data_9H9Y
# 
_entry.id   9H9Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9H9Y         pdb_00009h9y 10.2210/pdb9h9y/pdb 
WWPDB D_1292142898 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-05-07 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.title'                   
3 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H9Y 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-01 
_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                 2 
_pdbx_contact_author.email              g.roelfes@rug.nl 
_pdbx_contact_author.name_first         Gerard 
_pdbx_contact_author.name_last          Roelfes 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0364-9564 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Thunnissen, A.M.W.H.' 1 ? 
'Jiang, R.'            2 ? 
'Casilli, F.'          3 ? 
'Aalbers, F.'          4 ? 
'Roelfes, G.'          5 ? 
# 
_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                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Angew.Chem.Int.Ed.Engl. 
_citation.journal_id_ASTM           ACIEAY 
_citation.journal_id_CSD            0179 
_citation.journal_id_ISSN           1521-3773 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            64 
_citation.language                  ? 
_citation.page_first                e202423182 
_citation.page_last                 e202423182 
_citation.title                     
'An Artificial Copper-Michaelase Featuring a Genetically Encoded Bipyridine Ligand for Asymmetric Additions to Nitroalkenes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202423182 
_citation.pdbx_database_id_PubMed   39945539 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Jiang, R.'          1 0000-0003-3825-0534 
primary 'Casilli, F.'        2 0009-0007-2699-5439 
primary 'Thunnissen, A.W.H.' 3 0000-0002-1915-9850 
primary 'Roelfes, G.'        4 0000-0002-0364-9564 
# 
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 'Transcriptional regulator, PadR-like family' 15100.005 1  ? 
;Val15 replaced by (2,2'-bipyridin-5-yl)alanine, A92V, F93S
;
? 
;LmrR with residue Val15 replaced by (2,2'-bipyridin-5-yl)alanine, carrying a C-terminal strep-tag and with evolved mutations A92V, F93S
;
2 water   nat water                                         18.015    44 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;GAEIPKEMLRAQTN(BP5)ILLNVLKQGDNYVYGIIKQVKEASNGEMELNEATLYTIFKRLEKDGIISSYWGDESQGGRR
KYYRLTEIGHENMRLVSESWSRVDKIIENLEANKKSEAIKSRGGSGGWSHPQFEK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAEIPKEMLRAQTNXILLNVLKQGDNYVYGIIKQVKEASNGEMELNEATLYTIFKRLEKDGIISSYWGDESQGGRRKYYR
LTEIGHENMRLVSESWSRVDKIIENLEANKKSEAIKSRGGSGGWSHPQFEK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   GLU n 
1 4   ILE n 
1 5   PRO n 
1 6   LYS n 
1 7   GLU n 
1 8   MET n 
1 9   LEU n 
1 10  ARG n 
1 11  ALA n 
1 12  GLN n 
1 13  THR n 
1 14  ASN n 
1 15  BP5 n 
1 16  ILE n 
1 17  LEU n 
1 18  LEU n 
1 19  ASN n 
1 20  VAL n 
1 21  LEU n 
1 22  LYS n 
1 23  GLN n 
1 24  GLY n 
1 25  ASP n 
1 26  ASN n 
1 27  TYR n 
1 28  VAL n 
1 29  TYR n 
1 30  GLY n 
1 31  ILE n 
1 32  ILE n 
1 33  LYS n 
1 34  GLN n 
1 35  VAL n 
1 36  LYS n 
1 37  GLU n 
1 38  ALA n 
1 39  SER n 
1 40  ASN n 
1 41  GLY n 
1 42  GLU n 
1 43  MET n 
1 44  GLU n 
1 45  LEU n 
1 46  ASN n 
1 47  GLU n 
1 48  ALA n 
1 49  THR n 
1 50  LEU n 
1 51  TYR n 
1 52  THR n 
1 53  ILE n 
1 54  PHE n 
1 55  LYS n 
1 56  ARG n 
1 57  LEU n 
1 58  GLU n 
1 59  LYS n 
1 60  ASP n 
1 61  GLY n 
1 62  ILE n 
1 63  ILE n 
1 64  SER n 
1 65  SER n 
1 66  TYR n 
1 67  TRP n 
1 68  GLY n 
1 69  ASP n 
1 70  GLU n 
1 71  SER n 
1 72  GLN n 
1 73  GLY n 
1 74  GLY n 
1 75  ARG n 
1 76  ARG n 
1 77  LYS n 
1 78  TYR n 
1 79  TYR n 
1 80  ARG n 
1 81  LEU n 
1 82  THR n 
1 83  GLU n 
1 84  ILE n 
1 85  GLY n 
1 86  HIS n 
1 87  GLU n 
1 88  ASN n 
1 89  MET n 
1 90  ARG n 
1 91  LEU n 
1 92  VAL n 
1 93  SER n 
1 94  GLU n 
1 95  SER n 
1 96  TRP n 
1 97  SER n 
1 98  ARG n 
1 99  VAL n 
1 100 ASP n 
1 101 LYS n 
1 102 ILE n 
1 103 ILE n 
1 104 GLU n 
1 105 ASN n 
1 106 LEU n 
1 107 GLU n 
1 108 ALA n 
1 109 ASN n 
1 110 LYS n 
1 111 LYS n 
1 112 SER n 
1 113 GLU n 
1 114 ALA n 
1 115 ILE n 
1 116 LYS n 
1 117 SER n 
1 118 ARG n 
1 119 GLY n 
1 120 GLY n 
1 121 SER n 
1 122 GLY n 
1 123 GLY n 
1 124 TRP n 
1 125 SER n 
1 126 HIS n 
1 127 PRO n 
1 128 GLN n 
1 129 PHE n 
1 130 GLU n 
1 131 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   131 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 llmg_0323 
_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      'Lactococcus cremoris subsp. cremoris MG1363' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     416870 
_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 
BP5 'L-peptide linking' n "3-(2,2'-BIPYRIDIN-5-YL)-L-ALANINE" ? 'C13 H13 N3 O2'  243.261 
GLN 'L-peptide linking' y GLUTAMINE                           ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                     ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                             ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                           ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                               ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                          ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                             ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                              ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                          ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                       ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                             ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                              ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                           ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                          ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                            ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                              ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   PRO 5   5   5   PRO PRO A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   MET 8   8   8   MET MET A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  BP5 15  15  15  BP5 DRG A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  GLN 23  23  23  GLN GLN A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  GLN 34  34  34  GLN GLN A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  MET 43  43  43  MET MET 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  ASN 46  46  46  ASN ASN A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  TYR 66  66  66  TYR TYR A . n 
A 1 67  TRP 67  67  67  TRP TRP A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  GLU 70  70  ?   ?   ?   A . n 
A 1 71  SER 71  71  ?   ?   ?   A . n 
A 1 72  GLN 72  72  ?   ?   ?   A . n 
A 1 73  GLY 73  73  ?   ?   ?   A . n 
A 1 74  GLY 74  74  ?   ?   ?   A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  MET 89  89  89  MET MET A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  TRP 96  96  96  TRP TRP A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 ALA 108 108 ?   ?   ?   A . n 
A 1 109 ASN 109 109 ?   ?   ?   A . n 
A 1 110 LYS 110 110 ?   ?   ?   A . n 
A 1 111 LYS 111 111 ?   ?   ?   A . n 
A 1 112 SER 112 112 ?   ?   ?   A . n 
A 1 113 GLU 113 113 ?   ?   ?   A . n 
A 1 114 ALA 114 114 ?   ?   ?   A . n 
A 1 115 ILE 115 115 ?   ?   ?   A . n 
A 1 116 LYS 116 116 ?   ?   ?   A . n 
A 1 117 SER 117 117 ?   ?   ?   A . n 
A 1 118 ARG 118 118 ?   ?   ?   A . n 
A 1 119 GLY 119 119 ?   ?   ?   A . n 
A 1 120 GLY 120 120 ?   ?   ?   A . n 
A 1 121 SER 121 121 ?   ?   ?   A . n 
A 1 122 GLY 122 122 ?   ?   ?   A . n 
A 1 123 GLY 123 123 ?   ?   ?   A . n 
A 1 124 TRP 124 124 ?   ?   ?   A . n 
A 1 125 SER 125 125 ?   ?   ?   A . n 
A 1 126 HIS 126 126 ?   ?   ?   A . n 
A 1 127 PRO 127 127 ?   ?   ?   A . n 
A 1 128 GLN 128 128 ?   ?   ?   A . n 
A 1 129 PHE 129 129 ?   ?   ?   A . n 
A 1 130 GLU 130 130 ?   ?   ?   A . n 
A 1 131 LYS 131 131 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        BP5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   BP5 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1  201 26 HOH HOH A . 
B 2 HOH 2  202 37 HOH HOH A . 
B 2 HOH 3  203 21 HOH HOH A . 
B 2 HOH 4  204 32 HOH HOH A . 
B 2 HOH 5  205 22 HOH HOH A . 
B 2 HOH 6  206 5  HOH HOH A . 
B 2 HOH 7  207 11 HOH HOH A . 
B 2 HOH 8  208 29 HOH HOH A . 
B 2 HOH 9  209 6  HOH HOH A . 
B 2 HOH 10 210 30 HOH HOH A . 
B 2 HOH 11 211 1  HOH HOH A . 
B 2 HOH 12 212 13 HOH HOH A . 
B 2 HOH 13 213 41 HOH HOH A . 
B 2 HOH 14 214 3  HOH HOH A . 
B 2 HOH 15 215 20 HOH HOH A . 
B 2 HOH 16 216 8  HOH HOH A . 
B 2 HOH 17 217 44 HOH HOH A . 
B 2 HOH 18 218 4  HOH HOH A . 
B 2 HOH 19 219 7  HOH HOH A . 
B 2 HOH 20 220 31 HOH HOH A . 
B 2 HOH 21 221 18 HOH HOH A . 
B 2 HOH 22 222 2  HOH HOH A . 
B 2 HOH 23 223 36 HOH HOH A . 
B 2 HOH 24 224 34 HOH HOH A . 
B 2 HOH 25 225 28 HOH HOH A . 
B 2 HOH 26 226 25 HOH HOH A . 
B 2 HOH 27 227 19 HOH HOH A . 
B 2 HOH 28 228 14 HOH HOH A . 
B 2 HOH 29 229 16 HOH HOH A . 
B 2 HOH 30 230 9  HOH HOH A . 
B 2 HOH 31 231 12 HOH HOH A . 
B 2 HOH 32 232 23 HOH HOH A . 
B 2 HOH 33 233 40 HOH HOH A . 
B 2 HOH 34 234 33 HOH HOH A . 
B 2 HOH 35 235 27 HOH HOH A . 
B 2 HOH 36 236 39 HOH HOH A . 
B 2 HOH 37 237 15 HOH HOH A . 
B 2 HOH 38 238 17 HOH HOH A . 
B 2 HOH 39 239 38 HOH HOH A . 
B 2 HOH 40 240 10 HOH HOH A . 
B 2 HOH 41 241 24 HOH HOH A . 
B 2 HOH 42 242 43 HOH HOH A . 
B 2 HOH 43 243 42 HOH HOH A . 
B 2 HOH 44 244 35 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425    4 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.21.1_5286 5 
# 
_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                     9H9Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     35.039 
_cell.length_a_esd                 ? 
_cell.length_b                     35.039 
_cell.length_b_esd                 ? 
_cell.length_c                     166.834 
_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                         9H9Y 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_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                   9H9Y 
_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             1.70 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          27.46 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_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    'sodium nitrate, Bis-Tris propane, PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.96546 
_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 MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.96546 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H9Y 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               34.29 
_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                                     17381 
_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                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                23.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.98 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.064 
_reflns.pdbx_Rpim_I_all                                0.013 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       414448 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.063 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.50 
_reflns_shell.d_res_low                                     1.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           17282 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             813 
_reflns_shell.percent_possible_obs                          95.5 
_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                               21.3 
_reflns_shell.pdbx_chi_squared                              0.95 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               3.256 
_reflns_shell.pdbx_Rpim_I_all                               0.692 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.524 
_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                                  3.178 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9H9Y 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.50 
_refine.ls_d_res_low                             34.29 
_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                     17337 
_refine.ls_number_reflns_R_free                  896 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.98 
_refine.ls_percent_reflns_R_free                 5.17 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2113 
_refine.ls_R_factor_R_free                       0.2823 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2080 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 30.13 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.18 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        839 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             44 
_refine_hist.number_atoms_total               883 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        34.29 
# 
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' ? 0.010  ? 881  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.983  ? 1188 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.099 ? 345  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046  ? 126  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 150  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.50 1.59  . . 152 2611 96.00  . . . . 0.2921 . . . . . . . . . . . 0.2969 
'X-RAY DIFFRACTION' 1.59 1.72  . . 155 2606 97.00  . . . . 0.2682 . . . . . . . . . . . 0.3278 
'X-RAY DIFFRACTION' 1.72 1.89  . . 155 2674 98.00  . . . . 0.2456 . . . . . . . . . . . 0.2482 
'X-RAY DIFFRACTION' 1.89 2.16  . . 151 2734 98.00  . . . . 0.2157 . . . . . . . . . . . 0.3179 
'X-RAY DIFFRACTION' 2.16 2.73  . . 144 2787 99.00  . . . . 0.2155 . . . . . . . . . . . 0.2567 
'X-RAY DIFFRACTION' 2.73 34.29 . . 139 3029 100.00 . . . . 0.1946 . . . . . . . . . . . 0.2842 
# 
_struct.entry_id                     9H9Y 
_struct.title                        'Crystal structure of metal-free LmrR_V15Bpy variant BVS in a closed state' 
_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        9H9Y 
_struct_keywords.text            
'artificial metalloenzyme, unnatural amino acid, bipyridine, copper-binding, LmrR, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A2RI36_LACLM 
_struct_ref.pdbx_db_accession          A2RI36 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AEIPKEMLRAQTNVILLNVLKQGDNYVYGIIKQVKEASNGEMELNEATLYTIFKRLEKDGIISSYWGDESQGGRRKYYRL
TEIGHENMRLAFESWSRVDKIIENLEANKKSEAIK
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9H9Y 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 116 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A2RI36 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  116 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       116 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9H9Y GLY A 1   ? UNP A2RI36 ?   ?  'expression tag'      1   1  
1 9H9Y BP5 A 15  ? UNP A2RI36 VAL 15 'engineered mutation' 15  2  
1 9H9Y VAL A 92  ? UNP A2RI36 ALA 92 'engineered mutation' 92  3  
1 9H9Y SER A 93  ? UNP A2RI36 PHE 93 'engineered mutation' 93  4  
1 9H9Y SER A 117 ? UNP A2RI36 ?   ?  'expression tag'      117 5  
1 9H9Y ARG A 118 ? UNP A2RI36 ?   ?  'expression tag'      118 6  
1 9H9Y GLY A 119 ? UNP A2RI36 ?   ?  'expression tag'      119 7  
1 9H9Y GLY A 120 ? UNP A2RI36 ?   ?  'expression tag'      120 8  
1 9H9Y SER A 121 ? UNP A2RI36 ?   ?  'expression tag'      121 9  
1 9H9Y GLY A 122 ? UNP A2RI36 ?   ?  'expression tag'      122 10 
1 9H9Y GLY A 123 ? UNP A2RI36 ?   ?  'expression tag'      123 11 
1 9H9Y TRP A 124 ? UNP A2RI36 ?   ?  'expression tag'      124 12 
1 9H9Y SER A 125 ? UNP A2RI36 ?   ?  'expression tag'      125 13 
1 9H9Y HIS A 126 ? UNP A2RI36 ?   ?  'expression tag'      126 14 
1 9H9Y PRO A 127 ? UNP A2RI36 ?   ?  'expression tag'      127 15 
1 9H9Y GLN A 128 ? UNP A2RI36 ?   ?  'expression tag'      128 16 
1 9H9Y PHE A 129 ? UNP A2RI36 ?   ?  'expression tag'      129 17 
1 9H9Y GLU A 130 ? UNP A2RI36 ?   ?  'expression tag'      130 18 
1 9H9Y LYS A 131 ? UNP A2RI36 ?   ?  'expression tag'      131 19 
# 
_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)' 4630  ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  10680 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z      1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 7_645 y+1,x-1,-z 0.0000000000 1.0000000000 0.0000000000 35.0390000000 1.0000000000 0.0000000000 
0.0000000000 -35.0390000000 0.0000000000 0.0000000000 -1.0000000000 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 PRO A 5  ? GLY A 24  ? PRO A 5  GLY A 24  1 ? 20 
HELX_P HELX_P2 AA2 VAL A 28 ? SER A 39  ? VAL A 28 SER A 39  1 ? 12 
HELX_P HELX_P3 AA3 ASN A 46 ? ASP A 60  ? ASN A 46 ASP A 60  1 ? 15 
HELX_P HELX_P4 AA4 THR A 82 ? GLU A 107 ? THR A 82 GLU A 107 1 ? 26 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A ASN 14 C ? ? ? 1_555 A BP5 15 N ? ? A ASN 14 A BP5 15 1_555 ? ? ? ? ? ? ? 1.320 ? ? 
covale2 covale both ? A BP5 15 C ? ? ? 1_555 A ILE 16 N ? ? A BP5 15 A ILE 16 1_555 ? ? ? ? ? ? ? 1.325 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      BP5 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       15 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       BP5 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        15 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                ? 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        BP5 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Non-standard residue' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_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 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASN A 26 ? TYR A 27 ? ASN A 26 TYR A 27 
AA1 2 LYS A 77 ? LEU A 81 ? LYS A 77 LEU A 81 
AA1 3 ILE A 63 ? TRP A 67 ? ILE A 63 TRP A 67 
# 
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 ASN A 26 ? N ASN A 26 O TYR A 79 ? O TYR A 79 
AA1 2 3 O TYR A 78 ? O TYR A 78 N TYR A 66 ? N TYR A 66 
# 
_pdbx_entry_details.entry_id                   9H9Y 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 19.5160 -15.0186 -6.5798  0.3085 ? 0.0177  ? -0.0672 ? 0.3560 ? -0.0033 ? 0.3181 ? 0.3778  ? 
0.2523  ? 0.4861 ? 0.0210 ? 0.2389  ? 0.5002 ? -0.0508 ? -0.0493 ? -0.1126 ? 0.0477  ? 0.2438  ? 0.0454  ? 0.2784  ? -0.0525 ? 
-0.0005 ? 
2 'X-RAY DIFFRACTION' ? refined 23.9391 -13.6209 -18.2672 0.2279 ? 0.0020  ? -0.0124 ? 0.3742 ? 0.0226  ? 0.4002 ? 0.3634  ? 
0.4902  ? 0.2474 ? 0.5579 ? 0.4394  ? 0.6440 ? -0.1157 ? 0.4563  ? -0.2524 ? -0.3192 ? 0.0690  ? -0.2651 ? -0.1305 ? 0.4775  ? 
0.0004  ? 
3 'X-RAY DIFFRACTION' ? refined 10.7665 -18.1388 -14.4870 0.2531 ? -0.0126 ? -0.0326 ? 0.2953 ? -0.0091 ? 0.3248 ? 0.1152  ? 
0.0393  ? 0.0498 ? 0.1475 ? 0.0672  ? 0.1395 ? -0.0997 ? 0.1285  ? -0.0916 ? -0.1436 ? 0.1443  ? 0.2599  ? 0.1068  ? 0.2015  ? 
0.0003  ? 
4 'X-RAY DIFFRACTION' ? refined 8.5234  -9.4915  -21.2576 0.2900 ? 0.0118  ? -0.0842 ? 0.3077 ? -0.0167 ? 0.3173 ? 0.2556  ? 
-0.4784 ? 0.3345 ? 0.4440 ? 0.0179  ? 0.2276 ? -0.0296 ? 0.0407  ? -0.0729 ? -0.1057 ? 0.0541  ? 0.1541  ? 0.0320  ? 0.2747  ? 
0.0001  ? 
5 'X-RAY DIFFRACTION' ? refined 18.7055 -5.4757  1.1705   0.4005 ? 0.0200  ? -0.0296 ? 0.3879 ? 0.0232  ? 0.3700 ? -0.0057 ? 
0.3154  ? 0.8192 ? 0.2673 ? -0.2729 ? 0.1281 ? -0.2301 ? -0.1982 ? 0.6556  ? 0.0881  ? -0.1941 ? -0.1096 ? -0.3252 ? -0.3547 ? 
0.0002  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 23 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 24 through 46 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 47 through 59 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 60 through 82 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 83 through 107 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 1   ? A GLY 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A GLU 70  ? A GLU 70  
4  1 Y 1 A SER 71  ? A SER 71  
5  1 Y 1 A GLN 72  ? A GLN 72  
6  1 Y 1 A GLY 73  ? A GLY 73  
7  1 Y 1 A GLY 74  ? A GLY 74  
8  1 Y 1 A ALA 108 ? A ALA 108 
9  1 Y 1 A ASN 109 ? A ASN 109 
10 1 Y 1 A LYS 110 ? A LYS 110 
11 1 Y 1 A LYS 111 ? A LYS 111 
12 1 Y 1 A SER 112 ? A SER 112 
13 1 Y 1 A GLU 113 ? A GLU 113 
14 1 Y 1 A ALA 114 ? A ALA 114 
15 1 Y 1 A ILE 115 ? A ILE 115 
16 1 Y 1 A LYS 116 ? A LYS 116 
17 1 Y 1 A SER 117 ? A SER 117 
18 1 Y 1 A ARG 118 ? A ARG 118 
19 1 Y 1 A GLY 119 ? A GLY 119 
20 1 Y 1 A GLY 120 ? A GLY 120 
21 1 Y 1 A SER 121 ? A SER 121 
22 1 Y 1 A GLY 122 ? A GLY 122 
23 1 Y 1 A GLY 123 ? A GLY 123 
24 1 Y 1 A TRP 124 ? A TRP 124 
25 1 Y 1 A SER 125 ? A SER 125 
26 1 Y 1 A HIS 126 ? A HIS 126 
27 1 Y 1 A PRO 127 ? A PRO 127 
28 1 Y 1 A GLN 128 ? A GLN 128 
29 1 Y 1 A PHE 129 ? A PHE 129 
30 1 Y 1 A GLU 130 ? A GLU 130 
31 1 Y 1 A LYS 131 ? A LYS 131 
# 
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  
BP5 C9   C Y N 74  
BP5 C8   C Y N 75  
BP5 C7   C Y N 76  
BP5 C6   C Y N 77  
BP5 C5   C Y N 78  
BP5 C4   C Y N 79  
BP5 C3   C Y N 80  
BP5 C2   C Y N 81  
BP5 C1   C Y N 82  
BP5 C12  C N N 83  
BP5 C11  C Y N 84  
BP5 N1   N Y N 85  
BP5 N2   N Y N 86  
BP5 CA   C N S 87  
BP5 C    C N N 88  
BP5 OXT  O N N 89  
BP5 O    O N N 90  
BP5 N    N N N 91  
BP5 H8   H N N 92  
BP5 H7   H N N 93  
BP5 H5   H N N 94  
BP5 H4   H N N 95  
BP5 H3   H N N 96  
BP5 H1   H N N 97  
BP5 H121 H N N 98  
BP5 H122 H N N 99  
BP5 H11  H N N 100 
BP5 HA   H N N 101 
BP5 HXT  H N N 102 
BP5 H    H N N 103 
BP5 H2   H N N 104 
GLN N    N N N 105 
GLN CA   C N S 106 
GLN C    C N N 107 
GLN O    O N N 108 
GLN CB   C N N 109 
GLN CG   C N N 110 
GLN CD   C N N 111 
GLN OE1  O N N 112 
GLN NE2  N N N 113 
GLN OXT  O N N 114 
GLN H    H N N 115 
GLN H2   H N N 116 
GLN HA   H N N 117 
GLN HB2  H N N 118 
GLN HB3  H N N 119 
GLN HG2  H N N 120 
GLN HG3  H N N 121 
GLN HE21 H N N 122 
GLN HE22 H N N 123 
GLN HXT  H N N 124 
GLU N    N N N 125 
GLU CA   C N S 126 
GLU C    C N N 127 
GLU O    O N N 128 
GLU CB   C N N 129 
GLU CG   C N N 130 
GLU CD   C N N 131 
GLU OE1  O N N 132 
GLU OE2  O N N 133 
GLU OXT  O N N 134 
GLU H    H N N 135 
GLU H2   H N N 136 
GLU HA   H N N 137 
GLU HB2  H N N 138 
GLU HB3  H N N 139 
GLU HG2  H N N 140 
GLU HG3  H N N 141 
GLU HE2  H N N 142 
GLU HXT  H N N 143 
GLY N    N N N 144 
GLY CA   C N N 145 
GLY C    C N N 146 
GLY O    O N N 147 
GLY OXT  O N N 148 
GLY H    H N N 149 
GLY H2   H N N 150 
GLY HA2  H N N 151 
GLY HA3  H N N 152 
GLY HXT  H N N 153 
HIS N    N N N 154 
HIS CA   C N S 155 
HIS C    C N N 156 
HIS O    O N N 157 
HIS CB   C N N 158 
HIS CG   C Y N 159 
HIS ND1  N Y N 160 
HIS CD2  C Y N 161 
HIS CE1  C Y N 162 
HIS NE2  N Y N 163 
HIS OXT  O N N 164 
HIS H    H N N 165 
HIS H2   H N N 166 
HIS HA   H N N 167 
HIS HB2  H N N 168 
HIS HB3  H N N 169 
HIS HD1  H N N 170 
HIS HD2  H N N 171 
HIS HE1  H N N 172 
HIS HE2  H N N 173 
HIS HXT  H N N 174 
HOH O    O N N 175 
HOH H1   H N N 176 
HOH H2   H N N 177 
ILE N    N N N 178 
ILE CA   C N S 179 
ILE C    C N N 180 
ILE O    O N N 181 
ILE CB   C N S 182 
ILE CG1  C N N 183 
ILE CG2  C N N 184 
ILE CD1  C N N 185 
ILE OXT  O N N 186 
ILE H    H N N 187 
ILE H2   H N N 188 
ILE HA   H N N 189 
ILE HB   H N N 190 
ILE HG12 H N N 191 
ILE HG13 H N N 192 
ILE HG21 H N N 193 
ILE HG22 H N N 194 
ILE HG23 H N N 195 
ILE HD11 H N N 196 
ILE HD12 H N N 197 
ILE HD13 H N N 198 
ILE HXT  H N N 199 
LEU N    N N N 200 
LEU CA   C N S 201 
LEU C    C N N 202 
LEU O    O N N 203 
LEU CB   C N N 204 
LEU CG   C N N 205 
LEU CD1  C N N 206 
LEU CD2  C N N 207 
LEU OXT  O N N 208 
LEU H    H N N 209 
LEU H2   H N N 210 
LEU HA   H N N 211 
LEU HB2  H N N 212 
LEU HB3  H N N 213 
LEU HG   H N N 214 
LEU HD11 H N N 215 
LEU HD12 H N N 216 
LEU HD13 H N N 217 
LEU HD21 H N N 218 
LEU HD22 H N N 219 
LEU HD23 H N N 220 
LEU HXT  H N N 221 
LYS N    N N N 222 
LYS CA   C N S 223 
LYS C    C N N 224 
LYS O    O N N 225 
LYS CB   C N N 226 
LYS CG   C N N 227 
LYS CD   C N N 228 
LYS CE   C N N 229 
LYS NZ   N N N 230 
LYS OXT  O N N 231 
LYS H    H N N 232 
LYS H2   H N N 233 
LYS HA   H N N 234 
LYS HB2  H N N 235 
LYS HB3  H N N 236 
LYS HG2  H N N 237 
LYS HG3  H N N 238 
LYS HD2  H N N 239 
LYS HD3  H N N 240 
LYS HE2  H N N 241 
LYS HE3  H N N 242 
LYS HZ1  H N N 243 
LYS HZ2  H N N 244 
LYS HZ3  H N N 245 
LYS HXT  H N N 246 
MET N    N N N 247 
MET CA   C N S 248 
MET C    C N N 249 
MET O    O N N 250 
MET CB   C N N 251 
MET CG   C N N 252 
MET SD   S N N 253 
MET CE   C N N 254 
MET OXT  O N N 255 
MET H    H N N 256 
MET H2   H N N 257 
MET HA   H N N 258 
MET HB2  H N N 259 
MET HB3  H N N 260 
MET HG2  H N N 261 
MET HG3  H N N 262 
MET HE1  H N N 263 
MET HE2  H N N 264 
MET HE3  H N N 265 
MET HXT  H N N 266 
PHE N    N N N 267 
PHE CA   C N S 268 
PHE C    C N N 269 
PHE O    O N N 270 
PHE CB   C N N 271 
PHE CG   C Y N 272 
PHE CD1  C Y N 273 
PHE CD2  C Y N 274 
PHE CE1  C Y N 275 
PHE CE2  C Y N 276 
PHE CZ   C Y N 277 
PHE OXT  O N N 278 
PHE H    H N N 279 
PHE H2   H N N 280 
PHE HA   H N N 281 
PHE HB2  H N N 282 
PHE HB3  H N N 283 
PHE HD1  H N N 284 
PHE HD2  H N N 285 
PHE HE1  H N N 286 
PHE HE2  H N N 287 
PHE HZ   H N N 288 
PHE HXT  H N N 289 
PRO N    N N N 290 
PRO CA   C N S 291 
PRO C    C N N 292 
PRO O    O N N 293 
PRO CB   C N N 294 
PRO CG   C N N 295 
PRO CD   C N N 296 
PRO OXT  O N N 297 
PRO H    H N N 298 
PRO HA   H N N 299 
PRO HB2  H N N 300 
PRO HB3  H N N 301 
PRO HG2  H N N 302 
PRO HG3  H N N 303 
PRO HD2  H N N 304 
PRO HD3  H N N 305 
PRO HXT  H N N 306 
SER N    N N N 307 
SER CA   C N S 308 
SER C    C N N 309 
SER O    O N N 310 
SER CB   C N N 311 
SER OG   O N N 312 
SER OXT  O N N 313 
SER H    H N N 314 
SER H2   H N N 315 
SER HA   H N N 316 
SER HB2  H N N 317 
SER HB3  H N N 318 
SER HG   H N N 319 
SER HXT  H N N 320 
THR N    N N N 321 
THR CA   C N S 322 
THR C    C N N 323 
THR O    O N N 324 
THR CB   C N R 325 
THR OG1  O N N 326 
THR CG2  C N N 327 
THR OXT  O N N 328 
THR H    H N N 329 
THR H2   H N N 330 
THR HA   H N N 331 
THR HB   H N N 332 
THR HG1  H N N 333 
THR HG21 H N N 334 
THR HG22 H N N 335 
THR HG23 H N N 336 
THR HXT  H N N 337 
TRP N    N N N 338 
TRP CA   C N S 339 
TRP C    C N N 340 
TRP O    O N N 341 
TRP CB   C N N 342 
TRP CG   C Y N 343 
TRP CD1  C Y N 344 
TRP CD2  C Y N 345 
TRP NE1  N Y N 346 
TRP CE2  C Y N 347 
TRP CE3  C Y N 348 
TRP CZ2  C Y N 349 
TRP CZ3  C Y N 350 
TRP CH2  C Y N 351 
TRP OXT  O N N 352 
TRP H    H N N 353 
TRP H2   H N N 354 
TRP HA   H N N 355 
TRP HB2  H N N 356 
TRP HB3  H N N 357 
TRP HD1  H N N 358 
TRP HE1  H N N 359 
TRP HE3  H N N 360 
TRP HZ2  H N N 361 
TRP HZ3  H N N 362 
TRP HH2  H N N 363 
TRP HXT  H N N 364 
TYR N    N N N 365 
TYR CA   C N S 366 
TYR C    C N N 367 
TYR O    O N N 368 
TYR CB   C N N 369 
TYR CG   C Y N 370 
TYR CD1  C Y N 371 
TYR CD2  C Y N 372 
TYR CE1  C Y N 373 
TYR CE2  C Y N 374 
TYR CZ   C Y N 375 
TYR OH   O N N 376 
TYR OXT  O N N 377 
TYR H    H N N 378 
TYR H2   H N N 379 
TYR HA   H N N 380 
TYR HB2  H N N 381 
TYR HB3  H N N 382 
TYR HD1  H N N 383 
TYR HD2  H N N 384 
TYR HE1  H N N 385 
TYR HE2  H N N 386 
TYR HH   H N N 387 
TYR HXT  H N N 388 
VAL N    N N N 389 
VAL CA   C N S 390 
VAL C    C N N 391 
VAL O    O N N 392 
VAL CB   C N N 393 
VAL CG1  C N N 394 
VAL CG2  C N N 395 
VAL OXT  O N N 396 
VAL H    H N N 397 
VAL H2   H N N 398 
VAL HA   H N N 399 
VAL HB   H N N 400 
VAL HG11 H N N 401 
VAL HG12 H N N 402 
VAL HG13 H N N 403 
VAL HG21 H N N 404 
VAL HG22 H N N 405 
VAL HG23 H N N 406 
VAL HXT  H N N 407 
# 
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  
BP5 C9  C12  sing N N 70  
BP5 C9  C8   doub Y N 71  
BP5 C9  C11  sing Y N 72  
BP5 C8  C7   sing Y N 73  
BP5 C8  H8   sing N N 74  
BP5 C7  C6   doub Y N 75  
BP5 C7  H7   sing N N 76  
BP5 C6  N2   sing Y N 77  
BP5 C6  C3   sing N N 78  
BP5 C5  C1   doub Y N 79  
BP5 C5  C4   sing Y N 80  
BP5 C5  H5   sing N N 81  
BP5 C4  N1   doub Y N 82  
BP5 C4  H4   sing N N 83  
BP5 C3  C2   doub Y N 84  
BP5 C3  N1   sing Y N 85  
BP5 C2  C1   sing Y N 86  
BP5 C2  H3   sing N N 87  
BP5 C1  H1   sing N N 88  
BP5 C12 CA   sing N N 89  
BP5 C12 H121 sing N N 90  
BP5 C12 H122 sing N N 91  
BP5 C11 N2   doub Y N 92  
BP5 C11 H11  sing N N 93  
BP5 CA  C    sing N N 94  
BP5 CA  N    sing N N 95  
BP5 CA  HA   sing N N 96  
BP5 C   O    doub N N 97  
BP5 C   OXT  sing N N 98  
BP5 OXT HXT  sing N N 99  
BP5 N   H    sing N N 100 
BP5 N   H2   sing N N 101 
GLN N   CA   sing N N 102 
GLN N   H    sing N N 103 
GLN N   H2   sing N N 104 
GLN CA  C    sing N N 105 
GLN CA  CB   sing N N 106 
GLN CA  HA   sing N N 107 
GLN C   O    doub N N 108 
GLN C   OXT  sing N N 109 
GLN CB  CG   sing N N 110 
GLN CB  HB2  sing N N 111 
GLN CB  HB3  sing N N 112 
GLN CG  CD   sing N N 113 
GLN CG  HG2  sing N N 114 
GLN CG  HG3  sing N N 115 
GLN CD  OE1  doub N N 116 
GLN CD  NE2  sing N N 117 
GLN NE2 HE21 sing N N 118 
GLN NE2 HE22 sing N N 119 
GLN OXT HXT  sing N N 120 
GLU N   CA   sing N N 121 
GLU N   H    sing N N 122 
GLU N   H2   sing N N 123 
GLU CA  C    sing N N 124 
GLU CA  CB   sing N N 125 
GLU CA  HA   sing N N 126 
GLU C   O    doub N N 127 
GLU C   OXT  sing N N 128 
GLU CB  CG   sing N N 129 
GLU CB  HB2  sing N N 130 
GLU CB  HB3  sing N N 131 
GLU CG  CD   sing N N 132 
GLU CG  HG2  sing N N 133 
GLU CG  HG3  sing N N 134 
GLU CD  OE1  doub N N 135 
GLU CD  OE2  sing N N 136 
GLU OE2 HE2  sing N N 137 
GLU OXT HXT  sing N N 138 
GLY N   CA   sing N N 139 
GLY N   H    sing N N 140 
GLY N   H2   sing N N 141 
GLY CA  C    sing N N 142 
GLY CA  HA2  sing N N 143 
GLY CA  HA3  sing N N 144 
GLY C   O    doub N N 145 
GLY C   OXT  sing N N 146 
GLY OXT HXT  sing N N 147 
HIS N   CA   sing N N 148 
HIS N   H    sing N N 149 
HIS N   H2   sing N N 150 
HIS CA  C    sing N N 151 
HIS CA  CB   sing N N 152 
HIS CA  HA   sing N N 153 
HIS C   O    doub N N 154 
HIS C   OXT  sing N N 155 
HIS CB  CG   sing N N 156 
HIS CB  HB2  sing N N 157 
HIS CB  HB3  sing N N 158 
HIS CG  ND1  sing Y N 159 
HIS CG  CD2  doub Y N 160 
HIS ND1 CE1  doub Y N 161 
HIS ND1 HD1  sing N N 162 
HIS CD2 NE2  sing Y N 163 
HIS CD2 HD2  sing N N 164 
HIS CE1 NE2  sing Y N 165 
HIS CE1 HE1  sing N N 166 
HIS NE2 HE2  sing N N 167 
HIS OXT HXT  sing N N 168 
HOH O   H1   sing N N 169 
HOH O   H2   sing N N 170 
ILE N   CA   sing N N 171 
ILE N   H    sing N N 172 
ILE N   H2   sing N N 173 
ILE CA  C    sing N N 174 
ILE CA  CB   sing N N 175 
ILE CA  HA   sing N N 176 
ILE C   O    doub N N 177 
ILE C   OXT  sing N N 178 
ILE CB  CG1  sing N N 179 
ILE CB  CG2  sing N N 180 
ILE CB  HB   sing N N 181 
ILE CG1 CD1  sing N N 182 
ILE CG1 HG12 sing N N 183 
ILE CG1 HG13 sing N N 184 
ILE CG2 HG21 sing N N 185 
ILE CG2 HG22 sing N N 186 
ILE CG2 HG23 sing N N 187 
ILE CD1 HD11 sing N N 188 
ILE CD1 HD12 sing N N 189 
ILE CD1 HD13 sing N N 190 
ILE OXT HXT  sing N N 191 
LEU N   CA   sing N N 192 
LEU N   H    sing N N 193 
LEU N   H2   sing N N 194 
LEU CA  C    sing N N 195 
LEU CA  CB   sing N N 196 
LEU CA  HA   sing N N 197 
LEU C   O    doub N N 198 
LEU C   OXT  sing N N 199 
LEU CB  CG   sing N N 200 
LEU CB  HB2  sing N N 201 
LEU CB  HB3  sing N N 202 
LEU CG  CD1  sing N N 203 
LEU CG  CD2  sing N N 204 
LEU CG  HG   sing N N 205 
LEU CD1 HD11 sing N N 206 
LEU CD1 HD12 sing N N 207 
LEU CD1 HD13 sing N N 208 
LEU CD2 HD21 sing N N 209 
LEU CD2 HD22 sing N N 210 
LEU CD2 HD23 sing N N 211 
LEU OXT HXT  sing N N 212 
LYS N   CA   sing N N 213 
LYS N   H    sing N N 214 
LYS N   H2   sing N N 215 
LYS CA  C    sing N N 216 
LYS CA  CB   sing N N 217 
LYS CA  HA   sing N N 218 
LYS C   O    doub N N 219 
LYS C   OXT  sing N N 220 
LYS CB  CG   sing N N 221 
LYS CB  HB2  sing N N 222 
LYS CB  HB3  sing N N 223 
LYS CG  CD   sing N N 224 
LYS CG  HG2  sing N N 225 
LYS CG  HG3  sing N N 226 
LYS CD  CE   sing N N 227 
LYS CD  HD2  sing N N 228 
LYS CD  HD3  sing N N 229 
LYS CE  NZ   sing N N 230 
LYS CE  HE2  sing N N 231 
LYS CE  HE3  sing N N 232 
LYS NZ  HZ1  sing N N 233 
LYS NZ  HZ2  sing N N 234 
LYS NZ  HZ3  sing N N 235 
LYS OXT HXT  sing N N 236 
MET N   CA   sing N N 237 
MET N   H    sing N N 238 
MET N   H2   sing N N 239 
MET CA  C    sing N N 240 
MET CA  CB   sing N N 241 
MET CA  HA   sing N N 242 
MET C   O    doub N N 243 
MET C   OXT  sing N N 244 
MET CB  CG   sing N N 245 
MET CB  HB2  sing N N 246 
MET CB  HB3  sing N N 247 
MET CG  SD   sing N N 248 
MET CG  HG2  sing N N 249 
MET CG  HG3  sing N N 250 
MET SD  CE   sing N N 251 
MET CE  HE1  sing N N 252 
MET CE  HE2  sing N N 253 
MET CE  HE3  sing N N 254 
MET OXT HXT  sing N N 255 
PHE N   CA   sing N N 256 
PHE N   H    sing N N 257 
PHE N   H2   sing N N 258 
PHE CA  C    sing N N 259 
PHE CA  CB   sing N N 260 
PHE CA  HA   sing N N 261 
PHE C   O    doub N N 262 
PHE C   OXT  sing N N 263 
PHE CB  CG   sing N N 264 
PHE CB  HB2  sing N N 265 
PHE CB  HB3  sing N N 266 
PHE CG  CD1  doub Y N 267 
PHE CG  CD2  sing Y N 268 
PHE CD1 CE1  sing Y N 269 
PHE CD1 HD1  sing N N 270 
PHE CD2 CE2  doub Y N 271 
PHE CD2 HD2  sing N N 272 
PHE CE1 CZ   doub Y N 273 
PHE CE1 HE1  sing N N 274 
PHE CE2 CZ   sing Y N 275 
PHE CE2 HE2  sing N N 276 
PHE CZ  HZ   sing N N 277 
PHE OXT HXT  sing N N 278 
PRO N   CA   sing N N 279 
PRO N   CD   sing N N 280 
PRO N   H    sing N N 281 
PRO CA  C    sing N N 282 
PRO CA  CB   sing N N 283 
PRO CA  HA   sing N N 284 
PRO C   O    doub N N 285 
PRO C   OXT  sing N N 286 
PRO CB  CG   sing N N 287 
PRO CB  HB2  sing N N 288 
PRO CB  HB3  sing N N 289 
PRO CG  CD   sing N N 290 
PRO CG  HG2  sing N N 291 
PRO CG  HG3  sing N N 292 
PRO CD  HD2  sing N N 293 
PRO CD  HD3  sing N N 294 
PRO OXT HXT  sing N N 295 
SER N   CA   sing N N 296 
SER N   H    sing N N 297 
SER N   H2   sing N N 298 
SER CA  C    sing N N 299 
SER CA  CB   sing N N 300 
SER CA  HA   sing N N 301 
SER C   O    doub N N 302 
SER C   OXT  sing N N 303 
SER CB  OG   sing N N 304 
SER CB  HB2  sing N N 305 
SER CB  HB3  sing N N 306 
SER OG  HG   sing N N 307 
SER OXT HXT  sing N N 308 
THR N   CA   sing N N 309 
THR N   H    sing N N 310 
THR N   H2   sing N N 311 
THR CA  C    sing N N 312 
THR CA  CB   sing N N 313 
THR CA  HA   sing N N 314 
THR C   O    doub N N 315 
THR C   OXT  sing N N 316 
THR CB  OG1  sing N N 317 
THR CB  CG2  sing N N 318 
THR CB  HB   sing N N 319 
THR OG1 HG1  sing N N 320 
THR CG2 HG21 sing N N 321 
THR CG2 HG22 sing N N 322 
THR CG2 HG23 sing N N 323 
THR OXT HXT  sing N N 324 
TRP N   CA   sing N N 325 
TRP N   H    sing N N 326 
TRP N   H2   sing N N 327 
TRP CA  C    sing N N 328 
TRP CA  CB   sing N N 329 
TRP CA  HA   sing N N 330 
TRP C   O    doub N N 331 
TRP C   OXT  sing N N 332 
TRP CB  CG   sing N N 333 
TRP CB  HB2  sing N N 334 
TRP CB  HB3  sing N N 335 
TRP CG  CD1  doub Y N 336 
TRP CG  CD2  sing Y N 337 
TRP CD1 NE1  sing Y N 338 
TRP CD1 HD1  sing N N 339 
TRP CD2 CE2  doub Y N 340 
TRP CD2 CE3  sing Y N 341 
TRP NE1 CE2  sing Y N 342 
TRP NE1 HE1  sing N N 343 
TRP CE2 CZ2  sing Y N 344 
TRP CE3 CZ3  doub Y N 345 
TRP CE3 HE3  sing N N 346 
TRP CZ2 CH2  doub Y N 347 
TRP CZ2 HZ2  sing N N 348 
TRP CZ3 CH2  sing Y N 349 
TRP CZ3 HZ3  sing N N 350 
TRP CH2 HH2  sing N N 351 
TRP OXT HXT  sing N N 352 
TYR N   CA   sing N N 353 
TYR N   H    sing N N 354 
TYR N   H2   sing N N 355 
TYR CA  C    sing N N 356 
TYR CA  CB   sing N N 357 
TYR CA  HA   sing N N 358 
TYR C   O    doub N N 359 
TYR C   OXT  sing N N 360 
TYR CB  CG   sing N N 361 
TYR CB  HB2  sing N N 362 
TYR CB  HB3  sing N N 363 
TYR CG  CD1  doub Y N 364 
TYR CG  CD2  sing Y N 365 
TYR CD1 CE1  sing Y N 366 
TYR CD1 HD1  sing N N 367 
TYR CD2 CE2  doub Y N 368 
TYR CD2 HD2  sing N N 369 
TYR CE1 CZ   doub Y N 370 
TYR CE1 HE1  sing N N 371 
TYR CE2 CZ   sing Y N 372 
TYR CE2 HE2  sing N N 373 
TYR CZ  OH   sing N N 374 
TYR OH  HH   sing N N 375 
TYR OXT HXT  sing N N 376 
VAL N   CA   sing N N 377 
VAL N   H    sing N N 378 
VAL N   H2   sing N N 379 
VAL CA  C    sing N N 380 
VAL CA  CB   sing N N 381 
VAL CA  HA   sing N N 382 
VAL C   O    doub N N 383 
VAL C   OXT  sing N N 384 
VAL CB  CG1  sing N N 385 
VAL CB  CG2  sing N N 386 
VAL CB  HB   sing N N 387 
VAL CG1 HG11 sing N N 388 
VAL CG1 HG12 sing N N 389 
VAL CG1 HG13 sing N N 390 
VAL CG2 HG21 sing N N 391 
VAL CG2 HG22 sing N N 392 
VAL CG2 HG23 sing N N 393 
VAL OXT HXT  sing N N 394 
# 
_pdbx_audit_support.funding_organization   'European Research Council (ERC)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           885396 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6I8N 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H9Y 
_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]   0.028540 
_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]   0.028540 
_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]   0.005994 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . GLU A 1 3   ? 27.877 -28.290 1.429   1.00 60.47  ? 3   GLU A N    1 
ATOM   2    C CA   . GLU A 1 3   ? 27.198 -27.776 0.244   1.00 68.32  ? 3   GLU A CA   1 
ATOM   3    C C    . GLU A 1 3   ? 26.156 -26.707 0.559   1.00 59.99  ? 3   GLU A C    1 
ATOM   4    O O    . GLU A 1 3   ? 25.522 -26.731 1.612   1.00 60.88  ? 3   GLU A O    1 
ATOM   5    C CB   . GLU A 1 3   ? 26.530 -28.912 -0.513  1.00 72.44  ? 3   GLU A CB   1 
ATOM   6    C CG   . GLU A 1 3   ? 27.488 -29.749 -1.314  1.00 88.33  ? 3   GLU A CG   1 
ATOM   7    C CD   . GLU A 1 3   ? 26.770 -30.808 -2.109  1.00 107.24 ? 3   GLU A CD   1 
ATOM   8    O OE1  . GLU A 1 3   ? 25.544 -30.959 -1.914  1.00 102.57 ? 3   GLU A OE1  1 
ATOM   9    O OE2  . GLU A 1 3   ? 27.426 -31.485 -2.929  1.00 107.30 ? 3   GLU A OE2  1 
ATOM   10   N N    . ILE A 1 4   ? 25.971 -25.791 -0.384  1.00 55.12  ? 4   ILE A N    1 
ATOM   11   C CA   . ILE A 1 4   ? 25.065 -24.649 -0.195  1.00 50.48  ? 4   ILE A CA   1 
ATOM   12   C C    . ILE A 1 4   ? 23.618 -25.117 -0.299  1.00 51.07  ? 4   ILE A C    1 
ATOM   13   O O    . ILE A 1 4   ? 23.258 -25.782 -1.284  1.00 46.12  ? 4   ILE A O    1 
ATOM   14   C CB   . ILE A 1 4   ? 25.357 -23.564 -1.239  1.00 48.20  ? 4   ILE A CB   1 
ATOM   15   C CG1  . ILE A 1 4   ? 26.654 -22.839 -0.905  1.00 46.64  ? 4   ILE A CG1  1 
ATOM   16   C CG2  . ILE A 1 4   ? 24.190 -22.592 -1.346  1.00 46.26  ? 4   ILE A CG2  1 
ATOM   17   C CD1  . ILE A 1 4   ? 27.223 -22.077 -2.068  1.00 46.01  ? 4   ILE A CD1  1 
ATOM   18   H HA   . ILE A 1 4   ? 25.204 -24.280 0.691   1.00 60.72  ? 4   ILE A HA   1 
ATOM   19   H HB   . ILE A 1 4   ? 25.467 -23.992 -2.103  1.00 57.97  ? 4   ILE A HB   1 
ATOM   20   H HG12 . ILE A 1 4   ? 26.485 -22.208 -0.188  1.00 56.10  ? 4   ILE A HG12 1 
ATOM   21   H HG13 . ILE A 1 4   ? 27.315 -23.491 -0.624  1.00 56.10  ? 4   ILE A HG13 1 
ATOM   22   H HG21 . ILE A 1 4   ? 24.507 -21.760 -1.731  1.00 55.64  ? 4   ILE A HG21 1 
ATOM   23   H HG22 . ILE A 1 4   ? 23.506 -22.980 -1.913  1.00 55.64  ? 4   ILE A HG22 1 
ATOM   24   H HG23 . ILE A 1 4   ? 23.832 -22.430 -0.459  1.00 55.64  ? 4   ILE A HG23 1 
ATOM   25   H HD11 . ILE A 1 4   ? 28.019 -21.604 -1.777  1.00 55.35  ? 4   ILE A HD11 1 
ATOM   26   H HD12 . ILE A 1 4   ? 27.449 -22.701 -2.775  1.00 55.35  ? 4   ILE A HD12 1 
ATOM   27   H HD13 . ILE A 1 4   ? 26.560 -21.444 -2.386  1.00 55.35  ? 4   ILE A HD13 1 
ATOM   28   N N    . PRO A 1 5   ? 22.752 -24.771 0.653   1.00 47.68  ? 5   PRO A N    1 
ATOM   29   C CA   . PRO A 1 5   ? 21.334 -25.128 0.519   1.00 46.50  ? 5   PRO A CA   1 
ATOM   30   C C    . PRO A 1 5   ? 20.758 -24.643 -0.805  1.00 46.50  ? 5   PRO A C    1 
ATOM   31   O O    . PRO A 1 5   ? 21.054 -23.545 -1.272  1.00 40.20  ? 5   PRO A O    1 
ATOM   32   C CB   . PRO A 1 5   ? 20.673 -24.427 1.712   1.00 48.23  ? 5   PRO A CB   1 
ATOM   33   C CG   . PRO A 1 5   ? 21.760 -24.230 2.703   1.00 49.37  ? 5   PRO A CG   1 
ATOM   34   C CD   . PRO A 1 5   ? 23.036 -24.050 1.912   1.00 45.32  ? 5   PRO A CD   1 
ATOM   35   H HA   . PRO A 1 5   ? 21.216 -26.087 0.596   1.00 55.93  ? 5   PRO A HA   1 
ATOM   36   H HB2  . PRO A 1 5   ? 20.304 -23.575 1.429   1.00 58.01  ? 5   PRO A HB2  1 
ATOM   37   H HB3  . PRO A 1 5   ? 19.971 -24.988 2.075   1.00 58.01  ? 5   PRO A HB3  1 
ATOM   38   H HG2  . PRO A 1 5   ? 21.574 -23.440 3.235   1.00 59.38  ? 5   PRO A HG2  1 
ATOM   39   H HG3  . PRO A 1 5   ? 21.821 -25.010 3.277   1.00 59.38  ? 5   PRO A HG3  1 
ATOM   40   H HD2  . PRO A 1 5   ? 23.209 -23.111 1.741   1.00 54.51  ? 5   PRO A HD2  1 
ATOM   41   H HD3  . PRO A 1 5   ? 23.790 -24.447 2.375   1.00 54.51  ? 5   PRO A HD3  1 
ATOM   42   N N    . LYS A 1 6   ? 19.913 -25.470 -1.416  1.00 42.81  ? 6   LYS A N    1 
ATOM   43   C CA   . LYS A 1 6   ? 19.281 -25.044 -2.656  1.00 42.91  ? 6   LYS A CA   1 
ATOM   44   C C    . LYS A 1 6   ? 18.434 -23.801 -2.450  1.00 39.89  ? 6   LYS A C    1 
ATOM   45   O O    . LYS A 1 6   ? 18.322 -22.977 -3.367  1.00 39.03  ? 6   LYS A O    1 
ATOM   46   C CB   . LYS A 1 6   ? 18.441 -26.178 -3.227  1.00 56.44  ? 6   LYS A CB   1 
ATOM   47   C CG   . LYS A 1 6   ? 19.278 -27.398 -3.587  1.00 64.35  ? 6   LYS A CG   1 
ATOM   48   C CD   . LYS A 1 6   ? 18.452 -28.456 -4.296  1.00 77.88  ? 6   LYS A CD   1 
ATOM   49   C CE   . LYS A 1 6   ? 19.326 -29.618 -4.739  1.00 87.23  ? 6   LYS A CE   1 
ATOM   50   N NZ   . LYS A 1 6   ? 18.559 -30.637 -5.508  1.00 101.21 ? 6   LYS A NZ   1 
ATOM   51   H H    . LYS A 1 6   ? 19.697 -26.256 -1.142  1.00 51.50  ? 6   LYS A H    1 
ATOM   52   H HA   . LYS A 1 6   ? 19.970 -24.828 -3.304  1.00 51.62  ? 6   LYS A HA   1 
ATOM   53   H HB2  . LYS A 1 6   ? 17.783 -26.448 -2.568  1.00 67.87  ? 6   LYS A HB2  1 
ATOM   54   H HB3  . LYS A 1 6   ? 17.997 -25.869 -4.032  1.00 67.87  ? 6   LYS A HB3  1 
ATOM   55   H HG2  . LYS A 1 6   ? 19.999 -27.129 -4.178  1.00 77.35  ? 6   LYS A HG2  1 
ATOM   56   H HG3  . LYS A 1 6   ? 19.641 -27.788 -2.777  1.00 77.35  ? 6   LYS A HG3  1 
ATOM   57   H HD2  . LYS A 1 6   ? 17.772 -28.794 -3.692  1.00 93.59  ? 6   LYS A HD2  1 
ATOM   58   H HD3  . LYS A 1 6   ? 18.034 -28.068 -5.081  1.00 93.59  ? 6   LYS A HD3  1 
ATOM   59   H HE2  . LYS A 1 6   ? 20.038 -29.284 -5.306  1.00 104.82 ? 6   LYS A HE2  1 
ATOM   60   H HE3  . LYS A 1 6   ? 19.701 -30.051 -3.956  1.00 104.82 ? 6   LYS A HE3  1 
ATOM   61   H HZ1  . LYS A 1 6   ? 19.099 -31.299 -5.759  1.00 121.59 ? 6   LYS A HZ1  1 
ATOM   62   H HZ2  . LYS A 1 6   ? 17.906 -30.972 -5.004  1.00 121.59 ? 6   LYS A HZ2  1 
ATOM   63   H HZ3  . LYS A 1 6   ? 18.202 -30.265 -6.233  1.00 121.59 ? 6   LYS A HZ3  1 
ATOM   64   N N    . GLU A 1 7   ? 17.854 -23.632 -1.253  1.00 40.39  ? 7   GLU A N    1 
ATOM   65   C CA   . GLU A 1 7   ? 17.062 -22.431 -0.993  1.00 40.60  ? 7   GLU A CA   1 
ATOM   66   C C    . GLU A 1 7   ? 17.933 -21.188 -1.100  1.00 39.55  ? 7   GLU A C    1 
ATOM   67   O O    . GLU A 1 7   ? 17.506 -20.147 -1.605  1.00 39.22  ? 7   GLU A O    1 
ATOM   68   C CB   . GLU A 1 7   ? 16.426 -22.471 0.399   1.00 47.85  ? 7   GLU A CB   1 
ATOM   69   C CG   . GLU A 1 7   ? 15.915 -23.818 0.853   1.00 68.61  ? 7   GLU A CG   1 
ATOM   70   C CD   . GLU A 1 7   ? 16.972 -24.621 1.595   1.00 77.27  ? 7   GLU A CD   1 
ATOM   71   O OE1  . GLU A 1 7   ? 17.269 -24.308 2.774   1.00 76.14  ? 7   GLU A OE1  1 
ATOM   72   O OE2  . GLU A 1 7   ? 17.522 -25.558 0.980   1.00 56.53  ? 7   GLU A OE2  1 
ATOM   73   H H    . GLU A 1 7   ? 17.903 -24.184 -0.595  1.00 48.60  ? 7   GLU A H    1 
ATOM   74   H HA   . GLU A 1 7   ? 16.348 -22.398 -1.649  1.00 48.86  ? 7   GLU A HA   1 
ATOM   75   H HB2  . GLU A 1 7   ? 17.090 -22.183 1.045   1.00 57.55  ? 7   GLU A HB2  1 
ATOM   76   H HB3  . GLU A 1 7   ? 15.671 -21.862 0.405   1.00 57.55  ? 7   GLU A HB3  1 
ATOM   77   H HG2  . GLU A 1 7   ? 15.163 -23.686 1.451   1.00 82.47  ? 7   GLU A HG2  1 
ATOM   78   H HG3  . GLU A 1 7   ? 15.638 -24.329 0.077   1.00 82.47  ? 7   GLU A HG3  1 
ATOM   79   N N    . MET A 1 8   ? 19.156 -21.279 -0.592  1.00 37.60  ? 8   MET A N    1 
ATOM   80   C CA   . MET A 1 8   ? 20.073 -20.150 -0.619  1.00 37.58  ? 8   MET A CA   1 
ATOM   81   C C    . MET A 1 8   ? 20.475 -19.816 -2.047  1.00 30.67  ? 8   MET A C    1 
ATOM   82   O O    . MET A 1 8   ? 20.424 -18.654 -2.455  1.00 31.10  ? 8   MET A O    1 
ATOM   83   C CB   . MET A 1 8   ? 21.285 -20.497 0.239   1.00 40.56  ? 8   MET A CB   1 
ATOM   84   C CG   . MET A 1 8   ? 22.077 -19.341 0.728   1.00 38.33  ? 8   MET A CG   1 
ATOM   85   S SD   . MET A 1 8   ? 23.310 -19.833 1.932   1.00 36.79  ? 8   MET A SD   1 
ATOM   86   C CE   . MET A 1 8   ? 22.431 -19.736 3.477   1.00 32.85  ? 8   MET A CE   1 
ATOM   87   H H    . MET A 1 8   ? 19.481 -21.985 -0.224  1.00 45.26  ? 8   MET A H    1 
ATOM   88   H HA   . MET A 1 8   ? 19.647 -19.364 -0.241  1.00 45.22  ? 8   MET A HA   1 
ATOM   89   H HB2  . MET A 1 8   ? 20.977 -20.985 1.018   1.00 48.81  ? 8   MET A HB2  1 
ATOM   90   H HB3  . MET A 1 8   ? 21.881 -21.053 -0.287  1.00 48.81  ? 8   MET A HB3  1 
ATOM   91   H HG2  . MET A 1 8   ? 22.533 -18.927 -0.022  1.00 46.14  ? 8   MET A HG2  1 
ATOM   92   H HG3  . MET A 1 8   ? 21.481 -18.701 1.148   1.00 46.14  ? 8   MET A HG3  1 
ATOM   93   H HE1  . MET A 1 8   ? 23.044 -19.937 4.201   1.00 39.56  ? 8   MET A HE1  1 
ATOM   94   H HE2  . MET A 1 8   ? 22.076 -18.840 3.582   1.00 39.56  ? 8   MET A HE2  1 
ATOM   95   H HE3  . MET A 1 8   ? 21.706 -20.381 3.468   1.00 39.56  ? 8   MET A HE3  1 
ATOM   96   N N    . LEU A 1 9   ? 20.839 -20.834 -2.836  1.00 37.29  ? 9   LEU A N    1 
ATOM   97   C CA   . LEU A 1 9   ? 21.195 -20.586 -4.227  1.00 36.90  ? 9   LEU A CA   1 
ATOM   98   C C    . LEU A 1 9   ? 20.025 -19.959 -4.971  1.00 35.51  ? 9   LEU A C    1 
ATOM   99   O O    . LEU A 1 9   ? 20.202 -19.033 -5.764  1.00 34.50  ? 9   LEU A O    1 
ATOM   100  C CB   . LEU A 1 9   ? 21.627 -21.888 -4.904  1.00 39.41  ? 9   LEU A CB   1 
ATOM   101  C CG   . LEU A 1 9   ? 21.742 -21.805 -6.427  1.00 65.39  ? 9   LEU A CG   1 
ATOM   102  C CD1  . LEU A 1 9   ? 22.781 -20.754 -6.826  1.00 60.43  ? 9   LEU A CD1  1 
ATOM   103  C CD2  . LEU A 1 9   ? 22.075 -23.164 -7.040  1.00 71.36  ? 9   LEU A CD2  1 
ATOM   104  H H    . LEU A 1 9   ? 20.885 -21.657 -2.591  1.00 44.88  ? 9   LEU A H    1 
ATOM   105  H HA   . LEU A 1 9   ? 21.947 -19.974 -4.260  1.00 44.42  ? 9   LEU A HA   1 
ATOM   106  H HB2  . LEU A 1 9   ? 22.497 -22.141 -4.558  1.00 47.42  ? 9   LEU A HB2  1 
ATOM   107  H HB3  . LEU A 1 9   ? 20.975 -22.575 -4.696  1.00 47.42  ? 9   LEU A HB3  1 
ATOM   108  H HG   . LEU A 1 9   ? 20.883 -21.536 -6.786  1.00 78.60  ? 9   LEU A HG   1 
ATOM   109  H HD11 . LEU A 1 9   ? 22.970 -20.841 -7.774  1.00 72.65  ? 9   LEU A HD11 1 
ATOM   110  H HD12 . LEU A 1 9   ? 22.424 -19.872 -6.640  1.00 72.65  ? 9   LEU A HD12 1 
ATOM   111  H HD13 . LEU A 1 9   ? 23.591 -20.899 -6.313  1.00 72.65  ? 9   LEU A HD13 1 
ATOM   112  H HD21 . LEU A 1 9   ? 22.164 -23.064 -8.001  1.00 85.77  ? 9   LEU A HD21 1 
ATOM   113  H HD22 . LEU A 1 9   ? 22.910 -23.485 -6.663  1.00 85.77  ? 9   LEU A HD22 1 
ATOM   114  H HD23 . LEU A 1 9   ? 21.360 -23.787 -6.837  1.00 85.77  ? 9   LEU A HD23 1 
ATOM   115  N N    . ARG A 1 10  ? 18.816 -20.465 -4.747  1.00 33.45  ? 10  ARG A N    1 
ATOM   116  C CA   . ARG A 1 10  ? 17.652 -19.890 -5.410  1.00 36.29  ? 10  ARG A CA   1 
ATOM   117  C C    . ARG A 1 10  ? 17.466 -18.429 -5.025  1.00 32.87  ? 10  ARG A C    1 
ATOM   118  O O    . ARG A 1 10  ? 17.130 -17.586 -5.872  1.00 32.46  ? 10  ARG A O    1 
ATOM   119  C CB   . ARG A 1 10  ? 16.408 -20.721 -5.068  1.00 37.47  ? 10  ARG A CB   1 
ATOM   120  C CG   . ARG A 1 10  ? 15.074 -20.137 -5.520  1.00 47.48  ? 10  ARG A CG   1 
ATOM   121  C CD   . ARG A 1 10  ? 15.052 -19.744 -7.004  1.00 53.23  ? 10  ARG A CD   1 
ATOM   122  N NE   . ARG A 1 10  ? 15.556 -20.785 -7.896  1.00 62.41  ? 10  ARG A NE   1 
ATOM   123  C CZ   . ARG A 1 10  ? 14.799 -21.652 -8.559  1.00 66.16  ? 10  ARG A CZ   1 
ATOM   124  N NH1  . ARG A 1 10  ? 13.482 -21.670 -8.420  1.00 59.21  ? 10  ARG A NH1  1 
ATOM   125  N NH2  . ARG A 1 10  ? 15.379 -22.521 -9.384  1.00 56.06  ? 10  ARG A NH2  1 
ATOM   126  H H    . ARG A 1 10  ? 18.646 -21.129 -4.227  1.00 40.27  ? 10  ARG A H    1 
ATOM   127  H HA   . ARG A 1 10  ? 17.777 -19.921 -6.372  1.00 43.69  ? 10  ARG A HA   1 
ATOM   128  H HB2  . ARG A 1 10  ? 16.498 -21.591 -5.490  1.00 45.10  ? 10  ARG A HB2  1 
ATOM   129  H HB3  . ARG A 1 10  ? 16.366 -20.823 -4.105  1.00 45.10  ? 10  ARG A HB3  1 
ATOM   130  H HG2  . ARG A 1 10  ? 14.378 -20.797 -5.377  1.00 57.11  ? 10  ARG A HG2  1 
ATOM   131  H HG3  . ARG A 1 10  ? 14.888 -19.341 -4.999  1.00 57.11  ? 10  ARG A HG3  1 
ATOM   132  H HD2  . ARG A 1 10  ? 14.137 -19.552 -7.262  1.00 64.01  ? 10  ARG A HD2  1 
ATOM   133  H HD3  . ARG A 1 10  ? 15.604 -18.956 -7.127  1.00 64.01  ? 10  ARG A HD3  1 
ATOM   134  H HE   . ARG A 1 10  ? 16.408 -20.841 -7.999  1.00 75.03  ? 10  ARG A HE   1 
ATOM   135  H HH11 . ARG A 1 10  ? 13.097 -21.112 -7.891  1.00 71.18  ? 10  ARG A HH11 1 
ATOM   136  H HH12 . ARG A 1 10  ? 13.011 -22.241 -8.859  1.00 71.18  ? 10  ARG A HH12 1 
ATOM   137  H HH21 . ARG A 1 10  ? 16.234 -22.516 -9.483  1.00 67.40  ? 10  ARG A HH21 1 
ATOM   138  H HH22 . ARG A 1 10  ? 14.899 -23.087 -9.819  1.00 67.40  ? 10  ARG A HH22 1 
ATOM   139  N N    . ALA A 1 11  ? 17.634 -18.116 -3.746  1.00 31.65  ? 11  ALA A N    1 
ATOM   140  C CA   . ALA A 1 11  ? 17.448 -16.744 -3.296  1.00 29.36  ? 11  ALA A CA   1 
ATOM   141  C C    . ALA A 1 11  ? 18.443 -15.825 -3.981  1.00 30.15  ? 11  ALA A C    1 
ATOM   142  O O    . ALA A 1 11  ? 18.091 -14.708 -4.404  1.00 27.94  ? 11  ALA A O    1 
ATOM   143  C CB   . ALA A 1 11  ? 17.601 -16.672 -1.783  1.00 28.29  ? 11  ALA A CB   1 
ATOM   144  H H    . ALA A 1 11  ? 17.853 -18.671 -3.127  1.00 38.11  ? 11  ALA A H    1 
ATOM   145  H HA   . ALA A 1 11  ? 16.552 -16.448 -3.519  1.00 35.37  ? 11  ALA A HA   1 
ATOM   146  H HB1  . ALA A 1 11  ? 17.544 -15.744 -1.504  1.00 34.09  ? 11  ALA A HB1  1 
ATOM   147  H HB2  . ALA A 1 11  ? 16.890 -17.185 -1.369  1.00 34.09  ? 11  ALA A HB2  1 
ATOM   148  H HB3  . ALA A 1 11  ? 18.463 -17.040 -1.535  1.00 34.09  ? 11  ALA A HB3  1 
ATOM   149  N N    . GLN A 1 12  ? 19.668 -16.300 -4.147  1.00 27.61  ? 12  GLN A N    1 
ATOM   150  C CA   . GLN A 1 12  ? 20.692 -15.469 -4.765  1.00 29.34  ? 12  GLN A CA   1 
ATOM   151  C C    . GLN A 1 12  ? 20.379 -15.262 -6.235  1.00 28.15  ? 12  GLN A C    1 
ATOM   152  O O    . GLN A 1 12  ? 20.508 -14.152 -6.761  1.00 27.97  ? 12  GLN A O    1 
ATOM   153  C CB   . GLN A 1 12  ? 22.054 -16.126 -4.611  1.00 27.16  ? 12  GLN A CB   1 
ATOM   154  C CG   . GLN A 1 12  ? 22.534 -16.245 -3.162  1.00 29.13  ? 12  GLN A CG   1 
ATOM   155  C CD   . GLN A 1 12  ? 23.747 -17.086 -2.973  1.00 28.06  ? 12  GLN A CD   1 
ATOM   156  O OE1  . GLN A 1 12  ? 24.129 -17.892 -3.822  1.00 31.32  ? 12  GLN A OE1  1 
ATOM   157  N NE2  . GLN A 1 12  ? 24.363 -16.912 -1.827  1.00 30.64  ? 12  GLN A NE2  1 
ATOM   158  H H    . GLN A 1 12  ? 19.930 -17.086 -3.915  1.00 33.27  ? 12  GLN A H    1 
ATOM   159  H HA   . GLN A 1 12  ? 20.719 -14.606 -4.322  1.00 35.35  ? 12  GLN A HA   1 
ATOM   160  H HB2  . GLN A 1 12  ? 22.009 -17.022 -4.980  1.00 32.73  ? 12  GLN A HB2  1 
ATOM   161  H HB3  . GLN A 1 12  ? 22.708 -15.600 -5.096  1.00 32.73  ? 12  GLN A HB3  1 
ATOM   162  H HG2  . GLN A 1 12  ? 22.742 -15.356 -2.832  1.00 35.09  ? 12  GLN A HG2  1 
ATOM   163  H HG3  . GLN A 1 12  ? 21.823 -16.637 -2.632  1.00 35.09  ? 12  GLN A HG3  1 
ATOM   164  H HE21 . GLN A 1 12  ? 24.058 -16.347 -1.255  1.00 36.90  ? 12  GLN A HE21 1 
ATOM   165  H HE22 . GLN A 1 12  ? 25.073 -17.365 -1.647  1.00 36.90  ? 12  GLN A HE22 1 
ATOM   166  N N    . THR A 1 13  ? 19.976 -16.339 -6.914  1.00 29.33  ? 13  THR A N    1 
ATOM   167  C CA   . THR A 1 13  ? 19.629 -16.230 -8.321  1.00 26.96  ? 13  THR A CA   1 
ATOM   168  C C    . THR A 1 13  ? 18.476 -15.270 -8.517  1.00 29.20  ? 13  THR A C    1 
ATOM   169  O O    . THR A 1 13  ? 18.492 -14.471 -9.456  1.00 27.35  ? 13  THR A O    1 
ATOM   170  C CB   . THR A 1 13  ? 19.293 -17.604 -8.883  1.00 29.42  ? 13  THR A CB   1 
ATOM   171  O OG1  . THR A 1 13  ? 20.414 -18.469 -8.684  1.00 32.74  ? 13  THR A OG1  1 
ATOM   172  C CG2  . THR A 1 13  ? 19.002 -17.544 -10.351 1.00 29.67  ? 13  THR A CG2  1 
ATOM   173  H H    . THR A 1 13  ? 19.897 -17.130 -6.585  1.00 35.33  ? 13  THR A H    1 
ATOM   174  H HA   . THR A 1 13  ? 20.392 -15.889 -8.814  1.00 32.48  ? 13  THR A HA   1 
ATOM   175  H HB   . THR A 1 13  ? 18.504 -17.945 -8.432  1.00 35.44  ? 13  THR A HB   1 
ATOM   176  H HG1  . THR A 1 13  ? 20.550 -18.580 -7.863  1.00 39.42  ? 13  THR A HG1  1 
ATOM   177  H HG21 . THR A 1 13  ? 18.989 -18.440 -10.724 1.00 35.73  ? 13  THR A HG21 1 
ATOM   178  H HG22 . THR A 1 13  ? 18.139 -17.128 -10.502 1.00 35.73  ? 13  THR A HG22 1 
ATOM   179  H HG23 . THR A 1 13  ? 19.685 -17.025 -10.804 1.00 35.73  ? 13  THR A HG23 1 
ATOM   180  N N    . ASN A 1 14  ? 17.445 -15.369 -7.686  1.00 28.15  ? 14  ASN A N    1 
ATOM   181  C CA   . ASN A 1 14  ? 16.303 -14.462 -7.772  1.00 31.07  ? 14  ASN A CA   1 
ATOM   182  C C    . ASN A 1 14  ? 16.764 -13.003 -7.671  1.00 26.99  ? 14  ASN A C    1 
ATOM   183  O O    . ASN A 1 14  ? 16.293 -12.119 -8.402  1.00 27.38  ? 14  ASN A O    1 
ATOM   184  C CB   . ASN A 1 14  ? 15.286 -14.760 -6.651  1.00 29.70  ? 14  ASN A CB   1 
ATOM   185  C CG   . ASN A 1 14  ? 14.320 -15.851 -6.998  1.00 39.57  ? 14  ASN A CG   1 
ATOM   186  O OD1  . ASN A 1 14  ? 13.793 -15.898 -8.106  1.00 46.26  ? 14  ASN A OD1  1 
ATOM   187  N ND2  . ASN A 1 14  ? 14.037 -16.709 -6.034  1.00 49.47  ? 14  ASN A ND2  1 
ATOM   188  H H    . ASN A 1 14  ? 17.381 -15.955 -7.060  1.00 33.91  ? 14  ASN A H    1 
ATOM   189  H HA   . ASN A 1 14  ? 15.860 -14.591 -8.625  1.00 37.42  ? 14  ASN A HA   1 
ATOM   190  H HB2  . ASN A 1 14  ? 15.769 -15.032 -5.855  1.00 35.78  ? 14  ASN A HB2  1 
ATOM   191  H HB3  . ASN A 1 14  ? 14.774 -13.956 -6.470  1.00 35.78  ? 14  ASN A HB3  1 
ATOM   192  H HD21 . ASN A 1 14  ? 13.488 -17.355 -6.181  1.00 59.50  ? 14  ASN A HD21 1 
ATOM   193  H HD22 . ASN A 1 14  ? 14.402 -16.622 -5.260  1.00 59.50  ? 14  ASN A HD22 1 
HETATM 194  C C9   . BP5 A 1 15  ? 19.704 -10.214 -4.748  1.00 26.53  ? 15  BP5 A C9   1 
HETATM 195  C C8   . BP5 A 1 15  ? 21.026 -10.425 -4.452  1.00 30.13  ? 15  BP5 A C8   1 
HETATM 196  C C7   . BP5 A 1 15  ? 21.802 -9.369  -4.045  1.00 28.90  ? 15  BP5 A C7   1 
HETATM 197  C C6   . BP5 A 1 15  ? 21.242 -8.109  -3.955  1.00 30.33  ? 15  BP5 A C6   1 
HETATM 198  C C5   . BP5 A 1 15  ? 23.552 -4.952  -2.441  1.00 37.04  ? 15  BP5 A C5   1 
HETATM 199  C C4   . BP5 A 1 15  ? 22.279 -4.782  -2.934  1.00 37.98  ? 15  BP5 A C4   1 
HETATM 200  C C3   . BP5 A 1 15  ? 22.075 -6.998  -3.455  1.00 34.71  ? 15  BP5 A C3   1 
HETATM 201  C C2   . BP5 A 1 15  ? 23.341 -7.251  -2.960  1.00 36.06  ? 15  BP5 A C2   1 
HETATM 202  C C1   . BP5 A 1 15  ? 24.093 -6.211  -2.455  1.00 35.76  ? 15  BP5 A C1   1 
HETATM 203  C C12  . BP5 A 1 15  ? 18.908 -11.424 -5.142  1.00 30.53  ? 15  BP5 A C12  1 
HETATM 204  C C11  . BP5 A 1 15  ? 19.194 -8.919  -4.596  1.00 28.30  ? 15  BP5 A C11  1 
HETATM 205  N N1   . BP5 A 1 15  ? 21.528 -5.782  -3.434  1.00 36.91  ? 15  BP5 A N1   1 
HETATM 206  N N2   . BP5 A 1 15  ? 19.935 -7.879  -4.207  1.00 34.94  ? 15  BP5 A N2   1 
HETATM 207  C CA   . BP5 A 1 15  ? 18.087 -11.354 -6.423  1.00 25.28  ? 15  BP5 A CA   1 
HETATM 208  C C    . BP5 A 1 15  ? 18.861 -10.820 -7.611  1.00 27.48  ? 15  BP5 A C    1 
HETATM 209  O O    . BP5 A 1 15  ? 18.638 -9.676  -8.023  1.00 26.36  ? 15  BP5 A O    1 
HETATM 210  N N    . BP5 A 1 15  ? 17.637 -12.740 -6.717  1.00 26.01  ? 15  BP5 A N    1 
HETATM 211  H H5   . BP5 A 1 15  ? 24.039 -4.219  -2.101  1.00 44.58  ? 15  BP5 A H5   1 
HETATM 212  H H4   . BP5 A 1 15  ? 21.906 -3.915  -2.924  1.00 45.71  ? 15  BP5 A H4   1 
HETATM 213  H H3   . BP5 A 1 15  ? 23.686 -8.129  -2.968  1.00 43.41  ? 15  BP5 A H3   1 
HETATM 214  H H11  . BP5 A 1 15  ? 18.277 -8.769  -4.777  1.00 34.09  ? 15  BP5 A H11  1 
ATOM   215  N N    . ILE A 1 16  ? 19.772 -11.623 -8.141  1.00 26.52  ? 16  ILE A N    1 
ATOM   216  C CA   . ILE A 1 16  ? 20.550 -11.216 -9.308  1.00 26.59  ? 16  ILE A CA   1 
ATOM   217  C C    . ILE A 1 16  ? 19.661 -10.949 -10.518 1.00 28.81  ? 16  ILE A C    1 
ATOM   218  O O    . ILE A 1 16  ? 19.806 -9.931  -11.176 1.00 27.15  ? 16  ILE A O    1 
ATOM   219  C CB   . ILE A 1 16  ? 21.604 -12.271 -9.652  1.00 27.29  ? 16  ILE A CB   1 
ATOM   220  C CG1  . ILE A 1 16  ? 22.651 -12.349 -8.531  1.00 28.18  ? 16  ILE A CG1  1 
ATOM   221  C CG2  . ILE A 1 16  ? 22.236 -11.974 -11.015 1.00 28.09  ? 16  ILE A CG2  1 
ATOM   222  C CD1  . ILE A 1 16  ? 23.547 -13.527 -8.641  1.00 31.23  ? 16  ILE A CD1  1 
ATOM   223  H H    . ILE A 1 16  ? 19.960 -12.409 -7.846  1.00 31.96  ? 16  ILE A H    1 
ATOM   224  H HA   . ILE A 1 16  ? 20.996 -10.384 -9.085  1.00 32.05  ? 16  ILE A HA   1 
ATOM   225  H HB   . ILE A 1 16  ? 21.177 -13.139 -9.719  1.00 32.88  ? 16  ILE A HB   1 
ATOM   226  H HG12 . ILE A 1 16  ? 23.202 -11.551 -8.562  1.00 33.95  ? 16  ILE A HG12 1 
ATOM   227  H HG13 . ILE A 1 16  ? 22.192 -12.403 -7.678  1.00 33.95  ? 16  ILE A HG13 1 
ATOM   228  H HG21 . ILE A 1 16  ? 23.086 -12.438 -11.077 1.00 33.84  ? 16  ILE A HG21 1 
ATOM   229  H HG22 . ILE A 1 16  ? 21.639 -12.282 -11.714 1.00 33.84  ? 16  ILE A HG22 1 
ATOM   230  H HG23 . ILE A 1 16  ? 22.375 -11.017 -11.097 1.00 33.84  ? 16  ILE A HG23 1 
ATOM   231  H HD11 . ILE A 1 16  ? 24.048 -13.621 -7.816  1.00 37.61  ? 16  ILE A HD11 1 
ATOM   232  H HD12 . ILE A 1 16  ? 23.010 -14.320 -8.794  1.00 37.61  ? 16  ILE A HD12 1 
ATOM   233  H HD13 . ILE A 1 16  ? 24.157 -13.392 -9.384  1.00 37.61  ? 16  ILE A HD13 1 
ATOM   234  N N    . LEU A 1 17  ? 18.699 -11.826 -10.806 1.00 25.97  ? 17  LEU A N    1 
ATOM   235  C CA   . LEU A 1 17  ? 17.821 -11.618 -11.957 1.00 27.60  ? 17  LEU A CA   1 
ATOM   236  C C    . LEU A 1 17  ? 16.976 -10.358 -11.796 1.00 30.17  ? 17  LEU A C    1 
ATOM   237  O O    . LEU A 1 17  ? 16.771 -9.610  -12.754 1.00 28.95  ? 17  LEU A O    1 
ATOM   238  C CB   . LEU A 1 17  ? 16.930 -12.840 -12.142 1.00 29.31  ? 17  LEU A CB   1 
ATOM   239  C CG   . LEU A 1 17  ? 17.695 -14.089 -12.563 1.00 26.62  ? 17  LEU A CG   1 
ATOM   240  C CD1  . LEU A 1 17  ? 16.743 -15.288 -12.617 1.00 31.83  ? 17  LEU A CD1  1 
ATOM   241  C CD2  . LEU A 1 17  ? 18.372 -13.933 -13.915 1.00 35.02  ? 17  LEU A CD2  1 
ATOM   242  H H    . LEU A 1 17  ? 18.536 -12.541 -10.357 1.00 31.30  ? 17  LEU A H    1 
ATOM   243  H HA   . LEU A 1 17  ? 18.366 -11.506 -12.752 1.00 33.26  ? 17  LEU A HA   1 
ATOM   244  H HB2  . LEU A 1 17  ? 16.484 -13.032 -11.302 1.00 35.31  ? 17  LEU A HB2  1 
ATOM   245  H HB3  . LEU A 1 17  ? 16.273 -12.647 -12.829 1.00 35.31  ? 17  LEU A HB3  1 
ATOM   246  H HG   . LEU A 1 17  ? 18.392 -14.240 -11.905 1.00 32.08  ? 17  LEU A HG   1 
ATOM   247  H HD11 . LEU A 1 17  ? 17.248 -16.083 -12.848 1.00 38.33  ? 17  LEU A HD11 1 
ATOM   248  H HD12 . LEU A 1 17  ? 16.327 -15.400 -11.748 1.00 38.33  ? 17  LEU A HD12 1 
ATOM   249  H HD13 . LEU A 1 17  ? 16.063 -15.121 -13.290 1.00 38.33  ? 17  LEU A HD13 1 
ATOM   250  H HD21 . LEU A 1 17  ? 18.830 -14.759 -14.136 1.00 42.16  ? 17  LEU A HD21 1 
ATOM   251  H HD22 . LEU A 1 17  ? 17.698 -13.739 -14.585 1.00 42.16  ? 17  LEU A HD22 1 
ATOM   252  H HD23 . LEU A 1 17  ? 19.010 -13.204 -13.867 1.00 42.16  ? 17  LEU A HD23 1 
ATOM   253  N N    . LEU A 1 18  ? 16.426 -10.127 -10.606 1.00 27.23  ? 18  LEU A N    1 
ATOM   254  C CA   . LEU A 1 18  ? 15.644 -8.908  -10.404 1.00 27.63  ? 18  LEU A CA   1 
ATOM   255  C C    . LEU A 1 18  ? 16.529 -7.692  -10.626 1.00 26.86  ? 18  LEU A C    1 
ATOM   256  O O    . LEU A 1 18  ? 16.108 -6.722  -11.255 1.00 27.23  ? 18  LEU A O    1 
ATOM   257  C CB   . LEU A 1 18  ? 15.050 -8.885  -8.996  1.00 28.70  ? 18  LEU A CB   1 
ATOM   258  C CG   . LEU A 1 18  ? 13.956 -9.873  -8.673  1.00 27.92  ? 18  LEU A CG   1 
ATOM   259  C CD1  . LEU A 1 18  ? 13.776 -9.925  -7.167  1.00 33.30  ? 18  LEU A CD1  1 
ATOM   260  C CD2  . LEU A 1 18  ? 12.726 -9.399  -9.377  1.00 29.54  ? 18  LEU A CD2  1 
ATOM   261  H H    . LEU A 1 18  ? 16.488 -10.642 -9.920  1.00 32.81  ? 18  LEU A H    1 
ATOM   262  H HA   . LEU A 1 18  ? 14.905 -8.887  -11.031 1.00 33.30  ? 18  LEU A HA   1 
ATOM   263  H HB2  . LEU A 1 18  ? 15.771 -9.054  -8.369  1.00 34.57  ? 18  LEU A HB2  1 
ATOM   264  H HB3  . LEU A 1 18  ? 14.681 -8.001  -8.846  1.00 34.57  ? 18  LEU A HB3  1 
ATOM   265  H HG   . LEU A 1 18  ? 14.155 -10.776 -8.965  1.00 33.64  ? 18  LEU A HG   1 
ATOM   266  H HD11 . LEU A 1 18  ? 13.008 -10.480 -6.960  1.00 40.10  ? 18  LEU A HD11 1 
ATOM   267  H HD12 . LEU A 1 18  ? 14.575 -10.302 -6.767  1.00 40.10  ? 18  LEU A HD12 1 
ATOM   268  H HD13 . LEU A 1 18  ? 13.632 -9.025  -6.835  1.00 40.10  ? 18  LEU A HD13 1 
ATOM   269  H HD21 . LEU A 1 18  ? 11.997 -10.009 -9.184  1.00 35.58  ? 18  LEU A HD21 1 
ATOM   270  H HD22 . LEU A 1 18  ? 12.505 -8.508  -9.063  1.00 35.58  ? 18  LEU A HD22 1 
ATOM   271  H HD23 . LEU A 1 18  ? 12.896 -9.380  -10.332 1.00 35.58  ? 18  LEU A HD23 1 
ATOM   272  N N    . ASN A 1 19  ? 17.784 -7.756  -10.180 1.00 29.10  ? 19  ASN A N    1 
ATOM   273  C CA   . ASN A 1 19  ? 18.684 -6.630  -10.363 1.00 28.00  ? 19  ASN A CA   1 
ATOM   274  C C    . ASN A 1 19  ? 18.985 -6.403  -11.834 1.00 30.62  ? 19  ASN A C    1 
ATOM   275  O O    . ASN A 1 19  ? 19.029 -5.257  -12.292 1.00 32.84  ? 19  ASN A O    1 
ATOM   276  C CB   . ASN A 1 19  ? 19.974 -6.830  -9.584  1.00 29.63  ? 19  ASN A CB   1 
ATOM   277  C CG   . ASN A 1 19  ? 20.564 -5.506  -9.162  1.00 38.85  ? 19  ASN A CG   1 
ATOM   278  O OD1  . ASN A 1 19  ? 20.306 -4.996  -8.064  1.00 40.35  ? 19  ASN A OD1  1 
ATOM   279  N ND2  . ASN A 1 19  ? 21.336 -4.918  -10.056 1.00 44.70  ? 19  ASN A ND2  1 
ATOM   280  H H    . ASN A 1 19  ? 18.130 -8.432  -9.775  1.00 35.06  ? 19  ASN A H    1 
ATOM   281  H HA   . ASN A 1 19  ? 18.250 -5.838  -10.009 1.00 33.74  ? 19  ASN A HA   1 
ATOM   282  H HB2  . ASN A 1 19  ? 19.793 -7.353  -8.788  1.00 35.69  ? 19  ASN A HB2  1 
ATOM   283  H HB3  . ASN A 1 19  ? 20.620 -7.289  -10.143 1.00 35.69  ? 19  ASN A HB3  1 
ATOM   284  H HD21 . ASN A 1 19  ? 21.702 -4.161  -9.877  1.00 53.78  ? 19  ASN A HD21 1 
ATOM   285  H HD22 . ASN A 1 19  ? 21.473 -5.293  -10.818 1.00 53.78  ? 19  ASN A HD22 1 
ATOM   286  N N    . VAL A 1 20  ? 19.169 -7.478  -12.606 1.00 28.43  ? 20  VAL A N    1 
ATOM   287  C CA   . VAL A 1 20  ? 19.372 -7.299  -14.043 1.00 28.34  ? 20  VAL A CA   1 
ATOM   288  C C    . VAL A 1 20  ? 18.204 -6.544  -14.656 1.00 28.82  ? 20  VAL A C    1 
ATOM   289  O O    . VAL A 1 20  ? 18.394 -5.645  -15.484 1.00 29.82  ? 20  VAL A O    1 
ATOM   290  C CB   . VAL A 1 20  ? 19.561 -8.649  -14.747 1.00 29.64  ? 20  VAL A CB   1 
ATOM   291  C CG1  . VAL A 1 20  ? 19.578 -8.484  -16.275 1.00 31.70  ? 20  VAL A CG1  1 
ATOM   292  C CG2  . VAL A 1 20  ? 20.832 -9.346  -14.281 1.00 30.05  ? 20  VAL A CG2  1 
ATOM   293  H H    . VAL A 1 20  ? 19.179 -8.292  -12.331 1.00 34.25  ? 20  VAL A H    1 
ATOM   294  H HA   . VAL A 1 20  ? 20.181 -6.777  -14.159 1.00 34.14  ? 20  VAL A HA   1 
ATOM   295  H HB   . VAL A 1 20  ? 18.806 -9.209  -14.510 1.00 35.71  ? 20  VAL A HB   1 
ATOM   296  H HG11 . VAL A 1 20  ? 19.902 -9.305  -16.678 1.00 38.18  ? 20  VAL A HG11 1 
ATOM   297  H HG12 . VAL A 1 20  ? 18.676 -8.300  -16.583 1.00 38.18  ? 20  VAL A HG12 1 
ATOM   298  H HG13 . VAL A 1 20  ? 20.164 -7.747  -16.508 1.00 38.18  ? 20  VAL A HG13 1 
ATOM   299  H HG21 . VAL A 1 20  ? 20.850 -10.245 -14.645 1.00 36.19  ? 20  VAL A HG21 1 
ATOM   300  H HG22 . VAL A 1 20  ? 21.601 -8.846  -14.597 1.00 36.19  ? 20  VAL A HG22 1 
ATOM   301  H HG23 . VAL A 1 20  ? 20.836 -9.381  -13.312 1.00 36.19  ? 20  VAL A HG23 1 
ATOM   302  N N    . LEU A 1 21  ? 16.969 -6.944  -14.318 1.00 27.70  ? 21  LEU A N    1 
ATOM   303  C CA   . LEU A 1 21  ? 15.794 -6.311  -14.907 1.00 25.40  ? 21  LEU A CA   1 
ATOM   304  C C    . LEU A 1 21  ? 15.633 -4.882  -14.412 1.00 28.84  ? 21  LEU A C    1 
ATOM   305  O O    . LEU A 1 21  ? 15.039 -4.045  -15.118 1.00 28.00  ? 21  LEU A O    1 
ATOM   306  C CB   . LEU A 1 21  ? 14.558 -7.125  -14.574 1.00 28.05  ? 21  LEU A CB   1 
ATOM   307  C CG   . LEU A 1 21  ? 14.545 -8.465  -15.270 1.00 26.07  ? 21  LEU A CG   1 
ATOM   308  C CD1  . LEU A 1 21  ? 13.267 -9.217  -14.865 1.00 28.56  ? 21  LEU A CD1  1 
ATOM   309  C CD2  . LEU A 1 21  ? 14.556 -8.332  -16.780 1.00 29.69  ? 21  LEU A CD2  1 
ATOM   310  H H    . LEU A 1 21  ? 16.793 -7.572  -13.757 1.00 33.37  ? 21  LEU A H    1 
ATOM   311  H HA   . LEU A 1 21  ? 15.891 -6.288  -15.871 1.00 30.62  ? 21  LEU A HA   1 
ATOM   312  H HB2  . LEU A 1 21  ? 14.529 -7.281  -13.618 1.00 33.80  ? 21  LEU A HB2  1 
ATOM   313  H HB3  . LEU A 1 21  ? 13.770 -6.632  -14.854 1.00 33.80  ? 21  LEU A HB3  1 
ATOM   314  H HG   . LEU A 1 21  ? 15.343 -8.950  -15.008 1.00 31.42  ? 21  LEU A HG   1 
ATOM   315  H HD11 . LEU A 1 21  ? 13.248 -10.074 -15.319 1.00 34.41  ? 21  LEU A HD11 1 
ATOM   316  H HD12 . LEU A 1 21  ? 13.270 -9.351  -13.905 1.00 34.41  ? 21  LEU A HD12 1 
ATOM   317  H HD13 . LEU A 1 21  ? 12.495 -8.690  -15.123 1.00 34.41  ? 21  LEU A HD13 1 
ATOM   318  H HD21 . LEU A 1 21  ? 14.316 -9.185  -17.174 1.00 35.76  ? 21  LEU A HD21 1 
ATOM   319  H HD22 . LEU A 1 21  ? 13.913 -7.654  -17.042 1.00 35.76  ? 21  LEU A HD22 1 
ATOM   320  H HD23 . LEU A 1 21  ? 15.445 -8.073  -17.068 1.00 35.76  ? 21  LEU A HD23 1 
ATOM   321  N N    . LYS A 1 22  ? 16.201 -4.579  -13.235 1.00 29.34  ? 22  LYS A N    1 
ATOM   322  C CA   . LYS A 1 22  ? 16.196 -3.199  -12.764 1.00 32.92  ? 22  LYS A CA   1 
ATOM   323  C C    . LYS A 1 22  ? 17.047 -2.341  -13.669 1.00 32.98  ? 22  LYS A C    1 
ATOM   324  O O    . LYS A 1 22  ? 16.704 -1.185  -13.920 1.00 39.23  ? 22  LYS A O    1 
ATOM   325  C CB   . LYS A 1 22  ? 16.674 -3.152  -11.324 1.00 33.54  ? 22  LYS A CB   1 
ATOM   326  C CG   . LYS A 1 22  ? 16.989 -1.780  -10.769 1.00 38.52  ? 22  LYS A CG   1 
ATOM   327  C CD   . LYS A 1 22  ? 17.805 -1.952  -9.508  1.00 41.00  ? 22  LYS A CD   1 
ATOM   328  C CE   . LYS A 1 22  ? 18.559 -0.697  -9.117  1.00 47.06  ? 22  LYS A CE   1 
ATOM   329  N NZ   . LYS A 1 22  ? 19.303 -0.958  -7.858  1.00 58.54  ? 22  LYS A NZ   1 
ATOM   330  H H    . LYS A 1 22  ? 16.584 -5.142  -12.709 1.00 35.34  ? 22  LYS A H    1 
ATOM   331  H HA   . LYS A 1 22  ? 15.296 -2.836  -12.771 1.00 39.63  ? 22  LYS A HA   1 
ATOM   332  H HB2  . LYS A 1 22  ? 15.981 -3.534  -10.763 1.00 40.38  ? 22  LYS A HB2  1 
ATOM   333  H HB3  . LYS A 1 22  ? 17.484 -3.680  -11.257 1.00 40.38  ? 22  LYS A HB3  1 
ATOM   334  H HG2  . LYS A 1 22  ? 17.503 -1.269  -11.413 1.00 46.36  ? 22  LYS A HG2  1 
ATOM   335  H HG3  . LYS A 1 22  ? 16.167 -1.310  -10.554 1.00 46.36  ? 22  LYS A HG3  1 
ATOM   336  H HD2  . LYS A 1 22  ? 17.211 -2.184  -8.777  1.00 49.33  ? 22  LYS A HD2  1 
ATOM   337  H HD3  . LYS A 1 22  ? 18.454 -2.660  -9.646  1.00 49.33  ? 22  LYS A HD3  1 
ATOM   338  H HE2  . LYS A 1 22  ? 19.191 -0.459  -9.814  1.00 56.61  ? 22  LYS A HE2  1 
ATOM   339  H HE3  . LYS A 1 22  ? 17.936 0.032   -8.971  1.00 56.61  ? 22  LYS A HE3  1 
ATOM   340  H HZ1  . LYS A 1 22  ? 19.692 -0.209  -7.574  1.00 70.38  ? 22  LYS A HZ1  1 
ATOM   341  H HZ2  . LYS A 1 22  ? 18.744 -1.249  -7.230  1.00 70.38  ? 22  LYS A HZ2  1 
ATOM   342  H HZ3  . LYS A 1 22  ? 19.929 -1.574  -7.997  1.00 70.38  ? 22  LYS A HZ3  1 
ATOM   343  N N    . GLN A 1 23  ? 18.113 -2.900  -14.214 1.00 32.05  ? 23  GLN A N    1 
ATOM   344  C CA   . GLN A 1 23  ? 18.960 -2.152  -15.137 1.00 31.33  ? 23  GLN A CA   1 
ATOM   345  C C    . GLN A 1 23  ? 18.255 -1.917  -16.467 1.00 33.84  ? 23  GLN A C    1 
ATOM   346  O O    . GLN A 1 23  ? 18.616 -0.983  -17.182 1.00 37.96  ? 23  GLN A O    1 
ATOM   347  C CB   . GLN A 1 23  ? 20.276 -2.890  -15.364 1.00 30.80  ? 23  GLN A CB   1 
ATOM   348  C CG   . GLN A 1 23  ? 20.989 -3.315  -14.082 1.00 35.77  ? 23  GLN A CG   1 
ATOM   349  C CD   . GLN A 1 23  ? 21.077 -2.226  -13.040 1.00 42.20  ? 23  GLN A CD   1 
ATOM   350  O OE1  . GLN A 1 23  ? 20.876 -2.477  -11.852 1.00 46.48  ? 23  GLN A OE1  1 
ATOM   351  N NE2  . GLN A 1 23  ? 21.385 -1.016  -13.470 1.00 39.73  ? 23  GLN A NE2  1 
ATOM   352  H H    . GLN A 1 23  ? 18.371 -3.707  -14.069 1.00 38.59  ? 23  GLN A H    1 
ATOM   353  H HA   . GLN A 1 23  ? 19.177 -1.291  -14.747 1.00 37.73  ? 23  GLN A HA   1 
ATOM   354  H HB2  . GLN A 1 23  ? 20.097 -3.692  -15.879 1.00 37.10  ? 23  GLN A HB2  1 
ATOM   355  H HB3  . GLN A 1 23  ? 20.877 -2.308  -15.855 1.00 37.10  ? 23  GLN A HB3  1 
ATOM   356  H HG2  . GLN A 1 23  ? 20.507 -4.059  -13.690 1.00 43.06  ? 23  GLN A HG2  1 
ATOM   357  H HG3  . GLN A 1 23  ? 21.894 -3.585  -14.304 1.00 43.06  ? 23  GLN A HG3  1 
ATOM   358  H HE21 . GLN A 1 23  ? 21.524 -0.879  -14.308 1.00 47.81  ? 23  GLN A HE21 1 
ATOM   359  H HE22 . GLN A 1 23  ? 21.447 -0.365  -12.912 1.00 47.81  ? 23  GLN A HE22 1 
ATOM   360  N N    . GLY A 1 24  ? 17.265 -2.729  -16.805 1.00 30.09  ? 24  GLY A N    1 
ATOM   361  C CA   . GLY A 1 24  ? 16.466 -2.541  -17.996 1.00 28.53  ? 24  GLY A CA   1 
ATOM   362  C C    . GLY A 1 24  ? 15.814 -3.835  -18.436 1.00 26.81  ? 24  GLY A C    1 
ATOM   363  O O    . GLY A 1 24  ? 16.291 -4.936  -18.130 1.00 27.49  ? 24  GLY A O    1 
ATOM   364  H H    . GLY A 1 24  ? 17.031 -3.417  -16.345 1.00 36.25  ? 24  GLY A H    1 
ATOM   365  H HA2  . GLY A 1 24  ? 15.770 -1.888  -17.820 1.00 34.37  ? 24  GLY A HA2  1 
ATOM   366  H HA3  . GLY A 1 24  ? 17.028 -2.216  -18.716 1.00 34.37  ? 24  GLY A HA3  1 
ATOM   367  N N    . ASP A 1 25  ? 14.747 -3.674  -19.229 1.00 28.02  ? 25  ASP A N    1 
ATOM   368  C CA   . ASP A 1 25  ? 14.042 -4.835  -19.778 1.00 27.56  ? 25  ASP A CA   1 
ATOM   369  C C    . ASP A 1 25  ? 15.048 -5.689  -20.547 1.00 26.36  ? 25  ASP A C    1 
ATOM   370  O O    . ASP A 1 25  ? 16.018 -5.166  -21.115 1.00 27.07  ? 25  ASP A O    1 
ATOM   371  C CB   . ASP A 1 25  ? 12.887 -4.451  -20.721 1.00 26.25  ? 25  ASP A CB   1 
ATOM   372  C CG   . ASP A 1 25  ? 11.874 -3.517  -20.091 1.00 28.37  ? 25  ASP A CG   1 
ATOM   373  O OD1  . ASP A 1 25  ? 12.024 -3.175  -18.892 1.00 28.45  ? 25  ASP A OD1  1 
ATOM   374  O OD2  . ASP A 1 25  ? 10.912 -3.157  -20.823 1.00 27.90  ? 25  ASP A OD2  1 
ATOM   375  H H    . ASP A 1 25  ? 14.417 -2.914  -19.460 1.00 33.76  ? 25  ASP A H    1 
ATOM   376  H HA   . ASP A 1 25  ? 13.641 -5.329  -19.046 1.00 33.21  ? 25  ASP A HA   1 
ATOM   377  H HB2  . ASP A 1 25  ? 13.255 -4.006  -21.501 1.00 31.64  ? 25  ASP A HB2  1 
ATOM   378  H HB3  . ASP A 1 25  ? 12.421 -5.258  -20.989 1.00 31.64  ? 25  ASP A HB3  1 
ATOM   379  N N    . ASN A 1 26  ? 14.826 -7.003  -20.584 1.00 25.60  ? 26  ASN A N    1 
ATOM   380  C CA   . ASN A 1 26  ? 15.840 -7.886  -21.161 1.00 27.44  ? 26  ASN A CA   1 
ATOM   381  C C    . ASN A 1 26  ? 15.191 -9.216  -21.498 1.00 27.31  ? 26  ASN A C    1 
ATOM   382  O O    . ASN A 1 26  ? 14.071 -9.515  -21.079 1.00 26.47  ? 26  ASN A O    1 
ATOM   383  C CB   . ASN A 1 26  ? 17.055 -8.045  -20.210 1.00 27.49  ? 26  ASN A CB   1 
ATOM   384  C CG   . ASN A 1 26  ? 18.384 -8.160  -20.945 1.00 28.39  ? 26  ASN A CG   1 
ATOM   385  O OD1  . ASN A 1 26  ? 18.459 -8.671  -22.063 1.00 28.53  ? 26  ASN A OD1  1 
ATOM   386  N ND2  . ASN A 1 26  ? 19.424 -7.655  -20.317 1.00 31.72  ? 26  ASN A ND2  1 
ATOM   387  H H    . ASN A 1 26  ? 14.119 -7.396  -20.291 1.00 30.86  ? 26  ASN A H    1 
ATOM   388  H HA   . ASN A 1 26  ? 16.169 -7.509  -21.992 1.00 33.06  ? 26  ASN A HA   1 
ATOM   389  H HB2  . ASN A 1 26  ? 17.102 -7.269  -19.629 1.00 33.12  ? 26  ASN A HB2  1 
ATOM   390  H HB3  . ASN A 1 26  ? 16.936 -8.849  -19.680 1.00 33.12  ? 26  ASN A HB3  1 
ATOM   391  H HD21 . ASN A 1 26  ? 20.203 -7.689  -20.680 1.00 38.20  ? 26  ASN A HD21 1 
ATOM   392  H HD22 . ASN A 1 26  ? 19.324 -7.291  -19.544 1.00 38.20  ? 26  ASN A HD22 1 
ATOM   393  N N    . TYR A 1 27  ? 15.918 -10.032 -22.258 1.00 26.54  ? 27  TYR A N    1 
ATOM   394  C CA   . TYR A 1 27  ? 15.459 -11.331 -22.703 1.00 27.71  ? 27  TYR A CA   1 
ATOM   395  C C    . TYR A 1 27  ? 16.413 -12.389 -22.173 1.00 30.21  ? 27  TYR A C    1 
ATOM   396  O O    . TYR A 1 27  ? 17.527 -12.073 -21.734 1.00 26.14  ? 27  TYR A O    1 
ATOM   397  C CB   . TYR A 1 27  ? 15.356 -11.383 -24.247 1.00 31.16  ? 27  TYR A CB   1 
ATOM   398  C CG   . TYR A 1 27  ? 16.668 -11.212 -24.985 1.00 32.43  ? 27  TYR A CG   1 
ATOM   399  C CD1  . TYR A 1 27  ? 17.216 -9.949  -25.203 1.00 36.31  ? 27  TYR A CD1  1 
ATOM   400  C CD2  . TYR A 1 27  ? 17.329 -12.309 -25.505 1.00 38.82  ? 27  TYR A CD2  1 
ATOM   401  C CE1  . TYR A 1 27  ? 18.402 -9.802  -25.902 1.00 41.75  ? 27  TYR A CE1  1 
ATOM   402  C CE2  . TYR A 1 27  ? 18.506 -12.170 -26.196 1.00 40.63  ? 27  TYR A CE2  1 
ATOM   403  C CZ   . TYR A 1 27  ? 19.043 -10.928 -26.392 1.00 43.55  ? 27  TYR A CZ   1 
ATOM   404  O OH   . TYR A 1 27  ? 20.224 -10.809 -27.091 1.00 51.58  ? 27  TYR A OH   1 
ATOM   405  H H    . TYR A 1 27  ? 16.709 -9.842  -22.536 1.00 31.98  ? 27  TYR A H    1 
ATOM   406  H HA   . TYR A 1 27  ? 14.575 -11.525 -22.355 1.00 33.39  ? 27  TYR A HA   1 
ATOM   407  H HB2  . TYR A 1 27  ? 14.990 -12.244 -24.501 1.00 37.52  ? 27  TYR A HB2  1 
ATOM   408  H HB3  . TYR A 1 27  ? 14.764 -10.672 -24.539 1.00 37.52  ? 27  TYR A HB3  1 
ATOM   409  H HD1  . TYR A 1 27  ? 16.779 -9.196  -24.875 1.00 43.70  ? 27  TYR A HD1  1 
ATOM   410  H HD2  . TYR A 1 27  ? 16.968 -13.157 -25.383 1.00 46.72  ? 27  TYR A HD2  1 
ATOM   411  H HE1  . TYR A 1 27  ? 18.764 -8.956  -26.041 1.00 50.23  ? 27  TYR A HE1  1 
ATOM   412  H HE2  . TYR A 1 27  ? 18.939 -12.922 -26.531 1.00 48.89  ? 27  TYR A HE2  1 
ATOM   413  H HH   . TYR A 1 27  ? 20.404 -9.998  -27.215 1.00 62.03  ? 27  TYR A HH   1 
ATOM   414  N N    . VAL A 1 28  ? 15.964 -13.647 -22.195 1.00 29.56  ? 28  VAL A N    1 
ATOM   415  C CA   . VAL A 1 28  ? 16.678 -14.681 -21.431 1.00 26.17  ? 28  VAL A CA   1 
ATOM   416  C C    . VAL A 1 28  ? 18.149 -14.761 -21.835 1.00 28.56  ? 28  VAL A C    1 
ATOM   417  O O    . VAL A 1 28  ? 19.044 -14.786 -20.975 1.00 27.00  ? 28  VAL A O    1 
ATOM   418  C CB   . VAL A 1 28  ? 15.973 -16.043 -21.568 1.00 24.03  ? 28  VAL A CB   1 
ATOM   419  C CG1  . VAL A 1 28  ? 16.846 -17.187 -21.118 1.00 30.02  ? 28  VAL A CG1  1 
ATOM   420  C CG2  . VAL A 1 28  ? 14.697 -16.024 -20.786 1.00 33.11  ? 28  VAL A CG2  1 
ATOM   421  H H    . VAL A 1 28  ? 15.274 -13.921 -22.628 1.00 35.61  ? 28  VAL A H    1 
ATOM   422  H HA   . VAL A 1 28  ? 16.653 -14.423 -20.496 1.00 31.54  ? 28  VAL A HA   1 
ATOM   423  H HB   . VAL A 1 28  ? 15.780 -16.192 -22.507 1.00 28.97  ? 28  VAL A HB   1 
ATOM   424  H HG11 . VAL A 1 28  ? 16.316 -17.999 -21.097 1.00 36.16  ? 28  VAL A HG11 1 
ATOM   425  H HG12 . VAL A 1 28  ? 17.581 -17.288 -21.742 1.00 36.16  ? 28  VAL A HG12 1 
ATOM   426  H HG13 . VAL A 1 28  ? 17.188 -16.993 -20.231 1.00 36.16  ? 28  VAL A HG13 1 
ATOM   427  H HG21 . VAL A 1 28  ? 14.439 -16.936 -20.581 1.00 39.87  ? 28  VAL A HG21 1 
ATOM   428  H HG22 . VAL A 1 28  ? 14.836 -15.527 -19.965 1.00 39.87  ? 28  VAL A HG22 1 
ATOM   429  H HG23 . VAL A 1 28  ? 14.007 -15.597 -21.318 1.00 39.87  ? 28  VAL A HG23 1 
ATOM   430  N N    . TYR A 1 29  ? 18.451 -14.853 -23.133 1.00 29.48  ? 29  TYR A N    1 
ATOM   431  C CA   . TYR A 1 29  ? 19.857 -15.034 -23.498 1.00 32.60  ? 29  TYR A CA   1 
ATOM   432  C C    . TYR A 1 29  ? 20.664 -13.799 -23.125 1.00 30.76  ? 29  TYR A C    1 
ATOM   433  O O    . TYR A 1 29  ? 21.835 -13.889 -22.718 1.00 33.88  ? 29  TYR A O    1 
ATOM   434  C CB   . TYR A 1 29  ? 20.001 -15.298 -24.991 1.00 36.45  ? 29  TYR A CB   1 
ATOM   435  C CG   . TYR A 1 29  ? 19.296 -16.524 -25.477 1.00 46.17  ? 29  TYR A CG   1 
ATOM   436  C CD1  . TYR A 1 29  ? 19.479 -17.755 -24.858 1.00 43.57  ? 29  TYR A CD1  1 
ATOM   437  C CD2  . TYR A 1 29  ? 18.424 -16.447 -26.554 1.00 55.54  ? 29  TYR A CD2  1 
ATOM   438  C CE1  . TYR A 1 29  ? 18.815 -18.879 -25.310 1.00 50.03  ? 29  TYR A CE1  1 
ATOM   439  C CE2  . TYR A 1 29  ? 17.759 -17.560 -27.014 1.00 53.08  ? 29  TYR A CE2  1 
ATOM   440  C CZ   . TYR A 1 29  ? 17.955 -18.774 -26.390 1.00 59.13  ? 29  TYR A CZ   1 
ATOM   441  O OH   . TYR A 1 29  ? 17.290 -19.891 -26.849 1.00 65.08  ? 29  TYR A OH   1 
ATOM   442  H H    . TYR A 1 29  ? 17.893 -14.815 -23.786 1.00 35.52  ? 29  TYR A H    1 
ATOM   443  H HA   . TYR A 1 29  ? 20.201 -15.806 -23.021 1.00 39.25  ? 29  TYR A HA   1 
ATOM   444  H HB2  . TYR A 1 29  ? 19.637 -14.540 -25.474 1.00 43.87  ? 29  TYR A HB2  1 
ATOM   445  H HB3  . TYR A 1 29  ? 20.943 -15.402 -25.196 1.00 43.87  ? 29  TYR A HB3  1 
ATOM   446  H HD1  . TYR A 1 29  ? 20.055 -17.823 -24.131 1.00 52.42  ? 29  TYR A HD1  1 
ATOM   447  H HD2  . TYR A 1 29  ? 18.287 -15.628 -26.973 1.00 66.79  ? 29  TYR A HD2  1 
ATOM   448  H HE1  . TYR A 1 29  ? 18.946 -19.700 -24.893 1.00 60.17  ? 29  TYR A HE1  1 
ATOM   449  H HE2  . TYR A 1 29  ? 17.182 -17.494 -27.740 1.00 63.83  ? 29  TYR A HE2  1 
ATOM   450  H HH   . TYR A 1 29  ? 17.493 -20.559 -26.382 1.00 78.24  ? 29  TYR A HH   1 
ATOM   451  N N    . GLY A 1 30  ? 20.055 -12.625 -23.269 1.00 30.85  ? 30  GLY A N    1 
ATOM   452  C CA   . GLY A 1 30  ? 20.723 -11.403 -22.900 1.00 28.97  ? 30  GLY A CA   1 
ATOM   453  C C    . GLY A 1 30  ? 21.054 -11.341 -21.425 1.00 29.09  ? 30  GLY A C    1 
ATOM   454  O O    . GLY A 1 30  ? 22.129 -10.878 -21.041 1.00 27.44  ? 30  GLY A O    1 
ATOM   455  H H    . GLY A 1 30  ? 19.259 -12.518 -23.576 1.00 37.15  ? 30  GLY A H    1 
ATOM   456  H HA2  . GLY A 1 30  ? 21.551 -11.327 -23.401 1.00 34.90  ? 30  GLY A HA2  1 
ATOM   457  H HA3  . GLY A 1 30  ? 20.153 -10.649 -23.116 1.00 34.90  ? 30  GLY A HA3  1 
ATOM   458  N N    . ILE A 1 31  ? 20.133 -11.802 -20.578 1.00 27.22  ? 31  ILE A N    1 
ATOM   459  C CA   . ILE A 1 31  ? 20.366 -11.857 -19.135 1.00 24.56  ? 31  ILE A CA   1 
ATOM   460  C C    . ILE A 1 31  ? 21.487 -12.832 -18.814 1.00 28.09  ? 31  ILE A C    1 
ATOM   461  O O    . ILE A 1 31  ? 22.363 -12.560 -17.979 1.00 26.16  ? 31  ILE A O    1 
ATOM   462  C CB   . ILE A 1 31  ? 19.044 -12.231 -18.437 1.00 27.34  ? 31  ILE A CB   1 
ATOM   463  C CG1  . ILE A 1 31  ? 18.017 -11.147 -18.652 1.00 24.70  ? 31  ILE A CG1  1 
ATOM   464  C CG2  . ILE A 1 31  ? 19.237 -12.468 -16.962 1.00 28.84  ? 31  ILE A CG2  1 
ATOM   465  C CD1  . ILE A 1 31  ? 16.604 -11.604 -18.352 1.00 26.68  ? 31  ILE A CD1  1 
ATOM   466  H H    . ILE A 1 31  ? 19.359 -12.091 -20.815 1.00 32.80  ? 31  ILE A H    1 
ATOM   467  H HA   . ILE A 1 31  ? 20.649 -10.987 -18.812 1.00 29.03  ? 31  ILE A HA   1 
ATOM   468  H HB   . ILE A 1 31  ? 18.731 -13.059 -18.834 1.00 32.94  ? 31  ILE A HB   1 
ATOM   469  H HG12 . ILE A 1 31  ? 18.221 -10.400 -18.068 1.00 29.77  ? 31  ILE A HG12 1 
ATOM   470  H HG13 . ILE A 1 31  ? 18.049 -10.862 -19.579 1.00 29.77  ? 31  ILE A HG13 1 
ATOM   471  H HG21 . ILE A 1 31  ? 18.383 -12.373 -16.513 1.00 34.74  ? 31  ILE A HG21 1 
ATOM   472  H HG22 . ILE A 1 31  ? 19.583 -13.365 -16.829 1.00 34.74  ? 31  ILE A HG22 1 
ATOM   473  H HG23 . ILE A 1 31  ? 19.867 -11.816 -16.618 1.00 34.74  ? 31  ILE A HG23 1 
ATOM   474  H HD11 . ILE A 1 31  ? 16.010 -10.838 -18.393 1.00 32.15  ? 31  ILE A HD11 1 
ATOM   475  H HD12 . ILE A 1 31  ? 16.339 -12.264 -19.011 1.00 32.15  ? 31  ILE A HD12 1 
ATOM   476  H HD13 . ILE A 1 31  ? 16.580 -11.994 -17.464 1.00 32.15  ? 31  ILE A HD13 1 
ATOM   477  N N    . ILE A 1 32  ? 21.474 -13.994 -19.455 1.00 27.69  ? 32  ILE A N    1 
ATOM   478  C CA   . ILE A 1 32  ? 22.531 -14.956 -19.206 1.00 28.65  ? 32  ILE A CA   1 
ATOM   479  C C    . ILE A 1 32  ? 23.878 -14.319 -19.520 1.00 31.35  ? 32  ILE A C    1 
ATOM   480  O O    . ILE A 1 32  ? 24.839 -14.415 -18.747 1.00 32.59  ? 32  ILE A O    1 
ATOM   481  C CB   . ILE A 1 32  ? 22.291 -16.241 -20.013 1.00 31.20  ? 32  ILE A CB   1 
ATOM   482  C CG1  . ILE A 1 32  ? 21.052 -16.944 -19.462 1.00 32.02  ? 32  ILE A CG1  1 
ATOM   483  C CG2  . ILE A 1 32  ? 23.557 -17.115 -19.922 1.00 33.78  ? 32  ILE A CG2  1 
ATOM   484  C CD1  . ILE A 1 32  ? 20.605 -18.109 -20.339 1.00 34.56  ? 32  ILE A CD1  1 
ATOM   485  H H    . ILE A 1 32  ? 20.879 -14.242 -20.023 1.00 33.36  ? 32  ILE A H    1 
ATOM   486  H HA   . ILE A 1 32  ? 22.528 -15.204 -18.269 1.00 34.51  ? 32  ILE A HA   1 
ATOM   487  H HB   . ILE A 1 32  ? 22.124 -16.049 -20.949 1.00 37.57  ? 32  ILE A HB   1 
ATOM   488  H HG12 . ILE A 1 32  ? 21.252 -17.291 -18.579 1.00 38.55  ? 32  ILE A HG12 1 
ATOM   489  H HG13 . ILE A 1 32  ? 20.323 -16.307 -19.412 1.00 38.55  ? 32  ILE A HG13 1 
ATOM   490  H HG21 . ILE A 1 32  ? 23.335 -18.022 -20.183 1.00 40.67  ? 32  ILE A HG21 1 
ATOM   491  H HG22 . ILE A 1 32  ? 24.233 -16.755 -20.518 1.00 40.67  ? 32  ILE A HG22 1 
ATOM   492  H HG23 . ILE A 1 32  ? 23.883 -17.104 -19.008 1.00 40.67  ? 32  ILE A HG23 1 
ATOM   493  H HD11 . ILE A 1 32  ? 19.746 -18.430 -20.024 1.00 41.61  ? 32  ILE A HD11 1 
ATOM   494  H HD12 . ILE A 1 32  ? 20.528 -17.802 -21.256 1.00 41.61  ? 32  ILE A HD12 1 
ATOM   495  H HD13 . ILE A 1 32  ? 21.264 -18.818 -20.282 1.00 41.61  ? 32  ILE A HD13 1 
ATOM   496  N N    . LYS A 1 33  ? 23.972 -13.659 -20.668 1.00 28.16  ? 33  LYS A N    1 
ATOM   497  C CA   . LYS A 1 33  ? 25.227 -13.025 -21.040 1.00 33.09  ? 33  LYS A CA   1 
ATOM   498  C C    . LYS A 1 33  ? 25.653 -11.998 -19.998 1.00 32.26  ? 33  LYS A C    1 
ATOM   499  O O    . LYS A 1 33  ? 26.825 -11.930 -19.617 1.00 31.35  ? 33  LYS A O    1 
ATOM   500  C CB   . LYS A 1 33  ? 25.096 -12.371 -22.417 1.00 37.42  ? 33  LYS A CB   1 
ATOM   501  C CG   . LYS A 1 33  ? 26.421 -11.763 -22.899 1.00 39.61  ? 33  LYS A CG   1 
ATOM   502  C CD   . LYS A 1 33  ? 26.332 -11.132 -24.289 1.00 52.19  ? 33  LYS A CD   1 
ATOM   503  C CE   . LYS A 1 33  ? 27.620 -10.366 -24.620 1.00 60.62  ? 33  LYS A CE   1 
ATOM   504  N NZ   . LYS A 1 33  ? 27.646 -9.772  -25.990 1.00 72.63  ? 33  LYS A NZ   1 
ATOM   505  H H    . LYS A 1 33  ? 23.335 -13.565 -21.238 1.00 33.88  ? 33  LYS A H    1 
ATOM   506  H HA   . LYS A 1 33  ? 25.916 -13.706 -21.092 1.00 39.84  ? 33  LYS A HA   1 
ATOM   507  H HB2  . LYS A 1 33  ? 24.817 -13.040 -23.061 1.00 45.04  ? 33  LYS A HB2  1 
ATOM   508  H HB3  . LYS A 1 33  ? 24.436 -11.661 -22.369 1.00 45.04  ? 33  LYS A HB3  1 
ATOM   509  H HG2  . LYS A 1 33  ? 26.694 -11.071 -22.277 1.00 47.66  ? 33  LYS A HG2  1 
ATOM   510  H HG3  . LYS A 1 33  ? 27.093 -12.462 -22.934 1.00 47.66  ? 33  LYS A HG3  1 
ATOM   511  H HD2  . LYS A 1 33  ? 26.207 -11.828 -24.953 1.00 62.76  ? 33  LYS A HD2  1 
ATOM   512  H HD3  . LYS A 1 33  ? 25.587 -10.511 -24.316 1.00 62.76  ? 33  LYS A HD3  1 
ATOM   513  H HE2  . LYS A 1 33  ? 27.722 -9.641  -23.984 1.00 72.88  ? 33  LYS A HE2  1 
ATOM   514  H HE3  . LYS A 1 33  ? 28.371 -10.976 -24.550 1.00 72.88  ? 33  LYS A HE3  1 
ATOM   515  H HZ1  . LYS A 1 33  ? 28.410 -9.333  -26.117 1.00 87.29  ? 33  LYS A HZ1  1 
ATOM   516  H HZ2  . LYS A 1 33  ? 27.577 -10.415 -26.602 1.00 87.29  ? 33  LYS A HZ2  1 
ATOM   517  H HZ3  . LYS A 1 33  ? 26.967 -9.206  -26.089 1.00 87.29  ? 33  LYS A HZ3  1 
ATOM   518  N N    . GLN A 1 34  ? 24.725 -11.158 -19.554 1.00 31.25  ? 34  GLN A N    1 
ATOM   519  C CA   . GLN A 1 34  ? 25.083 -10.108 -18.607 1.00 31.07  ? 34  GLN A CA   1 
ATOM   520  C C    . GLN A 1 34  ? 25.537 -10.688 -17.275 1.00 32.49  ? 34  GLN A C    1 
ATOM   521  O O    . GLN A 1 34  ? 26.444 -10.140 -16.626 1.00 28.53  ? 34  GLN A O    1 
ATOM   522  C CB   . GLN A 1 34  ? 23.909 -9.156  -18.386 1.00 30.50  ? 34  GLN A CB   1 
ATOM   523  C CG   . GLN A 1 34  ? 23.756 -8.039  -19.401 1.00 46.79  ? 34  GLN A CG   1 
ATOM   524  C CD   . GLN A 1 34  ? 22.895 -6.901  -18.876 1.00 48.26  ? 34  GLN A CD   1 
ATOM   525  O OE1  . GLN A 1 34  ? 22.834 -6.656  -17.666 1.00 49.44  ? 34  GLN A OE1  1 
ATOM   526  N NE2  . GLN A 1 34  ? 22.227 -6.199  -19.784 1.00 53.73  ? 34  GLN A NE2  1 
ATOM   527  H H    . GLN A 1 34  ? 23.895 -11.174 -19.779 1.00 37.63  ? 34  GLN A H    1 
ATOM   528  H HA   . GLN A 1 34  ? 25.816 -9.600  -18.989 1.00 37.41  ? 34  GLN A HA   1 
ATOM   529  H HB2  . GLN A 1 34  ? 23.090 -9.676  -18.405 1.00 36.74  ? 34  GLN A HB2  1 
ATOM   530  H HB3  . GLN A 1 34  ? 24.017 -8.740  -17.516 1.00 36.74  ? 34  GLN A HB3  1 
ATOM   531  H HG2  . GLN A 1 34  ? 24.631 -7.682  -19.617 1.00 56.28  ? 34  GLN A HG2  1 
ATOM   532  H HG3  . GLN A 1 34  ? 23.335 -8.392  -20.201 1.00 56.28  ? 34  GLN A HG3  1 
ATOM   533  H HE21 . GLN A 1 34  ? 22.296 -6.399  -20.618 1.00 64.61  ? 34  GLN A HE21 1 
ATOM   534  H HE22 . GLN A 1 34  ? 21.726 -5.545  -19.538 1.00 64.61  ? 34  GLN A HE22 1 
ATOM   535  N N    . VAL A 1 35  ? 24.906 -11.777 -16.828 1.00 30.59  ? 35  VAL A N    1 
ATOM   536  C CA   . VAL A 1 35  ? 25.315 -12.366 -15.558 1.00 28.44  ? 35  VAL A CA   1 
ATOM   537  C C    . VAL A 1 35  ? 26.637 -13.103 -15.698 1.00 31.44  ? 35  VAL A C    1 
ATOM   538  O O    . VAL A 1 35  ? 27.480 -13.059 -14.796 1.00 35.18  ? 35  VAL A O    1 
ATOM   539  C CB   . VAL A 1 35  ? 24.219 -13.290 -15.018 1.00 30.87  ? 35  VAL A CB   1 
ATOM   540  C CG1  . VAL A 1 35  ? 24.734 -14.063 -13.823 1.00 32.48  ? 35  VAL A CG1  1 
ATOM   541  C CG2  . VAL A 1 35  ? 22.990 -12.471 -14.627 1.00 32.21  ? 35  VAL A CG2  1 
ATOM   542  H H    . VAL A 1 35  ? 24.260 -12.179 -17.230 1.00 36.84  ? 35  VAL A H    1 
ATOM   543  H HA   . VAL A 1 35  ? 25.444 -11.643 -14.924 1.00 34.27  ? 35  VAL A HA   1 
ATOM   544  H HB   . VAL A 1 35  ? 23.964 -13.921 -15.709 1.00 37.17  ? 35  VAL A HB   1 
ATOM   545  H HG11 . VAL A 1 35  ? 23.981 -14.454 -13.351 1.00 39.12  ? 35  VAL A HG11 1 
ATOM   546  H HG12 . VAL A 1 35  ? 25.329 -14.764 -14.132 1.00 39.12  ? 35  VAL A HG12 1 
ATOM   547  H HG13 . VAL A 1 35  ? 25.213 -13.457 -13.237 1.00 39.12  ? 35  VAL A HG13 1 
ATOM   548  H HG21 . VAL A 1 35  ? 22.339 -13.058 -14.213 1.00 38.78  ? 35  VAL A HG21 1 
ATOM   549  H HG22 . VAL A 1 35  ? 23.257 -11.780 -14.001 1.00 38.78  ? 35  VAL A HG22 1 
ATOM   550  H HG23 . VAL A 1 35  ? 22.612 -12.068 -15.424 1.00 38.78  ? 35  VAL A HG23 1 
ATOM   551  N N    . LYS A 1 36  ? 26.873 -13.752 -16.835 1.00 32.36  ? 36  LYS A N    1 
ATOM   552  C CA   . LYS A 1 36  ? 28.179 -14.365 -17.053 1.00 34.22  ? 36  LYS A CA   1 
ATOM   553  C C    . LYS A 1 36  ? 29.285 -13.311 -16.976 1.00 35.34  ? 36  LYS A C    1 
ATOM   554  O O    . LYS A 1 36  ? 30.317 -13.501 -16.317 1.00 36.74  ? 36  LYS A O    1 
ATOM   555  C CB   . LYS A 1 36  ? 28.187 -15.088 -18.400 1.00 31.94  ? 36  LYS A CB   1 
ATOM   556  C CG   . LYS A 1 36  ? 29.480 -15.930 -18.686 1.00 37.86  ? 36  LYS A CG   1 
ATOM   557  C CD   . LYS A 1 36  ? 29.562 -16.279 -20.200 1.00 46.97  ? 36  LYS A CD   1 
ATOM   558  C CE   . LYS A 1 36  ? 30.424 -17.500 -20.524 1.00 56.84  ? 36  LYS A CE   1 
ATOM   559  N NZ   . LYS A 1 36  ? 31.731 -17.542 -19.827 1.00 64.60  ? 36  LYS A NZ   1 
ATOM   560  H H    . LYS A 1 36  ? 26.310 -13.850 -17.477 1.00 38.97  ? 36  LYS A H    1 
ATOM   561  H HA   . LYS A 1 36  ? 28.351 -15.025 -16.363 1.00 41.20  ? 36  LYS A HA   1 
ATOM   562  H HB2  . LYS A 1 36  ? 27.431 -15.696 -18.428 1.00 38.46  ? 36  LYS A HB2  1 
ATOM   563  H HB3  . LYS A 1 36  ? 28.107 -14.427 -19.105 1.00 38.46  ? 36  LYS A HB3  1 
ATOM   564  H HG2  . LYS A 1 36  ? 30.265 -15.416 -18.443 1.00 45.57  ? 36  LYS A HG2  1 
ATOM   565  H HG3  . LYS A 1 36  ? 29.452 -16.755 -18.177 1.00 45.57  ? 36  LYS A HG3  1 
ATOM   566  H HD2  . LYS A 1 36  ? 28.666 -16.460 -20.525 1.00 56.50  ? 36  LYS A HD2  1 
ATOM   567  H HD3  . LYS A 1 36  ? 29.939 -15.521 -20.672 1.00 56.50  ? 36  LYS A HD3  1 
ATOM   568  H HE2  . LYS A 1 36  ? 29.934 -18.298 -20.273 1.00 68.34  ? 36  LYS A HE2  1 
ATOM   569  H HE3  . LYS A 1 36  ? 30.602 -17.506 -21.478 1.00 68.34  ? 36  LYS A HE3  1 
ATOM   570  H HZ1  . LYS A 1 36  ? 32.196 -18.252 -20.095 1.00 77.66  ? 36  LYS A HZ1  1 
ATOM   571  H HZ2  . LYS A 1 36  ? 32.197 -16.806 -20.010 1.00 77.66  ? 36  LYS A HZ2  1 
ATOM   572  H HZ3  . LYS A 1 36  ? 31.606 -17.593 -18.948 1.00 77.66  ? 36  LYS A HZ3  1 
ATOM   573  N N    . GLU A 1 37  ? 29.072 -12.169 -17.622 1.00 36.04  ? 37  GLU A N    1 
ATOM   574  C CA   . GLU A 1 37  ? 30.084 -11.119 -17.604 1.00 34.98  ? 37  GLU A CA   1 
ATOM   575  C C    . GLU A 1 37  ? 30.297 -10.572 -16.204 1.00 33.34  ? 37  GLU A C    1 
ATOM   576  O O    . GLU A 1 37  ? 31.447 -10.408 -15.760 1.00 35.81  ? 37  GLU A O    1 
ATOM   577  C CB   . GLU A 1 37  ? 29.692 -9.985  -18.537 1.00 40.04  ? 37  GLU A CB   1 
ATOM   578  C CG   . GLU A 1 37  ? 29.837 -10.306 -19.989 1.00 44.01  ? 37  GLU A CG   1 
ATOM   579  C CD   . GLU A 1 37  ? 29.560 -9.100  -20.846 1.00 62.17  ? 37  GLU A CD   1 
ATOM   580  O OE1  . GLU A 1 37  ? 29.598 -7.969  -20.307 1.00 64.05  ? 37  GLU A OE1  1 
ATOM   581  O OE2  . GLU A 1 37  ? 29.281 -9.286  -22.048 1.00 63.69  ? 37  GLU A OE2  1 
ATOM   582  H H    . GLU A 1 37  ? 28.363 -11.980 -18.071 1.00 43.39  ? 37  GLU A H    1 
ATOM   583  H HA   . GLU A 1 37  ? 30.916 -11.506 -17.916 1.00 42.12  ? 37  GLU A HA   1 
ATOM   584  H HB2  . GLU A 1 37  ? 28.762 -9.759  -18.377 1.00 48.18  ? 37  GLU A HB2  1 
ATOM   585  H HB3  . GLU A 1 37  ? 30.256 -9.219  -18.348 1.00 48.18  ? 37  GLU A HB3  1 
ATOM   586  H HG2  . GLU A 1 37  ? 30.743 -10.604 -20.164 1.00 52.94  ? 37  GLU A HG2  1 
ATOM   587  H HG3  . GLU A 1 37  ? 29.206 -11.003 -20.228 1.00 52.94  ? 37  GLU A HG3  1 
ATOM   588  N N    . ALA A 1 38  ? 29.204 -10.218 -15.520 1.00 32.47  ? 38  ALA A N    1 
ATOM   589  C CA   . ALA A 1 38  ? 29.275 -9.589  -14.202 1.00 29.88  ? 38  ALA A CA   1 
ATOM   590  C C    . ALA A 1 38  ? 29.843 -10.523 -13.147 1.00 33.51  ? 38  ALA A C    1 
ATOM   591  O O    . ALA A 1 38  ? 30.331 -10.049 -12.110 1.00 39.20  ? 38  ALA A O    1 
ATOM   592  C CB   . ALA A 1 38  ? 27.895 -9.091  -13.773 1.00 33.10  ? 38  ALA A CB   1 
ATOM   593  H H    . ALA A 1 38  ? 28.400 -10.335 -15.801 1.00 39.10  ? 38  ALA A H    1 
ATOM   594  H HA   . ALA A 1 38  ? 29.858 -8.817  -14.261 1.00 35.99  ? 38  ALA A HA   1 
ATOM   595  H HB1  . ALA A 1 38  ? 27.955 -8.729  -12.875 1.00 39.86  ? 38  ALA A HB1  1 
ATOM   596  H HB2  . ALA A 1 38  ? 27.603 -8.400  -14.388 1.00 39.86  ? 38  ALA A HB2  1 
ATOM   597  H HB3  . ALA A 1 38  ? 27.272 -9.834  -13.789 1.00 39.86  ? 38  ALA A HB3  1 
ATOM   598  N N    . SER A 1 39  ? 29.809 -11.832 -13.393 1.00 33.91  ? 39  SER A N    1 
ATOM   599  C CA   . SER A 1 39  ? 30.398 -12.802 -12.489 1.00 35.57  ? 39  SER A CA   1 
ATOM   600  C C    . SER A 1 39  ? 31.798 -13.240 -12.921 1.00 37.77  ? 39  SER A C    1 
ATOM   601  O O    . SER A 1 39  ? 32.376 -14.142 -12.298 1.00 40.45  ? 39  SER A O    1 
ATOM   602  C CB   . SER A 1 39  ? 29.494 -14.024 -12.373 1.00 38.33  ? 39  SER A CB   1 
ATOM   603  O OG   . SER A 1 39  ? 29.520 -14.771 -13.568 1.00 39.64  ? 39  SER A OG   1 
ATOM   604  H H    . SER A 1 39  ? 29.443 -12.182 -14.088 1.00 40.82  ? 39  SER A H    1 
ATOM   605  H HA   . SER A 1 39  ? 30.471 -12.401 -11.609 1.00 42.82  ? 39  SER A HA   1 
ATOM   606  H HB2  . SER A 1 39  ? 29.806 -14.582 -11.643 1.00 46.13  ? 39  SER A HB2  1 
ATOM   607  H HB3  . SER A 1 39  ? 28.585 -13.731 -12.202 1.00 46.13  ? 39  SER A HB3  1 
ATOM   608  H HG   . SER A 1 39  ? 29.395 -14.265 -14.227 1.00 47.70  ? 39  SER A HG   1 
ATOM   609  N N    . ASN A 1 40  ? 32.358 -12.606 -13.955 1.00 33.25  ? 40  ASN A N    1 
ATOM   610  C CA   . ASN A 1 40  ? 33.671 -12.953 -14.504 1.00 40.28  ? 40  ASN A CA   1 
ATOM   611  C C    . ASN A 1 40  ? 33.747 -14.411 -14.954 1.00 49.50  ? 40  ASN A C    1 
ATOM   612  O O    . ASN A 1 40  ? 34.757 -15.094 -14.742 1.00 43.54  ? 40  ASN A O    1 
ATOM   613  C CB   . ASN A 1 40  ? 34.760 -12.652 -13.483 1.00 43.78  ? 40  ASN A CB   1 
ATOM   614  C CG   . ASN A 1 40  ? 34.698 -11.235 -12.977 1.00 43.39  ? 40  ASN A CG   1 
ATOM   615  O OD1  . ASN A 1 40  ? 34.401 -10.299 -13.729 1.00 41.84  ? 40  ASN A OD1  1 
ATOM   616  N ND2  . ASN A 1 40  ? 34.960 -11.062 -11.685 1.00 42.70  ? 40  ASN A ND2  1 
ATOM   617  H H    . ASN A 1 40  ? 31.985 -11.950 -14.368 1.00 40.04  ? 40  ASN A H    1 
ATOM   618  H HA   . ASN A 1 40  ? 33.817 -12.415 -15.298 1.00 48.47  ? 40  ASN A HA   1 
ATOM   619  H HB2  . ASN A 1 40  ? 34.657 -13.247 -12.724 1.00 52.67  ? 40  ASN A HB2  1 
ATOM   620  H HB3  . ASN A 1 40  ? 35.627 -12.787 -13.895 1.00 52.67  ? 40  ASN A HB3  1 
ATOM   621  H HD21 . ASN A 1 40  ? 34.939 -10.273 -11.343 1.00 51.38  ? 40  ASN A HD21 1 
ATOM   622  H HD22 . ASN A 1 40  ? 35.151 -11.739 -11.190 1.00 51.38  ? 40  ASN A HD22 1 
ATOM   623  N N    . GLY A 1 41  ? 32.700 -14.881 -15.622 1.00 43.31  ? 41  GLY A N    1 
ATOM   624  C CA   . GLY A 1 41  ? 32.616 -16.259 -16.044 1.00 45.41  ? 41  GLY A CA   1 
ATOM   625  C C    . GLY A 1 41  ? 32.088 -17.212 -15.002 1.00 42.90  ? 41  GLY A C    1 
ATOM   626  O O    . GLY A 1 41  ? 31.696 -18.333 -15.352 1.00 56.79  ? 41  GLY A O    1 
ATOM   627  H H    . GLY A 1 41  ? 32.017 -14.407 -15.843 1.00 52.10  ? 41  GLY A H    1 
ATOM   628  H HA2  . GLY A 1 41  ? 32.030 -16.312 -16.815 1.00 54.63  ? 41  GLY A HA2  1 
ATOM   629  H HA3  . GLY A 1 41  ? 33.502 -16.560 -16.299 1.00 54.63  ? 41  GLY A HA3  1 
ATOM   630  N N    . GLU A 1 42  ? 32.005 -16.787 -13.744 1.00 41.84  ? 42  GLU A N    1 
ATOM   631  C CA   . GLU A 1 42  ? 31.757 -17.728 -12.659 1.00 45.89  ? 42  GLU A CA   1 
ATOM   632  C C    . GLU A 1 42  ? 30.341 -18.290 -12.699 1.00 46.61  ? 42  GLU A C    1 
ATOM   633  O O    . GLU A 1 42  ? 30.143 -19.471 -12.405 1.00 49.12  ? 42  GLU A O    1 
ATOM   634  C CB   . GLU A 1 42  ? 32.041 -17.050 -11.314 1.00 53.86  ? 42  GLU A CB   1 
ATOM   635  C CG   . GLU A 1 42  ? 32.250 -17.996 -10.119 1.00 63.35  ? 42  GLU A CG   1 
ATOM   636  C CD   . GLU A 1 42  ? 33.370 -19.008 -10.309 1.00 76.94  ? 42  GLU A CD   1 
ATOM   637  O OE1  . GLU A 1 42  ? 34.258 -18.792 -11.166 1.00 73.37  ? 42  GLU A OE1  1 
ATOM   638  O OE2  . GLU A 1 42  ? 33.351 -20.036 -9.594  1.00 66.96  ? 42  GLU A OE2  1 
ATOM   639  H H    . GLU A 1 42  ? 32.088 -15.968 -13.495 1.00 50.34  ? 42  GLU A H    1 
ATOM   640  H HA   . GLU A 1 42  ? 32.362 -18.480 -12.756 1.00 55.20  ? 42  GLU A HA   1 
ATOM   641  H HB2  . GLU A 1 42  ? 32.848 -16.520 -11.406 1.00 64.77  ? 42  GLU A HB2  1 
ATOM   642  H HB3  . GLU A 1 42  ? 31.290 -16.476 -11.098 1.00 64.77  ? 42  GLU A HB3  1 
ATOM   643  H HG2  . GLU A 1 42  ? 32.464 -17.464 -9.337  1.00 76.15  ? 42  GLU A HG2  1 
ATOM   644  H HG3  . GLU A 1 42  ? 31.430 -18.492 -9.969  1.00 76.15  ? 42  GLU A HG3  1 
ATOM   645  N N    . MET A 1 43  ? 29.342 -17.474 -13.056 1.00 39.61  ? 43  MET A N    1 
ATOM   646  C CA   . MET A 1 43  ? 27.938 -17.877 -13.005 1.00 42.50  ? 43  MET A CA   1 
ATOM   647  C C    . MET A 1 43  ? 27.361 -17.901 -14.413 1.00 35.73  ? 43  MET A C    1 
ATOM   648  O O    . MET A 1 43  ? 27.103 -16.846 -15.003 1.00 40.02  ? 43  MET A O    1 
ATOM   649  C CB   . MET A 1 43  ? 27.142 -16.931 -12.113 1.00 36.72  ? 43  MET A CB   1 
ATOM   650  C CG   . MET A 1 43  ? 25.687 -17.339 -11.886 1.00 38.30  ? 43  MET A CG   1 
ATOM   651  S SD   . MET A 1 43  ? 24.907 -16.193 -10.747 1.00 39.82  ? 43  MET A SD   1 
ATOM   652  C CE   . MET A 1 43  ? 25.849 -16.506 -9.258  1.00 44.78  ? 43  MET A CE   1 
ATOM   653  H H    . MET A 1 43  ? 29.459 -16.670 -13.335 1.00 47.67  ? 43  MET A H    1 
ATOM   654  H HA   . MET A 1 43  ? 27.891 -18.774 -12.640 1.00 51.14  ? 43  MET A HA   1 
ATOM   655  H HB2  . MET A 1 43  ? 27.572 -16.891 -11.244 1.00 44.20  ? 43  MET A HB2  1 
ATOM   656  H HB3  . MET A 1 43  ? 27.138 -16.052 -12.522 1.00 44.20  ? 43  MET A HB3  1 
ATOM   657  H HG2  . MET A 1 43  ? 25.206 -17.319 -12.728 1.00 46.09  ? 43  MET A HG2  1 
ATOM   658  H HG3  . MET A 1 43  ? 25.652 -18.231 -11.505 1.00 46.09  ? 43  MET A HG3  1 
ATOM   659  H HE1  . MET A 1 43  ? 25.434 -16.037 -8.518  1.00 53.87  ? 43  MET A HE1  1 
ATOM   660  H HE2  . MET A 1 43  ? 25.855 -17.460 -9.084  1.00 53.87  ? 43  MET A HE2  1 
ATOM   661  H HE3  . MET A 1 43  ? 26.756 -16.187 -9.386  1.00 53.87  ? 43  MET A HE3  1 
ATOM   662  N N    . GLU A 1 44  ? 27.159 -19.108 -14.941 1.00 39.94  ? 44  GLU A N    1 
ATOM   663  C CA   . GLU A 1 44  ? 26.570 -19.341 -16.256 1.00 40.13  ? 44  GLU A CA   1 
ATOM   664  C C    . GLU A 1 44  ? 25.181 -19.912 -15.989 1.00 41.42  ? 44  GLU A C    1 
ATOM   665  O O    . GLU A 1 44  ? 25.028 -21.115 -15.750 1.00 38.46  ? 44  GLU A O    1 
ATOM   666  C CB   . GLU A 1 44  ? 27.424 -20.289 -17.095 1.00 40.75  ? 44  GLU A CB   1 
ATOM   667  C CG   . GLU A 1 44  ? 28.839 -19.786 -17.345 1.00 57.32  ? 44  GLU A CG   1 
ATOM   668  C CD   . GLU A 1 44  ? 29.483 -20.398 -18.586 1.00 69.73  ? 44  GLU A CD   1 
ATOM   669  O OE1  . GLU A 1 44  ? 28.744 -20.777 -19.524 1.00 58.61  ? 44  GLU A OE1  1 
ATOM   670  O OE2  . GLU A 1 44  ? 30.732 -20.489 -18.623 1.00 63.65  ? 44  GLU A OE2  1 
ATOM   671  H H    . GLU A 1 44  ? 27.366 -19.838 -14.536 1.00 48.06  ? 44  GLU A H    1 
ATOM   672  H HA   . GLU A 1 44  ? 26.500 -18.511 -16.752 1.00 48.29  ? 44  GLU A HA   1 
ATOM   673  H HB2  . GLU A 1 44  ? 27.490 -21.140 -16.634 1.00 49.03  ? 44  GLU A HB2  1 
ATOM   674  H HB3  . GLU A 1 44  ? 26.997 -20.412 -17.957 1.00 49.03  ? 44  GLU A HB3  1 
ATOM   675  H HG2  . GLU A 1 44  ? 28.814 -18.824 -17.465 1.00 68.92  ? 44  GLU A HG2  1 
ATOM   676  H HG3  . GLU A 1 44  ? 29.392 -20.010 -16.580 1.00 68.92  ? 44  GLU A HG3  1 
ATOM   677  N N    . LEU A 1 45  ? 24.176 -19.040 -15.981 1.00 35.23  ? 45  LEU A N    1 
ATOM   678  C CA   . LEU A 1 45  ? 22.828 -19.490 -15.707 1.00 35.89  ? 45  LEU A CA   1 
ATOM   679  C C    . LEU A 1 45  ? 22.292 -20.276 -16.894 1.00 33.94  ? 45  LEU A C    1 
ATOM   680  O O    . LEU A 1 45  ? 22.637 -20.014 -18.055 1.00 35.16  ? 45  LEU A O    1 
ATOM   681  C CB   . LEU A 1 45  ? 21.909 -18.309 -15.413 1.00 34.69  ? 45  LEU A CB   1 
ATOM   682  C CG   . LEU A 1 45  ? 22.287 -17.431 -14.212 1.00 36.07  ? 45  LEU A CG   1 
ATOM   683  C CD1  . LEU A 1 45  ? 21.311 -16.299 -14.048 1.00 35.78  ? 45  LEU A CD1  1 
ATOM   684  C CD2  . LEU A 1 45  ? 22.352 -18.301 -12.941 1.00 37.19  ? 45  LEU A CD2  1 
ATOM   685  H H    . LEU A 1 45  ? 24.253 -18.196 -16.129 1.00 42.41  ? 45  LEU A H    1 
ATOM   686  H HA   . LEU A 1 45  ? 22.831 -20.063 -14.924 1.00 43.21  ? 45  LEU A HA   1 
ATOM   687  H HB2  . LEU A 1 45  ? 21.898 -17.735 -16.195 1.00 41.77  ? 45  LEU A HB2  1 
ATOM   688  H HB3  . LEU A 1 45  ? 21.019 -18.656 -15.244 1.00 41.77  ? 45  LEU A HB3  1 
ATOM   689  H HG   . LEU A 1 45  ? 23.160 -17.033 -14.359 1.00 43.42  ? 45  LEU A HG   1 
ATOM   690  H HD11 . LEU A 1 45  ? 21.582 -15.756 -13.291 1.00 43.07  ? 45  LEU A HD11 1 
ATOM   691  H HD12 . LEU A 1 45  ? 21.309 -15.763 -14.856 1.00 43.07  ? 45  LEU A HD12 1 
ATOM   692  H HD13 . LEU A 1 45  ? 20.426 -16.666 -13.892 1.00 43.07  ? 45  LEU A HD13 1 
ATOM   693  H HD21 . LEU A 1 45  ? 22.348 -17.723 -12.162 1.00 44.76  ? 45  LEU A HD21 1 
ATOM   694  H HD22 . LEU A 1 45  ? 21.580 -18.888 -12.921 1.00 44.76  ? 45  LEU A HD22 1 
ATOM   695  H HD23 . LEU A 1 45  ? 23.167 -18.826 -12.959 1.00 44.76  ? 45  LEU A HD23 1 
ATOM   696  N N    . ASN A 1 46  ? 21.455 -21.258 -16.581 1.00 33.63  ? 46  ASN A N    1 
ATOM   697  C CA   . ASN A 1 46  ? 20.769 -22.037 -17.587 1.00 38.45  ? 46  ASN A CA   1 
ATOM   698  C C    . ASN A 1 46  ? 19.415 -21.444 -17.973 1.00 31.11  ? 46  ASN A C    1 
ATOM   699  O O    . ASN A 1 46  ? 18.661 -20.906 -17.149 1.00 32.03  ? 46  ASN A O    1 
ATOM   700  C CB   . ASN A 1 46  ? 20.559 -23.470 -17.108 1.00 40.77  ? 46  ASN A CB   1 
ATOM   701  C CG   . ASN A 1 46  ? 20.121 -24.374 -18.224 1.00 46.09  ? 46  ASN A CG   1 
ATOM   702  O OD1  . ASN A 1 46  ? 18.964 -24.809 -18.286 1.00 51.02  ? 46  ASN A OD1  1 
ATOM   703  N ND2  . ASN A 1 46  ? 21.038 -24.639 -19.147 1.00 52.15  ? 46  ASN A ND2  1 
ATOM   704  H H    . ASN A 1 46  ? 21.268 -21.492 -15.774 1.00 40.49  ? 46  ASN A H    1 
ATOM   705  H HA   . ASN A 1 46  ? 21.325 -22.033 -18.381 1.00 46.27  ? 46  ASN A HA   1 
ATOM   706  H HB2  . ASN A 1 46  ? 21.392 -23.813 -16.749 1.00 49.06  ? 46  ASN A HB2  1 
ATOM   707  H HB3  . ASN A 1 46  ? 19.873 -23.481 -16.422 1.00 49.06  ? 46  ASN A HB3  1 
ATOM   708  H HD21 . ASN A 1 46  ? 20.845 -25.151 -19.810 1.00 62.71  ? 46  ASN A HD21 1 
ATOM   709  H HD22 . ASN A 1 46  ? 21.825 -24.298 -19.081 1.00 62.71  ? 46  ASN A HD22 1 
ATOM   710  N N    . GLU A 1 47  ? 19.136 -21.512 -19.265 1.00 34.04  ? 47  GLU A N    1 
ATOM   711  C CA   . GLU A 1 47  ? 17.876 -21.013 -19.787 1.00 33.89  ? 47  GLU A CA   1 
ATOM   712  C C    . GLU A 1 47  ? 16.690 -21.554 -19.001 1.00 30.46  ? 47  GLU A C    1 
ATOM   713  O O    . GLU A 1 47  ? 15.775 -20.809 -18.623 1.00 27.72  ? 47  GLU A O    1 
ATOM   714  C CB   . GLU A 1 47  ? 17.841 -21.421 -21.251 1.00 38.67  ? 47  GLU A CB   1 
ATOM   715  C CG   . GLU A 1 47  ? 16.664 -21.132 -22.049 1.00 42.99  ? 47  GLU A CG   1 
ATOM   716  C CD   . GLU A 1 47  ? 16.910 -21.595 -23.464 1.00 44.94  ? 47  GLU A CD   1 
ATOM   717  O OE1  . GLU A 1 47  ? 17.689 -22.561 -23.680 1.00 53.57  ? 47  GLU A OE1  1 
ATOM   718  O OE2  . GLU A 1 47  ? 16.376 -20.943 -24.357 1.00 42.63  ? 47  GLU A OE2  1 
ATOM   719  H H    . GLU A 1 47  ? 19.660 -21.843 -19.862 1.00 40.99  ? 47  GLU A H    1 
ATOM   720  H HA   . GLU A 1 47  ? 17.810 -20.048 -19.713 1.00 40.80  ? 47  GLU A HA   1 
ATOM   721  H HB2  . GLU A 1 47  ? 18.582 -20.978 -21.693 1.00 46.54  ? 47  GLU A HB2  1 
ATOM   722  H HB3  . GLU A 1 47  ? 17.961 -22.383 -21.286 1.00 46.54  ? 47  GLU A HB3  1 
ATOM   723  H HG2  . GLU A 1 47  ? 15.896 -21.605 -21.690 1.00 51.72  ? 47  GLU A HG2  1 
ATOM   724  H HG3  . GLU A 1 47  ? 16.493 -20.177 -22.053 1.00 51.72  ? 47  GLU A HG3  1 
ATOM   725  N N    . ALA A 1 48  ? 16.666 -22.857 -18.759 1.00 29.12  ? 48  ALA A N    1 
ATOM   726  C CA   . ALA A 1 48  ? 15.499 -23.435 -18.097 1.00 28.04  ? 48  ALA A CA   1 
ATOM   727  C C    . ALA A 1 48  ? 15.353 -22.949 -16.671 1.00 25.00  ? 48  ALA A C    1 
ATOM   728  O O    . ALA A 1 48  ? 14.226 -22.839 -16.174 1.00 28.38  ? 48  ALA A O    1 
ATOM   729  C CB   . ALA A 1 48  ? 15.582 -24.956 -18.112 1.00 28.06  ? 48  ALA A CB   1 
ATOM   730  H H    . ALA A 1 48  ? 17.290 -23.414 -18.960 1.00 35.08  ? 48  ALA A H    1 
ATOM   731  H HA   . ALA A 1 48  ? 14.709 -23.164 -18.591 1.00 33.78  ? 48  ALA A HA   1 
ATOM   732  H HB1  . ALA A 1 48  ? 14.774 -25.321 -17.717 1.00 33.81  ? 48  ALA A HB1  1 
ATOM   733  H HB2  . ALA A 1 48  ? 15.668 -25.259 -19.029 1.00 33.81  ? 48  ALA A HB2  1 
ATOM   734  H HB3  . ALA A 1 48  ? 16.356 -25.235 -17.598 1.00 33.81  ? 48  ALA A HB3  1 
ATOM   735  N N    . THR A 1 49  ? 16.468 -22.601 -16.016 1.00 29.58  ? 49  THR A N    1 
ATOM   736  C CA   . THR A 1 49  ? 16.401 -22.043 -14.676 1.00 27.67  ? 49  THR A CA   1 
ATOM   737  C C    . THR A 1 49  ? 15.708 -20.701 -14.702 1.00 24.67  ? 49  THR A C    1 
ATOM   738  O O    . THR A 1 49  ? 14.845 -20.413 -13.861 1.00 26.57  ? 49  THR A O    1 
ATOM   739  C CB   . THR A 1 49  ? 17.797 -21.880 -14.101 1.00 31.47  ? 49  THR A CB   1 
ATOM   740  O OG1  . THR A 1 49  ? 18.472 -23.147 -14.082 1.00 32.32  ? 49  THR A OG1  1 
ATOM   741  C CG2  . THR A 1 49  ? 17.719 -21.300 -12.696 1.00 37.65  ? 49  THR A CG2  1 
ATOM   742  H H    . THR A 1 49  ? 17.265 -22.680 -16.328 1.00 35.63  ? 49  THR A H    1 
ATOM   743  H HA   . THR A 1 49  ? 15.906 -22.653 -14.107 1.00 33.34  ? 49  THR A HA   1 
ATOM   744  H HB   . THR A 1 49  ? 18.312 -21.269 -14.651 1.00 37.89  ? 49  THR A HB   1 
ATOM   745  H HG1  . THR A 1 49  ? 19.238 -23.060 -13.748 1.00 38.92  ? 49  THR A HG1  1 
ATOM   746  H HG21 . THR A 1 49  ? 18.578 -21.386 -12.254 1.00 45.31  ? 49  THR A HG21 1 
ATOM   747  H HG22 . THR A 1 49  ? 17.478 -20.362 -12.738 1.00 45.31  ? 49  THR A HG22 1 
ATOM   748  H HG23 . THR A 1 49  ? 17.050 -21.774 -12.179 1.00 45.31  ? 49  THR A HG23 1 
ATOM   749  N N    . LEU A 1 50  ? 16.061 -19.867 -15.677 1.00 26.89  ? 50  LEU A N    1 
ATOM   750  C CA   . LEU A 1 50  ? 15.379 -18.589 -15.814 1.00 28.45  ? 50  LEU A CA   1 
ATOM   751  C C    . LEU A 1 50  ? 13.894 -18.766 -16.126 1.00 25.49  ? 50  LEU A C    1 
ATOM   752  O O    . LEU A 1 50  ? 13.063 -17.989 -15.639 1.00 26.08  ? 50  LEU A O    1 
ATOM   753  C CB   . LEU A 1 50  ? 16.065 -17.752 -16.892 1.00 25.15  ? 50  LEU A CB   1 
ATOM   754  C CG   . LEU A 1 50  ? 17.145 -16.828 -16.370 1.00 29.15  ? 50  LEU A CG   1 
ATOM   755  C CD1  . LEU A 1 50  ? 18.214 -17.753 -15.762 1.00 30.28  ? 50  LEU A CD1  1 
ATOM   756  C CD2  . LEU A 1 50  ? 17.714 -15.961 -17.433 1.00 35.03  ? 50  LEU A CD2  1 
ATOM   757  H H    . LEU A 1 50  ? 16.677 -20.015 -16.258 1.00 32.41  ? 50  LEU A H    1 
ATOM   758  H HA   . LEU A 1 50  ? 15.441 -18.111 -14.972 1.00 34.27  ? 50  LEU A HA   1 
ATOM   759  H HB2  . LEU A 1 50  ? 16.476 -18.352 -17.534 1.00 30.31  ? 50  LEU A HB2  1 
ATOM   760  H HB3  . LEU A 1 50  ? 15.396 -17.204 -17.330 1.00 30.31  ? 50  LEU A HB3  1 
ATOM   761  H HG   . LEU A 1 50  ? 16.795 -16.207 -15.713 1.00 35.11  ? 50  LEU A HG   1 
ATOM   762  H HD11 . LEU A 1 50  ? 19.046 -17.263 -15.679 1.00 36.48  ? 50  LEU A HD11 1 
ATOM   763  H HD12 . LEU A 1 50  ? 17.916 -18.049 -14.888 1.00 36.48  ? 50  LEU A HD12 1 
ATOM   764  H HD13 . LEU A 1 50  ? 18.338 -18.519 -16.345 1.00 36.48  ? 50  LEU A HD13 1 
ATOM   765  H HD21 . LEU A 1 50  ? 18.278 -15.287 -17.023 1.00 42.16  ? 50  LEU A HD21 1 
ATOM   766  H HD22 . LEU A 1 50  ? 18.238 -16.507 -18.039 1.00 42.16  ? 50  LEU A HD22 1 
ATOM   767  H HD23 . LEU A 1 50  ? 16.988 -15.536 -17.916 1.00 42.16  ? 50  LEU A HD23 1 
ATOM   768  N N    . TYR A 1 51  ? 13.525 -19.751 -16.955 1.00 24.35  ? 51  TYR A N    1 
ATOM   769  C CA   . TYR A 1 51  ? 12.097 -19.867 -17.261 1.00 23.94  ? 51  TYR A CA   1 
ATOM   770  C C    . TYR A 1 51  ? 11.307 -20.272 -16.025 1.00 23.74  ? 51  TYR A C    1 
ATOM   771  O O    . TYR A 1 51  ? 10.217 -19.772 -15.802 1.00 25.29  ? 51  TYR A O    1 
ATOM   772  C CB   . TYR A 1 51  ? 11.830 -20.860 -18.379 1.00 24.68  ? 51  TYR A CB   1 
ATOM   773  C CG   . TYR A 1 51  ? 12.455 -20.506 -19.663 1.00 26.96  ? 51  TYR A CG   1 
ATOM   774  C CD1  . TYR A 1 51  ? 12.330 -19.239 -20.201 1.00 31.89  ? 51  TYR A CD1  1 
ATOM   775  C CD2  . TYR A 1 51  ? 13.193 -21.444 -20.347 1.00 32.39  ? 51  TYR A CD2  1 
ATOM   776  C CE1  . TYR A 1 51  ? 12.910 -18.930 -21.386 1.00 31.87  ? 51  TYR A CE1  1 
ATOM   777  C CE2  . TYR A 1 51  ? 13.729 -21.145 -21.532 1.00 33.46  ? 51  TYR A CE2  1 
ATOM   778  C CZ   . TYR A 1 51  ? 13.646 -19.868 -22.027 1.00 30.34  ? 51  TYR A CZ   1 
ATOM   779  O OH   . TYR A 1 51  ? 14.279 -19.623 -23.239 1.00 38.20  ? 51  TYR A OH   1 
ATOM   780  H H    . TYR A 1 51  ? 14.046 -20.325 -17.327 1.00 29.36  ? 51  TYR A H    1 
ATOM   781  H HA   . TYR A 1 51  ? 11.799 -18.998 -17.572 1.00 28.06  ? 51  TYR A HA   1 
ATOM   782  H HB2  . TYR A 1 51  ? 12.175 -21.727 -18.113 1.00 29.75  ? 51  TYR A HB2  1 
ATOM   783  H HB3  . TYR A 1 51  ? 10.872 -20.914 -18.523 1.00 29.75  ? 51  TYR A HB3  1 
ATOM   784  H HD1  . TYR A 1 51  ? 11.842 -18.592 -19.746 1.00 38.40  ? 51  TYR A HD1  1 
ATOM   785  H HD2  . TYR A 1 51  ? 13.319 -22.290 -19.982 1.00 39.01  ? 51  TYR A HD2  1 
ATOM   786  H HE1  . TYR A 1 51  ? 12.804 -18.083 -21.755 1.00 38.38  ? 51  TYR A HE1  1 
ATOM   787  H HE2  . TYR A 1 51  ? 14.162 -21.805 -22.025 1.00 40.28  ? 51  TYR A HE2  1 
ATOM   788  H HH   . TYR A 1 51  ? 14.750 -20.284 -23.456 1.00 45.97  ? 51  TYR A HH   1 
ATOM   789  N N    . THR A 1 52  ? 11.863 -21.160 -15.192 1.00 24.72  ? 52  THR A N    1 
ATOM   790  C CA   . THR A 1 52  ? 11.222 -21.471 -13.912 1.00 24.18  ? 52  THR A CA   1 
ATOM   791  C C    . THR A 1 52  ? 11.020 -20.220 -13.061 1.00 25.06  ? 52  THR A C    1 
ATOM   792  O O    . THR A 1 52  ? 9.916  -19.934 -12.573 1.00 27.57  ? 52  THR A O    1 
ATOM   793  C CB   . THR A 1 52  ? 12.092 -22.484 -13.165 1.00 26.78  ? 52  THR A CB   1 
ATOM   794  O OG1  . THR A 1 52  ? 12.177 -23.722 -13.900 1.00 28.49  ? 52  THR A OG1  1 
ATOM   795  C CG2  . THR A 1 52  ? 11.511 -22.751 -11.795 1.00 33.52  ? 52  THR A CG2  1 
ATOM   796  H H    . THR A 1 52  ? 12.595 -21.587 -15.342 1.00 29.80  ? 52  THR A H    1 
ATOM   797  H HA   . THR A 1 52  ? 10.346 -21.852 -14.079 1.00 29.15  ? 52  THR A HA   1 
ATOM   798  H HB   . THR A 1 52  ? 12.987 -22.124 -13.065 1.00 32.27  ? 52  THR A HB   1 
ATOM   799  H HG1  . THR A 1 52  ? 12.573 -23.596 -14.630 1.00 34.33  ? 52  THR A HG1  1 
ATOM   800  H HG21 . THR A 1 52  ? 11.885 -23.568 -11.429 1.00 40.35  ? 52  THR A HG21 1 
ATOM   801  H HG22 . THR A 1 52  ? 11.719 -22.015 -11.198 1.00 40.35  ? 52  THR A HG22 1 
ATOM   802  H HG23 . THR A 1 52  ? 10.548 -22.845 -11.855 1.00 40.35  ? 52  THR A HG23 1 
ATOM   803  N N    . ILE A 1 53  ? 12.093 -19.463 -12.866 1.00 25.72  ? 53  ILE A N    1 
ATOM   804  C CA   . ILE A 1 53  ? 12.037 -18.290 -11.992 1.00 29.04  ? 53  ILE A CA   1 
ATOM   805  C C    . ILE A 1 53  ? 11.086 -17.242 -12.539 1.00 26.77  ? 53  ILE A C    1 
ATOM   806  O O    . ILE A 1 53  ? 10.289 -16.669 -11.794 1.00 27.17  ? 53  ILE A O    1 
ATOM   807  C CB   . ILE A 1 53  ? 13.450 -17.725 -11.785 1.00 28.51  ? 53  ILE A CB   1 
ATOM   808  C CG1  . ILE A 1 53  ? 14.272 -18.750 -10.996 1.00 30.68  ? 53  ILE A CG1  1 
ATOM   809  C CG2  . ILE A 1 53  ? 13.399 -16.333 -11.132 1.00 29.06  ? 53  ILE A CG2  1 
ATOM   810  C CD1  . ILE A 1 53  ? 15.727 -18.415 -10.908 1.00 32.32  ? 53  ILE A CD1  1 
ATOM   811  H H    . ILE A 1 53  ? 12.863 -19.602 -13.224 1.00 30.99  ? 53  ILE A H    1 
ATOM   812  H HA   . ILE A 1 53  ? 11.688 -18.568 -11.130 1.00 34.99  ? 53  ILE A HA   1 
ATOM   813  H HB   . ILE A 1 53  ? 13.889 -17.587 -12.639 1.00 34.35  ? 53  ILE A HB   1 
ATOM   814  H HG12 . ILE A 1 53  ? 13.924 -18.800 -10.092 1.00 36.95  ? 53  ILE A HG12 1 
ATOM   815  H HG13 . ILE A 1 53  ? 14.193 -19.614 -11.430 1.00 36.95  ? 53  ILE A HG13 1 
ATOM   816  H HG21 . ILE A 1 53  ? 14.279 -16.114 -10.787 1.00 35.00  ? 53  ILE A HG21 1 
ATOM   817  H HG22 . ILE A 1 53  ? 13.133 -15.681 -11.798 1.00 35.00  ? 53  ILE A HG22 1 
ATOM   818  H HG23 . ILE A 1 53  ? 12.754 -16.348 -10.407 1.00 35.00  ? 53  ILE A HG23 1 
ATOM   819  H HD11 . ILE A 1 53  ? 16.191 -19.139 -10.458 1.00 38.91  ? 53  ILE A HD11 1 
ATOM   820  H HD12 . ILE A 1 53  ? 16.081 -18.302 -11.804 1.00 38.91  ? 53  ILE A HD12 1 
ATOM   821  H HD13 . ILE A 1 53  ? 15.832 -17.592 -10.405 1.00 38.91  ? 53  ILE A HD13 1 
ATOM   822  N N    . PHE A 1 54  ? 11.148 -16.973 -13.837 1.00 25.69  ? 54  PHE A N    1 
ATOM   823  C CA   . PHE A 1 54  ? 10.285 -15.945 -14.411 1.00 24.67  ? 54  PHE A CA   1 
ATOM   824  C C    . PHE A 1 54  ? 8.842  -16.351 -14.374 1.00 25.20  ? 54  PHE A C    1 
ATOM   825  O O    . PHE A 1 54  ? 7.977  -15.480 -14.311 1.00 27.21  ? 54  PHE A O    1 
ATOM   826  C CB   . PHE A 1 54  ? 10.744 -15.642 -15.826 1.00 24.73  ? 54  PHE A CB   1 
ATOM   827  C CG   . PHE A 1 54  ? 12.041 -14.812 -15.879 1.00 26.19  ? 54  PHE A CG   1 
ATOM   828  C CD1  . PHE A 1 54  ? 12.639 -14.300 -14.719 1.00 26.12  ? 54  PHE A CD1  1 
ATOM   829  C CD2  . PHE A 1 54  ? 12.661 -14.565 -17.069 1.00 28.72  ? 54  PHE A CD2  1 
ATOM   830  C CE1  . PHE A 1 54  ? 13.810 -13.562 -14.753 1.00 27.20  ? 54  PHE A CE1  1 
ATOM   831  C CE2  . PHE A 1 54  ? 13.836 -13.816 -17.107 1.00 26.64  ? 54  PHE A CE2  1 
ATOM   832  C CZ   . PHE A 1 54  ? 14.395 -13.304 -15.957 1.00 25.48  ? 54  PHE A CZ   1 
ATOM   833  H H    . PHE A 1 54  ? 11.670 -17.363 -14.398 1.00 30.96  ? 54  PHE A H    1 
ATOM   834  H HA   . PHE A 1 54  ? 10.359 -15.128 -13.895 1.00 29.74  ? 54  PHE A HA   1 
ATOM   835  H HB2  . PHE A 1 54  ? 10.906 -16.478 -16.289 1.00 29.81  ? 54  PHE A HB2  1 
ATOM   836  H HB3  . PHE A 1 54  ? 10.050 -15.139 -16.280 1.00 29.81  ? 54  PHE A HB3  1 
ATOM   837  H HD1  . PHE A 1 54  ? 12.235 -14.462 -13.897 1.00 31.48  ? 54  PHE A HD1  1 
ATOM   838  H HD2  . PHE A 1 54  ? 12.298 -14.898 -17.858 1.00 34.59  ? 54  PHE A HD2  1 
ATOM   839  H HE1  . PHE A 1 54  ? 14.192 -13.246 -13.966 1.00 32.78  ? 54  PHE A HE1  1 
ATOM   840  H HE2  . PHE A 1 54  ? 14.250 -13.659 -17.924 1.00 32.11  ? 54  PHE A HE2  1 
ATOM   841  H HZ   . PHE A 1 54  ? 15.166 -12.787 -16.002 1.00 30.71  ? 54  PHE A HZ   1 
ATOM   842  N N    . LYS A 1 55  ? 8.546  -17.643 -14.507 1.00 24.27  ? 55  LYS A N    1 
ATOM   843  C CA   . LYS A 1 55  ? 7.163  -18.062 -14.363 1.00 25.49  ? 55  LYS A CA   1 
ATOM   844  C C    . LYS A 1 55  ? 6.623  -17.645 -13.006 1.00 28.41  ? 55  LYS A C    1 
ATOM   845  O O    . LYS A 1 55  ? 5.514  -17.113 -12.903 1.00 30.05  ? 55  LYS A O    1 
ATOM   846  C CB   . LYS A 1 55  ? 7.020  -19.568 -14.541 1.00 30.15  ? 55  LYS A CB   1 
ATOM   847  C CG   . LYS A 1 55  ? 5.598  -20.070 -14.200 1.00 35.24  ? 55  LYS A CG   1 
ATOM   848  C CD   . LYS A 1 55  ? 5.549  -21.588 -14.282 1.00 45.11  ? 55  LYS A CD   1 
ATOM   849  C CE   . LYS A 1 55  ? 4.195  -22.120 -13.825 1.00 56.14  ? 55  LYS A CE   1 
ATOM   850  N NZ   . LYS A 1 55  ? 3.866  -21.662 -12.443 1.00 73.07  ? 55  LYS A NZ   1 
ATOM   851  H H    . LYS A 1 55  ? 9.109  -18.271 -14.674 1.00 29.25  ? 55  LYS A H    1 
ATOM   852  H HA   . LYS A 1 55  ? 6.643  -17.637 -15.063 1.00 30.73  ? 55  LYS A HA   1 
ATOM   853  H HB2  . LYS A 1 55  ? 7.207  -19.797 -15.465 1.00 36.32  ? 55  LYS A HB2  1 
ATOM   854  H HB3  . LYS A 1 55  ? 7.647  -20.018 -13.954 1.00 36.32  ? 55  LYS A HB3  1 
ATOM   855  H HG2  . LYS A 1 55  ? 5.362  -19.799 -13.299 1.00 42.42  ? 55  LYS A HG2  1 
ATOM   856  H HG3  . LYS A 1 55  ? 4.961  -19.704 -14.834 1.00 42.42  ? 55  LYS A HG3  1 
ATOM   857  H HD2  . LYS A 1 55  ? 5.694  -21.866 -15.199 1.00 54.26  ? 55  LYS A HD2  1 
ATOM   858  H HD3  . LYS A 1 55  ? 6.235  -21.963 -13.708 1.00 54.26  ? 55  LYS A HD3  1 
ATOM   859  H HE2  . LYS A 1 55  ? 3.504  -21.799 -14.425 1.00 67.50  ? 55  LYS A HE2  1 
ATOM   860  H HE3  . LYS A 1 55  ? 4.213  -23.090 -13.829 1.00 67.50  ? 55  LYS A HE3  1 
ATOM   861  H HZ1  . LYS A 1 55  ? 3.105  -22.035 -12.171 1.00 87.82  ? 55  LYS A HZ1  1 
ATOM   862  H HZ2  . LYS A 1 55  ? 4.518  -21.894 -11.882 1.00 87.82  ? 55  LYS A HZ2  1 
ATOM   863  H HZ3  . LYS A 1 55  ? 3.775  -20.777 -12.429 1.00 87.82  ? 55  LYS A HZ3  1 
ATOM   864  N N    . ARG A 1 56  ? 7.407  -17.874 -11.958 1.00 26.42  ? 56  ARG A N    1 
ATOM   865  C CA   . ARG A 1 56  ? 6.939  -17.522 -10.622 1.00 30.04  ? 56  ARG A CA   1 
ATOM   866  C C    . ARG A 1 56  ? 6.801  -16.024 -10.485 1.00 31.73  ? 56  ARG A C    1 
ATOM   867  O O    . ARG A 1 56  ? 5.802  -15.529 -9.954  1.00 31.47  ? 56  ARG A O    1 
ATOM   868  C CB   . ARG A 1 56  ? 7.876  -18.076 -9.540  1.00 33.25  ? 56  ARG A CB   1 
ATOM   869  C CG   . ARG A 1 56  ? 7.284  -17.870 -8.127  1.00 42.77  ? 56  ARG A CG   1 
ATOM   870  C CD   . ARG A 1 56  ? 8.230  -18.260 -7.009  1.00 60.49  ? 56  ARG A CD   1 
ATOM   871  N NE   . ARG A 1 56  ? 9.600  -17.915 -7.363  1.00 89.65  ? 56  ARG A NE   1 
ATOM   872  C CZ   . ARG A 1 56  ? 10.183 -16.755 -7.095  1.00 80.61  ? 56  ARG A CZ   1 
ATOM   873  N NH1  . ARG A 1 56  ? 9.588  -15.834 -6.350  1.00 67.28  ? 56  ARG A NH1  1 
ATOM   874  N NH2  . ARG A 1 56  ? 11.392 -16.510 -7.593  1.00 60.40  ? 56  ARG A NH2  1 
ATOM   875  H H    . ARG A 1 56  ? 8.193  -18.222 -11.991 1.00 31.84  ? 56  ARG A H    1 
ATOM   876  H HA   . ARG A 1 56  ? 6.072  -17.934 -10.486 1.00 36.19  ? 56  ARG A HA   1 
ATOM   877  H HB2  . ARG A 1 56  ? 8.005  -19.027 -9.683  1.00 40.03  ? 56  ARG A HB2  1 
ATOM   878  H HB3  . ARG A 1 56  ? 8.728  -17.615 -9.586  1.00 40.03  ? 56  ARG A HB3  1 
ATOM   879  H HG2  . ARG A 1 56  ? 7.063  -16.932 -8.013  1.00 51.45  ? 56  ARG A HG2  1 
ATOM   880  H HG3  . ARG A 1 56  ? 6.484  -18.412 -8.040  1.00 51.45  ? 56  ARG A HG3  1 
ATOM   881  H HD2  . ARG A 1 56  ? 7.990  -17.785 -6.199  1.00 72.72  ? 56  ARG A HD2  1 
ATOM   882  H HD3  . ARG A 1 56  ? 8.180  -19.218 -6.860  1.00 72.72  ? 56  ARG A HD3  1 
ATOM   883  H HE   . ARG A 1 56  ? 10.065 -18.509 -7.776  1.00 107.72 ? 56  ARG A HE   1 
ATOM   884  H HH11 . ARG A 1 56  ? 8.805  -15.982 -6.027  1.00 80.87  ? 56  ARG A HH11 1 
ATOM   885  H HH12 . ARG A 1 56  ? 9.986  -15.089 -6.190  1.00 80.87  ? 56  ARG A HH12 1 
ATOM   886  H HH21 . ARG A 1 56  ? 11.784 -17.100 -8.081  1.00 72.61  ? 56  ARG A HH21 1 
ATOM   887  H HH22 . ARG A 1 56  ? 11.781 -15.761 -7.427  1.00 72.61  ? 56  ARG A HH22 1 
ATOM   888  N N    . LEU A 1 57  ? 7.800  -15.279 -10.943 1.00 25.23  ? 57  LEU A N    1 
ATOM   889  C CA   . LEU A 1 57  ? 7.761  -13.824 -10.791 1.00 26.66  ? 57  LEU A CA   1 
ATOM   890  C C    . LEU A 1 57  ? 6.634  -13.193 -11.592 1.00 25.36  ? 57  LEU A C    1 
ATOM   891  O O    . LEU A 1 57  ? 6.017  -12.200 -11.165 1.00 27.23  ? 57  LEU A O    1 
ATOM   892  C CB   . LEU A 1 57  ? 9.086  -13.215 -11.232 1.00 29.12  ? 57  LEU A CB   1 
ATOM   893  C CG   . LEU A 1 57  ? 10.322 -13.561 -10.389 1.00 26.31  ? 57  LEU A CG   1 
ATOM   894  C CD1  . LEU A 1 57  ? 11.514 -12.958 -10.943 1.00 29.24  ? 57  LEU A CD1  1 
ATOM   895  C CD2  . LEU A 1 57  ? 10.037 -13.059 -8.966  1.00 31.31  ? 57  LEU A CD2  1 
ATOM   896  H H    . LEU A 1 57  ? 8.500  -15.582 -11.340 1.00 30.41  ? 57  LEU A H    1 
ATOM   897  H HA   . LEU A 1 57  ? 7.619  -13.627 -9.852  1.00 32.12  ? 57  LEU A HA   1 
ATOM   898  H HB2  . LEU A 1 57  ? 9.267  -13.514 -12.137 1.00 35.08  ? 57  LEU A HB2  1 
ATOM   899  H HB3  . LEU A 1 57  ? 8.993  -12.249 -11.215 1.00 35.08  ? 57  LEU A HB3  1 
ATOM   900  H HG   . LEU A 1 57  ? 10.494 -14.516 -10.378 1.00 31.70  ? 57  LEU A HG   1 
ATOM   901  H HD11 . LEU A 1 57  ? 12.293 -13.359 -10.527 1.00 35.22  ? 57  LEU A HD11 1 
ATOM   902  H HD12 . LEU A 1 57  ? 11.532 -13.115 -11.900 1.00 35.22  ? 57  LEU A HD12 1 
ATOM   903  H HD13 . LEU A 1 57  ? 11.497 -12.005 -10.764 1.00 35.22  ? 57  LEU A HD13 1 
ATOM   904  H HD21 . LEU A 1 57  ? 10.879 -12.907 -8.510  1.00 37.71  ? 57  LEU A HD21 1 
ATOM   905  H HD22 . LEU A 1 57  ? 9.534  -12.231 -9.019  1.00 37.71  ? 57  LEU A HD22 1 
ATOM   906  H HD23 . LEU A 1 57  ? 9.520  -13.730 -8.492  1.00 37.71  ? 57  LEU A HD23 1 
ATOM   907  N N    . GLU A 1 58  ? 6.314  -13.774 -12.735 1.00 26.01  ? 58  GLU A N    1 
ATOM   908  C CA   . GLU A 1 58  ? 5.211  -13.259 -13.526 1.00 27.26  ? 58  GLU A CA   1 
ATOM   909  C C    . GLU A 1 58  ? 3.887  -13.557 -12.831 1.00 31.41  ? 58  GLU A C    1 
ATOM   910  O O    . GLU A 1 58  ? 3.003  -12.690 -12.753 1.00 30.05  ? 58  GLU A O    1 
ATOM   911  C CB   . GLU A 1 58  ? 5.282  -13.917 -14.904 1.00 31.09  ? 58  GLU A CB   1 
ATOM   912  C CG   . GLU A 1 58  ? 4.744  -13.081 -16.044 1.00 44.25  ? 58  GLU A CG   1 
ATOM   913  C CD   . GLU A 1 58  ? 5.313  -13.541 -17.385 1.00 46.80  ? 58  GLU A CD   1 
ATOM   914  O OE1  . GLU A 1 58  ? 5.910  -14.656 -17.441 1.00 44.73  ? 58  GLU A OE1  1 
ATOM   915  O OE2  . GLU A 1 58  ? 5.170  -12.799 -18.376 1.00 45.29  ? 58  GLU A OE2  1 
ATOM   916  H H    . GLU A 1 58  ? 6.713  -14.458 -13.072 1.00 31.34  ? 58  GLU A H    1 
ATOM   917  H HA   . GLU A 1 58  ? 5.271  -12.297 -13.638 1.00 32.85  ? 58  GLU A HA   1 
ATOM   918  H HB2  . GLU A 1 58  ? 6.211  -14.115 -15.101 1.00 37.44  ? 58  GLU A HB2  1 
ATOM   919  H HB3  . GLU A 1 58  ? 4.766  -14.739 -14.877 1.00 37.44  ? 58  GLU A HB3  1 
ATOM   920  H HG2  . GLU A 1 58  ? 3.778  -13.165 -16.076 1.00 53.24  ? 58  GLU A HG2  1 
ATOM   921  H HG3  . GLU A 1 58  ? 4.992  -12.153 -15.908 1.00 53.24  ? 58  GLU A HG3  1 
ATOM   922  N N    . LYS A 1 59  ? 3.729  -14.780 -12.335 1.00 29.57  ? 59  LYS A N    1 
ATOM   923  C CA   . LYS A 1 59  ? 2.537  -15.151 -11.582 1.00 35.38  ? 59  LYS A CA   1 
ATOM   924  C C    . LYS A 1 59  ? 2.333  -14.207 -10.417 1.00 36.40  ? 59  LYS A C    1 
ATOM   925  O O    . LYS A 1 59  ? 1.207  -13.798 -10.126 1.00 35.75  ? 59  LYS A O    1 
ATOM   926  C CB   . LYS A 1 59  ? 2.664  -16.598 -11.091 1.00 38.56  ? 59  LYS A CB   1 
ATOM   927  C CG   . LYS A 1 59  ? 1.816  -16.980 -9.864  1.00 42.72  ? 59  LYS A CG   1 
ATOM   928  C CD   . LYS A 1 59  ? 2.294  -18.310 -9.220  1.00 55.02  ? 59  LYS A CD   1 
ATOM   929  C CE   . LYS A 1 59  ? 2.252  -19.482 -10.204 1.00 65.39  ? 59  LYS A CE   1 
ATOM   930  N NZ   . LYS A 1 59  ? 2.753  -20.761 -9.603  1.00 68.75  ? 59  LYS A NZ   1 
ATOM   931  H H    . LYS A 1 59  ? 4.301  -15.418 -12.419 1.00 35.61  ? 59  LYS A H    1 
ATOM   932  H HA   . LYS A 1 59  ? 1.759  -15.100 -12.159 1.00 42.59  ? 59  LYS A HA   1 
ATOM   933  H HB2  . LYS A 1 59  ? 2.399  -17.187 -11.815 1.00 46.40  ? 59  LYS A HB2  1 
ATOM   934  H HB3  . LYS A 1 59  ? 3.591  -16.757 -10.857 1.00 46.40  ? 59  LYS A HB3  1 
ATOM   935  H HG2  . LYS A 1 59  ? 1.884  -16.279 -9.198  1.00 51.40  ? 59  LYS A HG2  1 
ATOM   936  H HG3  . LYS A 1 59  ? 0.892  -17.091 -10.137 1.00 51.40  ? 59  LYS A HG3  1 
ATOM   937  H HD2  . LYS A 1 59  ? 3.209  -18.205 -8.916  1.00 66.16  ? 59  LYS A HD2  1 
ATOM   938  H HD3  . LYS A 1 59  ? 1.718  -18.525 -8.470  1.00 66.16  ? 59  LYS A HD3  1 
ATOM   939  H HE2  . LYS A 1 59  ? 1.336  -19.623 -10.489 1.00 78.60  ? 59  LYS A HE2  1 
ATOM   940  H HE3  . LYS A 1 59  ? 2.809  -19.272 -10.970 1.00 78.60  ? 59  LYS A HE3  1 
ATOM   941  H HZ1  . LYS A 1 59  ? 2.686  -21.422 -10.196 1.00 82.63  ? 59  LYS A HZ1  1 
ATOM   942  H HZ2  . LYS A 1 59  ? 3.606  -20.672 -9.365  1.00 82.63  ? 59  LYS A HZ2  1 
ATOM   943  H HZ3  . LYS A 1 59  ? 2.272  -20.968 -8.884  1.00 82.63  ? 59  LYS A HZ3  1 
ATOM   944  N N    . ASP A 1 60  ? 3.415  -13.840 -9.740  1.00 30.25  ? 60  ASP A N    1 
ATOM   945  C CA   . ASP A 1 60  ? 3.317  -12.955 -8.585  1.00 31.74  ? 60  ASP A CA   1 
ATOM   946  C C    . ASP A 1 60  ? 3.167  -11.475 -8.952  1.00 32.95  ? 60  ASP A C    1 
ATOM   947  O O    . ASP A 1 60  ? 2.981  -10.645 -8.053  1.00 35.19  ? 60  ASP A O    1 
ATOM   948  C CB   . ASP A 1 60  ? 4.537  -13.147 -7.679  1.00 33.25  ? 60  ASP A CB   1 
ATOM   949  C CG   . ASP A 1 60  ? 4.559  -14.486 -6.985  1.00 38.76  ? 60  ASP A CG   1 
ATOM   950  O OD1  . ASP A 1 60  ? 3.514  -15.156 -6.926  1.00 43.92  ? 60  ASP A OD1  1 
ATOM   951  O OD2  . ASP A 1 60  ? 5.644  -14.862 -6.490  1.00 45.55  ? 60  ASP A OD2  1 
ATOM   952  H H    . ASP A 1 60  ? 4.215  -14.090 -9.929  1.00 36.43  ? 60  ASP A H    1 
ATOM   953  H HA   . ASP A 1 60  ? 2.525  -13.202 -8.082  1.00 38.22  ? 60  ASP A HA   1 
ATOM   954  H HB2  . ASP A 1 60  ? 5.342  -13.077 -8.216  1.00 40.03  ? 60  ASP A HB2  1 
ATOM   955  H HB3  . ASP A 1 60  ? 4.533  -12.458 -6.997  1.00 40.03  ? 60  ASP A HB3  1 
ATOM   956  N N    . GLY A 1 61  ? 3.187  -11.118 -10.231 1.00 29.26  ? 61  GLY A N    1 
ATOM   957  C CA   . GLY A 1 61  ? 3.048  -9.758  -10.640 1.00 28.63  ? 61  GLY A CA   1 
ATOM   958  C C    . GLY A 1 61  ? 4.269  -8.889  -10.478 1.00 27.27  ? 61  GLY A C    1 
ATOM   959  O O    . GLY A 1 61  ? 4.142  -7.656  -10.550 1.00 27.31  ? 61  GLY A O    1 
ATOM   960  H H    . GLY A 1 61  ? 3.283  -11.669 -10.884 1.00 35.25  ? 61  GLY A H    1 
ATOM   961  H HA2  . GLY A 1 61  ? 2.805  -9.744  -11.579 1.00 34.50  ? 61  GLY A HA2  1 
ATOM   962  H HA3  . GLY A 1 61  ? 2.334  -9.354  -10.123 1.00 34.50  ? 61  GLY A HA3  1 
ATOM   963  N N    . ILE A 1 62  ? 5.437  -9.499  -10.266 1.00 27.63  ? 62  ILE A N    1 
ATOM   964  C CA   . ILE A 1 62  ? 6.674  -8.765  -10.050 1.00 26.79  ? 62  ILE A CA   1 
ATOM   965  C C    . ILE A 1 62  ? 7.293  -8.370  -11.384 1.00 25.24  ? 62  ILE A C    1 
ATOM   966  O O    . ILE A 1 62  ? 7.984  -7.345  -11.485 1.00 25.99  ? 62  ILE A O    1 
ATOM   967  C CB   . ILE A 1 62  ? 7.644  -9.623  -9.216  1.00 28.09  ? 62  ILE A CB   1 
ATOM   968  C CG1  . ILE A 1 62  ? 7.018  -9.857  -7.837  1.00 32.15  ? 62  ILE A CG1  1 
ATOM   969  C CG2  . ILE A 1 62  ? 8.980  -8.930  -9.100  1.00 27.68  ? 62  ILE A CG2  1 
ATOM   970  C CD1  . ILE A 1 62  ? 6.776  -8.620  -7.071  1.00 35.65  ? 62  ILE A CD1  1 
ATOM   971  H H    . ILE A 1 62  ? 5.539  -10.353 -10.242 1.00 33.29  ? 62  ILE A H    1 
ATOM   972  H HA   . ILE A 1 62  ? 6.484  -7.953  -9.556  1.00 32.28  ? 62  ILE A HA   1 
ATOM   973  H HB   . ILE A 1 62  ? 7.793  -10.478 -9.648  1.00 33.85  ? 62  ILE A HB   1 
ATOM   974  H HG12 . ILE A 1 62  ? 6.165  -10.303 -7.954  1.00 38.71  ? 62  ILE A HG12 1 
ATOM   975  H HG13 . ILE A 1 62  ? 7.615  -10.415 -7.314  1.00 38.71  ? 62  ILE A HG13 1 
ATOM   976  H HG21 . ILE A 1 62  ? 9.511  -9.379  -8.425  1.00 33.35  ? 62  ILE A HG21 1 
ATOM   977  H HG22 . ILE A 1 62  ? 9.432  -8.970  -9.957  1.00 33.35  ? 62  ILE A HG22 1 
ATOM   978  H HG23 . ILE A 1 62  ? 8.835  -8.005  -8.845  1.00 33.35  ? 62  ILE A HG23 1 
ATOM   979  H HD11 . ILE A 1 62  ? 6.469  -8.854  -6.181  1.00 42.92  ? 62  ILE A HD11 1 
ATOM   980  H HD12 . ILE A 1 62  ? 7.603  -8.116  -7.015  1.00 42.92  ? 62  ILE A HD12 1 
ATOM   981  H HD13 . ILE A 1 62  ? 6.099  -8.094  -7.527  1.00 42.92  ? 62  ILE A HD13 1 
ATOM   982  N N    . ILE A 1 63  ? 7.115  -9.200  -12.402 1.00 25.93  ? 63  ILE A N    1 
ATOM   983  C CA   . ILE A 1 63  ? 7.576  -8.912  -13.749 1.00 27.00  ? 63  ILE A CA   1 
ATOM   984  C C    . ILE A 1 63  ? 6.422  -9.225  -14.695 1.00 28.06  ? 63  ILE A C    1 
ATOM   985  O O    . ILE A 1 63  ? 5.483  -9.962  -14.371 1.00 27.00  ? 63  ILE A O    1 
ATOM   986  C CB   . ILE A 1 63  ? 8.847  -9.706  -14.162 1.00 26.51  ? 63  ILE A CB   1 
ATOM   987  C CG1  . ILE A 1 63  ? 8.520  -11.193 -14.422 1.00 25.38  ? 63  ILE A CG1  1 
ATOM   988  C CG2  . ILE A 1 63  ? 9.922  -9.583  -13.121 1.00 26.14  ? 63  ILE A CG2  1 
ATOM   989  C CD1  . ILE A 1 63  ? 9.677  -12.041 -14.723 1.00 25.22  ? 63  ILE A CD1  1 
ATOM   990  H H    . ILE A 1 63  ? 6.717  -9.959  -12.334 1.00 31.24  ? 63  ILE A H    1 
ATOM   991  H HA   . ILE A 1 63  ? 7.804  -7.971  -13.809 1.00 32.54  ? 63  ILE A HA   1 
ATOM   992  H HB   . ILE A 1 63  ? 9.173  -9.318  -14.989 1.00 31.95  ? 63  ILE A HB   1 
ATOM   993  H HG12 . ILE A 1 63  ? 8.092  -11.556 -13.631 1.00 30.58  ? 63  ILE A HG12 1 
ATOM   994  H HG13 . ILE A 1 63  ? 7.916  -11.246 -15.179 1.00 30.58  ? 63  ILE A HG13 1 
ATOM   995  H HG21 . ILE A 1 63  ? 10.740 -9.978  -13.462 1.00 31.50  ? 63  ILE A HG21 1 
ATOM   996  H HG22 . ILE A 1 63  ? 10.066 -8.644  -12.925 1.00 31.50  ? 63  ILE A HG22 1 
ATOM   997  H HG23 . ILE A 1 63  ? 9.640  -10.049 -12.318 1.00 31.50  ? 63  ILE A HG23 1 
ATOM   998  H HD11 . ILE A 1 63  ? 9.364  -12.929 -14.960 1.00 30.40  ? 63  ILE A HD11 1 
ATOM   999  H HD12 . ILE A 1 63  ? 10.167 -11.655 -15.465 1.00 30.40  ? 63  ILE A HD12 1 
ATOM   1000 H HD13 . ILE A 1 63  ? 10.246 -12.090 -13.939 1.00 30.40  ? 63  ILE A HD13 1 
ATOM   1001 N N    . SER A 1 64  ? 6.559  -8.719  -15.907 1.00 24.94  ? 64  SER A N    1 
ATOM   1002 C CA   . SER A 1 64  ? 5.684  -9.103  -17.000 1.00 25.64  ? 64  SER A CA   1 
ATOM   1003 C C    . SER A 1 64  ? 6.501  -9.250  -18.266 1.00 26.04  ? 64  SER A C    1 
ATOM   1004 O O    . SER A 1 64  ? 7.664  -8.858  -18.329 1.00 27.12  ? 64  SER A O    1 
ATOM   1005 C CB   . SER A 1 64  ? 4.569  -8.085  -17.212 1.00 24.91  ? 64  SER A CB   1 
ATOM   1006 O OG   . SER A 1 64  ? 4.996  -6.892  -17.884 1.00 26.71  ? 64  SER A OG   1 
ATOM   1007 H H    . SER A 1 64  ? 7.160  -8.144  -16.126 1.00 30.07  ? 64  SER A H    1 
ATOM   1008 H HA   . SER A 1 64  ? 5.282  -9.961  -16.791 1.00 30.91  ? 64  SER A HA   1 
ATOM   1009 H HB2  . SER A 1 64  ? 3.874  -8.502  -17.745 1.00 30.03  ? 64  SER A HB2  1 
ATOM   1010 H HB3  . SER A 1 64  ? 4.216  -7.835  -16.344 1.00 30.03  ? 64  SER A HB3  1 
ATOM   1011 H HG   . SER A 1 64  ? 5.274  -7.080  -18.654 1.00 32.18  ? 64  SER A HG   1 
ATOM   1012 N N    . SER A 1 65  ? 5.899  -9.849  -19.278 1.00 26.18  ? 65  SER A N    1 
ATOM   1013 C CA   . SER A 1 65  ? 6.591  -10.153 -20.512 1.00 24.62  ? 65  SER A CA   1 
ATOM   1014 C C    . SER A 1 65  ? 5.886  -9.541  -21.700 1.00 23.92  ? 65  SER A C    1 
ATOM   1015 O O    . SER A 1 65  ? 4.679  -9.290  -21.681 1.00 27.27  ? 65  SER A O    1 
ATOM   1016 C CB   . SER A 1 65  ? 6.741  -11.677 -20.724 1.00 29.61  ? 65  SER A CB   1 
ATOM   1017 O OG   . SER A 1 65  ? 5.476  -12.268 -20.870 1.00 31.64  ? 65  SER A OG   1 
ATOM   1018 H H    . SER A 1 65  ? 5.075  -10.093 -19.272 1.00 31.55  ? 65  SER A H    1 
ATOM   1019 H HA   . SER A 1 65  ? 7.477  -9.762  -20.464 1.00 29.68  ? 65  SER A HA   1 
ATOM   1020 H HB2  . SER A 1 65  ? 7.263  -11.838 -21.526 1.00 35.67  ? 65  SER A HB2  1 
ATOM   1021 H HB3  . SER A 1 65  ? 7.187  -12.064 -19.955 1.00 35.67  ? 65  SER A HB3  1 
ATOM   1022 H HG   . SER A 1 65  ? 4.966  -12.009 -20.255 1.00 38.10  ? 65  SER A HG   1 
ATOM   1023 N N    . TYR A 1 66  ? 6.650  -9.410  -22.774 1.00 24.26  ? 66  TYR A N    1 
ATOM   1024 C CA   . TYR A 1 66  ? 6.108  -8.888  -24.013 1.00 24.16  ? 66  TYR A CA   1 
ATOM   1025 C C    . TYR A 1 66  ? 7.028  -9.269  -25.151 1.00 25.75  ? 66  TYR A C    1 
ATOM   1026 O O    . TYR A 1 66  ? 8.178  -9.615  -24.923 1.00 26.65  ? 66  TYR A O    1 
ATOM   1027 C CB   . TYR A 1 66  ? 5.950  -7.392  -23.940 1.00 25.57  ? 66  TYR A CB   1 
ATOM   1028 C CG   . TYR A 1 66  ? 7.192  -6.562  -23.738 1.00 24.34  ? 66  TYR A CG   1 
ATOM   1029 C CD1  . TYR A 1 66  ? 7.693  -6.270  -22.455 1.00 25.37  ? 66  TYR A CD1  1 
ATOM   1030 C CD2  . TYR A 1 66  ? 7.901  -6.078  -24.830 1.00 26.88  ? 66  TYR A CD2  1 
ATOM   1031 C CE1  . TYR A 1 66  ? 8.808  -5.441  -22.280 1.00 26.34  ? 66  TYR A CE1  1 
ATOM   1032 C CE2  . TYR A 1 66  ? 9.022  -5.279  -24.663 1.00 25.31  ? 66  TYR A CE2  1 
ATOM   1033 C CZ   . TYR A 1 66  ? 9.483  -4.984  -23.395 1.00 26.40  ? 66  TYR A CZ   1 
ATOM   1034 O OH   . TYR A 1 66  ? 10.607 -4.175  -23.276 1.00 30.54  ? 66  TYR A OH   1 
ATOM   1035 H H    . TYR A 1 66  ? 7.484  -9.616  -22.809 1.00 29.24  ? 66  TYR A H    1 
ATOM   1036 H HA   . TYR A 1 66  ? 5.241  -9.288  -24.183 1.00 28.31  ? 66  TYR A HA   1 
ATOM   1037 H HB2  . TYR A 1 66  ? 5.550  -7.096  -24.772 1.00 30.82  ? 66  TYR A HB2  1 
ATOM   1038 H HB3  . TYR A 1 66  ? 5.359  -7.193  -23.198 1.00 30.82  ? 66  TYR A HB3  1 
ATOM   1039 H HD1  . TYR A 1 66  ? 7.274  -6.634  -21.709 1.00 30.58  ? 66  TYR A HD1  1 
ATOM   1040 H HD2  . TYR A 1 66  ? 7.619  -6.295  -25.689 1.00 32.39  ? 66  TYR A HD2  1 
ATOM   1041 H HE1  . TYR A 1 66  ? 9.090  -5.201  -21.427 1.00 31.75  ? 66  TYR A HE1  1 
ATOM   1042 H HE2  . TYR A 1 66  ? 9.465  -4.940  -25.407 1.00 30.50  ? 66  TYR A HE2  1 
ATOM   1043 H HH   . TYR A 1 66  ? 10.663 -3.875  -22.494 1.00 36.79  ? 66  TYR A HH   1 
ATOM   1044 N N    . TRP A 1 67  ? 6.495  -9.251  -26.373 1.00 27.48  ? 67  TRP A N    1 
ATOM   1045 C CA   . TRP A 1 67  ? 7.285  -9.650  -27.536 1.00 34.31  ? 67  TRP A CA   1 
ATOM   1046 C C    . TRP A 1 67  ? 8.068  -8.476  -28.107 1.00 35.37  ? 67  TRP A C    1 
ATOM   1047 O O    . TRP A 1 67  ? 7.599  -7.338  -28.082 1.00 33.92  ? 67  TRP A O    1 
ATOM   1048 C CB   . TRP A 1 67  ? 6.370  -10.258 -28.603 1.00 38.76  ? 67  TRP A CB   1 
ATOM   1049 C CG   . TRP A 1 67  ? 5.629  -11.440 -28.067 1.00 38.41  ? 67  TRP A CG   1 
ATOM   1050 C CD1  . TRP A 1 67  ? 4.306  -11.506 -27.740 1.00 39.04  ? 67  TRP A CD1  1 
ATOM   1051 C CD2  . TRP A 1 67  ? 6.191  -12.721 -27.756 1.00 37.72  ? 67  TRP A CD2  1 
ATOM   1052 N NE1  . TRP A 1 67  ? 4.009  -12.763 -27.254 1.00 46.59  ? 67  TRP A NE1  1 
ATOM   1053 C CE2  . TRP A 1 67  ? 5.151  -13.521 -27.254 1.00 42.02  ? 67  TRP A CE2  1 
ATOM   1054 C CE3  . TRP A 1 67  ? 7.471  -13.268 -27.871 1.00 41.37  ? 67  TRP A CE3  1 
ATOM   1055 C CZ2  . TRP A 1 67  ? 5.355  -14.840 -26.864 1.00 43.27  ? 67  TRP A CZ2  1 
ATOM   1056 C CZ3  . TRP A 1 67  ? 7.671  -14.572 -27.481 1.00 43.24  ? 67  TRP A CZ3  1 
ATOM   1057 C CH2  . TRP A 1 67  ? 6.619  -15.344 -26.984 1.00 42.09  ? 67  TRP A CH2  1 
ATOM   1058 H H    . TRP A 1 67  ? 5.688  -9.015  -26.552 1.00 33.11  ? 67  TRP A H    1 
ATOM   1059 H HA   . TRP A 1 67  ? 7.938  -10.316 -27.268 1.00 41.31  ? 67  TRP A HA   1 
ATOM   1060 H HB2  . TRP A 1 67  ? 5.723  -9.594  -28.889 1.00 46.64  ? 67  TRP A HB2  1 
ATOM   1061 H HB3  . TRP A 1 67  ? 6.904  -10.548 -29.359 1.00 46.64  ? 67  TRP A HB3  1 
ATOM   1062 H HD1  . TRP A 1 67  ? 3.697  -10.810 -27.831 1.00 46.98  ? 67  TRP A HD1  1 
ATOM   1063 H HE1  . TRP A 1 67  ? 3.233  -13.028 -26.995 1.00 56.04  ? 67  TRP A HE1  1 
ATOM   1064 H HE3  . TRP A 1 67  ? 8.174  -12.761 -28.206 1.00 49.78  ? 67  TRP A HE3  1 
ATOM   1065 H HZ2  . TRP A 1 67  ? 4.658  -15.360 -26.536 1.00 52.06  ? 67  TRP A HZ2  1 
ATOM   1066 H HZ3  . TRP A 1 67  ? 8.520  -14.945 -27.549 1.00 52.02  ? 67  TRP A HZ3  1 
ATOM   1067 H HH2  . TRP A 1 67  ? 6.783  -16.222 -26.727 1.00 50.64  ? 67  TRP A HH2  1 
ATOM   1068 N N    . GLY A 1 68  ? 9.280  -8.746  -28.581 1.00 40.70  ? 68  GLY A N    1 
ATOM   1069 C CA   . GLY A 1 68  ? 10.036 -7.768  -29.337 1.00 46.74  ? 68  GLY A CA   1 
ATOM   1070 C C    . GLY A 1 68  ? 9.652  -7.777  -30.807 1.00 56.72  ? 68  GLY A C    1 
ATOM   1071 O O    . GLY A 1 68  ? 8.697  -8.429  -31.233 1.00 55.42  ? 68  GLY A O    1 
ATOM   1072 H H    . GLY A 1 68  ? 9.686  -9.497  -28.475 1.00 48.97  ? 68  GLY A H    1 
ATOM   1073 H HA2  . GLY A 1 68  ? 9.869  -6.882  -28.980 1.00 56.22  ? 68  GLY A HA2  1 
ATOM   1074 H HA3  . GLY A 1 68  ? 10.983 -7.965  -29.265 1.00 56.22  ? 68  GLY A HA3  1 
ATOM   1075 N N    . ASP A 1 69  ? 10.429 -7.043  -31.600 1.00 64.48  ? 69  ASP A N    1 
ATOM   1076 C CA   . ASP A 1 69  ? 10.145 -6.928  -33.033 1.00 66.92  ? 69  ASP A CA   1 
ATOM   1077 C C    . ASP A 1 69  ? 10.061 -8.304  -33.691 1.00 71.75  ? 69  ASP A C    1 
ATOM   1078 O O    . ASP A 1 69  ? 9.564  -8.448  -34.802 1.00 77.69  ? 69  ASP A O    1 
ATOM   1079 C CB   . ASP A 1 69  ? 11.211 -6.088  -33.744 1.00 80.51  ? 69  ASP A CB   1 
ATOM   1080 C CG   . ASP A 1 69  ? 10.858 -5.809  -35.199 1.00 95.62  ? 69  ASP A CG   1 
ATOM   1081 O OD1  . ASP A 1 69  ? 9.688  -6.026  -35.583 1.00 92.05  ? 69  ASP A OD1  1 
ATOM   1082 O OD2  . ASP A 1 69  ? 11.748 -5.374  -35.957 1.00 102.18 ? 69  ASP A OD2  1 
ATOM   1083 H H    . ASP A 1 69  ? 11.121 -6.606  -31.337 1.00 77.51  ? 69  ASP A H    1 
ATOM   1084 H HA   . ASP A 1 69  ? 9.291  -6.480  -33.136 1.00 80.44  ? 69  ASP A HA   1 
ATOM   1085 H HB2  . ASP A 1 69  ? 11.302 -5.237  -33.288 1.00 96.75  ? 69  ASP A HB2  1 
ATOM   1086 H HB3  . ASP A 1 69  ? 12.055 -6.566  -33.726 1.00 96.75  ? 69  ASP A HB3  1 
ATOM   1087 N N    . ARG A 1 75  ? 10.692 -15.257 -32.702 1.00 46.65  ? 75  ARG A N    1 
ATOM   1088 C CA   . ARG A 1 75  ? 9.979  -14.294 -31.866 1.00 49.45  ? 75  ARG A CA   1 
ATOM   1089 C C    . ARG A 1 75  ? 10.516 -14.296 -30.436 1.00 44.63  ? 75  ARG A C    1 
ATOM   1090 O O    . ARG A 1 75  ? 10.572 -15.340 -29.781 1.00 42.49  ? 75  ARG A O    1 
ATOM   1091 C CB   . ARG A 1 75  ? 8.490  -14.606 -31.876 1.00 50.67  ? 75  ARG A CB   1 
ATOM   1092 C CG   . ARG A 1 75  ? 7.601  -13.497 -31.377 1.00 49.83  ? 75  ARG A CG   1 
ATOM   1093 C CD   . ARG A 1 75  ? 6.156  -13.924 -31.520 1.00 50.87  ? 75  ARG A CD   1 
ATOM   1094 N NE   . ARG A 1 75  ? 5.227  -12.901 -31.060 1.00 53.46  ? 75  ARG A NE   1 
ATOM   1095 C CZ   . ARG A 1 75  ? 4.839  -11.867 -31.791 1.00 56.21  ? 75  ARG A CZ   1 
ATOM   1096 N NH1  . ARG A 1 75  ? 5.278  -11.692 -33.027 1.00 59.37  ? 75  ARG A NH1  1 
ATOM   1097 N NH2  . ARG A 1 75  ? 3.994  -10.985 -31.266 1.00 59.75  ? 75  ARG A NH2  1 
ATOM   1098 N N    . ARG A 1 76  ? 10.877 -13.118 -29.940 1.00 39.90  ? 76  ARG A N    1 
ATOM   1099 C CA   . ARG A 1 76  ? 11.698 -12.984 -28.743 1.00 39.73  ? 76  ARG A CA   1 
ATOM   1100 C C    . ARG A 1 76  ? 10.912 -12.393 -27.586 1.00 36.41  ? 76  ARG A C    1 
ATOM   1101 O O    . ARG A 1 76  ? 10.200 -11.399 -27.755 1.00 36.37  ? 76  ARG A O    1 
ATOM   1102 C CB   . ARG A 1 76  ? 12.915 -12.109 -29.037 1.00 39.91  ? 76  ARG A CB   1 
ATOM   1103 C CG   . ARG A 1 76  ? 13.760 -11.763 -27.840 1.00 35.49  ? 76  ARG A CG   1 
ATOM   1104 C CD   . ARG A 1 76  ? 15.125 -11.351 -28.327 1.00 40.65  ? 76  ARG A CD   1 
ATOM   1105 N NE   . ARG A 1 76  ? 15.846 -12.488 -28.883 1.00 39.35  ? 76  ARG A NE   1 
ATOM   1106 C CZ   . ARG A 1 76  ? 17.083 -12.434 -29.354 1.00 47.36  ? 76  ARG A CZ   1 
ATOM   1107 N NH1  . ARG A 1 76  ? 17.744 -11.289 -29.440 1.00 44.63  ? 76  ARG A NH1  1 
ATOM   1108 N NH2  . ARG A 1 76  ? 17.673 -13.559 -29.744 1.00 47.89  ? 76  ARG A NH2  1 
ATOM   1109 H HA   . ARG A 1 76  ? 11.983 -13.869 -28.467 1.00 47.81  ? 76  ARG A HA   1 
ATOM   1110 H HB2  . ARG A 1 76  ? 13.484 -12.577 -29.668 1.00 48.03  ? 76  ARG A HB2  1 
ATOM   1111 H HB3  . ARG A 1 76  ? 12.606 -11.275 -29.425 1.00 48.03  ? 76  ARG A HB3  1 
ATOM   1112 H HG2  . ARG A 1 76  ? 13.361 -11.025 -27.352 1.00 42.72  ? 76  ARG A HG2  1 
ATOM   1113 H HG3  . ARG A 1 76  ? 13.849 -12.535 -27.260 1.00 42.72  ? 76  ARG A HG3  1 
ATOM   1114 H HD2  . ARG A 1 76  ? 15.031 -10.678 -29.019 1.00 48.92  ? 76  ARG A HD2  1 
ATOM   1115 H HD3  . ARG A 1 76  ? 15.639 -10.995 -27.585 1.00 48.92  ? 76  ARG A HD3  1 
ATOM   1116 H HE   . ARG A 1 76  ? 15.441 -13.246 -28.908 1.00 47.35  ? 76  ARG A HE   1 
ATOM   1117 H HH11 . ARG A 1 76  ? 17.370 -10.557 -29.188 1.00 53.70  ? 76  ARG A HH11 1 
ATOM   1118 H HH12 . ARG A 1 76  ? 18.546 -11.278 -29.749 1.00 53.70  ? 76  ARG A HH12 1 
ATOM   1119 H HH21 . ARG A 1 76  ? 17.252 -14.306 -29.689 1.00 57.61  ? 76  ARG A HH21 1 
ATOM   1120 H HH22 . ARG A 1 76  ? 18.476 -13.539 -30.051 1.00 57.61  ? 76  ARG A HH22 1 
ATOM   1121 N N    . LYS A 1 77  ? 11.057 -12.997 -26.410 1.00 32.48  ? 77  LYS A N    1 
ATOM   1122 C CA   . LYS A 1 77  ? 10.294 -12.592 -25.241 1.00 29.37  ? 77  LYS A CA   1 
ATOM   1123 C C    . LYS A 1 77  ? 11.153 -11.704 -24.358 1.00 25.75  ? 77  LYS A C    1 
ATOM   1124 O O    . LYS A 1 77  ? 12.245 -12.087 -23.930 1.00 28.44  ? 77  LYS A O    1 
ATOM   1125 C CB   . LYS A 1 77  ? 9.787  -13.809 -24.467 1.00 32.21  ? 77  LYS A CB   1 
ATOM   1126 C CG   . LYS A 1 77  ? 8.713  -13.497 -23.458 1.00 32.66  ? 77  LYS A CG   1 
ATOM   1127 C CD   . LYS A 1 77  ? 8.157  -14.785 -22.815 1.00 35.67  ? 77  LYS A CD   1 
ATOM   1128 C CE   . LYS A 1 77  ? 6.680  -14.978 -23.016 1.00 48.05  ? 77  LYS A CE   1 
ATOM   1129 N NZ   . LYS A 1 77  ? 6.259  -16.255 -22.351 1.00 48.74  ? 77  LYS A NZ   1 
ATOM   1130 H H    . LYS A 1 77  ? 11.597 -13.650 -26.267 1.00 39.11  ? 77  LYS A H    1 
ATOM   1131 H HA   . LYS A 1 77  ? 9.524  -12.075 -25.525 1.00 35.38  ? 77  LYS A HA   1 
ATOM   1132 H HB2  . LYS A 1 77  ? 9.421  -14.448 -25.099 1.00 38.79  ? 77  LYS A HB2  1 
ATOM   1133 H HB3  . LYS A 1 77  ? 10.533 -14.206 -23.990 1.00 38.79  ? 77  LYS A HB3  1 
ATOM   1134 H HG2  . LYS A 1 77  ? 9.082  -12.940 -22.756 1.00 39.32  ? 77  LYS A HG2  1 
ATOM   1135 H HG3  . LYS A 1 77  ? 7.982  -13.036 -23.898 1.00 39.32  ? 77  LYS A HG3  1 
ATOM   1136 H HD2  . LYS A 1 77  ? 8.610  -15.549 -23.204 1.00 42.94  ? 77  LYS A HD2  1 
ATOM   1137 H HD3  . LYS A 1 77  ? 8.322  -14.752 -21.859 1.00 42.94  ? 77  LYS A HD3  1 
ATOM   1138 H HE2  . LYS A 1 77  ? 6.193  -14.240 -22.618 1.00 57.80  ? 77  LYS A HE2  1 
ATOM   1139 H HE3  . LYS A 1 77  ? 6.480  -15.035 -23.963 1.00 57.80  ? 77  LYS A HE3  1 
ATOM   1140 H HZ1  . LYS A 1 77  ? 5.375  -16.346 -22.398 1.00 58.63  ? 77  LYS A HZ1  1 
ATOM   1141 H HZ2  . LYS A 1 77  ? 6.642  -16.949 -22.754 1.00 58.63  ? 77  LYS A HZ2  1 
ATOM   1142 H HZ3  . LYS A 1 77  ? 6.503  -16.247 -21.495 1.00 58.63  ? 77  LYS A HZ3  1 
ATOM   1143 N N    . TYR A 1 78  ? 10.657 -10.510 -24.105 1.00 27.92  ? 78  TYR A N    1 
ATOM   1144 C CA   . TYR A 1 78  ? 11.295 -9.571  -23.203 1.00 25.00  ? 78  TYR A CA   1 
ATOM   1145 C C    . TYR A 1 78  ? 10.555 -9.535  -21.873 1.00 25.93  ? 78  TYR A C    1 
ATOM   1146 O O    . TYR A 1 78  ? 9.358  -9.794  -21.807 1.00 24.28  ? 78  TYR A O    1 
ATOM   1147 C CB   . TYR A 1 78  ? 11.345 -8.167  -23.833 1.00 29.45  ? 78  TYR A CB   1 
ATOM   1148 C CG   . TYR A 1 78  ? 12.475 -8.023  -24.847 1.00 33.02  ? 78  TYR A CG   1 
ATOM   1149 C CD1  . TYR A 1 78  ? 12.308 -8.425  -26.164 1.00 43.22  ? 78  TYR A CD1  1 
ATOM   1150 C CD2  . TYR A 1 78  ? 13.689 -7.462  -24.488 1.00 39.99  ? 78  TYR A CD2  1 
ATOM   1151 C CE1  . TYR A 1 78  ? 13.336 -8.297  -27.092 1.00 43.73  ? 78  TYR A CE1  1 
ATOM   1152 C CE2  . TYR A 1 78  ? 14.722 -7.339  -25.405 1.00 43.34  ? 78  TYR A CE2  1 
ATOM   1153 C CZ   . TYR A 1 78  ? 14.534 -7.752  -26.708 1.00 48.63  ? 78  TYR A CZ   1 
ATOM   1154 O OH   . TYR A 1 78  ? 15.558 -7.615  -27.625 1.00 53.86  ? 78  TYR A OH   1 
ATOM   1155 H H    . TYR A 1 78  ? 9.930  -10.210 -24.453 1.00 33.63  ? 78  TYR A H    1 
ATOM   1156 H HA   . TYR A 1 78  ? 12.207 -9.849  -23.026 1.00 30.14  ? 78  TYR A HA   1 
ATOM   1157 H HB2  . TYR A 1 78  ? 10.507 -7.995  -24.289 1.00 35.48  ? 78  TYR A HB2  1 
ATOM   1158 H HB3  . TYR A 1 78  ? 11.483 -7.510  -23.133 1.00 35.48  ? 78  TYR A HB3  1 
ATOM   1159 H HD1  . TYR A 1 78  ? 11.494 -8.787  -26.432 1.00 52.00  ? 78  TYR A HD1  1 
ATOM   1160 H HD2  . TYR A 1 78  ? 13.813 -7.162  -23.617 1.00 48.12  ? 78  TYR A HD2  1 
ATOM   1161 H HE1  . TYR A 1 78  ? 13.212 -8.579  -27.969 1.00 52.61  ? 78  TYR A HE1  1 
ATOM   1162 H HE2  . TYR A 1 78  ? 15.539 -6.980  -25.143 1.00 52.14  ? 78  TYR A HE2  1 
ATOM   1163 H HH   . TYR A 1 78  ? 15.344 -7.978  -28.352 1.00 64.76  ? 78  TYR A HH   1 
ATOM   1164 N N    . TYR A 1 79  ? 11.306 -9.265  -20.810 1.00 25.49  ? 79  TYR A N    1 
ATOM   1165 C CA   . TYR A 1 79  ? 10.796 -9.186  -19.451 1.00 24.09  ? 79  TYR A CA   1 
ATOM   1166 C C    . TYR A 1 79  ? 11.071 -7.808  -18.878 1.00 25.50  ? 79  TYR A C    1 
ATOM   1167 O O    . TYR A 1 79  ? 12.117 -7.207  -19.153 1.00 25.36  ? 79  TYR A O    1 
ATOM   1168 C CB   . TYR A 1 79  ? 11.438 -10.276 -18.585 1.00 27.18  ? 79  TYR A CB   1 
ATOM   1169 C CG   . TYR A 1 79  ? 11.048 -11.635 -19.019 1.00 28.51  ? 79  TYR A CG   1 
ATOM   1170 C CD1  . TYR A 1 79  ? 9.892  -12.243 -18.519 1.00 25.99  ? 79  TYR A CD1  1 
ATOM   1171 C CD2  . TYR A 1 79  ? 11.836 -12.328 -19.911 1.00 31.23  ? 79  TYR A CD2  1 
ATOM   1172 C CE1  . TYR A 1 79  ? 9.536  -13.528 -18.930 1.00 27.13  ? 79  TYR A CE1  1 
ATOM   1173 C CE2  . TYR A 1 79  ? 11.491 -13.573 -20.322 1.00 31.62  ? 79  TYR A CE2  1 
ATOM   1174 C CZ   . TYR A 1 79  ? 10.349 -14.165 -19.827 1.00 31.63  ? 79  TYR A CZ   1 
ATOM   1175 O OH   . TYR A 1 79  ? 10.024 -15.433 -20.248 1.00 39.50  ? 79  TYR A OH   1 
ATOM   1176 H H    . TYR A 1 79  ? 12.152 -9.118  -20.856 1.00 30.72  ? 79  TYR A H    1 
ATOM   1177 H HA   . TYR A 1 79  ? 9.835  -9.313  -19.440 1.00 28.24  ? 79  TYR A HA   1 
ATOM   1178 H HB2  . TYR A 1 79  ? 12.403 -10.203 -18.647 1.00 32.76  ? 79  TYR A HB2  1 
ATOM   1179 H HB3  . TYR A 1 79  ? 11.154 -10.158 -17.665 1.00 32.76  ? 79  TYR A HB3  1 
ATOM   1180 H HD1  . TYR A 1 79  ? 9.357  -11.788 -17.908 1.00 31.33  ? 79  TYR A HD1  1 
ATOM   1181 H HD2  . TYR A 1 79  ? 12.614 -11.936 -20.237 1.00 37.61  ? 79  TYR A HD2  1 
ATOM   1182 H HE1  . TYR A 1 79  ? 8.768  -13.939 -18.605 1.00 32.69  ? 79  TYR A HE1  1 
ATOM   1183 H HE2  . TYR A 1 79  ? 12.023 -14.027 -20.935 1.00 38.08  ? 79  TYR A HE2  1 
ATOM   1184 H HH   . TYR A 1 79  ? 10.586 -15.701 -20.813 1.00 47.54  ? 79  TYR A HH   1 
ATOM   1185 N N    . ARG A 1 80  ? 10.141 -7.335  -18.062 1.00 24.80  ? 80  ARG A N    1 
ATOM   1186 C CA   . ARG A 1 80  ? 10.254 -6.049  -17.403 1.00 24.44  ? 80  ARG A CA   1 
ATOM   1187 C C    . ARG A 1 80  ? 9.806  -6.172  -15.959 1.00 23.93  ? 80  ARG A C    1 
ATOM   1188 O O    . ARG A 1 80  ? 8.832  -6.859  -15.669 1.00 25.98  ? 80  ARG A O    1 
ATOM   1189 C CB   . ARG A 1 80  ? 9.407  -5.006  -18.108 1.00 24.99  ? 80  ARG A CB   1 
ATOM   1190 C CG   . ARG A 1 80  ? 7.946  -5.395  -18.286 1.00 25.55  ? 80  ARG A CG   1 
ATOM   1191 C CD   . ARG A 1 80  ? 7.121  -4.226  -18.908 1.00 29.33  ? 80  ARG A CD   1 
ATOM   1192 N NE   . ARG A 1 80  ? 6.839  -3.214  -17.900 1.00 32.34  ? 80  ARG A NE   1 
ATOM   1193 C CZ   . ARG A 1 80  ? 5.819  -3.280  -17.055 1.00 28.57  ? 80  ARG A CZ   1 
ATOM   1194 N NH1  . ARG A 1 80  ? 5.079  -4.364  -16.945 1.00 28.59  ? 80  ARG A NH1  1 
ATOM   1195 N NH2  . ARG A 1 80  ? 5.568  -2.238  -16.262 1.00 36.14  ? 80  ARG A NH2  1 
ATOM   1196 H H    . ARG A 1 80  ? 9.416  -7.754  -17.870 1.00 29.89  ? 80  ARG A H    1 
ATOM   1197 H HA   . ARG A 1 80  ? 11.180 -5.762  -17.408 1.00 29.46  ? 80  ARG A HA   1 
ATOM   1198 H HB2  . ARG A 1 80  ? 9.430  -4.186  -17.590 1.00 30.12  ? 80  ARG A HB2  1 
ATOM   1199 H HB3  . ARG A 1 80  ? 9.778  -4.851  -18.991 1.00 30.12  ? 80  ARG A HB3  1 
ATOM   1200 H HG2  . ARG A 1 80  ? 7.887  -6.161  -18.878 1.00 30.79  ? 80  ARG A HG2  1 
ATOM   1201 H HG3  . ARG A 1 80  ? 7.564  -5.614  -17.422 1.00 30.79  ? 80  ARG A HG3  1 
ATOM   1202 H HD2  . ARG A 1 80  ? 7.628  -3.815  -19.626 1.00 35.33  ? 80  ARG A HD2  1 
ATOM   1203 H HD3  . ARG A 1 80  ? 6.280  -4.566  -19.250 1.00 35.33  ? 80  ARG A HD3  1 
ATOM   1204 H HE   . ARG A 1 80  ? 7.363  -2.534  -17.849 1.00 38.94  ? 80  ARG A HE   1 
ATOM   1205 H HH11 . ARG A 1 80  ? 5.253  -5.053  -17.429 1.00 34.45  ? 80  ARG A HH11 1 
ATOM   1206 H HH12 . ARG A 1 80  ? 4.423  -4.382  -16.390 1.00 34.45  ? 80  ARG A HH12 1 
ATOM   1207 H HH21 . ARG A 1 80  ? 6.065  -1.538  -16.303 1.00 43.50  ? 80  ARG A HH21 1 
ATOM   1208 H HH22 . ARG A 1 80  ? 4.910  -2.267  -15.709 1.00 43.50  ? 80  ARG A HH22 1 
ATOM   1209 N N    . LEU A 1 81  ? 10.441 -5.421  -15.068 1.00 25.41  ? 81  LEU A N    1 
ATOM   1210 C CA   . LEU A 1 81  ? 9.852  -5.207  -13.753 1.00 24.92  ? 81  LEU A CA   1 
ATOM   1211 C C    . LEU A 1 81  ? 8.549  -4.435  -13.893 1.00 26.71  ? 81  LEU A C    1 
ATOM   1212 O O    . LEU A 1 81  ? 8.441  -3.498  -14.699 1.00 30.43  ? 81  LEU A O    1 
ATOM   1213 C CB   . LEU A 1 81  ? 10.786 -4.406  -12.858 1.00 28.97  ? 81  LEU A CB   1 
ATOM   1214 C CG   . LEU A 1 81  ? 12.023 -5.050  -12.306 1.00 28.17  ? 81  LEU A CG   1 
ATOM   1215 C CD1  . LEU A 1 81  ? 12.776 -4.006  -11.461 1.00 32.31  ? 81  LEU A CD1  1 
ATOM   1216 C CD2  . LEU A 1 81  ? 11.689 -6.315  -11.508 1.00 28.06  ? 81  LEU A CD2  1 
ATOM   1217 H H    . LEU A 1 81  ? 11.198 -5.033  -15.197 1.00 30.63  ? 81  LEU A H    1 
ATOM   1218 H HA   . LEU A 1 81  ? 9.692  -6.071  -13.341 1.00 30.04  ? 81  LEU A HA   1 
ATOM   1219 H HB2  . LEU A 1 81  ? 11.086 -3.638  -13.369 1.00 34.90  ? 81  LEU A HB2  1 
ATOM   1220 H HB3  . LEU A 1 81  ? 10.269 -4.113  -12.091 1.00 34.90  ? 81  LEU A HB3  1 
ATOM   1221 H HG   . LEU A 1 81  ? 12.603 -5.344  -13.025 1.00 33.94  ? 81  LEU A HG   1 
ATOM   1222 H HD11 . LEU A 1 81  ? 13.491 -4.448  -10.977 1.00 38.90  ? 81  LEU A HD11 1 
ATOM   1223 H HD12 . LEU A 1 81  ? 13.145 -3.330  -12.050 1.00 38.90  ? 81  LEU A HD12 1 
ATOM   1224 H HD13 . LEU A 1 81  ? 12.156 -3.599  -10.837 1.00 38.90  ? 81  LEU A HD13 1 
ATOM   1225 H HD21 . LEU A 1 81  ? 12.494 -6.636  -11.073 1.00 33.80  ? 81  LEU A HD21 1 
ATOM   1226 H HD22 . LEU A 1 81  ? 11.017 -6.100  -10.842 1.00 33.80  ? 81  LEU A HD22 1 
ATOM   1227 H HD23 . LEU A 1 81  ? 11.349 -6.991  -12.115 1.00 33.80  ? 81  LEU A HD23 1 
ATOM   1228 N N    . THR A 1 82  ? 7.536  -4.841  -13.135 1.00 26.90  ? 82  THR A N    1 
ATOM   1229 C CA   . THR A 1 82  ? 6.290  -4.096  -13.096 1.00 27.33  ? 82  THR A CA   1 
ATOM   1230 C C    . THR A 1 82  ? 6.459  -2.885  -12.186 1.00 28.66  ? 82  THR A C    1 
ATOM   1231 O O    . THR A 1 82  ? 7.451  -2.748  -11.481 1.00 30.81  ? 82  THR A O    1 
ATOM   1232 C CB   . THR A 1 82  ? 5.164  -4.979  -12.594 1.00 25.99  ? 82  THR A CB   1 
ATOM   1233 O OG1  . THR A 1 82  ? 5.436  -5.357  -11.247 1.00 27.25  ? 82  THR A OG1  1 
ATOM   1234 C CG2  . THR A 1 82  ? 4.973  -6.194  -13.469 1.00 28.96  ? 82  THR A CG2  1 
ATOM   1235 H H    . THR A 1 82  ? 7.548  -5.542  -12.637 1.00 32.42  ? 82  THR A H    1 
ATOM   1236 H HA   . THR A 1 82  ? 6.056  -3.794  -13.988 1.00 32.93  ? 82  THR A HA   1 
ATOM   1237 H HB   . THR A 1 82  ? 4.326  -4.491  -12.624 1.00 31.33  ? 82  THR A HB   1 
ATOM   1238 H HG1  . THR A 1 82  ? 5.089  -6.103  -11.082 1.00 32.84  ? 82  THR A HG1  1 
ATOM   1239 H HG21 . THR A 1 82  ? 4.228  -6.723  -13.144 1.00 34.89  ? 82  THR A HG21 1 
ATOM   1240 H HG22 . THR A 1 82  ? 4.790  -5.920  -14.382 1.00 34.89  ? 82  THR A HG22 1 
ATOM   1241 H HG23 . THR A 1 82  ? 5.775  -6.739  -13.459 1.00 34.89  ? 82  THR A HG23 1 
ATOM   1242 N N    . GLU A 1 83  ? 5.418  -2.049  -12.135 1.00 33.15  ? 83  GLU A N    1 
ATOM   1243 C CA   . GLU A 1 83  ? 5.442  -0.936  -11.196 1.00 33.12  ? 83  GLU A CA   1 
ATOM   1244 C C    . GLU A 1 83  ? 5.655  -1.460  -9.791  1.00 33.16  ? 83  GLU A C    1 
ATOM   1245 O O    . GLU A 1 83  ? 6.551  -1.009  -9.068  1.00 35.44  ? 83  GLU A O    1 
ATOM   1246 C CB   . GLU A 1 83  ? 4.156  -0.125  -11.309 1.00 38.55  ? 83  GLU A CB   1 
ATOM   1247 C CG   . GLU A 1 83  ? 4.064  0.615   -12.625 1.00 36.00  ? 83  GLU A CG   1 
ATOM   1248 C CD   . GLU A 1 83  ? 2.852  1.519   -12.710 1.00 50.50  ? 83  GLU A CD   1 
ATOM   1249 O OE1  . GLU A 1 83  ? 2.072  1.568   -11.738 1.00 49.34  ? 83  GLU A OE1  1 
ATOM   1250 O OE2  . GLU A 1 83  ? 2.686  2.173   -13.756 1.00 47.45  ? 83  GLU A OE2  1 
ATOM   1251 H H    . GLU A 1 83  ? 4.711  -2.105  -12.620 1.00 39.91  ? 83  GLU A H    1 
ATOM   1252 H HA   . GLU A 1 83  ? 6.170  -0.333  -11.411 1.00 39.23  ? 83  GLU A HA   1 
ATOM   1253 H HB2  . GLU A 1 83  ? 3.395  -0.723  -11.244 1.00 46.40  ? 83  GLU A HB2  1 
ATOM   1254 H HB3  . GLU A 1 83  ? 4.127  0.527   -10.592 1.00 46.40  ? 83  GLU A HB3  1 
ATOM   1255 H HG2  . GLU A 1 83  ? 4.855  1.165   -12.734 1.00 43.33  ? 83  GLU A HG2  1 
ATOM   1256 H HG3  . GLU A 1 83  ? 4.006  -0.030  -13.347 1.00 43.33  ? 83  GLU A HG3  1 
ATOM   1257 N N    . ILE A 1 84  ? 4.892  -2.481  -9.402  1.00 32.52  ? 84  ILE A N    1 
ATOM   1258 C CA   . ILE A 1 84  ? 5.072  -2.999  -8.058  1.00 35.97  ? 84  ILE A CA   1 
ATOM   1259 C C    . ILE A 1 84  ? 6.375  -3.781  -7.948  1.00 35.21  ? 84  ILE A C    1 
ATOM   1260 O O    . ILE A 1 84  ? 6.978  -3.839  -6.873  1.00 37.68  ? 84  ILE A O    1 
ATOM   1261 C CB   . ILE A 1 84  ? 3.864  -3.846  -7.637  1.00 39.23  ? 84  ILE A CB   1 
ATOM   1262 C CG1  . ILE A 1 84  ? 3.951  -4.111  -6.136  1.00 56.61  ? 84  ILE A CG1  1 
ATOM   1263 C CG2  . ILE A 1 84  ? 3.824  -5.106  -8.413  1.00 31.88  ? 84  ILE A CG2  1 
ATOM   1264 C CD1  . ILE A 1 84  ? 3.949  -2.841  -5.288  1.00 60.64  ? 84  ILE A CD1  1 
ATOM   1265 H H    . ILE A 1 84  ? 4.291  -2.871  -9.878  1.00 38.35  ? 84  ILE A H    1 
ATOM   1266 H HA   . ILE A 1 84  ? 5.127  -2.245  -7.450  1.00 43.29  ? 84  ILE A HA   1 
ATOM   1267 H HB   . ILE A 1 84  ? 3.041  -3.367  -7.823  1.00 47.21  ? 84  ILE A HB   1 
ATOM   1268 H HG12 . ILE A 1 84  ? 3.188  -4.647  -5.868  1.00 68.07  ? 84  ILE A HG12 1 
ATOM   1269 H HG13 . ILE A 1 84  ? 4.774  -4.590  -5.951  1.00 68.07  ? 84  ILE A HG13 1 
ATOM   1270 H HG21 . ILE A 1 84  ? 2.953  -5.518  -8.304  1.00 38.39  ? 84  ILE A HG21 1 
ATOM   1271 H HG22 . ILE A 1 84  ? 3.980  -4.906  -9.349  1.00 38.39  ? 84  ILE A HG22 1 
ATOM   1272 H HG23 . ILE A 1 84  ? 4.515  -5.702  -8.083  1.00 38.39  ? 84  ILE A HG23 1 
ATOM   1273 H HD11 . ILE A 1 84  ? 3.712  -3.071  -4.376  1.00 72.91  ? 84  ILE A HD11 1 
ATOM   1274 H HD12 . ILE A 1 84  ? 4.834  -2.445  -5.311  1.00 72.91  ? 84  ILE A HD12 1 
ATOM   1275 H HD13 . ILE A 1 84  ? 3.299  -2.220  -5.652  1.00 72.91  ? 84  ILE A HD13 1 
ATOM   1276 N N    . GLY A 1 85  ? 6.830  -4.401  -9.040  1.00 31.00  ? 85  GLY A N    1 
ATOM   1277 C CA   . GLY A 1 85  ? 8.100  -5.099  -9.007  1.00 31.82  ? 85  GLY A CA   1 
ATOM   1278 C C    . GLY A 1 85  ? 9.237  -4.185  -8.604  1.00 30.49  ? 85  GLY A C    1 
ATOM   1279 O O    . GLY A 1 85  ? 10.150 -4.597  -7.889  1.00 30.32  ? 85  GLY A O    1 
ATOM   1280 H H    . GLY A 1 85  ? 6.425  -4.427  -9.799  1.00 37.34  ? 85  GLY A H    1 
ATOM   1281 H HA2  . GLY A 1 85  ? 8.051  -5.828  -8.368  1.00 38.32  ? 85  GLY A HA2  1 
ATOM   1282 H HA3  . GLY A 1 85  ? 8.293  -5.462  -9.885  1.00 38.32  ? 85  GLY A HA3  1 
ATOM   1283 N N    . HIS A 1 86  ? 9.183  -2.923  -9.043  1.00 31.49  ? 86  HIS A N    1 
ATOM   1284 C CA   . HIS A 1 86  ? 10.217 -1.958  -8.662  1.00 32.33  ? 86  HIS A CA   1 
ATOM   1285 C C    . HIS A 1 86  ? 10.216 -1.716  -7.159  1.00 33.08  ? 86  HIS A C    1 
ATOM   1286 O O    . HIS A 1 86  ? 11.283 -1.552  -6.558  1.00 33.24  ? 86  HIS A O    1 
ATOM   1287 C CB   . HIS A 1 86  ? 10.029 -0.636  -9.412  1.00 33.30  ? 86  HIS A CB   1 
ATOM   1288 C CG   . HIS A 1 86  ? 10.608 -0.640  -10.795 1.00 35.00  ? 86  HIS A CG   1 
ATOM   1289 N ND1  . HIS A 1 86  ? 11.928 -0.338  -11.055 1.00 39.69  ? 86  HIS A ND1  1 
ATOM   1290 C CD2  . HIS A 1 86  ? 10.049 -0.937  -11.993 1.00 40.20  ? 86  HIS A CD2  1 
ATOM   1291 C CE1  . HIS A 1 86  ? 12.154 -0.446  -12.354 1.00 40.05  ? 86  HIS A CE1  1 
ATOM   1292 N NE2  . HIS A 1 86  ? 11.029 -0.802  -12.946 1.00 37.48  ? 86  HIS A NE2  1 
ATOM   1293 H H    . HIS A 1 86  ? 8.568  -2.606  -9.554  1.00 37.11  ? 86  HIS A H    1 
ATOM   1294 H HA   . HIS A 1 86  ? 11.082 -2.315  -8.916  1.00 38.12  ? 86  HIS A HA   1 
ATOM   1295 H HB2  . HIS A 1 86  ? 9.080  -0.453  -9.489  1.00 39.48  ? 86  HIS A HB2  1 
ATOM   1296 H HB3  . HIS A 1 86  ? 10.464 0.072   -8.911  1.00 39.48  ? 86  HIS A HB3  1 
ATOM   1297 H HD1  . HIS A 1 86  ? 12.512 -0.115  -10.465 1.00 47.76  ? 86  HIS A HD1  1 
ATOM   1298 H HD2  . HIS A 1 86  ? 9.165  -1.185  -12.142 1.00 48.37  ? 86  HIS A HD2  1 
ATOM   1299 H HE1  . HIS A 1 86  ? 12.968 -0.297  -12.779 1.00 48.20  ? 86  HIS A HE1  1 
ATOM   1300 N N    . GLU A 1 87  ? 9.039  -1.734  -6.533  1.00 34.50  ? 87  GLU A N    1 
ATOM   1301 C CA   . GLU A 1 87  ? 8.996  -1.653  -5.080  1.00 35.60  ? 87  GLU A CA   1 
ATOM   1302 C C    . GLU A 1 87  ? 9.612  -2.896  -4.447  1.00 38.07  ? 87  GLU A C    1 
ATOM   1303 O O    . GLU A 1 87  ? 10.442 -2.799  -3.539  1.00 38.19  ? 87  GLU A O    1 
ATOM   1304 C CB   . GLU A 1 87  ? 7.554  -1.454  -4.622  1.00 40.56  ? 87  GLU A CB   1 
ATOM   1305 C CG   . GLU A 1 87  ? 7.406  -1.304  -3.125  1.00 55.45  ? 87  GLU A CG   1 
ATOM   1306 C CD   . GLU A 1 87  ? 8.125  -0.087  -2.572  1.00 63.04  ? 87  GLU A CD   1 
ATOM   1307 O OE1  . GLU A 1 87  ? 8.424  0.849   -3.347  1.00 64.32  ? 87  GLU A OE1  1 
ATOM   1308 O OE2  . GLU A 1 87  ? 8.393  -0.070  -1.353  1.00 58.04  ? 87  GLU A OE2  1 
ATOM   1309 H H    . GLU A 1 87  ? 8.272  -1.791  -6.918  1.00 41.53  ? 87  GLU A H    1 
ATOM   1310 H HA   . GLU A 1 87  ? 9.512  -0.887  -4.783  1.00 42.85  ? 87  GLU A HA   1 
ATOM   1311 H HB2  . GLU A 1 87  ? 7.204  -0.649  -5.036  1.00 48.80  ? 87  GLU A HB2  1 
ATOM   1312 H HB3  . GLU A 1 87  ? 7.031  -2.223  -4.897  1.00 48.80  ? 87  GLU A HB3  1 
ATOM   1313 H HG2  . GLU A 1 87  ? 6.464  -1.218  -2.909  1.00 66.68  ? 87  GLU A HG2  1 
ATOM   1314 H HG3  . GLU A 1 87  ? 7.774  -2.091  -2.692  1.00 66.68  ? 87  GLU A HG3  1 
ATOM   1315 N N    . ASN A 1 88  ? 9.210  -4.076  -4.902  1.00 34.56  ? 88  ASN A N    1 
ATOM   1316 C CA   A ASN A 1 88  ? 9.812  -5.282  -4.352  0.42 37.22  ? 88  ASN A CA   1 
ATOM   1317 C CA   B ASN A 1 88  ? 9.810  -5.313  -4.402  0.58 37.21  ? 88  ASN A CA   1 
ATOM   1318 C C    . ASN A 1 88  ? 11.319 -5.296  -4.586  1.00 35.99  ? 88  ASN A C    1 
ATOM   1319 O O    . ASN A 1 88  ? 12.078 -5.753  -3.720  1.00 37.04  ? 88  ASN A O    1 
ATOM   1320 C CB   A ASN A 1 88  ? 9.136  -6.517  -4.939  0.42 40.40  ? 88  ASN A CB   1 
ATOM   1321 C CB   B ASN A 1 88  ? 9.191  -6.507  -5.132  0.58 40.33  ? 88  ASN A CB   1 
ATOM   1322 C CG   A ASN A 1 88  ? 7.849  -6.879  -4.202  0.42 43.02  ? 88  ASN A CG   1 
ATOM   1323 C CG   B ASN A 1 88  ? 9.844  -7.830  -4.766  0.58 38.15  ? 88  ASN A CG   1 
ATOM   1324 O OD1  A ASN A 1 88  ? 7.046  -6.009  -3.848  0.42 48.71  ? 88  ASN A OD1  1 
ATOM   1325 O OD1  B ASN A 1 88  ? 9.586  -8.390  -3.704  0.58 43.57  ? 88  ASN A OD1  1 
ATOM   1326 N ND2  A ASN A 1 88  ? 7.658  -8.170  -3.954  0.42 46.90  ? 88  ASN A ND2  1 
ATOM   1327 N ND2  B ASN A 1 88  ? 10.682 -8.336  -5.652  0.58 33.79  ? 88  ASN A ND2  1 
ATOM   1328 H H    A ASN A 1 88  ? 8.611  -4.202  -5.506  0.42 41.60  ? 88  ASN A H    1 
ATOM   1329 H H    B ASN A 1 88  ? 8.597  -4.192  -5.494  0.58 41.60  ? 88  ASN A H    1 
ATOM   1330 H HA   A ASN A 1 88  ? 9.670  -5.307  -3.392  0.42 44.80  ? 88  ASN A HA   1 
ATOM   1331 H HA   B ASN A 1 88  ? 9.626  -5.403  -3.454  0.58 44.78  ? 88  ASN A HA   1 
ATOM   1332 H HB2  A ASN A 1 88  ? 8.914  -6.346  -5.868  0.42 48.62  ? 88  ASN A HB2  1 
ATOM   1333 H HB2  B ASN A 1 88  ? 8.250  -6.565  -4.901  0.58 48.53  ? 88  ASN A HB2  1 
ATOM   1334 H HB3  A ASN A 1 88  ? 9.742  -7.272  -4.876  0.42 48.62  ? 88  ASN A HB3  1 
ATOM   1335 H HB3  B ASN A 1 88  ? 9.291  -6.379  -6.088  0.58 48.53  ? 88  ASN A HB3  1 
ATOM   1336 H HD21 A ASN A 1 88  ? 6.949  -8.428  -3.542  0.42 56.42  ? 88  ASN A HD21 1 
ATOM   1337 H HD21 B ASN A 1 88  ? 11.078 -9.082  -5.493  0.58 40.68  ? 88  ASN A HD21 1 
ATOM   1338 H HD22 A ASN A 1 88  ? 8.244  -8.747  -4.206  0.42 56.42  ? 88  ASN A HD22 1 
ATOM   1339 H HD22 B ASN A 1 88  ? 10.833 -7.919  -6.389  0.58 40.68  ? 88  ASN A HD22 1 
ATOM   1340 N N    . MET A 1 89  ? 11.777 -4.787  -5.724  1.00 32.49  ? 89  MET A N    1 
ATOM   1341 C CA   . MET A 1 89  ? 13.221 -4.706  -5.927  1.00 30.27  ? 89  MET A CA   1 
ATOM   1342 C C    . MET A 1 89  ? 13.857 -3.815  -4.870  1.00 34.92  ? 89  MET A C    1 
ATOM   1343 O O    . MET A 1 89  ? 14.913 -4.147  -4.321  1.00 34.04  ? 89  MET A O    1 
ATOM   1344 C CB   . MET A 1 89  ? 13.534 -4.195  -7.324  1.00 30.75  ? 89  MET A CB   1 
ATOM   1345 C CG   . MET A 1 89  ? 15.021 -3.927  -7.586  1.00 40.28  ? 89  MET A CG   1 
ATOM   1346 S SD   . MET A 1 89  ? 16.016 -5.363  -8.063  1.00 41.52  ? 89  MET A SD   1 
ATOM   1347 C CE   . MET A 1 89  ? 15.900 -6.367  -6.589  1.00 35.22  ? 89  MET A CE   1 
ATOM   1348 H H    . MET A 1 89  ? 11.293 -4.492  -6.371  1.00 39.13  ? 89  MET A H    1 
ATOM   1349 H HA   . MET A 1 89  ? 13.597 -5.598  -5.860  1.00 36.46  ? 89  MET A HA   1 
ATOM   1350 H HB2  . MET A 1 89  ? 13.238 -4.856  -7.968  1.00 37.03  ? 89  MET A HB2  1 
ATOM   1351 H HB3  . MET A 1 89  ? 13.058 -3.361  -7.461  1.00 37.03  ? 89  MET A HB3  1 
ATOM   1352 H HG2  . MET A 1 89  ? 15.090 -3.280  -8.306  1.00 48.47  ? 89  MET A HG2  1 
ATOM   1353 H HG3  . MET A 1 89  ? 15.412 -3.565  -6.776  1.00 48.47  ? 89  MET A HG3  1 
ATOM   1354 H HE1  . MET A 1 89  ? 16.685 -6.934  -6.531  1.00 42.40  ? 89  MET A HE1  1 
ATOM   1355 H HE2  . MET A 1 89  ? 15.853 -5.786  -5.814  1.00 42.40  ? 89  MET A HE2  1 
ATOM   1356 H HE3  . MET A 1 89  ? 15.101 -6.914  -6.642  1.00 42.40  ? 89  MET A HE3  1 
ATOM   1357 N N    . ARG A 1 90  ? 13.214 -2.692  -4.550  1.00 34.39  ? 90  ARG A N    1 
ATOM   1358 C CA   . ARG A 1 90  ? 13.793 -1.782  -3.566  1.00 36.87  ? 90  ARG A CA   1 
ATOM   1359 C C    . ARG A 1 90  ? 13.868 -2.425  -2.190  1.00 39.15  ? 90  ARG A C    1 
ATOM   1360 O O    . ARG A 1 90  ? 14.883 -2.303  -1.491  1.00 37.80  ? 90  ARG A O    1 
ATOM   1361 C CB   . ARG A 1 90  ? 12.969 -0.503  -3.498  1.00 40.63  ? 90  ARG A CB   1 
ATOM   1362 C CG   . ARG A 1 90  ? 13.684 0.642   -2.811  1.00 43.65  ? 90  ARG A CG   1 
ATOM   1363 C CD   . ARG A 1 90  ? 12.802 1.867   -2.729  1.00 47.83  ? 90  ARG A CD   1 
ATOM   1364 N NE   . ARG A 1 90  ? 11.560 1.572   -2.028  1.00 58.70  ? 90  ARG A NE   1 
ATOM   1365 C CZ   . ARG A 1 90  ? 11.451 1.458   -0.712  1.00 67.61  ? 90  ARG A CZ   1 
ATOM   1366 N NH1  . ARG A 1 90  ? 12.496 1.609   0.084   1.00 69.56  ? 90  ARG A NH1  1 
ATOM   1367 N NH2  . ARG A 1 90  ? 10.262 1.184   -0.182  1.00 69.24  ? 90  ARG A NH2  1 
ATOM   1368 H H    . ARG A 1 90  ? 12.461 -2.440  -4.880  1.00 41.41  ? 90  ARG A H    1 
ATOM   1369 H HA   . ARG A 1 90  ? 14.694 -1.558  -3.845  1.00 44.38  ? 90  ARG A HA   1 
ATOM   1370 H HB2  . ARG A 1 90  ? 12.755 -0.220  -4.401  1.00 48.89  ? 90  ARG A HB2  1 
ATOM   1371 H HB3  . ARG A 1 90  ? 12.153 -0.682  -3.005  1.00 48.89  ? 90  ARG A HB3  1 
ATOM   1372 H HG2  . ARG A 1 90  ? 13.924 0.377   -1.909  1.00 52.51  ? 90  ARG A HG2  1 
ATOM   1373 H HG3  . ARG A 1 90  ? 14.482 0.871   -3.312  1.00 52.51  ? 90  ARG A HG3  1 
ATOM   1374 H HD2  . ARG A 1 90  ? 13.267 2.568   -2.247  1.00 57.54  ? 90  ARG A HD2  1 
ATOM   1375 H HD3  . ARG A 1 90  ? 12.584 2.168   -3.625  1.00 57.54  ? 90  ARG A HD3  1 
ATOM   1376 H HE   . ARG A 1 90  ? 10.849 1.464   -2.500  1.00 70.58  ? 90  ARG A HE   1 
ATOM   1377 H HH11 . ARG A 1 90  ? 13.269 1.784   -0.250  1.00 83.61  ? 90  ARG A HH11 1 
ATOM   1378 H HH12 . ARG A 1 90  ? 12.403 1.531   0.935   1.00 83.61  ? 90  ARG A HH12 1 
ATOM   1379 H HH21 . ARG A 1 90  ? 9.577  1.083   -0.691  1.00 83.23  ? 90  ARG A HH21 1 
ATOM   1380 H HH22 . ARG A 1 90  ? 10.179 1.108   0.671   1.00 83.23  ? 90  ARG A HH22 1 
ATOM   1381 N N    . LEU A 1 91  ? 12.796 -3.099  -1.772  1.00 37.18  ? 91  LEU A N    1 
ATOM   1382 C CA   . LEU A 1 91  ? 12.833 -3.784  -0.484  1.00 37.51  ? 91  LEU A CA   1 
ATOM   1383 C C    . LEU A 1 91  ? 13.855 -4.914  -0.488  1.00 34.35  ? 91  LEU A C    1 
ATOM   1384 O O    . LEU A 1 91  ? 14.577 -5.122  0.500   1.00 34.99  ? 91  LEU A O    1 
ATOM   1385 C CB   . LEU A 1 91  ? 11.450 -4.325  -0.156  1.00 43.51  ? 91  LEU A CB   1 
ATOM   1386 C CG   . LEU A 1 91  ? 10.353 -3.308  0.139   1.00 51.27  ? 91  LEU A CG   1 
ATOM   1387 C CD1  . LEU A 1 91  ? 9.015  -4.012  0.188   1.00 56.97  ? 91  LEU A CD1  1 
ATOM   1388 C CD2  . LEU A 1 91  ? 10.675 -2.604  1.442   1.00 43.35  ? 91  LEU A CD2  1 
ATOM   1389 H H    . LEU A 1 91  ? 12.056 -3.173  -2.204  1.00 44.75  ? 91  LEU A H    1 
ATOM   1390 H HA   . LEU A 1 91  ? 13.088 -3.149  0.204   1.00 45.15  ? 91  LEU A HA   1 
ATOM   1391 H HB2  . LEU A 1 91  ? 11.150 -4.852  -0.913  1.00 52.35  ? 91  LEU A HB2  1 
ATOM   1392 H HB3  . LEU A 1 91  ? 11.531 -4.889  0.630   1.00 52.35  ? 91  LEU A HB3  1 
ATOM   1393 H HG   . LEU A 1 91  ? 10.297 -2.634  -0.556  1.00 61.66  ? 91  LEU A HG   1 
ATOM   1394 H HD11 . LEU A 1 91  ? 8.324  -3.364  0.396   1.00 68.50  ? 91  LEU A HD11 1 
ATOM   1395 H HD12 . LEU A 1 91  ? 8.839  -4.417  -0.676  1.00 68.50  ? 91  LEU A HD12 1 
ATOM   1396 H HD13 . LEU A 1 91  ? 9.043  -4.697  0.874   1.00 68.50  ? 91  LEU A HD13 1 
ATOM   1397 H HD21 . LEU A 1 91  ? 9.862  -2.217  1.802   1.00 52.15  ? 91  LEU A HD21 1 
ATOM   1398 H HD22 . LEU A 1 91  ? 11.039 -3.249  2.068   1.00 52.15  ? 91  LEU A HD22 1 
ATOM   1399 H HD23 . LEU A 1 91  ? 11.327 -1.906  1.271   1.00 52.15  ? 91  LEU A HD23 1 
ATOM   1400 N N    . VAL A 1 92  ? 13.916 -5.679  -1.578  1.00 34.46  ? 92  VAL A N    1 
ATOM   1401 C CA   . VAL A 1 92  ? 14.907 -6.746  -1.681  1.00 31.39  ? 92  VAL A CA   1 
ATOM   1402 C C    . VAL A 1 92  ? 16.311 -6.172  -1.581  1.00 32.09  ? 92  VAL A C    1 
ATOM   1403 O O    . VAL A 1 92  ? 17.158 -6.674  -0.827  1.00 30.36  ? 92  VAL A O    1 
ATOM   1404 C CB   . VAL A 1 92  ? 14.707 -7.523  -2.991  1.00 30.04  ? 92  VAL A CB   1 
ATOM   1405 C CG1  . VAL A 1 92  ? 15.874 -8.422  -3.286  1.00 31.13  ? 92  VAL A CG1  1 
ATOM   1406 C CG2  . VAL A 1 92  ? 13.417 -8.352  -2.915  1.00 32.75  ? 92  VAL A CG2  1 
ATOM   1407 H H    . VAL A 1 92  ? 13.401 -5.601  -2.263  1.00 41.49  ? 92  VAL A H    1 
ATOM   1408 H HA   . VAL A 1 92  ? 14.785 -7.361  -0.941  1.00 37.81  ? 92  VAL A HA   1 
ATOM   1409 H HB   . VAL A 1 92  ? 14.638 -6.883  -3.717  1.00 36.19  ? 92  VAL A HB   1 
ATOM   1410 H HG11 . VAL A 1 92  ? 15.627 -9.039  -3.993  1.00 37.49  ? 92  VAL A HG11 1 
ATOM   1411 H HG12 . VAL A 1 92  ? 16.627 -7.879  -3.568  1.00 37.49  ? 92  VAL A HG12 1 
ATOM   1412 H HG13 . VAL A 1 92  ? 16.104 -8.915  -2.483  1.00 37.49  ? 92  VAL A HG13 1 
ATOM   1413 H HG21 . VAL A 1 92  ? 13.088 -8.507  -3.814  1.00 39.44  ? 92  VAL A HG21 1 
ATOM   1414 H HG22 . VAL A 1 92  ? 13.610 -9.198  -2.483  1.00 39.44  ? 92  VAL A HG22 1 
ATOM   1415 H HG23 . VAL A 1 92  ? 12.756 -7.861  -2.402  1.00 39.44  ? 92  VAL A HG23 1 
ATOM   1416 N N    . SER A 1 93  ? 16.588 -5.131  -2.359  1.00 32.22  ? 93  SER A N    1 
ATOM   1417 C CA   . SER A 1 93  ? 17.906 -4.509  -2.325  1.00 33.21  ? 93  SER A CA   1 
ATOM   1418 C C    . SER A 1 93  ? 18.262 -4.052  -0.920  1.00 35.39  ? 93  SER A C    1 
ATOM   1419 O O    . SER A 1 93  ? 19.387 -4.274  -0.455  1.00 34.08  ? 93  SER A O    1 
ATOM   1420 C CB   . SER A 1 93  ? 17.947 -3.332  -3.293  1.00 34.98  ? 93  SER A CB   1 
ATOM   1421 O OG   . SER A 1 93  ? 17.934 -3.744  -4.647  1.00 38.07  ? 93  SER A OG   1 
ATOM   1422 H H    . SER A 1 93  ? 16.037 -4.769  -2.910  1.00 38.80  ? 93  SER A H    1 
ATOM   1423 H HA   . SER A 1 93  ? 18.568 -5.160  -2.608  1.00 39.99  ? 93  SER A HA   1 
ATOM   1424 H HB2  . SER A 1 93  ? 17.171 -2.773  -3.132  1.00 42.11  ? 93  SER A HB2  1 
ATOM   1425 H HB3  . SER A 1 93  ? 18.759 -2.827  -3.131  1.00 42.11  ? 93  SER A HB3  1 
ATOM   1426 H HG   . SER A 1 93  ? 17.209 -4.131  -4.822  1.00 45.82  ? 93  SER A HG   1 
ATOM   1427 N N    . GLU A 1 94  ? 17.319 -3.415  -0.224  1.00 32.37  ? 94  GLU A N    1 
ATOM   1428 C CA   . GLU A 1 94  ? 17.609 -2.947  1.129   1.00 35.05  ? 94  GLU A CA   1 
ATOM   1429 C C    . GLU A 1 94  ? 17.942 -4.112  2.052   1.00 36.40  ? 94  GLU A C    1 
ATOM   1430 O O    . GLU A 1 94  ? 18.844 -4.009  2.894   1.00 35.86  ? 94  GLU A O    1 
ATOM   1431 C CB   . GLU A 1 94  ? 16.428 -2.159  1.695   1.00 46.80  ? 94  GLU A CB   1 
ATOM   1432 C CG   . GLU A 1 94  ? 16.241 -0.795  1.086   1.00 57.57  ? 94  GLU A CG   1 
ATOM   1433 C CD   . GLU A 1 94  ? 15.240 0.048   1.860   1.00 68.44  ? 94  GLU A CD   1 
ATOM   1434 O OE1  . GLU A 1 94  ? 14.804 -0.387  2.953   1.00 63.48  ? 94  GLU A OE1  1 
ATOM   1435 O OE2  . GLU A 1 94  ? 14.892 1.146   1.372   1.00 67.59  ? 94  GLU A OE2  1 
ATOM   1436 H H    . GLU A 1 94  ? 16.524 -3.247  -0.504  1.00 38.98  ? 94  GLU A H    1 
ATOM   1437 H HA   . GLU A 1 94  ? 18.374 -2.352  1.086   1.00 42.20  ? 94  GLU A HA   1 
ATOM   1438 H HB2  . GLU A 1 94  ? 15.616 -2.664  1.538   1.00 56.29  ? 94  GLU A HB2  1 
ATOM   1439 H HB3  . GLU A 1 94  ? 16.565 -2.038  2.648   1.00 56.29  ? 94  GLU A HB3  1 
ATOM   1440 H HG2  . GLU A 1 94  ? 17.092 -0.329  1.083   1.00 69.22  ? 94  GLU A HG2  1 
ATOM   1441 H HG3  . GLU A 1 94  ? 15.915 -0.894  0.178   1.00 69.22  ? 94  GLU A HG3  1 
ATOM   1442 N N    . SER A 1 95  ? 17.196 -5.208  1.952   1.00 36.06  ? 95  SER A N    1 
ATOM   1443 C CA   . SER A 1 95  ? 17.456 -6.324  2.851   1.00 36.19  ? 95  SER A CA   1 
ATOM   1444 C C    . SER A 1 95  ? 18.831 -6.922  2.594   1.00 30.88  ? 95  SER A C    1 
ATOM   1445 O O    . SER A 1 95  ? 19.514 -7.344  3.530   1.00 33.74  ? 95  SER A O    1 
ATOM   1446 C CB   . SER A 1 95  ? 16.382 -7.404  2.713   1.00 31.72  ? 95  SER A CB   1 
ATOM   1447 O OG   . SER A 1 95  ? 16.511 -8.154  1.515   1.00 31.92  ? 95  SER A OG   1 
ATOM   1448 H H    . SER A 1 95  ? 16.556 -5.327  1.390   1.00 43.41  ? 95  SER A H    1 
ATOM   1449 H HA   . SER A 1 95  ? 17.421 -5.990  3.761   1.00 43.56  ? 95  SER A HA   1 
ATOM   1450 H HB2  . SER A 1 95  ? 16.457 -8.011  3.466   1.00 38.20  ? 95  SER A HB2  1 
ATOM   1451 H HB3  . SER A 1 95  ? 15.512 -6.976  2.717   1.00 38.20  ? 95  SER A HB3  1 
ATOM   1452 H HG   . SER A 1 95  ? 16.668 -7.640  0.870   1.00 38.43  ? 95  SER A HG   1 
ATOM   1453 N N    . TRP A 1 96  ? 19.246 -6.992  1.333   1.00 29.16  ? 96  TRP A N    1 
ATOM   1454 C CA   A TRP A 1 96  ? 20.541 -7.595  1.025   0.46 29.96  ? 96  TRP A CA   1 
ATOM   1455 C CA   B TRP A 1 96  ? 20.538 -7.590  1.023   0.54 29.94  ? 96  TRP A CA   1 
ATOM   1456 C C    . TRP A 1 96  ? 21.685 -6.665  1.431   1.00 30.16  ? 96  TRP A C    1 
ATOM   1457 O O    . TRP A 1 96  ? 22.722 -7.116  1.940   1.00 30.31  ? 96  TRP A O    1 
ATOM   1458 C CB   A TRP A 1 96  ? 20.630 -7.946  -0.466  0.46 31.08  ? 96  TRP A CB   1 
ATOM   1459 C CB   B TRP A 1 96  ? 20.608 -7.914  -0.469  0.54 31.11  ? 96  TRP A CB   1 
ATOM   1460 C CG   A TRP A 1 96  ? 19.918 -9.208  -0.867  0.46 29.79  ? 96  TRP A CG   1 
ATOM   1461 C CG   B TRP A 1 96  ? 21.330 -9.162  -0.736  0.54 30.35  ? 96  TRP A CG   1 
ATOM   1462 C CD1  A TRP A 1 96  ? 18.575 -9.368  -1.050  0.46 30.57  ? 96  TRP A CD1  1 
ATOM   1463 C CD1  B TRP A 1 96  ? 22.666 -9.347  -0.693  0.54 29.11  ? 96  TRP A CD1  1 
ATOM   1464 C CD2  A TRP A 1 96  ? 20.519 -10.475 -1.159  0.46 29.73  ? 96  TRP A CD2  1 
ATOM   1465 C CD2  B TRP A 1 96  ? 20.758 -10.437 -1.054  0.54 29.94  ? 96  TRP A CD2  1 
ATOM   1466 N NE1  A TRP A 1 96  ? 18.301 -10.667 -1.442  0.46 27.27  ? 96  TRP A NE1  1 
ATOM   1467 N NE1  B TRP A 1 96  ? 22.978 -10.643 -0.985  0.54 29.72  ? 96  TRP A NE1  1 
ATOM   1468 C CE2  A TRP A 1 96  ? 19.481 -11.365 -1.506  0.46 29.31  ? 96  TRP A CE2  1 
ATOM   1469 C CE2  B TRP A 1 96  ? 21.821 -11.344 -1.198  0.54 29.47  ? 96  TRP A CE2  1 
ATOM   1470 C CE3  A TRP A 1 96  ? 21.837 -10.943 -1.164  0.46 29.50  ? 96  TRP A CE3  1 
ATOM   1471 C CE3  B TRP A 1 96  ? 19.457 -10.895 -1.231  0.54 29.24  ? 96  TRP A CE3  1 
ATOM   1472 C CZ2  A TRP A 1 96  ? 19.724 -12.699 -1.848  0.46 30.38  ? 96  TRP A CZ2  1 
ATOM   1473 C CZ2  B TRP A 1 96  ? 21.627 -12.687 -1.524  0.54 30.30  ? 96  TRP A CZ2  1 
ATOM   1474 C CZ3  A TRP A 1 96  ? 22.074 -12.263 -1.511  0.46 30.52  ? 96  TRP A CZ3  1 
ATOM   1475 C CZ3  B TRP A 1 96  ? 19.257 -12.224 -1.551  0.54 30.15  ? 96  TRP A CZ3  1 
ATOM   1476 C CH2  A TRP A 1 96  ? 21.024 -13.129 -1.831  0.46 30.54  ? 96  TRP A CH2  1 
ATOM   1477 C CH2  B TRP A 1 96  ? 20.339 -13.112 -1.695  0.54 30.30  ? 96  TRP A CH2  1 
ATOM   1478 H H    . TRP A 1 96  ? 18.809 -6.707  0.649   1.00 35.12  ? 96  TRP A H    1 
ATOM   1479 H HA   . TRP A 1 96  ? 20.627 -8.422  1.525   1.00 36.07  ? 96  TRP A HA   1 
ATOM   1480 H HB2  A TRP A 1 96  ? 20.242 -7.218  -0.977  0.46 37.43  ? 96  TRP A HB2  1 
ATOM   1481 H HB2  B TRP A 1 96  ? 19.707 -8.007  -0.817  0.54 37.46  ? 96  TRP A HB2  1 
ATOM   1482 H HB3  A TRP A 1 96  ? 21.566 -8.053  -0.701  0.46 37.43  ? 96  TRP A HB3  1 
ATOM   1483 H HB3  B TRP A 1 96  ? 21.069 -7.195  -0.929  0.54 37.46  ? 96  TRP A HB3  1 
ATOM   1484 H HD1  A TRP A 1 96  ? 17.937 -8.702  -0.929  0.46 36.82  ? 96  TRP A HD1  1 
ATOM   1485 H HD1  B TRP A 1 96  ? 23.287 -8.685  -0.492  0.54 35.07  ? 96  TRP A HD1  1 
ATOM   1486 H HE1  A TRP A 1 96  ? 17.521 -10.984 -1.616  0.46 32.86  ? 96  TRP A HE1  1 
ATOM   1487 H HE1  B TRP A 1 96  ? 23.774 -10.968 -1.028  0.54 35.80  ? 96  TRP A HE1  1 
ATOM   1488 H HE3  A TRP A 1 96  ? 22.541 -10.378 -0.938  0.46 35.54  ? 96  TRP A HE3  1 
ATOM   1489 H HE3  B TRP A 1 96  ? 18.735 -10.316 -1.136  0.54 35.23  ? 96  TRP A HE3  1 
ATOM   1490 H HZ2  A TRP A 1 96  ? 19.029 -13.273 -2.079  0.46 36.59  ? 96  TRP A HZ2  1 
ATOM   1491 H HZ2  B TRP A 1 96  ? 22.345 -13.269 -1.622  0.54 36.50  ? 96  TRP A HZ2  1 
ATOM   1492 H HZ3  A TRP A 1 96  ? 22.948 -12.579 -1.532  0.46 36.76  ? 96  TRP A HZ3  1 
ATOM   1493 H HZ3  B TRP A 1 96  ? 18.390 -12.538 -1.674  0.54 36.32  ? 96  TRP A HZ3  1 
ATOM   1494 H HH2  A TRP A 1 96  ? 21.212 -14.016 -2.038  0.46 36.78  ? 96  TRP A HH2  1 
ATOM   1495 H HH2  B TRP A 1 96  ? 20.176 -14.002 -1.909  0.54 36.50  ? 96  TRP A HH2  1 
ATOM   1496 N N    . SER A 1 97  ? 21.523 -5.368  1.227   1.00 29.99  ? 97  SER A N    1 
ATOM   1497 C CA   . SER A 1 97  ? 22.513 -4.437  1.748   1.00 30.72  ? 97  SER A CA   1 
ATOM   1498 C C    . SER A 1 97  ? 22.607 -4.549  3.262   1.00 31.93  ? 97  SER A C    1 
ATOM   1499 O O    . SER A 1 97  ? 23.697 -4.446  3.835   1.00 31.96  ? 97  SER A O    1 
ATOM   1500 C CB   . SER A 1 97  ? 22.143 -3.006  1.374   1.00 36.03  ? 97  SER A CB   1 
ATOM   1501 O OG   . SER A 1 97  ? 22.219 -2.817  -0.019  1.00 39.37  ? 97  SER A OG   1 
ATOM   1502 H H    . SER A 1 97  ? 20.867 -5.009  0.802   1.00 35.31  ? 97  SER A H    1 
ATOM   1503 H HA   . SER A 1 97  ? 23.374 -4.647  1.353   1.00 36.58  ? 97  SER A HA   1 
ATOM   1504 H HB2  . SER A 1 97  ? 21.236 -2.827  1.668   1.00 43.37  ? 97  SER A HB2  1 
ATOM   1505 H HB3  . SER A 1 97  ? 22.759 -2.396  1.810   1.00 43.37  ? 97  SER A HB3  1 
ATOM   1506 H HG   . SER A 1 97  ? 21.639 -3.286  -0.405  1.00 47.38  ? 97  SER A HG   1 
ATOM   1507 N N    . ARG A 1 98  ? 21.464 -4.722  3.920   1.00 32.59  ? 98  ARG A N    1 
ATOM   1508 C CA   A ARG A 1 98  ? 21.454 -4.866  5.374   0.50 37.62  ? 98  ARG A CA   1 
ATOM   1509 C CA   B ARG A 1 98  ? 21.454 -4.866  5.374   0.50 37.62  ? 98  ARG A CA   1 
ATOM   1510 C C    . ARG A 1 98  ? 22.240 -6.090  5.789   1.00 33.43  ? 98  ARG A C    1 
ATOM   1511 O O    . ARG A 1 98  ? 23.041 -6.045  6.725   1.00 32.74  ? 98  ARG A O    1 
ATOM   1512 C CB   A ARG A 1 98  ? 20.011 -4.947  5.883   0.50 42.34  ? 98  ARG A CB   1 
ATOM   1513 C CB   B ARG A 1 98  ? 20.009 -4.941  5.879   0.50 42.34  ? 98  ARG A CB   1 
ATOM   1514 C CG   A ARG A 1 98  ? 19.857 -4.720  7.378   0.50 48.02  ? 98  ARG A CG   1 
ATOM   1515 C CG   B ARG A 1 98  ? 19.844 -4.776  7.381   0.50 48.01  ? 98  ARG A CG   1 
ATOM   1516 C CD   A ARG A 1 98  ? 18.455 -5.087  7.870   0.50 52.93  ? 98  ARG A CD   1 
ATOM   1517 C CD   B ARG A 1 98  ? 18.355 -4.801  7.782   0.50 53.02  ? 98  ARG A CD   1 
ATOM   1518 N NE   A ARG A 1 98  ? 17.434 -4.926  6.838   0.50 53.20  ? 98  ARG A NE   1 
ATOM   1519 N NE   B ARG A 1 98  ? 17.555 -3.899  6.959   0.50 54.57  ? 98  ARG A NE   1 
ATOM   1520 C CZ   A ARG A 1 98  ? 16.988 -3.757  6.397   0.50 53.84  ? 98  ARG A CZ   1 
ATOM   1521 C CZ   B ARG A 1 98  ? 16.555 -4.275  6.170   0.50 53.22  ? 98  ARG A CZ   1 
ATOM   1522 N NH1  A ARG A 1 98  ? 17.485 -2.614  6.841   0.50 55.39  ? 98  ARG A NH1  1 
ATOM   1523 N NH1  B ARG A 1 98  ? 16.113 -5.523  6.155   0.50 50.11  ? 98  ARG A NH1  1 
ATOM   1524 N NH2  A ARG A 1 98  ? 16.021 -3.734  5.481   0.50 53.70  ? 98  ARG A NH2  1 
ATOM   1525 N NH2  B ARG A 1 98  ? 15.977 -3.372  5.383   0.50 53.81  ? 98  ARG A NH2  1 
ATOM   1526 H H    . ARG A 1 98  ? 20.686 -4.760  3.555   1.00 39.24  ? 98  ARG A H    1 
ATOM   1527 H HA   . ARG A 1 98  ? 21.867 -4.086  5.776   1.00 45.28  ? 98  ARG A HA   1 
ATOM   1528 H HB2  A ARG A 1 98  ? 19.485 -4.271  5.429   0.50 50.95  ? 98  ARG A HB2  1 
ATOM   1529 H HB2  B ARG A 1 98  ? 19.497 -4.237  5.451   0.50 50.94  ? 98  ARG A HB2  1 
ATOM   1530 H HB3  A ARG A 1 98  ? 19.662 -5.829  5.683   0.50 50.95  ? 98  ARG A HB3  1 
ATOM   1531 H HB3  B ARG A 1 98  ? 19.645 -5.808  5.640   0.50 50.94  ? 98  ARG A HB3  1 
ATOM   1532 H HG2  A ARG A 1 98  ? 20.499 -5.272  7.853   0.50 57.75  ? 98  ARG A HG2  1 
ATOM   1533 H HG2  B ARG A 1 98  ? 20.297 -5.502  7.837   0.50 57.75  ? 98  ARG A HG2  1 
ATOM   1534 H HG3  A ARG A 1 98  ? 20.013 -3.784  7.577   0.50 57.75  ? 98  ARG A HG3  1 
ATOM   1535 H HG3  B ARG A 1 98  ? 20.222 -3.926  7.656   0.50 57.75  ? 98  ARG A HG3  1 
ATOM   1536 H HD2  A ARG A 1 98  ? 18.451 -6.015  8.153   0.50 63.65  ? 98  ARG A HD2  1 
ATOM   1537 H HD2  B ARG A 1 98  ? 18.010 -5.700  7.671   0.50 63.76  ? 98  ARG A HD2  1 
ATOM   1538 H HD3  A ARG A 1 98  ? 18.221 -4.512  8.615   0.50 63.65  ? 98  ARG A HD3  1 
ATOM   1539 H HD3  B ARG A 1 98  ? 18.269 -4.524  8.707   0.50 63.76  ? 98  ARG A HD3  1 
ATOM   1540 H HE   A ARG A 1 98  ? 17.099 -5.639  6.492   0.50 63.98  ? 98  ARG A HE   1 
ATOM   1541 H HE   B ARG A 1 98  ? 17.746 -3.061  6.986   0.50 65.62  ? 98  ARG A HE   1 
ATOM   1542 H HH11 A ARG A 1 98  ? 18.112 -2.617  7.430   0.50 66.60  ? 98  ARG A HH11 1 
ATOM   1543 H HH11 B ARG A 1 98  ? 16.475 -6.114  6.664   0.50 60.27  ? 98  ARG A HH11 1 
ATOM   1544 H HH12 A ARG A 1 98  ? 17.181 -1.867  6.542   0.50 66.60  ? 98  ARG A HH12 1 
ATOM   1545 H HH12 B ARG A 1 98  ? 15.463 -5.742  5.635   0.50 60.27  ? 98  ARG A HH12 1 
ATOM   1546 H HH21 A ARG A 1 98  ? 15.694 -4.471  5.183   0.50 64.57  ? 98  ARG A HH21 1 
ATOM   1547 H HH21 B ARG A 1 98  ? 16.253 -2.557  5.389   0.50 64.70  ? 98  ARG A HH21 1 
ATOM   1548 H HH22 A ARG A 1 98  ? 15.724 -2.982  5.188   0.50 64.57  ? 98  ARG A HH22 1 
ATOM   1549 H HH22 B ARG A 1 98  ? 15.329 -3.602  4.868   0.50 64.70  ? 98  ARG A HH22 1 
ATOM   1550 N N    . VAL A 1 99  ? 22.032 -7.230  5.104   1.00 31.25  ? 99  VAL A N    1 
ATOM   1551 C CA   . VAL A 1 99  ? 22.817 -8.429  5.401   1.00 31.71  ? 99  VAL A CA   1 
ATOM   1552 C C    . VAL A 1 99  ? 24.304 -8.107  5.320   1.00 29.22  ? 99  VAL A C    1 
ATOM   1553 O O    . VAL A 1 99  ? 25.089 -8.438  6.214   1.00 28.27  ? 99  VAL A O    1 
ATOM   1554 C CB   . VAL A 1 99  ? 22.454 -9.577  4.441   1.00 32.82  ? 99  VAL A CB   1 
ATOM   1555 C CG1  . VAL A 1 99  ? 23.552 -10.652 4.447   1.00 33.68  ? 99  VAL A CG1  1 
ATOM   1556 C CG2  . VAL A 1 99  ? 21.117 -10.185 4.805   1.00 33.53  ? 99  VAL A CG2  1 
ATOM   1557 H H    . VAL A 1 99  ? 21.452 -7.328  4.476   1.00 37.64  ? 99  VAL A H    1 
ATOM   1558 H HA   . VAL A 1 99  ? 22.606 -8.715  6.303   1.00 38.19  ? 99  VAL A HA   1 
ATOM   1559 H HB   . VAL A 1 99  ? 22.384 -9.215  3.544   1.00 39.52  ? 99  VAL A HB   1 
ATOM   1560 H HG11 . VAL A 1 99  ? 23.195 -11.470 4.066   1.00 40.55  ? 99  VAL A HG11 1 
ATOM   1561 H HG12 . VAL A 1 99  ? 24.303 -10.341 3.918   1.00 40.55  ? 99  VAL A HG12 1 
ATOM   1562 H HG13 . VAL A 1 99  ? 23.834 -10.810 5.362   1.00 40.55  ? 99  VAL A HG13 1 
ATOM   1563 H HG21 . VAL A 1 99  ? 20.840 -10.786 4.096   1.00 40.37  ? 99  VAL A HG21 1 
ATOM   1564 H HG22 . VAL A 1 99  ? 21.209 -10.676 5.637   1.00 40.37  ? 99  VAL A HG22 1 
ATOM   1565 H HG23 . VAL A 1 99  ? 20.465 -9.475  4.911   1.00 40.37  ? 99  VAL A HG23 1 
ATOM   1566 N N    . ASP A 1 100 ? 24.721 -7.498  4.218   1.00 31.07  ? 100 ASP A N    1 
ATOM   1567 C CA   . ASP A 1 100 ? 26.141 -7.209  4.044   1.00 30.23  ? 100 ASP A CA   1 
ATOM   1568 C C    . ASP A 1 100 ? 26.697 -6.386  5.204   1.00 32.92  ? 100 ASP A C    1 
ATOM   1569 O O    . ASP A 1 100 ? 27.787 -6.684  5.715   1.00 35.70  ? 100 ASP A O    1 
ATOM   1570 C CB   . ASP A 1 100 ? 26.362 -6.512  2.711   1.00 36.38  ? 100 ASP A CB   1 
ATOM   1571 C CG   . ASP A 1 100 ? 26.228 -7.456  1.533   1.00 45.19  ? 100 ASP A CG   1 
ATOM   1572 O OD1  . ASP A 1 100 ? 26.548 -8.654  1.679   1.00 49.13  ? 100 ASP A OD1  1 
ATOM   1573 O OD2  . ASP A 1 100 ? 25.800 -7.000  0.456   1.00 49.49  ? 100 ASP A OD2  1 
ATOM   1574 H H    . ASP A 1 100 ? 24.217 -7.246  3.569   1.00 37.42  ? 100 ASP A H    1 
ATOM   1575 H HA   . ASP A 1 100 ? 26.634 -8.044  4.029   1.00 36.41  ? 100 ASP A HA   1 
ATOM   1576 H HB2  . ASP A 1 100 ? 25.703 -5.808  2.608   1.00 43.79  ? 100 ASP A HB2  1 
ATOM   1577 H HB3  . ASP A 1 100 ? 27.255 -6.135  2.694   1.00 43.79  ? 100 ASP A HB3  1 
ATOM   1578 N N    . LYS A 1 101 ? 25.949 -5.391  5.669   1.00 30.98  ? 101 LYS A N    1 
ATOM   1579 C CA   . LYS A 1 101 ? 26.437 -4.557  6.765   1.00 36.40  ? 101 LYS A CA   1 
ATOM   1580 C C    . LYS A 1 101 ? 26.553 -5.370  8.047   1.00 34.55  ? 101 LYS A C    1 
ATOM   1581 O O    . LYS A 1 101 ? 27.509 -5.195  8.813   1.00 32.27  ? 101 LYS A O    1 
ATOM   1582 C CB   . LYS A 1 101 ? 25.532 -3.335  6.962   1.00 41.42  ? 101 LYS A CB   1 
ATOM   1583 C CG   . LYS A 1 101 ? 24.402 -3.479  7.975   1.00 54.70  ? 101 LYS A CG   1 
ATOM   1584 C CD   . LYS A 1 101 ? 23.620 -2.159  8.212   1.00 54.85  ? 101 LYS A CD   1 
ATOM   1585 C CE   . LYS A 1 101 ? 22.367 -2.428  9.063   1.00 55.98  ? 101 LYS A CE   1 
ATOM   1586 N NZ   . LYS A 1 101 ? 21.292 -1.404  8.942   1.00 60.66  ? 101 LYS A NZ   1 
ATOM   1587 H H    . LYS A 1 101 ? 25.169 -5.179  5.375   1.00 37.31  ? 101 LYS A H    1 
ATOM   1588 H HA   . LYS A 1 101 ? 27.318 -4.221  6.538   1.00 43.82  ? 101 LYS A HA   1 
ATOM   1589 H HB2  . LYS A 1 101 ? 26.085 -2.595  7.258   1.00 49.84  ? 101 LYS A HB2  1 
ATOM   1590 H HB3  . LYS A 1 101 ? 25.123 -3.123  6.109   1.00 49.84  ? 101 LYS A HB3  1 
ATOM   1591 H HG2  . LYS A 1 101 ? 23.773 -4.143  7.652   1.00 65.78  ? 101 LYS A HG2  1 
ATOM   1592 H HG3  . LYS A 1 101 ? 24.775 -3.761  8.825   1.00 65.78  ? 101 LYS A HG3  1 
ATOM   1593 H HD2  . LYS A 1 101 ? 24.185 -1.526  8.683   1.00 65.96  ? 101 LYS A HD2  1 
ATOM   1594 H HD3  . LYS A 1 101 ? 23.343 -1.786  7.361   1.00 65.96  ? 101 LYS A HD3  1 
ATOM   1595 H HE2  . LYS A 1 101 ? 21.989 -3.279  8.792   1.00 67.31  ? 101 LYS A HE2  1 
ATOM   1596 H HE3  . LYS A 1 101 ? 22.630 -2.463  9.996   1.00 67.31  ? 101 LYS A HE3  1 
ATOM   1597 H HZ1  . LYS A 1 101 ? 20.560 -1.678  9.369   1.00 72.93  ? 101 LYS A HZ1  1 
ATOM   1598 H HZ2  . LYS A 1 101 ? 21.562 -0.635  9.298   1.00 72.93  ? 101 LYS A HZ2  1 
ATOM   1599 H HZ3  . LYS A 1 101 ? 21.093 -1.271  8.085   1.00 72.93  ? 101 LYS A HZ3  1 
ATOM   1600 N N    . ILE A 1 102 ? 25.577 -6.244  8.303   1.00 30.28  ? 102 ILE A N    1 
ATOM   1601 C CA   . ILE A 1 102 ? 25.611 -7.122  9.478   1.00 29.69  ? 102 ILE A CA   1 
ATOM   1602 C C    . ILE A 1 102 ? 26.860 -7.999  9.455   1.00 33.09  ? 102 ILE A C    1 
ATOM   1603 O O    . ILE A 1 102 ? 27.567 -8.132  10.459  1.00 32.47  ? 102 ILE A O    1 
ATOM   1604 C CB   . ILE A 1 102 ? 24.331 -7.966  9.549   1.00 29.36  ? 102 ILE A CB   1 
ATOM   1605 C CG1  . ILE A 1 102 ? 23.113 -7.078  9.875   1.00 31.43  ? 102 ILE A CG1  1 
ATOM   1606 C CG2  . ILE A 1 102 ? 24.501 -9.096  10.561  1.00 29.98  ? 102 ILE A CG2  1 
ATOM   1607 C CD1  . ILE A 1 102 ? 21.767 -7.750  9.644   1.00 33.31  ? 102 ILE A CD1  1 
ATOM   1608 H H    . ILE A 1 102 ? 24.879 -6.351  7.810   1.00 36.47  ? 102 ILE A H    1 
ATOM   1609 H HA   . ILE A 1 102 ? 25.653 -6.568  10.273  1.00 35.76  ? 102 ILE A HA   1 
ATOM   1610 H HB   . ILE A 1 102 ? 24.171 -8.368  8.680   1.00 35.37  ? 102 ILE A HB   1 
ATOM   1611 H HG12 . ILE A 1 102 ? 23.158 -6.822  10.809  1.00 37.85  ? 102 ILE A HG12 1 
ATOM   1612 H HG13 . ILE A 1 102 ? 23.147 -6.288  9.313   1.00 37.85  ? 102 ILE A HG13 1 
ATOM   1613 H HG21 . ILE A 1 102 ? 23.627 -9.449  10.790  1.00 36.11  ? 102 ILE A HG21 1 
ATOM   1614 H HG22 . ILE A 1 102 ? 25.046 -9.795  10.167  1.00 36.11  ? 102 ILE A HG22 1 
ATOM   1615 H HG23 . ILE A 1 102 ? 24.935 -8.747  11.355  1.00 36.11  ? 102 ILE A HG23 1 
ATOM   1616 H HD11 . ILE A 1 102 ? 21.063 -7.093  9.760   1.00 40.11  ? 102 ILE A HD11 1 
ATOM   1617 H HD12 . ILE A 1 102 ? 21.742 -8.106  8.743   1.00 40.11  ? 102 ILE A HD12 1 
ATOM   1618 H HD13 . ILE A 1 102 ? 21.659 -8.468  10.287  1.00 40.11  ? 102 ILE A HD13 1 
ATOM   1619 N N    . ILE A 1 103 ? 27.128 -8.621  8.308   1.00 29.49  ? 103 ILE A N    1 
ATOM   1620 C CA   . ILE A 1 103 ? 28.274 -9.516  8.185   1.00 31.38  ? 103 ILE A CA   1 
ATOM   1621 C C    . ILE A 1 103 ? 29.566 -8.756  8.434   1.00 36.32  ? 103 ILE A C    1 
ATOM   1622 O O    . ILE A 1 103 ? 30.451 -9.227  9.157   1.00 39.67  ? 103 ILE A O    1 
ATOM   1623 C CB   . ILE A 1 103 ? 28.240 -10.196 6.804   1.00 33.69  ? 103 ILE A CB   1 
ATOM   1624 C CG1  . ILE A 1 103 ? 26.991 -11.093 6.699   1.00 34.16  ? 103 ILE A CG1  1 
ATOM   1625 C CG2  . ILE A 1 103 ? 29.505 -11.005 6.573   1.00 36.40  ? 103 ILE A CG2  1 
ATOM   1626 C CD1  . ILE A 1 103 ? 27.026 -12.335 7.584   1.00 33.63  ? 103 ILE A CD1  1 
ATOM   1627 H H    . ILE A 1 103 ? 26.663 -8.542  7.589   1.00 35.52  ? 103 ILE A H    1 
ATOM   1628 H HA   . ILE A 1 103 ? 28.221 -10.210 8.860   1.00 37.79  ? 103 ILE A HA   1 
ATOM   1629 H HB   . ILE A 1 103 ? 28.194 -9.511  6.120   1.00 40.57  ? 103 ILE A HB   1 
ATOM   1630 H HG12 . ILE A 1 103 ? 26.214 -10.572 6.955   1.00 41.13  ? 103 ILE A HG12 1 
ATOM   1631 H HG13 . ILE A 1 103 ? 26.901 -11.392 5.780   1.00 41.13  ? 103 ILE A HG13 1 
ATOM   1632 H HG21 . ILE A 1 103 ? 29.372 -11.588 5.809   1.00 43.81  ? 103 ILE A HG21 1 
ATOM   1633 H HG22 . ILE A 1 103 ? 30.241 -10.397 6.401   1.00 43.81  ? 103 ILE A HG22 1 
ATOM   1634 H HG23 . ILE A 1 103 ? 29.691 -11.534 7.364   1.00 43.81  ? 103 ILE A HG23 1 
ATOM   1635 H HD11 . ILE A 1 103 ? 26.213 -12.846 7.444   1.00 40.49  ? 103 ILE A HD11 1 
ATOM   1636 H HD12 . ILE A 1 103 ? 27.799 -12.870 7.347   1.00 40.49  ? 103 ILE A HD12 1 
ATOM   1637 H HD13 . ILE A 1 103 ? 27.087 -12.059 8.512   1.00 40.49  ? 103 ILE A HD13 1 
ATOM   1638 N N    . GLU A 1 104 ? 29.675 -7.544  7.912   1.00 36.65  ? 104 GLU A N    1 
ATOM   1639 C CA   . GLU A 1 104 ? 30.905 -6.803  8.148   1.00 40.39  ? 104 GLU A CA   1 
ATOM   1640 C C    . GLU A 1 104 ? 31.082 -6.476  9.626   1.00 44.44  ? 104 GLU A C    1 
ATOM   1641 O O    . GLU A 1 104 ? 32.190 -6.581  10.159  1.00 46.13  ? 104 GLU A O    1 
ATOM   1642 C CB   . GLU A 1 104 ? 30.916 -5.547  7.303   1.00 44.13  ? 104 GLU A CB   1 
ATOM   1643 C CG   . GLU A 1 104 ? 32.163 -4.726  7.504   1.00 56.43  ? 104 GLU A CG   1 
ATOM   1644 C CD   . GLU A 1 104 ? 32.400 -3.785  6.352   1.00 78.66  ? 104 GLU A CD   1 
ATOM   1645 O OE1  . GLU A 1 104 ? 32.694 -4.277  5.240   1.00 88.37  ? 104 GLU A OE1  1 
ATOM   1646 O OE2  . GLU A 1 104 ? 32.266 -2.560  6.550   1.00 76.24  ? 104 GLU A OE2  1 
ATOM   1647 H H    . GLU A 1 104 ? 29.079 -7.145  7.438   1.00 44.12  ? 104 GLU A H    1 
ATOM   1648 H HA   . GLU A 1 104 ? 31.661 -7.347  7.879   1.00 48.60  ? 104 GLU A HA   1 
ATOM   1649 H HB2  . GLU A 1 104 ? 30.866 -5.795  6.367   1.00 53.09  ? 104 GLU A HB2  1 
ATOM   1650 H HB3  . GLU A 1 104 ? 30.153 -4.998  7.543   1.00 53.09  ? 104 GLU A HB3  1 
ATOM   1651 H HG2  . GLU A 1 104 ? 32.073 -4.199  8.313   1.00 67.85  ? 104 GLU A HG2  1 
ATOM   1652 H HG3  . GLU A 1 104 ? 32.928 -5.318  7.576   1.00 67.85  ? 104 GLU A HG3  1 
ATOM   1653 N N    . ASN A 1 105 ? 30.007 -6.099  10.318  1.00 36.08  ? 105 ASN A N    1 
ATOM   1654 C CA   . ASN A 1 105 ? 30.139 -5.819  11.747  1.00 40.13  ? 105 ASN A CA   1 
ATOM   1655 C C    . ASN A 1 105 ? 30.538 -7.068  12.530  1.00 41.30  ? 105 ASN A C    1 
ATOM   1656 O O    . ASN A 1 105 ? 31.333 -6.987  13.474  1.00 48.96  ? 105 ASN A O    1 
ATOM   1657 C CB   . ASN A 1 105 ? 28.839 -5.211  12.277  1.00 36.32  ? 105 ASN A CB   1 
ATOM   1658 C CG   . ASN A 1 105 ? 28.693 -3.756  11.886  1.00 37.39  ? 105 ASN A CG   1 
ATOM   1659 O OD1  . ASN A 1 105 ? 29.697 -3.068  11.653  1.00 43.42  ? 105 ASN A OD1  1 
ATOM   1660 N ND2  . ASN A 1 105 ? 27.475 -3.267  11.831  1.00 37.27  ? 105 ASN A ND2  1 
ATOM   1661 H H    . ASN A 1 105 ? 29.216 -6.000  9.995   1.00 43.43  ? 105 ASN A H    1 
ATOM   1662 H HA   . ASN A 1 105 ? 30.844 -5.166  11.879  1.00 48.29  ? 105 ASN A HA   1 
ATOM   1663 H HB2  . ASN A 1 105 ? 28.086 -5.701  11.912  1.00 43.72  ? 105 ASN A HB2  1 
ATOM   1664 H HB3  . ASN A 1 105 ? 28.833 -5.267  13.246  1.00 43.72  ? 105 ASN A HB3  1 
ATOM   1665 H HD21 . ASN A 1 105 ? 27.352 -2.445  11.612  1.00 44.86  ? 105 ASN A HD21 1 
ATOM   1666 H HD22 . ASN A 1 105 ? 26.801 -3.770  12.013  1.00 44.86  ? 105 ASN A HD22 1 
ATOM   1667 N N    . LEU A 1 106 ? 30.009 -8.237  12.149  1.00 36.40  ? 106 LEU A N    1 
ATOM   1668 C CA   . LEU A 1 106 ? 30.319 -9.475  12.859  1.00 37.62  ? 106 LEU A CA   1 
ATOM   1669 C C    . LEU A 1 106 ? 31.775 -9.898  12.729  1.00 39.23  ? 106 LEU A C    1 
ATOM   1670 O O    . LEU A 1 106 ? 32.249 -10.667 13.569  1.00 44.87  ? 106 LEU A O    1 
ATOM   1671 C CB   . LEU A 1 106 ? 29.423 -10.613 12.353  1.00 36.43  ? 106 LEU A CB   1 
ATOM   1672 C CG   . LEU A 1 106 ? 27.957 -10.485 12.753  1.00 32.41  ? 106 LEU A CG   1 
ATOM   1673 C CD1  . LEU A 1 106 ? 27.080 -11.457 11.966  1.00 34.82  ? 106 LEU A CD1  1 
ATOM   1674 C CD2  . LEU A 1 106 ? 27.793 -10.690 14.246  1.00 31.36  ? 106 LEU A CD2  1 
ATOM   1675 H H    . LEU A 1 106 ? 29.470 -8.336  11.486  1.00 43.82  ? 106 LEU A H    1 
ATOM   1676 H HA   . LEU A 1 106 ? 30.137 -9.324  13.800  1.00 45.28  ? 106 LEU A HA   1 
ATOM   1677 H HB2  . LEU A 1 106 ? 29.463 -10.629 11.384  1.00 43.85  ? 106 LEU A HB2  1 
ATOM   1678 H HB3  . LEU A 1 106 ? 29.755 -11.450 12.713  1.00 43.85  ? 106 LEU A HB3  1 
ATOM   1679 H HG   . LEU A 1 106 ? 27.654 -9.589  12.540  1.00 39.02  ? 106 LEU A HG   1 
ATOM   1680 H HD11 . LEU A 1 106 ? 26.169 -11.398 12.293  1.00 41.92  ? 106 LEU A HD11 1 
ATOM   1681 H HD12 . LEU A 1 106 ? 27.110 -11.219 11.026  1.00 41.92  ? 106 LEU A HD12 1 
ATOM   1682 H HD13 . LEU A 1 106 ? 27.418 -12.358 12.089  1.00 41.92  ? 106 LEU A HD13 1 
ATOM   1683 H HD21 . LEU A 1 106 ? 26.850 -10.788 14.450  1.00 37.77  ? 106 LEU A HD21 1 
ATOM   1684 H HD22 . LEU A 1 106 ? 28.273 -11.491 14.510  1.00 37.77  ? 106 LEU A HD22 1 
ATOM   1685 H HD23 . LEU A 1 106 ? 28.154 -9.920  14.712  1.00 37.77  ? 106 LEU A HD23 1 
ATOM   1686 N N    . GLU A 1 107 ? 32.491 -9.418  11.717  1.00 50.84  ? 107 GLU A N    1 
ATOM   1687 C CA   . GLU A 1 107 ? 33.871 -9.833  11.482  1.00 52.67  ? 107 GLU A CA   1 
ATOM   1688 C C    . GLU A 1 107 ? 34.874 -8.876  12.128  1.00 53.04  ? 107 GLU A C    1 
ATOM   1689 O O    . GLU A 1 107 ? 34.527 -7.759  12.517  1.00 55.20  ? 107 GLU A O    1 
ATOM   1690 C CB   . GLU A 1 107 ? 34.135 -9.929  9.974   1.00 51.23  ? 107 GLU A CB   1 
ATOM   1691 C CG   . GLU A 1 107 ? 33.310 -10.988 9.222   1.00 48.15  ? 107 GLU A CG   1 
ATOM   1692 C CD   . GLU A 1 107 ? 33.887 -12.399 9.348   1.00 64.19  ? 107 GLU A CD   1 
ATOM   1693 O OE1  . GLU A 1 107 ? 34.921 -12.564 10.032  1.00 69.54  ? 107 GLU A OE1  1 
ATOM   1694 O OE2  . GLU A 1 107 ? 33.309 -13.344 8.759   1.00 57.66  ? 107 GLU A OE2  1 
ATOM   1695 H H    . GLU A 1 107 ? 32.198 -8.844  11.147  1.00 61.14  ? 107 GLU A H    1 
ATOM   1696 H HA   . GLU A 1 107 ? 34.008 -10.705 11.883  1.00 63.33  ? 107 GLU A HA   1 
ATOM   1697 H HB2  . GLU A 1 107 ? 33.934 -9.069  9.574   1.00 61.62  ? 107 GLU A HB2  1 
ATOM   1698 H HB3  . GLU A 1 107 ? 35.071 -10.146 9.842   1.00 61.62  ? 107 GLU A HB3  1 
ATOM   1699 H HG2  . GLU A 1 107 ? 32.410 -11.000 9.583   1.00 57.91  ? 107 GLU A HG2  1 
ATOM   1700 H HG3  . GLU A 1 107 ? 33.287 -10.758 8.280   1.00 57.91  ? 107 GLU A HG3  1 
HETATM 1701 O O    . HOH B 2 .   ? 19.476 -1.884  3.681   1.00 46.80  ? 201 HOH A O    1 
HETATM 1702 O O    . HOH B 2 .   ? 20.170 -4.744  -5.596  1.00 37.92  ? 202 HOH A O    1 
HETATM 1703 O O    . HOH B 2 .   ? 15.084 -22.215 -26.094 1.00 37.04  ? 203 HOH A O    1 
HETATM 1704 O O    . HOH B 2 .   ? 24.654 -18.079 -6.301  1.00 38.32  ? 204 HOH A O    1 
HETATM 1705 O O    . HOH B 2 .   ? 10.745 -10.769 -4.890  1.00 45.72  ? 205 HOH A O    1 
HETATM 1706 O O    . HOH B 2 .   ? 2.920  -10.262 -14.293 1.00 35.17  ? 206 HOH A O    1 
HETATM 1707 O O    . HOH B 2 .   ? 9.427  -1.201  -15.425 1.00 38.20  ? 207 HOH A O    1 
HETATM 1708 O O    . HOH B 2 .   ? 4.554  2.160   -15.595 1.00 40.08  ? 208 HOH A O    1 
HETATM 1709 O O    . HOH B 2 .   ? 13.503 -14.367 -23.526 1.00 29.69  ? 209 HOH A O    1 
HETATM 1710 O O    . HOH B 2 .   ? 9.173  -1.170  -20.371 1.00 40.43  ? 210 HOH A O    1 
HETATM 1711 O O    . HOH B 2 .   ? 12.612 -3.805  -16.273 1.00 26.13  ? 211 HOH A O    1 
HETATM 1712 O O    . HOH B 2 .   ? 6.519  -18.441 -23.932 1.00 38.18  ? 212 HOH A O    1 
HETATM 1713 O O    . HOH B 2 .   ? 26.046 -4.287  0.337   1.00 46.44  ? 213 HOH A O    1 
HETATM 1714 O O    . HOH B 2 .   ? 18.974 -5.496  -18.208 1.00 30.42  ? 214 HOH A O    1 
HETATM 1715 O O    . HOH B 2 .   ? 8.268  -21.751 -11.339 1.00 39.79  ? 215 HOH A O    1 
HETATM 1716 O O    . HOH B 2 .   ? 3.663  -7.127  -20.315 1.00 28.75  ? 216 HOH A O    1 
HETATM 1717 O O    . HOH B 2 .   ? 14.033 0.615   -9.556  1.00 49.06  ? 217 HOH A O    1 
HETATM 1718 O O    . HOH B 2 .   ? 8.662  -19.071 -17.966 1.00 29.81  ? 218 HOH A O    1 
HETATM 1719 O O    . HOH B 2 .   ? 24.727 -16.365 -16.514 1.00 31.70  ? 219 HOH A O    1 
HETATM 1720 O O    . HOH B 2 .   ? 7.909  -0.658  -18.183 1.00 37.74  ? 220 HOH A O    1 
HETATM 1721 O O    . HOH B 2 .   ? 23.076 -17.516 -8.600  1.00 40.73  ? 221 HOH A O    1 
HETATM 1722 O O    . HOH B 2 .   ? 13.770 -25.744 -15.102 1.00 30.47  ? 222 HOH A O    1 
HETATM 1723 O O    . HOH B 2 .   ? 23.498 -20.979 -20.589 1.00 44.46  ? 223 HOH A O    1 
HETATM 1724 O O    . HOH B 2 .   ? 15.160 -17.706 -25.169 1.00 45.75  ? 224 HOH A O    1 
HETATM 1725 O O    . HOH B 2 .   ? 1.725  -6.263  -11.298 1.00 36.25  ? 225 HOH A O    1 
HETATM 1726 O O    . HOH B 2 .   ? 21.224 -22.287 -13.875 1.00 40.02  ? 226 HOH A O    1 
HETATM 1727 O O    . HOH B 2 .   ? 19.760 -7.111  -24.125 1.00 41.53  ? 227 HOH A O    1 
HETATM 1728 O O    . HOH B 2 .   ? 7.830  -16.564 -18.484 1.00 39.28  ? 228 HOH A O    1 
HETATM 1729 O O    . HOH B 2 .   ? 21.045 -22.205 -21.353 1.00 41.80  ? 229 HOH A O    1 
HETATM 1730 O O    . HOH B 2 .   ? 14.229 -0.902  -20.138 1.00 33.51  ? 230 HOH A O    1 
HETATM 1731 O O    . HOH B 2 .   ? 3.311  -2.158  -14.311 1.00 41.40  ? 231 HOH A O    1 
HETATM 1732 O O    . HOH B 2 .   ? 13.948 -16.737 -3.036  1.00 45.08  ? 232 HOH A O    1 
HETATM 1733 O O    . HOH B 2 .   ? 28.454 -2.299  8.852   1.00 44.25  ? 233 HOH A O    1 
HETATM 1734 O O    . HOH B 2 .   ? 18.362 -8.057  6.270   1.00 45.06  ? 234 HOH A O    1 
HETATM 1735 O O    . HOH B 2 .   ? 31.012 -10.717 16.379  1.00 49.35  ? 235 HOH A O    1 
HETATM 1736 O O    . HOH B 2 .   ? 6.977  0.483   -15.946 1.00 43.52  ? 236 HOH A O    1 
HETATM 1737 O O    . HOH B 2 .   ? 2.469  -3.519  -11.105 1.00 33.20  ? 237 HOH A O    1 
HETATM 1738 O O    . HOH B 2 .   ? 13.243 -1.216  -15.219 1.00 43.61  ? 238 HOH A O    1 
HETATM 1739 O O    . HOH B 2 .   ? 32.760 -13.452 5.557   1.00 51.43  ? 239 HOH A O    1 
HETATM 1740 O O    . HOH B 2 .   ? 16.443 -25.330 -22.284 1.00 39.70  ? 240 HOH A O    1 
HETATM 1741 O O    . HOH B 2 .   ? 14.753 -24.918 -12.071 1.00 49.16  ? 241 HOH A O    1 
HETATM 1742 O O    . HOH B 2 .   ? 21.714 -12.332 -29.853 1.00 50.37  ? 242 HOH A O    1 
HETATM 1743 O O    . HOH B 2 .   ? 22.276 -9.816  -30.145 1.00 54.72  ? 243 HOH A O    1 
HETATM 1744 O O    . HOH B 2 .   ? 24.852 -19.957 -22.758 1.00 50.63  ? 244 HOH A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLU A 3   ? 0.8458 0.7049 0.7469 0.0885  -0.1435 -0.0440 3   GLU A N   
2    C CA  . GLU A 3   ? 0.9389 0.8097 0.8474 0.0808  -0.1381 -0.0422 3   GLU A CA  
3    C C   . GLU A 3   ? 0.8259 0.7133 0.7400 0.0750  -0.1286 -0.0313 3   GLU A C   
4    O O   . GLU A 3   ? 0.8389 0.7253 0.7490 0.0733  -0.1279 -0.0211 3   GLU A O   
5    C CB  . GLU A 3   ? 0.9972 0.8544 0.9007 0.0729  -0.1451 -0.0379 3   GLU A CB  
6    C CG  . GLU A 3   ? 1.2028 1.0488 1.1046 0.0774  -0.1531 -0.0509 3   GLU A CG  
7    C CD  . GLU A 3   ? 1.4479 1.2812 1.3453 0.0693  -0.1597 -0.0464 3   GLU A CD  
8    O OE1 . GLU A 3   ? 1.3903 1.2221 1.2848 0.0604  -0.1585 -0.0325 3   GLU A OE1 
9    O OE2 . GLU A 3   ? 1.4515 1.2770 1.3485 0.0719  -0.1661 -0.0570 3   GLU A OE2 
10   N N   . ILE A 4   ? 0.7561 0.6587 0.6794 0.0718  -0.1220 -0.0336 4   ILE A N   
11   C CA  . ILE A 4   ? 0.6895 0.6091 0.6196 0.0672  -0.1132 -0.0251 4   ILE A CA  
12   C C   . ILE A 4   ? 0.6988 0.6154 0.6261 0.0565  -0.1138 -0.0116 4   ILE A C   
13   O O   . ILE A 4   ? 0.6389 0.5486 0.5649 0.0503  -0.1174 -0.0111 4   ILE A O   
14   C CB  . ILE A 4   ? 0.6519 0.5872 0.5922 0.0667  -0.1072 -0.0322 4   ILE A CB  
15   C CG1 . ILE A 4   ? 0.6288 0.5710 0.5723 0.0769  -0.1048 -0.0436 4   ILE A CG1 
16   C CG2 . ILE A 4   ? 0.6201 0.5703 0.5672 0.0596  -0.1000 -0.0225 4   ILE A CG2 
17   C CD1 . ILE A 4   ? 0.6145 0.5682 0.5655 0.0765  -0.1015 -0.0532 4   ILE A CD1 
28   N N   . PRO A 5   ? 0.6541 0.5769 0.5808 0.0538  -0.1103 -0.0009 5   PRO A N   
29   C CA  . PRO A 5   ? 0.6399 0.5623 0.5645 0.0431  -0.1102 0.0118  5   PRO A CA  
30   C C   . PRO A 5   ? 0.6343 0.5658 0.5667 0.0362  -0.1064 0.0119  5   PRO A C   
31   O O   . PRO A 5   ? 0.5469 0.4923 0.4883 0.0384  -0.1006 0.0065  5   PRO A O   
32   C CB  . PRO A 5   ? 0.6573 0.5917 0.5834 0.0429  -0.1049 0.0203  5   PRO A CB  
33   C CG  . PRO A 5   ? 0.6729 0.6058 0.5971 0.0533  -0.1053 0.0138  5   PRO A CG  
34   C CD  . PRO A 5   ? 0.6210 0.5520 0.5488 0.0604  -0.1063 -0.0002 5   PRO A CD  
42   N N   . LYS A 6   ? 0.5916 0.5149 0.5200 0.0274  -0.1100 0.0185  6   LYS A N   
43   C CA  . LYS A 6   ? 0.5878 0.5194 0.5232 0.0202  -0.1065 0.0196  6   LYS A CA  
44   C C   . LYS A 6   ? 0.5404 0.4910 0.4842 0.0172  -0.0983 0.0258  6   LYS A C   
45   O O   . LYS A 6   ? 0.5229 0.4845 0.4753 0.0149  -0.0940 0.0229  6   LYS A O   
46   C CB  . LYS A 6   ? 0.7655 0.6847 0.6945 0.0110  -0.1117 0.0268  6   LYS A CB  
47   C CG  . LYS A 6   ? 0.8744 0.7746 0.7960 0.0140  -0.1206 0.0197  6   LYS A CG  
48   C CD  . LYS A 6   ? 1.0514 0.9399 0.9676 0.0047  -0.1258 0.0262  6   LYS A CD  
49   C CE  . LYS A 6   ? 1.1781 1.0483 1.0881 0.0082  -0.1352 0.0178  6   LYS A CE  
50   N NZ  . LYS A 6   ? 1.3607 1.2192 1.2657 -0.0006 -0.1406 0.0235  6   LYS A NZ  
64   N N   . GLU A 7   ? 0.5459 0.5011 0.4875 0.0174  -0.0963 0.0338  7   GLU A N   
65   C CA  . GLU A 7   ? 0.5394 0.5136 0.4896 0.0155  -0.0890 0.0387  7   GLU A CA  
66   C C   . GLU A 7   ? 0.5191 0.5053 0.4783 0.0231  -0.0843 0.0293  7   GLU A C   
67   O O   . GLU A 7   ? 0.5073 0.5074 0.4756 0.0209  -0.0793 0.0296  7   GLU A O   
68   C CB  . GLU A 7   ? 0.6312 0.6094 0.5774 0.0153  -0.0880 0.0474  7   GLU A CB  
69   C CG  . GLU A 7   ? 0.9030 0.8665 0.8374 0.0097  -0.0941 0.0555  7   GLU A CG  
70   C CD  . GLU A 7   ? 1.0208 0.9690 0.9461 0.0166  -0.1002 0.0510  7   GLU A CD  
71   O OE1 . GLU A 7   ? 1.0054 0.9579 0.9295 0.0221  -0.0987 0.0513  7   GLU A OE1 
72   O OE2 . GLU A 7   ? 0.7654 0.6973 0.6852 0.0168  -0.1066 0.0466  7   GLU A OE2 
79   N N   . MET A 8   ? 0.4972 0.4779 0.4536 0.0322  -0.0862 0.0211  8   MET A N   
80   C CA  . MET A 8   ? 0.4908 0.4822 0.4546 0.0398  -0.0821 0.0119  8   MET A CA  
81   C C   . MET A 8   ? 0.4007 0.3945 0.3700 0.0375  -0.0817 0.0045  8   MET A C   
82   O O   . MET A 8   ? 0.3988 0.4061 0.3767 0.0373  -0.0770 0.0025  8   MET A O   
83   C CB  . MET A 8   ? 0.5331 0.5165 0.4915 0.0496  -0.0849 0.0049  8   MET A CB  
84   C CG  . MET A 8   ? 0.4991 0.4940 0.4634 0.0581  -0.0804 -0.0018 8   MET A CG  
85   S SD  . MET A 8   ? 0.4852 0.4704 0.4423 0.0690  -0.0836 -0.0079 8   MET A SD  
86   C CE  . MET A 8   ? 0.4345 0.4246 0.3891 0.0687  -0.0815 0.0033  8   MET A CE  
96   N N   . LEU A 9   ? 0.4906 0.4714 0.4548 0.0353  -0.0870 0.0006  9   LEU A N   
97   C CA  . LEU A 9   ? 0.4831 0.4668 0.4522 0.0322  -0.0868 -0.0065 9   LEU A CA  
98   C C   . LEU A 9   ? 0.4598 0.4537 0.4356 0.0230  -0.0830 0.0008  9   LEU A C   
99   O O   . LEU A 9   ? 0.4412 0.4455 0.4244 0.0215  -0.0799 -0.0035 9   LEU A O   
100  C CB  . LEU A 9   ? 0.5222 0.4903 0.4847 0.0309  -0.0936 -0.0111 9   LEU A CB  
101  C CG  . LEU A 9   ? 0.8488 0.8198 0.8158 0.0253  -0.0937 -0.0166 9   LEU A CG  
102  C CD1 . LEU A 9   ? 0.7799 0.7627 0.7534 0.0301  -0.0904 -0.0275 9   LEU A CD1 
103  C CD2 . LEU A 9   ? 0.9319 0.8873 0.8923 0.0240  -0.1009 -0.0208 9   LEU A CD2 
115  N N   . ARG A 10  ? 0.4357 0.4265 0.4086 0.0164  -0.0835 0.0119  10  ARG A N   
116  C CA  . ARG A 10  ? 0.4664 0.4669 0.4457 0.0077  -0.0801 0.0190  10  ARG A CA  
117  C C   . ARG A 10  ? 0.4144 0.4319 0.4026 0.0104  -0.0743 0.0194  10  ARG A C   
118  O O   . ARG A 10  ? 0.4035 0.4306 0.3993 0.0061  -0.0716 0.0191  10  ARG A O   
119  C CB  . ARG A 10  ? 0.4851 0.4798 0.4588 0.0007  -0.0817 0.0308  10  ARG A CB  
120  C CG  . ARG A 10  ? 0.6061 0.6117 0.5861 -0.0078 -0.0779 0.0392  10  ARG A CG  
121  C CD  . ARG A 10  ? 0.6757 0.6848 0.6620 -0.0133 -0.0771 0.0355  10  ARG A CD  
122  N NE  . ARG A 10  ? 0.7982 0.7939 0.7793 -0.0157 -0.0819 0.0310  10  ARG A NE  
123  C CZ  . ARG A 10  ? 0.8495 0.8373 0.8269 -0.0239 -0.0845 0.0367  10  ARG A CZ  
124  N NH1 . ARG A 10  ? 0.7601 0.7515 0.7379 -0.0309 -0.0829 0.0475  10  ARG A NH1 
125  N NH2 . ARG A 10  ? 0.7266 0.7031 0.7002 -0.0250 -0.0891 0.0310  10  ARG A NH2 
139  N N   . ALA A 11  ? 0.3979 0.4192 0.3853 0.0171  -0.0727 0.0205  11  ALA A N   
140  C CA  . ALA A 11  ? 0.3608 0.3981 0.3567 0.0203  -0.0677 0.0207  11  ALA A CA  
141  C C   . ALA A 11  ? 0.3668 0.4099 0.3686 0.0240  -0.0664 0.0108  11  ALA A C   
142  O O   . ALA A 11  ? 0.3322 0.3872 0.3423 0.0219  -0.0635 0.0110  11  ALA A O   
143  C CB  . ALA A 11  ? 0.3475 0.3869 0.3406 0.0275  -0.0666 0.0226  11  ALA A CB  
149  N N   . GLN A 12  ? 0.3391 0.3738 0.3364 0.0290  -0.0690 0.0018  12  GLN A N   
150  C CA  . GLN A 12  ? 0.3574 0.3982 0.3594 0.0322  -0.0680 -0.0082 12  GLN A CA  
151  C C   . GLN A 12  ? 0.3400 0.3836 0.3462 0.0235  -0.0683 -0.0090 12  GLN A C   
152  O O   . GLN A 12  ? 0.3318 0.3859 0.3449 0.0223  -0.0660 -0.0119 12  GLN A O   
153  C CB  . GLN A 12  ? 0.3348 0.3664 0.3307 0.0394  -0.0711 -0.0181 12  GLN A CB  
154  C CG  . GLN A 12  ? 0.3620 0.3910 0.3539 0.0487  -0.0709 -0.0185 12  GLN A CG  
155  C CD  . GLN A 12  ? 0.3545 0.3722 0.3395 0.0553  -0.0749 -0.0273 12  GLN A CD  
156  O OE1 . GLN A 12  ? 0.3998 0.4089 0.3814 0.0529  -0.0788 -0.0322 12  GLN A OE1 
157  N NE2 . GLN A 12  ? 0.3877 0.4056 0.3707 0.0640  -0.0742 -0.0295 12  GLN A NE2 
166  N N   . THR A 13  ? 0.3596 0.3933 0.3614 0.0172  -0.0714 -0.0065 13  THR A N   
167  C CA  . THR A 13  ? 0.3276 0.3635 0.3331 0.0083  -0.0717 -0.0068 13  THR A CA  
168  C C   . THR A 13  ? 0.3498 0.3967 0.3628 0.0024  -0.0684 0.0011  13  THR A C   
169  O O   . THR A 13  ? 0.3219 0.3764 0.3408 -0.0021 -0.0675 -0.0014 13  THR A O   
170  C CB  . THR A 13  ? 0.3652 0.3881 0.3645 0.0029  -0.0757 -0.0045 13  THR A CB  
171  O OG1 . THR A 13  ? 0.4129 0.4255 0.4056 0.0092  -0.0796 -0.0128 13  THR A OG1 
172  C CG2 . THR A 13  ? 0.3664 0.3915 0.3693 -0.0062 -0.0761 -0.0054 13  THR A CG2 
180  N N   . ASN A 14  ? 0.3363 0.3842 0.3489 0.0017  -0.0671 0.0105  14  ASN A N   
181  C CA  . ASN A 14  ? 0.3671 0.4263 0.3872 -0.0031 -0.0643 0.0177  14  ASN A CA  
182  C C   . ASN A 14  ? 0.3087 0.3802 0.3365 0.0013  -0.0619 0.0129  14  ASN A C   
183  O O   . ASN A 14  ? 0.3086 0.3883 0.3435 -0.0038 -0.0611 0.0141  14  ASN A O   
184  C CB  . ASN A 14  ? 0.3500 0.4104 0.3681 -0.0028 -0.0632 0.0271  14  ASN A CB  
185  C CG  . ASN A 14  ? 0.4793 0.5317 0.4925 -0.0109 -0.0650 0.0350  14  ASN A CG  
186  O OD1 . ASN A 14  ? 0.5633 0.6154 0.5790 -0.0188 -0.0655 0.0370  14  ASN A OD1 
187  N ND2 . ASN A 14  ? 0.6091 0.6552 0.6152 -0.0094 -0.0662 0.0401  14  ASN A ND2 
194  C C9  . BP5 A 15  ? 0.2939 0.3859 0.3282 0.0334  -0.0566 -0.0061 15  BP5 A C9  
195  C C8  . BP5 A 15  ? 0.3425 0.4301 0.3723 0.0405  -0.0572 -0.0146 15  BP5 A C8  
196  C C7  . BP5 A 15  ? 0.3231 0.4185 0.3564 0.0471  -0.0558 -0.0203 15  BP5 A C7  
197  C C6  . BP5 A 15  ? 0.3347 0.4416 0.3762 0.0466  -0.0542 -0.0174 15  BP5 A C6  
198  C C5  . BP5 A 15  ? 0.4095 0.5377 0.4601 0.0677  -0.0512 -0.0333 15  BP5 A C5  
199  C C4  . BP5 A 15  ? 0.4188 0.5500 0.4743 0.0602  -0.0518 -0.0259 15  BP5 A C4  
200  C C3  . BP5 A 15  ? 0.3866 0.5010 0.4314 0.0540  -0.0531 -0.0233 15  BP5 A C3  
201  C C2  . BP5 A 15  ? 0.4066 0.5172 0.4463 0.0617  -0.0529 -0.0309 15  BP5 A C2  
202  C C1  . BP5 A 15  ? 0.3994 0.5172 0.4420 0.0686  -0.0517 -0.0359 15  BP5 A C1  
203  C C12 . BP5 A 15  ? 0.3491 0.4321 0.3787 0.0264  -0.0583 0.0001  15  BP5 A C12 
204  C C11 . BP5 A 15  ? 0.3094 0.4136 0.3521 0.0337  -0.0549 -0.0039 15  BP5 A C11 
205  N N1  . BP5 A 15  ? 0.4083 0.5331 0.4610 0.0533  -0.0525 -0.0208 15  BP5 A N1  
206  N N2  . BP5 A 15  ? 0.3900 0.5013 0.4363 0.0402  -0.0540 -0.0094 15  BP5 A N2  
207  C CA  . BP5 A 15  ? 0.2810 0.3652 0.3142 0.0158  -0.0591 0.0037  15  BP5 A CA  
208  C C   . BP5 A 15  ? 0.3075 0.3936 0.3432 0.0129  -0.0602 -0.0038 15  BP5 A C   
209  O O   . BP5 A 15  ? 0.2877 0.3832 0.3305 0.0105  -0.0595 -0.0038 15  BP5 A O   
210  N N   . BP5 A 15  ? 0.2964 0.3691 0.3228 0.0106  -0.0612 0.0080  15  BP5 A N   
215  N N   . ILE A 16  ? 0.2999 0.3777 0.3300 0.0129  -0.0622 -0.0105 16  ILE A N   
216  C CA  . ILE A 16  ? 0.2994 0.3799 0.3312 0.0093  -0.0634 -0.0183 16  ILE A CA  
217  C C   . ILE A 16  ? 0.3250 0.4086 0.3613 -0.0018 -0.0640 -0.0137 16  ILE A C   
218  O O   . ILE A 16  ? 0.2995 0.3911 0.3410 -0.0052 -0.0639 -0.0161 16  ILE A O   
219  C CB  . ILE A 16  ? 0.3135 0.3850 0.3384 0.0113  -0.0658 -0.0266 16  ILE A CB  
220  C CG1 . ILE A 16  ? 0.3267 0.3962 0.3478 0.0226  -0.0655 -0.0327 16  ILE A CG1 
221  C CG2 . ILE A 16  ? 0.3218 0.3971 0.3484 0.0053  -0.0671 -0.0340 16  ILE A CG2 
222  C CD1 . ILE A 16  ? 0.3712 0.4304 0.3851 0.0258  -0.0685 -0.0399 16  ILE A CD1 
234  N N   . LEU A 17  ? 0.2917 0.3690 0.3260 -0.0078 -0.0647 -0.0067 17  LEU A N   
235  C CA  . LEU A 17  ? 0.3101 0.3900 0.3486 -0.0184 -0.0652 -0.0021 17  LEU A CA  
236  C C   . LEU A 17  ? 0.3364 0.4268 0.3830 -0.0201 -0.0637 0.0034  17  LEU A C   
237  O O   . LEU A 17  ? 0.3175 0.4132 0.3691 -0.0268 -0.0644 0.0032  17  LEU A O   
238  C CB  . LEU A 17  ? 0.3362 0.4070 0.3705 -0.0237 -0.0662 0.0048  17  LEU A CB  
239  C CG  . LEU A 17  ? 0.3083 0.3680 0.3353 -0.0235 -0.0688 -0.0010 17  LEU A CG  
240  C CD1 . LEU A 17  ? 0.3790 0.4290 0.4013 -0.0285 -0.0702 0.0069  17  LEU A CD1 
241  C CD2 . LEU A 17  ? 0.4134 0.4754 0.4419 -0.0290 -0.0703 -0.0086 17  LEU A CD2 
253  N N   . LEU A 18  ? 0.2977 0.3913 0.3457 -0.0144 -0.0619 0.0084  18  LEU A N   
254  C CA  . LEU A 18  ? 0.2965 0.4007 0.3528 -0.0150 -0.0610 0.0127  18  LEU A CA  
255  C C   . LEU A 18  ? 0.2830 0.3940 0.3434 -0.0123 -0.0616 0.0057  18  LEU A C   
256  O O   . LEU A 18  ? 0.2835 0.4009 0.3504 -0.0172 -0.0628 0.0070  18  LEU A O   
257  C CB  . LEU A 18  ? 0.3085 0.4163 0.3655 -0.0084 -0.0589 0.0177  18  LEU A CB  
258  C CG  . LEU A 18  ? 0.3011 0.4049 0.3548 -0.0121 -0.0583 0.0262  18  LEU A CG  
259  C CD1 . LEU A 18  ? 0.3686 0.4758 0.4210 -0.0043 -0.0564 0.0288  18  LEU A CD1 
260  C CD2 . LEU A 18  ? 0.3175 0.4271 0.3777 -0.0202 -0.0586 0.0324  18  LEU A CD2 
272  N N   . ASN A 19  ? 0.3134 0.4226 0.3698 -0.0050 -0.0613 -0.0020 19  ASN A N   
273  C CA  . ASN A 19  ? 0.2962 0.4120 0.3557 -0.0026 -0.0621 -0.0088 19  ASN A CA  
274  C C   . ASN A 19  ? 0.3290 0.4452 0.3892 -0.0119 -0.0643 -0.0123 19  ASN A C   
275  O O   . ASN A 19  ? 0.3532 0.4762 0.4184 -0.0149 -0.0658 -0.0133 19  ASN A O   
276  C CB  . ASN A 19  ? 0.3191 0.4328 0.3737 0.0070  -0.0612 -0.0165 19  ASN A CB  
277  C CG  . ASN A 19  ? 0.4317 0.5539 0.4904 0.0124  -0.0610 -0.0205 19  ASN A CG  
278  O OD1 . ASN A 19  ? 0.4482 0.5748 0.5099 0.0195  -0.0596 -0.0181 19  ASN A OD1 
279  N ND2 . ASN A 19  ? 0.5047 0.6299 0.5639 0.0086  -0.0628 -0.0266 19  ASN A ND2 
286  N N   . VAL A 20  ? 0.3052 0.4144 0.3605 -0.0170 -0.0651 -0.0140 20  VAL A N   
287  C CA  . VAL A 20  ? 0.3033 0.4140 0.3595 -0.0268 -0.0672 -0.0170 20  VAL A CA  
288  C C   . VAL A 20  ? 0.3057 0.4209 0.3685 -0.0351 -0.0682 -0.0095 20  VAL A C   
289  O O   . VAL A 20  ? 0.3154 0.4359 0.3816 -0.0410 -0.0703 -0.0116 20  VAL A O   
290  C CB  . VAL A 20  ? 0.3245 0.4270 0.3749 -0.0311 -0.0679 -0.0192 20  VAL A CB  
291  C CG1 . VAL A 20  ? 0.3492 0.4543 0.4012 -0.0425 -0.0699 -0.0211 20  VAL A CG1 
292  C CG2 . VAL A 20  ? 0.3331 0.4314 0.3772 -0.0232 -0.0678 -0.0281 20  VAL A CG2 
302  N N   . LEU A 21  ? 0.2917 0.4045 0.3562 -0.0363 -0.0672 -0.0008 21  LEU A N   
303  C CA  . LEU A 21  ? 0.2591 0.3760 0.3301 -0.0441 -0.0684 0.0061  21  LEU A CA  
304  C C   . LEU A 21  ? 0.2975 0.4230 0.3753 -0.0404 -0.0694 0.0067  21  LEU A C   
305  O O   . LEU A 21  ? 0.2836 0.4132 0.3671 -0.0471 -0.0718 0.0096  21  LEU A O   
306  C CB  . LEU A 21  ? 0.2940 0.4072 0.3647 -0.0456 -0.0670 0.0147  21  LEU A CB  
307  C CG  . LEU A 21  ? 0.2739 0.3781 0.3386 -0.0512 -0.0670 0.0151  21  LEU A CG  
308  C CD1 . LEU A 21  ? 0.3068 0.4076 0.3708 -0.0530 -0.0658 0.0244  21  LEU A CD1 
309  C CD2 . LEU A 21  ? 0.3191 0.4235 0.3853 -0.0620 -0.0691 0.0138  21  LEU A CD2 
321  N N   . LYS A 22  ? 0.3032 0.4311 0.3805 -0.0298 -0.0679 0.0037  22  LYS A N   
322  C CA  . LYS A 22  ? 0.3437 0.4797 0.4273 -0.0257 -0.0693 0.0031  22  LYS A CA  
323  C C   . LYS A 22  ? 0.3434 0.4819 0.4276 -0.0302 -0.0724 -0.0027 22  LYS A C   
324  O O   . LYS A 22  ? 0.4189 0.5626 0.5090 -0.0327 -0.0754 -0.0012 22  LYS A O   
325  C CB  . LYS A 22  ? 0.3514 0.4892 0.4337 -0.0135 -0.0668 0.0008  22  LYS A CB  
326  C CG  . LYS A 22  ? 0.4102 0.5557 0.4979 -0.0076 -0.0683 -0.0019 22  LYS A CG  
327  C CD  . LYS A 22  ? 0.4425 0.5883 0.5268 0.0038  -0.0655 -0.0060 22  LYS A CD  
328  C CE  . LYS A 22  ? 0.5163 0.6682 0.6036 0.0096  -0.0670 -0.0110 22  LYS A CE  
329  N NZ  . LYS A 22  ? 0.6628 0.8147 0.7468 0.0207  -0.0640 -0.0146 22  LYS A NZ  
343  N N   . GLN A 23  ? 0.3349 0.4700 0.4129 -0.0320 -0.0722 -0.0092 23  GLN A N   
344  C CA  . GLN A 23  ? 0.3247 0.4632 0.4024 -0.0377 -0.0751 -0.0150 23  GLN A CA  
345  C C   . GLN A 23  ? 0.3555 0.4943 0.4361 -0.0505 -0.0781 -0.0111 23  GLN A C   
346  O O   . GLN A 23  ? 0.4058 0.5486 0.4879 -0.0563 -0.0816 -0.0134 23  GLN A O   
347  C CB  . GLN A 23  ? 0.3213 0.4574 0.3916 -0.0362 -0.0739 -0.0237 23  GLN A CB  
348  C CG  . GLN A 23  ? 0.3861 0.5203 0.4527 -0.0237 -0.0710 -0.0277 23  GLN A CG  
349  C CD  . GLN A 23  ? 0.4645 0.6040 0.5349 -0.0154 -0.0709 -0.0274 23  GLN A CD  
350  O OE1 . GLN A 23  ? 0.5191 0.6575 0.5896 -0.0063 -0.0685 -0.0254 23  GLN A OE1 
351  N NE2 . GLN A 23  ? 0.4302 0.5756 0.5037 -0.0186 -0.0739 -0.0294 23  GLN A NE2 
360  N N   . GLY A 24  ? 0.3899 0.3594 0.3941 -0.0550 -0.1019 0.1038  24  GLY A N   
361  C CA  . GLY A 24  ? 0.3812 0.3392 0.3637 -0.0563 -0.1062 0.1006  24  GLY A CA  
362  C C   . GLY A 24  ? 0.3557 0.3164 0.3464 -0.0459 -0.1030 0.0886  24  GLY A C   
363  O O   . GLY A 24  ? 0.3527 0.3285 0.3633 -0.0395 -0.0945 0.0823  24  GLY A O   
367  N N   . ASP A 25  ? 0.3817 0.3273 0.3557 -0.0448 -0.1100 0.0854  25  ASP A N   
368  C CA  . ASP A 25  ? 0.3741 0.3207 0.3525 -0.0358 -0.1074 0.0739  25  ASP A CA  
369  C C   . ASP A 25  ? 0.3506 0.3184 0.3325 -0.0368 -0.0942 0.0684  25  ASP A C   
370  O O   . ASP A 25  ? 0.3600 0.3374 0.3310 -0.0465 -0.0891 0.0731  25  ASP A O   
371  C CB  . ASP A 25  ? 0.3705 0.2996 0.3274 -0.0362 -0.1165 0.0717  25  ASP A CB  
372  C CG  . ASP A 25  ? 0.4059 0.3139 0.3581 -0.0356 -0.1303 0.0764  25  ASP A CG  
373  O OD1 . ASP A 25  ? 0.4029 0.3096 0.3685 -0.0351 -0.1326 0.0812  25  ASP A OD1 
374  O OD2 . ASP A 25  ? 0.4106 0.3036 0.3459 -0.0356 -0.1390 0.0747  25  ASP A OD2 
379  N N   . ASN A 26  ? 0.3334 0.3089 0.3305 -0.0272 -0.0885 0.0579  26  ASN A N   
380  C CA  . ASN A 26  ? 0.3469 0.3439 0.3517 -0.0269 -0.0755 0.0518  26  ASN A CA  
381  C C   . ASN A 26  ? 0.3419 0.3403 0.3555 -0.0165 -0.0722 0.0396  26  ASN A C   
382  O O   . ASN A 26  ? 0.3345 0.3192 0.3520 -0.0092 -0.0791 0.0361  26  ASN A O   
383  C CB  . ASN A 26  ? 0.3351 0.3486 0.3608 -0.0271 -0.0689 0.0551  26  ASN A CB  
384  C CG  . ASN A 26  ? 0.3396 0.3749 0.3642 -0.0337 -0.0575 0.0539  26  ASN A CG  
385  O OD1 . ASN A 26  ? 0.3416 0.3842 0.3583 -0.0345 -0.0512 0.0466  26  ASN A OD1 
386  N ND2 . ASN A 26  ? 0.3757 0.4215 0.4081 -0.0391 -0.0547 0.0609  26  ASN A ND2 
393  N N   . TYR A 27  ? 0.3250 0.3409 0.3425 -0.0160 -0.0612 0.0324  27  TYR A N   
394  C CA  . TYR A 27  ? 0.3361 0.3555 0.3614 -0.0069 -0.0565 0.0203  27  TYR A CA  
395  C C   . TYR A 27  ? 0.3529 0.3910 0.4039 -0.0006 -0.0468 0.0148  27  TYR A C   
396  O O   . TYR A 27  ? 0.2941 0.3452 0.3539 -0.0047 -0.0426 0.0199  27  TYR A O   
397  C CB  . TYR A 27  ? 0.3859 0.4076 0.3904 -0.0121 -0.0526 0.0153  27  TYR A CB  
398  C CG  . TYR A 27  ? 0.3971 0.4383 0.3967 -0.0212 -0.0422 0.0158  27  TYR A CG  
399  C CD1 . TYR A 27  ? 0.4522 0.4925 0.4348 -0.0337 -0.0442 0.0258  27  TYR A CD1 
400  C CD2 . TYR A 27  ? 0.4678 0.5280 0.4791 -0.0176 -0.0303 0.0055  27  TYR A CD2 
401  C CE1 . TYR A 27  ? 0.5167 0.5754 0.4941 -0.0429 -0.0342 0.0254  27  TYR A CE1 
402  C CE2 . TYR A 27  ? 0.4856 0.5648 0.4933 -0.0262 -0.0204 0.0046  27  TYR A CE2 
403  C CZ  . TYR A 27  ? 0.5284 0.6072 0.5191 -0.0391 -0.0221 0.0144  27  TYR A CZ  
404  O OH  . TYR A 27  ? 0.6247 0.7235 0.6116 -0.0485 -0.0115 0.0126  27  TYR A OH  
414  N N   . VAL A 28  ? 0.3402 0.3794 0.4034 0.0096  -0.0439 0.0044  28  VAL A N   
415  C CA  . VAL A 28  ? 0.2842 0.3364 0.3739 0.0175  -0.0377 -0.0003 28  VAL A CA  
416  C C   . VAL A 28  ? 0.3042 0.3799 0.4009 0.0131  -0.0270 -0.0012 28  VAL A C   
417  O O   . VAL A 28  ? 0.2752 0.3611 0.3894 0.0139  -0.0250 0.0022  28  VAL A O   
418  C CB  . VAL A 28  ? 0.2549 0.3041 0.3539 0.0284  -0.0358 -0.0121 28  VAL A CB  
419  C CG1 . VAL A 28  ? 0.3175 0.3820 0.4412 0.0360  -0.0281 -0.0185 28  VAL A CG1 
420  C CG2 . VAL A 28  ? 0.3769 0.4055 0.4756 0.0332  -0.0459 -0.0109 28  VAL A CG2 
430  N N   . TYR A 29  ? 0.3168 0.4024 0.4011 0.0082  -0.0198 -0.0067 29  TYR A N   
431  C CA  . TYR A 29  ? 0.3452 0.4549 0.4385 0.0044  -0.0088 -0.0095 29  TYR A CA  
432  C C   . TYR A 29  ? 0.3221 0.4365 0.4102 -0.0062 -0.0102 0.0020  29  TYR A C   
433  O O   . TYR A 29  ? 0.3502 0.4826 0.4545 -0.0070 -0.0041 0.0024  29  TYR A O   
434  C CB  . TYR A 29  ? 0.3955 0.5148 0.4746 -0.0004 -0.0006 -0.0177 29  TYR A CB  
435  C CG  . TYR A 29  ? 0.5181 0.6348 0.6015 0.0092  0.0019  -0.0296 29  TYR A CG  
436  C CD1 . TYR A 29  ? 0.4744 0.5976 0.5835 0.0212  0.0052  -0.0375 29  TYR A CD1 
437  C CD2 . TYR A 29  ? 0.6476 0.7542 0.7086 0.0060  0.0004  -0.0329 29  TYR A CD2 
438  C CE1 . TYR A 29  ? 0.5563 0.6761 0.6684 0.0297  0.0075  -0.0485 29  TYR A CE1 
439  C CE2 . TYR A 29  ? 0.6161 0.7202 0.6804 0.0143  0.0029  -0.0439 29  TYR A CE2 
440  C CZ  . TYR A 29  ? 0.6821 0.7928 0.7719 0.0261  0.0066  -0.0517 29  TYR A CZ  
441  O OH  . TYR A 29  ? 0.7576 0.8652 0.8501 0.0342  0.0090  -0.0627 29  TYR A OH  
451  N N   . GLY A 30  ? 0.3363 0.4343 0.4016 -0.0143 -0.0184 0.0112  30  GLY A N   
452  C CA  . GLY A 30  ? 0.3143 0.4139 0.3726 -0.0247 -0.0206 0.0226  30  GLY A CA  
453  C C   . GLY A 30  ? 0.3088 0.4085 0.3880 -0.0201 -0.0242 0.0286  30  GLY A C   
454  O O   . GLY A 30  ? 0.2812 0.3941 0.3672 -0.0258 -0.0206 0.0338  30  GLY A O   
458  N N   . ILE A 31  ? 0.2867 0.3718 0.3759 -0.0105 -0.0314 0.0278  31  ILE A N   
459  C CA  . ILE A 31  ? 0.2468 0.3306 0.3559 -0.0059 -0.0351 0.0327  31  ILE A CA  
460  C C   . ILE A 31  ? 0.2759 0.3811 0.4102 -0.0003 -0.0264 0.0268  31  ILE A C   
461  O O   . ILE A 31  ? 0.2440 0.3583 0.3916 -0.0020 -0.0257 0.0324  31  ILE A O   
462  C CB  . ILE A 31  ? 0.2877 0.3510 0.4000 0.0025  -0.0441 0.0313  31  ILE A CB  
463  C CG1 . ILE A 31  ? 0.2685 0.3118 0.3581 -0.0033 -0.0536 0.0376  31  ILE A CG1 
464  C CG2 . ILE A 31  ? 0.3002 0.3620 0.4335 0.0074  -0.0475 0.0350  31  ILE A CG2 
465  C CD1 . ILE A 31  ? 0.2997 0.3246 0.3893 0.0046  -0.0610 0.0330  31  ILE A CD1 
477  N N   . ILE A 32  ? 0.2656 0.3790 0.4074 0.0069  -0.0199 0.0151  32  ILE A N   
478  C CA  . ILE A 32  ? 0.2629 0.3964 0.4293 0.0131  -0.0120 0.0084  32  ILE A CA  
479  C C   . ILE A 32  ? 0.2899 0.4444 0.4568 0.0038  -0.0049 0.0115  32  ILE A C   
480  O O   . ILE A 32  ? 0.2949 0.4623 0.4811 0.0051  -0.0029 0.0136  32  ILE A O   
481  C CB  . ILE A 32  ? 0.2915 0.4305 0.4634 0.0214  -0.0058 -0.0054 32  ILE A CB  
482  C CG1 . ILE A 32  ? 0.3075 0.4265 0.4825 0.0311  -0.0131 -0.0083 32  ILE A CG1 
483  C CG2 . ILE A 32  ? 0.3080 0.4707 0.5046 0.0265  0.0031  -0.0128 32  ILE A CG2 
484  C CD1 . ILE A 32  ? 0.3390 0.4595 0.5147 0.0384  -0.0080 -0.0213 32  ILE A CD1 
496  N N   . LYS A 33  ? 0.2555 0.4137 0.4008 -0.0064 -0.0010 0.0117  33  LYS A N   
497  C CA  . LYS A 33  ? 0.3118 0.4900 0.4554 -0.0167 0.0063  0.0142  33  LYS A CA  
498  C C   . LYS A 33  ? 0.3017 0.4770 0.4470 -0.0226 0.0008  0.0270  33  LYS A C   
499  O O   . LYS A 33  ? 0.2790 0.4731 0.4391 -0.0249 0.0059  0.0280  33  LYS A O   
500  C CB  . LYS A 33  ? 0.3761 0.5542 0.4915 -0.0283 0.0098  0.0137  33  LYS A CB  
501  C CG  . LYS A 33  ? 0.3975 0.5976 0.5097 -0.0404 0.0186  0.0148  33  LYS A CG  
502  C CD  . LYS A 33  ? 0.5669 0.7665 0.6495 -0.0532 0.0223  0.0142  33  LYS A CD  
503  C CE  . LYS A 33  ? 0.6688 0.8883 0.7463 -0.0671 0.0300  0.0170  33  LYS A CE  
504  N NZ  . LYS A 33  ? 0.8306 1.0507 0.8784 -0.0812 0.0343  0.0161  33  LYS A NZ  
518  N N   . GLN A 34  ? 0.3016 0.4541 0.4317 -0.0255 -0.0095 0.0366  34  GLN A N   
519  C CA  . GLN A 34  ? 0.3007 0.4493 0.4304 -0.0319 -0.0149 0.0489  34  GLN A CA  
520  C C   . GLN A 34  ? 0.3075 0.4616 0.4653 -0.0235 -0.0163 0.0497  34  GLN A C   
521  O O   . GLN A 34  ? 0.2514 0.4154 0.4171 -0.0286 -0.0155 0.0564  34  GLN A O   
522  C CB  . GLN A 34  ? 0.3092 0.4312 0.4184 -0.0355 -0.0263 0.0577  34  GLN A CB  
523  C CG  . GLN A 34  ? 0.5278 0.6431 0.6068 -0.0482 -0.0275 0.0628  34  GLN A CG  
524  C CD  . GLN A 34  ? 0.5597 0.6510 0.6229 -0.0525 -0.0395 0.0738  34  GLN A CD  
525  O OE1 . GLN A 34  ? 0.5728 0.6580 0.6478 -0.0499 -0.0450 0.0799  34  GLN A OE1 
526  N NE2 . GLN A 34  ? 0.6425 0.7199 0.6790 -0.0592 -0.0439 0.0760  34  GLN A NE2 
535  N N   . VAL A 35  ? 0.2810 0.4280 0.4532 -0.0112 -0.0188 0.0432  35  VAL A N   
536  C CA  . VAL A 35  ? 0.2441 0.3947 0.4418 -0.0035 -0.0208 0.0441  35  VAL A CA  
537  C C   . VAL A 35  ? 0.2663 0.4432 0.4852 -0.0004 -0.0115 0.0371  35  VAL A C   
538  O O   . VAL A 35  ? 0.3046 0.4911 0.5408 0.0001  -0.0119 0.0411  35  VAL A O   
539  C CB  . VAL A 35  ? 0.2781 0.4115 0.4831 0.0077  -0.0268 0.0395  35  VAL A CB  
540  C CG1 . VAL A 35  ? 0.2883 0.4264 0.5196 0.0157  -0.0282 0.0390  35  VAL A CG1 
541  C CG2 . VAL A 35  ? 0.3091 0.4177 0.4970 0.0044  -0.0368 0.0470  35  VAL A CG2 
551  N N   . LYS A 36  ? 0.2738 0.4636 0.4921 0.0014  -0.0031 0.0262  36  LYS A N   
552  C CA  . LYS A 36  ? 0.2816 0.4985 0.5200 0.0035  0.0062  0.0187  36  LYS A CA  
553  C C   . LYS A 36  ? 0.2914 0.5238 0.5276 -0.0082 0.0096  0.0260  36  LYS A C   
554  O O   . LYS A 36  ? 0.2966 0.5453 0.5541 -0.0063 0.0118  0.0262  36  LYS A O   
555  C CB  . LYS A 36  ? 0.2504 0.4781 0.4849 0.0053  0.0152  0.0057  36  LYS A CB  
556  C CG  . LYS A 36  ? 0.3078 0.5646 0.5663 0.0095  0.0254  -0.0053 36  LYS A CG  
557  C CD  . LYS A 36  ? 0.4225 0.6915 0.6707 0.0064  0.0355  -0.0168 36  LYS A CD  
558  C CE  . LYS A 36  ? 0.5312 0.8236 0.8049 0.0152  0.0445  -0.0314 36  LYS A CE  
559  N NZ  . LYS A 36  ? 0.6141 0.9278 0.9128 0.0164  0.0471  -0.0314 36  LYS A NZ  
573  N N   . GLU A 37  ? 0.3110 0.5377 0.5208 -0.0207 0.0095  0.0325  37  GLU A N   
574  C CA  . GLU A 37  ? 0.2948 0.5349 0.4995 -0.0331 0.0128  0.0396  37  GLU A CA  
575  C C   . GLU A 37  ? 0.2727 0.5068 0.4872 -0.0334 0.0054  0.0509  37  GLU A C   
576  O O   . GLU A 37  ? 0.2928 0.5456 0.5221 -0.0363 0.0092  0.0526  37  GLU A O   
577  C CB  . GLU A 37  ? 0.3729 0.6037 0.5447 -0.0467 0.0125  0.0452  37  GLU A CB  
578  C CG  . GLU A 37  ? 0.4231 0.6654 0.5835 -0.0507 0.0217  0.0351  37  GLU A CG  
579  C CD  . GLU A 37  ? 0.6676 0.9002 0.7944 -0.0656 0.0206  0.0419  37  GLU A CD  
580  O OE1 . GLU A 37  ? 0.6983 0.9213 0.8139 -0.0739 0.0147  0.0542  37  GLU A OE1 
581  O OE2 . GLU A 37  ? 0.6918 0.9253 0.8029 -0.0691 0.0252  0.0352  37  GLU A OE2 
588  N N   . ALA A 38  ? 0.2732 0.4817 0.4789 -0.0315 -0.0050 0.0586  38  ALA A N   
589  C CA  . ALA A 38  ? 0.2413 0.4412 0.4529 -0.0332 -0.0125 0.0698  38  ALA A CA  
590  C C   . ALA A 38  ? 0.2740 0.4832 0.5160 -0.0230 -0.0130 0.0670  38  ALA A C   
591  O O   . ALA A 38  ? 0.3428 0.5532 0.5936 -0.0257 -0.0167 0.0754  38  ALA A O   
592  C CB  . ALA A 38  ? 0.2971 0.4678 0.4930 -0.0329 -0.0231 0.0766  38  ALA A CB  
598  N N   . SER A 39  ? 0.2717 0.4871 0.5294 -0.0117 -0.0097 0.0556  39  SER A N   
599  C CA  . SER A 39  ? 0.2803 0.5046 0.5668 -0.0016 -0.0104 0.0520  39  SER A CA  
600  C C   . SER A 39  ? 0.2919 0.5465 0.5966 -0.0009 -0.0009 0.0442  39  SER A C   
601  O O   . SER A 39  ? 0.3141 0.5782 0.6444 0.0084  -0.0012 0.0395  39  SER A O   
602  C CB  . SER A 39  ? 0.3171 0.5280 0.6112 0.0112  -0.0138 0.0441  39  SER A CB  
603  O OG  . SER A 39  ? 0.3305 0.5517 0.6240 0.0151  -0.0060 0.0319  39  SER A OG  
609  N N   . ASN A 40  ? 0.2339 0.5036 0.5259 -0.0110 0.0072  0.0425  40  ASN A N   
610  C CA  . ASN A 40  ? 0.3075 0.6077 0.6151 -0.0119 0.0175  0.0338  40  ASN A CA  
611  C C   . ASN A 40  ? 0.4147 0.7247 0.7412 0.0010  0.0222  0.0188  40  ASN A C   
612  O O   . ASN A 40  ? 0.3237 0.6548 0.6759 0.0070  0.0262  0.0116  40  ASN A O   
613  C CB  . ASN A 40  ? 0.3409 0.6551 0.6676 -0.0135 0.0162  0.0396  40  ASN A CB  
614  C CG  . ASN A 40  ? 0.3451 0.6493 0.6541 -0.0260 0.0115  0.0543  40  ASN A CG  
615  O OD1 . ASN A 40  ? 0.3360 0.6348 0.6190 -0.0373 0.0135  0.0584  40  ASN A OD1 
616  N ND2 . ASN A 40  ? 0.3333 0.6337 0.6555 -0.0242 0.0048  0.0626  40  ASN A ND2 
623  N N   . GLY A 41  ? 0.3455 0.6408 0.6592 0.0051  0.0217  0.0136  41  GLY A N   
624  C CA  . GLY A 41  ? 0.3651 0.6661 0.6943 0.0173  0.0254  -0.0002 41  GLY A CA  
625  C C   . GLY A 41  ? 0.3328 0.6184 0.6788 0.0307  0.0169  -0.0006 41  GLY A C   
626  O O   . GLY A 41  ? 0.5071 0.7900 0.8606 0.0409  0.0182  -0.0110 41  GLY A O   
630  N N   . GLU A 42  ? 0.3220 0.5958 0.6720 0.0304  0.0081  0.0106  42  GLU A N   
631  C CA  . GLU A 42  ? 0.3707 0.6333 0.7397 0.0422  0.0004  0.0101  42  GLU A CA  
632  C C   . GLU A 42  ? 0.3921 0.6293 0.7498 0.0483  -0.0048 0.0080  42  GLU A C   
633  O O   . GLU A 42  ? 0.4204 0.6529 0.7930 0.0598  -0.0071 0.0008  42  GLU A O   
634  C CB  . GLU A 42  ? 0.4719 0.7284 0.8462 0.0385  -0.0074 0.0230  42  GLU A CB  
635  C CG  . GLU A 42  ? 0.5889 0.8375 0.9806 0.0488  -0.0143 0.0220  42  GLU A CG  
636  C CD  . GLU A 42  ? 0.7499 1.0163 1.1571 0.0566  -0.0092 0.0106  42  GLU A CD  
637  O OE1 . GLU A 42  ? 0.6904 0.9860 1.1113 0.0537  -0.0002 0.0053  42  GLU A OE1 
638  O OE2 . GLU A 42  ? 0.6296 0.8803 1.0342 0.0647  -0.0140 0.0072  42  GLU A OE2 
645  N N   . MET A 43  ? 0.3176 0.5382 0.6493 0.0409  -0.0072 0.0138  43  MET A N   
646  C CA  . MET A 43  ? 0.3662 0.5622 0.6865 0.0457  -0.0130 0.0126  43  MET A CA  
647  C C   . MET A 43  ? 0.2866 0.4825 0.5885 0.0435  -0.0071 0.0053  43  MET A C   
648  O O   . MET A 43  ? 0.3491 0.5422 0.6293 0.0332  -0.0062 0.0107  43  MET A O   
649  C CB  . MET A 43  ? 0.3047 0.4792 0.6114 0.0397  -0.0223 0.0252  43  MET A CB  
650  C CG  . MET A 43  ? 0.3362 0.4855 0.6334 0.0445  -0.0290 0.0239  43  MET A CG  
651  S SD  . MET A 43  ? 0.3669 0.4944 0.6518 0.0370  -0.0395 0.0378  43  MET A SD  
652  C CE  . MET A 43  ? 0.4196 0.5525 0.7292 0.0401  -0.0434 0.0432  43  MET A CE  
662  N N   . GLU A 44  ? 0.3365 0.5345 0.6466 0.0530  -0.0035 -0.0067 44  GLU A N   
663  C CA  . GLU A 44  ? 0.3442 0.5417 0.6388 0.0524  0.0021  -0.0151 44  GLU A CA  
664  C C   . GLU A 44  ? 0.3711 0.5439 0.6588 0.0590  -0.0048 -0.0167 44  GLU A C   
665  O O   . GLU A 44  ? 0.3297 0.4997 0.6320 0.0697  -0.0053 -0.0246 44  GLU A O   
666  C CB  . GLU A 44  ? 0.3395 0.5596 0.6491 0.0577  0.0122  -0.0285 44  GLU A CB  
667  C CG  . GLU A 44  ? 0.5376 0.7843 0.8560 0.0512  0.0196  -0.0285 44  GLU A CG  
668  C CD  . GLU A 44  ? 0.6856 0.9546 1.0092 0.0521  0.0313  -0.0423 44  GLU A CD  
669  O OE1 . GLU A 44  ? 0.5513 0.8140 0.8616 0.0530  0.0344  -0.0493 44  GLU A OE1 
670  O OE2 . GLU A 44  ? 0.5945 0.8879 0.9358 0.0516  0.0375  -0.0466 44  GLU A OE2 
677  N N   . LEU A 45  ? 0.3060 0.4605 0.5720 0.0526  -0.0106 -0.0092 45  LEU A N   
678  C CA  . LEU A 45  ? 0.3243 0.4561 0.5834 0.0579  -0.0173 -0.0108 45  LEU A CA  
679  C C   . LEU A 45  ? 0.3018 0.4340 0.5536 0.0622  -0.0119 -0.0225 45  LEU A C   
680  O O   . LEU A 45  ? 0.3165 0.4612 0.5584 0.0571  -0.0046 -0.0263 45  LEU A O   
681  C CB  . LEU A 45  ? 0.3219 0.4354 0.5608 0.0500  -0.0250 -0.0005 45  LEU A CB  
682  C CG  . LEU A 45  ? 0.3389 0.4492 0.5824 0.0448  -0.0310 0.0116  45  LEU A CG  
683  C CD1 . LEU A 45  ? 0.3481 0.4401 0.5712 0.0375  -0.0384 0.0201  45  LEU A CD1 
684  C CD2 . LEU A 45  ? 0.3480 0.4528 0.6123 0.0531  -0.0355 0.0112  45  LEU A CD2 
696  N N   . ASN A 46  ? 0.3009 0.4193 0.5575 0.0711  -0.0154 -0.0284 46  ASN A N   
697  C CA  . ASN A 46  ? 0.3655 0.4809 0.6145 0.0755  -0.0116 -0.0392 46  ASN A CA  
698  C C   . ASN A 46  ? 0.2866 0.3834 0.5119 0.0711  -0.0168 -0.0366 46  ASN A C   
699  O O   . ASN A 46  ? 0.3059 0.3858 0.5255 0.0692  -0.0254 -0.0292 46  ASN A O   
700  C CB  . ASN A 46  ? 0.3911 0.5010 0.6570 0.0874  -0.0126 -0.0477 46  ASN A CB  
701  C CG  . ASN A 46  ? 0.4594 0.5710 0.7207 0.0923  -0.0066 -0.0601 46  ASN A CG  
702  O OD1 . ASN A 46  ? 0.5305 0.6253 0.7829 0.0956  -0.0103 -0.0637 46  ASN A OD1 
703  N ND2 . ASN A 46  ? 0.5274 0.6598 0.7942 0.0923  0.0029  -0.0672 46  ASN A ND2 
710  N N   . GLU A 47  ? 0.4100 0.5001 0.3834 -0.0051 -0.0288 -0.0549 47  GLU A N   
711  C CA  . GLU A 47  ? 0.4081 0.4901 0.3893 -0.0118 -0.0347 -0.0498 47  GLU A CA  
712  C C   . GLU A 47  ? 0.3637 0.4347 0.3589 -0.0084 -0.0341 -0.0454 47  GLU A C   
713  O O   . GLU A 47  ? 0.3270 0.3940 0.3322 -0.0114 -0.0355 -0.0396 47  GLU A O   
714  C CB  . GLU A 47  ? 0.4720 0.5518 0.4455 -0.0169 -0.0406 -0.0534 47  GLU A CB  
715  C CG  . GLU A 47  ? 0.5277 0.5991 0.5067 -0.0238 -0.0474 -0.0497 47  GLU A CG  
716  C CD  . GLU A 47  ? 0.5558 0.6269 0.5247 -0.0279 -0.0523 -0.0544 47  GLU A CD  
717  O OE1 . GLU A 47  ? 0.6669 0.7404 0.6280 -0.0237 -0.0503 -0.0602 47  GLU A OE1 
718  O OE2 . GLU A 47  ? 0.5275 0.5964 0.4959 -0.0355 -0.0582 -0.0522 47  GLU A OE2 
725  N N   . ALA A 48  ? 0.3481 0.4139 0.3444 -0.0024 -0.0322 -0.0482 48  ALA A N   
726  C CA  . ALA A 48  ? 0.3337 0.3885 0.3432 0.0003  -0.0319 -0.0441 48  ALA A CA  
727  C C   . ALA A 48  ? 0.2919 0.3479 0.3101 0.0044  -0.0266 -0.0398 48  ALA A C   
728  O O   . ALA A 48  ? 0.3333 0.3815 0.3636 0.0039  -0.0274 -0.0346 48  ALA A O   
729  C CB  . ALA A 48  ? 0.3363 0.3855 0.3444 0.0062  -0.0307 -0.0482 48  ALA A CB  
735  N N   . THR A 49  ? 0.3487 0.4146 0.3607 0.0082  -0.0213 -0.0418 49  THR A N   
736  C CA  . THR A 49  ? 0.3213 0.3893 0.3408 0.0118  -0.0162 -0.0378 49  THR A CA  
737  C C   . THR A 49  ? 0.2811 0.3493 0.3070 0.0052  -0.0190 -0.0322 49  THR A C   
738  O O   . THR A 49  ? 0.3029 0.3660 0.3404 0.0061  -0.0177 -0.0271 49  THR A O   
739  C CB  . THR A 49  ? 0.3686 0.4479 0.3791 0.0165  -0.0105 -0.0414 49  THR A CB  
740  O OG1 . THR A 49  ? 0.3814 0.4607 0.3859 0.0228  -0.0080 -0.0468 49  THR A OG1 
741  C CG2 . THR A 49  ? 0.4437 0.5249 0.4619 0.0202  -0.0052 -0.0373 49  THR A CG2 
749  N N   . LEU A 50  ? 0.3099 0.3837 0.3282 -0.0014 -0.0230 -0.0332 50  LEU A N   
750  C CA  . LEU A 50  ? 0.3279 0.4013 0.3518 -0.0081 -0.0264 -0.0280 50  LEU A CA  
751  C C   . LEU A 50  ? 0.2905 0.3521 0.3257 -0.0116 -0.0314 -0.0238 50  LEU A C   
752  O O   . LEU A 50  ? 0.2956 0.3542 0.3410 -0.0138 -0.0321 -0.0183 50  LEU A O   
753  C CB  . LEU A 50  ? 0.2872 0.3684 0.2999 -0.0147 -0.0300 -0.0303 50  LEU A CB  
754  C CG  . LEU A 50  ? 0.3360 0.4289 0.3425 -0.0140 -0.0257 -0.0310 50  LEU A CG  
755  C CD1 . LEU A 50  ? 0.3508 0.4488 0.3511 -0.0058 -0.0196 -0.0361 50  LEU A CD1 
756  C CD2 . LEU A 50  ? 0.4116 0.5114 0.4078 -0.0211 -0.0295 -0.0327 50  LEU A CD2 
768  N N   . TYR A 51  ? 0.2789 0.3337 0.3127 -0.0122 -0.0351 -0.0262 51  TYR A N   
769  C CA  . TYR A 51  ? 0.2737 0.3176 0.3185 -0.0158 -0.0400 -0.0221 51  TYR A CA  
770  C C   . TYR A 51  ? 0.2689 0.3061 0.3269 -0.0106 -0.0362 -0.0183 51  TYR A C   
771  O O   . TYR A 51  ? 0.2867 0.3182 0.3559 -0.0135 -0.0384 -0.0132 51  TYR A O   
772  C CB  . TYR A 51  ? 0.2864 0.3240 0.3273 -0.0176 -0.0448 -0.0255 51  TYR A CB  
773  C CG  . TYR A 51  ? 0.3176 0.3605 0.3462 -0.0233 -0.0492 -0.0289 51  TYR A CG  
774  C CD1 . TYR A 51  ? 0.3793 0.4257 0.4066 -0.0305 -0.0531 -0.0263 51  TYR A CD1 
775  C CD2 . TYR A 51  ? 0.3893 0.4339 0.4075 -0.0215 -0.0494 -0.0350 51  TYR A CD2 
776  C CE1 . TYR A 51  ? 0.3815 0.4326 0.3971 -0.0359 -0.0571 -0.0295 51  TYR A CE1 
777  C CE2 . TYR A 51  ? 0.4050 0.4541 0.4121 -0.0268 -0.0534 -0.0382 51  TYR A CE2 
778  C CZ  . TYR A 51  ? 0.3648 0.4178 0.3702 -0.0340 -0.0569 -0.0355 51  TYR A CZ  
779  O OH  . TYR A 51  ? 0.4668 0.5247 0.4598 -0.0392 -0.0607 -0.0392 51  TYR A OH  
789  N N   . THR A 52  ? 0.2815 0.3196 0.3382 -0.0028 -0.0303 -0.0208 52  THR A N   
790  C CA  . THR A 52  ? 0.2724 0.3052 0.3410 0.0025  -0.0259 -0.0172 52  THR A CA  
791  C C   . THR A 52  ? 0.2801 0.3168 0.3553 0.0012  -0.0236 -0.0123 52  THR A C   
792  O O   . THR A 52  ? 0.3098 0.3401 0.3975 0.0001  -0.0243 -0.0072 52  THR A O   
793  C CB  . THR A 52  ? 0.3062 0.3412 0.3700 0.0110  -0.0196 -0.0210 52  THR A CB  
794  O OG1 . THR A 52  ? 0.3312 0.3614 0.3900 0.0125  -0.0217 -0.0254 52  THR A OG1 
795  C CG2 . THR A 52  ? 0.3894 0.4196 0.4645 0.0164  -0.0147 -0.0172 52  THR A CG2 
803  N N   . ILE A 53  ? 0.2876 0.3349 0.3546 0.0015  -0.0208 -0.0139 53  ILE A N   
804  C CA  . ILE A 53  ? 0.3264 0.3783 0.3989 0.0009  -0.0181 -0.0097 53  ILE A CA  
805  C C   . ILE A 53  ? 0.2965 0.3453 0.3754 -0.0069 -0.0238 -0.0051 53  ILE A C   
806  O O   . ILE A 53  ? 0.2987 0.3446 0.3889 -0.0072 -0.0229 -0.0001 53  ILE A O   
807  C CB  . ILE A 53  ? 0.3194 0.3835 0.3805 0.0025  -0.0143 -0.0128 53  ILE A CB  
808  C CG1 . ILE A 53  ? 0.3474 0.4138 0.4045 0.0111  -0.0080 -0.0166 53  ILE A CG1 
809  C CG2 . ILE A 53  ? 0.3231 0.3923 0.3886 0.0002  -0.0128 -0.0086 53  ILE A CG2 
810  C CD1 . ILE A 53  ? 0.3682 0.4465 0.4132 0.0131  -0.0045 -0.0207 53  ILE A CD1 
822  N N   . PHE A 54  ? 0.2847 0.3343 0.3569 -0.0132 -0.0298 -0.0068 54  PHE A N   
823  C CA  . PHE A 54  ? 0.2709 0.3178 0.3486 -0.0208 -0.0357 -0.0025 54  PHE A CA  
824  C C   . PHE A 54  ? 0.2771 0.3125 0.3680 -0.0218 -0.0387 0.0013  54  PHE A C   
825  O O   . PHE A 54  ? 0.3005 0.3332 0.4003 -0.0261 -0.0416 0.0060  54  PHE A O   
826  C CB  . PHE A 54  ? 0.2744 0.3247 0.3407 -0.0272 -0.0413 -0.0055 54  PHE A CB  
827  C CG  . PHE A 54  ? 0.2927 0.3550 0.3473 -0.0281 -0.0390 -0.0079 54  PHE A CG  
828  C CD1 . PHE A 54  ? 0.2893 0.3584 0.3447 -0.0239 -0.0327 -0.0070 54  PHE A CD1 
829  C CD2 . PHE A 54  ? 0.3272 0.3940 0.3699 -0.0332 -0.0429 -0.0112 54  PHE A CD2 
830  C CE1 . PHE A 54  ? 0.3028 0.3829 0.3479 -0.0248 -0.0306 -0.0093 54  PHE A CE1 
831  C CE2 . PHE A 54  ? 0.3008 0.3786 0.3330 -0.0342 -0.0407 -0.0134 54  PHE A CE2 
832  C CZ  . PHE A 54  ? 0.2833 0.3678 0.3169 -0.0301 -0.0346 -0.0124 54  PHE A CZ  
842  N N   . LYS A 55  ? 0.2670 0.2957 0.3593 -0.0185 -0.0387 -0.0009 55  LYS A N   
843  C CA  . LYS A 55  ? 0.2817 0.2995 0.3874 -0.0190 -0.0411 0.0028  55  LYS A CA  
844  C C   . LYS A 55  ? 0.3150 0.3316 0.4327 -0.0158 -0.0365 0.0075  55  LYS A C   
845  O O   . LYS A 55  ? 0.3337 0.3451 0.4629 -0.0192 -0.0393 0.0122  55  LYS A O   
846  C CB  . LYS A 55  ? 0.3432 0.3542 0.4483 -0.0150 -0.0408 -0.0003 55  LYS A CB  
847  C CG  . LYS A 55  ? 0.4064 0.4062 0.5263 -0.0147 -0.0422 0.0036  55  LYS A CG  
848  C CD  . LYS A 55  ? 0.5338 0.5273 0.6528 -0.0101 -0.0412 0.0004  55  LYS A CD  
849  C CE  . LYS A 55  ? 0.6723 0.6550 0.8059 -0.0093 -0.0418 0.0042  55  LYS A CE  
850  N NZ  . LYS A 55  ? 0.8831 0.8663 1.0268 -0.0058 -0.0364 0.0085  55  LYS A NZ  
864  N N   . ARG A 56  ? 0.2890 0.3107 0.4043 -0.0092 -0.0294 0.0062  56  ARG A N   
865  C CA  . ARG A 56  ? 0.3315 0.3522 0.4578 -0.0058 -0.0246 0.0104  56  ARG A CA  
866  C C   . ARG A 56  ? 0.3502 0.3757 0.4796 -0.0104 -0.0258 0.0141  56  ARG A C   
867  O O   . ARG A 56  ? 0.3443 0.3655 0.4861 -0.0117 -0.0262 0.0189  56  ARG A O   
868  C CB  . ARG A 56  ? 0.3720 0.3973 0.4940 0.0023  -0.0168 0.0081  56  ARG A CB  
869  C CG  . ARG A 56  ? 0.4893 0.5122 0.6234 0.0062  -0.0117 0.0125  56  ARG A CG  
870  C CD  . ARG A 56  ? 0.7134 0.7415 0.8433 0.0139  -0.0041 0.0106  56  ARG A CD  
871  N NE  . ARG A 56  ? 1.0839 1.1225 1.1999 0.0141  -0.0030 0.0064  56  ARG A NE  
872  C CZ  . ARG A 56  ? 0.9676 1.0148 1.0804 0.0124  -0.0016 0.0073  56  ARG A CZ  
873  N NH1 . ARG A 56  ? 0.7956 0.8427 0.9179 0.0112  -0.0003 0.0121  56  ARG A NH1 
874  N NH2 . ARG A 56  ? 0.7130 0.7691 0.8128 0.0119  -0.0014 0.0031  56  ARG A NH2 
888  N N   . LEU A 57  ? 0.2685 0.3031 0.3868 -0.0129 -0.0264 0.0119  57  LEU A N   
889  C CA  . LEU A 57  ? 0.2843 0.3239 0.4047 -0.0172 -0.0274 0.0153  57  LEU A CA  
890  C C   . LEU A 57  ? 0.2674 0.3011 0.3950 -0.0246 -0.0347 0.0189  57  LEU A C   
891  O O   . LEU A 57  ? 0.2882 0.3216 0.4246 -0.0271 -0.0353 0.0234  57  LEU A O   
892  C CB  . LEU A 57  ? 0.3166 0.3669 0.4228 -0.0188 -0.0269 0.0118  57  LEU A CB  
893  C CG  . LEU A 57  ? 0.2809 0.3391 0.3796 -0.0119 -0.0196 0.0084  57  LEU A CG  
894  C CD1 . LEU A 57  ? 0.3191 0.3873 0.4045 -0.0143 -0.0198 0.0051  57  LEU A CD1 
895  C CD2 . LEU A 57  ? 0.3408 0.3997 0.4492 -0.0082 -0.0142 0.0124  57  LEU A CD2 
907  N N   . GLU A 58  ? 0.2783 0.3070 0.4029 -0.0280 -0.0402 0.0171  58  GLU A N   
908  C CA  . GLU A 58  ? 0.2939 0.3164 0.4254 -0.0349 -0.0475 0.0204  58  GLU A CA  
909  C C   . GLU A 58  ? 0.3440 0.3576 0.4918 -0.0333 -0.0471 0.0246  58  GLU A C   
910  O O   . GLU A 58  ? 0.3245 0.3355 0.4820 -0.0372 -0.0500 0.0291  58  GLU A O   
911  C CB  . GLU A 58  ? 0.3461 0.3657 0.4694 -0.0384 -0.0532 0.0169  58  GLU A CB  
912  C CG  . GLU A 58  ? 0.5135 0.5313 0.6365 -0.0469 -0.0611 0.0188  58  GLU A CG  
913  C CD  . GLU A 58  ? 0.5498 0.5685 0.6597 -0.0502 -0.0655 0.0142  58  GLU A CD  
914  O OE1 . GLU A 58  ? 0.5257 0.5448 0.6291 -0.0457 -0.0628 0.0098  58  GLU A OE1 
915  O OE2 . GLU A 58  ? 0.5318 0.5510 0.6380 -0.0571 -0.0717 0.0150  58  GLU A OE2 
922  N N   . LYS A 59  ? 0.3212 0.3300 0.4722 -0.0276 -0.0436 0.0232  59  LYS A N   
923  C CA  . LYS A 59  ? 0.3926 0.3931 0.5586 -0.0255 -0.0424 0.0270  59  LYS A CA  
924  C C   . LYS A 59  ? 0.4016 0.4053 0.5761 -0.0240 -0.0382 0.0311  59  LYS A C   
925  O O   . LYS A 59  ? 0.3908 0.3893 0.5783 -0.0261 -0.0400 0.0354  59  LYS A O   
926  C CB  . LYS A 59  ? 0.4342 0.4306 0.6002 -0.0187 -0.0380 0.0244  59  LYS A CB  
927  C CG  . LYS A 59  ? 0.4842 0.4749 0.6640 -0.0142 -0.0335 0.0279  59  LYS A CG  
928  C CD  . LYS A 59  ? 0.6416 0.6305 0.8184 -0.0067 -0.0278 0.0249  59  LYS A CD  
929  C CE  . LYS A 59  ? 0.7765 0.7599 0.9482 -0.0070 -0.0314 0.0212  59  LYS A CE  
930  N NZ  . LYS A 59  ? 0.8207 0.8023 0.9890 0.0003  -0.0261 0.0182  59  LYS A NZ  
944  N N   . ASP A 60  ? 0.3533 0.3476 0.4484 0.0590  -0.0488 0.0165  60  ASP A N   
945  C CA  . ASP A 60  ? 0.3716 0.3690 0.4654 0.0613  -0.0453 0.0188  60  ASP A CA  
946  C C   . ASP A 60  ? 0.3877 0.3860 0.4783 0.0548  -0.0487 0.0173  60  ASP A C   
947  O O   . ASP A 60  ? 0.4158 0.4158 0.5055 0.0566  -0.0468 0.0192  60  ASP A O   
948  C CB  . ASP A 60  ? 0.3906 0.3969 0.4757 0.0675  -0.0415 0.0166  60  ASP A CB  
949  C CG  . ASP A 60  ? 0.4598 0.4648 0.5480 0.0751  -0.0371 0.0191  60  ASP A CG  
950  O OD1 . ASP A 60  ? 0.5244 0.5217 0.6228 0.0764  -0.0360 0.0239  60  ASP A OD1 
951  O OD2 . ASP A 60  ? 0.5463 0.5578 0.6267 0.0799  -0.0349 0.0161  60  ASP A OD2 
956  N N   . GLY A 61  ? 0.3422 0.3385 0.4310 0.0477  -0.0539 0.0142  61  GLY A N   
957  C CA  . GLY A 61  ? 0.3354 0.3318 0.4208 0.0413  -0.0575 0.0128  61  GLY A CA  
958  C C   . GLY A 61  ? 0.3183 0.3243 0.3934 0.0398  -0.0579 0.0091  61  GLY A C   
959  O O   . GLY A 61  ? 0.3195 0.3259 0.3923 0.0352  -0.0606 0.0086  61  GLY A O   
963  N N   . ILE A 62  ? 0.3223 0.3359 0.3917 0.0436  -0.0558 0.0064  62  ILE A N   
964  C CA  . ILE A 62  ? 0.3112 0.3347 0.3719 0.0428  -0.0560 0.0029  62  ILE A CA  
965  C C   . ILE A 62  ? 0.2923 0.3189 0.3478 0.0355  -0.0602 -0.0009 62  ILE A C   
966  O O   . ILE A 62  ? 0.3016 0.3342 0.3518 0.0316  -0.0620 -0.0030 62  ILE A O   
967  C CB  . ILE A 62  ? 0.3266 0.3570 0.3838 0.0504  -0.0518 0.0014  62  ILE A CB  
968  C CG1 . ILE A 62  ? 0.3776 0.4048 0.4391 0.0579  -0.0474 0.0056  62  ILE A CG1 
969  C CG2 . ILE A 62  ? 0.3206 0.3614 0.3697 0.0494  -0.0525 -0.0028 62  ILE A CG2 
970  C CD1 . ILE A 62  ? 0.4220 0.4499 0.4827 0.0579  -0.0479 0.0069  62  ILE A CD1 
982  N N   . ILE A 63  ? 0.3018 0.3247 0.3585 0.0342  -0.0617 -0.0017 63  ILE A N   
983  C CA  . ILE A 63  ? 0.3166 0.3412 0.3682 0.0281  -0.0655 -0.0048 63  ILE A CA  
984  C C   . ILE A 63  ? 0.3319 0.3453 0.3889 0.0254  -0.0689 -0.0035 63  ILE A C   
985  O O   . ILE A 63  ? 0.3184 0.3242 0.3833 0.0288  -0.0680 -0.0007 63  ILE A O   
986  C CB  . ILE A 63  ? 0.3096 0.3429 0.3548 0.0306  -0.0646 -0.0085 63  ILE A CB  
987  C CG1 . ILE A 63  ? 0.2958 0.3240 0.3443 0.0356  -0.0643 -0.0083 63  ILE A CG1 
988  C CG2 . ILE A 63  ? 0.3028 0.3463 0.3440 0.0346  -0.0612 -0.0099 63  ILE A CG2 
989  C CD1 . ILE A 63  ? 0.2933 0.3295 0.3355 0.0390  -0.0636 -0.0119 63  ILE A CD1 
1001 N N   . SER A 64  ? 0.2941 0.3067 0.3469 0.0195  -0.0728 -0.0056 64  SER A N   
1002 C CA  . SER A 64  ? 0.3052 0.3078 0.3613 0.0174  -0.0767 -0.0056 64  SER A CA  
1003 C C   . SER A 64  ? 0.3116 0.3180 0.3597 0.0153  -0.0792 -0.0092 64  SER A C   
1004 O O   . SER A 64  ? 0.3243 0.3412 0.3649 0.0140  -0.0780 -0.0112 64  SER A O   
1005 C CB  . SER A 64  ? 0.2976 0.2914 0.3574 0.0120  -0.0797 -0.0039 64  SER A CB  
1006 O OG  . SER A 64  ? 0.3218 0.3185 0.3744 0.0054  -0.0823 -0.0057 64  SER A OG  
1012 N N   . SER A 65  ? 0.3156 0.3135 0.3655 0.0154  -0.0829 -0.0099 65  SER A N   
1013 C CA  . SER A 65  ? 0.2975 0.2981 0.3397 0.0149  -0.0855 -0.0132 65  SER A CA  
1014 C C   . SER A 65  ? 0.2922 0.2837 0.3330 0.0100  -0.0904 -0.0139 65  SER A C   
1015 O O   . SER A 65  ? 0.3358 0.3166 0.3836 0.0082  -0.0927 -0.0122 65  SER A O   
1016 C CB  . SER A 65  ? 0.3607 0.3601 0.4042 0.0217  -0.0861 -0.0145 65  SER A CB  
1017 O OG  . SER A 65  ? 0.3875 0.3741 0.4404 0.0233  -0.0890 -0.0129 65  SER A OG  
1023 N N   . TYR A 66  ? 0.2980 0.2939 0.3297 0.0085  -0.0921 -0.0164 66  TYR A N   
1024 C CA  . TYR A 66  ? 0.3006 0.2881 0.3291 0.0046  -0.0968 -0.0175 66  TYR A CA  
1025 C C   . TYR A 66  ? 0.3222 0.3151 0.3410 0.0064  -0.0981 -0.0203 66  TYR A C   
1026 O O   . TYR A 66  ? 0.3313 0.3362 0.3453 0.0089  -0.0949 -0.0212 66  TYR A O   
1027 C CB  . TYR A 66  ? 0.3191 0.3067 0.3457 -0.0027 -0.0970 -0.0162 66  TYR A CB  
1028 C CG  . TYR A 66  ? 0.3015 0.3024 0.3208 -0.0062 -0.0939 -0.0163 66  TYR A CG  
1029 C CD1 . TYR A 66  ? 0.3108 0.3204 0.3327 -0.0058 -0.0899 -0.0149 66  TYR A CD1 
1030 C CD2 . TYR A 66  ? 0.3352 0.3405 0.3455 -0.0093 -0.0950 -0.0175 66  TYR A CD2 
1031 C CE1 . TYR A 66  ? 0.3210 0.3424 0.3375 -0.0093 -0.0878 -0.0150 66  TYR A CE1 
1032 C CE2 . TYR A 66  ? 0.3129 0.3307 0.3180 -0.0130 -0.0923 -0.0171 66  TYR A CE2 
1033 C CZ  . TYR A 66  ? 0.3229 0.3487 0.3315 -0.0130 -0.0890 -0.0160 66  TYR A CZ  
1034 O OH  . TYR A 66  ? 0.3727 0.4106 0.3772 -0.0168 -0.0870 -0.0158 66  TYR A OH  
1044 N N   . TRP A 67  ? 0.3483 0.3318 0.3641 0.0058  -0.1030 -0.0217 67  TRP A N   
1045 C CA  . TRP A 67  ? 0.4367 0.4244 0.4426 0.0086  -0.1046 -0.0243 67  TRP A CA  
1046 C C   . TRP A 67  ? 0.4507 0.4461 0.4472 0.0029  -0.1031 -0.0240 67  TRP A C   
1047 O O   . TRP A 67  ? 0.4335 0.4248 0.4306 -0.0035 -0.1037 -0.0226 67  TRP A O   
1048 C CB  . TRP A 67  ? 0.4974 0.4709 0.5042 0.0120  -0.1109 -0.0262 67  TRP A CB  
1049 C CG  . TRP A 67  ? 0.4920 0.4581 0.5092 0.0174  -0.1127 -0.0261 67  TRP A CG  
1050 C CD1 . TRP A 67  ? 0.5006 0.4539 0.5289 0.0167  -0.1152 -0.0248 67  TRP A CD1 
1051 C CD2 . TRP A 67  ? 0.4813 0.4527 0.4993 0.0244  -0.1119 -0.0271 67  TRP A CD2 
1052 N NE1 . TRP A 67  ? 0.5944 0.5448 0.6310 0.0226  -0.1159 -0.0245 67  TRP A NE1 
1053 C CE2 . TRP A 67  ? 0.5352 0.4962 0.5653 0.0274  -0.1141 -0.0260 67  TRP A CE2 
1054 C CE3 . TRP A 67  ? 0.5261 0.5099 0.5359 0.0284  -0.1096 -0.0289 67  TRP A CE3 
1055 C CZ2 . TRP A 67  ? 0.5493 0.5115 0.5832 0.0341  -0.1143 -0.0265 67  TRP A CZ2 
1056 C CZ3 . TRP A 67  ? 0.5483 0.5334 0.5612 0.0352  -0.1100 -0.0298 67  TRP A CZ3 
1057 C CH2 . TRP A 67  ? 0.5335 0.5075 0.5582 0.0379  -0.1124 -0.0286 67  TRP A CH2 
1068 N N   . GLY A 68  ? 0.5170 0.5242 0.5051 0.0051  -0.1011 -0.0252 68  GLY A N   
1069 C CA  . GLY A 68  ? 0.5942 0.6085 0.5731 0.0004  -0.0999 -0.0247 68  GLY A CA  
1070 C C   . GLY A 68  ? 0.7260 0.7314 0.6977 0.0017  -0.1044 -0.0261 68  GLY A C   
1071 O O   . GLY A 68  ? 0.7130 0.7053 0.6875 0.0056  -0.1092 -0.0278 68  GLY A O   
1075 N N   . ASP A 69  ? 0.8249 0.8376 0.7874 -0.0014 -0.1030 -0.0254 69  ASP A N   
1076 C CA  . ASP A 69  ? 0.8613 0.8660 0.8153 0.0000  -0.1068 -0.0265 69  ASP A CA  
1077 C C   . ASP A 69  ? 0.9249 0.9253 0.8761 0.0096  -0.1103 -0.0297 69  ASP A C   
1078 O O   . ASP A 69  ? 1.0053 0.9956 0.9511 0.0127  -0.1150 -0.0313 69  ASP A O   
1079 C CB  . ASP A 69  ? 1.0330 1.0490 0.9771 -0.0037 -0.1035 -0.0248 69  ASP A CB  
1080 C CG  . ASP A 69  ? 1.2305 1.2374 1.1651 -0.0026 -0.1072 -0.0254 69  ASP A CG  
1081 O OD1 . ASP A 69  ? 1.1902 1.1807 1.1265 -0.0006 -0.1126 -0.0273 69  ASP A OD1 
1082 O OD2 . ASP A 69  ? 1.3137 1.3296 1.2390 -0.0035 -0.1046 -0.0240 69  ASP A OD2 
1087 N N   . ARG A 75  ? 0.6027 0.6051 0.5646 0.0505  -0.1202 -0.0411 75  ARG A N   
1088 C CA  . ARG A 75  ? 0.6366 0.6346 0.6076 0.0421  -0.1174 -0.0380 75  ARG A CA  
1089 C C   . ARG A 75  ? 0.5702 0.5788 0.5468 0.0399  -0.1112 -0.0363 75  ARG A C   
1090 O O   . ARG A 75  ? 0.5413 0.5506 0.5226 0.0449  -0.1113 -0.0371 75  ARG A O   
1091 C CB  . ARG A 75  ? 0.6547 0.6345 0.6359 0.0428  -0.1230 -0.0380 75  ARG A CB  
1092 C CG  . ARG A 75  ? 0.6440 0.6170 0.6325 0.0346  -0.1216 -0.0353 75  ARG A CG  
1093 C CD  . ARG A 75  ? 0.6596 0.6149 0.6583 0.0361  -0.1277 -0.0357 75  ARG A CD  
1094 N NE  . ARG A 75  ? 0.6923 0.6406 0.6983 0.0288  -0.1267 -0.0333 75  ARG A NE  
1095 C CZ  . ARG A 75  ? 0.7306 0.6730 0.7320 0.0241  -0.1286 -0.0335 75  ARG A CZ  
1096 N NH1 . ARG A 75  ? 0.7746 0.7169 0.7641 0.0259  -0.1311 -0.0357 75  ARG A NH1 
1097 N NH2 . ARG A 75  ? 0.7753 0.7116 0.7835 0.0177  -0.1279 -0.0314 75  ARG A NH2 
1098 N N   . ARG A 76  ? 0.5079 0.5240 0.4841 0.0325  -0.1061 -0.0339 76  ARG A N   
1099 C CA  . ARG A 76  ? 0.5007 0.5297 0.4792 0.0309  -0.1001 -0.0328 76  ARG A CA  
1100 C C   . ARG A 76  ? 0.4570 0.4808 0.4458 0.0259  -0.0981 -0.0300 76  ARG A C   
1101 O O   . ARG A 76  ? 0.4580 0.4748 0.4489 0.0200  -0.0992 -0.0283 76  ARG A O   
1102 C CB  . ARG A 76  ? 0.5009 0.5447 0.4709 0.0269  -0.0959 -0.0323 76  ARG A CB  
1103 C CG  . ARG A 76  ? 0.4397 0.4964 0.4124 0.0245  -0.0902 -0.0314 76  ARG A CG  
1104 C CD  . ARG A 76  ? 0.5027 0.5752 0.4668 0.0233  -0.0869 -0.0318 76  ARG A CD  
1105 N NE  . ARG A 76  ? 0.4863 0.5650 0.4437 0.0311  -0.0878 -0.0347 76  ARG A NE  
1106 C CZ  . ARG A 76  ? 0.5855 0.6787 0.5351 0.0322  -0.0851 -0.0355 76  ARG A CZ  
1107 N NH1 . ARG A 76  ? 0.5484 0.6513 0.4963 0.0256  -0.0814 -0.0333 76  ARG A NH1 
1108 N NH2 . ARG A 76  ? 0.5925 0.6909 0.5363 0.0402  -0.0862 -0.0385 76  ARG A NH2 
1121 N N   . LYS A 77  ? 0.4040 0.4313 0.3987 0.0288  -0.0953 -0.0296 77  LYS A N   
1122 C CA  . LYS A 77  ? 0.3631 0.3855 0.3675 0.0258  -0.0933 -0.0269 77  LYS A CA  
1123 C C   . LYS A 77  ? 0.3136 0.3484 0.3165 0.0218  -0.0879 -0.0258 77  LYS A C   
1124 O O   . LYS A 77  ? 0.3449 0.3915 0.3443 0.0248  -0.0847 -0.0272 77  LYS A O   
1125 C CB  . LYS A 77  ? 0.3982 0.4151 0.4106 0.0318  -0.0935 -0.0266 77  LYS A CB  
1126 C CG  . LYS A 77  ? 0.4029 0.4117 0.4261 0.0296  -0.0923 -0.0233 77  LYS A CG  
1127 C CD  . LYS A 77  ? 0.4403 0.4430 0.4720 0.0358  -0.0927 -0.0224 77  LYS A CD  
1128 C CE  . LYS A 77  ? 0.5989 0.5862 0.6408 0.0353  -0.0967 -0.0205 77  LYS A CE  
1129 N NZ  . LYS A 77  ? 0.6063 0.5889 0.6568 0.0413  -0.0967 -0.0192 77  LYS A NZ  
1143 N N   . TYR A 78  ? 0.3411 0.3727 0.3468 0.0153  -0.0876 -0.0235 78  TYR A N   
1144 C CA  . TYR A 78  ? 0.3010 0.3422 0.3068 0.0114  -0.0836 -0.0223 78  TYR A CA  
1145 C C   . TYR A 78  ? 0.3115 0.3477 0.3261 0.0123  -0.0820 -0.0201 78  TYR A C   
1146 O O   . TYR A 78  ? 0.2924 0.3167 0.3136 0.0130  -0.0841 -0.0187 78  TYR A O   
1147 C CB  . TYR A 78  ? 0.3584 0.4003 0.3603 0.0036  -0.0847 -0.0212 78  TYR A CB  
1148 C CG  . TYR A 78  ? 0.4033 0.4554 0.3960 0.0026  -0.0842 -0.0227 78  TYR A CG  
1149 C CD1 . TYR A 78  ? 0.5359 0.5832 0.5230 0.0042  -0.0874 -0.0239 78  TYR A CD1 
1150 C CD2 . TYR A 78  ? 0.4877 0.5541 0.4776 0.0003  -0.0807 -0.0226 78  TYR A CD2 
1151 C CE1 . TYR A 78  ? 0.5421 0.5992 0.5204 0.0039  -0.0864 -0.0248 78  TYR A CE1 
1152 C CE2 . TYR A 78  ? 0.5292 0.6058 0.5115 -0.0006 -0.0798 -0.0234 78  TYR A CE2 
1153 C CZ  . TYR A 78  ? 0.5998 0.6719 0.5760 0.0013  -0.0824 -0.0243 78  TYR A CZ  
1154 O OH  . TYR A 78  ? 0.6651 0.7478 0.6334 0.0010  -0.0810 -0.0246 78  TYR A OH  
1164 N N   . TYR A 79  ? 0.3025 0.3484 0.3174 0.0129  -0.0781 -0.0199 79  TYR A N   
1165 C CA  . TYR A 79  ? 0.2834 0.3267 0.3052 0.0148  -0.0758 -0.0179 79  TYR A CA  
1166 C C   . TYR A 79  ? 0.2997 0.3479 0.3211 0.0096  -0.0749 -0.0168 79  TYR A C   
1167 O O   . TYR A 79  ? 0.2964 0.3547 0.3125 0.0065  -0.0744 -0.0180 79  TYR A O   
1168 C CB  . TYR A 79  ? 0.3205 0.3698 0.3426 0.0221  -0.0724 -0.0191 79  TYR A CB  
1169 C CG  . TYR A 79  ? 0.3388 0.3820 0.3624 0.0274  -0.0739 -0.0199 79  TYR A CG  
1170 C CD1 . TYR A 79  ? 0.3078 0.3400 0.3398 0.0304  -0.0743 -0.0174 79  TYR A CD1 
1171 C CD2 . TYR A 79  ? 0.3737 0.4222 0.3907 0.0298  -0.0752 -0.0229 79  TYR A CD2 
1172 C CE1 . TYR A 79  ? 0.3234 0.3496 0.3579 0.0353  -0.0764 -0.0180 79  TYR A CE1 
1173 C CE2 . TYR A 79  ? 0.3802 0.4227 0.3985 0.0350  -0.0775 -0.0239 79  TYR A CE2 
1174 C CZ  . TYR A 79  ? 0.3811 0.4124 0.4084 0.0375  -0.0783 -0.0214 79  TYR A CZ  
1175 O OH  . TYR A 79  ? 0.4822 0.5072 0.5114 0.0428  -0.0812 -0.0224 79  TYR A OH  
1185 N N   . ARG A 80  ? 0.2912 0.3324 0.3186 0.0090  -0.0750 -0.0143 80  ARG A N   
1186 C CA  . ARG A 80  ? 0.2856 0.3298 0.3132 0.0050  -0.0750 -0.0131 80  ARG A CA  
1187 C C   . ARG A 80  ? 0.2780 0.3203 0.3111 0.0100  -0.0725 -0.0113 80  ARG A C   
1188 O O   . ARG A 80  ? 0.3049 0.3387 0.3436 0.0135  -0.0719 -0.0094 80  ARG A O   
1189 C CB  . ARG A 80  ? 0.2952 0.3312 0.3232 -0.0020 -0.0790 -0.0118 80  ARG A CB  
1190 C CG  . ARG A 80  ? 0.3048 0.3271 0.3388 -0.0011 -0.0809 -0.0101 80  ARG A CG  
1191 C CD  . ARG A 80  ? 0.3555 0.3697 0.3892 -0.0082 -0.0852 -0.0093 80  ARG A CD  
1192 N NE  . ARG A 80  ? 0.3928 0.4071 0.4289 -0.0098 -0.0852 -0.0076 80  ARG A NE  
1193 C CZ  . ARG A 80  ? 0.3450 0.3527 0.3878 -0.0070 -0.0848 -0.0053 80  ARG A CZ  
1194 N NH1 . ARG A 80  ? 0.3454 0.3468 0.3942 -0.0023 -0.0834 -0.0043 80  ARG A NH1 
1195 N NH2 . ARG A 80  ? 0.4406 0.4483 0.4842 -0.0086 -0.0856 -0.0040 80  ARG A NH2 
1209 N N   . LEU A 81  ? 0.2947 0.3442 0.3267 0.0101  -0.0713 -0.0115 81  LEU A N   
1210 C CA  . LEU A 81  ? 0.2881 0.3343 0.3246 0.0141  -0.0698 -0.0093 81  LEU A CA  
1211 C C   . LEU A 81  ? 0.3129 0.3487 0.3533 0.0100  -0.0729 -0.0067 81  LEU A C   
1212 O O   . LEU A 81  ? 0.3613 0.3954 0.3995 0.0029  -0.0766 -0.0070 81  LEU A O   
1213 C CB  . LEU A 81  ? 0.3372 0.3924 0.3712 0.0149  -0.0693 -0.0105 81  LEU A CB  
1214 C CG  . LEU A 81  ? 0.3246 0.3901 0.3557 0.0204  -0.0660 -0.0131 81  LEU A CG  
1215 C CD1 . LEU A 81  ? 0.3750 0.4476 0.4048 0.0203  -0.0669 -0.0141 81  LEU A CD1 
1216 C CD2 . LEU A 81  ? 0.3234 0.3857 0.3569 0.0291  -0.0621 -0.0123 81  LEU A CD2 
1228 N N   . THR A 82  ? 0.3157 0.3444 0.3621 0.0146  -0.0713 -0.0039 82  THR A N   
1229 C CA  . THR A 82  ? 0.3228 0.3423 0.3734 0.0115  -0.0739 -0.0014 82  THR A CA  
1230 C C   . THR A 82  ? 0.3391 0.3620 0.3880 0.0112  -0.0749 -0.0010 82  THR A C   
1231 O O   . THR A 82  ? 0.3644 0.3959 0.4102 0.0142  -0.0734 -0.0023 82  THR A O   
1232 C CB  . THR A 82  ? 0.3059 0.3175 0.3643 0.0168  -0.0714 0.0017  82  THR A CB  
1233 O OG1 . THR A 82  ? 0.3200 0.3359 0.3795 0.0244  -0.0670 0.0031  82  THR A OG1 
1234 C CG2 . THR A 82  ? 0.3440 0.3515 0.4048 0.0175  -0.0713 0.0012  82  THR A CG2 
1242 N N   . GLU A 83  ? 0.4239 0.3968 0.4388 0.0669  -0.0407 0.0404  83  GLU A N   
1243 C CA  . GLU A 83  ? 0.4179 0.3913 0.4490 0.0756  -0.0562 0.0211  83  GLU A CA  
1244 C C   . GLU A 83  ? 0.4155 0.4087 0.4359 0.0796  -0.0499 0.0086  83  GLU A C   
1245 O O   . GLU A 83  ? 0.4435 0.4330 0.4702 0.0805  -0.0573 0.0043  83  GLU A O   
1246 C CB  . GLU A 83  ? 0.4826 0.4561 0.5260 0.0841  -0.0663 0.0060  83  GLU A CB  
1247 C CG  . GLU A 83  ? 0.4531 0.4038 0.5108 0.0795  -0.0766 0.0168  83  GLU A CG  
1248 C CD  . GLU A 83  ? 0.6324 0.5816 0.7049 0.0878  -0.0887 0.0009  83  GLU A CD  
1249 O OE1 . GLU A 83  ? 0.6122 0.5790 0.6836 0.0979  -0.0886 -0.0187 83  GLU A OE1 
1250 O OE2 . GLU A 83  ? 0.5958 0.5261 0.6810 0.0839  -0.0986 0.0082  83  GLU A OE2 
1257 N N   . ILE A 84  ? 0.4062 0.4201 0.4092 0.0811  -0.0360 0.0042  84  ILE A N   
1258 C CA  . ILE A 84  ? 0.4468 0.4804 0.4394 0.0838  -0.0304 -0.0078 84  ILE A CA  
1259 C C   . ILE A 84  ? 0.4416 0.4728 0.4236 0.0743  -0.0221 0.0068  84  ILE A C   
1260 O O   . ILE A 84  ? 0.4712 0.5093 0.4512 0.0750  -0.0229 -0.0013 84  ILE A O   
1261 C CB  . ILE A 84  ? 0.4851 0.5431 0.4623 0.0878  -0.0192 -0.0170 84  ILE A CB  
1262 C CG1 . ILE A 84  ? 0.7009 0.7792 0.6710 0.0918  -0.0170 -0.0337 84  ILE A CG1 
1263 C CG2 . ILE A 84  ? 0.3972 0.4582 0.3557 0.0793  -0.0041 0.0017  84  ILE A CG2 
1264 C CD1 . ILE A 84  ? 0.7470 0.8224 0.7347 0.1013  -0.0325 -0.0537 84  ILE A CD1 
1276 N N   . GLY A 85  ? 0.3939 0.4150 0.3690 0.0653  -0.0142 0.0283  85  GLY A N   
1277 C CA  . GLY A 85  ? 0.4082 0.4260 0.3749 0.0564  -0.0069 0.0426  85  GLY A CA  
1278 C C   . GLY A 85  ? 0.3909 0.3946 0.3730 0.0560  -0.0192 0.0417  85  GLY A C   
1279 O O   . GLY A 85  ? 0.3894 0.3965 0.3662 0.0522  -0.0158 0.0431  85  GLY A O   
1283 N N   . HIS A 86  ? 0.4025 0.3899 0.4040 0.0597  -0.0346 0.0392  86  HIS A N   
1284 C CA  . HIS A 86  ? 0.4128 0.3859 0.4296 0.0600  -0.0486 0.0384  86  HIS A CA  
1285 C C   . HIS A 86  ? 0.4186 0.4028 0.4356 0.0671  -0.0532 0.0186  86  HIS A C   
1286 O O   . HIS A 86  ? 0.4217 0.3997 0.4415 0.0646  -0.0572 0.0207  86  HIS A O   
1287 C CB  . HIS A 86  ? 0.4244 0.3790 0.4617 0.0630  -0.0660 0.0384  86  HIS A CB  
1288 C CG  . HIS A 86  ? 0.4504 0.3881 0.4914 0.0536  -0.0655 0.0609  86  HIS A CG  
1289 N ND1 . HIS A 86  ? 0.5122 0.4356 0.5603 0.0470  -0.0709 0.0751  86  HIS A ND1 
1290 C CD2 . HIS A 86  ? 0.5188 0.4520 0.5566 0.0494  -0.0598 0.0720  86  HIS A CD2 
1291 C CE1 . HIS A 86  ? 0.5202 0.4322 0.5694 0.0392  -0.0684 0.0936  86  HIS A CE1 
1292 N NE2 . HIS A 86  ? 0.4881 0.4050 0.5311 0.0404  -0.0618 0.0919  86  HIS A NE2 
1300 N N   . GLU A 87  ? 0.4322 0.4330 0.4456 0.0755  -0.0520 -0.0001 87  GLU A N   
1301 C CA  . GLU A 87  ? 0.4427 0.4564 0.4534 0.0815  -0.0541 -0.0189 87  GLU A CA  
1302 C C   . GLU A 87  ? 0.4759 0.5022 0.4684 0.0740  -0.0396 -0.0137 87  GLU A C   
1303 O O   . GLU A 87  ? 0.4778 0.5022 0.4709 0.0728  -0.0427 -0.0175 87  GLU A O   
1304 C CB  . GLU A 87  ? 0.5000 0.5306 0.5103 0.0919  -0.0551 -0.0395 87  GLU A CB  
1305 C CG  . GLU A 87  ? 0.6847 0.7297 0.6926 0.0988  -0.0577 -0.0605 87  GLU A CG  
1306 C CD  . GLU A 87  ? 0.7810 0.8095 0.8048 0.1036  -0.0753 -0.0680 87  GLU A CD  
1307 O OE1 . GLU A 87  ? 0.7988 0.8067 0.8383 0.1042  -0.0884 -0.0610 87  GLU A OE1 
1308 O OE2 . GLU A 87  ? 0.7164 0.7522 0.7365 0.1064  -0.0767 -0.0805 87  GLU A OE2 
1315 N N   . ASN A 88  ? 0.4327 0.4714 0.4089 0.0688  -0.0242 -0.0049 88  ASN A N   
1316 C CA  A ASN A 88  ? 0.4682 0.5185 0.4274 0.0610  -0.0115 0.0006  88  ASN A CA  
1317 C CA  B ASN A 88  ? 0.4682 0.5184 0.4270 0.0607  -0.0111 0.0014  88  ASN A CA  
1318 C C   . ASN A 88  ? 0.4572 0.4901 0.4204 0.0525  -0.0127 0.0170  88  ASN A C   
1319 O O   . ASN A 88  ? 0.4711 0.5082 0.4281 0.0481  -0.0095 0.0158  88  ASN A O   
1320 C CB  A ASN A 88  ? 0.5099 0.5743 0.4510 0.0567  0.0035  0.0092  88  ASN A CB  
1321 C CB  B ASN A 88  ? 0.5096 0.5715 0.4514 0.0561  0.0036  0.0119  88  ASN A CB  
1322 C CG  A ASN A 88  ? 0.5382 0.6270 0.4695 0.0632  0.0077  -0.0084 88  ASN A CG  
1323 C CG  B ASN A 88  ? 0.4845 0.5568 0.4082 0.0469  0.0162  0.0204  88  ASN A CG  
1324 O OD1 A ASN A 88  ? 0.6057 0.6978 0.5473 0.0728  -0.0010 -0.0249 88  ASN A OD1 
1325 O OD1 B ASN A 88  ? 0.5505 0.6415 0.4635 0.0471  0.0205  0.0085  88  ASN A OD1 
1326 N ND2 A ASN A 88  ? 0.5880 0.6948 0.4994 0.0578  0.0204  -0.0050 88  ASN A ND2 
1327 N ND2 B ASN A 88  ? 0.4343 0.4950 0.3546 0.0385  0.0220  0.0409  88  ASN A ND2 
1340 N N   . MET A 89  ? 0.4157 0.4294 0.3895 0.0497  -0.0177 0.0323  89  MET A N   
1341 C CA  . MET A 89  ? 0.3911 0.3888 0.3703 0.0421  -0.0198 0.0477  89  MET A CA  
1342 C C   . MET A 89  ? 0.4486 0.4388 0.4394 0.0458  -0.0329 0.0370  89  MET A C   
1343 O O   . MET A 89  ? 0.4394 0.4263 0.4274 0.0400  -0.0308 0.0424  89  MET A O   
1344 C CB  . MET A 89  ? 0.3997 0.3788 0.3897 0.0389  -0.0245 0.0649  89  MET A CB  
1345 C CG  . MET A 89  ? 0.5234 0.4853 0.5217 0.0317  -0.0289 0.0811  89  MET A CG  
1346 S SD  . MET A 89  ? 0.5432 0.5081 0.5260 0.0196  -0.0112 0.1023  89  MET A SD  
1347 C CE  . MET A 89  ? 0.4621 0.4477 0.4285 0.0195  -0.0017 0.0882  89  MET A CE  
1357 N N   . ARG A 90  ? 0.4389 0.4258 0.4422 0.0556  -0.0467 0.0214  90  ARG A N   
1358 C CA  . ARG A 90  ? 0.4698 0.4477 0.4836 0.0600  -0.0606 0.0113  90  ARG A CA  
1359 C C   . ARG A 90  ? 0.4976 0.4906 0.4993 0.0598  -0.0539 -0.0013 90  ARG A C   
1360 O O   . ARG A 90  ? 0.4828 0.4671 0.4864 0.0565  -0.0580 0.0006  90  ARG A O   
1361 C CB  . ARG A 90  ? 0.5141 0.4871 0.5426 0.0714  -0.0768 -0.0044 90  ARG A CB  
1362 C CG  . ARG A 90  ? 0.5530 0.5101 0.5953 0.0758  -0.0948 -0.0103 90  ARG A CG  
1363 C CD  . ARG A 90  ? 0.6027 0.5561 0.6588 0.0876  -0.1113 -0.0271 90  ARG A CD  
1364 N NE  . ARG A 90  ? 0.7358 0.7109 0.7838 0.0956  -0.1052 -0.0479 90  ARG A NE  
1365 C CZ  . ARG A 90  ? 0.8470 0.8335 0.8884 0.1001  -0.1042 -0.0644 90  ARG A CZ  
1366 N NH1 . ARG A 90  ? 0.8748 0.8518 0.9163 0.0975  -0.1090 -0.0630 90  ARG A NH1 
1367 N NH2 . ARG A 90  ? 0.8629 0.8707 0.8973 0.1071  -0.0982 -0.0825 90  ARG A NH2 
1381 N N   . LEU A 91  ? 0.4694 0.4846 0.4586 0.0629  -0.0443 -0.0141 91  LEU A N   
1382 C CA  . LEU A 91  ? 0.4726 0.5037 0.4490 0.0614  -0.0376 -0.0258 91  LEU A CA  
1383 C C   . LEU A 91  ? 0.4363 0.4678 0.4012 0.0489  -0.0259 -0.0101 91  LEU A C   
1384 O O   . LEU A 91  ? 0.4456 0.4768 0.4071 0.0449  -0.0261 -0.0136 91  LEU A O   
1385 C CB  . LEU A 91  ? 0.5439 0.6003 0.5090 0.0664  -0.0296 -0.0407 91  LEU A CB  
1386 C CG  . LEU A 91  ? 0.6374 0.6982 0.6124 0.0795  -0.0401 -0.0605 91  LEU A CG  
1387 C CD1 . LEU A 91  ? 0.7053 0.7912 0.6681 0.0827  -0.0298 -0.0700 91  LEU A CD1 
1388 C CD2 . LEU A 91  ? 0.5361 0.5945 0.5164 0.0848  -0.0504 -0.0771 91  LEU A CD2 
1400 N N   . VAL A 92  ? 0.4397 0.4717 0.3980 0.0424  -0.0157 0.0071  92  VAL A N   
1401 C CA  . VAL A 92  ? 0.4044 0.4361 0.3524 0.0309  -0.0051 0.0227  92  VAL A CA  
1402 C C   . VAL A 92  ? 0.4163 0.4267 0.3763 0.0267  -0.0133 0.0328  92  VAL A C   
1403 O O   . VAL A 92  ? 0.3961 0.4063 0.3510 0.0200  -0.0102 0.0345  92  VAL A O   
1404 C CB  . VAL A 92  ? 0.3893 0.4227 0.3295 0.0261  0.0057  0.0397  92  VAL A CB  
1405 C CG1 . VAL A 92  ? 0.4069 0.4355 0.3402 0.0150  0.0143  0.0578  92  VAL A CG1 
1406 C CG2 . VAL A 92  ? 0.4212 0.4776 0.3456 0.0285  0.0153  0.0310  92  VAL A CG2 
1416 N N   . SER A 93  ? 0.4189 0.4106 0.3948 0.0298  -0.0242 0.0404  93  SER A N   
1417 C CA  . SER A 93  ? 0.4343 0.4053 0.4224 0.0261  -0.0334 0.0513  93  SER A CA  
1418 C C   . SER A 93  ? 0.4619 0.4301 0.4527 0.0288  -0.0419 0.0373  93  SER A C   
1419 O O   . SER A 93  ? 0.4481 0.4078 0.4390 0.0218  -0.0418 0.0451  93  SER A O   
1420 C CB  . SER A 93  ? 0.4569 0.4102 0.4621 0.0302  -0.0465 0.0586  93  SER A CB  
1421 O OG  . SER A 93  ? 0.4972 0.4487 0.5008 0.0253  -0.0390 0.0756  93  SER A OG  
1427 N N   . GLU A 94  ? 0.4206 0.3956 0.4137 0.0388  -0.0495 0.0167  94  GLU A N   
1428 C CA  . GLU A 94  ? 0.4550 0.4269 0.4500 0.0419  -0.0581 0.0025  94  GLU A CA  
1429 C C   . GLU A 94  ? 0.4729 0.4577 0.4524 0.0336  -0.0459 -0.0001 94  GLU A C   
1430 O O   . GLU A 94  ? 0.4689 0.4437 0.4498 0.0297  -0.0501 0.0000  94  GLU A O   
1431 C CB  . GLU A 94  ? 0.5999 0.5799 0.5984 0.0546  -0.0668 -0.0204 94  GLU A CB  
1432 C CG  . GLU A 94  ? 0.7358 0.6996 0.7520 0.0632  -0.0836 -0.0210 94  GLU A CG  
1433 C CD  . GLU A 94  ? 0.8700 0.8400 0.8906 0.0761  -0.0941 -0.0452 94  GLU A CD  
1434 O OE1 . GLU A 94  ? 0.8053 0.7913 0.8153 0.0780  -0.0885 -0.0613 94  GLU A OE1 
1435 O OE2 . GLU A 94  ? 0.8581 0.8173 0.8928 0.0841  -0.1084 -0.0483 94  GLU A OE2 
1442 N N   . SER A 95  ? 0.4663 0.4729 0.4309 0.0308  -0.0317 -0.0030 95  SER A N   
1443 C CA  . SER A 95  ? 0.4684 0.4884 0.4181 0.0224  -0.0214 -0.0064 95  SER A CA  
1444 C C   . SER A 95  ? 0.4055 0.4132 0.3545 0.0105  -0.0167 0.0132  95  SER A C   
1445 O O   . SER A 95  ? 0.4436 0.4504 0.3879 0.0036  -0.0153 0.0112  95  SER A O   
1446 C CB  . SER A 95  ? 0.4086 0.4547 0.3419 0.0213  -0.0082 -0.0116 95  SER A CB  
1447 O OG  . SER A 95  ? 0.4126 0.4593 0.3408 0.0156  0.0014  0.0066  95  SER A OG  
1453 N N   . TRP A 96  ? 0.3852 0.3836 0.3389 0.0076  -0.0139 0.0322  96  TRP A N   
1454 C CA  A TRP A 96  ? 0.3990 0.3871 0.3523 -0.0034 -0.0086 0.0513  96  TRP A CA  
1455 C CA  B TRP A 96  ? 0.3987 0.3869 0.3521 -0.0034 -0.0087 0.0512  96  TRP A CA  
1456 C C   . TRP A 96  ? 0.4045 0.3694 0.3723 -0.0041 -0.0212 0.0564  96  TRP A C   
1457 O O   . TRP A 96  ? 0.4090 0.3673 0.3752 -0.0129 -0.0190 0.0634  96  TRP A O   
1458 C CB  A TRP A 96  ? 0.4139 0.3997 0.3674 -0.0061 -0.0017 0.0701  96  TRP A CB  
1459 C CB  B TRP A 96  ? 0.4141 0.3999 0.3679 -0.0058 -0.0020 0.0698  96  TRP A CB  
1460 C CG  A TRP A 96  ? 0.3965 0.4025 0.3327 -0.0094 0.0129  0.0713  96  TRP A CG  
1461 C CG  B TRP A 96  ? 0.4066 0.3967 0.3499 -0.0168 0.0106  0.0838  96  TRP A CG  
1462 C CD1 A TRP A 96  ? 0.4037 0.4257 0.3321 -0.0031 0.0163  0.0608  96  TRP A CD1 
1463 C CD1 B TRP A 96  ? 0.3936 0.3710 0.3415 -0.0250 0.0110  0.0974  96  TRP A CD1 
1464 C CD2 A TRP A 96  ? 0.3978 0.4094 0.3224 -0.0197 0.0252  0.0843  96  TRP A CD2 
1465 C CD2 B TRP A 96  ? 0.4008 0.4098 0.3269 -0.0207 0.0243  0.0853  96  TRP A CD2 
1466 N NE1 A TRP A 96  ? 0.3625 0.3994 0.2743 -0.0090 0.0297  0.0673  96  TRP A NE1 
1467 N NE1 B TRP A 96  ? 0.4024 0.3893 0.3377 -0.0337 0.0240  0.1070  96  TRP A NE1 
1468 C CE2 A TRP A 96  ? 0.3913 0.4221 0.3004 -0.0190 0.0350  0.0813  96  TRP A CE2 
1469 C CE2 B TRP A 96  ? 0.3974 0.4037 0.3186 -0.0313 0.0321  0.0998  96  TRP A CE2 
1470 C CE3 A TRP A 96  ? 0.3977 0.3996 0.3236 -0.0292 0.0283  0.0985  96  TRP A CE3 
1471 C CE3 B TRP A 96  ? 0.3898 0.4172 0.3041 -0.0164 0.0302  0.0764  96  TRP A CE3 
1472 C CZ2 A TRP A 96  ? 0.4065 0.4468 0.3009 -0.0273 0.0471  0.0917  96  TRP A CZ2 
1473 C CZ2 B TRP A 96  ? 0.4085 0.4296 0.3132 -0.0373 0.0447  0.1052  96  TRP A CZ2 
1474 C CZ3 A TRP A 96  ? 0.4118 0.4237 0.3240 -0.0374 0.0408  0.1081  96  TRP A CZ3 
1475 C CZ3 B TRP A 96  ? 0.4021 0.4441 0.2995 -0.0225 0.0427  0.0826  96  TRP A CZ3 
1476 C CH2 A TRP A 96  ? 0.4111 0.4419 0.3073 -0.0363 0.0497  0.1044  96  TRP A CH2 
1477 C CH2 B TRP A 96  ? 0.4068 0.4454 0.2992 -0.0328 0.0496  0.0967  96  TRP A CH2 
1496 N N   . SER A 97  ? 0.4019 0.3536 0.3838 0.0047  -0.0353 0.0533  97  SER A N   
1497 C CA  . SER A 97  ? 0.4142 0.3442 0.4088 0.0049  -0.0491 0.0565  97  SER A CA  
1498 C C   . SER A 97  ? 0.4307 0.3631 0.4192 0.0041  -0.0511 0.0411  97  SER A C   
1499 O O   . SER A 97  ? 0.4350 0.3523 0.4272 -0.0016 -0.0556 0.0476  97  SER A O   
1500 C CB  . SER A 97  ? 0.4807 0.3980 0.4902 0.0156  -0.0657 0.0526  97  SER A CB  
1501 O OG  . SER A 97  ? 0.5225 0.4343 0.5392 0.0148  -0.0656 0.0685  97  SER A OG  
1507 N N   . ARG A 98  ? 0.4360 0.3867 0.4155 0.0098  -0.0484 0.0208  98  ARG A N   
1508 C CA  A ARG A 98  ? 0.5006 0.4558 0.4732 0.0087  -0.0497 0.0048  98  ARG A CA  
1509 C CA  B ARG A 98  ? 0.5006 0.4558 0.4732 0.0087  -0.0497 0.0048  98  ARG A CA  
1510 C C   . ARG A 98  ? 0.4497 0.4090 0.4116 -0.0050 -0.0383 0.0127  98  ARG A C   
1511 O O   . ARG A 98  ? 0.4444 0.3926 0.4069 -0.0103 -0.0425 0.0116  98  ARG A O   
1512 C CB  A ARG A 98  ? 0.5556 0.5337 0.5195 0.0167  -0.0470 -0.0176 98  ARG A CB  
1513 C CB  B ARG A 98  ? 0.5556 0.5336 0.5196 0.0168  -0.0471 -0.0176 98  ARG A CB  
1514 C CG  A ARG A 98  ? 0.6280 0.6088 0.5875 0.0189  -0.0522 -0.0370 98  ARG A CG  
1515 C CG  B ARG A 98  ? 0.6278 0.6096 0.5868 0.0185  -0.0515 -0.0370 98  ARG A CG  
1516 C CD  A ARG A 98  ? 0.6848 0.6932 0.6331 0.0245  -0.0461 -0.0577 98  ARG A CD  
1517 C CD  B ARG A 98  ? 0.6857 0.6919 0.6371 0.0274  -0.0489 -0.0588 98  ARG A CD  
1518 N NE  A ARG A 98  ? 0.6839 0.7030 0.6346 0.0325  -0.0439 -0.0580 98  ARG A NE  
1519 N NE  B ARG A 98  ? 0.7023 0.7072 0.6639 0.0396  -0.0559 -0.0619 98  ARG A NE  
1520 C CZ  A ARG A 98  ? 0.6908 0.7007 0.6544 0.0441  -0.0554 -0.0624 98  ARG A CZ  
1521 C CZ  B ARG A 98  ? 0.6809 0.7029 0.6384 0.0428  -0.0482 -0.0627 98  ARG A CZ  
1522 N NH1 A ARG A 98  ? 0.7131 0.7027 0.6887 0.0499  -0.0709 -0.0662 98  ARG A NH1 
1523 N NH1 B ARG A 98  ? 0.6393 0.6832 0.5816 0.0362  -0.0336 -0.0623 98  ARG A NH1 
1524 N NH2 A ARG A 98  ? 0.6850 0.7056 0.6497 0.0499  -0.0523 -0.0628 98  ARG A NH2 
1525 N NH2 B ARG A 98  ? 0.6863 0.7027 0.6553 0.0528  -0.0563 -0.0636 98  ARG A NH2 
1550 N N   . VAL A 99  ? 0.4203 0.3952 0.3720 -0.0114 -0.0242 0.0209  99  VAL A N   
1551 C CA  . VAL A 99  ? 0.4281 0.4065 0.3702 -0.0248 -0.0140 0.0294  99  VAL A CA  
1552 C C   . VAL A 99  ? 0.4011 0.3547 0.3544 -0.0312 -0.0195 0.0464  99  VAL A C   
1553 O O   . VAL A 99  ? 0.3920 0.3389 0.3433 -0.0395 -0.0199 0.0463  99  VAL A O   
1554 C CB  . VAL A 99  ? 0.4402 0.4354 0.3715 -0.0294 0.0000  0.0389  99  VAL A CB  
1555 C CG1 . VAL A 99  ? 0.4537 0.4463 0.3796 -0.0431 0.0083  0.0531  99  VAL A CG1 
1556 C CG2 . VAL A 99  ? 0.4452 0.4669 0.3620 -0.0264 0.0066  0.0224  99  VAL A CG2 
1566 N N   . ASP A 100 ? 0.4251 0.3650 0.3903 -0.0283 -0.0236 0.0619  100 ASP A N   
1567 C CA  . ASP A 100 ? 0.4183 0.3358 0.3945 -0.0345 -0.0286 0.0800  100 ASP A CA  
1568 C C   . ASP A 100 ? 0.4560 0.3558 0.4390 -0.0334 -0.0417 0.0730  100 ASP A C   
1569 O O   . ASP A 100 ? 0.4948 0.3826 0.4791 -0.0425 -0.0418 0.0814  100 ASP A O   
1570 C CB  . ASP A 100 ? 0.4957 0.4023 0.4841 -0.0302 -0.0332 0.0958  100 ASP A CB  
1571 C CG  . ASP A 100 ? 0.6055 0.5243 0.5872 -0.0346 -0.0192 0.1083  100 ASP A CG  
1572 O OD1 . ASP A 100 ? 0.6558 0.5843 0.6267 -0.0437 -0.0072 0.1123  100 ASP A OD1 
1573 O OD2 . ASP A 100 ? 0.6584 0.5766 0.6455 -0.0291 -0.0209 0.1142  100 ASP A OD2 
1578 N N   . LYS A 101 ? 0.4308 0.3288 0.4176 -0.0224 -0.0529 0.0572  101 LYS A N   
1579 C CA  . LYS A 101 ? 0.5035 0.3835 0.4961 -0.0203 -0.0665 0.0503  101 LYS A CA  
1580 C C   . LYS A 101 ? 0.4818 0.3686 0.4623 -0.0285 -0.0604 0.0393  101 LYS A C   
1581 O O   . LYS A 101 ? 0.4579 0.3267 0.4416 -0.0342 -0.0664 0.0433  101 LYS A O   
1582 C CB  . LYS A 101 ? 0.5658 0.4437 0.5643 -0.0059 -0.0800 0.0345  101 LYS A CB  
1583 C CG  . LYS A 101 ? 0.7316 0.6276 0.7193 -0.0004 -0.0779 0.0092  101 LYS A CG  
1584 C CD  . LYS A 101 ? 0.7325 0.6237 0.7279 0.0146  -0.0931 -0.0064 101 LYS A CD  
1585 C CE  . LYS A 101 ? 0.7430 0.6573 0.7269 0.0202  -0.0884 -0.0314 101 LYS A CE  
1586 N NZ  . LYS A 101 ? 0.7988 0.7171 0.7890 0.0354  -0.0985 -0.0467 101 LYS A NZ  
1600 N N   . ILE A 102 ? 0.4238 0.3363 0.3904 -0.0294 -0.0492 0.0257  102 ILE A N   
1601 C CA  . ILE A 102 ? 0.4173 0.3394 0.3713 -0.0386 -0.0430 0.0150  102 ILE A CA  
1602 C C   . ILE A 102 ? 0.4636 0.3769 0.4168 -0.0533 -0.0365 0.0320  102 ILE A C   
1603 O O   . ILE A 102 ? 0.4599 0.3620 0.4118 -0.0613 -0.0395 0.0302  102 ILE A O   
1604 C CB  . ILE A 102 ? 0.4077 0.3610 0.3470 -0.0374 -0.0320 0.0003  102 ILE A CB  
1605 C CG1 . ILE A 102 ? 0.4308 0.3927 0.3709 -0.0232 -0.0392 -0.0198 102 ILE A CG1 
1606 C CG2 . ILE A 102 ? 0.4162 0.3809 0.3420 -0.0501 -0.0243 -0.0065 102 ILE A CG2 
1607 C CD1 . ILE A 102 ? 0.4484 0.4407 0.3766 -0.0197 -0.0292 -0.0314 102 ILE A CD1 
1619 N N   . ILE A 103 ? 0.4163 0.3343 0.3698 -0.0573 -0.0276 0.0483  103 ILE A N   
1620 C CA  . ILE A 103 ? 0.4425 0.3543 0.3954 -0.0708 -0.0206 0.0645  103 ILE A CA  
1621 C C   . ILE A 103 ? 0.5103 0.3927 0.4769 -0.0736 -0.0311 0.0771  103 ILE A C   
1622 O O   . ILE A 103 ? 0.5563 0.4292 0.5219 -0.0846 -0.0304 0.0809  103 ILE A O   
1623 C CB  . ILE A 103 ? 0.4689 0.3911 0.4201 -0.0722 -0.0098 0.0794  103 ILE A CB  
1624 C CG1 . ILE A 103 ? 0.4706 0.4216 0.4059 -0.0710 0.0006  0.0672  103 ILE A CG1 
1625 C CG2 . ILE A 103 ? 0.5054 0.4193 0.4582 -0.0849 -0.0036 0.0974  103 ILE A CG2 
1626 C CD1 . ILE A 103 ? 0.4639 0.4289 0.3851 -0.0828 0.0081  0.0599  103 ILE A CD1 
1638 N N   . GLU A 104 ? 0.5154 0.3824 0.4949 -0.0640 -0.0422 0.0830  104 GLU A N   
1639 C CA  . GLU A 104 ? 0.5678 0.4067 0.5600 -0.0665 -0.0534 0.0961  104 GLU A CA  
1640 C C   . GLU A 104 ? 0.6239 0.4510 0.6136 -0.0683 -0.0619 0.0831  104 GLU A C   
1641 O O   . GLU A 104 ? 0.6502 0.4591 0.6436 -0.0775 -0.0648 0.0927  104 GLU A O   
1642 C CB  . GLU A 104 ? 0.6150 0.4409 0.6208 -0.0558 -0.0653 0.1044  104 GLU A CB  
1643 C CG  . GLU A 104 ? 0.7761 0.5730 0.7950 -0.0579 -0.0784 0.1191  104 GLU A CG  
1644 C CD  . GLU A 104 ? 1.0565 0.8431 1.0891 -0.0512 -0.0874 0.1340  104 GLU A CD  
1645 O OE1 . GLU A 104 ? 1.1765 0.9697 1.2114 -0.0552 -0.0785 0.1494  104 GLU A OE1 
1646 O OE2 . GLU A 104 ? 1.0279 0.8003 1.0685 -0.0420 -0.1038 0.1301  104 GLU A OE2 
1653 N N   . ASN A 105 ? 0.5169 0.3539 0.5002 -0.0601 -0.0658 0.0614  105 ASN A N   
1654 C CA  . ASN A 105 ? 0.5729 0.3992 0.5525 -0.0619 -0.0733 0.0482  105 ASN A CA  
1655 C C   . ASN A 105 ? 0.5890 0.4221 0.5579 -0.0773 -0.0630 0.0462  105 ASN A C   
1656 O O   . ASN A 105 ? 0.6919 0.5064 0.6618 -0.0847 -0.0687 0.0473  105 ASN A O   
1657 C CB  . ASN A 105 ? 0.5223 0.3610 0.4968 -0.0495 -0.0785 0.0246  105 ASN A CB  
1658 C CG  . ASN A 105 ? 0.5368 0.3599 0.5237 -0.0353 -0.0942 0.0253  105 ASN A CG  
1659 O OD1 . ASN A 105 ? 0.6178 0.4157 0.6163 -0.0358 -0.1046 0.0413  105 ASN A OD1 
1660 N ND2 . ASN A 105 ? 0.5312 0.3687 0.5162 -0.0230 -0.0968 0.0084  105 ASN A ND2 
1667 N N   . LEU A 106 ? 0.5220 0.3807 0.4805 -0.0826 -0.0487 0.0438  106 LEU A N   
1668 C CA  . LEU A 106 ? 0.5382 0.4053 0.4860 -0.0976 -0.0398 0.0412  106 LEU A CA  
1669 C C   . LEU A 106 ? 0.5626 0.4106 0.5174 -0.1102 -0.0385 0.0615  106 LEU A C   
1670 O O   . LEU A 106 ? 0.6365 0.4830 0.5854 -0.1233 -0.0356 0.0592  106 LEU A O   
1671 C CB  . LEU A 106 ? 0.5168 0.4155 0.4519 -0.0998 -0.0261 0.0359  106 LEU A CB  
1672 C CG  . LEU A 106 ? 0.4616 0.3831 0.3867 -0.0907 -0.0254 0.0136  106 LEU A CG  
1673 C CD1 . LEU A 106 ? 0.4861 0.4364 0.4006 -0.0907 -0.0131 0.0126  106 LEU A CD1 
1674 C CD2 . LEU A 106 ? 0.4504 0.3747 0.3665 -0.0971 -0.0281 -0.0040 106 LEU A CD2 
1686 N N   . GLU A 107 ? 0.7101 0.5439 0.6776 -0.1071 -0.0411 0.0810  107 GLU A N   
1687 C CA  . GLU A 107 ? 0.7348 0.5558 0.7105 -0.1160 -0.0381 0.0995  107 GLU A CA  
1688 C C   . GLU A 107 ? 0.7413 0.5448 0.7290 -0.1088 -0.0471 0.0994  107 GLU A C   
1689 O O   . GLU A 107 ? 0.7753 0.5565 0.7654 -0.1059 -0.0628 0.0979  107 GLU A O   
1690 C CB  . GLU A 107 ? 0.7098 0.5436 0.6933 -0.1066 -0.0295 0.1109  107 GLU A CB  
1691 C CG  . GLU A 107 ? 0.6668 0.5235 0.6391 -0.1105 -0.0175 0.1113  107 GLU A CG  
1692 C CD  . GLU A 107 ? 0.8636 0.7411 0.8341 -0.1101 -0.0035 0.1038  107 GLU A CD  
1693 O OE1 . GLU A 107 ? 0.9303 0.8037 0.9080 -0.1080 -0.0029 0.0993  107 GLU A OE1 
1694 O OE2 . GLU A 107 ? 0.7769 0.6743 0.7396 -0.1100 0.0058  0.1020  107 GLU A OE2 
# 
