO 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                   118 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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 
EDO non-polymer         . 1,2-ETHANEDIOL          'ETHYLENE GLYCOL'               'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE               ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'         ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                 ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE               ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                   ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ?                               'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'            ?                               'Na 1'           22.990  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                               'C4 H10 O3'      106.120 
PHE 'L-peptide linking' y PHENYLALANINE           ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                 ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE               ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   THR 1   1   1   THR THR A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   SER 4   4   4   SER SER A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   SER 9   9   9   SER SER A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  ARG 13  13  13  ARG ARG A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  THR 17  17  17  THR THR A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  TYR 22  22  22  TYR TYR A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  GLN 26  26  26  GLN GLN A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  ASN 39  39  39  ASN ASN A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  HIS 54  54  54  HIS HIS A . n 
A 1 55  TRP 55  55  55  TRP TRP A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  PHE 69  69  69  PHE PHE A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  MET 71  71  71  MET MET A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  TRP 84  84  84  TRP TRP A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
B 1 1   THR 1   1   ?   ?   ?   B . n 
B 1 2   LYS 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   SER 4   4   4   SER SER B . n 
B 1 5   ALA 5   5   5   ALA ALA B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   GLU 7   7   7   GLU GLU B . n 
B 1 8   ALA 8   8   8   ALA ALA B . n 
B 1 9   SER 9   9   9   SER SER B . n 
B 1 10  LYS 10  10  10  LYS LYS B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  PRO 12  12  12  PRO PRO B . n 
B 1 13  ARG 13  13  13  ARG ARG B . n 
B 1 14  GLN 14  14  14  GLN GLN B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  ARG 16  16  16  ARG ARG B . n 
B 1 17  THR 17  17  17  THR THR B . n 
B 1 18  ALA 18  18  18  ALA ALA B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  LYS 20  20  20  LYS LYS B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  TYR 22  22  22  TYR TYR B . n 
B 1 23  ASN 23  23  23  ASN ASN B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  GLN 26  26  26  GLN GLN B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  PHE 28  28  28  PHE PHE B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  ARG 30  30  30  ARG ARG B . n 
B 1 31  ARG 31  31  31  ARG ARG B . n 
B 1 32  GLY 32  32  32  GLY GLY B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  GLU 34  34  34  GLU GLU B . n 
B 1 35  GLN 35  35  35  GLN GLN B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  GLN 37  37  37  GLN GLN B . n 
B 1 38  GLY 38  38  38  GLY GLY B . n 
B 1 39  ASN 39  39  39  ASN ASN B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  ASP 42  42  42  ASP ASP B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  GLU 44  44  44  GLU GLU B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  GLN 48  48  48  GLN GLN B . n 
B 1 49  GLY 49  49  49  GLY GLY B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  ASP 51  51  51  ASP ASP B . n 
B 1 52  TYR 52  52  52  TYR TYR B . n 
B 1 53  LYS 53  53  53  LYS LYS B . n 
B 1 54  HIS 54  54  54  HIS HIS B . n 
B 1 55  TRP 55  55  55  TRP TRP B . n 
B 1 56  PRO 56  56  56  PRO PRO B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  GLN 60  60  60  GLN GLN B . n 
B 1 61  PHE 61  61  61  PHE PHE B . n 
B 1 62  ALA 62  62  62  ALA ALA B . n 
B 1 63  PRO 63  63  63  PRO PRO B . n 
B 1 64  SER 64  64  64  SER SER B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  SER 66  66  66  SER SER B . n 
B 1 67  ALA 67  67  67  ALA ALA B . n 
B 1 68  PHE 68  68  68  PHE PHE B . n 
B 1 69  PHE 69  69  69  PHE PHE B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  MET 71  71  71  MET MET B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  MET 76  76  76  MET MET B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  THR 79  79  79  THR THR B . n 
B 1 80  PRO 80  80  80  PRO PRO B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  THR 83  83  83  THR THR B . n 
B 1 84  TRP 84  84  84  TRP TRP B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  TYR 87  87  87  TYR TYR B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  GLY 89  89  89  GLY GLY B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  LYS 92  92  92  LYS LYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  ASP 94  94  94  ASP ASP B . n 
B 1 95  ASP 95  95  95  ASP ASP B . n 
B 1 96  LYS 96  96  96  LYS LYS B . n 
B 1 97  ASP 97  97  97  ASP ASP B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 PHE 100 100 100 PHE PHE B . n 
B 1 101 LYS 101 101 101 LYS LYS B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 GLN 103 103 103 GLN GLN B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 ASN 108 108 108 ASN ASN B . n 
B 1 109 LYS 109 109 109 LYS LYS B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 ILE 111 111 111 ILE ILE B . n 
B 1 112 ASP 112 112 112 ASP ASP B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 LYS 115 115 115 LYS LYS B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 PHE 117 117 117 PHE PHE B . n 
B 1 118 PRO 118 118 118 PRO PRO B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 PEG 1  201 201 PEG PEG A . 
D 2 PEG 1  202 202 PEG PEG A . 
E 3 EDO 1  203 203 EDO EDO A . 
F 4 GOL 1  204 149 GOL GOL A . 
G 5 NA  1  205 3   NA  NA  A . 
H 5 NA  1  206 4   NA  NA  A . 
I 3 EDO 1  201 201 EDO EDO B . 
J 3 EDO 1  202 204 EDO EDO B . 
K 3 EDO 1  203 205 EDO EDO B . 
L 3 EDO 1  204 206 EDO EDO B . 
M 5 NA  1  205 1   NA  NA  B . 
N 6 HOH 1  301 3   HOH HOH A . 
N 6 HOH 2  302 4   HOH HOH A . 
N 6 HOH 3  303 109 HOH HOH A . 
N 6 HOH 4  304 110 HOH HOH A . 
N 6 HOH 5  305 142 HOH HOH A . 
N 6 HOH 6  306 71  HOH HOH A . 
N 6 HOH 7  307 92  HOH HOH A . 
N 6 HOH 8  308 63  HOH HOH A . 
N 6 HOH 9  309 10  HOH HOH A . 
N 6 HOH 10 310 37  HOH HOH A . 
N 6 HOH 11 311 108 HOH HOH A . 
N 6 HOH 12 312 99  HOH HOH A . 
N 6 HOH 13 313 16  HOH HOH A . 
N 6 HOH 14 314 107 HOH HOH A . 
N 6 HOH 15 315 84  HOH HOH A . 
N 6 HOH 16 316 146 HOH HOH A . 
N 6 HOH 17 317 101 HOH HOH A . 
N 6 HOH 18 318 64  HOH HOH A . 
N 6 HOH 19 319 38  HOH HOH A . 
N 6 HOH 20 320 61  HOH HOH A . 
N 6 HOH 21 321 90  HOH HOH A . 
N 6 HOH 22 322 34  HOH HOH A . 
N 6 HOH 23 323 81  HOH HOH A . 
N 6 HOH 24 324 77  HOH HOH A . 
N 6 HOH 25 325 29  HOH HOH A . 
N 6 HOH 26 326 148 HOH HOH A . 
N 6 HOH 27 327 59  HOH HOH A . 
N 6 HOH 28 328 116 HOH HOH A . 
N 6 HOH 29 329 19  HOH HOH A . 
N 6 HOH 30 330 56  HOH HOH A . 
N 6 HOH 31 331 31  HOH HOH A . 
N 6 HOH 32 332 32  HOH HOH A . 
N 6 HOH 33 333 70  HOH HOH A . 
N 6 HOH 34 334 117 HOH HOH A . 
N 6 HOH 35 335 121 HOH HOH A . 
N 6 HOH 36 336 11  HOH HOH A . 
N 6 HOH 37 337 35  HOH HOH A . 
N 6 HOH 38 338 9   HOH HOH A . 
N 6 HOH 39 339 20  HOH HOH A . 
N 6 HOH 40 340 104 HOH HOH A . 
N 6 HOH 41 341 22  HOH HOH A . 
N 6 HOH 42 342 97  HOH HOH A . 
N 6 HOH 43 343 96  HOH HOH A . 
N 6 HOH 44 344 143 HOH HOH A . 
N 6 HOH 45 345 67  HOH HOH A . 
N 6 HOH 46 346 28  HOH HOH A . 
N 6 HOH 47 347 60  HOH HOH A . 
N 6 HOH 48 348 43  HOH HOH A . 
N 6 HOH 49 349 12  HOH HOH A . 
N 6 HOH 50 350 18  HOH HOH A . 
N 6 HOH 51 351 54  HOH HOH A . 
N 6 HOH 52 352 5   HOH HOH A . 
N 6 HOH 53 353 21  HOH HOH A . 
N 6 HOH 54 354 49  HOH HOH A . 
N 6 HOH 55 355 5   HOH HOH A . 
N 6 HOH 56 356 18  HOH HOH A . 
N 6 HOH 57 357 39  HOH HOH A . 
N 6 HOH 58 358 48  HOH HOH A . 
N 6 HOH 59 359 15  HOH HOH A . 
N 6 HOH 60 360 118 HOH HOH A . 
N 6 HOH 61 361 1   HOH HOH A . 
N 6 HOH 62 362 6   HOH HOH A . 
N 6 HOH 63 363 95  HOH HOH A . 
N 6 HOH 64 364 40  HOH HOH A . 
N 6 HOH 65 365 33  HOH HOH A . 
N 6 HOH 66 366 25  HOH HOH A . 
N 6 HOH 67 367 51  HOH HOH A . 
N 6 HOH 68 368 76  HOH HOH A . 
N 6 HOH 69 369 105 HOH HOH A . 
N 6 HOH 70 370 102 HOH HOH A . 
N 6 HOH 71 371 30  HOH HOH A . 
N 6 HOH 72 372 91  HOH HOH A . 
N 6 HOH 73 373 8   HOH HOH A . 
N 6 HOH 74 374 111 HOH HOH A . 
N 6 HOH 75 375 58  HOH HOH A . 
N 6 HOH 76 376 68  HOH HOH A . 
N 6 HOH 77 377 6   HOH HOH A . 
N 6 HOH 78 378 75  HOH HOH A . 
N 6 HOH 79 379 106 HOH HOH A . 
N 6 HOH 80 380 98  HOH HOH A . 
N 6 HOH 81 381 115 HOH HOH A . 
N 6 HOH 82 382 66  HOH HOH A . 
N 6 HOH 83 383 2   HOH HOH A . 
N 6 HOH 84 384 123 HOH HOH A . 
N 6 HOH 85 385 100 HOH HOH A . 
N 6 HOH 86 386 145 HOH HOH A . 
N 6 HOH 87 387 87  HOH HOH A . 
N 6 HOH 88 388 83  HOH HOH A . 
N 6 HOH 89 389 85  HOH HOH A . 
N 6 HOH 90 390 1   HOH HOH A . 
N 6 HOH 91 391 8   HOH HOH A . 
N 6 HOH 92 392 144 HOH HOH A . 
N 6 HOH 93 393 147 HOH HOH A . 
N 6 HOH 94 394 82  HOH HOH A . 
O 6 HOH 1  301 136 HOH HOH B . 
O 6 HOH 2  302 137 HOH HOH B . 
O 6 HOH 3  303 42  HOH HOH B . 
O 6 HOH 4  304 10  HOH HOH B . 
O 6 HOH 5  305 103 HOH HOH B . 
O 6 HOH 6  306 14  HOH HOH B . 
O 6 HOH 7  307 125 HOH HOH B . 
O 6 HOH 8  308 7   HOH HOH B . 
O 6 HOH 9  309 139 HOH HOH B . 
O 6 HOH 10 310 126 HOH HOH B . 
O 6 HOH 11 311 3   HOH HOH B . 
O 6 HOH 12 312 112 HOH HOH B . 
O 6 HOH 13 313 79  HOH HOH B . 
O 6 HOH 14 314 93  HOH HOH B . 
O 6 HOH 15 315 134 HOH HOH B . 
O 6 HOH 16 316 78  HOH HOH B . 
O 6 HOH 17 317 120 HOH HOH B . 
O 6 HOH 18 318 13  HOH HOH B . 
O 6 HOH 19 319 141 HOH HOH B . 
O 6 HOH 20 320 55  HOH HOH B . 
O 6 HOH 21 321 14  HOH HOH B . 
O 6 HOH 22 322 69  HOH HOH B . 
O 6 HOH 23 323 9   HOH HOH B . 
O 6 HOH 24 324 135 HOH HOH B . 
O 6 HOH 25 325 22  HOH HOH B . 
O 6 HOH 26 326 41  HOH HOH B . 
O 6 HOH 27 327 7   HOH HOH B . 
O 6 HOH 28 328 128 HOH HOH B . 
O 6 HOH 29 329 47  HOH HOH B . 
O 6 HOH 30 330 86  HOH HOH B . 
O 6 HOH 31 331 65  HOH HOH B . 
O 6 HOH 32 332 4   HOH HOH B . 
O 6 HOH 33 333 50  HOH HOH B . 
O 6 HOH 34 334 15  HOH HOH B . 
O 6 HOH 35 335 17  HOH HOH B . 
O 6 HOH 36 336 12  HOH HOH B . 
O 6 HOH 37 337 80  HOH HOH B . 
O 6 HOH 38 338 26  HOH HOH B . 
O 6 HOH 39 339 124 HOH HOH B . 
O 6 HOH 40 340 94  HOH HOH B . 
O 6 HOH 41 341 140 HOH HOH B . 
O 6 HOH 42 342 138 HOH HOH B . 
O 6 HOH 43 343 36  HOH HOH B . 
O 6 HOH 44 344 131 HOH HOH B . 
O 6 HOH 45 345 24  HOH HOH B . 
O 6 HOH 46 346 23  HOH HOH B . 
O 6 HOH 47 347 13  HOH HOH B . 
O 6 HOH 48 348 113 HOH HOH B . 
O 6 HOH 49 349 62  HOH HOH B . 
O 6 HOH 50 350 122 HOH HOH B . 
O 6 HOH 51 351 44  HOH HOH B . 
O 6 HOH 52 352 57  HOH HOH B . 
O 6 HOH 53 353 27  HOH HOH B . 
O 6 HOH 54 354 45  HOH HOH B . 
O 6 HOH 55 355 17  HOH HOH B . 
O 6 HOH 56 356 46  HOH HOH B . 
O 6 HOH 57 357 52  HOH HOH B . 
O 6 HOH 58 358 16  HOH HOH B . 
O 6 HOH 59 359 53  HOH HOH B . 
O 6 HOH 60 360 20  HOH HOH B . 
O 6 HOH 61 361 74  HOH HOH B . 
O 6 HOH 62 362 19  HOH HOH B . 
O 6 HOH 63 363 130 HOH HOH B . 
O 6 HOH 64 364 89  HOH HOH B . 
O 6 HOH 65 365 73  HOH HOH B . 
O 6 HOH 66 366 114 HOH HOH B . 
O 6 HOH 67 367 11  HOH HOH B . 
O 6 HOH 68 368 88  HOH HOH B . 
O 6 HOH 69 369 129 HOH HOH B . 
O 6 HOH 70 370 127 HOH HOH B . 
O 6 HOH 71 371 119 HOH HOH B . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MoRDa  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8R6E 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     43.620 
_cell.length_a_esd                 ? 
_cell.length_b                     47.372 
_cell.length_b_esd                 ? 
_cell.length_c                     134.625 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8R6E 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_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                   8R6E 
_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             2.62 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.10 
_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    '0.2M sodium chloride, 0.1M sodium/potassium phosphate 6.5 and 25% PEG1000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            297 
# 
_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 PILATUS3 X 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-08 
_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   0.873128 
_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                        'ESRF BEAMLINE ID23-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.873128 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8R6E 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.53 
_reflns.d_resolution_low                               47.37 
_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                                     43189 
_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                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.53 
_reflns_shell.d_res_low                                     1.55 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1968 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.291 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -3.94 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            5.88 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.94 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               38.809 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.952 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 8R6E 
_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                            1.53 
_refine.ls_d_res_low                             44.73 
_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                     40897 
_refine.ls_number_reflns_R_free                  2104 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.22671 
_refine.ls_R_factor_R_free                       0.26653 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.22475 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.090 
_refine.pdbx_overall_ESU_R_Free                  0.095 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             5.809 
_refine.overall_SU_ML                            0.164 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.53 
_refine_hist.d_res_low                        44.73 
_refine_hist.number_atoms_solvent             165 
_refine_hist.number_atoms_total               2064 
_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        1856 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_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' ? 0.008  0.012  2011 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1937 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.713  1.847  2706 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.586  1.803  4472 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.972  5.000  252  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 7.817  5.000  16   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.196 10.000 356  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.082  0.200  276  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  2402 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  498  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.414  3.509  954  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.403  3.508  954  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.821  6.266  1194 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.825  6.265  1195 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.406  4.016  1057 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.404  4.017  1058 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.623  7.070  1503 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.603  37.12  2334 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.602  37.12  2334 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.530 
_refine_ls_shell.d_res_low                        1.570 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             159 
_refine_ls_shell.number_reflns_R_work             2973 
_refine_ls_shell.percent_reflns_obs               99.87 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.490 
_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   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.489 
# 
_struct.entry_id                     8R6E 
_struct.title                        'SARS-CoV-2 Nucleocapsid dimerization domain' 
_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        8R6E 
_struct_keywords.text            'VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 5 ? 
N N N 6 ? 
O N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A7T7WQ79_SARS2 
_struct_ref.pdbx_db_accession          A0A7T7WQ79 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTP
SGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFP
;
_struct_ref.pdbx_align_begin           247 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8R6E A 1 ? 118 ? A0A7T7WQ79 247 ? 364 ? 1 118 
2 1 8R6E B 1 ? 118 ? A0A7T7WQ79 247 ? 364 ? 1 118 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7140  ? 
1 MORE         -39   ? 
1 'SSA (A^2)'  12490 ? 
# 
_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,G,H,I,J,K,L,M,N,O 
# 
_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 4   ? SER A 9   ? SER A 4   SER A 9   1 ? 6  
HELX_P HELX_P2  AA2 LYS A 10  ? LYS A 11  ? LYS A 10  LYS A 11  5 ? 2  
HELX_P HELX_P3  AA3 PRO A 12  ? ARG A 16  ? PRO A 12  ARG A 16  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 23  ? GLY A 29  ? ASN A 23  GLY A 29  1 ? 7  
HELX_P HELX_P5  AA5 ASP A 42  ? GLY A 49  ? ASP A 42  GLY A 49  1 ? 8  
HELX_P HELX_P6  AA6 THR A 50  ? TYR A 52  ? THR A 50  TYR A 52  5 ? 3  
HELX_P HELX_P7  AA7 HIS A 54  ? GLN A 60  ? HIS A 54  GLN A 60  1 ? 7  
HELX_P HELX_P8  AA8 SER A 64  ? SER A 72  ? SER A 64  SER A 72  1 ? 9  
HELX_P HELX_P9  AA9 ASN A 99  ? ILE A 111 ? ASN A 99  ILE A 111 1 ? 13 
HELX_P HELX_P10 AB1 ASP A 112 ? PHE A 117 ? ASP A 112 PHE A 117 5 ? 6  
HELX_P HELX_P11 AB2 SER B 4   ? SER B 9   ? SER B 4   SER B 9   1 ? 6  
HELX_P HELX_P12 AB3 LYS B 10  ? LYS B 11  ? LYS B 10  LYS B 11  5 ? 2  
HELX_P HELX_P13 AB4 PRO B 12  ? ARG B 16  ? PRO B 12  ARG B 16  5 ? 5  
HELX_P HELX_P14 AB5 ASN B 23  ? GLY B 29  ? ASN B 23  GLY B 29  1 ? 7  
HELX_P HELX_P15 AB6 ASP B 42  ? GLY B 49  ? ASP B 42  GLY B 49  1 ? 8  
HELX_P HELX_P16 AB7 THR B 50  ? TYR B 52  ? THR B 50  TYR B 52  5 ? 3  
HELX_P HELX_P17 AB8 HIS B 54  ? GLN B 60  ? HIS B 54  GLN B 60  1 ? 7  
HELX_P HELX_P18 AB9 SER B 64  ? SER B 72  ? SER B 64  SER B 72  1 ? 9  
HELX_P HELX_P19 AC1 ASN B 99  ? ILE B 111 ? ASN B 99  ILE B 111 1 ? 13 
HELX_P HELX_P20 AC2 ASP B 112 ? PHE B 117 ? ASP B 112 PHE B 117 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A GLU 44  OE2 ? ? ? 1_555 G NA . NA ? ? A GLU 44  A NA 205 1_555 ? ? ? ? ? ? ? 2.981 ? ? 
metalc2 metalc ? ? A GLN 48  OE1 ? ? ? 1_555 G NA . NA ? ? A GLN 48  A NA 205 1_555 ? ? ? ? ? ? ? 2.231 ? ? 
metalc3 metalc ? ? A ASN 99  OD1 ? ? ? 1_555 H NA . NA ? ? A ASN 99  A NA 206 1_555 ? ? ? ? ? ? ? 2.650 ? ? 
metalc4 metalc ? ? A ASP 102 OD2 ? ? ? 1_555 H NA . NA ? ? A ASP 102 A NA 206 1_555 ? ? ? ? ? ? ? 2.219 ? ? 
metalc5 metalc ? ? B THR 36  O   ? ? ? 1_555 M NA . NA ? ? B THR 36  B NA 205 1_555 ? ? ? ? ? ? ? 2.797 ? ? 
metalc6 metalc ? ? B THR 36  OG1 ? ? ? 1_555 M NA . NA ? ? B THR 36  B NA 205 1_555 ? ? ? ? ? ? ? 2.209 ? ? 
metalc7 metalc ? ? B THR 116 O   ? ? ? 1_555 M NA . NA ? ? B THR 116 B NA 205 4_455 ? ? ? ? ? ? ? 3.074 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OE2 ? A GLU 44 ? A GLU 44 ? 1_555 NA ? G NA . ? A NA 205 ? 1_555 OE1 ? A GLN 48  ? A GLN 48  ? 1_555 98.6  ? 
2 OD1 ? A ASN 99 ? A ASN 99 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 OD2 ? A ASP 102 ? A ASP 102 ? 1_555 122.7 ? 
3 O   ? B THR 36 ? B THR 36 ? 1_555 NA ? M NA . ? B NA 205 ? 1_555 OG1 ? B THR 36  ? B THR 36  ? 1_555 77.4  ? 
4 O   ? B THR 36 ? B THR 36 ? 1_555 NA ? M NA . ? B NA 205 ? 1_555 O   ? B THR 116 ? B THR 116 ? 1_555 38.9  ? 
5 OG1 ? B THR 36 ? B THR 36 ? 1_555 NA ? M NA . ? B NA 205 ? 1_555 O   ? B THR 116 ? B THR 116 ? 1_555 87.8  ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   4 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 73 ? THR A 79 ? ARG A 73 THR A 79 
AA1 2 GLY A 82 ? LYS A 92 ? GLY A 82 LYS A 92 
AA1 3 GLY B 82 ? LYS B 92 ? GLY B 82 LYS B 92 
AA1 4 ARG B 73 ? THR B 79 ? ARG B 73 THR B 79 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 73 ? N ARG A 73 O THR A 88 ? O THR A 88 
AA1 2 3 N ILE A 91 ? N ILE A 91 O LEU B 85 ? O LEU B 85 
AA1 3 4 O THR B 88 ? O THR B 88 N ARG B 73 ? N ARG B 73 
# 
_pdbx_entry_details.entry_id                   8R6E 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    TYR 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     22 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -152.33 
_pdbx_validate_torsion.psi             89.74 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     47 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.122 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 B THR 1 ? B THR 1 
2 1 Y 1 B LYS 2 ? B LYS 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  
EDO C1   C  N N 74  
EDO O1   O  N N 75  
EDO C2   C  N N 76  
EDO O2   O  N N 77  
EDO H11  H  N N 78  
EDO H12  H  N N 79  
EDO HO1  H  N N 80  
EDO H21  H  N N 81  
EDO H22  H  N N 82  
EDO HO2  H  N N 83  
GLN N    N  N N 84  
GLN CA   C  N S 85  
GLN C    C  N N 86  
GLN O    O  N N 87  
GLN CB   C  N N 88  
GLN CG   C  N N 89  
GLN CD   C  N N 90  
GLN OE1  O  N N 91  
GLN NE2  N  N N 92  
GLN OXT  O  N N 93  
GLN H    H  N N 94  
GLN H2   H  N N 95  
GLN HA   H  N N 96  
GLN HB2  H  N N 97  
GLN HB3  H  N N 98  
GLN HG2  H  N N 99  
GLN HG3  H  N N 100 
GLN HE21 H  N N 101 
GLN HE22 H  N N 102 
GLN HXT  H  N N 103 
GLU N    N  N N 104 
GLU CA   C  N S 105 
GLU C    C  N N 106 
GLU O    O  N N 107 
GLU CB   C  N N 108 
GLU CG   C  N N 109 
GLU CD   C  N N 110 
GLU OE1  O  N N 111 
GLU OE2  O  N N 112 
GLU OXT  O  N N 113 
GLU H    H  N N 114 
GLU H2   H  N N 115 
GLU HA   H  N N 116 
GLU HB2  H  N N 117 
GLU HB3  H  N N 118 
GLU HG2  H  N N 119 
GLU HG3  H  N N 120 
GLU HE2  H  N N 121 
GLU HXT  H  N N 122 
GLY N    N  N N 123 
GLY CA   C  N N 124 
GLY C    C  N N 125 
GLY O    O  N N 126 
GLY OXT  O  N N 127 
GLY H    H  N N 128 
GLY H2   H  N N 129 
GLY HA2  H  N N 130 
GLY HA3  H  N N 131 
GLY HXT  H  N N 132 
GOL C1   C  N N 133 
GOL O1   O  N N 134 
GOL C2   C  N N 135 
GOL O2   O  N N 136 
GOL C3   C  N N 137 
GOL O3   O  N N 138 
GOL H11  H  N N 139 
GOL H12  H  N N 140 
GOL HO1  H  N N 141 
GOL H2   H  N N 142 
GOL HO2  H  N N 143 
GOL H31  H  N N 144 
GOL H32  H  N N 145 
GOL HO3  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
NA  NA   NA N N 260 
PEG C1   C  N N 261 
PEG O1   O  N N 262 
PEG C2   C  N N 263 
PEG O2   O  N N 264 
PEG C3   C  N N 265 
PEG C4   C  N N 266 
PEG O4   O  N N 267 
PEG H11  H  N N 268 
PEG H12  H  N N 269 
PEG HO1  H  N N 270 
PEG H21  H  N N 271 
PEG H22  H  N N 272 
PEG H31  H  N N 273 
PEG H32  H  N N 274 
PEG H41  H  N N 275 
PEG H42  H  N N 276 
PEG HO4  H  N N 277 
PHE N    N  N N 278 
PHE CA   C  N S 279 
PHE C    C  N N 280 
PHE O    O  N N 281 
PHE CB   C  N N 282 
PHE CG   C  Y N 283 
PHE CD1  C  Y N 284 
PHE CD2  C  Y N 285 
PHE CE1  C  Y N 286 
PHE CE2  C  Y N 287 
PHE CZ   C  Y N 288 
PHE OXT  O  N N 289 
PHE H    H  N N 290 
PHE H2   H  N N 291 
PHE HA   H  N N 292 
PHE HB2  H  N N 293 
PHE HB3  H  N N 294 
PHE HD1  H  N N 295 
PHE HD2  H  N N 296 
PHE HE1  H  N N 297 
PHE HE2  H  N N 298 
PHE HZ   H  N N 299 
PHE HXT  H  N N 300 
PRO N    N  N N 301 
PRO CA   C  N S 302 
PRO C    C  N N 303 
PRO O    O  N N 304 
PRO CB   C  N N 305 
PRO CG   C  N N 306 
PRO CD   C  N N 307 
PRO OXT  O  N N 308 
PRO H    H  N N 309 
PRO HA   H  N N 310 
PRO HB2  H  N N 311 
PRO HB3  H  N N 312 
PRO HG2  H  N N 313 
PRO HG3  H  N N 314 
PRO HD2  H  N N 315 
PRO HD3  H  N N 316 
PRO HXT  H  N N 317 
SER N    N  N N 318 
SER CA   C  N S 319 
SER C    C  N N 320 
SER O    O  N N 321 
SER CB   C  N N 322 
SER OG   O  N N 323 
SER OXT  O  N N 324 
SER H    H  N N 325 
SER H2   H  N N 326 
SER HA   H  N N 327 
SER HB2  H  N N 328 
SER HB3  H  N N 329 
SER HG   H  N N 330 
SER HXT  H  N N 331 
THR N    N  N N 332 
THR CA   C  N S 333 
THR C    C  N N 334 
THR O    O  N N 335 
THR CB   C  N R 336 
THR OG1  O  N N 337 
THR CG2  C  N N 338 
THR OXT  O  N N 339 
THR H    H  N N 340 
THR H2   H  N N 341 
THR HA   H  N N 342 
THR HB   H  N N 343 
THR HG1  H  N N 344 
THR HG21 H  N N 345 
THR HG22 H  N N 346 
THR HG23 H  N N 347 
THR HXT  H  N N 348 
TRP N    N  N N 349 
TRP CA   C  N S 350 
TRP C    C  N N 351 
TRP O    O  N N 352 
TRP CB   C  N N 353 
TRP CG   C  Y N 354 
TRP CD1  C  Y N 355 
TRP CD2  C  Y N 356 
TRP NE1  N  Y N 357 
TRP CE2  C  Y N 358 
TRP CE3  C  Y N 359 
TRP CZ2  C  Y N 360 
TRP CZ3  C  Y N 361 
TRP CH2  C  Y N 362 
TRP OXT  O  N N 363 
TRP H    H  N N 364 
TRP H2   H  N N 365 
TRP HA   H  N N 366 
TRP HB2  H  N N 367 
TRP HB3  H  N N 368 
TRP HD1  H  N N 369 
TRP HE1  H  N N 370 
TRP HE3  H  N N 371 
TRP HZ2  H  N N 372 
TRP HZ3  H  N N 373 
TRP HH2  H  N N 374 
TRP HXT  H  N N 375 
TYR N    N  N N 376 
TYR CA   C  N S 377 
TYR C    C  N N 378 
TYR O    O  N N 379 
TYR CB   C  N N 380 
TYR CG   C  Y N 381 
TYR CD1  C  Y N 382 
TYR CD2  C  Y N 383 
TYR CE1  C  Y N 384 
TYR CE2  C  Y N 385 
TYR CZ   C  Y N 386 
TYR OH   O  N N 387 
TYR OXT  O  N N 388 
TYR H    H  N N 389 
TYR H2   H  N N 390 
TYR HA   H  N N 391 
TYR HB2  H  N N 392 
TYR HB3  H  N N 393 
TYR HD1  H  N N 394 
TYR HD2  H  N N 395 
TYR HE1  H  N N 396 
TYR HE2  H  N N 397 
TYR HH   H  N N 398 
TYR HXT  H  N N 399 
VAL N    N  N N 400 
VAL CA   C  N S 401 
VAL C    C  N N 402 
VAL O    O  N N 403 
VAL CB   C  N N 404 
VAL CG1  C  N N 405 
VAL CG2  C  N N 406 
VAL OXT  O  N N 407 
VAL H    H  N N 408 
VAL H2   H  N N 409 
VAL HA   H  N N 410 
VAL HB   H  N N 411 
VAL HG11 H  N N 412 
VAL HG12 H  N N 413 
VAL HG13 H  N N 414 
VAL HG21 H  N N 415 
VAL HG22 H  N N 416 
VAL HG23 H  N N 417 
VAL HXT  H  N N 418 
# 
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  
EDO C1  O1   sing N N 70  
EDO C1  C2   sing N N 71  
EDO C1  H11  sing N N 72  
EDO C1  H12  sing N N 73  
EDO O1  HO1  sing N N 74  
EDO C2  O2   sing N N 75  
EDO C2  H21  sing N N 76  
EDO C2  H22  sing N N 77  
EDO O2  HO2  sing N N 78  
GLN N   CA   sing N N 79  
GLN N   H    sing N N 80  
GLN N   H2   sing N N 81  
GLN CA  C    sing N N 82  
GLN CA  CB   sing N N 83  
GLN CA  HA   sing N N 84  
GLN C   O    doub N N 85  
GLN C   OXT  sing N N 86  
GLN CB  CG   sing N N 87  
GLN CB  HB2  sing N N 88  
GLN CB  HB3  sing N N 89  
GLN CG  CD   sing N N 90  
GLN CG  HG2  sing N N 91  
GLN CG  HG3  sing N N 92  
GLN CD  OE1  doub N N 93  
GLN CD  NE2  sing N N 94  
GLN NE2 HE21 sing N N 95  
GLN NE2 HE22 sing N N 96  
GLN OXT HXT  sing N N 97  
GLU N   CA   sing N N 98  
GLU N   H    sing N N 99  
GLU N   H2   sing N N 100 
GLU CA  C    sing N N 101 
GLU CA  CB   sing N N 102 
GLU CA  HA   sing N N 103 
GLU C   O    doub N N 104 
GLU C   OXT  sing N N 105 
GLU CB  CG   sing N N 106 
GLU CB  HB2  sing N N 107 
GLU CB  HB3  sing N N 108 
GLU CG  CD   sing N N 109 
GLU CG  HG2  sing N N 110 
GLU CG  HG3  sing N N 111 
GLU CD  OE1  doub N N 112 
GLU CD  OE2  sing N N 113 
GLU OE2 HE2  sing N N 114 
GLU OXT HXT  sing N N 115 
GLY N   CA   sing N N 116 
GLY N   H    sing N N 117 
GLY N   H2   sing N N 118 
GLY CA  C    sing N N 119 
GLY CA  HA2  sing N N 120 
GLY CA  HA3  sing N N 121 
GLY C   O    doub N N 122 
GLY C   OXT  sing N N 123 
GLY OXT HXT  sing N N 124 
GOL C1  O1   sing N N 125 
GOL C1  C2   sing N N 126 
GOL C1  H11  sing N N 127 
GOL C1  H12  sing N N 128 
GOL O1  HO1  sing N N 129 
GOL C2  O2   sing N N 130 
GOL C2  C3   sing N N 131 
GOL C2  H2   sing N N 132 
GOL O2  HO2  sing N N 133 
GOL C3  O3   sing N N 134 
GOL C3  H31  sing N N 135 
GOL C3  H32  sing N N 136 
GOL O3  HO3  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PEG C1  O1   sing N N 246 
PEG C1  C2   sing N N 247 
PEG C1  H11  sing N N 248 
PEG C1  H12  sing N N 249 
PEG O1  HO1  sing N N 250 
PEG C2  O2   sing N N 251 
PEG C2  H21  sing N N 252 
PEG C2  H22  sing N N 253 
PEG O2  C3   sing N N 254 
PEG C3  C4   sing N N 255 
PEG C3  H31  sing N N 256 
PEG C3  H32  sing N N 257 
PEG C4  O4   sing N N 258 
PEG C4  H41  sing N N 259 
PEG C4  H42  sing N N 260 
PEG O4  HO4  sing N N 261 
PHE N   CA   sing N N 262 
PHE N   H    sing N N 263 
PHE N   H2   sing N N 264 
PHE CA  C    sing N N 265 
PHE CA  CB   sing N N 266 
PHE CA  HA   sing N N 267 
PHE C   O    doub N N 268 
PHE C   OXT  sing N N 269 
PHE CB  CG   sing N N 270 
PHE CB  HB2  sing N N 271 
PHE CB  HB3  sing N N 272 
PHE CG  CD1  doub Y N 273 
PHE CG  CD2  sing Y N 274 
PHE CD1 CE1  sing Y N 275 
PHE CD1 HD1  sing N N 276 
PHE CD2 CE2  doub Y N 277 
PHE CD2 HD2  sing N N 278 
PHE CE1 CZ   doub Y N 279 
PHE CE1 HE1  sing N N 280 
PHE CE2 CZ   sing Y N 281 
PHE CE2 HE2  sing N N 282 
PHE CZ  HZ   sing N N 283 
PHE OXT HXT  sing N N 284 
PRO N   CA   sing N N 285 
PRO N   CD   sing N N 286 
PRO N   H    sing N N 287 
PRO CA  C    sing N N 288 
PRO CA  CB   sing N N 289 
PRO CA  HA   sing N N 290 
PRO C   O    doub N N 291 
PRO C   OXT  sing N N 292 
PRO CB  CG   sing N N 293 
PRO CB  HB2  sing N N 294 
PRO CB  HB3  sing N N 295 
PRO CG  CD   sing N N 296 
PRO CG  HG2  sing N N 297 
PRO CG  HG3  sing N N 298 
PRO CD  HD2  sing N N 299 
PRO CD  HD3  sing N N 300 
PRO OXT HXT  sing N N 301 
SER N   CA   sing N N 302 
SER N   H    sing N N 303 
SER N   H2   sing N N 304 
SER CA  C    sing N N 305 
SER CA  CB   sing N N 306 
SER CA  HA   sing N N 307 
SER C   O    doub N N 308 
SER C   OXT  sing N N 309 
SER CB  OG   sing N N 310 
SER CB  HB2  sing N N 311 
SER CB  HB3  sing N N 312 
SER OG  HG   sing N N 313 
SER OXT HXT  sing N N 314 
THR N   CA   sing N N 315 
THR N   H    sing N N 316 
THR N   H2   sing N N 317 
THR CA  C    sing N N 318 
THR CA  CB   sing N N 319 
THR CA  HA   sing N N 320 
THR C   O    doub N N 321 
THR C   OXT  sing N N 322 
THR CB  OG1  sing N N 323 
THR CB  CG2  sing N N 324 
THR CB  HB   sing N N 325 
THR OG1 HG1  sing N N 326 
THR CG2 HG21 sing N N 327 
THR CG2 HG22 sing N N 328 
THR CG2 HG23 sing N N 329 
THR OXT HXT  sing N N 330 
TRP N   CA   sing N N 331 
TRP N   H    sing N N 332 
TRP N   H2   sing N N 333 
TRP CA  C    sing N N 334 
TRP CA  CB   sing N N 335 
TRP CA  HA   sing N N 336 
TRP C   O    doub N N 337 
TRP C   OXT  sing N N 338 
TRP CB  CG   sing N N 339 
TRP CB  HB2  sing N N 340 
TRP CB  HB3  sing N N 341 
TRP CG  CD1  doub Y N 342 
TRP CG  CD2  sing Y N 343 
TRP CD1 NE1  sing Y N 344 
TRP CD1 HD1  sing N N 345 
TRP CD2 CE2  doub Y N 346 
TRP CD2 CE3  sing Y N 347 
TRP NE1 CE2  sing Y N 348 
TRP NE1 HE1  sing N N 349 
TRP CE2 CZ2  sing Y N 350 
TRP CE3 CZ3  doub Y N 351 
TRP CE3 HE3  sing N N 352 
TRP CZ2 CH2  doub Y N 353 
TRP CZ2 HZ2  sing N N 354 
TRP CZ3 CH2  sing Y N 355 
TRP CZ3 HZ3  sing N N 356 
TRP CH2 HH2  sing N N 357 
TRP OXT HXT  sing N N 358 
TYR N   CA   sing N N 359 
TYR N   H    sing N N 360 
TYR N   H2   sing N N 361 
TYR CA  C    sing N N 362 
TYR CA  CB   sing N N 363 
TYR CA  HA   sing N N 364 
TYR C   O    doub N N 365 
TYR C   OXT  sing N N 366 
TYR CB  CG   sing N N 367 
TYR CB  HB2  sing N N 368 
TYR CB  HB3  sing N N 369 
TYR CG  CD1  doub Y N 370 
TYR CG  CD2  sing Y N 371 
TYR CD1 CE1  sing Y N 372 
TYR CD1 HD1  sing N N 373 
TYR CD2 CE2  doub Y N 374 
TYR CD2 HD2  sing N N 375 
TYR CE1 CZ   doub Y N 376 
TYR CE1 HE1  sing N N 377 
TYR CE2 CZ   sing Y N 378 
TYR CE2 HE2  sing N N 379 
TYR CZ  OH   sing N N 380 
TYR OH  HH   sing N N 381 
TYR OXT HXT  sing N N 382 
VAL N   CA   sing N N 383 
VAL N   H    sing N N 384 
VAL N   H2   sing N N 385 
VAL CA  C    sing N N 386 
VAL CA  CB   sing N N 387 
VAL CA  HA   sing N N 388 
VAL C   O    doub N N 389 
VAL C   OXT  sing N N 390 
VAL CB  CG1  sing N N 391 
VAL CB  CG2  sing N N 392 
VAL CB  HB   sing N N 393 
VAL CG1 HG11 sing N N 394 
VAL CG1 HG12 sing N N 395 
VAL CG1 HG13 sing N N 396 
VAL CG2 HG21 sing N N 397 
VAL CG2 HG22 sing N N 398 
VAL CG2 HG23 sing N N 399 
VAL OXT HXT  sing N N 400 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other private'                             ?      'The Edmond and Benjamin de Rothschild Foundation' 1 
'Israel Science Foundation'                 Israel 338/19                                             2 
'Israel Ministry of Science and Technology' Israel 2020000381                                         3 
# 
_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   6yun 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8R6E 
_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]   0.022925 
_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]   0.021110 
_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]   0.007428 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . THR A 1 1   ? -11.878 4.407   44.786 1.00 97.37  ? 1   THR A N   1 
ATOM   2    C  CA  . THR A 1 1   ? -11.308 3.045   44.660 1.00 93.51  ? 1   THR A CA  1 
ATOM   3    C  C   . THR A 1 1   ? -11.314 2.624   43.185 1.00 77.54  ? 1   THR A C   1 
ATOM   4    O  O   . THR A 1 1   ? -12.113 3.100   42.380 1.00 70.69  ? 1   THR A O   1 
ATOM   5    C  CB  . THR A 1 1   ? -12.071 2.082   45.579 1.00 100.67 ? 1   THR A CB  1 
ATOM   6    O  OG1 . THR A 1 1   ? -11.309 0.879   45.654 1.00 96.77  ? 1   THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 1   ? -13.492 1.796   45.118 1.00 103.76 ? 1   THR A CG2 1 
ATOM   8    N  N   . LYS A 1 2   ? -10.377 1.740   42.833 1.00 67.03  ? 2   LYS A N   1 
ATOM   9    C  CA  . LYS A 1 2   ? -10.260 1.216   41.484 1.00 68.72  ? 2   LYS A CA  1 
ATOM   10   C  C   . LYS A 1 2   ? -11.371 0.184   41.237 1.00 57.11  ? 2   LYS A C   1 
ATOM   11   O  O   . LYS A 1 2   ? -11.780 -0.557  42.142 1.00 50.24  ? 2   LYS A O   1 
ATOM   12   C  CB  . LYS A 1 2   ? -8.835  0.666   41.323 1.00 71.77  ? 2   LYS A CB  1 
ATOM   13   C  CG  . LYS A 1 2   ? -8.278  0.645   39.906 1.00 80.38  ? 2   LYS A CG  1 
ATOM   14   C  CD  . LYS A 1 2   ? -6.755  0.576   39.913 1.00 80.54  ? 2   LYS A CD  1 
ATOM   15   C  CE  . LYS A 1 2   ? -6.122  1.908   40.197 1.00 77.02  ? 2   LYS A CE  1 
ATOM   16   N  NZ  . LYS A 1 2   ? -4.846  1.737   40.901 1.00 72.45  ? 2   LYS A NZ  1 
ATOM   17   N  N   . LYS A 1 3   ? -11.858 0.138   39.995 1.00 46.23  ? 3   LYS A N   1 
ATOM   18   C  CA  A LYS A 1 3   ? -12.892 -0.804  39.628 0.50 44.02  ? 3   LYS A CA  1 
ATOM   19   C  CA  B LYS A 1 3   ? -12.894 -0.802  39.612 0.50 45.22  ? 3   LYS A CA  1 
ATOM   20   C  C   . LYS A 1 3   ? -12.291 -2.209  39.554 1.00 42.30  ? 3   LYS A C   1 
ATOM   21   O  O   . LYS A 1 3   ? -11.195 -2.399  39.038 1.00 42.91  ? 3   LYS A O   1 
ATOM   22   C  CB  A LYS A 1 3   ? -13.507 -0.302  38.319 0.50 45.37  ? 3   LYS A CB  1 
ATOM   23   C  CB  B LYS A 1 3   ? -13.498 -0.341  38.277 0.50 48.27  ? 3   LYS A CB  1 
ATOM   24   C  CG  A LYS A 1 3   ? -14.420 -1.303  37.658 0.50 45.26  ? 3   LYS A CG  1 
ATOM   25   C  CG  B LYS A 1 3   ? -13.656 1.176   38.106 0.50 50.81  ? 3   LYS A CG  1 
ATOM   26   C  CD  A LYS A 1 3   ? -15.566 -0.693  36.869 0.50 47.18  ? 3   LYS A CD  1 
ATOM   27   C  CD  B LYS A 1 3   ? -14.763 1.600   37.147 0.50 49.71  ? 3   LYS A CD  1 
ATOM   28   C  CE  A LYS A 1 3   ? -15.186 0.482   36.066 0.50 44.81  ? 3   LYS A CE  1 
ATOM   29   C  CE  B LYS A 1 3   ? -14.778 3.072   36.833 0.50 49.14  ? 3   LYS A CE  1 
ATOM   30   N  NZ  A LYS A 1 3   ? -15.964 0.442   34.826 0.50 44.39  ? 3   LYS A NZ  1 
ATOM   31   N  NZ  B LYS A 1 3   ? -14.185 3.356   35.523 0.50 48.27  ? 3   LYS A NZ  1 
ATOM   32   N  N   . SER A 1 4   ? -13.018 -3.201  40.071 1.00 40.86  ? 4   SER A N   1 
ATOM   33   C  CA  . SER A 1 4   ? -12.604 -4.589  39.993 1.00 38.31  ? 4   SER A CA  1 
ATOM   34   C  C   . SER A 1 4   ? -12.534 -5.065  38.545 1.00 36.58  ? 4   SER A C   1 
ATOM   35   O  O   . SER A 1 4   ? -13.200 -4.495  37.689 1.00 31.27  ? 4   SER A O   1 
ATOM   36   C  CB  . SER A 1 4   ? -13.541 -5.456  40.760 1.00 39.55  ? 4   SER A CB  1 
ATOM   37   O  OG  . SER A 1 4   ? -14.827 -5.480  40.165 1.00 39.87  ? 4   SER A OG  1 
ATOM   38   N  N   . ALA A 1 5   ? -11.807 -6.166  38.322 1.00 32.95  ? 5   ALA A N   1 
ATOM   39   C  CA  . ALA A 1 5   ? -11.804 -6.844  37.041 1.00 34.53  ? 5   ALA A CA  1 
ATOM   40   C  C   . ALA A 1 5   ? -13.225 -7.276  36.659 1.00 38.37  ? 5   ALA A C   1 
ATOM   41   O  O   . ALA A 1 5   ? -13.596 -7.162  35.496 1.00 34.04  ? 5   ALA A O   1 
ATOM   42   C  CB  . ALA A 1 5   ? -10.832 -8.019  37.072 1.00 32.54  ? 5   ALA A CB  1 
ATOM   43   N  N   . ALA A 1 6   ? -14.002 -7.824  37.612 1.00 38.99  ? 6   ALA A N   1 
ATOM   44   C  CA  . ALA A 1 6   ? -15.371 -8.275  37.344 1.00 34.17  ? 6   ALA A CA  1 
ATOM   45   C  C   . ALA A 1 6   ? -16.228 -7.140  36.760 1.00 28.96  ? 6   ALA A C   1 
ATOM   46   O  O   . ALA A 1 6   ? -16.925 -7.335  35.776 1.00 34.80  ? 6   ALA A O   1 
ATOM   47   C  CB  . ALA A 1 6   ? -15.998 -8.817  38.606 1.00 33.50  ? 6   ALA A CB  1 
ATOM   48   N  N   . GLU A 1 7   ? -16.133 -5.937  37.343 1.00 32.65  ? 7   GLU A N   1 
ATOM   49   C  CA  A GLU A 1 7   ? -16.891 -4.779  36.902 0.60 32.77  ? 7   GLU A CA  1 
ATOM   50   C  CA  B GLU A 1 7   ? -16.889 -4.777  36.899 0.40 32.16  ? 7   GLU A CA  1 
ATOM   51   C  C   . GLU A 1 7   ? -16.344 -4.217  35.582 1.00 36.01  ? 7   GLU A C   1 
ATOM   52   O  O   . GLU A 1 7   ? -17.111 -3.989  34.645 1.00 38.34  ? 7   GLU A O   1 
ATOM   53   C  CB  A GLU A 1 7   ? -16.883 -3.650  37.936 0.60 34.96  ? 7   GLU A CB  1 
ATOM   54   C  CB  B GLU A 1 7   ? -16.873 -3.682  37.966 0.40 32.40  ? 7   GLU A CB  1 
ATOM   55   C  CG  A GLU A 1 7   ? -17.936 -3.735  39.041 0.60 40.57  ? 7   GLU A CG  1 
ATOM   56   C  CG  B GLU A 1 7   ? -17.551 -2.386  37.530 0.40 33.74  ? 7   GLU A CG  1 
ATOM   57   C  CD  A GLU A 1 7   ? -19.370 -3.954  38.595 0.60 40.04  ? 7   GLU A CD  1 
ATOM   58   C  CD  B GLU A 1 7   ? -18.055 -1.519  38.668 0.40 37.71  ? 7   GLU A CD  1 
ATOM   59   O  OE1 A GLU A 1 7   ? -20.009 -4.893  39.111 0.60 39.78  ? 7   GLU A OE1 1 
ATOM   60   O  OE1 B GLU A 1 7   ? -19.221 -1.121  38.569 0.40 38.34  ? 7   GLU A OE1 1 
ATOM   61   O  OE2 A GLU A 1 7   ? -19.809 -3.199  37.709 0.60 43.05  ? 7   GLU A OE2 1 
ATOM   62   O  OE2 B GLU A 1 7   ? -17.319 -1.238  39.636 0.40 41.95  ? 7   GLU A OE2 1 
ATOM   63   N  N   . ALA A 1 8   ? -15.028 -3.943  35.527 1.00 33.38  ? 8   ALA A N   1 
ATOM   64   C  CA  . ALA A 1 8   ? -14.372 -3.360  34.354 1.00 33.88  ? 8   ALA A CA  1 
ATOM   65   C  C   . ALA A 1 8   ? -14.528 -4.229  33.096 1.00 32.23  ? 8   ALA A C   1 
ATOM   66   O  O   . ALA A 1 8   ? -14.610 -3.707  31.988 1.00 31.61  ? 8   ALA A O   1 
ATOM   67   C  CB  . ALA A 1 8   ? -12.909 -3.112  34.700 1.00 34.91  ? 8   ALA A CB  1 
ATOM   68   N  N   . SER A 1 9   ? -14.597 -5.558  33.255 1.00 25.59  ? 9   SER A N   1 
ATOM   69   C  CA  . SER A 1 9   ? -14.726 -6.462  32.130 1.00 25.96  ? 9   SER A CA  1 
ATOM   70   C  C   . SER A 1 9   ? -16.129 -6.389  31.492 1.00 32.79  ? 9   SER A C   1 
ATOM   71   O  O   . SER A 1 9   ? -16.364 -6.905  30.398 1.00 31.82  ? 9   SER A O   1 
ATOM   72   C  CB  . SER A 1 9   ? -14.422 -7.885  32.535 1.00 31.62  ? 9   SER A CB  1 
ATOM   73   O  OG  . SER A 1 9   ? -15.295 -8.310  33.581 1.00 37.88  ? 9   SER A OG  1 
ATOM   74   N  N   . LYS A 1 10  ? -17.078 -5.743  32.155 1.00 29.73  ? 10  LYS A N   1 
ATOM   75   C  CA  . LYS A 1 10  ? -18.419 -5.671  31.600 1.00 33.56  ? 10  LYS A CA  1 
ATOM   76   C  C   . LYS A 1 10  ? -18.459 -4.633  30.485 1.00 33.76  ? 10  LYS A C   1 
ATOM   77   O  O   . LYS A 1 10  ? -19.399 -4.634  29.720 1.00 36.40  ? 10  LYS A O   1 
ATOM   78   C  CB  . LYS A 1 10  ? -19.455 -5.262  32.655 1.00 37.23  ? 10  LYS A CB  1 
ATOM   79   C  CG  . LYS A 1 10  ? -19.554 -6.232  33.833 1.00 40.97  ? 10  LYS A CG  1 
ATOM   80   C  CD  . LYS A 1 10  ? -20.541 -5.799  34.907 1.00 39.17  ? 10  LYS A CD  1 
ATOM   81   C  CE  . LYS A 1 10  ? -20.787 -6.923  35.862 1.00 45.41  ? 10  LYS A CE  1 
ATOM   82   N  NZ  . LYS A 1 10  ? -21.844 -6.518  36.785 1.00 53.31  ? 10  LYS A NZ  1 
ATOM   83   N  N   . LYS A 1 11  ? -17.488 -3.716  30.400 1.00 35.46  ? 11  LYS A N   1 
ATOM   84   C  CA  . LYS A 1 11  ? -17.456 -2.809  29.255 1.00 33.61  ? 11  LYS A CA  1 
ATOM   85   C  C   . LYS A 1 11  ? -17.182 -3.592  27.972 1.00 36.44  ? 11  LYS A C   1 
ATOM   86   O  O   . LYS A 1 11  ? -16.475 -4.596  27.986 1.00 31.83  ? 11  LYS A O   1 
ATOM   87   C  CB  . LYS A 1 11  ? -16.440 -1.712  29.520 1.00 35.17  ? 11  LYS A CB  1 
ATOM   88   C  CG  . LYS A 1 11  ? -16.991 -0.771  30.557 1.00 40.22  ? 11  LYS A CG  1 
ATOM   89   C  CD  . LYS A 1 11  ? -16.288 0.564   30.592 1.00 51.87  ? 11  LYS A CD  1 
ATOM   90   C  CE  . LYS A 1 11  ? -16.718 1.400   31.751 1.00 59.73  ? 11  LYS A CE  1 
ATOM   91   N  NZ  . LYS A 1 11  ? -17.964 2.095   31.440 1.00 68.13  ? 11  LYS A NZ  1 
ATOM   92   N  N   . PRO A 1 12  ? -17.734 -3.157  26.813 1.00 35.82  ? 12  PRO A N   1 
ATOM   93   C  CA  . PRO A 1 12  ? -17.299 -3.690  25.520 1.00 37.18  ? 12  PRO A CA  1 
ATOM   94   C  C   . PRO A 1 12  ? -15.784 -3.502  25.391 1.00 31.05  ? 12  PRO A C   1 
ATOM   95   O  O   . PRO A 1 12  ? -15.214 -2.524  25.897 1.00 26.49  ? 12  PRO A O   1 
ATOM   96   C  CB  . PRO A 1 12  ? -18.065 -2.923  24.445 1.00 37.08  ? 12  PRO A CB  1 
ATOM   97   C  CG  . PRO A 1 12  ? -18.715 -1.778  25.186 1.00 41.34  ? 12  PRO A CG  1 
ATOM   98   C  CD  . PRO A 1 12  ? -18.723 -2.078  26.686 1.00 35.57  ? 12  PRO A CD  1 
ATOM   99   N  N   . ARG A 1 13  ? -15.151 -4.445  24.695 1.00 27.81  ? 13  ARG A N   1 
ATOM   100  C  CA  A ARG A 1 13  ? -13.696 -4.519  24.656 0.50 28.92  ? 13  ARG A CA  1 
ATOM   101  C  CA  B ARG A 1 13  ? -13.698 -4.519  24.652 0.50 28.68  ? 13  ARG A CA  1 
ATOM   102  C  C   . ARG A 1 13  ? -13.100 -3.142  24.366 1.00 25.20  ? 13  ARG A C   1 
ATOM   103  O  O   . ARG A 1 13  ? -12.201 -2.692  25.058 1.00 29.06  ? 13  ARG A O   1 
ATOM   104  C  CB  A ARG A 1 13  ? -13.196 -5.583  23.671 0.50 29.20  ? 13  ARG A CB  1 
ATOM   105  C  CB  B ARG A 1 13  ? -13.246 -5.577  23.641 0.50 28.67  ? 13  ARG A CB  1 
ATOM   106  C  CG  A ARG A 1 13  ? -11.722 -5.912  23.851 0.50 32.88  ? 13  ARG A CG  1 
ATOM   107  C  CG  B ARG A 1 13  ? -11.805 -6.010  23.837 0.50 31.80  ? 13  ARG A CG  1 
ATOM   108  C  CD  A ARG A 1 13  ? -11.203 -7.043  22.964 0.50 33.52  ? 13  ARG A CD  1 
ATOM   109  C  CD  B ARG A 1 13  ? -11.430 -7.227  22.976 0.50 31.82  ? 13  ARG A CD  1 
ATOM   110  N  NE  A ARG A 1 13  ? -11.721 -8.326  23.443 0.50 34.46  ? 13  ARG A NE  1 
ATOM   111  N  NE  B ARG A 1 13  ? -9.982  -7.476  22.985 0.50 33.41  ? 13  ARG A NE  1 
ATOM   112  C  CZ  A ARG A 1 13  ? -11.051 -9.258  24.135 0.50 35.40  ? 13  ARG A CZ  1 
ATOM   113  C  CZ  B ARG A 1 13  ? -9.188  -7.340  21.923 0.50 34.27  ? 13  ARG A CZ  1 
ATOM   114  N  NH1 A ARG A 1 13  ? -9.759  -9.118  24.413 0.50 32.53  ? 13  ARG A NH1 1 
ATOM   115  N  NH1 B ARG A 1 13  ? -9.755  -7.177  20.741 0.50 38.13  ? 13  ARG A NH1 1 
ATOM   116  N  NH2 A ARG A 1 13  ? -11.709 -10.329 24.548 0.50 31.38  ? 13  ARG A NH2 1 
ATOM   117  N  NH2 B ARG A 1 13  ? -7.860  -7.353  22.033 0.50 23.47  ? 13  ARG A NH2 1 
ATOM   118  N  N   . GLN A 1 14  ? -13.577 -2.472  23.333 1.00 25.97  ? 14  GLN A N   1 
ATOM   119  C  CA  . GLN A 1 14  ? -12.953 -1.245  22.860 1.00 21.21  ? 14  GLN A CA  1 
ATOM   120  C  C   . GLN A 1 14  ? -13.146 -0.086  23.838 1.00 24.55  ? 14  GLN A C   1 
ATOM   121  O  O   . GLN A 1 14  ? -12.532 0.951   23.671 1.00 29.22  ? 14  GLN A O   1 
ATOM   122  C  CB  . GLN A 1 14  ? -13.508 -0.885  21.474 1.00 23.94  ? 14  GLN A CB  1 
ATOM   123  C  CG  . GLN A 1 14  ? -14.958 -0.407  21.427 1.00 24.79  ? 14  GLN A CG  1 
ATOM   124  C  CD  . GLN A 1 14  ? -16.015 -1.489  21.397 1.00 29.01  ? 14  GLN A CD  1 
ATOM   125  O  OE1 . GLN A 1 14  ? -15.755 -2.690  21.571 1.00 26.53  ? 14  GLN A OE1 1 
ATOM   126  N  NE2 . GLN A 1 14  ? -17.250 -1.060  21.149 1.00 31.16  ? 14  GLN A NE2 1 
ATOM   127  N  N   . LYS A 1 15  ? -14.020 -0.215  24.835 1.00 24.69  ? 15  LYS A N   1 
ATOM   128  C  CA  . LYS A 1 15  ? -14.205 0.818   25.853 1.00 25.65  ? 15  LYS A CA  1 
ATOM   129  C  C   . LYS A 1 15  ? -13.562 0.472   27.204 1.00 28.17  ? 15  LYS A C   1 
ATOM   130  O  O   . LYS A 1 15  ? -13.665 1.261   28.151 1.00 26.50  ? 15  LYS A O   1 
ATOM   131  C  CB  . LYS A 1 15  ? -15.697 1.055   26.089 1.00 28.41  ? 15  LYS A CB  1 
ATOM   132  C  CG  . LYS A 1 15  ? -16.446 1.540   24.833 1.00 28.38  ? 15  LYS A CG  1 
ATOM   133  C  CD  . LYS A 1 15  ? -15.900 2.860   24.324 1.00 24.91  ? 15  LYS A CD  1 
ATOM   134  C  CE  . LYS A 1 15  ? -16.789 3.488   23.338 1.00 28.59  ? 15  LYS A CE  1 
ATOM   135  N  NZ  . LYS A 1 15  ? -16.200 4.748   22.876 1.00 25.85  ? 15  LYS A NZ  1 
ATOM   136  N  N   . ARG A 1 16  ? -12.911 -0.692  27.319 1.00 28.31  ? 16  ARG A N   1 
ATOM   137  C  CA  . ARG A 1 16  ? -12.204 -1.065  28.541 1.00 30.08  ? 16  ARG A CA  1 
ATOM   138  C  C   . ARG A 1 16  ? -11.018 -0.139  28.866 1.00 28.63  ? 16  ARG A C   1 
ATOM   139  O  O   . ARG A 1 16  ? -10.433 0.460   27.973 1.00 28.45  ? 16  ARG A O   1 
ATOM   140  C  CB  . ARG A 1 16  ? -11.678 -2.496  28.414 1.00 24.59  ? 16  ARG A CB  1 
ATOM   141  C  CG  . ARG A 1 16  ? -12.845 -3.455  28.463 1.00 26.65  ? 16  ARG A CG  1 
ATOM   142  C  CD  . ARG A 1 16  ? -12.358 -4.864  28.188 1.00 28.20  ? 16  ARG A CD  1 
ATOM   143  N  NE  . ARG A 1 16  ? -13.514 -5.753  28.238 1.00 30.09  ? 16  ARG A NE  1 
ATOM   144  C  CZ  . ARG A 1 16  ? -13.484 -7.051  27.976 1.00 34.49  ? 16  ARG A CZ  1 
ATOM   145  N  NH1 . ARG A 1 16  ? -12.407 -7.620  27.474 1.00 31.75  ? 16  ARG A NH1 1 
ATOM   146  N  NH2 . ARG A 1 16  ? -14.550 -7.779  28.232 1.00 37.70  ? 16  ARG A NH2 1 
ATOM   147  N  N   . THR A 1 17  ? -10.728 0.007   30.170 1.00 26.17  ? 17  THR A N   1 
ATOM   148  C  CA  . THR A 1 17  ? -9.579  0.716   30.699 1.00 28.49  ? 17  THR A CA  1 
ATOM   149  C  C   . THR A 1 17  ? -8.758  -0.251  31.544 1.00 29.76  ? 17  THR A C   1 
ATOM   150  O  O   . THR A 1 17  ? -9.217  -0.740  32.573 1.00 26.17  ? 17  THR A O   1 
ATOM   151  C  CB  . THR A 1 17  ? -10.016 1.927   31.522 1.00 31.98  ? 17  THR A CB  1 
ATOM   152  O  OG1 . THR A 1 17  ? -10.664 2.777   30.601 1.00 34.82  ? 17  THR A OG1 1 
ATOM   153  C  CG2 . THR A 1 17  ? -8.863  2.735   32.077 1.00 34.60  ? 17  THR A CG2 1 
ATOM   154  N  N   . ALA A 1 18  ? -7.542  -0.549  31.082 1.00 29.60  ? 18  ALA A N   1 
ATOM   155  C  CA  . ALA A 1 18  ? -6.622  -1.359  31.877 1.00 28.15  ? 18  ALA A CA  1 
ATOM   156  C  C   . ALA A 1 18  ? -6.016  -0.535  33.011 1.00 29.12  ? 18  ALA A C   1 
ATOM   157  O  O   . ALA A 1 18  ? -5.717  0.655   32.835 1.00 24.15  ? 18  ALA A O   1 
ATOM   158  C  CB  . ALA A 1 18  ? -5.551  -1.989  31.015 1.00 28.80  ? 18  ALA A CB  1 
ATOM   159  N  N   . THR A 1 19  ? -5.881  -1.192  34.179 1.00 26.32  ? 19  THR A N   1 
ATOM   160  C  CA  . THR A 1 19  ? -5.295  -0.648  35.398 1.00 27.72  ? 19  THR A CA  1 
ATOM   161  C  C   . THR A 1 19  ? -4.563  -1.786  36.109 1.00 28.73  ? 19  THR A C   1 
ATOM   162  O  O   . THR A 1 19  ? -4.607  -2.935  35.656 1.00 26.36  ? 19  THR A O   1 
ATOM   163  C  CB  . THR A 1 19  ? -6.381  -0.111  36.347 1.00 31.95  ? 19  THR A CB  1 
ATOM   164  O  OG1 . THR A 1 19  ? -7.152  -1.194  36.876 1.00 32.12  ? 19  THR A OG1 1 
ATOM   165  C  CG2 . THR A 1 19  ? -7.317  0.892   35.720 1.00 32.33  ? 19  THR A CG2 1 
ATOM   166  N  N   . LYS A 1 20  ? -3.971  -1.504  37.276 1.00 28.48  ? 20  LYS A N   1 
ATOM   167  C  CA  . LYS A 1 20  ? -3.426  -2.591  38.083 1.00 33.60  ? 20  LYS A CA  1 
ATOM   168  C  C   . LYS A 1 20  ? -4.477  -3.638  38.464 1.00 33.78  ? 20  LYS A C   1 
ATOM   169  O  O   . LYS A 1 20  ? -4.156  -4.817  38.520 1.00 34.08  ? 20  LYS A O   1 
ATOM   170  C  CB  . LYS A 1 20  ? -2.725  -2.102  39.346 1.00 40.14  ? 20  LYS A CB  1 
ATOM   171  C  CG  . LYS A 1 20  ? -1.244  -1.914  39.132 1.00 47.75  ? 20  LYS A CG  1 
ATOM   172  C  CD  . LYS A 1 20  ? -0.497  -1.317  40.319 1.00 53.71  ? 20  LYS A CD  1 
ATOM   173  C  CE  . LYS A 1 20  ? -0.443  0.172   40.271 1.00 58.19  ? 20  LYS A CE  1 
ATOM   174  N  NZ  . LYS A 1 20  ? 0.839   0.657   40.800 1.00 66.14  ? 20  LYS A NZ  1 
ATOM   175  N  N   . ALA A 1 21  ? -5.725  -3.219  38.688 1.00 33.70  ? 21  ALA A N   1 
ATOM   176  C  CA  . ALA A 1 21  ? -6.803  -4.132  39.057 1.00 34.09  ? 21  ALA A CA  1 
ATOM   177  C  C   . ALA A 1 21  ? -7.334  -4.925  37.863 1.00 36.73  ? 21  ALA A C   1 
ATOM   178  O  O   . ALA A 1 21  ? -8.014  -5.929  38.055 1.00 36.94  ? 21  ALA A O   1 
ATOM   179  C  CB  . ALA A 1 21  ? -7.906  -3.322  39.684 1.00 37.69  ? 21  ALA A CB  1 
ATOM   180  N  N   . TYR A 1 22  ? -7.038  -4.469  36.624 1.00 32.45  ? 22  TYR A N   1 
ATOM   181  C  CA  . TYR A 1 22  ? -7.553  -5.108  35.424 1.00 29.43  ? 22  TYR A CA  1 
ATOM   182  C  C   . TYR A 1 22  ? -6.559  -4.853  34.298 1.00 30.85  ? 22  TYR A C   1 
ATOM   183  O  O   . TYR A 1 22  ? -6.601  -3.829  33.602 1.00 27.10  ? 22  TYR A O   1 
ATOM   184  C  CB  . TYR A 1 22  ? -8.945  -4.536  35.097 1.00 29.16  ? 22  TYR A CB  1 
ATOM   185  C  CG  . TYR A 1 22  ? -9.710  -5.222  33.976 1.00 26.72  ? 22  TYR A CG  1 
ATOM   186  C  CD1 . TYR A 1 22  ? -9.810  -6.602  33.883 1.00 25.64  ? 22  TYR A CD1 1 
ATOM   187  C  CD2 . TYR A 1 22  ? -10.323 -4.466  32.970 1.00 24.59  ? 22  TYR A CD2 1 
ATOM   188  C  CE1 . TYR A 1 22  ? -10.511 -7.208  32.848 1.00 25.74  ? 22  TYR A CE1 1 
ATOM   189  C  CE2 . TYR A 1 22  ? -11.027 -5.068  31.938 1.00 26.39  ? 22  TYR A CE2 1 
ATOM   190  C  CZ  . TYR A 1 22  ? -11.108 -6.441  31.868 1.00 26.98  ? 22  TYR A CZ  1 
ATOM   191  O  OH  . TYR A 1 22  ? -11.797 -7.005  30.842 1.00 27.21  ? 22  TYR A OH  1 
ATOM   192  N  N   . ASN A 1 23  ? -5.646  -5.793  34.140 1.00 30.19  ? 23  ASN A N   1 
ATOM   193  C  CA  . ASN A 1 23  ? -4.417  -5.482  33.434 1.00 34.76  ? 23  ASN A CA  1 
ATOM   194  C  C   . ASN A 1 23  ? -4.622  -5.676  31.923 1.00 30.76  ? 23  ASN A C   1 
ATOM   195  O  O   . ASN A 1 23  ? -5.695  -6.096  31.474 1.00 29.09  ? 23  ASN A O   1 
ATOM   196  C  CB  . ASN A 1 23  ? -3.227  -6.219  34.039 1.00 27.58  ? 23  ASN A CB  1 
ATOM   197  C  CG  . ASN A 1 23  ? -3.240  -7.699  33.766 1.00 30.97  ? 23  ASN A CG  1 
ATOM   198  O  OD1 . ASN A 1 23  ? -3.652  -8.155  32.692 1.00 30.22  ? 23  ASN A OD1 1 
ATOM   199  N  ND2 . ASN A 1 23  ? -2.828  -8.472  34.767 1.00 34.37  ? 23  ASN A ND2 1 
ATOM   200  N  N   . VAL A 1 24  ? -3.562  -5.392  31.148 1.00 28.37  ? 24  VAL A N   1 
ATOM   201  C  CA  . VAL A 1 24  ? -3.674  -5.373  29.702 1.00 28.95  ? 24  VAL A CA  1 
ATOM   202  C  C   . VAL A 1 24  ? -4.020  -6.769  29.185 1.00 28.62  ? 24  VAL A C   1 
ATOM   203  O  O   . VAL A 1 24  ? -4.859  -6.904  28.300 1.00 29.03  ? 24  VAL A O   1 
ATOM   204  C  CB  . VAL A 1 24  ? -2.390  -4.823  29.062 1.00 27.77  ? 24  VAL A CB  1 
ATOM   205  C  CG1 . VAL A 1 24  ? -2.321  -5.098  27.564 1.00 30.53  ? 24  VAL A CG1 1 
ATOM   206  C  CG2 . VAL A 1 24  ? -2.249  -3.338  29.350 1.00 29.77  ? 24  VAL A CG2 1 
ATOM   207  N  N   . THR A 1 25  ? -3.431  -7.807  29.786 1.00 27.10  ? 25  THR A N   1 
ATOM   208  C  CA  . THR A 1 25  ? -3.730  -9.160  29.338 1.00 28.59  ? 25  THR A CA  1 
ATOM   209  C  C   . THR A 1 25  ? -5.202  -9.476  29.621 1.00 29.83  ? 25  THR A C   1 
ATOM   210  O  O   . THR A 1 25  ? -5.881  -10.096 28.807 1.00 33.93  ? 25  THR A O   1 
ATOM   211  C  CB  . THR A 1 25  ? -2.851  -10.173 30.077 1.00 32.85  ? 25  THR A CB  1 
ATOM   212  O  OG1 . THR A 1 25  ? -1.502  -9.711  30.037 1.00 34.01  ? 25  THR A OG1 1 
ATOM   213  C  CG2 . THR A 1 25  ? -3.000  -11.561 29.482 1.00 33.32  ? 25  THR A CG2 1 
ATOM   214  N  N   . GLN A 1 26  ? -5.688  -9.080  30.795 1.00 29.96  ? 26  GLN A N   1 
ATOM   215  C  CA  . GLN A 1 26  ? -7.040  -9.441  31.203 1.00 32.89  ? 26  GLN A CA  1 
ATOM   216  C  C   . GLN A 1 26  ? -8.039  -8.711  30.317 1.00 31.72  ? 26  GLN A C   1 
ATOM   217  O  O   . GLN A 1 26  ? -8.994  -9.289  29.845 1.00 31.36  ? 26  GLN A O   1 
ATOM   218  C  CB  . GLN A 1 26  ? -7.234  -9.043  32.657 1.00 34.53  ? 26  GLN A CB  1 
ATOM   219  C  CG  . GLN A 1 26  ? -6.412  -9.849  33.649 1.00 36.24  ? 26  GLN A CG  1 
ATOM   220  C  CD  . GLN A 1 26  ? -6.635  -9.353  35.055 1.00 33.65  ? 26  GLN A CD  1 
ATOM   221  O  OE1 . GLN A 1 26  ? -6.325  -8.215  35.425 1.00 35.73  ? 26  GLN A OE1 1 
ATOM   222  N  NE2 . GLN A 1 26  ? -7.134  -10.254 35.878 1.00 37.74  ? 26  GLN A NE2 1 
ATOM   223  N  N   . ALA A 1 27  ? -7.764  -7.437  30.025 1.00 32.65  ? 27  ALA A N   1 
ATOM   224  C  CA  . ALA A 1 27  ? -8.653  -6.622  29.219 1.00 27.82  ? 27  ALA A CA  1 
ATOM   225  C  C   . ALA A 1 27  ? -8.550  -6.972  27.742 1.00 30.63  ? 27  ALA A C   1 
ATOM   226  O  O   . ALA A 1 27  ? -9.580  -6.944  27.052 1.00 31.12  ? 27  ALA A O   1 
ATOM   227  C  CB  . ALA A 1 27  ? -8.382  -5.136  29.471 1.00 29.53  ? 27  ALA A CB  1 
ATOM   228  N  N   . PHE A 1 28  ? -7.311  -7.161  27.230 1.00 29.59  ? 28  PHE A N   1 
ATOM   229  C  CA  . PHE A 1 28  ? -7.116  -7.083  25.791 1.00 27.53  ? 28  PHE A CA  1 
ATOM   230  C  C   . PHE A 1 28  ? -6.436  -8.327  25.238 1.00 25.92  ? 28  PHE A C   1 
ATOM   231  O  O   . PHE A 1 28  ? -6.138  -8.369  24.058 1.00 29.77  ? 28  PHE A O   1 
ATOM   232  C  CB  . PHE A 1 28  ? -6.332  -5.827  25.451 1.00 23.18  ? 28  PHE A CB  1 
ATOM   233  C  CG  . PHE A 1 28  ? -7.014  -4.555  25.947 1.00 25.71  ? 28  PHE A CG  1 
ATOM   234  C  CD1 . PHE A 1 28  ? -6.332  -3.660  26.761 1.00 25.10  ? 28  PHE A CD1 1 
ATOM   235  C  CD2 . PHE A 1 28  ? -8.320  -4.253  25.568 1.00 26.61  ? 28  PHE A CD2 1 
ATOM   236  C  CE1 . PHE A 1 28  ? -6.934  -2.484  27.207 1.00 26.80  ? 28  PHE A CE1 1 
ATOM   237  C  CE2 . PHE A 1 28  ? -8.938  -3.095  26.011 1.00 26.07  ? 28  PHE A CE2 1 
ATOM   238  C  CZ  . PHE A 1 28  ? -8.246  -2.200  26.820 1.00 27.08  ? 28  PHE A CZ  1 
ATOM   239  N  N   . GLY A 1 29  ? -6.150  -9.308  26.093 1.00 30.78  ? 29  GLY A N   1 
ATOM   240  C  CA  . GLY A 1 29  ? -5.528  -10.541 25.642 1.00 31.32  ? 29  GLY A CA  1 
ATOM   241  C  C   . GLY A 1 29  ? -4.002  -10.449 25.705 1.00 34.61  ? 29  GLY A C   1 
ATOM   242  O  O   . GLY A 1 29  ? -3.423  -9.353  25.785 1.00 32.09  ? 29  GLY A O   1 
ATOM   243  N  N   . ARG A 1 30  ? -3.367  -11.627 25.644 1.00 37.18  ? 30  ARG A N   1 
ATOM   244  C  CA  . ARG A 1 30  ? -1.916  -11.755 25.511 1.00 44.60  ? 30  ARG A CA  1 
ATOM   245  C  C   . ARG A 1 30  ? -1.423  -10.972 24.298 1.00 35.87  ? 30  ARG A C   1 
ATOM   246  O  O   . ARG A 1 30  ? -2.063  -11.004 23.243 1.00 34.53  ? 30  ARG A O   1 
ATOM   247  C  CB  . ARG A 1 30  ? -1.504  -13.217 25.289 1.00 49.14  ? 30  ARG A CB  1 
ATOM   248  C  CG  . ARG A 1 30  ? -1.486  -14.009 26.590 1.00 63.95  ? 30  ARG A CG  1 
ATOM   249  C  CD  . ARG A 1 30  ? -0.923  -15.421 26.487 1.00 74.62  ? 30  ARG A CD  1 
ATOM   250  N  NE  . ARG A 1 30  ? -1.509  -16.235 27.561 1.00 91.97  ? 30  ARG A NE  1 
ATOM   251  C  CZ  . ARG A 1 30  ? -2.621  -16.976 27.467 1.00 96.06  ? 30  ARG A CZ  1 
ATOM   252  N  NH1 . ARG A 1 30  ? -3.260  -17.088 26.312 1.00 99.93  ? 30  ARG A NH1 1 
ATOM   253  N  NH2 . ARG A 1 30  ? -3.102  -17.599 28.532 1.00 88.59  ? 30  ARG A NH2 1 
ATOM   254  N  N   . ARG A 1 31  ? -0.303  -10.246 24.461 1.00 34.83  ? 31  ARG A N   1 
ATOM   255  C  CA  . ARG A 1 31  ? 0.458   -9.754  23.324 1.00 34.25  ? 31  ARG A CA  1 
ATOM   256  C  C   . ARG A 1 31  ? 0.916   -10.937 22.458 1.00 37.65  ? 31  ARG A C   1 
ATOM   257  O  O   . ARG A 1 31  ? 1.167   -12.037 22.937 1.00 36.83  ? 31  ARG A O   1 
ATOM   258  C  CB  . ARG A 1 31  ? 1.632   -8.890  23.787 1.00 31.30  ? 31  ARG A CB  1 
ATOM   259  C  CG  . ARG A 1 31  ? 1.306   -7.421  24.062 1.00 33.51  ? 31  ARG A CG  1 
ATOM   260  C  CD  . ARG A 1 31  ? 0.503   -7.226  25.323 1.00 33.65  ? 31  ARG A CD  1 
ATOM   261  N  NE  . ARG A 1 31  ? -0.935  -7.449  25.163 1.00 29.99  ? 31  ARG A NE  1 
ATOM   262  C  CZ  . ARG A 1 31  ? -1.764  -6.691  24.440 1.00 31.29  ? 31  ARG A CZ  1 
ATOM   263  N  NH1 . ARG A 1 31  ? -3.062  -7.026  24.289 1.00 33.16  ? 31  ARG A NH1 1 
ATOM   264  N  NH2 . ARG A 1 31  ? -1.297  -5.612  23.839 1.00 29.33  ? 31  ARG A NH2 1 
ATOM   265  N  N   . GLY A 1 32  ? 0.952   -10.735 21.147 1.00 36.62  ? 32  GLY A N   1 
ATOM   266  C  CA  . GLY A 1 32  ? 1.332   -11.821 20.270 1.00 39.57  ? 32  GLY A CA  1 
ATOM   267  C  C   . GLY A 1 32  ? 1.468   -11.333 18.840 1.00 39.24  ? 32  GLY A C   1 
ATOM   268  O  O   . GLY A 1 32  ? 1.247   -10.150 18.567 1.00 43.41  ? 32  GLY A O   1 
ATOM   269  N  N   . PRO A 1 33  ? 1.838   -12.246 17.911 1.00 44.76  ? 33  PRO A N   1 
ATOM   270  C  CA  . PRO A 1 33  ? 2.099   -11.885 16.520 1.00 44.16  ? 33  PRO A CA  1 
ATOM   271  C  C   . PRO A 1 33  ? 0.921   -11.905 15.560 1.00 48.35  ? 33  PRO A C   1 
ATOM   272  O  O   . PRO A 1 33  ? 1.002   -11.312 14.482 1.00 42.97  ? 33  PRO A O   1 
ATOM   273  C  CB  . PRO A 1 33  ? 3.148   -12.949 16.162 1.00 49.50  ? 33  PRO A CB  1 
ATOM   274  C  CG  . PRO A 1 33  ? 2.693   -14.188 16.896 1.00 47.78  ? 33  PRO A CG  1 
ATOM   275  C  CD  . PRO A 1 33  ? 2.130   -13.664 18.198 1.00 42.68  ? 33  PRO A CD  1 
ATOM   276  N  N   . GLU A 1 34  ? -0.180  -12.537 15.978 1.00 48.57  ? 34  GLU A N   1 
ATOM   277  C  CA  . GLU A 1 34  ? -1.296  -12.780 15.076 1.00 54.73  ? 34  GLU A CA  1 
ATOM   278  C  C   . GLU A 1 34  ? -2.064  -11.484 14.842 1.00 53.68  ? 34  GLU A C   1 
ATOM   279  O  O   . GLU A 1 34  ? -2.023  -10.552 15.665 1.00 51.23  ? 34  GLU A O   1 
ATOM   280  C  CB  . GLU A 1 34  ? -2.236  -13.876 15.588 1.00 61.50  ? 34  GLU A CB  1 
ATOM   281  C  CG  . GLU A 1 34  ? -1.539  -15.201 15.900 1.00 70.61  ? 34  GLU A CG  1 
ATOM   282  C  CD  . GLU A 1 34  ? -0.759  -15.841 14.750 1.00 83.44  ? 34  GLU A CD  1 
ATOM   283  O  OE1 . GLU A 1 34  ? -0.983  -15.474 13.571 1.00 83.02  ? 34  GLU A OE1 1 
ATOM   284  O  OE2 . GLU A 1 34  ? 0.115   -16.699 15.038 1.00 88.56  ? 34  GLU A OE2 1 
ATOM   285  N  N   . GLN A 1 35  ? -2.819  -11.483 13.735 1.00 47.57  ? 35  GLN A N   1 
ATOM   286  C  CA  . GLN A 1 35  ? -3.509  -10.300 13.239 1.00 51.65  ? 35  GLN A CA  1 
ATOM   287  C  C   . GLN A 1 35  ? -4.557  -9.818  14.245 1.00 52.37  ? 35  GLN A C   1 
ATOM   288  O  O   . GLN A 1 35  ? -4.872  -8.634  14.318 1.00 48.86  ? 35  GLN A O   1 
ATOM   289  C  CB  . GLN A 1 35  ? -4.125  -10.611 11.877 1.00 61.40  ? 35  GLN A CB  1 
ATOM   290  C  CG  . GLN A 1 35  ? -3.979  -9.475  10.870 1.00 66.26  ? 35  GLN A CG  1 
ATOM   291  C  CD  . GLN A 1 35  ? -2.555  -8.968  10.786 1.00 69.31  ? 35  GLN A CD  1 
ATOM   292  O  OE1 . GLN A 1 35  ? -2.314  -7.768  10.634 1.00 61.74  ? 35  GLN A OE1 1 
ATOM   293  N  NE2 . GLN A 1 35  ? -1.589  -9.873  10.891 1.00 73.98  ? 35  GLN A NE2 1 
ATOM   294  N  N   . THR A 1 36  ? -5.034  -10.746 15.081 1.00 48.74  ? 36  THR A N   1 
ATOM   295  C  CA  . THR A 1 36  ? -6.085  -10.485 16.045 1.00 50.73  ? 36  THR A CA  1 
ATOM   296  C  C   . THR A 1 36  ? -5.520  -9.995  17.384 1.00 40.81  ? 36  THR A C   1 
ATOM   297  O  O   . THR A 1 36  ? -6.301  -9.581  18.227 1.00 39.89  ? 36  THR A O   1 
ATOM   298  C  CB  . THR A 1 36  ? -6.868  -11.785 16.218 1.00 49.02  ? 36  THR A CB  1 
ATOM   299  O  OG1 . THR A 1 36  ? -5.879  -12.759 16.505 1.00 53.45  ? 36  THR A OG1 1 
ATOM   300  C  CG2 . THR A 1 36  ? -7.519  -12.281 14.940 1.00 58.25  ? 36  THR A CG2 1 
ATOM   301  N  N   . GLN A 1 37  ? -4.200  -10.092 17.602 1.00 39.61  ? 37  GLN A N   1 
ATOM   302  C  CA  . GLN A 1 37  ? -3.618  -9.747  18.882 1.00 37.93  ? 37  GLN A CA  1 
ATOM   303  C  C   . GLN A 1 37  ? -2.974  -8.375  18.831 1.00 35.53  ? 37  GLN A C   1 
ATOM   304  O  O   . GLN A 1 37  ? -2.535  -7.918  17.781 1.00 34.86  ? 37  GLN A O   1 
ATOM   305  C  CB  . GLN A 1 37  ? -2.542  -10.744 19.255 1.00 41.19  ? 37  GLN A CB  1 
ATOM   306  C  CG  . GLN A 1 37  ? -3.060  -12.177 19.313 1.00 45.97  ? 37  GLN A CG  1 
ATOM   307  C  CD  . GLN A 1 37  ? -1.924  -13.157 19.504 1.00 47.78  ? 37  GLN A CD  1 
ATOM   308  O  OE1 . GLN A 1 37  ? -1.107  -13.358 18.602 1.00 58.57  ? 37  GLN A OE1 1 
ATOM   309  N  NE2 . GLN A 1 37  ? -1.829  -13.730 20.688 1.00 45.25  ? 37  GLN A NE2 1 
ATOM   310  N  N   . GLY A 1 38  ? -2.943  -7.717  19.988 1.00 32.38  ? 38  GLY A N   1 
ATOM   311  C  CA  . GLY A 1 38  ? -2.112  -6.545  20.154 1.00 33.34  ? 38  GLY A CA  1 
ATOM   312  C  C   . GLY A 1 38  ? -0.654  -6.970  20.350 1.00 35.08  ? 38  GLY A C   1 
ATOM   313  O  O   . GLY A 1 38  ? -0.359  -8.060  20.856 1.00 30.15  ? 38  GLY A O   1 
ATOM   314  N  N   . ASN A 1 39  ? 0.263   -6.061  20.002 1.00 32.27  ? 39  ASN A N   1 
ATOM   315  C  CA  . ASN A 1 39  ? 1.684   -6.348  20.138 1.00 30.41  ? 39  ASN A CA  1 
ATOM   316  C  C   . ASN A 1 39  ? 2.373   -5.351  21.064 1.00 27.06  ? 39  ASN A C   1 
ATOM   317  O  O   . ASN A 1 39  ? 3.606   -5.348  21.140 1.00 32.89  ? 39  ASN A O   1 
ATOM   318  C  CB  . ASN A 1 39  ? 2.380   -6.285  18.776 1.00 30.76  ? 39  ASN A CB  1 
ATOM   319  C  CG  . ASN A 1 39  ? 2.339   -4.893  18.178 1.00 33.54  ? 39  ASN A CG  1 
ATOM   320  O  OD1 . ASN A 1 39  ? 1.451   -4.100  18.499 1.00 30.58  ? 39  ASN A OD1 1 
ATOM   321  N  ND2 . ASN A 1 39  ? 3.292   -4.537  17.331 1.00 34.08  ? 39  ASN A ND2 1 
ATOM   322  N  N   . PHE A 1 40  ? 1.622   -4.492  21.746 1.00 25.52  ? 40  PHE A N   1 
ATOM   323  C  CA  . PHE A 1 40  ? 2.188   -3.351  22.455 1.00 26.63  ? 40  PHE A CA  1 
ATOM   324  C  C   . PHE A 1 40  ? 2.183   -3.539  23.954 1.00 28.26  ? 40  PHE A C   1 
ATOM   325  O  O   . PHE A 1 40  ? 1.167   -3.869  24.543 1.00 27.27  ? 40  PHE A O   1 
ATOM   326  C  CB  . PHE A 1 40  ? 1.443   -2.079  22.087 1.00 25.75  ? 40  PHE A CB  1 
ATOM   327  C  CG  . PHE A 1 40  ? 2.082   -0.765  22.502 1.00 23.43  ? 40  PHE A CG  1 
ATOM   328  C  CD1 . PHE A 1 40  ? 1.809   -0.196  23.729 1.00 23.66  ? 40  PHE A CD1 1 
ATOM   329  C  CD2 . PHE A 1 40  ? 2.985   -0.126  21.674 1.00 23.82  ? 40  PHE A CD2 1 
ATOM   330  C  CE1 . PHE A 1 40  ? 2.354   1.023   24.085 1.00 23.17  ? 40  PHE A CE1 1 
ATOM   331  C  CE2 . PHE A 1 40  ? 3.542   1.073   22.040 1.00 23.32  ? 40  PHE A CE2 1 
ATOM   332  C  CZ  . PHE A 1 40  ? 3.196   1.667   23.226 1.00 23.35  ? 40  PHE A CZ  1 
ATOM   333  N  N   . GLY A 1 41  ? 3.363   -3.310  24.551 1.00 26.54  ? 41  GLY A N   1 
ATOM   334  C  CA  . GLY A 1 41  ? 3.521   -3.249  25.991 1.00 31.99  ? 41  GLY A CA  1 
ATOM   335  C  C   . GLY A 1 41  ? 4.705   -4.089  26.477 1.00 29.49  ? 41  GLY A C   1 
ATOM   336  O  O   . GLY A 1 41  ? 4.803   -5.284  26.145 1.00 27.81  ? 41  GLY A O   1 
ATOM   337  N  N   . ASP A 1 42  ? 5.574   -3.460  27.283 1.00 29.49  ? 42  ASP A N   1 
ATOM   338  C  CA  . ASP A 1 42  ? 6.551   -4.214  28.072 1.00 30.22  ? 42  ASP A CA  1 
ATOM   339  C  C   . ASP A 1 42  ? 5.859   -4.762  29.313 1.00 29.59  ? 42  ASP A C   1 
ATOM   340  O  O   . ASP A 1 42  ? 4.661   -4.564  29.513 1.00 29.11  ? 42  ASP A O   1 
ATOM   341  C  CB  . ASP A 1 42  ? 7.816   -3.449  28.405 1.00 28.26  ? 42  ASP A CB  1 
ATOM   342  C  CG  . ASP A 1 42  ? 7.670   -2.349  29.435 1.00 33.58  ? 42  ASP A CG  1 
ATOM   343  O  OD1 . ASP A 1 42  ? 8.678   -1.605  29.623 1.00 32.57  ? 42  ASP A OD1 1 
ATOM   344  O  OD2 . ASP A 1 42  ? 6.575   -2.266  30.061 1.00 32.53  ? 42  ASP A OD2 1 
ATOM   345  N  N   . GLN A 1 43  ? 6.581   -5.454  30.189 1.00 29.54  ? 43  GLN A N   1 
ATOM   346  C  CA  A GLN A 1 43  ? 5.918   -6.187  31.259 0.60 29.29  ? 43  GLN A CA  1 
ATOM   347  C  CA  B GLN A 1 43  ? 5.906   -6.190  31.252 0.40 29.33  ? 43  GLN A CA  1 
ATOM   348  C  C   . GLN A 1 43  ? 5.281   -5.202  32.232 1.00 30.79  ? 43  GLN A C   1 
ATOM   349  O  O   . GLN A 1 43  ? 4.185   -5.421  32.736 1.00 29.87  ? 43  GLN A O   1 
ATOM   350  C  CB  A GLN A 1 43  ? 6.902   -7.155  31.916 0.60 36.28  ? 43  GLN A CB  1 
ATOM   351  C  CB  B GLN A 1 43  ? 6.829   -7.200  31.935 0.40 33.66  ? 43  GLN A CB  1 
ATOM   352  C  CG  A GLN A 1 43  ? 7.033   -8.477  31.167 0.60 39.74  ? 43  GLN A CG  1 
ATOM   353  C  CG  B GLN A 1 43  ? 7.134   -8.426  31.081 0.40 35.24  ? 43  GLN A CG  1 
ATOM   354  C  CD  A GLN A 1 43  ? 8.097   -9.409  31.712 0.60 44.03  ? 43  GLN A CD  1 
ATOM   355  C  CD  B GLN A 1 43  ? 6.114   -9.544  31.162 0.40 36.36  ? 43  GLN A CD  1 
ATOM   356  O  OE1 A GLN A 1 43  ? 8.131   -10.581 31.345 0.60 47.18  ? 43  GLN A OE1 1 
ATOM   357  O  OE1 B GLN A 1 43  ? 4.896   -9.344  31.252 0.40 38.09  ? 43  GLN A OE1 1 
ATOM   358  N  NE2 A GLN A 1 43  ? 8.978   -8.933  32.581 0.60 45.01  ? 43  GLN A NE2 1 
ATOM   359  N  NE2 B GLN A 1 43  ? 6.616   -10.766 31.117 0.40 39.23  ? 43  GLN A NE2 1 
ATOM   360  N  N   . GLU A 1 44  ? 5.970   -4.102  32.499 1.00 29.75  ? 44  GLU A N   1 
ATOM   361  C  CA  . GLU A 1 44  ? 5.455   -3.100  33.414 1.00 33.53  ? 44  GLU A CA  1 
ATOM   362  C  C   . GLU A 1 44  ? 4.137   -2.507  32.895 1.00 34.41  ? 44  GLU A C   1 
ATOM   363  O  O   . GLU A 1 44  ? 3.180   -2.363  33.650 1.00 32.65  ? 44  GLU A O   1 
ATOM   364  C  CB  . GLU A 1 44  ? 6.563   -2.060  33.567 1.00 36.31  ? 44  GLU A CB  1 
ATOM   365  C  CG  . GLU A 1 44  ? 6.418   -1.117  34.753 1.00 46.93  ? 44  GLU A CG  1 
ATOM   366  C  CD  . GLU A 1 44  ? 7.575   -0.113  34.864 1.00 57.70  ? 44  GLU A CD  1 
ATOM   367  O  OE1 . GLU A 1 44  ? 8.667   -0.321  34.270 1.00 63.73  ? 44  GLU A OE1 1 
ATOM   368  O  OE2 . GLU A 1 44  ? 7.337   0.953   35.477 1.00 67.46  ? 44  GLU A OE2 1 
ATOM   369  N  N   . LEU A 1 45  ? 4.096   -2.092  31.628 1.00 31.39  ? 45  LEU A N   1 
ATOM   370  C  CA  . LEU A 1 45  ? 2.879   -1.512  31.076 1.00 31.27  ? 45  LEU A CA  1 
ATOM   371  C  C   . LEU A 1 45  ? 1.754   -2.548  31.094 1.00 28.45  ? 45  LEU A C   1 
ATOM   372  O  O   . LEU A 1 45  ? 0.620   -2.236  31.438 1.00 26.09  ? 45  LEU A O   1 
ATOM   373  C  CB  . LEU A 1 45  ? 3.105   -0.968  29.670 1.00 29.04  ? 45  LEU A CB  1 
ATOM   374  C  CG  . LEU A 1 45  ? 1.839   -0.527  28.920 1.00 31.44  ? 45  LEU A CG  1 
ATOM   375  C  CD1 . LEU A 1 45  ? 1.021   0.446   29.742 1.00 35.08  ? 45  LEU A CD1 1 
ATOM   376  C  CD2 . LEU A 1 45  ? 2.217   0.136   27.596 1.00 33.27  ? 45  LEU A CD2 1 
ATOM   377  N  N   . ILE A 1 46  ? 2.067   -3.789  30.725 1.00 27.45  ? 46  ILE A N   1 
ATOM   378  C  CA  . ILE A 1 46  ? 1.062   -4.837  30.708 1.00 28.34  ? 46  ILE A CA  1 
ATOM   379  C  C   . ILE A 1 46  ? 0.417   -5.005  32.094 1.00 30.90  ? 46  ILE A C   1 
ATOM   380  O  O   . ILE A 1 46  ? -0.799  -5.169  32.214 1.00 30.06  ? 46  ILE A O   1 
ATOM   381  C  CB  . ILE A 1 46  ? 1.668   -6.154  30.199 1.00 29.56  ? 46  ILE A CB  1 
ATOM   382  C  CG1 . ILE A 1 46  ? 1.944   -6.078  28.720 1.00 30.32  ? 46  ILE A CG1 1 
ATOM   383  C  CG2 . ILE A 1 46  ? 0.777   -7.351  30.569 1.00 29.30  ? 46  ILE A CG2 1 
ATOM   384  C  CD1 . ILE A 1 46  ? 2.748   -7.238  28.178 1.00 33.23  ? 46  ILE A CD1 1 
ATOM   385  N  N   . ARG A 1 47  ? 1.226   -4.959  33.148 1.00 29.53  ? 47  ARG A N   1 
ATOM   386  C  CA  A ARG A 1 47  ? 0.776   -5.199  34.508 0.60 32.17  ? 47  ARG A CA  1 
ATOM   387  C  CA  B ARG A 1 47  ? 0.755   -5.209  34.506 0.40 31.64  ? 47  ARG A CA  1 
ATOM   388  C  C   . ARG A 1 47  ? 0.011   -3.988  35.045 1.00 30.95  ? 47  ARG A C   1 
ATOM   389  O  O   . ARG A 1 47  ? -0.863  -4.145  35.881 1.00 33.89  ? 47  ARG A O   1 
ATOM   390  C  CB  A ARG A 1 47  ? 2.066   -5.435  35.311 0.60 35.20  ? 47  ARG A CB  1 
ATOM   391  C  CB  B ARG A 1 47  ? 1.885   -5.606  35.483 0.40 34.06  ? 47  ARG A CB  1 
ATOM   392  C  CG  A ARG A 1 47  ? 1.990   -5.882  36.760 0.60 39.34  ? 47  ARG A CG  1 
ATOM   393  C  CG  B ARG A 1 47  ? 1.740   -5.161  36.940 0.40 36.97  ? 47  ARG A CG  1 
ATOM   394  C  CD  A ARG A 1 47  ? 3.387   -6.241  37.296 0.60 38.74  ? 47  ARG A CD  1 
ATOM   395  C  CD  B ARG A 1 47  ? 2.717   -5.745  37.972 0.40 39.51  ? 47  ARG A CD  1 
ATOM   396  N  NE  A ARG A 1 47  ? 4.235   -5.057  37.517 0.60 41.74  ? 47  ARG A NE  1 
ATOM   397  N  NE  B ARG A 1 47  ? 3.782   -4.843  38.427 0.40 41.69  ? 47  ARG A NE  1 
ATOM   398  C  CZ  A ARG A 1 47  ? 5.417   -4.778  36.947 0.60 35.54  ? 47  ARG A CZ  1 
ATOM   399  C  CZ  B ARG A 1 47  ? 3.664   -3.836  39.279 0.40 41.02  ? 47  ARG A CZ  1 
ATOM   400  N  NH1 A ARG A 1 47  ? 5.956   -5.608  36.059 0.60 33.01  ? 47  ARG A NH1 1 
ATOM   401  N  NH1 B ARG A 1 47  ? 4.739   -3.135  39.605 0.40 43.05  ? 47  ARG A NH1 1 
ATOM   402  N  NH2 A ARG A 1 47  ? 6.051   -3.662  37.282 0.60 37.06  ? 47  ARG A NH2 1 
ATOM   403  N  NH2 B ARG A 1 47  ? 2.490   -3.536  39.807 0.40 37.48  ? 47  ARG A NH2 1 
ATOM   404  N  N   . GLN A 1 48  ? 0.350   -2.774  34.588 1.00 25.95  ? 48  GLN A N   1 
ATOM   405  C  CA  . GLN A 1 48  ? -0.246  -1.583  35.196 1.00 28.49  ? 48  GLN A CA  1 
ATOM   406  C  C   . GLN A 1 48  ? -1.306  -0.852  34.354 1.00 27.48  ? 48  GLN A C   1 
ATOM   407  O  O   . GLN A 1 48  ? -2.022  0.004   34.884 1.00 24.14  ? 48  GLN A O   1 
ATOM   408  C  CB  . GLN A 1 48  ? 0.891   -0.626  35.529 1.00 31.12  ? 48  GLN A CB  1 
ATOM   409  C  CG  . GLN A 1 48  ? 1.826   -1.234  36.576 1.00 37.35  ? 48  GLN A CG  1 
ATOM   410  C  CD  . GLN A 1 48  ? 3.090   -0.458  36.846 1.00 42.01  ? 48  GLN A CD  1 
ATOM   411  O  OE1 . GLN A 1 48  ? 3.438   0.504   36.155 1.00 50.77  ? 48  GLN A OE1 1 
ATOM   412  N  NE2 . GLN A 1 48  ? 3.790   -0.906  37.873 1.00 52.89  ? 48  GLN A NE2 1 
ATOM   413  N  N   . GLY A 1 49  ? -1.333  -1.068  33.037 1.00 29.37  ? 49  GLY A N   1 
ATOM   414  C  CA  . GLY A 1 49  ? -2.243  -0.371  32.147 1.00 27.29  ? 49  GLY A CA  1 
ATOM   415  C  C   . GLY A 1 49  ? -2.132  1.137   32.356 1.00 27.85  ? 49  GLY A C   1 
ATOM   416  O  O   . GLY A 1 49  ? -1.026  1.640   32.282 1.00 28.27  ? 49  GLY A O   1 
ATOM   417  N  N   . THR A 1 50  ? -3.243  1.807   32.675 1.00 27.48  ? 50  THR A N   1 
ATOM   418  C  CA  . THR A 1 50  ? -3.283  3.264   32.739 1.00 30.01  ? 50  THR A CA  1 
ATOM   419  C  C   . THR A 1 50  ? -2.623  3.753   34.023 1.00 27.63  ? 50  THR A C   1 
ATOM   420  O  O   . THR A 1 50  ? -2.445  4.959   34.177 1.00 28.36  ? 50  THR A O   1 
ATOM   421  C  CB  . THR A 1 50  ? -4.709  3.820   32.593 1.00 31.72  ? 50  THR A CB  1 
ATOM   422  O  OG1 . THR A 1 50  ? -5.570  3.294   33.595 1.00 27.71  ? 50  THR A OG1 1 
ATOM   423  C  CG2 . THR A 1 50  ? -5.323  3.518   31.234 1.00 30.17  ? 50  THR A CG2 1 
ATOM   424  N  N   . ASP A 1 51  ? -2.257  2.832   34.935 1.00 29.09  ? 51  ASP A N   1 
ATOM   425  C  CA  . ASP A 1 51  ? -1.488  3.189   36.123 1.00 29.44  ? 51  ASP A CA  1 
ATOM   426  C  C   . ASP A 1 51  ? 0.015   3.274   35.836 1.00 31.84  ? 51  ASP A C   1 
ATOM   427  O  O   . ASP A 1 51  ? 0.774   3.685   36.707 1.00 29.84  ? 51  ASP A O   1 
ATOM   428  C  CB  . ASP A 1 51  ? -1.739  2.219   37.279 1.00 33.90  ? 51  ASP A CB  1 
ATOM   429  C  CG  . ASP A 1 51  ? -3.175  2.232   37.783 1.00 34.20  ? 51  ASP A CG  1 
ATOM   430  O  OD1 . ASP A 1 51  ? -3.749  1.141   38.029 1.00 32.92  ? 51  ASP A OD1 1 
ATOM   431  O  OD2 . ASP A 1 51  ? -3.741  3.339   37.793 1.00 32.65  ? 51  ASP A OD2 1 
ATOM   432  N  N   . TYR A 1 52  ? 0.479   2.800   34.665 1.00 31.20  ? 52  TYR A N   1 
ATOM   433  C  CA  . TYR A 1 52  ? 1.882   2.872   34.293 1.00 29.47  ? 52  TYR A CA  1 
ATOM   434  C  C   . TYR A 1 52  ? 2.370   4.303   34.429 1.00 29.19  ? 52  TYR A C   1 
ATOM   435  O  O   . TYR A 1 52  ? 1.672   5.214   33.995 1.00 27.59  ? 52  TYR A O   1 
ATOM   436  C  CB  . TYR A 1 52  ? 2.057   2.354   32.874 1.00 30.37  ? 52  TYR A CB  1 
ATOM   437  C  CG  . TYR A 1 52  ? 3.437   2.405   32.234 1.00 35.81  ? 52  TYR A CG  1 
ATOM   438  C  CD1 . TYR A 1 52  ? 3.676   3.232   31.132 1.00 34.22  ? 52  TYR A CD1 1 
ATOM   439  C  CD2 . TYR A 1 52  ? 4.475   1.577   32.664 1.00 38.10  ? 52  TYR A CD2 1 
ATOM   440  C  CE1 . TYR A 1 52  ? 4.909   3.255   30.505 1.00 33.78  ? 52  TYR A CE1 1 
ATOM   441  C  CE2 . TYR A 1 52  ? 5.703   1.572   32.020 1.00 37.97  ? 52  TYR A CE2 1 
ATOM   442  C  CZ  . TYR A 1 52  ? 5.921   2.430   30.950 1.00 35.84  ? 52  TYR A CZ  1 
ATOM   443  O  OH  . TYR A 1 52  ? 7.106   2.465   30.302 1.00 35.02  ? 52  TYR A OH  1 
ATOM   444  N  N   . LYS A 1 53  ? 3.633   4.456   34.865 1.00 30.66  ? 53  LYS A N   1 
ATOM   445  C  CA  A LYS A 1 53  ? 4.192   5.761   35.188 0.50 33.75  ? 53  LYS A CA  1 
ATOM   446  C  CA  B LYS A 1 53  ? 4.173   5.769   35.192 0.50 33.44  ? 53  LYS A CA  1 
ATOM   447  C  C   . LYS A 1 53  ? 4.252   6.646   33.940 1.00 29.74  ? 53  LYS A C   1 
ATOM   448  O  O   . LYS A 1 53  ? 4.071   7.857   34.033 1.00 30.47  ? 53  LYS A O   1 
ATOM   449  C  CB  A LYS A 1 53  ? 5.594   5.645   35.808 0.50 35.46  ? 53  LYS A CB  1 
ATOM   450  C  CB  B LYS A 1 53  ? 5.549   5.666   35.868 0.50 34.79  ? 53  LYS A CB  1 
ATOM   451  C  CG  A LYS A 1 53  ? 6.666   5.027   34.904 0.50 40.36  ? 53  LYS A CG  1 
ATOM   452  C  CG  B LYS A 1 53  ? 6.308   6.975   36.094 0.50 38.77  ? 53  LYS A CG  1 
ATOM   453  C  CD  A LYS A 1 53  ? 7.942   4.518   35.572 0.50 42.79  ? 53  LYS A CD  1 
ATOM   454  C  CD  B LYS A 1 53  ? 7.620   6.771   36.852 0.50 41.62  ? 53  LYS A CD  1 
ATOM   455  C  CE  A LYS A 1 53  ? 8.739   3.639   34.657 0.50 42.41  ? 53  LYS A CE  1 
ATOM   456  C  CE  B LYS A 1 53  ? 8.381   8.037   37.092 0.50 44.29  ? 53  LYS A CE  1 
ATOM   457  N  NZ  A LYS A 1 53  ? 10.134  3.525   35.096 0.50 45.82  ? 53  LYS A NZ  1 
ATOM   458  N  NZ  B LYS A 1 53  ? 9.734   7.726   37.554 0.50 46.30  ? 53  LYS A NZ  1 
ATOM   459  N  N   . HIS A 1 54  ? 4.505   6.051   32.764 1.00 28.66  ? 54  HIS A N   1 
ATOM   460  C  CA  . HIS A 1 54  ? 4.598   6.881   31.562 1.00 29.58  ? 54  HIS A CA  1 
ATOM   461  C  C   . HIS A 1 54  ? 3.331   6.775   30.704 1.00 31.48  ? 54  HIS A C   1 
ATOM   462  O  O   . HIS A 1 54  ? 3.346   7.166   29.538 1.00 34.25  ? 54  HIS A O   1 
ATOM   463  C  CB  . HIS A 1 54  ? 5.892   6.625   30.784 1.00 32.31  ? 54  HIS A CB  1 
ATOM   464  C  CG  . HIS A 1 54  ? 7.134   6.714   31.575 1.00 40.17  ? 54  HIS A CG  1 
ATOM   465  N  ND1 . HIS A 1 54  ? 7.538   7.836   32.267 1.00 41.46  ? 54  HIS A ND1 1 
ATOM   466  C  CD2 . HIS A 1 54  ? 8.065   5.766   31.807 1.00 41.85  ? 54  HIS A CD2 1 
ATOM   467  C  CE1 . HIS A 1 54  ? 8.685   7.573   32.893 1.00 38.46  ? 54  HIS A CE1 1 
ATOM   468  N  NE2 . HIS A 1 54  ? 9.031   6.328   32.605 1.00 42.33  ? 54  HIS A NE2 1 
ATOM   469  N  N   . TRP A 1 55  ? 2.205   6.348   31.284 1.00 29.36  ? 55  TRP A N   1 
ATOM   470  C  CA  . TRP A 1 55  ? 0.984   6.206   30.492 1.00 28.12  ? 55  TRP A CA  1 
ATOM   471  C  C   . TRP A 1 55  ? 0.611   7.501   29.753 1.00 27.18  ? 55  TRP A C   1 
ATOM   472  O  O   . TRP A 1 55  ? 0.283   7.451   28.580 1.00 26.78  ? 55  TRP A O   1 
ATOM   473  C  CB  . TRP A 1 55  ? -0.198  5.686   31.325 1.00 26.51  ? 55  TRP A CB  1 
ATOM   474  C  CG  . TRP A 1 55  ? -1.448  5.604   30.485 1.00 24.36  ? 55  TRP A CG  1 
ATOM   475  C  CD1 . TRP A 1 55  ? -2.556  6.403   30.520 1.00 24.09  ? 55  TRP A CD1 1 
ATOM   476  C  CD2 . TRP A 1 55  ? -1.651  4.695   29.381 1.00 25.94  ? 55  TRP A CD2 1 
ATOM   477  N  NE1 . TRP A 1 55  ? -3.435  6.047   29.530 1.00 26.42  ? 55  TRP A NE1 1 
ATOM   478  C  CE2 . TRP A 1 55  ? -2.900  5.007   28.809 1.00 25.14  ? 55  TRP A CE2 1 
ATOM   479  C  CE3 . TRP A 1 55  ? -0.878  3.685   28.805 1.00 25.35  ? 55  TRP A CE3 1 
ATOM   480  C  CZ2 . TRP A 1 55  ? -3.394  4.311   27.719 1.00 24.85  ? 55  TRP A CZ2 1 
ATOM   481  C  CZ3 . TRP A 1 55  ? -1.361  3.020   27.703 1.00 27.43  ? 55  TRP A CZ3 1 
ATOM   482  C  CH2 . TRP A 1 55  ? -2.590  3.356   27.153 1.00 25.64  ? 55  TRP A CH2 1 
ATOM   483  N  N   . PRO A 1 56  ? 0.593   8.695   30.387 1.00 24.76  ? 56  PRO A N   1 
ATOM   484  C  CA  . PRO A 1 56  ? 0.233   9.901   29.646 1.00 26.49  ? 56  PRO A CA  1 
ATOM   485  C  C   . PRO A 1 56  ? 1.055   10.170  28.390 1.00 28.87  ? 56  PRO A C   1 
ATOM   486  O  O   . PRO A 1 56  ? 0.538   10.735  27.422 1.00 29.56  ? 56  PRO A O   1 
ATOM   487  C  CB  . PRO A 1 56  ? 0.382   11.027  30.694 1.00 25.65  ? 56  PRO A CB  1 
ATOM   488  C  CG  . PRO A 1 56  ? 0.204   10.301  32.021 1.00 28.94  ? 56  PRO A CG  1 
ATOM   489  C  CD  . PRO A 1 56  ? 0.819   8.929   31.831 1.00 25.59  ? 56  PRO A CD  1 
ATOM   490  N  N   . GLN A 1 57  ? 2.342   9.803   28.407 1.00 28.43  ? 57  GLN A N   1 
ATOM   491  C  CA  . GLN A 1 57  ? 3.191   10.055  27.246 1.00 33.08  ? 57  GLN A CA  1 
ATOM   492  C  C   . GLN A 1 57  ? 2.918   9.039   26.120 1.00 28.19  ? 57  GLN A C   1 
ATOM   493  O  O   . GLN A 1 57  ? 3.330   9.241   24.985 1.00 27.46  ? 57  GLN A O   1 
ATOM   494  C  CB  . GLN A 1 57  ? 4.678   10.108  27.634 1.00 31.91  ? 57  GLN A CB  1 
ATOM   495  C  CG  . GLN A 1 57  ? 5.047   11.284  28.544 1.00 33.15  ? 57  GLN A CG  1 
ATOM   496  C  CD  . GLN A 1 57  ? 4.464   11.193  29.954 1.00 37.66  ? 57  GLN A CD  1 
ATOM   497  O  OE1 . GLN A 1 57  ? 4.476   10.142  30.601 1.00 33.77  ? 57  GLN A OE1 1 
ATOM   498  N  NE2 . GLN A 1 57  ? 3.891   12.275  30.459 1.00 34.30  ? 57  GLN A NE2 1 
ATOM   499  N  N   . ILE A 1 58  ? 2.257   7.925   26.439 1.00 25.39  ? 58  ILE A N   1 
ATOM   500  C  CA  . ILE A 1 58  ? 1.772   7.025   25.396 1.00 26.39  ? 58  ILE A CA  1 
ATOM   501  C  C   . ILE A 1 58  ? 0.386   7.479   24.906 1.00 24.08  ? 58  ILE A C   1 
ATOM   502  O  O   . ILE A 1 58  ? 0.129   7.549   23.711 1.00 25.33  ? 58  ILE A O   1 
ATOM   503  C  CB  . ILE A 1 58  ? 1.738   5.583   25.912 1.00 24.80  ? 58  ILE A CB  1 
ATOM   504  C  CG1 . ILE A 1 58  ? 3.116   5.055   26.156 1.00 27.46  ? 58  ILE A CG1 1 
ATOM   505  C  CG2 . ILE A 1 58  ? 0.958   4.681   24.952 1.00 26.32  ? 58  ILE A CG2 1 
ATOM   506  C  CD1 . ILE A 1 58  ? 3.132   3.849   27.080 1.00 31.03  ? 58  ILE A CD1 1 
ATOM   507  N  N   . ALA A 1 59  ? -0.512  7.798   25.844 1.00 25.16  ? 59  ALA A N   1 
ATOM   508  C  CA  . ALA A 1 59  ? -1.891  8.147   25.551 1.00 26.89  ? 59  ALA A CA  1 
ATOM   509  C  C   . ALA A 1 59  ? -1.976  9.420   24.699 1.00 27.26  ? 59  ALA A C   1 
ATOM   510  O  O   . ALA A 1 59  ? -2.971  9.632   24.029 1.00 27.19  ? 59  ALA A O   1 
ATOM   511  C  CB  . ALA A 1 59  ? -2.670  8.307   26.855 1.00 27.65  ? 59  ALA A CB  1 
ATOM   512  N  N   . GLN A 1 60  ? -0.926  10.240  24.658 1.00 26.13  ? 60  GLN A N   1 
ATOM   513  C  CA  . GLN A 1 60  ? -1.016  11.449  23.838 1.00 26.87  ? 60  GLN A CA  1 
ATOM   514  C  C   . GLN A 1 60  ? -1.064  11.098  22.346 1.00 25.06  ? 60  GLN A C   1 
ATOM   515  O  O   . GLN A 1 60  ? -1.318  11.969  21.508 1.00 24.48  ? 60  GLN A O   1 
ATOM   516  C  CB  . GLN A 1 60  ? 0.177   12.342  24.123 1.00 26.54  ? 60  GLN A CB  1 
ATOM   517  C  CG  . GLN A 1 60  ? 1.485   11.813  23.520 1.00 29.06  ? 60  GLN A CG  1 
ATOM   518  C  CD  . GLN A 1 60  ? 2.685   12.636  23.908 1.00 32.79  ? 60  GLN A CD  1 
ATOM   519  O  OE1 . GLN A 1 60  ? 2.722   13.833  23.630 1.00 33.63  ? 60  GLN A OE1 1 
ATOM   520  N  NE2 . GLN A 1 60  ? 3.646   12.014  24.572 1.00 29.39  ? 60  GLN A NE2 1 
ATOM   521  N  N   . PHE A 1 61  ? -0.818  9.832   22.005 1.00 24.06  ? 61  PHE A N   1 
ATOM   522  C  CA  . PHE A 1 61  ? -0.861  9.422   20.604 1.00 26.02  ? 61  PHE A CA  1 
ATOM   523  C  C   . PHE A 1 61  ? -2.172  8.717   20.244 1.00 27.00  ? 61  PHE A C   1 
ATOM   524  O  O   . PHE A 1 61  ? -2.404  8.406   19.072 1.00 28.36  ? 61  PHE A O   1 
ATOM   525  C  CB  . PHE A 1 61  ? 0.335   8.512   20.280 1.00 26.61  ? 61  PHE A CB  1 
ATOM   526  C  CG  . PHE A 1 61  ? 1.672   9.232   20.403 1.00 25.11  ? 61  PHE A CG  1 
ATOM   527  C  CD1 . PHE A 1 61  ? 2.009   10.274  19.546 1.00 27.25  ? 61  PHE A CD1 1 
ATOM   528  C  CD2 . PHE A 1 61  ? 2.564   8.909   21.425 1.00 26.41  ? 61  PHE A CD2 1 
ATOM   529  C  CE1 . PHE A 1 61  ? 3.166   11.017  19.745 1.00 29.22  ? 61  PHE A CE1 1 
ATOM   530  C  CE2 . PHE A 1 61  ? 3.759   9.599   21.562 1.00 27.18  ? 61  PHE A CE2 1 
ATOM   531  C  CZ  . PHE A 1 61  ? 4.055   10.655  20.740 1.00 26.36  ? 61  PHE A CZ  1 
ATOM   532  N  N   . ALA A 1 62  ? -2.985  8.368   21.262 1.00 26.99  ? 62  ALA A N   1 
ATOM   533  C  CA  . ALA A 1 62  ? -4.245  7.670   21.034 1.00 27.14  ? 62  ALA A CA  1 
ATOM   534  C  C   . ALA A 1 62  ? -5.263  8.663   20.490 1.00 28.27  ? 62  ALA A C   1 
ATOM   535  O  O   . ALA A 1 62  ? -5.313  9.843   20.901 1.00 26.78  ? 62  ALA A O   1 
ATOM   536  C  CB  . ALA A 1 62  ? -4.759  7.010   22.294 1.00 25.95  ? 62  ALA A CB  1 
ATOM   537  N  N   . PRO A 1 63  ? -6.046  8.250   19.478 1.00 26.54  ? 63  PRO A N   1 
ATOM   538  C  CA  . PRO A 1 63  ? -6.998  9.166   18.840 1.00 25.33  ? 63  PRO A CA  1 
ATOM   539  C  C   . PRO A 1 63  ? -8.282  9.387   19.638 1.00 26.26  ? 63  PRO A C   1 
ATOM   540  O  O   . PRO A 1 63  ? -8.789  8.485   20.293 1.00 23.40  ? 63  PRO A O   1 
ATOM   541  C  CB  . PRO A 1 63  ? -7.268  8.466   17.511 1.00 26.85  ? 63  PRO A CB  1 
ATOM   542  C  CG  . PRO A 1 63  ? -7.172  6.993   17.879 1.00 25.43  ? 63  PRO A CG  1 
ATOM   543  C  CD  . PRO A 1 63  ? -6.003  6.922   18.839 1.00 25.87  ? 63  PRO A CD  1 
ATOM   544  N  N   . SER A 1 64  ? -8.781  10.627  19.614 1.00 28.36  ? 64  SER A N   1 
ATOM   545  C  CA  . SER A 1 64  ? -10.154 10.921  20.001 1.00 31.71  ? 64  SER A CA  1 
ATOM   546  C  C   . SER A 1 64  ? -11.102 10.078  19.153 1.00 27.82  ? 64  SER A C   1 
ATOM   547  O  O   . SER A 1 64  ? -10.727 9.592   18.081 1.00 25.55  ? 64  SER A O   1 
ATOM   548  C  CB  . SER A 1 64  ? -10.452 12.384  19.828 1.00 32.68  ? 64  SER A CB  1 
ATOM   549  O  OG  . SER A 1 64  ? -10.398 12.770  18.454 1.00 27.87  ? 64  SER A OG  1 
ATOM   550  N  N   . ALA A 1 65  ? -12.359 9.954   19.577 1.00 24.48  ? 65  ALA A N   1 
ATOM   551  C  CA  . ALA A 1 65  ? -13.328 9.246   18.754 1.00 27.67  ? 65  ALA A CA  1 
ATOM   552  C  C   . ALA A 1 65  ? -13.473 9.937   17.387 1.00 24.62  ? 65  ALA A C   1 
ATOM   553  O  O   . ALA A 1 65  ? -13.568 9.257   16.376 1.00 24.05  ? 65  ALA A O   1 
ATOM   554  C  CB  . ALA A 1 65  ? -14.642 9.094   19.481 1.00 32.78  ? 65  ALA A CB  1 
ATOM   555  N  N   . SER A 1 66  ? -13.463 11.271  17.352 1.00 22.43  ? 66  SER A N   1 
ATOM   556  C  CA  . SER A 1 66  ? -13.619 12.010  16.119 1.00 25.08  ? 66  SER A CA  1 
ATOM   557  C  C   . SER A 1 66  ? -12.450 11.709  15.174 1.00 32.14  ? 66  SER A C   1 
ATOM   558  O  O   . SER A 1 66  ? -12.650 11.401  13.991 1.00 26.65  ? 66  SER A O   1 
ATOM   559  C  CB  . SER A 1 66  ? -13.712 13.504  16.429 1.00 27.30  ? 66  SER A CB  1 
ATOM   560  O  OG  . SER A 1 66  ? -13.864 14.303  15.266 1.00 28.63  ? 66  SER A OG  1 
ATOM   561  N  N   . ALA A 1 67  ? -11.214 11.746  15.724 1.00 26.59  ? 67  ALA A N   1 
ATOM   562  C  CA  . ALA A 1 67  ? -10.016 11.489  14.953 1.00 26.77  ? 67  ALA A CA  1 
ATOM   563  C  C   . ALA A 1 67  ? -9.922  10.014  14.550 1.00 25.72  ? 67  ALA A C   1 
ATOM   564  O  O   . ALA A 1 67  ? -9.365  9.687   13.504 1.00 25.73  ? 67  ALA A O   1 
ATOM   565  C  CB  . ALA A 1 67  ? -8.794  11.905  15.745 1.00 28.08  ? 67  ALA A CB  1 
ATOM   566  N  N   . PHE A 1 68  ? -10.418 9.122   15.391 1.00 23.60  ? 68  PHE A N   1 
ATOM   567  C  CA  . PHE A 1 68  ? -10.361 7.712   15.062 1.00 22.29  ? 68  PHE A CA  1 
ATOM   568  C  C   . PHE A 1 68  ? -11.172 7.440   13.792 1.00 25.74  ? 68  PHE A C   1 
ATOM   569  O  O   . PHE A 1 68  ? -10.695 6.736   12.874 1.00 26.87  ? 68  PHE A O   1 
ATOM   570  C  CB  . PHE A 1 68  ? -10.858 6.885   16.247 1.00 24.75  ? 68  PHE A CB  1 
ATOM   571  C  CG  . PHE A 1 68  ? -10.979 5.405   15.919 1.00 22.84  ? 68  PHE A CG  1 
ATOM   572  C  CD1 . PHE A 1 68  ? -9.875  4.585   15.966 1.00 25.98  ? 68  PHE A CD1 1 
ATOM   573  C  CD2 . PHE A 1 68  ? -12.195 4.841   15.552 1.00 25.34  ? 68  PHE A CD2 1 
ATOM   574  C  CE1 . PHE A 1 68  ? -9.973  3.207   15.679 1.00 26.93  ? 68  PHE A CE1 1 
ATOM   575  C  CE2 . PHE A 1 68  ? -12.281 3.466   15.264 1.00 25.98  ? 68  PHE A CE2 1 
ATOM   576  C  CZ  . PHE A 1 68  ? -11.150 2.669   15.310 1.00 25.80  ? 68  PHE A CZ  1 
ATOM   577  N  N   . PHE A 1 69  ? -12.392 7.980   13.740 1.00 25.14  ? 69  PHE A N   1 
ATOM   578  C  CA  . PHE A 1 69  ? -13.238 7.801   12.563 1.00 26.96  ? 69  PHE A CA  1 
ATOM   579  C  C   . PHE A 1 69  ? -12.829 8.768   11.440 1.00 28.37  ? 69  PHE A C   1 
ATOM   580  O  O   . PHE A 1 69  ? -13.206 8.525   10.305 1.00 26.20  ? 69  PHE A O   1 
ATOM   581  C  CB  . PHE A 1 69  ? -14.746 7.905   12.894 1.00 24.39  ? 69  PHE A CB  1 
ATOM   582  C  CG  . PHE A 1 69  ? -15.264 6.595   13.450 1.00 23.58  ? 69  PHE A CG  1 
ATOM   583  C  CD1 . PHE A 1 69  ? -15.502 6.423   14.805 1.00 25.61  ? 69  PHE A CD1 1 
ATOM   584  C  CD2 . PHE A 1 69  ? -15.480 5.525   12.603 1.00 23.79  ? 69  PHE A CD2 1 
ATOM   585  C  CE1 . PHE A 1 69  ? -15.887 5.189   15.299 1.00 26.28  ? 69  PHE A CE1 1 
ATOM   586  C  CE2 . PHE A 1 69  ? -15.919 4.307   13.100 1.00 26.66  ? 69  PHE A CE2 1 
ATOM   587  C  CZ  . PHE A 1 69  ? -16.118 4.136   14.449 1.00 25.91  ? 69  PHE A CZ  1 
ATOM   588  N  N   . GLY A 1 70  ? -12.125 9.862   11.760 1.00 27.84  ? 70  GLY A N   1 
ATOM   589  C  CA  . GLY A 1 70  ? -11.741 10.873  10.779 1.00 27.13  ? 70  GLY A CA  1 
ATOM   590  C  C   . GLY A 1 70  ? -10.433 10.550  10.041 1.00 31.07  ? 70  GLY A C   1 
ATOM   591  O  O   . GLY A 1 70  ? -10.288 10.818  8.845  1.00 27.67  ? 70  GLY A O   1 
ATOM   592  N  N   . MET A 1 71  ? -9.462  9.959   10.747 1.00 30.49  ? 71  MET A N   1 
ATOM   593  C  CA  . MET A 1 71  ? -8.134  9.711   10.199 1.00 29.51  ? 71  MET A CA  1 
ATOM   594  C  C   . MET A 1 71  ? -8.022  8.297   9.636  1.00 27.08  ? 71  MET A C   1 
ATOM   595  O  O   . MET A 1 71  ? -7.200  8.066   8.767  1.00 30.37  ? 71  MET A O   1 
ATOM   596  C  CB  . MET A 1 71  ? -7.049  9.829   11.275 1.00 29.80  ? 71  MET A CB  1 
ATOM   597  C  CG  . MET A 1 71  ? -6.942  11.199  11.917 1.00 28.43  ? 71  MET A CG  1 
ATOM   598  S  SD  . MET A 1 71  ? -5.577  11.239  13.092 1.00 28.75  ? 71  MET A SD  1 
ATOM   599  C  CE  . MET A 1 71  ? -5.802  9.665   13.953 1.00 34.65  ? 71  MET A CE  1 
ATOM   600  N  N   . SER A 1 72  ? -8.759  7.331   10.169 1.00 25.16  ? 72  SER A N   1 
ATOM   601  C  CA  . SER A 1 72  ? -8.478  5.939   9.834  1.00 25.68  ? 72  SER A CA  1 
ATOM   602  C  C   . SER A 1 72  ? -9.124  5.510   8.514  1.00 26.76  ? 72  SER A C   1 
ATOM   603  O  O   . SER A 1 72  ? -10.107 6.073   8.086  1.00 27.44  ? 72  SER A O   1 
ATOM   604  C  CB  . SER A 1 72  ? -8.939  4.998   10.937 1.00 25.98  ? 72  SER A CB  1 
ATOM   605  O  OG  . SER A 1 72  ? -8.557  5.465   12.227 1.00 28.14  ? 72  SER A OG  1 
ATOM   606  N  N   . ARG A 1 73  ? -8.654  4.386   7.976  1.00 29.02  ? 73  ARG A N   1 
ATOM   607  C  CA  . ARG A 1 73  ? -9.366  3.627   6.979  1.00 26.44  ? 73  ARG A CA  1 
ATOM   608  C  C   . ARG A 1 73  ? -10.202 2.564   7.671  1.00 29.88  ? 73  ARG A C   1 
ATOM   609  O  O   . ARG A 1 73  ? -9.675  1.650   8.307  1.00 28.86  ? 73  ARG A O   1 
ATOM   610  C  CB  . ARG A 1 73  ? -8.359  3.019   6.001  1.00 28.56  ? 73  ARG A CB  1 
ATOM   611  C  CG  . ARG A 1 73  ? -7.625  4.128   5.255  1.00 30.34  ? 73  ARG A CG  1 
ATOM   612  C  CD  . ARG A 1 73  ? -6.988  3.483   4.003  1.00 35.05  ? 73  ARG A CD  1 
ATOM   613  N  NE  . ARG A 1 73  ? -7.941  3.079   2.964  1.00 28.36  ? 73  ARG A NE  1 
ATOM   614  C  CZ  . ARG A 1 73  ? -8.687  3.917   2.255  1.00 29.31  ? 73  ARG A CZ  1 
ATOM   615  N  NH1 . ARG A 1 73  ? -9.658  3.406   1.534  1.00 32.84  ? 73  ARG A NH1 1 
ATOM   616  N  NH2 . ARG A 1 73  ? -8.538  5.231   2.320  1.00 28.75  ? 73  ARG A NH2 1 
ATOM   617  N  N   . ILE A 1 74  ? -11.527 2.717   7.511  1.00 26.46  ? 74  ILE A N   1 
ATOM   618  C  CA  . ILE A 1 74  ? -12.501 1.900   8.194  1.00 29.10  ? 74  ILE A CA  1 
ATOM   619  C  C   . ILE A 1 74  ? -13.081 0.927   7.178  1.00 31.65  ? 74  ILE A C   1 
ATOM   620  O  O   . ILE A 1 74  ? -13.454 1.341   6.091  1.00 32.48  ? 74  ILE A O   1 
ATOM   621  C  CB  . ILE A 1 74  ? -13.589 2.800   8.799  1.00 27.14  ? 74  ILE A CB  1 
ATOM   622  C  CG1 . ILE A 1 74  ? -13.012 3.849   9.798  1.00 26.27  ? 74  ILE A CG1 1 
ATOM   623  C  CG2 . ILE A 1 74  ? -14.698 1.947   9.420  1.00 26.62  ? 74  ILE A CG2 1 
ATOM   624  C  CD1 . ILE A 1 74  ? -12.440 3.215   11.054 1.00 28.96  ? 74  ILE A CD1 1 
ATOM   625  N  N   . GLY A 1 75  ? -13.224 -0.319  7.591  1.00 30.75  ? 75  GLY A N   1 
ATOM   626  C  CA  . GLY A 1 75  ? -13.858 -1.323  6.773  1.00 35.49  ? 75  GLY A CA  1 
ATOM   627  C  C   . GLY A 1 75  ? -14.710 -2.236  7.641  1.00 39.30  ? 75  GLY A C   1 
ATOM   628  O  O   . GLY A 1 75  ? -14.795 -2.075  8.861  1.00 32.33  ? 75  GLY A O   1 
ATOM   629  N  N   . MET A 1 76  ? -15.393 -3.160  6.976  1.00 44.71  ? 76  MET A N   1 
ATOM   630  C  CA  . MET A 1 76  ? -16.201 -4.153  7.655  1.00 48.48  ? 76  MET A CA  1 
ATOM   631  C  C   . MET A 1 76  ? -15.877 -5.512  7.063  1.00 48.25  ? 76  MET A C   1 
ATOM   632  O  O   . MET A 1 76  ? -15.760 -5.636  5.856  1.00 60.14  ? 76  MET A O   1 
ATOM   633  C  CB  . MET A 1 76  ? -17.700 -3.836  7.556  1.00 52.53  ? 76  MET A CB  1 
ATOM   634  C  CG  . MET A 1 76  ? -18.321 -3.551  8.912  1.00 63.89  ? 76  MET A CG  1 
ATOM   635  S  SD  . MET A 1 76  ? -20.101 -3.733  8.812  1.00 64.00  ? 76  MET A SD  1 
ATOM   636  C  CE  . MET A 1 76  ? -20.362 -1.961  8.663  1.00 62.94  ? 76  MET A CE  1 
ATOM   637  N  N   . GLU A 1 77  ? -15.698 -6.507  7.925  1.00 45.56  ? 77  GLU A N   1 
ATOM   638  C  CA  . GLU A 1 77  ? -15.389 -7.841  7.469  1.00 56.39  ? 77  GLU A CA  1 
ATOM   639  C  C   . GLU A 1 77  ? -16.285 -8.829  8.195  1.00 60.08  ? 77  GLU A C   1 
ATOM   640  O  O   . GLU A 1 77  ? -16.335 -8.826  9.421  1.00 46.54  ? 77  GLU A O   1 
ATOM   641  C  CB  . GLU A 1 77  ? -13.921 -8.164  7.713  1.00 66.92  ? 77  GLU A CB  1 
ATOM   642  C  CG  . GLU A 1 77  ? -13.031 -7.673  6.577  1.00 85.03  ? 77  GLU A CG  1 
ATOM   643  C  CD  . GLU A 1 77  ? -11.687 -8.370  6.552  1.00 101.64 ? 77  GLU A CD  1 
ATOM   644  O  OE1 . GLU A 1 77  ? -10.966 -8.181  5.554  1.00 114.22 ? 77  GLU A OE1 1 
ATOM   645  O  OE2 . GLU A 1 77  ? -11.362 -9.084  7.530  1.00 111.78 ? 77  GLU A OE2 1 
ATOM   646  N  N   . VAL A 1 78  ? -16.978 -9.659  7.412  1.00 57.32  ? 78  VAL A N   1 
ATOM   647  C  CA  . VAL A 1 78  ? -17.901 -10.646 7.939  1.00 60.95  ? 78  VAL A CA  1 
ATOM   648  C  C   . VAL A 1 78  ? -17.294 -12.031 7.756  1.00 59.77  ? 78  VAL A C   1 
ATOM   649  O  O   . VAL A 1 78  ? -16.860 -12.368 6.671  1.00 60.26  ? 78  VAL A O   1 
ATOM   650  C  CB  . VAL A 1 78  ? -19.246 -10.516 7.205  1.00 59.99  ? 78  VAL A CB  1 
ATOM   651  C  CG1 . VAL A 1 78  ? -20.271 -11.513 7.731  1.00 62.15  ? 78  VAL A CG1 1 
ATOM   652  C  CG2 . VAL A 1 78  ? -19.776 -9.089  7.265  1.00 53.59  ? 78  VAL A CG2 1 
ATOM   653  N  N   . THR A 1 79  ? -17.269 -12.832 8.821  1.00 67.71  ? 79  THR A N   1 
ATOM   654  C  CA  . THR A 1 79  ? -16.594 -14.113 8.785  1.00 68.46  ? 79  THR A CA  1 
ATOM   655  C  C   . THR A 1 79  ? -17.403 -15.068 9.646  1.00 74.86  ? 79  THR A C   1 
ATOM   656  O  O   . THR A 1 79  ? -18.286 -14.639 10.392 1.00 63.91  ? 79  THR A O   1 
ATOM   657  C  CB  . THR A 1 79  ? -15.165 -13.990 9.314  1.00 76.88  ? 79  THR A CB  1 
ATOM   658  O  OG1 . THR A 1 79  ? -15.249 -14.054 10.733 1.00 68.63  ? 79  THR A OG1 1 
ATOM   659  C  CG2 . THR A 1 79  ? -14.471 -12.694 8.927  1.00 77.18  ? 79  THR A CG2 1 
ATOM   660  N  N   . PRO A 1 80  ? -17.102 -16.380 9.608  1.00 82.78  ? 80  PRO A N   1 
ATOM   661  C  CA  . PRO A 1 80  ? -17.811 -17.319 10.474 1.00 82.32  ? 80  PRO A CA  1 
ATOM   662  C  C   . PRO A 1 80  ? -17.721 -16.982 11.963 1.00 75.14  ? 80  PRO A C   1 
ATOM   663  O  O   . PRO A 1 80  ? -18.549 -17.456 12.731 1.00 74.75  ? 80  PRO A O   1 
ATOM   664  C  CB  . PRO A 1 80  ? -17.209 -18.700 10.130 1.00 86.98  ? 80  PRO A CB  1 
ATOM   665  C  CG  . PRO A 1 80  ? -15.980 -18.411 9.273  1.00 88.36  ? 80  PRO A CG  1 
ATOM   666  C  CD  . PRO A 1 80  ? -16.146 -17.022 8.691  1.00 82.90  ? 80  PRO A CD  1 
ATOM   667  N  N   . SER A 1 81  ? -16.728 -16.173 12.370 1.00 79.32  ? 81  SER A N   1 
ATOM   668  C  CA  . SER A 1 81  ? -16.598 -15.765 13.765 1.00 84.73  ? 81  SER A CA  1 
ATOM   669  C  C   . SER A 1 81  ? -17.501 -14.572 14.112 1.00 76.61  ? 81  SER A C   1 
ATOM   670  O  O   . SER A 1 81  ? -17.831 -14.377 15.280 1.00 74.70  ? 81  SER A O   1 
ATOM   671  C  CB  . SER A 1 81  ? -15.141 -15.479 14.131 1.00 85.19  ? 81  SER A CB  1 
ATOM   672  O  OG  . SER A 1 81  ? -14.571 -14.391 13.401 1.00 83.67  ? 81  SER A OG  1 
ATOM   673  N  N   . GLY A 1 82  ? -17.866 -13.748 13.118 1.00 64.71  ? 82  GLY A N   1 
ATOM   674  C  CA  . GLY A 1 82  ? -18.675 -12.570 13.378 1.00 52.73  ? 82  GLY A CA  1 
ATOM   675  C  C   . GLY A 1 82  ? -18.378 -11.444 12.399 1.00 45.34  ? 82  GLY A C   1 
ATOM   676  O  O   . GLY A 1 82  ? -17.807 -11.669 11.350 1.00 48.72  ? 82  GLY A O   1 
ATOM   677  N  N   . THR A 1 83  ? -18.832 -10.240 12.756 1.00 44.30  ? 83  THR A N   1 
ATOM   678  C  CA  . THR A 1 83  ? -18.674 -9.038  11.959 1.00 41.11  ? 83  THR A CA  1 
ATOM   679  C  C   . THR A 1 83  ? -17.697 -8.123  12.703 1.00 41.93  ? 83  THR A C   1 
ATOM   680  O  O   . THR A 1 83  ? -17.874 -7.902  13.894 1.00 38.76  ? 83  THR A O   1 
ATOM   681  C  CB  . THR A 1 83  ? -20.048 -8.390  11.749 1.00 43.47  ? 83  THR A CB  1 
ATOM   682  O  OG1 . THR A 1 83  ? -20.884 -9.336  11.094 1.00 45.95  ? 83  THR A OG1 1 
ATOM   683  C  CG2 . THR A 1 83  ? -20.008 -7.125  10.910 1.00 40.99  ? 83  THR A CG2 1 
ATOM   684  N  N   . TRP A 1 84  ? -16.703 -7.576  11.973 1.00 42.52  ? 84  TRP A N   1 
ATOM   685  C  CA  . TRP A 1 84  ? -15.616 -6.777  12.513 1.00 38.70  ? 84  TRP A CA  1 
ATOM   686  C  C   . TRP A 1 84  ? -15.581 -5.432  11.806 1.00 32.77  ? 84  TRP A C   1 
ATOM   687  O  O   . TRP A 1 84  ? -15.737 -5.361  10.604 1.00 31.87  ? 84  TRP A O   1 
ATOM   688  C  CB  . TRP A 1 84  ? -14.275 -7.486  12.316 1.00 44.47  ? 84  TRP A CB  1 
ATOM   689  C  CG  . TRP A 1 84  ? -14.256 -8.893  12.843 1.00 44.12  ? 84  TRP A CG  1 
ATOM   690  C  CD1 . TRP A 1 84  ? -14.757 -10.011 12.237 1.00 52.81  ? 84  TRP A CD1 1 
ATOM   691  C  CD2 . TRP A 1 84  ? -13.713 -9.322  14.098 1.00 45.87  ? 84  TRP A CD2 1 
ATOM   692  N  NE1 . TRP A 1 84  ? -14.566 -11.107 13.033 1.00 54.98  ? 84  TRP A NE1 1 
ATOM   693  C  CE2 . TRP A 1 84  ? -13.927 -10.713 14.179 1.00 50.38  ? 84  TRP A CE2 1 
ATOM   694  C  CE3 . TRP A 1 84  ? -13.056 -8.670  15.142 1.00 48.54  ? 84  TRP A CE3 1 
ATOM   695  C  CZ2 . TRP A 1 84  ? -13.500 -11.462 15.268 1.00 50.19  ? 84  TRP A CZ2 1 
ATOM   696  C  CZ3 . TRP A 1 84  ? -12.612 -9.415  16.207 1.00 47.43  ? 84  TRP A CZ3 1 
ATOM   697  C  CH2 . TRP A 1 84  ? -12.843 -10.786 16.272 1.00 52.37  ? 84  TRP A CH2 1 
ATOM   698  N  N   . LEU A 1 85  ? -15.440 -4.357  12.574 1.00 29.64  ? 85  LEU A N   1 
ATOM   699  C  CA  . LEU A 1 85  ? -15.048 -3.064  12.033 1.00 27.03  ? 85  LEU A CA  1 
ATOM   700  C  C   . LEU A 1 85  ? -13.518 -3.000  12.073 1.00 30.33  ? 85  LEU A C   1 
ATOM   701  O  O   . LEU A 1 85  ? -12.912 -3.022  13.155 1.00 34.92  ? 85  LEU A O   1 
ATOM   702  C  CB  . LEU A 1 85  ? -15.662 -1.997  12.924 1.00 26.39  ? 85  LEU A CB  1 
ATOM   703  C  CG  . LEU A 1 85  ? -15.459 -0.556  12.496 1.00 28.35  ? 85  LEU A CG  1 
ATOM   704  C  CD1 . LEU A 1 85  ? -16.174 -0.311  11.185 1.00 36.85  ? 85  LEU A CD1 1 
ATOM   705  C  CD2 . LEU A 1 85  ? -15.945 0.390   13.552 1.00 30.91  ? 85  LEU A CD2 1 
ATOM   706  N  N   . THR A 1 86  ? -12.906 -2.878  10.900 1.00 30.68  ? 86  THR A N   1 
ATOM   707  C  CA  . THR A 1 86  ? -11.450 -2.856  10.778 1.00 27.26  ? 86  THR A CA  1 
ATOM   708  C  C   . THR A 1 86  ? -10.986 -1.406  10.704 1.00 25.16  ? 86  THR A C   1 
ATOM   709  O  O   . THR A 1 86  ? -11.696 -0.574  10.159 1.00 26.56  ? 86  THR A O   1 
ATOM   710  C  CB  . THR A 1 86  ? -11.039 -3.619  9.508  1.00 28.10  ? 86  THR A CB  1 
ATOM   711  O  OG1 . THR A 1 86  ? -11.558 -2.891  8.406  1.00 25.46  ? 86  THR A OG1 1 
ATOM   712  C  CG2 . THR A 1 86  ? -11.569 -5.034  9.448  1.00 29.20  ? 86  THR A CG2 1 
ATOM   713  N  N   . TYR A 1 87  ? -9.779  -1.130  11.227 1.00 25.03  ? 87  TYR A N   1 
ATOM   714  C  CA  . TYR A 1 87  ? -9.203  0.203   11.155 1.00 28.24  ? 87  TYR A CA  1 
ATOM   715  C  C   . TYR A 1 87  ? -7.699  0.108   10.909 1.00 26.87  ? 87  TYR A C   1 
ATOM   716  O  O   . TYR A 1 87  ? -7.052  -0.819  11.407 1.00 30.72  ? 87  TYR A O   1 
ATOM   717  C  CB  . TYR A 1 87  ? -9.512  0.989   12.427 1.00 26.56  ? 87  TYR A CB  1 
ATOM   718  C  CG  . TYR A 1 87  ? -9.005  0.328   13.710 1.00 26.01  ? 87  TYR A CG  1 
ATOM   719  C  CD1 . TYR A 1 87  ? -9.768  -0.608  14.393 1.00 27.80  ? 87  TYR A CD1 1 
ATOM   720  C  CD2 . TYR A 1 87  ? -7.763  0.667   14.231 1.00 26.25  ? 87  TYR A CD2 1 
ATOM   721  C  CE1 . TYR A 1 87  ? -9.317  -1.174  15.578 1.00 29.97  ? 87  TYR A CE1 1 
ATOM   722  C  CE2 . TYR A 1 87  ? -7.291  0.083   15.403 1.00 27.15  ? 87  TYR A CE2 1 
ATOM   723  C  CZ  . TYR A 1 87  ? -8.078  -0.814  16.092 1.00 29.58  ? 87  TYR A CZ  1 
ATOM   724  O  OH  . TYR A 1 87  ? -7.538  -1.390  17.203 1.00 25.99  ? 87  TYR A OH  1 
ATOM   725  N  N   . THR A 1 88  ? -7.179  1.072   10.141 1.00 27.67  ? 88  THR A N   1 
ATOM   726  C  CA  . THR A 1 88  ? -5.746  1.224   9.920  1.00 29.07  ? 88  THR A CA  1 
ATOM   727  C  C   . THR A 1 88  ? -5.485  2.709   9.776  1.00 28.78  ? 88  THR A C   1 
ATOM   728  O  O   . THR A 1 88  ? -6.360  3.436   9.325  1.00 28.45  ? 88  THR A O   1 
ATOM   729  C  CB  . THR A 1 88  ? -5.225  0.506   8.667  1.00 30.42  ? 88  THR A CB  1 
ATOM   730  O  OG1 . THR A 1 88  ? -5.801  1.184   7.552  1.00 25.17  ? 88  THR A OG1 1 
ATOM   731  C  CG2 . THR A 1 88  ? -5.704  -0.923  8.506  1.00 28.15  ? 88  THR A CG2 1 
ATOM   732  N  N   . GLY A 1 89  ? -4.252  3.132   10.081 1.00 26.86  ? 89  GLY A N   1 
ATOM   733  C  CA  . GLY A 1 89  ? -3.851  4.514   9.881  1.00 25.33  ? 89  GLY A CA  1 
ATOM   734  C  C   . GLY A 1 89  ? -2.424  4.738   10.357 1.00 24.13  ? 89  GLY A C   1 
ATOM   735  O  O   . GLY A 1 89  ? -1.737  3.801   10.739 1.00 24.91  ? 89  GLY A O   1 
ATOM   736  N  N   . ALA A 1 90  ? -2.026  6.008   10.419 1.00 22.26  ? 90  ALA A N   1 
ATOM   737  C  CA  . ALA A 1 90  ? -0.719  6.380   10.877 1.00 27.64  ? 90  ALA A CA  1 
ATOM   738  C  C   . ALA A 1 90  ? -0.792  7.770   11.491 1.00 28.44  ? 90  ALA A C   1 
ATOM   739  O  O   . ALA A 1 90  ? -1.473  8.619   10.970 1.00 28.58  ? 90  ALA A O   1 
ATOM   740  C  CB  . ALA A 1 90  ? 0.231   6.321   9.692  1.00 29.88  ? 90  ALA A CB  1 
ATOM   741  N  N   . ILE A 1 91  ? -0.116  7.958   12.610 1.00 27.57  ? 91  ILE A N   1 
ATOM   742  C  CA  . ILE A 1 91  ? -0.120  9.208   13.372 1.00 26.42  ? 91  ILE A CA  1 
ATOM   743  C  C   . ILE A 1 91  ? 1.316   9.752   13.380 1.00 29.19  ? 91  ILE A C   1 
ATOM   744  O  O   . ILE A 1 91  ? 2.259   9.074   13.789 1.00 26.13  ? 91  ILE A O   1 
ATOM   745  C  CB  . ILE A 1 91  ? -0.665  8.937   14.798 1.00 27.07  ? 91  ILE A CB  1 
ATOM   746  C  CG1 . ILE A 1 91  ? -2.165  8.702   14.775 1.00 28.98  ? 91  ILE A CG1 1 
ATOM   747  C  CG2 . ILE A 1 91  ? -0.330  10.042  15.796 1.00 30.87  ? 91  ILE A CG2 1 
ATOM   748  C  CD1 . ILE A 1 91  ? -2.630  7.750   15.873 1.00 30.68  ? 91  ILE A CD1 1 
ATOM   749  N  N   . LYS A 1 92  ? 1.471   10.989  12.905 1.00 28.88  ? 92  LYS A N   1 
ATOM   750  C  CA  . LYS A 1 92  ? 2.775   11.592  12.806 1.00 29.92  ? 92  LYS A CA  1 
ATOM   751  C  C   . LYS A 1 92  ? 3.211   12.150  14.163 1.00 28.06  ? 92  LYS A C   1 
ATOM   752  O  O   . LYS A 1 92  ? 2.476   12.906  14.776 1.00 30.34  ? 92  LYS A O   1 
ATOM   753  C  CB  . LYS A 1 92  ? 2.730   12.732  11.780 1.00 33.62  ? 92  LYS A CB  1 
ATOM   754  C  CG  . LYS A 1 92  ? 4.142   13.121  11.320 1.00 35.91  ? 92  LYS A CG  1 
ATOM   755  C  CD  . LYS A 1 92  ? 4.277   14.150  10.207 1.00 42.87  ? 92  LYS A CD  1 
ATOM   756  C  CE  . LYS A 1 92  ? 3.855   15.532  10.552 1.00 49.60  ? 92  LYS A CE  1 
ATOM   757  N  NZ  . LYS A 1 92  ? 4.561   16.053  11.723 1.00 62.40  ? 92  LYS A NZ  1 
ATOM   758  N  N   . LEU A 1 93  ? 4.433   11.812  14.608 1.00 28.38  ? 93  LEU A N   1 
ATOM   759  C  CA  . LEU A 1 93  ? 5.073   12.492  15.732 1.00 27.59  ? 93  LEU A CA  1 
ATOM   760  C  C   . LEU A 1 93  ? 5.453   13.911  15.332 1.00 27.15  ? 93  LEU A C   1 
ATOM   761  O  O   . LEU A 1 93  ? 5.643   14.226  14.161 1.00 30.27  ? 93  LEU A O   1 
ATOM   762  C  CB  . LEU A 1 93  ? 6.290   11.742  16.257 1.00 31.42  ? 93  LEU A CB  1 
ATOM   763  C  CG  . LEU A 1 93  ? 6.032   10.547  17.188 1.00 30.95  ? 93  LEU A CG  1 
ATOM   764  C  CD1 . LEU A 1 93  ? 5.246   9.430   16.569 1.00 29.94  ? 93  LEU A CD1 1 
ATOM   765  C  CD2 . LEU A 1 93  ? 7.342   9.933   17.685 1.00 33.78  ? 93  LEU A CD2 1 
ATOM   766  N  N   . ASP A 1 94  ? 5.425   14.810  16.298 1.00 29.27  ? 94  ASP A N   1 
ATOM   767  C  CA  . ASP A 1 94  ? 5.820   16.184  16.061 1.00 32.32  ? 94  ASP A CA  1 
ATOM   768  C  C   . ASP A 1 94  ? 7.309   16.340  16.370 1.00 38.20  ? 94  ASP A C   1 
ATOM   769  O  O   . ASP A 1 94  ? 7.692   16.429  17.519 1.00 33.49  ? 94  ASP A O   1 
ATOM   770  C  CB  . ASP A 1 94  ? 5.027   17.128  16.940 1.00 35.34  ? 94  ASP A CB  1 
ATOM   771  C  CG  . ASP A 1 94  ? 5.328   18.599  16.689 1.00 39.40  ? 94  ASP A CG  1 
ATOM   772  O  OD1 . ASP A 1 94  ? 4.681   19.430  17.334 1.00 43.78  ? 94  ASP A OD1 1 
ATOM   773  O  OD2 . ASP A 1 94  ? 6.246   18.892  15.881 1.00 42.77  ? 94  ASP A OD2 1 
ATOM   774  N  N   . ASP A 1 95  ? 8.160   16.444  15.346 1.00 40.68  ? 95  ASP A N   1 
ATOM   775  C  CA  . ASP A 1 95  ? 9.599   16.447  15.586 1.00 45.82  ? 95  ASP A CA  1 
ATOM   776  C  C   . ASP A 1 95  ? 10.050  17.821  16.098 1.00 41.96  ? 95  ASP A C   1 
ATOM   777  O  O   . ASP A 1 95  ? 11.196  17.969  16.480 1.00 46.63  ? 95  ASP A O   1 
ATOM   778  C  CB  . ASP A 1 95  ? 10.327  15.933  14.358 1.00 56.64  ? 95  ASP A CB  1 
ATOM   779  C  CG  . ASP A 1 95  ? 9.815   16.659  13.133 1.00 61.77  ? 95  ASP A CG  1 
ATOM   780  O  OD1 . ASP A 1 95  ? 9.185   15.993  12.276 1.00 78.03  ? 95  ASP A OD1 1 
ATOM   781  O  OD2 . ASP A 1 95  ? 9.894   17.907  13.159 1.00 60.54  ? 95  ASP A OD2 1 
ATOM   782  N  N   . LYS A 1 96  ? 9.144   18.791  16.234 1.00 43.38  ? 96  LYS A N   1 
ATOM   783  C  CA  . LYS A 1 96  ? 9.466   20.046  16.902 1.00 49.31  ? 96  LYS A CA  1 
ATOM   784  C  C   . LYS A 1 96  ? 9.083   20.000  18.387 1.00 43.49  ? 96  LYS A C   1 
ATOM   785  O  O   . LYS A 1 96  ? 9.265   20.980  19.102 1.00 34.60  ? 96  LYS A O   1 
ATOM   786  C  CB  . LYS A 1 96  ? 8.712   21.224  16.272 1.00 59.04  ? 96  LYS A CB  1 
ATOM   787  C  CG  . LYS A 1 96  ? 8.680   21.273  14.753 1.00 66.17  ? 96  LYS A CG  1 
ATOM   788  C  CD  . LYS A 1 96  ? 10.000  21.696  14.137 1.00 75.15  ? 96  LYS A CD  1 
ATOM   789  C  CE  . LYS A 1 96  ? 10.042  23.180  14.046 1.00 83.20  ? 96  LYS A CE  1 
ATOM   790  N  NZ  . LYS A 1 96  ? 11.091  23.603  13.117 1.00 89.42  ? 96  LYS A NZ  1 
ATOM   791  N  N   . ASP A 1 97  ? 8.470   18.899  18.845 1.00 37.79  ? 97  ASP A N   1 
ATOM   792  C  CA  . ASP A 1 97  ? 8.211   18.697  20.267 1.00 32.36  ? 97  ASP A CA  1 
ATOM   793  C  C   . ASP A 1 97  ? 9.555   18.482  20.959 1.00 28.09  ? 97  ASP A C   1 
ATOM   794  O  O   . ASP A 1 97  ? 10.311  17.560  20.599 1.00 29.85  ? 97  ASP A O   1 
ATOM   795  C  CB  . ASP A 1 97  ? 7.280   17.517  20.485 1.00 33.94  ? 97  ASP A CB  1 
ATOM   796  C  CG  . ASP A 1 97  ? 6.789   17.235  21.903 1.00 34.79  ? 97  ASP A CG  1 
ATOM   797  O  OD1 . ASP A 1 97  ? 5.619   16.788  21.984 1.00 38.97  ? 97  ASP A OD1 1 
ATOM   798  O  OD2 . ASP A 1 97  ? 7.546   17.450  22.898 1.00 29.30  ? 97  ASP A OD2 1 
ATOM   799  N  N   . PRO A 1 98  ? 9.843   19.265  22.029 1.00 33.93  ? 98  PRO A N   1 
ATOM   800  C  CA  . PRO A 1 98  ? 11.075  19.111  22.786 1.00 32.64  ? 98  PRO A CA  1 
ATOM   801  C  C   . PRO A 1 98  ? 11.287  17.670  23.262 1.00 26.96  ? 98  PRO A C   1 
ATOM   802  O  O   . PRO A 1 98  ? 12.415  17.283  23.498 1.00 27.41  ? 98  PRO A O   1 
ATOM   803  C  CB  . PRO A 1 98  ? 10.963  20.099  23.976 1.00 33.85  ? 98  PRO A CB  1 
ATOM   804  C  CG  . PRO A 1 98  ? 9.705   20.880  23.783 1.00 38.27  ? 98  PRO A CG  1 
ATOM   805  C  CD  . PRO A 1 98  ? 8.948   20.280  22.608 1.00 37.68  ? 98  PRO A CD  1 
ATOM   806  N  N   . ASN A 1 99  ? 10.228  16.890  23.428 1.00 25.10  ? 99  ASN A N   1 
ATOM   807  C  CA  . ASN A 1 99  ? 10.375  15.542  23.974 1.00 23.64  ? 99  ASN A CA  1 
ATOM   808  C  C   . ASN A 1 99  ? 10.345  14.486  22.874 1.00 25.60  ? 99  ASN A C   1 
ATOM   809  O  O   . ASN A 1 99  ? 10.220  13.284  23.165 1.00 22.99  ? 99  ASN A O   1 
ATOM   810  C  CB  . ASN A 1 99  ? 9.271   15.238  24.974 1.00 25.82  ? 99  ASN A CB  1 
ATOM   811  C  CG  . ASN A 1 99  ? 9.397   16.075  26.225 1.00 26.72  ? 99  ASN A CG  1 
ATOM   812  O  OD1 . ASN A 1 99  ? 10.487  16.199  26.780 1.00 28.69  ? 99  ASN A OD1 1 
ATOM   813  N  ND2 . ASN A 1 99  ? 8.294   16.660  26.669 1.00 28.57  ? 99  ASN A ND2 1 
ATOM   814  N  N   . PHE A 1 100 ? 10.484  14.921  21.618 1.00 24.23  ? 100 PHE A N   1 
ATOM   815  C  CA  . PHE A 1 100 ? 10.476  13.975  20.495 1.00 25.66  ? 100 PHE A CA  1 
ATOM   816  C  C   . PHE A 1 100 ? 11.351  12.741  20.747 1.00 27.63  ? 100 PHE A C   1 
ATOM   817  O  O   . PHE A 1 100 ? 10.886  11.613  20.640 1.00 26.38  ? 100 PHE A O   1 
ATOM   818  C  CB  . PHE A 1 100 ? 10.864  14.684  19.195 1.00 26.57  ? 100 PHE A CB  1 
ATOM   819  C  CG  . PHE A 1 100 ? 10.944  13.721  18.011 1.00 27.71  ? 100 PHE A CG  1 
ATOM   820  C  CD1 . PHE A 1 100 ? 12.136  13.087  17.667 1.00 28.14  ? 100 PHE A CD1 1 
ATOM   821  C  CD2 . PHE A 1 100 ? 9.828   13.471  17.222 1.00 32.84  ? 100 PHE A CD2 1 
ATOM   822  C  CE1 . PHE A 1 100 ? 12.189  12.197  16.602 1.00 32.69  ? 100 PHE A CE1 1 
ATOM   823  C  CE2 . PHE A 1 100 ? 9.894   12.583  16.140 1.00 37.78  ? 100 PHE A CE2 1 
ATOM   824  C  CZ  . PHE A 1 100 ? 11.061  11.915  15.859 1.00 35.19  ? 100 PHE A CZ  1 
ATOM   825  N  N   . LYS A 1 101 ? 12.634  12.950  21.094 1.00 29.19  ? 101 LYS A N   1 
ATOM   826  C  CA  . LYS A 1 101 ? 13.584  11.862  21.277 1.00 28.99  ? 101 LYS A CA  1 
ATOM   827  C  C   . LYS A 1 101 ? 13.160  10.878  22.365 1.00 27.89  ? 101 LYS A C   1 
ATOM   828  O  O   . LYS A 1 101 ? 13.297  9.664   22.217 1.00 26.91  ? 101 LYS A O   1 
ATOM   829  C  CB  . LYS A 1 101 ? 14.965  12.411  21.654 1.00 36.46  ? 101 LYS A CB  1 
ATOM   830  C  CG  . LYS A 1 101 ? 15.673  13.076  20.455 1.00 42.89  ? 101 LYS A CG  1 
ATOM   831  C  CD  . LYS A 1 101 ? 17.041  13.744  20.668 1.00 47.48  ? 101 LYS A CD  1 
ATOM   832  C  CE  . LYS A 1 101 ? 17.694  13.865  19.290 1.00 65.00  ? 101 LYS A CE  1 
ATOM   833  N  NZ  . LYS A 1 101 ? 18.952  14.616  19.108 1.00 72.27  ? 101 LYS A NZ  1 
ATOM   834  N  N   . ASP A 1 102 ? 12.649  11.398  23.478 1.00 28.96  ? 102 ASP A N   1 
ATOM   835  C  CA  . ASP A 1 102 ? 12.097  10.540  24.528 1.00 33.30  ? 102 ASP A CA  1 
ATOM   836  C  C   . ASP A 1 102 ? 10.855  9.781   24.049 1.00 27.32  ? 102 ASP A C   1 
ATOM   837  O  O   . ASP A 1 102 ? 10.596  8.649   24.491 1.00 22.54  ? 102 ASP A O   1 
ATOM   838  C  CB  . ASP A 1 102 ? 11.748  11.339  25.777 1.00 32.28  ? 102 ASP A CB  1 
ATOM   839  C  CG  . ASP A 1 102 ? 12.924  11.751  26.637 1.00 43.71  ? 102 ASP A CG  1 
ATOM   840  O  OD1 . ASP A 1 102 ? 14.022  11.203  26.366 1.00 40.67  ? 102 ASP A OD1 1 
ATOM   841  O  OD2 . ASP A 1 102 ? 12.708  12.629  27.561 1.00 39.90  ? 102 ASP A OD2 1 
ATOM   842  N  N   . GLN A 1 103 ? 10.067  10.410  23.186 1.00 22.12  ? 103 GLN A N   1 
ATOM   843  C  CA  . GLN A 1 103 ? 8.859   9.740   22.699 1.00 24.54  ? 103 GLN A CA  1 
ATOM   844  C  C   . GLN A 1 103 ? 9.260   8.516   21.878 1.00 26.54  ? 103 GLN A C   1 
ATOM   845  O  O   . GLN A 1 103 ? 8.625   7.466   21.985 1.00 25.94  ? 103 GLN A O   1 
ATOM   846  C  CB  . GLN A 1 103 ? 7.926   10.645  21.902 1.00 26.60  ? 103 GLN A CB  1 
ATOM   847  C  CG  . GLN A 1 103 ? 7.249   11.724  22.751 1.00 25.79  ? 103 GLN A CG  1 
ATOM   848  C  CD  . GLN A 1 103 ? 6.822   12.940  21.969 1.00 30.35  ? 103 GLN A CD  1 
ATOM   849  O  OE1 . GLN A 1 103 ? 6.925   13.002  20.734 1.00 32.21  ? 103 GLN A OE1 1 
ATOM   850  N  NE2 . GLN A 1 103 ? 6.334   13.934  22.702 1.00 31.98  ? 103 GLN A NE2 1 
ATOM   851  N  N   . VAL A 1 104 ? 10.292  8.657   21.038 1.00 25.12  ? 104 VAL A N   1 
ATOM   852  C  CA  . VAL A 1 104 ? 10.722  7.539   20.209 1.00 22.83  ? 104 VAL A CA  1 
ATOM   853  C  C   . VAL A 1 104 ? 11.224  6.418   21.101 1.00 27.05  ? 104 VAL A C   1 
ATOM   854  O  O   . VAL A 1 104 ? 10.890  5.251   20.895 1.00 25.55  ? 104 VAL A O   1 
ATOM   855  C  CB  . VAL A 1 104 ? 11.790  8.038   19.230 1.00 27.13  ? 104 VAL A CB  1 
ATOM   856  C  CG1 . VAL A 1 104 ? 12.554  6.875   18.573 1.00 24.97  ? 104 VAL A CG1 1 
ATOM   857  C  CG2 . VAL A 1 104 ? 11.187  8.996   18.199 1.00 28.89  ? 104 VAL A CG2 1 
ATOM   858  N  N   . ILE A 1 105 ? 12.039  6.790   22.095 1.00 29.04  ? 105 ILE A N   1 
ATOM   859  C  CA  . ILE A 1 105 ? 12.583  5.796   23.007 1.00 29.49  ? 105 ILE A CA  1 
ATOM   860  C  C   . ILE A 1 105 ? 11.443  5.085   23.733 1.00 28.45  ? 105 ILE A C   1 
ATOM   861  O  O   . ILE A 1 105 ? 11.439  3.854   23.843 1.00 29.95  ? 105 ILE A O   1 
ATOM   862  C  CB  . ILE A 1 105 ? 13.629  6.412   23.959 1.00 29.64  ? 105 ILE A CB  1 
ATOM   863  C  CG1 . ILE A 1 105 ? 14.897  6.764   23.200 1.00 34.20  ? 105 ILE A CG1 1 
ATOM   864  C  CG2 . ILE A 1 105 ? 13.984  5.484   25.124 1.00 33.50  ? 105 ILE A CG2 1 
ATOM   865  C  CD1 . ILE A 1 105 ? 15.764  7.773   23.926 1.00 35.95  ? 105 ILE A CD1 1 
ATOM   866  N  N   . LEU A 1 106 ? 10.464  5.858   24.209 1.00 26.67  ? 106 LEU A N   1 
ATOM   867  C  CA  . LEU A 1 106 ? 9.349   5.243   24.936 1.00 29.35  ? 106 LEU A CA  1 
ATOM   868  C  C   . LEU A 1 106 ? 8.588   4.268   24.050 1.00 28.32  ? 106 LEU A C   1 
ATOM   869  O  O   . LEU A 1 106 ? 8.357   3.137   24.443 1.00 25.17  ? 106 LEU A O   1 
ATOM   870  C  CB  . LEU A 1 106 ? 8.394   6.265   25.519 1.00 30.09  ? 106 LEU A CB  1 
ATOM   871  C  CG  . LEU A 1 106 ? 7.216   5.709   26.327 1.00 30.80  ? 106 LEU A CG  1 
ATOM   872  C  CD1 . LEU A 1 106 ? 7.593   4.846   27.491 1.00 34.33  ? 106 LEU A CD1 1 
ATOM   873  C  CD2 . LEU A 1 106 ? 6.422   6.891   26.788 1.00 29.91  ? 106 LEU A CD2 1 
ATOM   874  N  N   . LEU A 1 107 ? 8.273   4.677   22.820 1.00 24.80  ? 107 LEU A N   1 
ATOM   875  C  CA  . LEU A 1 107 ? 7.517   3.794   21.959 1.00 27.13  ? 107 LEU A CA  1 
ATOM   876  C  C   . LEU A 1 107 ? 8.309   2.543   21.585 1.00 26.32  ? 107 LEU A C   1 
ATOM   877  O  O   . LEU A 1 107 ? 7.733   1.464   21.646 1.00 27.36  ? 107 LEU A O   1 
ATOM   878  C  CB  . LEU A 1 107 ? 7.007   4.538   20.739 1.00 29.22  ? 107 LEU A CB  1 
ATOM   879  C  CG  . LEU A 1 107 ? 5.955   5.605   21.048 1.00 32.31  ? 107 LEU A CG  1 
ATOM   880  C  CD1 . LEU A 1 107 ? 5.779   6.552   19.866 1.00 34.21  ? 107 LEU A CD1 1 
ATOM   881  C  CD2 . LEU A 1 107 ? 4.621   5.003   21.447 1.00 31.35  ? 107 LEU A CD2 1 
ATOM   882  N  N   . ASN A 1 108 ? 9.618   2.660   21.324 1.00 29.87  ? 108 ASN A N   1 
ATOM   883  C  CA  . ASN A 1 108 ? 10.455  1.513   21.006 1.00 31.25  ? 108 ASN A CA  1 
ATOM   884  C  C   . ASN A 1 108 ? 10.534  0.520   22.156 1.00 33.71  ? 108 ASN A C   1 
ATOM   885  O  O   . ASN A 1 108 ? 10.754  -0.668  21.924 1.00 31.53  ? 108 ASN A O   1 
ATOM   886  C  CB  . ASN A 1 108 ? 11.877  1.924   20.652 1.00 35.77  ? 108 ASN A CB  1 
ATOM   887  C  CG  . ASN A 1 108 ? 11.983  2.486   19.245 1.00 44.99  ? 108 ASN A CG  1 
ATOM   888  O  OD1 . ASN A 1 108 ? 11.116  2.268   18.384 1.00 38.44  ? 108 ASN A OD1 1 
ATOM   889  N  ND2 . ASN A 1 108 ? 13.057  3.221   18.986 1.00 48.77  ? 108 ASN A ND2 1 
ATOM   890  N  N   . LYS A 1 109 ? 10.394  1.018   23.387 1.00 30.26  ? 109 LYS A N   1 
ATOM   891  C  CA  . LYS A 1 109 ? 10.414  0.157   24.560 1.00 35.62  ? 109 LYS A CA  1 
ATOM   892  C  C   . LYS A 1 109 ? 9.228   -0.813  24.628 1.00 30.03  ? 109 LYS A C   1 
ATOM   893  O  O   . LYS A 1 109 ? 9.289   -1.813  25.348 1.00 26.90  ? 109 LYS A O   1 
ATOM   894  C  CB  . LYS A 1 109 ? 10.393  1.074   25.785 1.00 45.78  ? 109 LYS A CB  1 
ATOM   895  C  CG  . LYS A 1 109 ? 10.834  0.424   27.063 1.00 55.63  ? 109 LYS A CG  1 
ATOM   896  C  CD  . LYS A 1 109 ? 10.590  1.295   28.289 1.00 63.76  ? 109 LYS A CD  1 
ATOM   897  C  CE  . LYS A 1 109 ? 11.355  2.562   28.261 1.00 67.68  ? 109 LYS A CE  1 
ATOM   898  N  NZ  . LYS A 1 109 ? 11.085  3.303   29.495 1.00 79.54  ? 109 LYS A NZ  1 
ATOM   899  N  N   . HIS A 1 110 ? 8.110   -0.478  23.977 1.00 26.74  ? 110 HIS A N   1 
ATOM   900  C  CA  . HIS A 1 110 ? 6.860   -1.230  24.099 1.00 24.88  ? 110 HIS A CA  1 
ATOM   901  C  C   . HIS A 1 110 ? 6.460   -1.996  22.846 1.00 25.81  ? 110 HIS A C   1 
ATOM   902  O  O   . HIS A 1 110 ? 5.717   -2.974  22.948 1.00 29.51  ? 110 HIS A O   1 
ATOM   903  C  CB  . HIS A 1 110 ? 5.737   -0.317  24.568 1.00 24.59  ? 110 HIS A CB  1 
ATOM   904  C  CG  . HIS A 1 110 ? 5.973   0.237   25.944 1.00 25.13  ? 110 HIS A CG  1 
ATOM   905  N  ND1 . HIS A 1 110 ? 5.886   -0.543  27.081 1.00 23.01  ? 110 HIS A ND1 1 
ATOM   906  C  CD2 . HIS A 1 110 ? 6.317   1.462   26.346 1.00 23.67  ? 110 HIS A CD2 1 
ATOM   907  C  CE1 . HIS A 1 110 ? 6.123   0.239   28.136 1.00 29.44  ? 110 HIS A CE1 1 
ATOM   908  N  NE2 . HIS A 1 110 ? 6.386   1.473   27.702 1.00 26.94  ? 110 HIS A NE2 1 
ATOM   909  N  N   . ILE A 1 111 ? 6.983   -1.610  21.668 1.00 27.04  ? 111 ILE A N   1 
ATOM   910  C  CA  . ILE A 1 111 ? 6.560   -2.267  20.432 1.00 27.98  ? 111 ILE A CA  1 
ATOM   911  C  C   . ILE A 1 111 ? 7.207   -3.644  20.347 1.00 28.48  ? 111 ILE A C   1 
ATOM   912  O  O   . ILE A 1 111 ? 8.424   -3.733  20.288 1.00 31.30  ? 111 ILE A O   1 
ATOM   913  C  CB  . ILE A 1 111 ? 6.888   -1.394  19.204 1.00 26.10  ? 111 ILE A CB  1 
ATOM   914  C  CG1 . ILE A 1 111 ? 6.027   -0.141  19.178 1.00 26.72  ? 111 ILE A CG1 1 
ATOM   915  C  CG2 . ILE A 1 111 ? 6.703   -2.176  17.908 1.00 25.65  ? 111 ILE A CG2 1 
ATOM   916  C  CD1 . ILE A 1 111 ? 6.543   0.939   18.242 1.00 29.59  ? 111 ILE A CD1 1 
ATOM   917  N  N   . ASP A 1 112 ? 6.390   -4.704  20.318 1.00 32.35  ? 112 ASP A N   1 
ATOM   918  C  CA  . ASP A 1 112 ? 6.823   -6.086  20.135 1.00 29.97  ? 112 ASP A CA  1 
ATOM   919  C  C   . ASP A 1 112 ? 7.744   -6.601  21.240 1.00 29.86  ? 112 ASP A C   1 
ATOM   920  O  O   . ASP A 1 112 ? 8.370   -7.649  21.089 1.00 31.38  ? 112 ASP A O   1 
ATOM   921  C  CB  . ASP A 1 112 ? 7.559   -6.294  18.827 1.00 33.82  ? 112 ASP A CB  1 
ATOM   922  C  CG  . ASP A 1 112 ? 6.676   -6.335  17.594 1.00 37.57  ? 112 ASP A CG  1 
ATOM   923  O  OD1 . ASP A 1 112 ? 5.483   -6.742  17.741 1.00 32.71  ? 112 ASP A OD1 1 
ATOM   924  O  OD2 . ASP A 1 112 ? 7.176   -5.922  16.531 1.00 38.32  ? 112 ASP A OD2 1 
ATOM   925  N  N   . ALA A 1 113 ? 7.784   -5.906  22.357 1.00 28.15  ? 113 ALA A N   1 
ATOM   926  C  CA  . ALA A 1 113 ? 8.602   -6.279  23.491 1.00 29.70  ? 113 ALA A CA  1 
ATOM   927  C  C   . ALA A 1 113 ? 8.205   -7.679  24.013 1.00 33.34  ? 113 ALA A C   1 
ATOM   928  O  O   . ALA A 1 113 ? 9.008   -8.381  24.600 1.00 32.53  ? 113 ALA A O   1 
ATOM   929  C  CB  . ALA A 1 113 ? 8.537   -5.122  24.498 1.00 30.64  ? 113 ALA A CB  1 
ATOM   930  N  N   . TYR A 1 114 ? 6.995   -8.168  23.733 1.00 33.55  ? 114 TYR A N   1 
ATOM   931  C  CA  . TYR A 1 114 ? 6.552   -9.479  24.209 1.00 37.86  ? 114 TYR A CA  1 
ATOM   932  C  C   . TYR A 1 114 ? 7.471   -10.592 23.684 1.00 39.69  ? 114 TYR A C   1 
ATOM   933  O  O   . TYR A 1 114 ? 7.530   -11.683 24.239 1.00 41.82  ? 114 TYR A O   1 
ATOM   934  C  CB  . TYR A 1 114 ? 5.108   -9.813  23.776 1.00 33.60  ? 114 TYR A CB  1 
ATOM   935  C  CG  . TYR A 1 114 ? 4.962   -10.136 22.297 1.00 30.80  ? 114 TYR A CG  1 
ATOM   936  C  CD1 . TYR A 1 114 ? 5.062   -11.439 21.833 1.00 30.39  ? 114 TYR A CD1 1 
ATOM   937  C  CD2 . TYR A 1 114 ? 4.799   -9.127  21.351 1.00 28.61  ? 114 TYR A CD2 1 
ATOM   938  C  CE1 . TYR A 1 114 ? 5.004   -11.727 20.489 1.00 32.84  ? 114 TYR A CE1 1 
ATOM   939  C  CE2 . TYR A 1 114 ? 4.701   -9.411  20.005 1.00 30.48  ? 114 TYR A CE2 1 
ATOM   940  C  CZ  . TYR A 1 114 ? 4.842   -10.713 19.562 1.00 33.85  ? 114 TYR A CZ  1 
ATOM   941  O  OH  . TYR A 1 114 ? 4.759   -10.952 18.220 1.00 36.35  ? 114 TYR A OH  1 
ATOM   942  N  N   . LYS A 1 115 ? 8.142   -10.335 22.568 1.00 36.92  ? 115 LYS A N   1 
ATOM   943  C  CA  . LYS A 1 115 ? 9.008   -11.338 21.977 1.00 42.88  ? 115 LYS A CA  1 
ATOM   944  C  C   . LYS A 1 115 ? 10.183  -11.694 22.892 1.00 42.72  ? 115 LYS A C   1 
ATOM   945  O  O   . LYS A 1 115 ? 10.781  -12.744 22.711 1.00 43.32  ? 115 LYS A O   1 
ATOM   946  C  CB  . LYS A 1 115 ? 9.541   -10.823 20.638 1.00 42.51  ? 115 LYS A CB  1 
ATOM   947  C  CG  . LYS A 1 115 ? 8.531   -10.803 19.531 1.00 43.83  ? 115 LYS A CG  1 
ATOM   948  C  CD  . LYS A 1 115 ? 9.099   -10.119 18.299 1.00 47.77  ? 115 LYS A CD  1 
ATOM   949  C  CE  . LYS A 1 115 ? 8.202   -10.205 17.123 1.00 50.32  ? 115 LYS A CE  1 
ATOM   950  N  NZ  . LYS A 1 115 ? 8.846   -9.577  15.963 1.00 58.24  ? 115 LYS A NZ  1 
ATOM   951  N  N   . THR A 1 116 ? 10.530  -10.831 23.852 1.00 37.73  ? 116 THR A N   1 
ATOM   952  C  CA  . THR A 1 116 ? 11.657  -11.076 24.738 1.00 37.35  ? 116 THR A CA  1 
ATOM   953  C  C   . THR A 1 116 ? 11.200  -11.721 26.057 1.00 44.56  ? 116 THR A C   1 
ATOM   954  O  O   . THR A 1 116 ? 12.000  -11.838 26.983 1.00 41.18  ? 116 THR A O   1 
ATOM   955  C  CB  . THR A 1 116 ? 12.360  -9.750  25.040 1.00 41.57  ? 116 THR A CB  1 
ATOM   956  O  OG1 . THR A 1 116 ? 11.509  -8.999  25.912 1.00 39.59  ? 116 THR A OG1 1 
ATOM   957  C  CG2 . THR A 1 116 ? 12.672  -8.937  23.795 1.00 44.69  ? 116 THR A CG2 1 
ATOM   958  N  N   . PHE A 1 117 ? 9.902   -12.023 26.218 1.00 40.52  ? 117 PHE A N   1 
ATOM   959  C  CA  . PHE A 1 117 ? 9.406   -12.313 27.558 1.00 43.30  ? 117 PHE A CA  1 
ATOM   960  C  C   . PHE A 1 117 ? 9.806   -13.735 27.909 1.00 49.07  ? 117 PHE A C   1 
ATOM   961  O  O   . PHE A 1 117 ? 9.706   -14.608 27.042 1.00 45.29  ? 117 PHE A O   1 
ATOM   962  C  CB  . PHE A 1 117 ? 7.885   -12.251 27.765 1.00 41.33  ? 117 PHE A CB  1 
ATOM   963  C  CG  . PHE A 1 117 ? 7.276   -10.862 27.691 1.00 39.27  ? 117 PHE A CG  1 
ATOM   964  C  CD1 . PHE A 1 117 ? 8.062   -9.718  27.759 1.00 39.18  ? 117 PHE A CD1 1 
ATOM   965  C  CD2 . PHE A 1 117 ? 5.897   -10.715 27.609 1.00 40.11  ? 117 PHE A CD2 1 
ATOM   966  C  CE1 . PHE A 1 117 ? 7.492   -8.466  27.637 1.00 42.52  ? 117 PHE A CE1 1 
ATOM   967  C  CE2 . PHE A 1 117 ? 5.333   -9.456  27.551 1.00 38.78  ? 117 PHE A CE2 1 
ATOM   968  C  CZ  . PHE A 1 117 ? 6.132   -8.338  27.594 1.00 39.58  ? 117 PHE A CZ  1 
ATOM   969  N  N   . PRO A 1 118 ? 10.184  -13.984 29.190 1.00 60.35  ? 118 PRO A N   1 
ATOM   970  C  CA  . PRO A 1 118 ? 10.503  -15.331 29.666 1.00 71.82  ? 118 PRO A CA  1 
ATOM   971  C  C   . PRO A 1 118 ? 9.584   -16.378 29.053 1.00 74.64  ? 118 PRO A C   1 
ATOM   972  O  O   . PRO A 1 118 ? 10.128  -17.176 28.276 1.00 82.68  ? 118 PRO A O   1 
ATOM   973  C  CB  . PRO A 1 118 ? 10.332  -15.168 31.189 1.00 70.61  ? 118 PRO A CB  1 
ATOM   974  C  CG  . PRO A 1 118 ? 10.839  -13.758 31.454 1.00 68.76  ? 118 PRO A CG  1 
ATOM   975  C  CD  . PRO A 1 118 ? 10.323  -12.969 30.256 1.00 65.42  ? 118 PRO A CD  1 
ATOM   976  O  OXT . PRO A 1 118 ? 8.365   -16.327 29.295 1.00 89.49  ? 118 PRO A OXT 1 
ATOM   977  N  N   . LYS B 1 3   ? -15.104 26.831  20.681 1.00 103.51 ? 3   LYS B N   1 
ATOM   978  C  CA  . LYS B 1 3   ? -13.814 26.430  20.058 1.00 100.43 ? 3   LYS B CA  1 
ATOM   979  C  C   . LYS B 1 3   ? -13.907 26.619  18.539 1.00 96.17  ? 3   LYS B C   1 
ATOM   980  O  O   . LYS B 1 3   ? -14.551 25.850  17.832 1.00 86.76  ? 3   LYS B O   1 
ATOM   981  C  CB  . LYS B 1 3   ? -13.481 25.000  20.511 1.00 98.15  ? 3   LYS B CB  1 
ATOM   982  C  CG  . LYS B 1 3   ? -12.005 24.710  20.730 1.00 100.77 ? 3   LYS B CG  1 
ATOM   983  C  CD  . LYS B 1 3   ? -11.333 25.694  21.685 1.00 102.27 ? 3   LYS B CD  1 
ATOM   984  C  CE  . LYS B 1 3   ? -11.921 25.698  23.064 1.00 94.57  ? 3   LYS B CE  1 
ATOM   985  N  NZ  . LYS B 1 3   ? -11.647 26.974  23.726 1.00 91.43  ? 3   LYS B NZ  1 
ATOM   986  N  N   . SER B 1 4   ? -13.253 27.668  18.033 1.00 93.78  ? 4   SER B N   1 
ATOM   987  C  CA  . SER B 1 4   ? -13.258 27.980  16.610 1.00 95.11  ? 4   SER B CA  1 
ATOM   988  C  C   . SER B 1 4   ? -12.424 26.957  15.833 1.00 98.37  ? 4   SER B C   1 
ATOM   989  O  O   . SER B 1 4   ? -11.742 26.131  16.435 1.00 90.98  ? 4   SER B O   1 
ATOM   990  C  CB  . SER B 1 4   ? -12.733 29.380  16.397 1.00 92.98  ? 4   SER B CB  1 
ATOM   991  O  OG  . SER B 1 4   ? -11.442 29.509  16.981 1.00 100.20 ? 4   SER B OG  1 
ATOM   992  N  N   . ALA B 1 5   ? -12.424 27.046  14.491 1.00 101.10 ? 5   ALA B N   1 
ATOM   993  C  CA  . ALA B 1 5   ? -11.463 26.311  13.671 1.00 99.48  ? 5   ALA B CA  1 
ATOM   994  C  C   . ALA B 1 5   ? -10.024 26.657  14.074 1.00 106.50 ? 5   ALA B C   1 
ATOM   995  O  O   . ALA B 1 5   ? -9.186  25.766  14.222 1.00 89.50  ? 5   ALA B O   1 
ATOM   996  C  CB  . ALA B 1 5   ? -11.700 26.546  12.187 1.00 87.75  ? 5   ALA B CB  1 
ATOM   997  N  N   . ALA B 1 6   ? -9.741  27.957  14.260 1.00 108.64 ? 6   ALA B N   1 
ATOM   998  C  CA  . ALA B 1 6   ? -8.412  28.422  14.643 1.00 100.67 ? 6   ALA B CA  1 
ATOM   999  C  C   . ALA B 1 6   ? -7.963  27.773  15.956 1.00 92.43  ? 6   ALA B C   1 
ATOM   1000 O  O   . ALA B 1 6   ? -6.825  27.330  16.048 1.00 85.44  ? 6   ALA B O   1 
ATOM   1001 C  CB  . ALA B 1 6   ? -8.386  29.933  14.732 1.00 93.40  ? 6   ALA B CB  1 
ATOM   1002 N  N   . GLU B 1 7   ? -8.861  27.697  16.949 1.00 85.67  ? 7   GLU B N   1 
ATOM   1003 C  CA  . GLU B 1 7   ? -8.568  27.111  18.250 1.00 84.23  ? 7   GLU B CA  1 
ATOM   1004 C  C   . GLU B 1 7   ? -8.425  25.585  18.184 1.00 78.47  ? 7   GLU B C   1 
ATOM   1005 O  O   . GLU B 1 7   ? -7.433  25.039  18.665 1.00 64.07  ? 7   GLU B O   1 
ATOM   1006 C  CB  . GLU B 1 7   ? -9.658  27.462  19.268 1.00 87.94  ? 7   GLU B CB  1 
ATOM   1007 C  CG  . GLU B 1 7   ? -9.389  28.746  20.045 1.00 96.19  ? 7   GLU B CG  1 
ATOM   1008 C  CD  . GLU B 1 7   ? -8.203  28.593  20.988 1.00 103.37 ? 7   GLU B CD  1 
ATOM   1009 O  OE1 . GLU B 1 7   ? -7.088  28.222  20.546 1.00 89.62  ? 7   GLU B OE1 1 
ATOM   1010 O  OE2 . GLU B 1 7   ? -8.404  28.846  22.196 1.00 111.29 ? 7   GLU B OE2 1 
ATOM   1011 N  N   . ALA B 1 8   ? -9.443  24.901  17.634 1.00 73.93  ? 8   ALA B N   1 
ATOM   1012 C  CA  . ALA B 1 8   ? -9.493  23.443  17.593 1.00 65.63  ? 8   ALA B CA  1 
ATOM   1013 C  C   . ALA B 1 8   ? -8.344  22.869  16.747 1.00 63.31  ? 8   ALA B C   1 
ATOM   1014 O  O   . ALA B 1 8   ? -7.879  21.760  17.016 1.00 51.85  ? 8   ALA B O   1 
ATOM   1015 C  CB  . ALA B 1 8   ? -10.858 23.000  17.092 1.00 66.84  ? 8   ALA B CB  1 
ATOM   1016 N  N   . SER B 1 9   ? -7.857  23.634  15.749 1.00 54.21  ? 9   SER B N   1 
ATOM   1017 C  CA  . SER B 1 9   ? -6.794  23.166  14.868 1.00 57.57  ? 9   SER B CA  1 
ATOM   1018 C  C   . SER B 1 9   ? -5.445  23.111  15.581 1.00 56.98  ? 9   SER B C   1 
ATOM   1019 O  O   . SER B 1 9   ? -4.512  22.501  15.061 1.00 46.48  ? 9   SER B O   1 
ATOM   1020 C  CB  . SER B 1 9   ? -6.686  24.017  13.623 1.00 58.27  ? 9   SER B CB  1 
ATOM   1021 O  OG  . SER B 1 9   ? -6.448  25.379  13.958 1.00 58.28  ? 9   SER B OG  1 
ATOM   1022 N  N   . LYS B 1 10  ? -5.343  23.747  16.757 1.00 57.82  ? 10  LYS B N   1 
ATOM   1023 C  CA  . LYS B 1 10  ? -4.092  23.789  17.493 1.00 61.15  ? 10  LYS B CA  1 
ATOM   1024 C  C   . LYS B 1 10  ? -3.773  22.415  18.075 1.00 58.16  ? 10  LYS B C   1 
ATOM   1025 O  O   . LYS B 1 10  ? -2.606  22.115  18.308 1.00 59.06  ? 10  LYS B O   1 
ATOM   1026 C  CB  . LYS B 1 10  ? -4.124  24.852  18.595 1.00 68.44  ? 10  LYS B CB  1 
ATOM   1027 C  CG  . LYS B 1 10  ? -4.289  26.253  18.024 1.00 73.30  ? 10  LYS B CG  1 
ATOM   1028 C  CD  . LYS B 1 10  ? -4.075  27.430  18.965 1.00 77.74  ? 10  LYS B CD  1 
ATOM   1029 C  CE  . LYS B 1 10  ? -4.042  28.684  18.137 1.00 80.99  ? 10  LYS B CE  1 
ATOM   1030 N  NZ  . LYS B 1 10  ? -3.607  29.855  18.894 1.00 86.41  ? 10  LYS B NZ  1 
ATOM   1031 N  N   . LYS B 1 11  ? -4.804  21.595  18.306 1.00 51.81  ? 11  LYS B N   1 
ATOM   1032 C  CA  . LYS B 1 11  ? -4.581  20.261  18.819 1.00 48.82  ? 11  LYS B CA  1 
ATOM   1033 C  C   . LYS B 1 11  ? -3.807  19.424  17.807 1.00 44.32  ? 11  LYS B C   1 
ATOM   1034 O  O   . LYS B 1 11  ? -3.935  19.601  16.590 1.00 39.75  ? 11  LYS B O   1 
ATOM   1035 C  CB  . LYS B 1 11  ? -5.915  19.609  19.178 1.00 51.53  ? 11  LYS B CB  1 
ATOM   1036 C  CG  . LYS B 1 11  ? -6.523  20.193  20.433 1.00 59.88  ? 11  LYS B CG  1 
ATOM   1037 C  CD  . LYS B 1 11  ? -6.896  19.105  21.435 1.00 67.24  ? 11  LYS B CD  1 
ATOM   1038 C  CE  . LYS B 1 11  ? -7.127  19.595  22.821 1.00 73.24  ? 11  LYS B CE  1 
ATOM   1039 N  NZ  . LYS B 1 11  ? -8.425  20.270  22.915 1.00 77.69  ? 11  LYS B NZ  1 
ATOM   1040 N  N   . PRO B 1 12  ? -2.958  18.487  18.278 1.00 40.24  ? 12  PRO B N   1 
ATOM   1041 C  CA  . PRO B 1 12  ? -2.406  17.453  17.411 1.00 40.88  ? 12  PRO B CA  1 
ATOM   1042 C  C   . PRO B 1 12  ? -3.549  16.745  16.684 1.00 34.71  ? 12  PRO B C   1 
ATOM   1043 O  O   . PRO B 1 12  ? -4.642  16.575  17.220 1.00 29.54  ? 12  PRO B O   1 
ATOM   1044 C  CB  . PRO B 1 12  ? -1.650  16.508  18.357 1.00 39.72  ? 12  PRO B CB  1 
ATOM   1045 C  CG  . PRO B 1 12  ? -1.338  17.378  19.554 1.00 40.66  ? 12  PRO B CG  1 
ATOM   1046 C  CD  . PRO B 1 12  ? -2.507  18.349  19.662 1.00 41.82  ? 12  PRO B CD  1 
ATOM   1047 N  N   . ARG B 1 13  ? -3.249  16.289  15.476 1.00 29.99  ? 13  ARG B N   1 
ATOM   1048 C  CA  A ARG B 1 13  ? -4.268  15.752  14.593 0.50 32.00  ? 13  ARG B CA  1 
ATOM   1049 C  CA  B ARG B 1 13  ? -4.265  15.750  14.594 0.50 32.70  ? 13  ARG B CA  1 
ATOM   1050 C  C   . ARG B 1 13  ? -5.089  14.705  15.337 1.00 30.07  ? 13  ARG B C   1 
ATOM   1051 O  O   . ARG B 1 13  ? -6.320  14.760  15.320 1.00 27.58  ? 13  ARG B O   1 
ATOM   1052 C  CB  A ARG B 1 13  ? -3.683  15.192  13.292 0.50 32.59  ? 13  ARG B CB  1 
ATOM   1053 C  CB  B ARG B 1 13  ? -3.626  15.178  13.326 0.50 34.42  ? 13  ARG B CB  1 
ATOM   1054 C  CG  A ARG B 1 13  ? -4.716  14.959  12.197 0.50 35.44  ? 13  ARG B CG  1 
ATOM   1055 C  CG  B ARG B 1 13  ? -4.496  15.269  12.081 0.50 38.53  ? 13  ARG B CG  1 
ATOM   1056 C  CD  A ARG B 1 13  ? -4.056  14.394  10.916 0.50 34.22  ? 13  ARG B CD  1 
ATOM   1057 C  CD  B ARG B 1 13  ? -3.754  14.694  10.877 0.50 37.90  ? 13  ARG B CD  1 
ATOM   1058 N  NE  A ARG B 1 13  ? -4.994  14.021  9.852  0.50 32.25  ? 13  ARG B NE  1 
ATOM   1059 N  NE  B ARG B 1 13  ? -4.516  14.892  9.644  0.50 38.60  ? 13  ARG B NE  1 
ATOM   1060 C  CZ  A ARG B 1 13  ? -5.125  12.825  9.290  0.50 30.08  ? 13  ARG B CZ  1 
ATOM   1061 C  CZ  B ARG B 1 13  ? -4.685  16.074  9.076  0.50 34.62  ? 13  ARG B CZ  1 
ATOM   1062 N  NH1 A ARG B 1 13  ? -4.383  11.798  9.652  0.50 33.68  ? 13  ARG B NH1 1 
ATOM   1063 N  NH1 B ARG B 1 13  ? -3.967  17.108  9.470  0.50 33.94  ? 13  ARG B NH1 1 
ATOM   1064 N  NH2 A ARG B 1 13  ? -6.049  12.634  8.389  0.50 25.83  ? 13  ARG B NH2 1 
ATOM   1065 N  NH2 B ARG B 1 13  ? -5.545  16.190  8.094  0.50 30.28  ? 13  ARG B NH2 1 
ATOM   1066 N  N   . GLN B 1 14  ? -4.413  13.757  15.992 1.00 28.32  ? 14  GLN B N   1 
ATOM   1067 C  CA  . GLN B 1 14  ? -5.115  12.627  16.592 1.00 27.25  ? 14  GLN B CA  1 
ATOM   1068 C  C   . GLN B 1 14  ? -5.987  13.033  17.794 1.00 27.64  ? 14  GLN B C   1 
ATOM   1069 O  O   . GLN B 1 14  ? -6.775  12.225  18.259 1.00 30.01  ? 14  GLN B O   1 
ATOM   1070 C  CB  . GLN B 1 14  ? -4.162  11.521  17.034 1.00 28.76  ? 14  GLN B CB  1 
ATOM   1071 C  CG  . GLN B 1 14  ? -3.251  11.888  18.213 1.00 27.99  ? 14  GLN B CG  1 
ATOM   1072 C  CD  . GLN B 1 14  ? -1.992  12.647  17.861 1.00 31.06  ? 14  GLN B CD  1 
ATOM   1073 O  OE1 . GLN B 1 14  ? -1.808  13.176  16.766 1.00 29.72  ? 14  GLN B OE1 1 
ATOM   1074 N  NE2 . GLN B 1 14  ? -1.097  12.741  18.821 1.00 33.74  ? 14  GLN B NE2 1 
ATOM   1075 N  N   . LYS B 1 15  ? -5.850  14.249  18.309 1.00 27.25  ? 15  LYS B N   1 
ATOM   1076 C  CA  . LYS B 1 15  ? -6.687  14.725  19.403 1.00 30.22  ? 15  LYS B CA  1 
ATOM   1077 C  C   . LYS B 1 15  ? -7.751  15.735  18.972 1.00 33.53  ? 15  LYS B C   1 
ATOM   1078 O  O   . LYS B 1 15  ? -8.479  16.257  19.822 1.00 33.47  ? 15  LYS B O   1 
ATOM   1079 C  CB  . LYS B 1 15  ? -5.833  15.445  20.454 1.00 28.04  ? 15  LYS B CB  1 
ATOM   1080 C  CG  . LYS B 1 15  ? -4.815  14.557  21.139 1.00 30.28  ? 15  LYS B CG  1 
ATOM   1081 C  CD  . LYS B 1 15  ? -5.455  13.354  21.797 1.00 27.14  ? 15  LYS B CD  1 
ATOM   1082 C  CE  . LYS B 1 15  ? -4.596  12.673  22.783 1.00 27.94  ? 15  LYS B CE  1 
ATOM   1083 N  NZ  . LYS B 1 15  ? -5.111  11.354  23.117 1.00 27.39  ? 15  LYS B NZ  1 
ATOM   1084 N  N   . ARG B 1 16  ? -7.849  16.031  17.666 1.00 32.95  ? 16  ARG B N   1 
ATOM   1085 C  CA  . ARG B 1 16  ? -8.865  16.952  17.172 1.00 33.39  ? 16  ARG B CA  1 
ATOM   1086 C  C   . ARG B 1 16  ? -10.277 16.381  17.347 1.00 32.52  ? 16  ARG B C   1 
ATOM   1087 O  O   . ARG B 1 16  ? -10.491 15.159  17.358 1.00 28.05  ? 16  ARG B O   1 
ATOM   1088 C  CB  . ARG B 1 16  ? -8.558  17.268  15.708 1.00 29.17  ? 16  ARG B CB  1 
ATOM   1089 C  CG  . ARG B 1 16  ? -7.352  18.174  15.593 1.00 30.34  ? 16  ARG B CG  1 
ATOM   1090 C  CD  . ARG B 1 16  ? -6.975  18.385  14.158 1.00 35.41  ? 16  ARG B CD  1 
ATOM   1091 N  NE  . ARG B 1 16  ? -5.771  19.206  14.040 1.00 37.84  ? 16  ARG B NE  1 
ATOM   1092 C  CZ  . ARG B 1 16  ? -5.151  19.517  12.913 1.00 42.19  ? 16  ARG B CZ  1 
ATOM   1093 N  NH1 . ARG B 1 16  ? -5.463  18.937  11.768 1.00 44.77  ? 16  ARG B NH1 1 
ATOM   1094 N  NH2 . ARG B 1 16  ? -4.186  20.402  12.953 1.00 47.15  ? 16  ARG B NH2 1 
ATOM   1095 N  N   . THR B 1 17  ? -11.226 17.315  17.530 1.00 35.24  ? 17  THR B N   1 
ATOM   1096 C  CA  . THR B 1 17  ? -12.656 17.024  17.565 1.00 32.76  ? 17  THR B CA  1 
ATOM   1097 C  C   . THR B 1 17  ? -13.314 17.799  16.426 1.00 34.73  ? 17  THR B C   1 
ATOM   1098 O  O   . THR B 1 17  ? -13.284 19.038  16.406 1.00 31.24  ? 17  THR B O   1 
ATOM   1099 C  CB  . THR B 1 17  ? -13.238 17.411  18.917 1.00 36.51  ? 17  THR B CB  1 
ATOM   1100 O  OG1 . THR B 1 17  ? -12.576 16.613  19.891 1.00 34.11  ? 17  THR B OG1 1 
ATOM   1101 C  CG2 . THR B 1 17  ? -14.716 17.093  19.013 1.00 41.68  ? 17  THR B CG2 1 
ATOM   1102 N  N   . ALA B 1 18  ? -13.885 17.069  15.459 1.00 31.94  ? 18  ALA B N   1 
ATOM   1103 C  CA  . ALA B 1 18  ? -14.634 17.764  14.415 1.00 33.96  ? 18  ALA B CA  1 
ATOM   1104 C  C   . ALA B 1 18  ? -16.023 18.164  14.929 1.00 31.26  ? 18  ALA B C   1 
ATOM   1105 O  O   . ALA B 1 18  ? -16.646 17.440  15.702 1.00 29.25  ? 18  ALA B O   1 
ATOM   1106 C  CB  . ALA B 1 18  ? -14.727 16.916  13.181 1.00 33.22  ? 18  ALA B CB  1 
ATOM   1107 N  N   . THR B 1 19  ? -16.473 19.345  14.491 1.00 34.50  ? 19  THR B N   1 
ATOM   1108 C  CA  . THR B 1 19  ? -17.786 19.919  14.802 1.00 37.69  ? 19  THR B CA  1 
ATOM   1109 C  C   . THR B 1 19  ? -18.258 20.660  13.555 1.00 41.57  ? 19  THR B C   1 
ATOM   1110 O  O   . THR B 1 19  ? -17.528 20.734  12.567 1.00 41.70  ? 19  THR B O   1 
ATOM   1111 C  CB  . THR B 1 19  ? -17.715 20.906  15.977 1.00 38.38  ? 19  THR B CB  1 
ATOM   1112 O  OG1 . THR B 1 19  ? -17.023 22.068  15.517 1.00 43.09  ? 19  THR B OG1 1 
ATOM   1113 C  CG2 . THR B 1 19  ? -16.992 20.355  17.189 1.00 43.63  ? 19  THR B CG2 1 
ATOM   1114 N  N   . LYS B 1 20  ? -19.425 21.306  13.625 1.00 45.40  ? 20  LYS B N   1 
ATOM   1115 C  CA  . LYS B 1 20  ? -19.862 22.145  12.516 1.00 45.53  ? 20  LYS B CA  1 
ATOM   1116 C  C   . LYS B 1 20  ? -18.881 23.295  12.278 1.00 42.73  ? 20  LYS B C   1 
ATOM   1117 O  O   . LYS B 1 20  ? -18.714 23.712  11.146 1.00 44.70  ? 20  LYS B O   1 
ATOM   1118 C  CB  . LYS B 1 20  ? -21.263 22.738  12.712 1.00 47.26  ? 20  LYS B CB  1 
ATOM   1119 C  CG  . LYS B 1 20  ? -22.376 21.725  12.765 1.00 55.40  ? 20  LYS B CG  1 
ATOM   1120 C  CD  . LYS B 1 20  ? -23.720 22.318  13.171 1.00 62.28  ? 20  LYS B CD  1 
ATOM   1121 C  CE  . LYS B 1 20  ? -24.727 21.206  13.322 1.00 71.15  ? 20  LYS B CE  1 
ATOM   1122 N  NZ  . LYS B 1 20  ? -26.058 21.710  13.669 1.00 74.22  ? 20  LYS B NZ  1 
ATOM   1123 N  N   . ALA B 1 21  ? -18.235 23.808  13.332 1.00 42.34  ? 21  ALA B N   1 
ATOM   1124 C  CA  . ALA B 1 21  ? -17.318 24.932  13.200 1.00 42.70  ? 21  ALA B CA  1 
ATOM   1125 C  C   . ALA B 1 21  ? -15.930 24.508  12.683 1.00 46.65  ? 21  ALA B C   1 
ATOM   1126 O  O   . ALA B 1 21  ? -15.130 25.354  12.269 1.00 49.70  ? 21  ALA B O   1 
ATOM   1127 C  CB  . ALA B 1 21  ? -17.196 25.611  14.530 1.00 42.11  ? 21  ALA B CB  1 
ATOM   1128 N  N   . TYR B 1 22  ? -15.636 23.203  12.735 1.00 43.36  ? 22  TYR B N   1 
ATOM   1129 C  CA  . TYR B 1 22  ? -14.349 22.661  12.353 1.00 36.47  ? 22  TYR B CA  1 
ATOM   1130 C  C   . TYR B 1 22  ? -14.571 21.230  11.881 1.00 37.68  ? 22  TYR B C   1 
ATOM   1131 O  O   . TYR B 1 22  ? -14.578 20.280  12.673 1.00 39.87  ? 22  TYR B O   1 
ATOM   1132 C  CB  . TYR B 1 22  ? -13.401 22.712  13.563 1.00 41.55  ? 22  TYR B CB  1 
ATOM   1133 C  CG  . TYR B 1 22  ? -11.940 22.351  13.304 1.00 38.70  ? 22  TYR B CG  1 
ATOM   1134 C  CD1 . TYR B 1 22  ? -11.242 22.897  12.226 1.00 43.32  ? 22  TYR B CD1 1 
ATOM   1135 C  CD2 . TYR B 1 22  ? -11.272 21.406  14.095 1.00 37.67  ? 22  TYR B CD2 1 
ATOM   1136 C  CE1 . TYR B 1 22  ? -9.924  22.535  11.957 1.00 44.56  ? 22  TYR B CE1 1 
ATOM   1137 C  CE2 . TYR B 1 22  ? -9.961  21.055  13.846 1.00 37.55  ? 22  TYR B CE2 1 
ATOM   1138 C  CZ  . TYR B 1 22  ? -9.287  21.608  12.768 1.00 42.35  ? 22  TYR B CZ  1 
ATOM   1139 O  OH  . TYR B 1 22  ? -7.982  21.245  12.551 1.00 46.38  ? 22  TYR B OH  1 
ATOM   1140 N  N   . ASN B 1 23  ? -14.824 21.091  10.593 1.00 34.48  ? 23  ASN B N   1 
ATOM   1141 C  CA  . ASN B 1 23  ? -15.496 19.895  10.101 1.00 38.86  ? 23  ASN B CA  1 
ATOM   1142 C  C   . ASN B 1 23  ? -14.462 18.806  9.816  1.00 32.98  ? 23  ASN B C   1 
ATOM   1143 O  O   . ASN B 1 23  ? -13.274 19.019  9.987  1.00 35.10  ? 23  ASN B O   1 
ATOM   1144 C  CB  . ASN B 1 23  ? -16.437 20.215  8.931  1.00 38.87  ? 23  ASN B CB  1 
ATOM   1145 C  CG  . ASN B 1 23  ? -15.712 20.614  7.670  1.00 45.30  ? 23  ASN B CG  1 
ATOM   1146 O  OD1 . ASN B 1 23  ? -14.648 20.088  7.362  1.00 44.65  ? 23  ASN B OD1 1 
ATOM   1147 N  ND2 . ASN B 1 23  ? -16.236 21.587  6.949  1.00 52.12  ? 23  ASN B ND2 1 
ATOM   1148 N  N   . VAL B 1 24  ? -14.925 17.653  9.339  1.00 29.82  ? 24  VAL B N   1 
ATOM   1149 C  CA  . VAL B 1 24  ? -14.052 16.510  9.202  1.00 31.73  ? 24  VAL B CA  1 
ATOM   1150 C  C   . VAL B 1 24  ? -12.981 16.795  8.152  1.00 38.20  ? 24  VAL B C   1 
ATOM   1151 O  O   . VAL B 1 24  ? -11.819 16.437  8.343  1.00 35.25  ? 24  VAL B O   1 
ATOM   1152 C  CB  . VAL B 1 24  ? -14.891 15.281  8.854  1.00 31.60  ? 24  VAL B CB  1 
ATOM   1153 C  CG1 . VAL B 1 24  ? -14.040 14.112  8.391  1.00 31.29  ? 24  VAL B CG1 1 
ATOM   1154 C  CG2 . VAL B 1 24  ? -15.756 14.893  10.046 1.00 33.73  ? 24  VAL B CG2 1 
ATOM   1155 N  N   . THR B 1 25  ? -13.353 17.473  7.059  1.00 37.02  ? 25  THR B N   1 
ATOM   1156 C  CA  . THR B 1 25  ? -12.371 17.837  6.044  1.00 37.54  ? 25  THR B CA  1 
ATOM   1157 C  C   . THR B 1 25  ? -11.307 18.754  6.649  1.00 32.70  ? 25  THR B C   1 
ATOM   1158 O  O   . THR B 1 25  ? -10.127 18.592  6.397  1.00 33.97  ? 25  THR B O   1 
ATOM   1159 C  CB  . THR B 1 25  ? -13.068 18.500  4.853  1.00 36.30  ? 25  THR B CB  1 
ATOM   1160 O  OG1 . THR B 1 25  ? -13.865 17.441  4.325  1.00 35.08  ? 25  THR B OG1 1 
ATOM   1161 C  CG2 . THR B 1 25  ? -12.078 18.967  3.795  1.00 40.76  ? 25  THR B CG2 1 
ATOM   1162 N  N   . GLN B 1 26  ? -11.739 19.756  7.404  1.00 33.89  ? 26  GLN B N   1 
ATOM   1163 C  CA  . GLN B 1 26  ? -10.813 20.745  7.915  1.00 36.62  ? 26  GLN B CA  1 
ATOM   1164 C  C   . GLN B 1 26  ? -9.895  20.099  8.950  1.00 39.01  ? 26  GLN B C   1 
ATOM   1165 O  O   . GLN B 1 26  ? -8.698  20.355  8.954  1.00 42.51  ? 26  GLN B O   1 
ATOM   1166 C  CB  . GLN B 1 26  ? -11.611 21.847  8.583  1.00 41.25  ? 26  GLN B CB  1 
ATOM   1167 C  CG  . GLN B 1 26  ? -12.442 22.677  7.615  1.00 44.66  ? 26  GLN B CG  1 
ATOM   1168 C  CD  . GLN B 1 26  ? -13.209 23.718  8.391  1.00 48.19  ? 26  GLN B CD  1 
ATOM   1169 O  OE1 . GLN B 1 26  ? -14.172 23.424  9.102  1.00 48.16  ? 26  GLN B OE1 1 
ATOM   1170 N  NE2 . GLN B 1 26  ? -12.708 24.942  8.350  1.00 57.80  ? 26  GLN B NE2 1 
ATOM   1171 N  N   . ALA B 1 27  ? -10.444 19.206  9.784  1.00 34.68  ? 27  ALA B N   1 
ATOM   1172 C  CA  . ALA B 1 27  ? -9.644  18.558  10.816 1.00 32.47  ? 27  ALA B CA  1 
ATOM   1173 C  C   . ALA B 1 27  ? -8.776  17.436  10.256 1.00 31.81  ? 27  ALA B C   1 
ATOM   1174 O  O   . ALA B 1 27  ? -7.665  17.250  10.745 1.00 36.51  ? 27  ALA B O   1 
ATOM   1175 C  CB  . ALA B 1 27  ? -10.529 18.031  11.929 1.00 35.08  ? 27  ALA B CB  1 
ATOM   1176 N  N   . PHE B 1 28  ? -9.301  16.621  9.332  1.00 30.72  ? 28  PHE B N   1 
ATOM   1177 C  CA  . PHE B 1 28  ? -8.694  15.334  9.040  1.00 31.03  ? 28  PHE B CA  1 
ATOM   1178 C  C   . PHE B 1 28  ? -8.443  15.125  7.547  1.00 32.08  ? 28  PHE B C   1 
ATOM   1179 O  O   . PHE B 1 28  ? -8.063  14.014  7.127  1.00 29.42  ? 28  PHE B O   1 
ATOM   1180 C  CB  . PHE B 1 28  ? -9.574  14.206  9.573  1.00 29.74  ? 28  PHE B CB  1 
ATOM   1181 C  CG  . PHE B 1 28  ? -9.857  14.322  11.063 1.00 31.77  ? 28  PHE B CG  1 
ATOM   1182 C  CD1 . PHE B 1 28  ? -11.159 14.380  11.545 1.00 33.72  ? 28  PHE B CD1 1 
ATOM   1183 C  CD2 . PHE B 1 28  ? -8.811  14.383  11.989 1.00 33.81  ? 28  PHE B CD2 1 
ATOM   1184 C  CE1 . PHE B 1 28  ? -11.417 14.478  12.908 1.00 29.89  ? 28  PHE B CE1 1 
ATOM   1185 C  CE2 . PHE B 1 28  ? -9.076  14.482  13.343 1.00 31.53  ? 28  PHE B CE2 1 
ATOM   1186 C  CZ  . PHE B 1 28  ? -10.374 14.532  13.801 1.00 29.95  ? 28  PHE B CZ  1 
ATOM   1187 N  N   . GLY B 1 29  ? -8.683  16.166  6.742  1.00 34.09  ? 29  GLY B N   1 
ATOM   1188 C  CA  . GLY B 1 29  ? -8.503  16.065  5.306  1.00 33.43  ? 29  GLY B CA  1 
ATOM   1189 C  C   . GLY B 1 29  ? -9.725  15.500  4.571  1.00 36.53  ? 29  GLY B C   1 
ATOM   1190 O  O   . GLY B 1 29  ? -10.595 14.864  5.167  1.00 31.58  ? 29  GLY B O   1 
ATOM   1191 N  N   . ARG B 1 30  ? -9.752  15.738  3.248  1.00 34.28  ? 30  ARG B N   1 
ATOM   1192 C  CA  A ARG B 1 30  ? -10.712 15.122  2.342  0.70 38.52  ? 30  ARG B CA  1 
ATOM   1193 C  CA  B ARG B 1 30  ? -10.740 15.134  2.367  0.30 35.14  ? 30  ARG B CA  1 
ATOM   1194 C  C   . ARG B 1 30  ? -10.688 13.609  2.478  1.00 31.74  ? 30  ARG B C   1 
ATOM   1195 O  O   . ARG B 1 30  ? -9.630  13.014  2.585  1.00 29.60  ? 30  ARG B O   1 
ATOM   1196 C  CB  A ARG B 1 30  ? -10.373 15.446  0.884  0.70 41.83  ? 30  ARG B CB  1 
ATOM   1197 C  CB  B ARG B 1 30  ? -10.481 15.593  0.927  0.30 36.25  ? 30  ARG B CB  1 
ATOM   1198 C  CG  A ARG B 1 30  ? -10.818 16.840  0.475  0.70 49.16  ? 30  ARG B CG  1 
ATOM   1199 C  CG  B ARG B 1 30  ? -10.410 17.102  0.740  0.30 38.68  ? 30  ARG B CG  1 
ATOM   1200 C  CD  A ARG B 1 30  ? -10.313 17.193  -0.931 0.70 54.23  ? 30  ARG B CD  1 
ATOM   1201 C  CD  B ARG B 1 30  ? -11.760 17.782  0.497  0.30 40.30  ? 30  ARG B CD  1 
ATOM   1202 N  NE  A ARG B 1 30  ? -11.189 18.134  -1.639 0.70 65.45  ? 30  ARG B NE  1 
ATOM   1203 N  NE  B ARG B 1 30  ? -11.585 19.226  0.288  0.30 38.60  ? 30  ARG B NE  1 
ATOM   1204 C  CZ  A ARG B 1 30  ? -11.174 18.360  -2.961 0.70 69.63  ? 30  ARG B CZ  1 
ATOM   1205 C  CZ  B ARG B 1 30  ? -12.562 20.120  0.235  0.30 38.11  ? 30  ARG B CZ  1 
ATOM   1206 N  NH1 A ARG B 1 30  ? -10.283 17.776  -3.744 0.70 58.54  ? 30  ARG B NH1 1 
ATOM   1207 N  NH1 B ARG B 1 30  ? -12.270 21.408  0.217  0.30 37.24  ? 30  ARG B NH1 1 
ATOM   1208 N  NH2 A ARG B 1 30  ? -12.056 19.185  -3.504 0.70 79.52  ? 30  ARG B NH2 1 
ATOM   1209 N  NH2 B ARG B 1 30  ? -13.823 19.728  0.254  0.30 37.75  ? 30  ARG B NH2 1 
ATOM   1210 N  N   . ARG B 1 31  ? -11.862 12.975  2.495  1.00 29.41  ? 31  ARG B N   1 
ATOM   1211 C  CA  . ARG B 1 31  ? -11.922 11.527  2.354  1.00 27.08  ? 31  ARG B CA  1 
ATOM   1212 C  C   . ARG B 1 31  ? -11.360 11.121  0.996  1.00 28.18  ? 31  ARG B C   1 
ATOM   1213 O  O   . ARG B 1 31  ? -11.410 11.871  0.013  1.00 29.98  ? 31  ARG B O   1 
ATOM   1214 C  CB  . ARG B 1 31  ? -13.379 11.048  2.497  1.00 30.49  ? 31  ARG B CB  1 
ATOM   1215 C  CG  . ARG B 1 31  ? -13.903 10.806  3.914  1.00 27.98  ? 31  ARG B CG  1 
ATOM   1216 C  CD  . ARG B 1 31  ? -14.100 12.103  4.669  1.00 28.45  ? 31  ARG B CD  1 
ATOM   1217 N  NE  . ARG B 1 31  ? -12.893 12.660  5.275  1.00 28.06  ? 31  ARG B NE  1 
ATOM   1218 C  CZ  . ARG B 1 31  ? -12.167 12.028  6.226  1.00 30.99  ? 31  ARG B CZ  1 
ATOM   1219 N  NH1 . ARG B 1 31  ? -10.986 12.527  6.555  1.00 27.46  ? 31  ARG B NH1 1 
ATOM   1220 N  NH2 . ARG B 1 31  ? -12.583 10.893  6.801  1.00 28.23  ? 31  ARG B NH2 1 
ATOM   1221 N  N   . GLY B 1 32  ? -10.838 9.907   0.919  1.00 31.24  ? 32  GLY B N   1 
ATOM   1222 C  CA  . GLY B 1 32  ? -10.232 9.460   -0.314 1.00 34.14  ? 32  GLY B CA  1 
ATOM   1223 C  C   . GLY B 1 32  ? -9.774  8.018   -0.188 1.00 30.63  ? 32  GLY B C   1 
ATOM   1224 O  O   . GLY B 1 32  ? -9.962  7.430   0.863  1.00 32.18  ? 32  GLY B O   1 
ATOM   1225 N  N   . PRO B 1 33  ? -9.196  7.434   -1.274 1.00 31.82  ? 33  PRO B N   1 
ATOM   1226 C  CA  . PRO B 1 33  ? -8.793  6.028   -1.297 1.00 30.42  ? 33  PRO B CA  1 
ATOM   1227 C  C   . PRO B 1 33  ? -7.359  5.693   -0.867 1.00 31.79  ? 33  PRO B C   1 
ATOM   1228 O  O   . PRO B 1 33  ? -6.986  4.522   -0.745 1.00 28.70  ? 33  PRO B O   1 
ATOM   1229 C  CB  . PRO B 1 33  ? -8.989  5.738   -2.798 1.00 33.56  ? 33  PRO B CB  1 
ATOM   1230 C  CG  . PRO B 1 33  ? -8.589  7.006   -3.507 1.00 29.67  ? 33  PRO B CG  1 
ATOM   1231 C  CD  . PRO B 1 33  ? -8.973  8.125   -2.557 1.00 32.46  ? 33  PRO B CD  1 
ATOM   1232 N  N   . GLU B 1 34  ? -6.539  6.720   -0.662 1.00 33.17  ? 34  GLU B N   1 
ATOM   1233 C  CA  . GLU B 1 34  ? -5.104  6.492   -0.458 1.00 35.86  ? 34  GLU B CA  1 
ATOM   1234 C  C   . GLU B 1 34  ? -4.834  5.934   0.945  1.00 41.58  ? 34  GLU B C   1 
ATOM   1235 O  O   . GLU B 1 34  ? -5.643  6.077   1.869  1.00 34.08  ? 34  GLU B O   1 
ATOM   1236 C  CB  . GLU B 1 34  ? -4.266  7.739   -0.727 1.00 35.55  ? 34  GLU B CB  1 
ATOM   1237 C  CG  . GLU B 1 34  ? -4.446  8.340   -2.124 1.00 35.38  ? 34  GLU B CG  1 
ATOM   1238 C  CD  . GLU B 1 34  ? -4.205  7.414   -3.322 1.00 39.58  ? 34  GLU B CD  1 
ATOM   1239 O  OE1 . GLU B 1 34  ? -3.539  6.386   -3.146 1.00 38.81  ? 34  GLU B OE1 1 
ATOM   1240 O  OE2 . GLU B 1 34  ? -4.729  7.687   -4.434 1.00 39.66  ? 34  GLU B OE2 1 
ATOM   1241 N  N   . GLN B 1 35  ? -3.640  5.353   1.090  1.00 43.45  ? 35  GLN B N   1 
ATOM   1242 C  CA  . GLN B 1 35  ? -3.327  4.376   2.119  1.00 48.58  ? 35  GLN B CA  1 
ATOM   1243 C  C   . GLN B 1 35  ? -3.392  5.001   3.506  1.00 40.85  ? 35  GLN B C   1 
ATOM   1244 O  O   . GLN B 1 35  ? -3.719  4.309   4.461  1.00 42.91  ? 35  GLN B O   1 
ATOM   1245 C  CB  . GLN B 1 35  ? -1.975  3.732   1.810  1.00 54.08  ? 35  GLN B CB  1 
ATOM   1246 C  CG  . GLN B 1 35  ? -1.668  2.466   2.603  1.00 64.71  ? 35  GLN B CG  1 
ATOM   1247 C  CD  . GLN B 1 35  ? -2.858  1.551   2.810  1.00 76.49  ? 35  GLN B CD  1 
ATOM   1248 O  OE1 . GLN B 1 35  ? -3.053  0.565   2.085  1.00 94.93  ? 35  GLN B OE1 1 
ATOM   1249 N  NE2 . GLN B 1 35  ? -3.663  1.860   3.820  1.00 74.40  ? 35  GLN B NE2 1 
ATOM   1250 N  N   . THR B 1 36  ? -3.190  6.306   3.626  1.00 37.94  ? 36  THR B N   1 
ATOM   1251 C  CA  . THR B 1 36  ? -3.379  6.889   4.946  1.00 37.87  ? 36  THR B CA  1 
ATOM   1252 C  C   . THR B 1 36  ? -4.302  8.106   4.876  1.00 41.88  ? 36  THR B C   1 
ATOM   1253 O  O   . THR B 1 36  ? -4.228  9.008   5.722  1.00 39.19  ? 36  THR B O   1 
ATOM   1254 C  CB  . THR B 1 36  ? -1.999  7.221   5.554  1.00 45.25  ? 36  THR B CB  1 
ATOM   1255 O  OG1 . THR B 1 36  ? -1.344  8.179   4.721  1.00 37.19  ? 36  THR B OG1 1 
ATOM   1256 C  CG2 . THR B 1 36  ? -1.131  5.992   5.773  1.00 38.11  ? 36  THR B CG2 1 
ATOM   1257 N  N   . GLN B 1 37  ? -5.209  8.134   3.874  1.00 40.35  ? 37  GLN B N   1 
ATOM   1258 C  CA  . GLN B 1 37  ? -6.354  9.045   3.900  1.00 39.90  ? 37  GLN B CA  1 
ATOM   1259 C  C   . GLN B 1 37  ? -7.527  8.349   4.604  1.00 28.05  ? 37  GLN B C   1 
ATOM   1260 O  O   . GLN B 1 37  ? -7.709  7.132   4.472  1.00 29.75  ? 37  GLN B O   1 
ATOM   1261 C  CB  . GLN B 1 37  ? -6.976  9.371   2.540  1.00 44.94  ? 37  GLN B CB  1 
ATOM   1262 C  CG  . GLN B 1 37  ? -6.330  10.496  1.757  1.00 51.78  ? 37  GLN B CG  1 
ATOM   1263 C  CD  . GLN B 1 37  ? -6.886  10.565  0.353  1.00 41.28  ? 37  GLN B CD  1 
ATOM   1264 O  OE1 . GLN B 1 37  ? -6.917  9.572   -0.381 1.00 34.39  ? 37  GLN B OE1 1 
ATOM   1265 N  NE2 . GLN B 1 37  ? -7.353  11.742  -0.009 1.00 45.25  ? 37  GLN B NE2 1 
ATOM   1266 N  N   . GLY B 1 38  ? -8.324  9.140   5.312  1.00 27.45  ? 38  GLY B N   1 
ATOM   1267 C  CA  . GLY B 1 38  ? -9.583  8.642   5.867  1.00 30.30  ? 38  GLY B CA  1 
ATOM   1268 C  C   . GLY B 1 38  ? -10.629 8.372   4.773  1.00 28.12  ? 38  GLY B C   1 
ATOM   1269 O  O   . GLY B 1 38  ? -10.674 9.108   3.802  1.00 28.90  ? 38  GLY B O   1 
ATOM   1270 N  N   . ASN B 1 39  ? -11.447 7.335   4.934  1.00 28.33  ? 39  ASN B N   1 
ATOM   1271 C  CA  . ASN B 1 39  ? -12.467 7.010   3.954  1.00 27.49  ? 39  ASN B CA  1 
ATOM   1272 C  C   . ASN B 1 39  ? -13.873 7.076   4.545  1.00 29.99  ? 39  ASN B C   1 
ATOM   1273 O  O   . ASN B 1 39  ? -14.810 6.632   3.887  1.00 30.64  ? 39  ASN B O   1 
ATOM   1274 C  CB  . ASN B 1 39  ? -12.292 5.603   3.398  1.00 25.09  ? 39  ASN B CB  1 
ATOM   1275 C  CG  . ASN B 1 39  ? -12.411 4.551   4.468  1.00 30.90  ? 39  ASN B CG  1 
ATOM   1276 O  OD1 . ASN B 1 39  ? -12.232 4.855   5.654  1.00 31.62  ? 39  ASN B OD1 1 
ATOM   1277 N  ND2 . ASN B 1 39  ? -12.689 3.315   4.084  1.00 31.96  ? 39  ASN B ND2 1 
ATOM   1278 N  N   . PHE B 1 40  ? -14.040 7.606   5.771  1.00 28.08  ? 40  PHE B N   1 
ATOM   1279 C  CA  . PHE B 1 40  ? -15.283 7.424   6.518  1.00 26.24  ? 40  PHE B CA  1 
ATOM   1280 C  C   . PHE B 1 40  ? -16.019 8.752   6.610  1.00 27.90  ? 40  PHE B C   1 
ATOM   1281 O  O   . PHE B 1 40  ? -15.474 9.780   7.024  1.00 25.29  ? 40  PHE B O   1 
ATOM   1282 C  CB  . PHE B 1 40  ? -15.047 6.844   7.915  1.00 29.88  ? 40  PHE B CB  1 
ATOM   1283 C  CG  . PHE B 1 40  ? -16.274 6.428   8.719  1.00 26.18  ? 40  PHE B CG  1 
ATOM   1284 C  CD1 . PHE B 1 40  ? -16.942 7.332   9.534  1.00 24.77  ? 40  PHE B CD1 1 
ATOM   1285 C  CD2 . PHE B 1 40  ? -16.724 5.119   8.685  1.00 23.18  ? 40  PHE B CD2 1 
ATOM   1286 C  CE1 . PHE B 1 40  ? -18.031 6.932   10.305 1.00 23.80  ? 40  PHE B CE1 1 
ATOM   1287 C  CE2 . PHE B 1 40  ? -17.814 4.716   9.455  1.00 25.21  ? 40  PHE B CE2 1 
ATOM   1288 C  CZ  . PHE B 1 40  ? -18.475 5.632   10.260 1.00 26.46  ? 40  PHE B CZ  1 
ATOM   1289 N  N   . GLY B 1 41  ? -17.306 8.710   6.242  1.00 27.41  ? 41  GLY B N   1 
ATOM   1290 C  CA  . GLY B 1 41  ? -18.172 9.866   6.396  1.00 29.54  ? 41  GLY B CA  1 
ATOM   1291 C  C   . GLY B 1 41  ? -18.973 10.128  5.118  1.00 33.44  ? 41  GLY B C   1 
ATOM   1292 O  O   . GLY B 1 41  ? -18.384 10.309  4.046  1.00 31.29  ? 41  GLY B O   1 
ATOM   1293 N  N   . ASP B 1 42  ? -20.308 10.174  5.240  1.00 30.74  ? 42  ASP B N   1 
ATOM   1294 C  CA  . ASP B 1 42  ? -21.148 10.749  4.197  1.00 30.92  ? 42  ASP B CA  1 
ATOM   1295 C  C   . ASP B 1 42  ? -21.125 12.268  4.340  1.00 27.79  ? 42  ASP B C   1 
ATOM   1296 O  O   . ASP B 1 42  ? -20.474 12.817  5.212  1.00 27.72  ? 42  ASP B O   1 
ATOM   1297 C  CB  . ASP B 1 42  ? -22.547 10.148  4.246  1.00 30.91  ? 42  ASP B CB  1 
ATOM   1298 C  CG  . ASP B 1 42  ? -23.438 10.607  5.392  1.00 32.75  ? 42  ASP B CG  1 
ATOM   1299 O  OD1 . ASP B 1 42  ? -24.541 10.021  5.521  1.00 42.69  ? 42  ASP B OD1 1 
ATOM   1300 O  OD2 . ASP B 1 42  ? -23.065 11.572  6.115  1.00 32.07  ? 42  ASP B OD2 1 
ATOM   1301 N  N   . GLN B 1 43  ? -21.882 12.983  3.517  1.00 30.08  ? 43  GLN B N   1 
ATOM   1302 C  CA  A GLN B 1 43  ? -21.738 14.437  3.471  0.50 34.09  ? 43  GLN B CA  1 
ATOM   1303 C  CA  B GLN B 1 43  ? -21.790 14.436  3.453  0.50 32.47  ? 43  GLN B CA  1 
ATOM   1304 C  C   . GLN B 1 43  ? -22.222 15.060  4.780  1.00 35.06  ? 43  GLN B C   1 
ATOM   1305 O  O   . GLN B 1 43  ? -21.671 16.069  5.255  1.00 34.72  ? 43  GLN B O   1 
ATOM   1306 C  CB  A GLN B 1 43  ? -22.416 15.038  2.236  0.50 37.81  ? 43  GLN B CB  1 
ATOM   1307 C  CB  B GLN B 1 43  ? -22.655 14.877  2.269  0.50 33.76  ? 43  GLN B CB  1 
ATOM   1308 C  CG  A GLN B 1 43  ? -21.547 14.972  0.980  0.50 38.14  ? 43  GLN B CG  1 
ATOM   1309 C  CG  B GLN B 1 43  ? -22.386 14.096  0.982  0.50 31.31  ? 43  GLN B CG  1 
ATOM   1310 C  CD  A GLN B 1 43  ? -22.198 15.515  -0.276 0.50 40.31  ? 43  GLN B CD  1 
ATOM   1311 C  CD  B GLN B 1 43  ? -23.484 13.142  0.557  0.50 29.91  ? 43  GLN B CD  1 
ATOM   1312 O  OE1 A GLN B 1 43  ? -21.795 16.547  -0.831 0.50 39.35  ? 43  GLN B OE1 1 
ATOM   1313 O  OE1 B GLN B 1 43  ? -24.092 13.349  -0.508 0.50 30.81  ? 43  GLN B OE1 1 
ATOM   1314 N  NE2 A GLN B 1 43  ? -23.214 14.804  -0.744 0.50 38.41  ? 43  GLN B NE2 1 
ATOM   1315 N  NE2 B GLN B 1 43  ? -23.742 12.088  1.338  0.50 24.29  ? 43  GLN B NE2 1 
ATOM   1316 N  N   . GLU B 1 44  ? -23.258 14.470  5.376  1.00 33.92  ? 44  GLU B N   1 
ATOM   1317 C  CA  . GLU B 1 44  ? -23.802 15.020  6.607  1.00 36.94  ? 44  GLU B CA  1 
ATOM   1318 C  C   . GLU B 1 44  ? -22.765 14.908  7.735  1.00 31.15  ? 44  GLU B C   1 
ATOM   1319 O  O   . GLU B 1 44  ? -22.510 15.875  8.465  1.00 31.72  ? 44  GLU B O   1 
ATOM   1320 C  CB  . GLU B 1 44  ? -25.111 14.287  6.932  1.00 42.85  ? 44  GLU B CB  1 
ATOM   1321 C  CG  . GLU B 1 44  ? -26.009 15.049  7.901  1.00 43.51  ? 44  GLU B CG  1 
ATOM   1322 C  CD  . GLU B 1 44  ? -27.203 14.254  8.404  1.00 46.52  ? 44  GLU B CD  1 
ATOM   1323 O  OE1 . GLU B 1 44  ? -27.334 13.046  8.140  1.00 41.39  ? 44  GLU B OE1 1 
ATOM   1324 O  OE2 . GLU B 1 44  ? -28.027 14.894  9.066  1.00 45.75  ? 44  GLU B OE2 1 
ATOM   1325 N  N   . LEU B 1 45  ? -22.213 13.706  7.903  1.00 29.68  ? 45  LEU B N   1 
ATOM   1326 C  CA  . LEU B 1 45  ? -21.204 13.488  8.942  1.00 34.09  ? 45  LEU B CA  1 
ATOM   1327 C  C   . LEU B 1 45  ? -19.990 14.385  8.712  1.00 33.69  ? 45  LEU B C   1 
ATOM   1328 O  O   . LEU B 1 45  ? -19.508 15.012  9.657  1.00 32.82  ? 45  LEU B O   1 
ATOM   1329 C  CB  . LEU B 1 45  ? -20.766 12.031  9.047  1.00 32.45  ? 45  LEU B CB  1 
ATOM   1330 C  CG  . LEU B 1 45  ? -19.622 11.754  10.032 1.00 32.76  ? 45  LEU B CG  1 
ATOM   1331 C  CD1 . LEU B 1 45  ? -19.915 12.357  11.406 1.00 37.47  ? 45  LEU B CD1 1 
ATOM   1332 C  CD2 . LEU B 1 45  ? -19.465 10.278  10.175 1.00 27.42  ? 45  LEU B CD2 1 
ATOM   1333 N  N   . ILE B 1 46  ? -19.540 14.491  7.459  1.00 31.66  ? 46  ILE B N   1 
ATOM   1334 C  CA  . ILE B 1 46  ? -18.358 15.295  7.159  1.00 30.38  ? 46  ILE B CA  1 
ATOM   1335 C  C   . ILE B 1 46  ? -18.578 16.727  7.619  1.00 33.14  ? 46  ILE B C   1 
ATOM   1336 O  O   . ILE B 1 46  ? -17.680 17.344  8.206  1.00 34.62  ? 46  ILE B O   1 
ATOM   1337 C  CB  . ILE B 1 46  ? -18.016 15.204  5.661  1.00 34.11  ? 46  ILE B CB  1 
ATOM   1338 C  CG1 . ILE B 1 46  ? -17.414 13.854  5.326  1.00 34.76  ? 46  ILE B CG1 1 
ATOM   1339 C  CG2 . ILE B 1 46  ? -17.145 16.363  5.182  1.00 34.78  ? 46  ILE B CG2 1 
ATOM   1340 C  CD1 . ILE B 1 46  ? -17.329 13.561  3.836  1.00 36.82  ? 46  ILE B CD1 1 
ATOM   1341 N  N   . ARG B 1 47  ? -19.781 17.266  7.362  1.00 35.62  ? 47  ARG B N   1 
ATOM   1342 C  CA  . ARG B 1 47  ? -20.022 18.676  7.630  1.00 37.22  ? 47  ARG B CA  1 
ATOM   1343 C  C   . ARG B 1 47  ? -20.300 18.931  9.102  1.00 34.31  ? 47  ARG B C   1 
ATOM   1344 O  O   . ARG B 1 47  ? -20.034 20.019  9.581  1.00 36.12  ? 47  ARG B O   1 
ATOM   1345 C  CB  . ARG B 1 47  ? -21.100 19.320  6.755  1.00 43.55  ? 47  ARG B CB  1 
ATOM   1346 C  CG  . ARG B 1 47  ? -22.548 18.880  6.799  1.00 49.11  ? 47  ARG B CG  1 
ATOM   1347 C  CD  . ARG B 1 47  ? -23.282 19.720  5.704  1.00 47.24  ? 47  ARG B CD  1 
ATOM   1348 N  NE  . ARG B 1 47  ? -24.507 19.057  5.278  1.00 44.16  ? 47  ARG B NE  1 
ATOM   1349 C  CZ  . ARG B 1 47  ? -25.529 18.921  6.103  1.00 51.25  ? 47  ARG B CZ  1 
ATOM   1350 N  NH1 . ARG B 1 47  ? -26.415 17.949  5.943  1.00 51.91  ? 47  ARG B NH1 1 
ATOM   1351 N  NH2 . ARG B 1 47  ? -25.591 19.696  7.163  1.00 52.48  ? 47  ARG B NH2 1 
ATOM   1352 N  N   . GLN B 1 48  ? -20.743 17.932  9.852  1.00 36.99  ? 48  GLN B N   1 
ATOM   1353 C  CA  . GLN B 1 48  ? -21.119 18.177  11.247 1.00 41.06  ? 48  GLN B CA  1 
ATOM   1354 C  C   . GLN B 1 48  ? -20.166 17.585  12.295 1.00 39.46  ? 48  GLN B C   1 
ATOM   1355 O  O   . GLN B 1 48  ? -20.190 17.975  13.459 1.00 38.12  ? 48  GLN B O   1 
ATOM   1356 C  CB  . GLN B 1 48  ? -22.500 17.565  11.454 1.00 39.64  ? 48  GLN B CB  1 
ATOM   1357 C  CG  . GLN B 1 48  ? -23.586 18.273  10.637 1.00 40.36  ? 48  GLN B CG  1 
ATOM   1358 C  CD  . GLN B 1 48  ? -24.943 17.612  10.769 1.00 43.84  ? 48  GLN B CD  1 
ATOM   1359 O  OE1 . GLN B 1 48  ? -25.081 16.442  11.137 1.00 41.90  ? 48  GLN B OE1 1 
ATOM   1360 N  NE2 . GLN B 1 48  ? -25.989 18.356  10.449 1.00 51.21  ? 48  GLN B NE2 1 
ATOM   1361 N  N   . GLY B 1 49  ? -19.393 16.573  11.917 1.00 37.22  ? 49  GLY B N   1 
ATOM   1362 C  CA  . GLY B 1 49  ? -18.469 15.970  12.851 1.00 37.74  ? 49  GLY B CA  1 
ATOM   1363 C  C   . GLY B 1 49  ? -19.230 15.431  14.055 1.00 35.28  ? 49  GLY B C   1 
ATOM   1364 O  O   . GLY B 1 49  ? -20.170 14.685  13.878 1.00 37.67  ? 49  GLY B O   1 
ATOM   1365 N  N   . THR B 1 50  ? -18.823 15.830  15.266 1.00 32.32  ? 50  THR B N   1 
ATOM   1366 C  CA  . THR B 1 50  ? -19.388 15.244  16.471 1.00 36.17  ? 50  THR B CA  1 
ATOM   1367 C  C   . THR B 1 50  ? -20.741 15.895  16.757 1.00 35.94  ? 50  THR B C   1 
ATOM   1368 O  O   . THR B 1 50  ? -21.439 15.416  17.635 1.00 36.24  ? 50  THR B O   1 
ATOM   1369 C  CB  . THR B 1 50  ? -18.438 15.347  17.673 1.00 35.70  ? 50  THR B CB  1 
ATOM   1370 O  OG1 . THR B 1 50  ? -18.106 16.706  17.902 1.00 31.21  ? 50  THR B OG1 1 
ATOM   1371 C  CG2 . THR B 1 50  ? -17.130 14.593  17.483 1.00 34.52  ? 50  THR B CG2 1 
ATOM   1372 N  N   . ASP B 1 51  ? -21.130 16.913  15.974 1.00 36.19  ? 51  ASP B N   1 
ATOM   1373 C  CA  . ASP B 1 51  ? -22.484 17.458  16.008 1.00 37.66  ? 51  ASP B CA  1 
ATOM   1374 C  C   . ASP B 1 51  ? -23.484 16.605  15.224 1.00 39.93  ? 51  ASP B C   1 
ATOM   1375 O  O   . ASP B 1 51  ? -24.688 16.831  15.351 1.00 43.09  ? 51  ASP B O   1 
ATOM   1376 C  CB  . ASP B 1 51  ? -22.532 18.903  15.540 1.00 42.75  ? 51  ASP B CB  1 
ATOM   1377 C  CG  . ASP B 1 51  ? -21.715 19.878  16.377 1.00 42.90  ? 51  ASP B CG  1 
ATOM   1378 O  OD1 . ASP B 1 51  ? -21.105 20.821  15.795 1.00 48.16  ? 51  ASP B OD1 1 
ATOM   1379 O  OD2 . ASP B 1 51  ? -21.620 19.650  17.585 1.00 47.29  ? 51  ASP B OD2 1 
ATOM   1380 N  N   . TYR B 1 52  ? -23.030 15.616  14.433 1.00 33.43  ? 52  TYR B N   1 
ATOM   1381 C  CA  . TYR B 1 52  ? -23.928 14.672  13.785 1.00 30.88  ? 52  TYR B CA  1 
ATOM   1382 C  C   . TYR B 1 52  ? -24.853 14.044  14.810 1.00 33.27  ? 52  TYR B C   1 
ATOM   1383 O  O   . TYR B 1 52  ? -24.387 13.580  15.839 1.00 29.96  ? 52  TYR B O   1 
ATOM   1384 C  CB  . TYR B 1 52  ? -23.140 13.543  13.135 1.00 29.22  ? 52  TYR B CB  1 
ATOM   1385 C  CG  . TYR B 1 52  ? -23.818 12.449  12.325 1.00 29.93  ? 52  TYR B CG  1 
ATOM   1386 C  CD1 . TYR B 1 52  ? -23.646 11.122  12.668 1.00 29.56  ? 52  TYR B CD1 1 
ATOM   1387 C  CD2 . TYR B 1 52  ? -24.498 12.713  11.151 1.00 31.32  ? 52  TYR B CD2 1 
ATOM   1388 C  CE1 . TYR B 1 52  ? -24.161 10.096  11.898 1.00 29.92  ? 52  TYR B CE1 1 
ATOM   1389 C  CE2 . TYR B 1 52  ? -25.035 11.694  10.367 1.00 27.81  ? 52  TYR B CE2 1 
ATOM   1390 C  CZ  . TYR B 1 52  ? -24.867 10.386  10.746 1.00 30.79  ? 52  TYR B CZ  1 
ATOM   1391 O  OH  . TYR B 1 52  ? -25.351 9.381   9.959  1.00 32.64  ? 52  TYR B OH  1 
ATOM   1392 N  N   . LYS B 1 53  ? -26.154 13.946  14.488 1.00 33.91  ? 53  LYS B N   1 
ATOM   1393 C  CA  . LYS B 1 53  ? -27.142 13.590  15.489 1.00 38.15  ? 53  LYS B CA  1 
ATOM   1394 C  C   . LYS B 1 53  ? -27.019 12.111  15.840 1.00 35.38  ? 53  LYS B C   1 
ATOM   1395 O  O   . LYS B 1 53  ? -27.392 11.726  16.945 1.00 37.58  ? 53  LYS B O   1 
ATOM   1396 C  CB  . LYS B 1 53  ? -28.567 13.994  15.066 1.00 41.98  ? 53  LYS B CB  1 
ATOM   1397 C  CG  . LYS B 1 53  ? -28.852 15.494  15.190 1.00 47.17  ? 53  LYS B CG  1 
ATOM   1398 C  CD  . LYS B 1 53  ? -28.468 16.010  16.574 1.00 57.81  ? 53  LYS B CD  1 
ATOM   1399 C  CE  . LYS B 1 53  ? -29.199 17.201  17.081 1.00 64.87  ? 53  LYS B CE  1 
ATOM   1400 N  NZ  . LYS B 1 53  ? -28.824 18.409  16.350 1.00 62.05  ? 53  LYS B NZ  1 
ATOM   1401 N  N   . HIS B 1 54  ? -26.503 11.273  14.934 1.00 29.29  ? 54  HIS B N   1 
ATOM   1402 C  CA  . HIS B 1 54  ? -26.278 9.879   15.283 1.00 29.30  ? 54  HIS B CA  1 
ATOM   1403 C  C   . HIS B 1 54  ? -24.815 9.594   15.685 1.00 30.24  ? 54  HIS B C   1 
ATOM   1404 O  O   . HIS B 1 54  ? -24.361 8.440   15.724 1.00 27.74  ? 54  HIS B O   1 
ATOM   1405 C  CB  . HIS B 1 54  ? -26.791 8.994   14.167 1.00 29.04  ? 54  HIS B CB  1 
ATOM   1406 C  CG  . HIS B 1 54  ? -28.239 8.697   14.335 1.00 37.61  ? 54  HIS B CG  1 
ATOM   1407 N  ND1 . HIS B 1 54  ? -29.236 9.546   13.936 1.00 34.96  ? 54  HIS B ND1 1 
ATOM   1408 C  CD2 . HIS B 1 54  ? -28.843 7.605   14.887 1.00 42.40  ? 54  HIS B CD2 1 
ATOM   1409 C  CE1 . HIS B 1 54  ? -30.396 8.972   14.208 1.00 39.49  ? 54  HIS B CE1 1 
ATOM   1410 N  NE2 . HIS B 1 54  ? -30.181 7.787   14.777 1.00 41.45  ? 54  HIS B NE2 1 
ATOM   1411 N  N   . TRP B 1 55  ? -24.093 10.645  16.038 1.00 24.31  ? 55  TRP B N   1 
ATOM   1412 C  CA  . TRP B 1 55  ? -22.695 10.469  16.427 1.00 27.26  ? 55  TRP B CA  1 
ATOM   1413 C  C   . TRP B 1 55  ? -22.549 9.464   17.575 1.00 31.73  ? 55  TRP B C   1 
ATOM   1414 O  O   . TRP B 1 55  ? -21.647 8.644   17.544 1.00 29.52  ? 55  TRP B O   1 
ATOM   1415 C  CB  . TRP B 1 55  ? -22.061 11.825  16.762 1.00 27.67  ? 55  TRP B CB  1 
ATOM   1416 C  CG  . TRP B 1 55  ? -20.641 11.639  17.220 1.00 30.07  ? 55  TRP B CG  1 
ATOM   1417 C  CD1 . TRP B 1 55  ? -20.121 11.780  18.476 1.00 31.45  ? 55  TRP B CD1 1 
ATOM   1418 C  CD2 . TRP B 1 55  ? -19.563 11.175  16.383 1.00 29.49  ? 55  TRP B CD2 1 
ATOM   1419 N  NE1 . TRP B 1 55  ? -18.788 11.438  18.485 1.00 31.20  ? 55  TRP B NE1 1 
ATOM   1420 C  CE2 . TRP B 1 55  ? -18.422 11.064  17.212 1.00 32.31  ? 55  TRP B CE2 1 
ATOM   1421 C  CE3 . TRP B 1 55  ? -19.460 10.854  15.023 1.00 30.00  ? 55  TRP B CE3 1 
ATOM   1422 C  CZ2 . TRP B 1 55  ? -17.183 10.659  16.702 1.00 31.84  ? 55  TRP B CZ2 1 
ATOM   1423 C  CZ3 . TRP B 1 55  ? -18.242 10.457  14.523 1.00 29.90  ? 55  TRP B CZ3 1 
ATOM   1424 C  CH2 . TRP B 1 55  ? -17.122 10.345  15.361 1.00 32.04  ? 55  TRP B CH2 1 
ATOM   1425 N  N   . PRO B 1 56  ? -23.390 9.456   18.642 1.00 34.17  ? 56  PRO B N   1 
ATOM   1426 C  CA  . PRO B 1 56  ? -23.254 8.449   19.693 1.00 30.81  ? 56  PRO B CA  1 
ATOM   1427 C  C   . PRO B 1 56  ? -23.234 7.005   19.232 1.00 29.29  ? 56  PRO B C   1 
ATOM   1428 O  O   . PRO B 1 56  ? -22.511 6.192   19.810 1.00 29.27  ? 56  PRO B O   1 
ATOM   1429 C  CB  . PRO B 1 56  ? -24.441 8.750   20.624 1.00 33.51  ? 56  PRO B CB  1 
ATOM   1430 C  CG  . PRO B 1 56  ? -24.565 10.269  20.503 1.00 36.47  ? 56  PRO B CG  1 
ATOM   1431 C  CD  . PRO B 1 56  ? -24.346 10.508  19.007 1.00 33.71  ? 56  PRO B CD  1 
ATOM   1432 N  N   . GLN B 1 57  ? -23.992 6.676   18.183 1.00 29.25  ? 57  GLN B N   1 
ATOM   1433 C  CA  . GLN B 1 57  ? -24.039 5.284   17.719 1.00 26.63  ? 57  GLN B CA  1 
ATOM   1434 C  C   . GLN B 1 57  ? -22.802 4.935   16.885 1.00 27.43  ? 57  GLN B C   1 
ATOM   1435 O  O   . GLN B 1 57  ? -22.546 3.757   16.638 1.00 29.16  ? 57  GLN B O   1 
ATOM   1436 C  CB  . GLN B 1 57  ? -25.322 4.984   16.936 1.00 30.83  ? 57  GLN B CB  1 
ATOM   1437 C  CG  . GLN B 1 57  ? -26.610 4.982   17.780 1.00 32.48  ? 57  GLN B CG  1 
ATOM   1438 C  CD  . GLN B 1 57  ? -26.948 6.347   18.343 1.00 34.43  ? 57  GLN B CD  1 
ATOM   1439 O  OE1 . GLN B 1 57  ? -26.896 7.369   17.632 1.00 32.28  ? 57  GLN B OE1 1 
ATOM   1440 N  NE2 . GLN B 1 57  ? -27.269 6.380   19.638 1.00 39.23  ? 57  GLN B NE2 1 
ATOM   1441 N  N   . ILE B 1 58  ? -22.051 5.965   16.441 1.00 25.63  ? 58  ILE B N   1 
ATOM   1442 C  CA  . ILE B 1 58  ? -20.767 5.709   15.810 1.00 28.47  ? 58  ILE B CA  1 
ATOM   1443 C  C   . ILE B 1 58  ? -19.680 5.614   16.886 1.00 27.69  ? 58  ILE B C   1 
ATOM   1444 O  O   . ILE B 1 58  ? -18.910 4.663   16.894 1.00 27.46  ? 58  ILE B O   1 
ATOM   1445 C  CB  . ILE B 1 58  ? -20.439 6.773   14.752 1.00 28.19  ? 58  ILE B CB  1 
ATOM   1446 C  CG1 . ILE B 1 58  ? -21.423 6.683   13.590 1.00 29.02  ? 58  ILE B CG1 1 
ATOM   1447 C  CG2 . ILE B 1 58  ? -18.987 6.632   14.279 1.00 27.46  ? 58  ILE B CG2 1 
ATOM   1448 C  CD1 . ILE B 1 58  ? -21.414 7.886   12.686 1.00 31.87  ? 58  ILE B CD1 1 
ATOM   1449 N  N   . ALA B 1 59  ? -19.635 6.623   17.766 1.00 25.59  ? 59  ALA B N   1 
ATOM   1450 C  CA  . ALA B 1 59  ? -18.635 6.738   18.807 1.00 25.36  ? 59  ALA B CA  1 
ATOM   1451 C  C   . ALA B 1 59  ? -18.610 5.530   19.760 1.00 25.55  ? 59  ALA B C   1 
ATOM   1452 O  O   . ALA B 1 59  ? -17.611 5.284   20.390 1.00 28.51  ? 59  ALA B O   1 
ATOM   1453 C  CB  . ALA B 1 59  ? -18.827 8.043   19.552 1.00 23.74  ? 59  ALA B CB  1 
ATOM   1454 N  N   . GLN B 1 60  ? -19.669 4.753   19.862 1.00 28.81  ? 60  GLN B N   1 
ATOM   1455 C  CA  . GLN B 1 60  ? -19.650 3.580   20.725 1.00 31.73  ? 60  GLN B CA  1 
ATOM   1456 C  C   . GLN B 1 60  ? -18.633 2.547   20.237 1.00 32.05  ? 60  GLN B C   1 
ATOM   1457 O  O   . GLN B 1 60  ? -18.314 1.588   20.954 1.00 30.36  ? 60  GLN B O   1 
ATOM   1458 C  CB  . GLN B 1 60  ? -21.047 2.962   20.801 1.00 38.26  ? 60  GLN B CB  1 
ATOM   1459 C  CG  . GLN B 1 60  ? -21.452 2.183   19.552 1.00 43.42  ? 60  GLN B CG  1 
ATOM   1460 C  CD  . GLN B 1 60  ? -22.879 1.656   19.609 1.00 46.31  ? 60  GLN B CD  1 
ATOM   1461 O  OE1 . GLN B 1 60  ? -23.196 0.823   20.462 1.00 37.14  ? 60  GLN B OE1 1 
ATOM   1462 N  NE2 . GLN B 1 60  ? -23.726 2.089   18.674 1.00 39.22  ? 60  GLN B NE2 1 
ATOM   1463 N  N   . PHE B 1 61  ? -18.142 2.707   19.005 1.00 29.96  ? 61  PHE B N   1 
ATOM   1464 C  CA  . PHE B 1 61  ? -17.152 1.761   18.477 1.00 31.09  ? 61  PHE B CA  1 
ATOM   1465 C  C   . PHE B 1 61  ? -15.725 2.319   18.569 1.00 30.21  ? 61  PHE B C   1 
ATOM   1466 O  O   . PHE B 1 61  ? -14.782 1.559   18.379 1.00 28.89  ? 61  PHE B O   1 
ATOM   1467 C  CB  . PHE B 1 61  ? -17.475 1.334   17.044 1.00 31.51  ? 61  PHE B CB  1 
ATOM   1468 C  CG  . PHE B 1 61  ? -18.811 0.611   16.925 1.00 27.97  ? 61  PHE B CG  1 
ATOM   1469 C  CD1 . PHE B 1 61  ? -18.953 -0.683  17.420 1.00 33.44  ? 61  PHE B CD1 1 
ATOM   1470 C  CD2 . PHE B 1 61  ? -19.911 1.221   16.341 1.00 30.70  ? 61  PHE B CD2 1 
ATOM   1471 C  CE1 . PHE B 1 61  ? -20.183 -1.326  17.388 1.00 36.37  ? 61  PHE B CE1 1 
ATOM   1472 C  CE2 . PHE B 1 61  ? -21.141 0.570   16.289 1.00 29.14  ? 61  PHE B CE2 1 
ATOM   1473 C  CZ  . PHE B 1 61  ? -21.273 -0.703  16.813 1.00 33.24  ? 61  PHE B CZ  1 
ATOM   1474 N  N   . ALA B 1 62  ? -15.566 3.603   18.928 1.00 26.17  ? 62  ALA B N   1 
ATOM   1475 C  CA  . ALA B 1 62  ? -14.252 4.219   19.038 1.00 30.17  ? 62  ALA B CA  1 
ATOM   1476 C  C   . ALA B 1 62  ? -13.548 3.723   20.306 1.00 29.83  ? 62  ALA B C   1 
ATOM   1477 O  O   . ALA B 1 62  ? -14.152 3.692   21.380 1.00 28.74  ? 62  ALA B O   1 
ATOM   1478 C  CB  . ALA B 1 62  ? -14.347 5.758   19.033 1.00 27.34  ? 62  ALA B CB  1 
ATOM   1479 N  N   . PRO B 1 63  ? -12.236 3.394   20.228 1.00 30.31  ? 63  PRO B N   1 
ATOM   1480 C  CA  . PRO B 1 63  ? -11.524 2.831   21.379 1.00 26.68  ? 63  PRO B CA  1 
ATOM   1481 C  C   . PRO B 1 63  ? -11.083 3.890   22.374 1.00 26.52  ? 63  PRO B C   1 
ATOM   1482 O  O   . PRO B 1 63  ? -10.723 5.005   22.001 1.00 26.54  ? 63  PRO B O   1 
ATOM   1483 C  CB  . PRO B 1 63  ? -10.350 2.119   20.736 1.00 29.54  ? 63  PRO B CB  1 
ATOM   1484 C  CG  . PRO B 1 63  ? -10.043 3.023   19.557 1.00 31.26  ? 63  PRO B CG  1 
ATOM   1485 C  CD  . PRO B 1 63  ? -11.401 3.491   19.031 1.00 30.71  ? 63  PRO B CD  1 
ATOM   1486 N  N   . SER B 1 64  ? -11.117 3.524   23.650 1.00 26.24  ? 64  SER B N   1 
ATOM   1487 C  CA  . SER B 1 64  ? -10.381 4.268   24.674 1.00 25.83  ? 64  SER B CA  1 
ATOM   1488 C  C   . SER B 1 64  ? -8.900  4.290   24.305 1.00 24.08  ? 64  SER B C   1 
ATOM   1489 O  O   . SER B 1 64  ? -8.415  3.448   23.551 1.00 24.92  ? 64  SER B O   1 
ATOM   1490 C  CB  . SER B 1 64  ? -10.589 3.624   26.043 1.00 27.19  ? 64  SER B CB  1 
ATOM   1491 O  OG  . SER B 1 64  ? -10.098 2.285   26.019 1.00 24.22  ? 64  SER B OG  1 
ATOM   1492 N  N   . ALA B 1 65  ? -8.148  5.210   24.897 1.00 23.92  ? 65  ALA B N   1 
ATOM   1493 C  CA  . ALA B 1 65  ? -6.696  5.170   24.760 1.00 25.11  ? 65  ALA B CA  1 
ATOM   1494 C  C   . ALA B 1 65  ? -6.124  3.822   25.192 1.00 24.91  ? 65  ALA B C   1 
ATOM   1495 O  O   . ALA B 1 65  ? -5.263  3.265   24.527 1.00 24.37  ? 65  ALA B O   1 
ATOM   1496 C  CB  . ALA B 1 65  ? -6.094  6.304   25.489 1.00 27.93  ? 65  ALA B CB  1 
ATOM   1497 N  N   . SER B 1 66  ? -6.631  3.249   26.291 1.00 25.05  ? 66  SER B N   1 
ATOM   1498 C  CA  . SER B 1 66  ? -6.093  1.994   26.787 1.00 25.58  ? 66  SER B CA  1 
ATOM   1499 C  C   . SER B 1 66  ? -6.326  0.880   25.762 1.00 22.73  ? 66  SER B C   1 
ATOM   1500 O  O   . SER B 1 66  ? -5.437  0.112   25.426 1.00 24.05  ? 66  SER B O   1 
ATOM   1501 C  CB  . SER B 1 66  ? -6.673  1.696   28.163 1.00 27.85  ? 66  SER B CB  1 
ATOM   1502 O  OG  . SER B 1 66  ? -6.212  0.439   28.657 1.00 29.84  ? 66  SER B OG  1 
ATOM   1503 N  N   . ALA B 1 67  ? -7.539  0.832   25.214 1.00 25.08  ? 67  ALA B N   1 
ATOM   1504 C  CA  . ALA B 1 67  ? -7.927  -0.183  24.243 1.00 26.08  ? 67  ALA B CA  1 
ATOM   1505 C  C   . ALA B 1 67  ? -7.238  0.026   22.896 1.00 24.84  ? 67  ALA B C   1 
ATOM   1506 O  O   . ALA B 1 67  ? -6.911  -0.934  22.184 1.00 23.96  ? 67  ALA B O   1 
ATOM   1507 C  CB  . ALA B 1 67  ? -9.446  -0.159  24.103 1.00 24.41  ? 67  ALA B CB  1 
ATOM   1508 N  N   . PHE B 1 68  ? -7.017  1.285   22.528 1.00 23.21  ? 68  PHE B N   1 
ATOM   1509 C  CA  . PHE B 1 68  ? -6.300  1.552   21.295 1.00 22.84  ? 68  PHE B CA  1 
ATOM   1510 C  C   . PHE B 1 68  ? -4.894  0.931   21.338 1.00 24.93  ? 68  PHE B C   1 
ATOM   1511 O  O   . PHE B 1 68  ? -4.457  0.261   20.395 1.00 25.70  ? 68  PHE B O   1 
ATOM   1512 C  CB  . PHE B 1 68  ? -6.226  3.060   21.071 1.00 24.96  ? 68  PHE B CB  1 
ATOM   1513 C  CG  . PHE B 1 68  ? -5.411  3.425   19.833 1.00 27.21  ? 68  PHE B CG  1 
ATOM   1514 C  CD1 . PHE B 1 68  ? -5.959  3.344   18.540 1.00 27.77  ? 68  PHE B CD1 1 
ATOM   1515 C  CD2 . PHE B 1 68  ? -4.085  3.831   19.965 1.00 27.52  ? 68  PHE B CD2 1 
ATOM   1516 C  CE1 . PHE B 1 68  ? -5.201  3.685   17.397 1.00 28.90  ? 68  PHE B CE1 1 
ATOM   1517 C  CE2 . PHE B 1 68  ? -3.329  4.190   18.829 1.00 28.76  ? 68  PHE B CE2 1 
ATOM   1518 C  CZ  . PHE B 1 68  ? -3.894  4.123   17.552 1.00 27.96  ? 68  PHE B CZ  1 
ATOM   1519 N  N   . PHE B 1 69  ? -4.179  1.149   22.451 1.00 24.07  ? 69  PHE B N   1 
ATOM   1520 C  CA  . PHE B 1 69  ? -2.840  0.600   22.632 1.00 24.83  ? 69  PHE B CA  1 
ATOM   1521 C  C   . PHE B 1 69  ? -2.876  -0.874  23.044 1.00 25.15  ? 69  PHE B C   1 
ATOM   1522 O  O   . PHE B 1 69  ? -1.874  -1.557  22.837 1.00 25.20  ? 69  PHE B O   1 
ATOM   1523 C  CB  . PHE B 1 69  ? -1.986  1.446   23.579 1.00 21.32  ? 69  PHE B CB  1 
ATOM   1524 C  CG  . PHE B 1 69  ? -1.382  2.636   22.852 1.00 22.72  ? 69  PHE B CG  1 
ATOM   1525 C  CD1 . PHE B 1 69  ? -1.933  3.904   22.962 1.00 21.93  ? 69  PHE B CD1 1 
ATOM   1526 C  CD2 . PHE B 1 69  ? -0.304  2.437   21.986 1.00 22.91  ? 69  PHE B CD2 1 
ATOM   1527 C  CE1 . PHE B 1 69  ? -1.421  4.955   22.225 1.00 24.69  ? 69  PHE B CE1 1 
ATOM   1528 C  CE2 . PHE B 1 69  ? 0.217   3.497   21.270 1.00 27.71  ? 69  PHE B CE2 1 
ATOM   1529 C  CZ  . PHE B 1 69  ? -0.325  4.751   21.420 1.00 25.67  ? 69  PHE B CZ  1 
ATOM   1530 N  N   . GLY B 1 70  ? -4.023  -1.365  23.524 1.00 23.11  ? 70  GLY B N   1 
ATOM   1531 C  CA  . GLY B 1 70  ? -4.124  -2.749  23.980 1.00 26.84  ? 70  GLY B CA  1 
ATOM   1532 C  C   . GLY B 1 70  ? -4.544  -3.724  22.891 1.00 27.81  ? 70  GLY B C   1 
ATOM   1533 O  O   . GLY B 1 70  ? -4.094  -4.860  22.877 1.00 25.56  ? 70  GLY B O   1 
ATOM   1534 N  N   . MET B 1 71  ? -5.431  -3.274  21.989 1.00 28.90  ? 71  MET B N   1 
ATOM   1535 C  CA  . MET B 1 71  ? -5.975  -4.111  20.941 1.00 28.47  ? 71  MET B CA  1 
ATOM   1536 C  C   . MET B 1 71  ? -5.160  -4.039  19.647 1.00 27.84  ? 71  MET B C   1 
ATOM   1537 O  O   . MET B 1 71  ? -5.139  -5.004  18.881 1.00 25.74  ? 71  MET B O   1 
ATOM   1538 C  CB  . MET B 1 71  ? -7.403  -3.669  20.586 1.00 26.36  ? 71  MET B CB  1 
ATOM   1539 C  CG  . MET B 1 71  ? -8.395  -3.798  21.733 1.00 30.96  ? 71  MET B CG  1 
ATOM   1540 S  SD  . MET B 1 71  ? -10.080 -3.315  21.276 1.00 33.77  ? 71  MET B SD  1 
ATOM   1541 C  CE  . MET B 1 71  ? -9.885  -1.812  20.298 1.00 32.14  ? 71  MET B CE  1 
ATOM   1542 N  N   . SER B 1 72  ? -4.634  -2.867  19.315 1.00 26.31  ? 72  SER B N   1 
ATOM   1543 C  CA  . SER B 1 72  ? -4.084  -2.660  17.981 1.00 31.14  ? 72  SER B CA  1 
ATOM   1544 C  C   . SER B 1 72  ? -2.686  -3.282  17.776 1.00 31.81  ? 72  SER B C   1 
ATOM   1545 O  O   . SER B 1 72  ? -1.927  -3.505  18.727 1.00 31.44  ? 72  SER B O   1 
ATOM   1546 C  CB  . SER B 1 72  ? -3.954  -1.165  17.688 1.00 28.82  ? 72  SER B CB  1 
ATOM   1547 O  OG  . SER B 1 72  ? -5.141  -0.447  17.974 1.00 28.57  ? 72  SER B OG  1 
ATOM   1548 N  N   . ARG B 1 73  ? -2.321  -3.456  16.499 1.00 28.58  ? 73  ARG B N   1 
ATOM   1549 C  CA  . ARG B 1 73  ? -0.947  -3.697  16.088 1.00 30.40  ? 73  ARG B CA  1 
ATOM   1550 C  C   . ARG B 1 73  ? -0.255  -2.370  15.805 1.00 29.93  ? 73  ARG B C   1 
ATOM   1551 O  O   . ARG B 1 73  ? -0.649  -1.646  14.892 1.00 29.40  ? 73  ARG B O   1 
ATOM   1552 C  CB  . ARG B 1 73  ? -0.937  -4.656  14.904 1.00 32.57  ? 73  ARG B CB  1 
ATOM   1553 C  CG  . ARG B 1 73  ? -1.598  -5.957  15.349 1.00 34.58  ? 73  ARG B CG  1 
ATOM   1554 C  CD  . ARG B 1 73  ? -1.284  -7.130  14.432 1.00 36.57  ? 73  ARG B CD  1 
ATOM   1555 N  NE  . ARG B 1 73  ? 0.145   -7.443  14.518 1.00 35.26  ? 73  ARG B NE  1 
ATOM   1556 C  CZ  . ARG B 1 73  ? 0.734   -8.101  15.512 1.00 32.27  ? 73  ARG B CZ  1 
ATOM   1557 N  NH1 . ARG B 1 73  ? 2.012   -8.290  15.465 1.00 35.69  ? 73  ARG B NH1 1 
ATOM   1558 N  NH2 . ARG B 1 73  ? 0.080   -8.570  16.549 1.00 37.32  ? 73  ARG B NH2 1 
ATOM   1559 N  N   . ILE B 1 74  ? 0.780   -2.065  16.605 1.00 29.62  ? 74  ILE B N   1 
ATOM   1560 C  CA  . ILE B 1 74  ? 1.417   -0.760  16.607 1.00 25.32  ? 74  ILE B CA  1 
ATOM   1561 C  C   . ILE B 1 74  ? 2.785   -0.915  15.975 1.00 28.12  ? 74  ILE B C   1 
ATOM   1562 O  O   . ILE B 1 74  ? 3.486   -1.854  16.303 1.00 29.24  ? 74  ILE B O   1 
ATOM   1563 C  CB  . ILE B 1 74  ? 1.538   -0.213  18.041 1.00 29.58  ? 74  ILE B CB  1 
ATOM   1564 C  CG1 . ILE B 1 74  ? 0.153   -0.059  18.728 1.00 32.85  ? 74  ILE B CG1 1 
ATOM   1565 C  CG2 . ILE B 1 74  ? 2.286   1.115   18.055 1.00 28.39  ? 74  ILE B CG2 1 
ATOM   1566 C  CD1 . ILE B 1 74  ? -0.724  1.004   18.087 1.00 34.55  ? 74  ILE B CD1 1 
ATOM   1567 N  N   . GLY B 1 75  ? 3.163   0.039   15.123 1.00 28.85  ? 75  GLY B N   1 
ATOM   1568 C  CA  . GLY B 1 75  ? 4.471   0.053   14.501 1.00 28.97  ? 75  GLY B CA  1 
ATOM   1569 C  C   . GLY B 1 75  ? 4.969   1.483   14.434 1.00 29.83  ? 75  GLY B C   1 
ATOM   1570 O  O   . GLY B 1 75  ? 4.269   2.406   14.826 1.00 28.24  ? 75  GLY B O   1 
ATOM   1571 N  N   . MET B 1 76  ? 6.229   1.616   14.041 1.00 32.92  ? 76  MET B N   1 
ATOM   1572 C  CA  A MET B 1 76  ? 6.846   2.912   13.842 0.60 34.73  ? 76  MET B CA  1 
ATOM   1573 C  CA  B MET B 1 76  ? 6.901   2.888   13.876 0.40 33.43  ? 76  MET B CA  1 
ATOM   1574 C  C   . MET B 1 76  ? 7.556   2.872   12.493 1.00 35.90  ? 76  MET B C   1 
ATOM   1575 O  O   . MET B 1 76  ? 8.158   1.873   12.116 1.00 33.49  ? 76  MET B O   1 
ATOM   1576 C  CB  A MET B 1 76  ? 7.817   3.285   14.968 0.60 37.29  ? 76  MET B CB  1 
ATOM   1577 C  CB  B MET B 1 76  ? 7.924   3.052   15.005 0.40 34.18  ? 76  MET B CB  1 
ATOM   1578 C  CG  A MET B 1 76  ? 7.367   4.478   15.807 0.60 40.29  ? 76  MET B CG  1 
ATOM   1579 C  CG  B MET B 1 76  ? 8.863   4.222   14.865 0.40 33.89  ? 76  MET B CG  1 
ATOM   1580 S  SD  A MET B 1 76  ? 8.588   5.099   16.994 0.60 49.29  ? 76  MET B SD  1 
ATOM   1581 S  SD  B MET B 1 76  ? 10.225  4.106   16.041 0.40 36.35  ? 76  MET B SD  1 
ATOM   1582 C  CE  A MET B 1 76  ? 9.985   5.681   16.025 0.60 47.48  ? 76  MET B CE  1 
ATOM   1583 C  CE  B MET B 1 76  ? 11.267  5.459   15.463 0.40 29.13  ? 76  MET B CE  1 
ATOM   1584 N  N   . GLU B 1 77  ? 7.405   3.952   11.740 1.00 34.82  ? 77  GLU B N   1 
ATOM   1585 C  CA  . GLU B 1 77  ? 8.059   4.080   10.456 1.00 36.11  ? 77  GLU B CA  1 
ATOM   1586 C  C   . GLU B 1 77  ? 8.690   5.455   10.370 1.00 34.48  ? 77  GLU B C   1 
ATOM   1587 O  O   . GLU B 1 77  ? 8.036   6.453   10.649 1.00 31.26  ? 77  GLU B O   1 
ATOM   1588 C  CB  . GLU B 1 77  ? 7.069   3.915   9.316  1.00 42.51  ? 77  GLU B CB  1 
ATOM   1589 C  CG  . GLU B 1 77  ? 6.826   2.455   8.951  1.00 55.68  ? 77  GLU B CG  1 
ATOM   1590 C  CD  . GLU B 1 77  ? 5.710   2.366   7.928  1.00 67.55  ? 77  GLU B CD  1 
ATOM   1591 O  OE1 . GLU B 1 77  ? 5.192   1.238   7.722  1.00 83.64  ? 77  GLU B OE1 1 
ATOM   1592 O  OE2 . GLU B 1 77  ? 5.352   3.430   7.355  1.00 66.07  ? 77  GLU B OE2 1 
ATOM   1593 N  N   . VAL B 1 78  ? 9.964   5.483   9.960  1.00 33.08  ? 78  VAL B N   1 
ATOM   1594 C  CA  . VAL B 1 78  ? 10.653  6.750   9.749  1.00 32.93  ? 78  VAL B CA  1 
ATOM   1595 C  C   . VAL B 1 78  ? 10.821  6.989   8.250  1.00 31.14  ? 78  VAL B C   1 
ATOM   1596 O  O   . VAL B 1 78  ? 11.269  6.112   7.551  1.00 30.41  ? 78  VAL B O   1 
ATOM   1597 C  CB  . VAL B 1 78  ? 12.001  6.679   10.484 1.00 32.89  ? 78  VAL B CB  1 
ATOM   1598 C  CG1 . VAL B 1 78  ? 12.721  8.008   10.407 1.00 35.19  ? 78  VAL B CG1 1 
ATOM   1599 C  CG2 . VAL B 1 78  ? 11.830  6.264   11.941 1.00 35.70  ? 78  VAL B CG2 1 
ATOM   1600 N  N   . THR B 1 79  ? 10.489  8.179   7.760  1.00 31.46  ? 79  THR B N   1 
ATOM   1601 C  CA  . THR B 1 79  ? 10.428  8.418   6.325  1.00 29.69  ? 79  THR B CA  1 
ATOM   1602 C  C   . THR B 1 79  ? 10.811  9.867   6.105  1.00 25.95  ? 79  THR B C   1 
ATOM   1603 O  O   . THR B 1 79  ? 10.886  10.647  7.058  1.00 25.59  ? 79  THR B O   1 
ATOM   1604 C  CB  . THR B 1 79  ? 9.004   8.174   5.772  1.00 32.35  ? 79  THR B CB  1 
ATOM   1605 O  OG1 . THR B 1 79  ? 8.217   9.318   6.083  1.00 32.51  ? 79  THR B OG1 1 
ATOM   1606 C  CG2 . THR B 1 79  ? 8.297   6.976   6.356  1.00 35.63  ? 79  THR B CG2 1 
ATOM   1607 N  N   . PRO B 1 80  ? 10.938  10.315  4.839  1.00 26.80  ? 80  PRO B N   1 
ATOM   1608 C  CA  . PRO B 1 80  ? 11.218  11.714  4.569  1.00 24.42  ? 80  PRO B CA  1 
ATOM   1609 C  C   . PRO B 1 80  ? 10.228  12.686  5.158  1.00 28.64  ? 80  PRO B C   1 
ATOM   1610 O  O   . PRO B 1 80  ? 10.568  13.871  5.342  1.00 30.07  ? 80  PRO B O   1 
ATOM   1611 C  CB  . PRO B 1 80  ? 11.275  11.781  3.043  1.00 27.32  ? 80  PRO B CB  1 
ATOM   1612 C  CG  . PRO B 1 80  ? 11.649  10.371  2.622  1.00 26.63  ? 80  PRO B CG  1 
ATOM   1613 C  CD  . PRO B 1 80  ? 10.999  9.465   3.642  1.00 26.19  ? 80  PRO B CD  1 
ATOM   1614 N  N   . SER B 1 81  ? 8.983   12.218  5.420  1.00 27.80  ? 81  SER B N   1 
ATOM   1615 C  CA  . SER B 1 81  ? 7.990   13.108  6.012  1.00 29.61  ? 81  SER B CA  1 
ATOM   1616 C  C   . SER B 1 81  ? 8.099   13.204  7.534  1.00 29.16  ? 81  SER B C   1 
ATOM   1617 O  O   . SER B 1 81  ? 7.601   14.171  8.117  1.00 29.88  ? 81  SER B O   1 
ATOM   1618 C  CB  . SER B 1 81  ? 6.575   12.717  5.618  1.00 31.35  ? 81  SER B CB  1 
ATOM   1619 O  OG  . SER B 1 81  ? 6.314   11.351  5.900  1.00 31.22  ? 81  SER B OG  1 
ATOM   1620 N  N   . GLY B 1 82  ? 8.706   12.204  8.181  1.00 30.90  ? 82  GLY B N   1 
ATOM   1621 C  CA  . GLY B 1 82  ? 8.908   12.260  9.626  1.00 28.52  ? 82  GLY B CA  1 
ATOM   1622 C  C   . GLY B 1 82  ? 8.821   10.866  10.227 1.00 26.99  ? 82  GLY B C   1 
ATOM   1623 O  O   . GLY B 1 82  ? 9.019   9.851   9.520  1.00 26.72  ? 82  GLY B O   1 
ATOM   1624 N  N   . THR B 1 83  ? 8.474   10.837  11.523 1.00 24.28  ? 83  THR B N   1 
ATOM   1625 C  CA  . THR B 1 83  ? 8.309   9.567   12.224 1.00 25.39  ? 83  THR B CA  1 
ATOM   1626 C  C   . THR B 1 83  ? 6.809   9.353   12.478 1.00 24.33  ? 83  THR B C   1 
ATOM   1627 O  O   . THR B 1 83  ? 6.145   10.268  12.951 1.00 23.08  ? 83  THR B O   1 
ATOM   1628 C  CB  . THR B 1 83  ? 9.146   9.624   13.514 1.00 26.96  ? 83  THR B CB  1 
ATOM   1629 O  OG1 . THR B 1 83  ? 10.511  9.939   13.185 1.00 28.55  ? 83  THR B OG1 1 
ATOM   1630 C  CG2 . THR B 1 83  ? 9.074   8.317   14.287 1.00 22.48  ? 83  THR B CG2 1 
ATOM   1631 N  N   . TRP B 1 84  ? 6.280   8.169   12.133 1.00 23.51  ? 84  TRP B N   1 
ATOM   1632 C  CA  . TRP B 1 84  ? 4.866   7.842   12.175 1.00 25.20  ? 84  TRP B CA  1 
ATOM   1633 C  C   . TRP B 1 84  ? 4.628   6.625   13.053 1.00 25.61  ? 84  TRP B C   1 
ATOM   1634 O  O   . TRP B 1 84  ? 5.369   5.649   12.972 1.00 29.52  ? 84  TRP B O   1 
ATOM   1635 C  CB  . TRP B 1 84  ? 4.341   7.528   10.765 1.00 27.26  ? 84  TRP B CB  1 
ATOM   1636 C  CG  . TRP B 1 84  ? 4.499   8.678   9.805  1.00 28.72  ? 84  TRP B CG  1 
ATOM   1637 C  CD1 . TRP B 1 84  ? 5.629   9.084   9.164  1.00 27.72  ? 84  TRP B CD1 1 
ATOM   1638 C  CD2 . TRP B 1 84  ? 3.450   9.563   9.382  1.00 29.62  ? 84  TRP B CD2 1 
ATOM   1639 N  NE1 . TRP B 1 84  ? 5.366   10.197  8.409  1.00 30.74  ? 84  TRP B NE1 1 
ATOM   1640 C  CE2 . TRP B 1 84  ? 4.036   10.508  8.518  1.00 29.98  ? 84  TRP B CE2 1 
ATOM   1641 C  CE3 . TRP B 1 84  ? 2.086   9.667   9.681  1.00 28.87  ? 84  TRP B CE3 1 
ATOM   1642 C  CZ2 . TRP B 1 84  ? 3.296   11.531  7.930  1.00 31.55  ? 84  TRP B CZ2 1 
ATOM   1643 C  CZ3 . TRP B 1 84  ? 1.358   10.683  9.098  1.00 31.75  ? 84  TRP B CZ3 1 
ATOM   1644 C  CH2 . TRP B 1 84  ? 1.958   11.596  8.222  1.00 30.50  ? 84  TRP B CH2 1 
ATOM   1645 N  N   . LEU B 1 85  ? 3.572   6.696   13.857 1.00 29.51  ? 85  LEU B N   1 
ATOM   1646 C  CA  . LEU B 1 85  ? 3.069   5.543   14.578 1.00 29.87  ? 85  LEU B CA  1 
ATOM   1647 C  C   . LEU B 1 85  ? 1.959   4.927   13.743 1.00 31.10  ? 85  LEU B C   1 
ATOM   1648 O  O   . LEU B 1 85  ? 0.947   5.572   13.471 1.00 31.49  ? 85  LEU B O   1 
ATOM   1649 C  CB  . LEU B 1 85  ? 2.560   6.047   15.923 1.00 29.98  ? 85  LEU B CB  1 
ATOM   1650 C  CG  . LEU B 1 85  ? 2.086   4.975   16.908 1.00 38.77  ? 85  LEU B CG  1 
ATOM   1651 C  CD1 . LEU B 1 85  ? 3.208   4.077   17.317 1.00 45.38  ? 85  LEU B CD1 1 
ATOM   1652 C  CD2 . LEU B 1 85  ? 1.542   5.618   18.161 1.00 47.28  ? 85  LEU B CD2 1 
ATOM   1653 N  N   . THR B 1 86  ? 2.159   3.678   13.332 1.00 28.67  ? 86  THR B N   1 
ATOM   1654 C  CA  . THR B 1 86  ? 1.171   2.984   12.538 1.00 27.80  ? 86  THR B CA  1 
ATOM   1655 C  C   . THR B 1 86  ? 0.302   2.136   13.452 1.00 28.08  ? 86  THR B C   1 
ATOM   1656 O  O   . THR B 1 86  ? 0.770   1.643   14.483 1.00 26.56  ? 86  THR B O   1 
ATOM   1657 C  CB  . THR B 1 86  ? 1.871   2.124   11.475 1.00 31.79  ? 86  THR B CB  1 
ATOM   1658 O  OG1 . THR B 1 86  ? 2.588   1.115   12.175 1.00 29.08  ? 86  THR B OG1 1 
ATOM   1659 C  CG2 . THR B 1 86  ? 2.815   2.938   10.608 1.00 30.53  ? 86  THR B CG2 1 
ATOM   1660 N  N   . TYR B 1 87  ? -0.966  1.926   13.040 1.00 26.98  ? 87  TYR B N   1 
ATOM   1661 C  CA  . TYR B 1 87  ? -1.889  1.098   13.796 1.00 27.80  ? 87  TYR B CA  1 
ATOM   1662 C  C   . TYR B 1 87  ? -2.798  0.340   12.849 1.00 26.95  ? 87  TYR B C   1 
ATOM   1663 O  O   . TYR B 1 87  ? -3.180  0.872   11.837 1.00 29.99  ? 87  TYR B O   1 
ATOM   1664 C  CB  . TYR B 1 87  ? -2.698  1.941   14.788 1.00 26.61  ? 87  TYR B CB  1 
ATOM   1665 C  CG  . TYR B 1 87  ? -3.540  3.030   14.169 1.00 25.20  ? 87  TYR B CG  1 
ATOM   1666 C  CD1 . TYR B 1 87  ? -3.009  4.292   13.952 1.00 26.77  ? 87  TYR B CD1 1 
ATOM   1667 C  CD2 . TYR B 1 87  ? -4.877  2.793   13.843 1.00 27.07  ? 87  TYR B CD2 1 
ATOM   1668 C  CE1 . TYR B 1 87  ? -3.795  5.292   13.411 1.00 27.29  ? 87  TYR B CE1 1 
ATOM   1669 C  CE2 . TYR B 1 87  ? -5.665  3.782   13.290 1.00 24.64  ? 87  TYR B CE2 1 
ATOM   1670 C  CZ  . TYR B 1 87  ? -5.122  5.031   13.084 1.00 26.85  ? 87  TYR B CZ  1 
ATOM   1671 O  OH  . TYR B 1 87  ? -5.919  5.995   12.564 1.00 24.17  ? 87  TYR B OH  1 
ATOM   1672 N  N   . THR B 1 88  ? -3.118  -0.900  13.207 1.00 27.79  ? 88  THR B N   1 
ATOM   1673 C  CA  . THR B 1 88  ? -4.167  -1.657  12.564 1.00 30.05  ? 88  THR B CA  1 
ATOM   1674 C  C   . THR B 1 88  ? -4.897  -2.433  13.642 1.00 31.07  ? 88  THR B C   1 
ATOM   1675 O  O   . THR B 1 88  ? -4.309  -2.772  14.663 1.00 29.17  ? 88  THR B O   1 
ATOM   1676 C  CB  . THR B 1 88  ? -3.641  -2.616  11.488 1.00 29.90  ? 88  THR B CB  1 
ATOM   1677 O  OG1 . THR B 1 88  ? -2.955  -3.644  12.203 1.00 32.86  ? 88  THR B OG1 1 
ATOM   1678 C  CG2 . THR B 1 88  ? -2.766  -1.894  10.484 1.00 30.60  ? 88  THR B CG2 1 
ATOM   1679 N  N   . GLY B 1 89  ? -6.174  -2.718  13.406 1.00 32.01  ? 89  GLY B N   1 
ATOM   1680 C  CA  . GLY B 1 89  ? -6.884  -3.637  14.276 1.00 30.44  ? 89  GLY B CA  1 
ATOM   1681 C  C   . GLY B 1 89  ? -8.323  -3.807  13.827 1.00 31.74  ? 89  GLY B C   1 
ATOM   1682 O  O   . GLY B 1 89  ? -8.742  -3.250  12.811 1.00 32.43  ? 89  GLY B O   1 
ATOM   1683 N  N   . ALA B 1 90  ? -9.101  -4.467  14.682 1.00 32.39  ? 90  ALA B N   1 
ATOM   1684 C  CA  . ALA B 1 90  ? -10.477 -4.778  14.361 1.00 33.41  ? 90  ALA B CA  1 
ATOM   1685 C  C   . ALA B 1 90  ? -11.279 -4.835  15.654 1.00 33.16  ? 90  ALA B C   1 
ATOM   1686 O  O   . ALA B 1 90  ? -10.779 -5.318  16.658 1.00 30.29  ? 90  ALA B O   1 
ATOM   1687 C  CB  . ALA B 1 90  ? -10.523 -6.066  13.580 1.00 35.96  ? 90  ALA B CB  1 
ATOM   1688 N  N   . ILE B 1 91  ? -12.499 -4.293  15.612 1.00 31.94  ? 91  ILE B N   1 
ATOM   1689 C  CA  . ILE B 1 91  ? -13.407 -4.276  16.752 1.00 32.76  ? 91  ILE B CA  1 
ATOM   1690 C  C   . ILE B 1 91  ? -14.630 -5.109  16.391 1.00 31.75  ? 91  ILE B C   1 
ATOM   1691 O  O   . ILE B 1 91  ? -15.283 -4.856  15.376 1.00 27.96  ? 91  ILE B O   1 
ATOM   1692 C  CB  . ILE B 1 91  ? -13.796 -2.832  17.105 1.00 35.27  ? 91  ILE B CB  1 
ATOM   1693 C  CG1 . ILE B 1 91  ? -12.597 -2.038  17.588 1.00 33.20  ? 91  ILE B CG1 1 
ATOM   1694 C  CG2 . ILE B 1 91  ? -14.921 -2.820  18.151 1.00 35.11  ? 91  ILE B CG2 1 
ATOM   1695 C  CD1 . ILE B 1 91  ? -12.771 -0.548  17.459 1.00 35.80  ? 91  ILE B CD1 1 
ATOM   1696 N  N   . LYS B 1 92  ? -14.910 -6.121  17.217 1.00 36.31  ? 92  LYS B N   1 
ATOM   1697 C  CA  . LYS B 1 92  ? -15.974 -7.057  16.910 1.00 42.37  ? 92  LYS B CA  1 
ATOM   1698 C  C   . LYS B 1 92  ? -17.331 -6.465  17.307 1.00 44.28  ? 92  LYS B C   1 
ATOM   1699 O  O   . LYS B 1 92  ? -17.494 -6.023  18.441 1.00 41.31  ? 92  LYS B O   1 
ATOM   1700 C  CB  . LYS B 1 92  ? -15.736 -8.375  17.645 1.00 44.12  ? 92  LYS B CB  1 
ATOM   1701 C  CG  . LYS B 1 92  ? -16.645 -9.487  17.165 1.00 50.01  ? 92  LYS B CG  1 
ATOM   1702 C  CD  . LYS B 1 92  ? -16.441 -10.809 17.876 1.00 55.66  ? 92  LYS B CD  1 
ATOM   1703 C  CE  . LYS B 1 92  ? -17.724 -11.569 17.846 1.00 64.95  ? 92  LYS B CE  1 
ATOM   1704 N  NZ  . LYS B 1 92  ? -17.492 -13.005 18.014 1.00 70.61  ? 92  LYS B NZ  1 
ATOM   1705 N  N   . LEU B 1 93  ? -18.284 -6.444  16.363 1.00 41.13  ? 93  LEU B N   1 
ATOM   1706 C  CA  . LEU B 1 93  ? -19.650 -6.051  16.661 1.00 43.59  ? 93  LEU B CA  1 
ATOM   1707 C  C   . LEU B 1 93  ? -20.310 -7.198  17.431 1.00 45.53  ? 93  LEU B C   1 
ATOM   1708 O  O   . LEU B 1 93  ? -19.947 -8.363  17.270 1.00 45.31  ? 93  LEU B O   1 
ATOM   1709 C  CB  . LEU B 1 93  ? -20.506 -5.680  15.451 1.00 44.17  ? 93  LEU B CB  1 
ATOM   1710 C  CG  . LEU B 1 93  ? -19.966 -4.670  14.434 1.00 47.48  ? 93  LEU B CG  1 
ATOM   1711 C  CD1 . LEU B 1 93  ? -21.168 -3.977  13.816 1.00 49.81  ? 93  LEU B CD1 1 
ATOM   1712 C  CD2 . LEU B 1 93  ? -18.993 -3.674  14.955 1.00 47.04  ? 93  LEU B CD2 1 
ATOM   1713 N  N   . ASP B 1 94  ? -21.295 -6.854  18.260 1.00 41.98  ? 94  ASP B N   1 
ATOM   1714 C  CA  . ASP B 1 94  ? -22.028 -7.854  19.017 1.00 43.30  ? 94  ASP B CA  1 
ATOM   1715 C  C   . ASP B 1 94  ? -23.298 -8.236  18.260 1.00 43.72  ? 94  ASP B C   1 
ATOM   1716 O  O   . ASP B 1 94  ? -24.286 -7.504  18.305 1.00 39.87  ? 94  ASP B O   1 
ATOM   1717 C  CB  . ASP B 1 94  ? -22.405 -7.351  20.394 1.00 41.93  ? 94  ASP B CB  1 
ATOM   1718 C  CG  . ASP B 1 94  ? -23.088 -8.409  21.254 1.00 47.75  ? 94  ASP B CG  1 
ATOM   1719 O  OD1 . ASP B 1 94  ? -23.418 -8.085  22.400 1.00 51.81  ? 94  ASP B OD1 1 
ATOM   1720 O  OD2 . ASP B 1 94  ? -23.306 -9.544  20.749 1.00 53.48  ? 94  ASP B OD2 1 
ATOM   1721 N  N   . ASP B 1 95  ? -23.281 -9.397  17.596 1.00 43.52  ? 95  ASP B N   1 
ATOM   1722 C  CA  . ASP B 1 95  ? -24.397 -9.766  16.747 1.00 50.19  ? 95  ASP B CA  1 
ATOM   1723 C  C   . ASP B 1 95  ? -25.579 -10.260 17.584 1.00 47.13  ? 95  ASP B C   1 
ATOM   1724 O  O   . ASP B 1 95  ? -26.629 -10.524 17.025 1.00 52.15  ? 95  ASP B O   1 
ATOM   1725 C  CB  . ASP B 1 95  ? -23.988 -10.697 15.617 1.00 57.28  ? 95  ASP B CB  1 
ATOM   1726 C  CG  . ASP B 1 95  ? -23.626 -12.123 16.002 1.00 64.16  ? 95  ASP B CG  1 
ATOM   1727 O  OD1 . ASP B 1 95  ? -23.296 -12.884 15.074 1.00 80.73  ? 95  ASP B OD1 1 
ATOM   1728 O  OD2 . ASP B 1 95  ? -23.685 -12.463 17.206 1.00 58.26  ? 95  ASP B OD2 1 
ATOM   1729 N  N   . LYS B 1 96  ? -25.435 -10.346 18.903 1.00 46.93  ? 96  LYS B N   1 
ATOM   1730 C  CA  . LYS B 1 96  ? -26.562 -10.648 19.769 1.00 52.21  ? 96  LYS B CA  1 
ATOM   1731 C  C   . LYS B 1 96  ? -27.266 -9.382  20.256 1.00 50.13  ? 96  LYS B C   1 
ATOM   1732 O  O   . LYS B 1 96  ? -28.303 -9.479  20.906 1.00 50.22  ? 96  LYS B O   1 
ATOM   1733 C  CB  . LYS B 1 96  ? -26.110 -11.494 20.967 1.00 55.58  ? 96  LYS B CB  1 
ATOM   1734 C  CG  . LYS B 1 96  ? -25.699 -12.909 20.557 1.00 67.75  ? 96  LYS B CG  1 
ATOM   1735 C  CD  . LYS B 1 96  ? -26.858 -13.799 20.103 1.00 82.23  ? 96  LYS B CD  1 
ATOM   1736 C  CE  . LYS B 1 96  ? -26.484 -15.006 19.284 1.00 86.04  ? 96  LYS B CE  1 
ATOM   1737 N  NZ  . LYS B 1 96  ? -26.404 -14.695 17.852 1.00 88.04  ? 96  LYS B NZ  1 
ATOM   1738 N  N   . ASP B 1 97  ? -26.718 -8.206  19.961 1.00 41.63  ? 97  ASP B N   1 
ATOM   1739 C  CA  . ASP B 1 97  ? -27.381 -6.966  20.317 1.00 37.09  ? 97  ASP B CA  1 
ATOM   1740 C  C   . ASP B 1 97  ? -28.548 -6.796  19.347 1.00 39.68  ? 97  ASP B C   1 
ATOM   1741 O  O   . ASP B 1 97  ? -28.394 -6.880  18.131 1.00 40.81  ? 97  ASP B O   1 
ATOM   1742 C  CB  . ASP B 1 97  ? -26.375 -5.833  20.394 1.00 38.55  ? 97  ASP B CB  1 
ATOM   1743 C  CG  . ASP B 1 97  ? -26.864 -4.417  20.651 1.00 39.96  ? 97  ASP B CG  1 
ATOM   1744 O  OD1 . ASP B 1 97  ? -25.997 -3.560  20.871 1.00 45.07  ? 97  ASP B OD1 1 
ATOM   1745 O  OD2 . ASP B 1 97  ? -28.063 -4.145  20.533 1.00 43.32  ? 97  ASP B OD2 1 
ATOM   1746 N  N   . PRO B 1 98  ? -29.780 -6.531  19.844 1.00 38.97  ? 98  PRO B N   1 
ATOM   1747 C  CA  . PRO B 1 98  ? -30.907 -6.319  18.943 1.00 40.62  ? 98  PRO B CA  1 
ATOM   1748 C  C   . PRO B 1 98  ? -30.653 -5.149  17.991 1.00 40.74  ? 98  PRO B C   1 
ATOM   1749 O  O   . PRO B 1 98  ? -31.228 -5.112  16.920 1.00 40.91  ? 98  PRO B O   1 
ATOM   1750 C  CB  . PRO B 1 98  ? -32.117 -6.059  19.864 1.00 43.42  ? 98  PRO B CB  1 
ATOM   1751 C  CG  . PRO B 1 98  ? -31.671 -6.444  21.253 1.00 45.24  ? 98  PRO B CG  1 
ATOM   1752 C  CD  . PRO B 1 98  ? -30.142 -6.409  21.267 1.00 42.63  ? 98  PRO B CD  1 
ATOM   1753 N  N   . ASN B 1 99  ? -29.764 -4.213  18.352 1.00 38.87  ? 99  ASN B N   1 
ATOM   1754 C  CA  . ASN B 1 99  ? -29.502 -3.076  17.479 1.00 42.30  ? 99  ASN B CA  1 
ATOM   1755 C  C   . ASN B 1 99  ? -28.423 -3.409  16.439 1.00 40.21  ? 99  ASN B C   1 
ATOM   1756 O  O   . ASN B 1 99  ? -28.025 -2.525  15.680 1.00 38.67  ? 99  ASN B O   1 
ATOM   1757 C  CB  . ASN B 1 99  ? -29.084 -1.839  18.260 1.00 45.61  ? 99  ASN B CB  1 
ATOM   1758 C  CG  . ASN B 1 99  ? -30.077 -1.415  19.319 1.00 49.13  ? 99  ASN B CG  1 
ATOM   1759 O  OD1 . ASN B 1 99  ? -31.255 -1.206  19.021 1.00 58.47  ? 99  ASN B OD1 1 
ATOM   1760 N  ND2 . ASN B 1 99  ? -29.622 -1.210  20.542 1.00 49.50  ? 99  ASN B ND2 1 
ATOM   1761 N  N   . PHE B 1 100 ? -27.982 -4.679  16.392 1.00 35.66  ? 100 PHE B N   1 
ATOM   1762 C  CA  . PHE B 1 100 ? -26.869 -5.056  15.535 1.00 35.08  ? 100 PHE B CA  1 
ATOM   1763 C  C   . PHE B 1 100 ? -27.100 -4.610  14.093 1.00 43.14  ? 100 PHE B C   1 
ATOM   1764 O  O   . PHE B 1 100 ? -26.260 -3.922  13.520 1.00 40.08  ? 100 PHE B O   1 
ATOM   1765 C  CB  . PHE B 1 100 ? -26.584 -6.551  15.617 1.00 35.97  ? 100 PHE B CB  1 
ATOM   1766 C  CG  . PHE B 1 100 ? -25.620 -7.067  14.550 1.00 40.40  ? 100 PHE B CG  1 
ATOM   1767 C  CD1 . PHE B 1 100 ? -26.103 -7.630  13.376 1.00 39.40  ? 100 PHE B CD1 1 
ATOM   1768 C  CD2 . PHE B 1 100 ? -24.236 -7.000  14.720 1.00 42.85  ? 100 PHE B CD2 1 
ATOM   1769 C  CE1 . PHE B 1 100 ? -25.239 -8.177  12.443 1.00 40.41  ? 100 PHE B CE1 1 
ATOM   1770 C  CE2 . PHE B 1 100 ? -23.363 -7.518  13.764 1.00 41.23  ? 100 PHE B CE2 1 
ATOM   1771 C  CZ  . PHE B 1 100 ? -23.865 -8.109  12.629 1.00 39.28  ? 100 PHE B CZ  1 
ATOM   1772 N  N   . LYS B 1 101 ? -28.255 -4.949  13.503 1.00 41.46  ? 101 LYS B N   1 
ATOM   1773 C  CA  . LYS B 1 101 ? -28.483 -4.683  12.095 1.00 36.60  ? 101 LYS B CA  1 
ATOM   1774 C  C   . LYS B 1 101 ? -28.447 -3.193  11.811 1.00 32.71  ? 101 LYS B C   1 
ATOM   1775 O  O   . LYS B 1 101 ? -27.972 -2.786  10.761 1.00 31.44  ? 101 LYS B O   1 
ATOM   1776 C  CB  . LYS B 1 101 ? -29.831 -5.251  11.648 1.00 46.25  ? 101 LYS B CB  1 
ATOM   1777 C  CG  . LYS B 1 101 ? -29.849 -6.758  11.489 1.00 54.27  ? 101 LYS B CG  1 
ATOM   1778 C  CD  . LYS B 1 101 ? -31.143 -7.329  10.903 1.00 63.24  ? 101 LYS B CD  1 
ATOM   1779 C  CE  . LYS B 1 101 ? -31.044 -8.824  10.718 1.00 73.48  ? 101 LYS B CE  1 
ATOM   1780 N  NZ  . LYS B 1 101 ? -32.324 -9.447  10.356 1.00 81.15  ? 101 LYS B NZ  1 
ATOM   1781 N  N   . ASP B 1 102 ? -28.981 -2.381  12.725 1.00 31.05  ? 102 ASP B N   1 
ATOM   1782 C  CA  . ASP B 1 102 ? -28.945 -0.937  12.555 1.00 37.39  ? 102 ASP B CA  1 
ATOM   1783 C  C   . ASP B 1 102 ? -27.508 -0.414  12.641 1.00 36.86  ? 102 ASP B C   1 
ATOM   1784 O  O   . ASP B 1 102 ? -27.176 0.613   12.031 1.00 36.72  ? 102 ASP B O   1 
ATOM   1785 C  CB  . ASP B 1 102 ? -29.852 -0.240  13.560 1.00 45.09  ? 102 ASP B CB  1 
ATOM   1786 C  CG  . ASP B 1 102 ? -31.357 -0.460  13.369 1.00 55.44  ? 102 ASP B CG  1 
ATOM   1787 O  OD1 . ASP B 1 102 ? -31.751 -1.036  12.321 1.00 51.81  ? 102 ASP B OD1 1 
ATOM   1788 O  OD2 . ASP B 1 102 ? -32.134 -0.063  14.269 1.00 58.76  ? 102 ASP B OD2 1 
ATOM   1789 N  N   . GLN B 1 103 ? -26.684 -1.084  13.451 1.00 28.55  ? 103 GLN B N   1 
ATOM   1790 C  CA  . GLN B 1 103 ? -25.304 -0.668  13.634 1.00 33.75  ? 103 GLN B CA  1 
ATOM   1791 C  C   . GLN B 1 103 ? -24.550 -0.895  12.321 1.00 36.29  ? 103 GLN B C   1 
ATOM   1792 O  O   . GLN B 1 103 ? -23.773 -0.046  11.892 1.00 32.93  ? 103 GLN B O   1 
ATOM   1793 C  CB  . GLN B 1 103 ? -24.618 -1.421  14.788 1.00 35.23  ? 103 GLN B CB  1 
ATOM   1794 C  CG  . GLN B 1 103 ? -25.065 -0.980  16.180 1.00 35.26  ? 103 GLN B CG  1 
ATOM   1795 C  CD  . GLN B 1 103 ? -24.828 -2.001  17.281 1.00 39.51  ? 103 GLN B CD  1 
ATOM   1796 O  OE1 . GLN B 1 103 ? -24.283 -3.097  17.080 1.00 39.38  ? 103 GLN B OE1 1 
ATOM   1797 N  NE2 . GLN B 1 103 ? -25.226 -1.603  18.482 1.00 37.00  ? 103 GLN B NE2 1 
ATOM   1798 N  N   . VAL B 1 104 ? -24.730 -2.073  11.716 1.00 34.92  ? 104 VAL B N   1 
ATOM   1799 C  CA  . VAL B 1 104 ? -24.117 -2.381  10.435 1.00 37.15  ? 104 VAL B CA  1 
ATOM   1800 C  C   . VAL B 1 104 ? -24.587 -1.363  9.386  1.00 37.42  ? 104 VAL B C   1 
ATOM   1801 O  O   . VAL B 1 104 ? -23.780 -0.831  8.626  1.00 37.10  ? 104 VAL B O   1 
ATOM   1802 C  CB  . VAL B 1 104 ? -24.479 -3.811  10.012 1.00 37.63  ? 104 VAL B CB  1 
ATOM   1803 C  CG1 . VAL B 1 104 ? -24.124 -4.100  8.562  1.00 42.87  ? 104 VAL B CG1 1 
ATOM   1804 C  CG2 . VAL B 1 104 ? -23.901 -4.849  10.938 1.00 35.66  ? 104 VAL B CG2 1 
ATOM   1805 N  N   . ILE B 1 105 ? -25.882 -1.053  9.360  1.00 33.20  ? 105 ILE B N   1 
ATOM   1806 C  CA  . ILE B 1 105 ? -26.414 -0.129  8.373  1.00 36.75  ? 105 ILE B CA  1 
ATOM   1807 C  C   . ILE B 1 105 ? -25.765 1.234   8.579  1.00 36.34  ? 105 ILE B C   1 
ATOM   1808 O  O   . ILE B 1 105 ? -25.372 1.872   7.590  1.00 33.63  ? 105 ILE B O   1 
ATOM   1809 C  CB  . ILE B 1 105 ? -27.970 -0.101  8.405  1.00 40.36  ? 105 ILE B CB  1 
ATOM   1810 C  CG1 . ILE B 1 105 ? -28.533 -1.346  7.702  1.00 42.38  ? 105 ILE B CG1 1 
ATOM   1811 C  CG2 . ILE B 1 105 ? -28.579 1.164   7.793  1.00 36.26  ? 105 ILE B CG2 1 
ATOM   1812 C  CD1 . ILE B 1 105 ? -29.981 -1.642  8.030  1.00 45.18  ? 105 ILE B CD1 1 
ATOM   1813 N  N   . LEU B 1 106 ? -25.645 1.668   9.845  1.00 34.64  ? 106 LEU B N   1 
ATOM   1814 C  CA  . LEU B 1 106 ? -25.110 2.993   10.109 1.00 36.77  ? 106 LEU B CA  1 
ATOM   1815 C  C   . LEU B 1 106 ? -23.630 3.033   9.689  1.00 33.29  ? 106 LEU B C   1 
ATOM   1816 O  O   . LEU B 1 106 ? -23.156 3.992   9.082  1.00 32.11  ? 106 LEU B O   1 
ATOM   1817 C  CB  . LEU B 1 106 ? -25.308 3.416   11.558 1.00 36.83  ? 106 LEU B CB  1 
ATOM   1818 C  CG  . LEU B 1 106 ? -24.661 4.752   11.966 1.00 42.83  ? 106 LEU B CG  1 
ATOM   1819 C  CD1 . LEU B 1 106 ? -24.977 5.954   11.090 1.00 41.86  ? 106 LEU B CD1 1 
ATOM   1820 C  CD2 . LEU B 1 106 ? -25.033 5.098   13.387 1.00 41.89  ? 106 LEU B CD2 1 
ATOM   1821 N  N   . LEU B 1 107 ? -22.894 1.975   9.967  1.00 31.57  ? 107 LEU B N   1 
ATOM   1822 C  CA  . LEU B 1 107 ? -21.474 1.997   9.608  1.00 34.81  ? 107 LEU B CA  1 
ATOM   1823 C  C   . LEU B 1 107 ? -21.295 1.978   8.082  1.00 36.57  ? 107 LEU B C   1 
ATOM   1824 O  O   . LEU B 1 107 ? -20.512 2.763   7.549  1.00 33.06  ? 107 LEU B O   1 
ATOM   1825 C  CB  . LEU B 1 107 ? -20.711 0.890   10.323 1.00 32.20  ? 107 LEU B CB  1 
ATOM   1826 C  CG  . LEU B 1 107 ? -20.579 1.114   11.838 1.00 35.47  ? 107 LEU B CG  1 
ATOM   1827 C  CD1 . LEU B 1 107 ? -20.065 -0.131  12.485 1.00 34.47  ? 107 LEU B CD1 1 
ATOM   1828 C  CD2 . LEU B 1 107 ? -19.740 2.348   12.233 1.00 32.84  ? 107 LEU B CD2 1 
ATOM   1829 N  N   . ASN B 1 108 ? -22.085 1.162   7.371  1.00 36.81  ? 108 ASN B N   1 
ATOM   1830 C  CA  . ASN B 1 108 ? -21.954 1.064   5.930  1.00 37.08  ? 108 ASN B CA  1 
ATOM   1831 C  C   . ASN B 1 108 ? -22.367 2.348   5.224  1.00 35.81  ? 108 ASN B C   1 
ATOM   1832 O  O   . ASN B 1 108 ? -21.934 2.606   4.119  1.00 38.98  ? 108 ASN B O   1 
ATOM   1833 C  CB  . ASN B 1 108 ? -22.708 -0.114  5.353  1.00 36.33  ? 108 ASN B CB  1 
ATOM   1834 C  CG  . ASN B 1 108 ? -21.900 -1.367  5.527  1.00 40.23  ? 108 ASN B CG  1 
ATOM   1835 O  OD1 . ASN B 1 108 ? -20.659 -1.311  5.489  1.00 42.96  ? 108 ASN B OD1 1 
ATOM   1836 N  ND2 . ASN B 1 108 ? -22.573 -2.484  5.764  1.00 44.90  ? 108 ASN B ND2 1 
ATOM   1837 N  N   . LYS B 1 109 ? -23.185 3.149   5.870  1.00 30.49  ? 109 LYS B N   1 
ATOM   1838 C  CA  . LYS B 1 109 ? -23.655 4.400   5.315  1.00 34.71  ? 109 LYS B CA  1 
ATOM   1839 C  C   . LYS B 1 109 ? -22.529 5.403   5.134  1.00 34.93  ? 109 LYS B C   1 
ATOM   1840 O  O   . LYS B 1 109 ? -22.662 6.369   4.371  1.00 31.31  ? 109 LYS B O   1 
ATOM   1841 C  CB  . LYS B 1 109 ? -24.699 4.869   6.325  1.00 40.26  ? 109 LYS B CB  1 
ATOM   1842 C  CG  . LYS B 1 109 ? -25.269 6.253   6.217  1.00 48.98  ? 109 LYS B CG  1 
ATOM   1843 C  CD  . LYS B 1 109 ? -26.537 6.335   7.054  1.00 48.59  ? 109 LYS B CD  1 
ATOM   1844 C  CE  . LYS B 1 109 ? -27.176 7.666   6.940  1.00 54.83  ? 109 LYS B CE  1 
ATOM   1845 N  NZ  . LYS B 1 109 ? -28.564 7.564   7.395  1.00 60.59  ? 109 LYS B NZ  1 
ATOM   1846 N  N   . HIS B 1 110 ? -21.477 5.235   5.952  1.00 31.35  ? 110 HIS B N   1 
ATOM   1847 C  CA  . HIS B 1 110 ? -20.368 6.162   5.940  1.00 30.58  ? 110 HIS B CA  1 
ATOM   1848 C  C   . HIS B 1 110 ? -19.098 5.605   5.295  1.00 27.38  ? 110 HIS B C   1 
ATOM   1849 O  O   . HIS B 1 110 ? -18.241 6.386   4.922  1.00 31.91  ? 110 HIS B O   1 
ATOM   1850 C  CB  . HIS B 1 110 ? -20.128 6.610   7.383  1.00 30.50  ? 110 HIS B CB  1 
ATOM   1851 C  CG  . HIS B 1 110 ? -21.264 7.397   7.917  1.00 27.11  ? 110 HIS B CG  1 
ATOM   1852 N  ND1 . HIS B 1 110 ? -21.504 8.698   7.541  1.00 28.27  ? 110 HIS B ND1 1 
ATOM   1853 C  CD2 . HIS B 1 110 ? -22.217 7.054   8.789  1.00 27.16  ? 110 HIS B CD2 1 
ATOM   1854 C  CE1 . HIS B 1 110 ? -22.579 9.140   8.198  1.00 29.23  ? 110 HIS B CE1 1 
ATOM   1855 N  NE2 . HIS B 1 110 ? -23.025 8.147   8.961  1.00 27.79  ? 110 HIS B NE2 1 
ATOM   1856 N  N   . ILE B 1 111 ? -18.953 4.286   5.168  1.00 27.67  ? 111 ILE B N   1 
ATOM   1857 C  CA  . ILE B 1 111 ? -17.714 3.725   4.658  1.00 30.47  ? 111 ILE B CA  1 
ATOM   1858 C  C   . ILE B 1 111 ? -17.640 3.937   3.141  1.00 37.07  ? 111 ILE B C   1 
ATOM   1859 O  O   . ILE B 1 111 ? -18.449 3.396   2.390  1.00 29.38  ? 111 ILE B O   1 
ATOM   1860 C  CB  . ILE B 1 111 ? -17.617 2.237   5.013  1.00 30.03  ? 111 ILE B CB  1 
ATOM   1861 C  CG1 . ILE B 1 111 ? -17.484 2.034   6.534  1.00 30.32  ? 111 ILE B CG1 1 
ATOM   1862 C  CG2 . ILE B 1 111 ? -16.465 1.566   4.243  1.00 33.20  ? 111 ILE B CG2 1 
ATOM   1863 C  CD1 . ILE B 1 111 ? -17.597 0.592   6.980  1.00 28.69  ? 111 ILE B CD1 1 
ATOM   1864 N  N   . ASP B 1 112 ? -16.630 4.693   2.692  1.00 38.25  ? 112 ASP B N   1 
ATOM   1865 C  CA  . ASP B 1 112 ? -16.339 4.911   1.270  1.00 38.84  ? 112 ASP B CA  1 
ATOM   1866 C  C   . ASP B 1 112 ? -17.429 5.696   0.547  1.00 40.00  ? 112 ASP B C   1 
ATOM   1867 O  O   . ASP B 1 112 ? -17.420 5.780   -0.674 1.00 38.47  ? 112 ASP B O   1 
ATOM   1868 C  CB  . ASP B 1 112 ? -16.095 3.618   0.500  1.00 35.81  ? 112 ASP B CB  1 
ATOM   1869 C  CG  . ASP B 1 112 ? -14.727 2.994   0.731  1.00 34.68  ? 112 ASP B CG  1 
ATOM   1870 O  OD1 . ASP B 1 112 ? -13.796 3.740   1.102  1.00 31.41  ? 112 ASP B OD1 1 
ATOM   1871 O  OD2 . ASP B 1 112 ? -14.630 1.761   0.638  1.00 41.81  ? 112 ASP B OD2 1 
ATOM   1872 N  N   . ALA B 1 113 ? -18.290 6.349   1.302  1.00 34.91  ? 113 ALA B N   1 
ATOM   1873 C  CA  . ALA B 1 113 ? -19.419 7.059   0.736  1.00 33.89  ? 113 ALA B CA  1 
ATOM   1874 C  C   . ALA B 1 113 ? -18.918 8.242   -0.105 1.00 36.54  ? 113 ALA B C   1 
ATOM   1875 O  O   . ALA B 1 113 ? -19.608 8.666   -1.039 1.00 33.24  ? 113 ALA B O   1 
ATOM   1876 C  CB  . ALA B 1 113 ? -20.428 7.389   1.898  1.00 30.19  ? 113 ALA B CB  1 
ATOM   1877 N  N   . TYR B 1 114 ? -17.677 8.708   0.128  1.00 33.16  ? 114 TYR B N   1 
ATOM   1878 C  CA  . TYR B 1 114 ? -17.102 9.858   -0.583 1.00 32.23  ? 114 TYR B CA  1 
ATOM   1879 C  C   . TYR B 1 114 ? -17.096 9.623   -2.107 1.00 28.28  ? 114 TYR B C   1 
ATOM   1880 O  O   . TYR B 1 114 ? -17.017 10.561  -2.901 1.00 30.40  ? 114 TYR B O   1 
ATOM   1881 C  CB  . TYR B 1 114 ? -15.654 10.182  -0.138 1.00 31.38  ? 114 TYR B CB  1 
ATOM   1882 C  CG  . TYR B 1 114 ? -14.628 9.154   -0.611 1.00 32.26  ? 114 TYR B CG  1 
ATOM   1883 C  CD1 . TYR B 1 114 ? -13.942 9.295   -1.825 1.00 30.60  ? 114 TYR B CD1 1 
ATOM   1884 C  CD2 . TYR B 1 114 ? -14.389 8.004   0.130  1.00 31.77  ? 114 TYR B CD2 1 
ATOM   1885 C  CE1 . TYR B 1 114 ? -13.097 8.302   -2.289 1.00 31.18  ? 114 TYR B CE1 1 
ATOM   1886 C  CE2 . TYR B 1 114 ? -13.533 7.014   -0.322 1.00 32.56  ? 114 TYR B CE2 1 
ATOM   1887 C  CZ  . TYR B 1 114 ? -12.889 7.161   -1.542 1.00 31.76  ? 114 TYR B CZ  1 
ATOM   1888 O  OH  . TYR B 1 114 ? -12.056 6.158   -1.937 1.00 31.38  ? 114 TYR B OH  1 
ATOM   1889 N  N   . LYS B 1 115 ? -17.063 8.364   -2.502 1.00 24.84  ? 115 LYS B N   1 
ATOM   1890 C  CA  . LYS B 1 115 ? -17.016 7.991   -3.894 1.00 31.26  ? 115 LYS B CA  1 
ATOM   1891 C  C   . LYS B 1 115 ? -18.226 8.477   -4.683 1.00 34.38  ? 115 LYS B C   1 
ATOM   1892 O  O   . LYS B 1 115 ? -18.139 8.580   -5.893 1.00 30.94  ? 115 LYS B O   1 
ATOM   1893 C  CB  . LYS B 1 115 ? -16.988 6.468   -3.970 1.00 28.26  ? 115 LYS B CB  1 
ATOM   1894 C  CG  . LYS B 1 115 ? -15.630 5.889   -3.677 1.00 32.44  ? 115 LYS B CG  1 
ATOM   1895 C  CD  . LYS B 1 115 ? -15.723 4.374   -3.735 1.00 36.29  ? 115 LYS B CD  1 
ATOM   1896 C  CE  . LYS B 1 115 ? -14.425 3.739   -3.401 1.00 45.05  ? 115 LYS B CE  1 
ATOM   1897 N  NZ  . LYS B 1 115 ? -14.625 2.287   -3.385 1.00 52.04  ? 115 LYS B NZ  1 
ATOM   1898 N  N   . THR B 1 116 ? -19.348 8.748   -4.000 1.00 31.83  ? 116 THR B N   1 
ATOM   1899 C  CA  . THR B 1 116 ? -20.582 9.061   -4.679 1.00 30.74  ? 116 THR B CA  1 
ATOM   1900 C  C   . THR B 1 116 ? -20.777 10.568  -4.739 1.00 30.36  ? 116 THR B C   1 
ATOM   1901 O  O   . THR B 1 116 ? -21.813 11.003  -5.187 1.00 32.56  ? 116 THR B O   1 
ATOM   1902 C  CB  . THR B 1 116 ? -21.760 8.371   -3.975 1.00 33.63  ? 116 THR B CB  1 
ATOM   1903 O  OG1 . THR B 1 116 ? -21.911 9.017   -2.725 1.00 30.38  ? 116 THR B OG1 1 
ATOM   1904 C  CG2 . THR B 1 116 ? -21.576 6.876   -3.768 1.00 31.23  ? 116 THR B CG2 1 
ATOM   1905 N  N   . PHE B 1 117 ? -19.826 11.376  -4.287 1.00 26.62  ? 117 PHE B N   1 
ATOM   1906 C  CA  . PHE B 1 117 ? -19.955 12.823  -4.398 1.00 26.56  ? 117 PHE B CA  1 
ATOM   1907 C  C   . PHE B 1 117 ? -18.601 13.470  -4.636 1.00 28.75  ? 117 PHE B C   1 
ATOM   1908 O  O   . PHE B 1 117 ? -17.550 12.873  -4.369 1.00 30.15  ? 117 PHE B O   1 
ATOM   1909 C  CB  . PHE B 1 117 ? -20.536 13.529  -3.167 1.00 33.01  ? 117 PHE B CB  1 
ATOM   1910 C  CG  . PHE B 1 117 ? -19.974 13.144  -1.803 1.00 35.62  ? 117 PHE B CG  1 
ATOM   1911 C  CD1 . PHE B 1 117 ? -20.515 12.088  -1.089 1.00 41.69  ? 117 PHE B CD1 1 
ATOM   1912 C  CD2 . PHE B 1 117 ? -18.923 13.854  -1.241 1.00 37.61  ? 117 PHE B CD2 1 
ATOM   1913 C  CE1 . PHE B 1 117 ? -20.039 11.770  0.179  1.00 46.63  ? 117 PHE B CE1 1 
ATOM   1914 C  CE2 . PHE B 1 117 ? -18.442 13.526  0.016  1.00 40.57  ? 117 PHE B CE2 1 
ATOM   1915 C  CZ  . PHE B 1 117 ? -18.980 12.464  0.711  1.00 42.86  ? 117 PHE B CZ  1 
ATOM   1916 N  N   . PRO B 1 118 ? -18.568 14.709  -5.184 1.00 31.19  ? 118 PRO B N   1 
ATOM   1917 C  CA  . PRO B 1 118 ? -17.309 15.398  -5.405 1.00 32.82  ? 118 PRO B CA  1 
ATOM   1918 C  C   . PRO B 1 118 ? -16.592 15.629  -4.066 1.00 42.64  ? 118 PRO B C   1 
ATOM   1919 O  O   . PRO B 1 118 ? -17.294 16.205  -3.188 1.00 34.28  ? 118 PRO B O   1 
ATOM   1920 C  CB  . PRO B 1 118 ? -17.666 16.717  -6.100 1.00 35.46  ? 118 PRO B CB  1 
ATOM   1921 C  CG  . PRO B 1 118 ? -19.131 16.575  -6.531 1.00 35.31  ? 118 PRO B CG  1 
ATOM   1922 C  CD  . PRO B 1 118 ? -19.715 15.426  -5.769 1.00 33.24  ? 118 PRO B CD  1 
ATOM   1923 O  OXT . PRO B 1 118 ? -15.390 15.235  -3.946 1.00 36.55  ? 118 PRO B OXT 1 
HETATM 1924 C  C1  . PEG C 2 .   ? -9.072  8.462   23.758 1.00 64.82  ? 201 PEG A C1  1 
HETATM 1925 O  O1  . PEG C 2 .   ? -7.890  9.245   23.610 1.00 58.10  ? 201 PEG A O1  1 
HETATM 1926 C  C2  . PEG C 2 .   ? -10.265 9.280   24.146 1.00 65.90  ? 201 PEG A C2  1 
HETATM 1927 O  O2  . PEG C 2 .   ? -11.318 9.070   23.207 1.00 74.31  ? 201 PEG A O2  1 
HETATM 1928 C  C3  . PEG C 2 .   ? -12.450 8.402   23.755 1.00 78.04  ? 201 PEG A C3  1 
HETATM 1929 C  C4  . PEG C 2 .   ? -13.268 7.822   22.653 1.00 72.13  ? 201 PEG A C4  1 
HETATM 1930 O  O4  . PEG C 2 .   ? -13.960 6.665   23.072 1.00 78.85  ? 201 PEG A O4  1 
HETATM 1931 C  C1  . PEG D 2 .   ? -7.245  -6.254  11.411 1.00 77.99  ? 202 PEG A C1  1 
HETATM 1932 O  O1  . PEG D 2 .   ? -7.417  -5.609  10.161 1.00 65.24  ? 202 PEG A O1  1 
HETATM 1933 C  C2  . PEG D 2 .   ? -7.508  -7.733  11.360 1.00 86.04  ? 202 PEG A C2  1 
HETATM 1934 O  O2  . PEG D 2 .   ? -8.720  -8.012  10.664 1.00 88.94  ? 202 PEG A O2  1 
HETATM 1935 C  C3  . PEG D 2 .   ? -9.111  -9.383  10.743 1.00 87.91  ? 202 PEG A C3  1 
HETATM 1936 C  C4  . PEG D 2 .   ? -10.517 -9.501  11.256 1.00 78.70  ? 202 PEG A C4  1 
HETATM 1937 O  O4  . PEG D 2 .   ? -10.690 -10.610 12.126 1.00 74.59  ? 202 PEG A O4  1 
HETATM 1938 C  C1  . EDO E 3 .   ? -11.449 -11.607 27.902 1.00 77.58  ? 203 EDO A C1  1 
HETATM 1939 O  O1  . EDO E 3 .   ? -11.615 -10.202 27.799 1.00 71.57  ? 203 EDO A O1  1 
HETATM 1940 C  C2  . EDO E 3 .   ? -12.745 -12.283 27.735 1.00 74.99  ? 203 EDO A C2  1 
HETATM 1941 O  O2  . EDO E 3 .   ? -13.763 -11.306 27.587 1.00 67.27  ? 203 EDO A O2  1 
HETATM 1942 C  C1  . GOL F 4 .   ? 18.198  3.491   22.549 0.70 51.60  ? 204 GOL A C1  1 
HETATM 1943 O  O1  . GOL F 4 .   ? 17.770  4.395   21.529 0.70 45.57  ? 204 GOL A O1  1 
HETATM 1944 C  C2  . GOL F 4 .   ? 18.918  4.229   23.654 0.70 46.15  ? 204 GOL A C2  1 
HETATM 1945 O  O2  . GOL F 4 .   ? 20.290  3.839   23.670 0.70 49.83  ? 204 GOL A O2  1 
HETATM 1946 C  C3  . GOL F 4 .   ? 18.838  5.731   23.508 0.70 49.09  ? 204 GOL A C3  1 
HETATM 1947 O  O3  . GOL F 4 .   ? 19.111  6.413   24.729 0.70 48.12  ? 204 GOL A O3  1 
HETATM 1948 NA NA  . NA  G 5 .   ? 4.814   2.243   36.403 1.00 51.24  ? 205 NA  A NA  1 
HETATM 1949 NA NA  . NA  H 5 .   ? 12.711  14.814  27.176 1.00 49.95  ? 206 NA  A NA  1 
HETATM 1950 C  C1  . EDO I 3 .   ? -20.366 9.419   23.545 1.00 72.13  ? 201 EDO B C1  1 
HETATM 1951 O  O1  . EDO I 3 .   ? -21.650 8.895   23.232 1.00 63.11  ? 201 EDO B O1  1 
HETATM 1952 C  C2  . EDO I 3 .   ? -20.096 10.669  22.804 1.00 69.80  ? 201 EDO B C2  1 
HETATM 1953 O  O2  . EDO I 3 .   ? -21.114 10.929  21.857 1.00 62.52  ? 201 EDO B O2  1 
HETATM 1954 C  C1  . EDO J 3 .   ? -33.274 -4.241  12.344 1.00 89.41  ? 202 EDO B C1  1 
HETATM 1955 O  O1  . EDO J 3 .   ? -33.598 -2.914  12.004 1.00 79.43  ? 202 EDO B O1  1 
HETATM 1956 C  C2  . EDO J 3 .   ? -34.134 -4.798  13.411 1.00 92.47  ? 202 EDO B C2  1 
HETATM 1957 O  O2  . EDO J 3 .   ? -35.210 -5.526  12.869 1.00 97.73  ? 202 EDO B O2  1 
HETATM 1958 C  C1  . EDO K 3 .   ? -1.857  20.241  9.637  1.00 74.94  ? 203 EDO B C1  1 
HETATM 1959 O  O1  . EDO K 3 .   ? -2.289  19.124  10.394 1.00 74.18  ? 203 EDO B O1  1 
HETATM 1960 C  C2  . EDO K 3 .   ? -2.841  21.346  9.607  1.00 68.05  ? 203 EDO B C2  1 
HETATM 1961 O  O2  . EDO K 3 .   ? -4.088  20.885  9.180  1.00 70.09  ? 203 EDO B O2  1 
HETATM 1962 C  C1  . EDO L 3 .   ? -21.428 1.642   1.531  1.00 62.70  ? 204 EDO B C1  1 
HETATM 1963 O  O1  . EDO L 3 .   ? -20.359 1.286   2.381  1.00 53.30  ? 204 EDO B O1  1 
HETATM 1964 C  C2  . EDO L 3 .   ? -21.144 2.866   0.732  1.00 63.07  ? 204 EDO B C2  1 
HETATM 1965 O  O2  . EDO L 3 .   ? -21.356 4.095   1.414  1.00 53.77  ? 204 EDO B O2  1 
HETATM 1966 NA NA  . NA  M 5 .   ? -1.674  10.148  5.666  1.00 52.03  ? 205 NA  B NA  1 
HETATM 1967 O  O   . HOH N 6 .   ? 5.466   -2.215  41.524 1.00 77.35  ? 301 HOH A O   1 
HETATM 1968 O  O   . HOH N 6 .   ? -7.927  0.762   2.934  1.00 53.96  ? 302 HOH A O   1 
HETATM 1969 O  O   . HOH N 6 .   ? 11.668  2.521   33.671 1.00 67.27  ? 303 HOH A O   1 
HETATM 1970 O  O   . HOH N 6 .   ? 3.922   16.281  20.427 1.00 46.09  ? 304 HOH A O   1 
HETATM 1971 O  O   . HOH N 6 .   ? -5.116  -6.978  38.079 1.00 44.66  ? 305 HOH A O   1 
HETATM 1972 O  O   . HOH N 6 .   ? -10.221 5.053   29.890 1.00 37.07  ? 306 HOH A O   1 
HETATM 1973 O  O   . HOH N 6 .   ? -15.951 -4.999  20.786 1.00 38.82  ? 307 HOH A O   1 
HETATM 1974 O  O   . HOH N 6 .   ? -17.433 -6.726  27.250 1.00 40.88  ? 308 HOH A O   1 
HETATM 1975 O  O   . HOH N 6 .   ? -11.749 -9.454  30.756 1.00 34.28  ? 309 HOH A O   1 
HETATM 1976 O  O   . HOH N 6 .   ? 8.711   0.297   31.183 1.00 38.87  ? 310 HOH A O   1 
HETATM 1977 O  O   . HOH N 6 .   ? 6.291   9.989   32.764 1.00 44.55  ? 311 HOH A O   1 
HETATM 1978 O  O   . HOH N 6 .   ? 4.597   -8.929  16.672 1.00 32.07  ? 312 HOH A O   1 
HETATM 1979 O  O   . HOH N 6 .   ? -1.806  -5.615  37.763 1.00 27.51  ? 313 HOH A O   1 
HETATM 1980 O  O   . HOH N 6 .   ? 3.555   -8.114  33.088 1.00 33.04  ? 314 HOH A O   1 
HETATM 1981 O  O   . HOH N 6 .   ? -1.702  12.029  27.575 1.00 38.42  ? 315 HOH A O   1 
HETATM 1982 O  O   . HOH N 6 .   ? 16.409  11.882  25.553 1.00 56.21  ? 316 HOH A O   1 
HETATM 1983 O  O   . HOH N 6 .   ? -9.725  -0.880  7.647  1.00 28.41  ? 317 HOH A O   1 
HETATM 1984 O  O   . HOH N 6 .   ? -15.693 -2.570  41.206 1.00 46.36  ? 318 HOH A O   1 
HETATM 1985 O  O   . HOH N 6 .   ? -1.295  14.562  21.919 1.00 35.49  ? 319 HOH A O   1 
HETATM 1986 O  O   . HOH N 6 .   ? -5.742  9.958   7.667  1.00 31.46  ? 320 HOH A O   1 
HETATM 1987 O  O   . HOH N 6 .   ? 13.916  12.520  29.904 1.00 47.76  ? 321 HOH A O   1 
HETATM 1988 O  O   . HOH N 6 .   ? 1.379   15.187  21.802 1.00 43.16  ? 322 HOH A O   1 
HETATM 1989 O  O   . HOH N 6 .   ? -14.242 3.805   27.701 1.00 44.16  ? 323 HOH A O   1 
HETATM 1990 O  O   . HOH N 6 .   ? -9.808  -1.082  37.094 1.00 44.46  ? 324 HOH A O   1 
HETATM 1991 O  O   . HOH N 6 .   ? -6.664  -7.243  19.488 1.00 38.17  ? 325 HOH A O   1 
HETATM 1992 O  O   . HOH N 6 .   ? 18.971  9.072   24.319 1.00 56.53  ? 326 HOH A O   1 
HETATM 1993 O  O   . HOH N 6 .   ? -13.527 1.909   30.772 1.00 36.91  ? 327 HOH A O   1 
HETATM 1994 O  O   . HOH N 6 .   ? 12.518  18.119  19.131 1.00 43.74  ? 328 HOH A O   1 
HETATM 1995 O  O   . HOH N 6 .   ? 10.746  -3.334  22.427 1.00 39.82  ? 329 HOH A O   1 
HETATM 1996 O  O   . HOH N 6 .   ? -8.100  6.285   21.742 1.00 28.75  ? 330 HOH A O   1 
HETATM 1997 O  O   . HOH N 6 .   ? 3.814   14.548  28.959 1.00 48.96  ? 331 HOH A O   1 
HETATM 1998 O  O   . HOH N 6 .   ? -12.969 10.994  22.167 1.00 35.33  ? 332 HOH A O   1 
HETATM 1999 O  O   . HOH N 6 .   ? 13.655  15.434  21.643 1.00 43.17  ? 333 HOH A O   1 
HETATM 2000 O  O   . HOH N 6 .   ? 11.606  5.452   27.874 1.00 48.33  ? 334 HOH A O   1 
HETATM 2001 O  O   . HOH N 6 .   ? 15.275  3.296   21.212 1.00 36.37  ? 335 HOH A O   1 
HETATM 2002 O  O   . HOH N 6 .   ? -4.091  -9.412  22.298 1.00 31.14  ? 336 HOH A O   1 
HETATM 2003 O  O   . HOH N 6 .   ? 4.755   -6.424  23.647 1.00 30.50  ? 337 HOH A O   1 
HETATM 2004 O  O   . HOH N 6 .   ? -11.928 8.121   7.889  1.00 25.77  ? 338 HOH A O   1 
HETATM 2005 O  O   . HOH N 6 .   ? 5.134   14.126  18.969 1.00 36.30  ? 339 HOH A O   1 
HETATM 2006 O  O   . HOH N 6 .   ? 2.617   -12.549 25.228 1.00 46.53  ? 340 HOH A O   1 
HETATM 2007 O  O   . HOH N 6 .   ? 9.969   -0.093  17.462 1.00 54.82  ? 341 HOH A O   1 
HETATM 2008 O  O   . HOH N 6 .   ? 1.380   -14.776 22.472 1.00 48.75  ? 342 HOH A O   1 
HETATM 2009 O  O   . HOH N 6 .   ? -15.676 6.604   25.274 1.00 53.45  ? 343 HOH A O   1 
HETATM 2010 O  O   . HOH N 6 .   ? -7.407  -9.234  38.465 1.00 53.47  ? 344 HOH A O   1 
HETATM 2011 O  O   . HOH N 6 .   ? -0.305  -10.511 32.434 1.00 38.76  ? 345 HOH A O   1 
HETATM 2012 O  O   . HOH N 6 .   ? -6.076  6.963   29.360 1.00 32.46  ? 346 HOH A O   1 
HETATM 2013 O  O   . HOH N 6 .   ? -0.218  6.916   35.179 1.00 44.44  ? 347 HOH A O   1 
HETATM 2014 O  O   . HOH N 6 .   ? -14.841 11.962  12.316 1.00 30.43  ? 348 HOH A O   1 
HETATM 2015 O  O   . HOH N 6 .   ? -10.887 0.053   34.700 1.00 30.32  ? 349 HOH A O   1 
HETATM 2016 O  O   . HOH N 6 .   ? -1.693  -7.821  37.263 1.00 53.84  ? 350 HOH A O   1 
HETATM 2017 O  O   . HOH N 6 .   ? -13.457 0.601   33.488 1.00 35.96  ? 351 HOH A O   1 
HETATM 2018 O  O   . HOH N 6 .   ? -13.081 -1.303  31.729 1.00 28.39  ? 352 HOH A O   1 
HETATM 2019 O  O   . HOH N 6 .   ? 11.733  7.694   26.945 1.00 37.54  ? 353 HOH A O   1 
HETATM 2020 O  O   . HOH N 6 .   ? 9.343   -6.173  29.855 1.00 33.74  ? 354 HOH A O   1 
HETATM 2021 O  O   . HOH N 6 .   ? -6.443  -0.212  5.122  1.00 59.68  ? 355 HOH A O   1 
HETATM 2022 O  O   . HOH N 6 .   ? -0.684  12.758  12.134 1.00 29.78  ? 356 HOH A O   1 
HETATM 2023 O  O   . HOH N 6 .   ? -15.257 10.513  9.837  1.00 30.43  ? 357 HOH A O   1 
HETATM 2024 O  O   . HOH N 6 .   ? 15.673  9.008   20.681 1.00 37.98  ? 358 HOH A O   1 
HETATM 2025 O  O   . HOH N 6 .   ? 6.102   13.404  25.551 1.00 25.88  ? 359 HOH A O   1 
HETATM 2026 O  O   . HOH N 6 .   ? 13.917  4.234   16.395 1.00 46.98  ? 360 HOH A O   1 
HETATM 2027 O  O   . HOH N 6 .   ? -14.131 12.923  19.656 1.00 29.61  ? 361 HOH A O   1 
HETATM 2028 O  O   . HOH N 6 .   ? 11.999  5.467   33.984 1.00 59.17  ? 362 HOH A O   1 
HETATM 2029 O  O   . HOH N 6 .   ? -19.734 -2.575  21.345 1.00 45.39  ? 363 HOH A O   1 
HETATM 2030 O  O   . HOH N 6 .   ? -4.072  7.395   8.865  1.00 42.92  ? 364 HOH A O   1 
HETATM 2031 O  O   . HOH N 6 .   ? -7.763  12.131  24.116 1.00 49.30  ? 365 HOH A O   1 
HETATM 2032 O  O   . HOH N 6 .   ? -16.317 13.367  13.953 1.00 27.96  ? 366 HOH A O   1 
HETATM 2033 O  O   . HOH N 6 .   ? 13.942  2.336   23.580 1.00 38.28  ? 367 HOH A O   1 
HETATM 2034 O  O   . HOH N 6 .   ? -16.659 -6.527  23.270 1.00 45.61  ? 368 HOH A O   1 
HETATM 2035 O  O   . HOH N 6 .   ? -4.836  -6.531  16.375 1.00 42.35  ? 369 HOH A O   1 
HETATM 2036 O  O   . HOH N 6 .   ? -5.519  6.223   7.198  1.00 40.35  ? 370 HOH A O   1 
HETATM 2037 O  O   . HOH N 6 .   ? 5.729   16.452  24.994 1.00 46.91  ? 371 HOH A O   1 
HETATM 2038 O  O   . HOH N 6 .   ? -13.259 -10.053 34.814 1.00 67.27  ? 372 HOH A O   1 
HETATM 2039 O  O   . HOH N 6 .   ? -2.910  -11.360 33.964 1.00 35.78  ? 373 HOH A O   1 
HETATM 2040 O  O   . HOH N 6 .   ? 6.011   18.921  25.020 1.00 45.57  ? 374 HOH A O   1 
HETATM 2041 O  O   . HOH N 6 .   ? 1.765   13.869  17.553 1.00 37.91  ? 375 HOH A O   1 
HETATM 2042 O  O   . HOH N 6 .   ? -17.134 -6.521  41.834 1.00 56.32  ? 376 HOH A O   1 
HETATM 2043 O  O   . HOH N 6 .   ? -15.656 -2.656  3.991  1.00 49.46  ? 377 HOH A O   1 
HETATM 2044 O  O   . HOH N 6 .   ? -18.759 6.438   23.138 1.00 40.12  ? 378 HOH A O   1 
HETATM 2045 O  O   . HOH N 6 .   ? 8.975   -3.969  31.754 1.00 42.04  ? 379 HOH A O   1 
HETATM 2046 O  O   . HOH N 6 .   ? 0.427   -10.092 27.542 1.00 41.45  ? 380 HOH A O   1 
HETATM 2047 O  O   . HOH N 6 .   ? -12.943 -0.323  3.441  1.00 58.66  ? 381 HOH A O   1 
HETATM 2048 O  O   . HOH N 6 .   ? -5.299  -14.213 25.820 1.00 47.58  ? 382 HOH A O   1 
HETATM 2049 O  O   . HOH N 6 .   ? 5.061   -8.607  35.130 1.00 51.35  ? 383 HOH A O   1 
HETATM 2050 O  O   . HOH N 6 .   ? 11.804  -9.370  29.241 1.00 59.18  ? 384 HOH A O   1 
HETATM 2051 O  O   . HOH N 6 .   ? 6.072   -9.320  14.089 1.00 53.57  ? 385 HOH A O   1 
HETATM 2052 O  O   . HOH N 6 .   ? -10.652 2.354   35.495 1.00 53.97  ? 386 HOH A O   1 
HETATM 2053 O  O   . HOH N 6 .   ? -17.206 3.981   28.307 1.00 52.29  ? 387 HOH A O   1 
HETATM 2054 O  O   . HOH N 6 .   ? -13.031 5.945   26.670 1.00 72.05  ? 388 HOH A O   1 
HETATM 2055 O  O   . HOH N 6 .   ? 8.207   11.263  26.380 1.00 39.85  ? 389 HOH A O   1 
HETATM 2056 O  O   . HOH N 6 .   ? 23.475  2.066   25.314 1.00 54.06  ? 390 HOH A O   1 
HETATM 2057 O  O   . HOH N 6 .   ? 1.415   16.724  16.472 1.00 51.04  ? 391 HOH A O   1 
HETATM 2058 O  O   . HOH N 6 .   ? -6.177  -1.926  42.786 1.00 56.91  ? 392 HOH A O   1 
HETATM 2059 O  O   . HOH N 6 .   ? 17.755  10.922  23.785 1.00 54.02  ? 393 HOH A O   1 
HETATM 2060 O  O   . HOH N 6 .   ? -7.738  -13.279 24.533 1.00 61.73  ? 394 HOH A O   1 
HETATM 2061 O  O   . HOH O 6 .   ? -29.582 9.194   6.134  1.00 47.98  ? 301 HOH B O   1 
HETATM 2062 O  O   . HOH O 6 .   ? 11.561  11.836  12.019 1.00 31.81  ? 302 HOH B O   1 
HETATM 2063 O  O   . HOH O 6 .   ? -11.733 4.087   -0.610 1.00 30.96  ? 303 HOH B O   1 
HETATM 2064 O  O   . HOH O 6 .   ? -19.561 22.368  8.914  1.00 50.13  ? 304 HOH B O   1 
HETATM 2065 O  O   . HOH O 6 .   ? -4.293  3.286   6.655  1.00 43.85  ? 305 HOH B O   1 
HETATM 2066 O  O   . HOH O 6 .   ? -21.543 6.597   22.283 1.00 33.32  ? 306 HOH B O   1 
HETATM 2067 O  O   . HOH O 6 .   ? -6.799  22.072  10.509 1.00 46.61  ? 307 HOH B O   1 
HETATM 2068 O  O   . HOH O 6 .   ? -28.428 17.233  9.879  1.00 44.11  ? 308 HOH B O   1 
HETATM 2069 O  O   . HOH O 6 .   ? -15.406 12.498  -2.686 1.00 39.15  ? 309 HOH B O   1 
HETATM 2070 O  O   . HOH O 6 .   ? -6.044  18.638  7.625  1.00 66.83  ? 310 HOH B O   1 
HETATM 2071 O  O   . HOH O 6 .   ? -1.399  -3.695  21.500 1.00 25.92  ? 311 HOH B O   1 
HETATM 2072 O  O   . HOH O 6 .   ? -7.911  2.224   -1.465 1.00 48.41  ? 312 HOH B O   1 
HETATM 2073 O  O   . HOH O 6 .   ? -27.165 15.141  11.943 1.00 38.17  ? 313 HOH B O   1 
HETATM 2074 O  O   . HOH O 6 .   ? -19.559 0.993   23.156 1.00 44.50  ? 314 HOH B O   1 
HETATM 2075 O  O   . HOH O 6 .   ? 8.136   -0.570  11.151 1.00 60.08  ? 315 HOH B O   1 
HETATM 2076 O  O   . HOH O 6 .   ? -13.786 14.987  3.389  1.00 47.93  ? 316 HOH B O   1 
HETATM 2077 O  O   . HOH O 6 .   ? -31.074 1.186   16.326 1.00 48.80  ? 317 HOH B O   1 
HETATM 2078 O  O   . HOH O 6 .   ? -20.108 -10.304 15.463 1.00 48.72  ? 318 HOH B O   1 
HETATM 2079 O  O   . HOH O 6 .   ? -4.474  -5.660  13.075 1.00 49.86  ? 319 HOH B O   1 
HETATM 2080 O  O   . HOH O 6 .   ? -13.348 13.537  -0.784 1.00 33.47  ? 320 HOH B O   1 
HETATM 2081 O  O   . HOH O 6 .   ? -26.056 1.390   5.047  1.00 39.11  ? 321 HOH B O   1 
HETATM 2082 O  O   . HOH O 6 .   ? -22.166 -4.078  18.395 1.00 44.27  ? 322 HOH B O   1 
HETATM 2083 O  O   . HOH O 6 .   ? -16.065 7.707   -7.347 1.00 48.37  ? 323 HOH B O   1 
HETATM 2084 O  O   . HOH O 6 .   ? -28.901 2.662   11.844 1.00 50.08  ? 324 HOH B O   1 
HETATM 2085 O  O   . HOH O 6 .   ? 7.987   13.299  12.540 1.00 30.56  ? 325 HOH B O   1 
HETATM 2086 O  O   . HOH O 6 .   ? -26.295 10.620  7.523  1.00 36.25  ? 326 HOH B O   1 
HETATM 2087 O  O   . HOH O 6 .   ? -11.087 6.717   19.931 1.00 29.51  ? 327 HOH B O   1 
HETATM 2088 O  O   . HOH O 6 .   ? -28.556 9.458   18.139 1.00 46.84  ? 328 HOH B O   1 
HETATM 2089 O  O   . HOH O 6 .   ? 11.997  11.241  9.470  1.00 39.77  ? 329 HOH B O   1 
HETATM 2090 O  O   . HOH O 6 .   ? -13.806 16.207  -1.957 1.00 49.92  ? 330 HOH B O   1 
HETATM 2091 O  O   . HOH O 6 .   ? -33.333 -2.820  18.272 1.00 46.95  ? 331 HOH B O   1 
HETATM 2092 O  O   . HOH O 6 .   ? 0.952   -1.005  12.760 1.00 28.56  ? 332 HOH B O   1 
HETATM 2093 O  O   . HOH O 6 .   ? -16.531 8.506   2.840  1.00 27.97  ? 333 HOH B O   1 
HETATM 2094 O  O   . HOH O 6 .   ? -24.921 7.107   2.895  1.00 41.43  ? 334 HOH B O   1 
HETATM 2095 O  O   . HOH O 6 .   ? -9.370  7.282   26.354 1.00 36.29  ? 335 HOH B O   1 
HETATM 2096 O  O   . HOH O 6 .   ? -20.118 17.673  3.534  1.00 42.97  ? 336 HOH B O   1 
HETATM 2097 O  O   . HOH O 6 .   ? -30.363 -6.482  14.596 1.00 41.96  ? 337 HOH B O   1 
HETATM 2098 O  O   . HOH O 6 .   ? -3.458  0.801   29.199 1.00 26.60  ? 338 HOH B O   1 
HETATM 2099 O  O   . HOH O 6 .   ? -10.269 18.344  20.516 1.00 54.06  ? 339 HOH B O   1 
HETATM 2100 O  O   . HOH O 6 .   ? -21.654 -0.977  22.021 1.00 48.19  ? 340 HOH B O   1 
HETATM 2101 O  O   . HOH O 6 .   ? -0.746  -4.852  10.895 1.00 52.34  ? 341 HOH B O   1 
HETATM 2102 O  O   . HOH O 6 .   ? -31.147 -3.582  14.531 1.00 43.77  ? 342 HOH B O   1 
HETATM 2103 O  O   . HOH O 6 .   ? -0.231  14.075  14.575 1.00 32.51  ? 343 HOH B O   1 
HETATM 2104 O  O   . HOH O 6 .   ? -15.745 19.127  2.961  1.00 48.86  ? 344 HOH B O   1 
HETATM 2105 O  O   . HOH O 6 .   ? -17.005 11.907  20.699 1.00 34.40  ? 345 HOH B O   1 
HETATM 2106 O  O   . HOH O 6 .   ? -8.163  12.016  5.046  1.00 32.12  ? 346 HOH B O   1 
HETATM 2107 O  O   . HOH O 6 .   ? -7.967  4.760   28.373 1.00 28.84  ? 347 HOH B O   1 
HETATM 2108 O  O   . HOH O 6 .   ? -5.338  2.335   0.209  1.00 52.35  ? 348 HOH B O   1 
HETATM 2109 O  O   . HOH O 6 .   ? -27.600 -4.978  8.888  1.00 41.56  ? 349 HOH B O   1 
HETATM 2110 O  O   . HOH O 6 .   ? -33.497 -6.775  16.150 1.00 42.04  ? 350 HOH B O   1 
HETATM 2111 O  O   . HOH O 6 .   ? -26.490 1.025   18.584 1.00 32.19  ? 351 HOH B O   1 
HETATM 2112 O  O   . HOH O 6 .   ? -0.940  -1.914  25.587 1.00 27.72  ? 352 HOH B O   1 
HETATM 2113 O  O   . HOH O 6 .   ? -10.029 20.016  17.966 1.00 37.43  ? 353 HOH B O   1 
HETATM 2114 O  O   . HOH O 6 .   ? -13.580 -6.284  19.826 1.00 35.62  ? 354 HOH B O   1 
HETATM 2115 O  O   . HOH O 6 .   ? -19.306 3.861   -1.904 1.00 49.96  ? 355 HOH B O   1 
HETATM 2116 O  O   . HOH O 6 .   ? -3.082  -0.691  27.037 1.00 31.92  ? 356 HOH B O   1 
HETATM 2117 O  O   . HOH O 6 .   ? 11.242  2.918   9.133  1.00 51.73  ? 357 HOH B O   1 
HETATM 2118 O  O   . HOH O 6 .   ? -25.420 12.453  3.782  1.00 45.36  ? 358 HOH B O   1 
HETATM 2119 O  O   . HOH O 6 .   ? -29.661 -0.306  23.390 1.00 37.47  ? 359 HOH B O   1 
HETATM 2120 O  O   . HOH O 6 .   ? 7.620   -1.090  13.715 1.00 54.55  ? 360 HOH B O   1 
HETATM 2121 O  O   . HOH O 6 .   ? -0.421  16.595  14.321 1.00 36.43  ? 361 HOH B O   1 
HETATM 2122 O  O   . HOH O 6 .   ? 5.492   -3.492  14.634 1.00 49.36  ? 362 HOH B O   1 
HETATM 2123 O  O   . HOH O 6 .   ? -7.269  17.115  1.994  1.00 46.21  ? 363 HOH B O   1 
HETATM 2124 O  O   . HOH O 6 .   ? -3.879  12.012  25.996 1.00 38.58  ? 364 HOH B O   1 
HETATM 2125 O  O   . HOH O 6 .   ? -11.225 2.192   -2.290 1.00 44.75  ? 365 HOH B O   1 
HETATM 2126 O  O   . HOH O 6 .   ? -12.151 0.276   -1.562 1.00 54.87  ? 366 HOH B O   1 
HETATM 2127 O  O   . HOH O 6 .   ? -18.508 19.559  4.446  1.00 47.13  ? 367 HOH B O   1 
HETATM 2128 O  O   . HOH O 6 .   ? -28.198 1.354   16.294 1.00 50.58  ? 368 HOH B O   1 
HETATM 2129 O  O   . HOH O 6 .   ? 1.978   -3.160  12.340 1.00 56.63  ? 369 HOH B O   1 
HETATM 2130 O  O   . HOH O 6 .   ? -18.205 14.455  21.209 1.00 48.51  ? 370 HOH B O   1 
HETATM 2131 O  O   . HOH O 6 .   ? -28.448 3.716   14.293 1.00 52.35  ? 371 HOH B O   1 
# 
