data_9EZK
# 
_entry.id   9EZK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EZK         pdb_00009ezk 10.2210/pdb9ezk/pdb 
WWPDB D_1292137902 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-12-04 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EZK 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-12 
_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              gideon.grogan@york.ac.uk 
_pdbx_contact_author.name_first         Gideon 
_pdbx_contact_author.name_last          Grogan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1383-7056 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ascham, A.'    1 ?                   
'Salihovic, A.' 2 ?                   
'Burley, G.'    3 0000-0002-4896-113X 
'Grogan, G.'    4 0000-0003-1383-7056 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Chem Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-6520 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                15399 
_citation.page_last                 15407 
_citation.title                     
;Gram-scale enzymatic synthesis of 2'-deoxyribonucleoside analogues using nucleoside transglycosylase-2.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1039/d4sc04938a 
_citation.pdbx_database_id_PubMed   39234214 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Salihovic, A.'       1 0009-0004-4710-0145 
primary 'Ascham, A.'          2 0000-0002-1930-4667 
primary 'Taladriz-Sender, A.' 3 0000-0002-8274-4761 
primary 'Bryson, S.'          4 ?                   
primary 'Withers, J.M.'       5 ?                   
primary 'McKean, I.J.W.'      6 ?                   
primary 'Hoskisson, P.A.'     7 0000-0003-4332-1640 
primary 'Grogan, G.'          8 0000-0003-1383-7056 
primary 'Burley, G.A.'        9 0000-0002-4896-113X 
# 
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 'Nucleoside deoxyribosyltransferase' 18098.354 2  ? ? ? ? 
2 water   nat water                                18.015    10 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MPKKTIYFGAGWFTDRQNKAYKEAMEALKENPTIDLENSYVPLDNQYKGIRVDEHPEYLHDKVWATATYNNDLNGIKTND
IMLGVYIPDEEDVGLGMELGYALSQGKYVLLVIPDEDYGKPINLMSWGVSDNVIKMSQLKDFNFNKPRFDFYEGAVY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPKKTIYFGAGWFTDRQNKAYKEAMEALKENPTIDLENSYVPLDNQYKGIRVDEHPEYLHDKVWATATYNNDLNGIKTND
IMLGVYIPDEEDVGLGMELGYALSQGKYVLLVIPDEDYGKPINLMSWGVSDNVIKMSQLKDFNFNKPRFDFYEGAVY
;
_entity_poly.pdbx_strand_id                 A,B 
_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   MET n 
1 2   PRO n 
1 3   LYS n 
1 4   LYS n 
1 5   THR n 
1 6   ILE n 
1 7   TYR n 
1 8   PHE n 
1 9   GLY n 
1 10  ALA n 
1 11  GLY n 
1 12  TRP n 
1 13  PHE n 
1 14  THR n 
1 15  ASP n 
1 16  ARG n 
1 17  GLN n 
1 18  ASN n 
1 19  LYS n 
1 20  ALA n 
1 21  TYR n 
1 22  LYS n 
1 23  GLU n 
1 24  ALA n 
1 25  MET n 
1 26  GLU n 
1 27  ALA n 
1 28  LEU n 
1 29  LYS n 
1 30  GLU n 
1 31  ASN n 
1 32  PRO n 
1 33  THR n 
1 34  ILE n 
1 35  ASP n 
1 36  LEU n 
1 37  GLU n 
1 38  ASN n 
1 39  SER n 
1 40  TYR n 
1 41  VAL n 
1 42  PRO n 
1 43  LEU n 
1 44  ASP n 
1 45  ASN n 
1 46  GLN n 
1 47  TYR n 
1 48  LYS n 
1 49  GLY n 
1 50  ILE n 
1 51  ARG n 
1 52  VAL n 
1 53  ASP n 
1 54  GLU n 
1 55  HIS n 
1 56  PRO n 
1 57  GLU n 
1 58  TYR n 
1 59  LEU n 
1 60  HIS n 
1 61  ASP n 
1 62  LYS n 
1 63  VAL n 
1 64  TRP n 
1 65  ALA n 
1 66  THR n 
1 67  ALA n 
1 68  THR n 
1 69  TYR n 
1 70  ASN n 
1 71  ASN n 
1 72  ASP n 
1 73  LEU n 
1 74  ASN n 
1 75  GLY n 
1 76  ILE n 
1 77  LYS n 
1 78  THR n 
1 79  ASN n 
1 80  ASP n 
1 81  ILE n 
1 82  MET n 
1 83  LEU n 
1 84  GLY n 
1 85  VAL n 
1 86  TYR n 
1 87  ILE n 
1 88  PRO n 
1 89  ASP n 
1 90  GLU n 
1 91  GLU n 
1 92  ASP n 
1 93  VAL n 
1 94  GLY n 
1 95  LEU n 
1 96  GLY n 
1 97  MET n 
1 98  GLU n 
1 99  LEU n 
1 100 GLY n 
1 101 TYR n 
1 102 ALA n 
1 103 LEU n 
1 104 SER n 
1 105 GLN n 
1 106 GLY n 
1 107 LYS n 
1 108 TYR n 
1 109 VAL n 
1 110 LEU n 
1 111 LEU n 
1 112 VAL n 
1 113 ILE n 
1 114 PRO n 
1 115 ASP n 
1 116 GLU n 
1 117 ASP n 
1 118 TYR n 
1 119 GLY n 
1 120 LYS n 
1 121 PRO n 
1 122 ILE n 
1 123 ASN n 
1 124 LEU n 
1 125 MET n 
1 126 SER n 
1 127 TRP n 
1 128 GLY n 
1 129 VAL n 
1 130 SER n 
1 131 ASP n 
1 132 ASN n 
1 133 VAL n 
1 134 ILE n 
1 135 LYS n 
1 136 MET n 
1 137 SER n 
1 138 GLN n 
1 139 LEU n 
1 140 LYS n 
1 141 ASP n 
1 142 PHE n 
1 143 ASN n 
1 144 PHE n 
1 145 ASN n 
1 146 LYS n 
1 147 PRO n 
1 148 ARG n 
1 149 PHE n 
1 150 ASP n 
1 151 PHE n 
1 152 TYR n 
1 153 GLU n 
1 154 GLY n 
1 155 ALA n 
1 156 VAL n 
1 157 TYR 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                   157 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ntd 
_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      'Lactobacillus leichmannii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     28039 
_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 
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   MET 1   1   1   MET MET A . n 
A 1 2   PRO 2   2   2   PRO PRO A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  TRP 12  12  12  TRP TRP A . n 
A 1 13  PHE 13  13  13  PHE PHE A . n 
A 1 14  THR 14  14  14  THR THR A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  MET 25  25  25  MET MET A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  GLN 46  46  46  GLN GLN A . n 
A 1 47  TYR 47  47  47  TYR TYR A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  ARG 51  51  51  ARG ARG A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  HIS 55  55  55  HIS HIS A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  TYR 58  58  58  TYR TYR A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  HIS 60  60  60  HIS HIS A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  TRP 64  64  64  TRP TRP A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  THR 78  78  78  THR THR A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ILE 81  81  81  ILE ILE A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  PRO 88  88  88  PRO PRO A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  MET 97  97  97  MET MET A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 GLN 105 105 105 GLN GLN A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 PRO 114 114 114 PRO PRO A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ASP 117 117 117 ASP ASP A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 ASN 123 123 123 ASN ASN A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 MET 125 125 125 MET MET A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 TRP 127 127 127 TRP TRP A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 ASN 132 132 132 ASN ASN A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 SER 137 137 137 SER SER A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 ASN 143 143 143 ASN ASN A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 ASN 145 145 145 ASN ASN A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   2   PRO PRO B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   LYS 4   4   4   LYS LYS B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   TYR 7   7   7   TYR TYR B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  ALA 10  10  10  ALA ALA B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  TRP 12  12  12  TRP TRP B . n 
B 1 13  PHE 13  13  13  PHE PHE B . n 
B 1 14  THR 14  14  14  THR THR B . n 
B 1 15  ASP 15  15  15  ASP ASP B . n 
B 1 16  ARG 16  16  16  ARG ARG B . n 
B 1 17  GLN 17  17  17  GLN GLN B . n 
B 1 18  ASN 18  18  18  ASN ASN B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  LYS 22  22  22  LYS LYS B . n 
B 1 23  GLU 23  23  23  GLU GLU B . n 
B 1 24  ALA 24  24  24  ALA ALA B . n 
B 1 25  MET 25  25  25  MET MET B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LEU 28  28  28  LEU LEU B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  GLU 30  30  30  GLU GLU B . n 
B 1 31  ASN 31  31  31  ASN ASN B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  ILE 34  34  34  ILE ILE B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  ASN 38  38  38  ASN ASN B . n 
B 1 39  SER 39  39  39  SER SER B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  ASP 44  44  44  ASP ASP B . n 
B 1 45  ASN 45  45  45  ASN ASN B . n 
B 1 46  GLN 46  46  46  GLN GLN B . n 
B 1 47  TYR 47  47  47  TYR TYR B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  GLY 49  49  49  GLY GLY B . n 
B 1 50  ILE 50  50  50  ILE ILE B . n 
B 1 51  ARG 51  51  51  ARG ARG B . n 
B 1 52  VAL 52  52  52  VAL VAL B . n 
B 1 53  ASP 53  53  53  ASP ASP B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  HIS 55  55  55  HIS HIS B . n 
B 1 56  PRO 56  56  56  PRO PRO B . n 
B 1 57  GLU 57  57  57  GLU GLU B . n 
B 1 58  TYR 58  58  58  TYR TYR B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  HIS 60  60  60  HIS HIS B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  LYS 62  62  62  LYS LYS B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  TRP 64  64  64  TRP TRP B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  THR 66  66  66  THR THR B . n 
B 1 67  ALA 67  67  67  ALA ALA B . n 
B 1 68  THR 68  68  68  THR THR B . n 
B 1 69  TYR 69  69  69  TYR TYR B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  LEU 73  73  73  LEU LEU B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  THR 78  78  78  THR THR B . n 
B 1 79  ASN 79  79  79  ASN ASN B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  ILE 81  81  81  ILE ILE B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  TYR 86  86  86  TYR TYR B . n 
B 1 87  ILE 87  87  87  ILE ILE B . n 
B 1 88  PRO 88  88  88  PRO PRO B . n 
B 1 89  ASP 89  89  89  ASP ASP B . n 
B 1 90  GLU 90  90  90  GLU GLU B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  GLY 94  94  94  GLY GLY B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  GLY 96  96  96  GLY GLY B . n 
B 1 97  MET 97  97  97  MET MET B . n 
B 1 98  GLU 98  98  98  GLU GLU B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 SER 104 104 104 SER SER B . n 
B 1 105 GLN 105 105 105 GLN GLN B . n 
B 1 106 GLY 106 106 106 GLY GLY B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 TYR 108 108 108 TYR TYR B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 PRO 114 114 114 PRO PRO B . n 
B 1 115 ASP 115 115 115 ASP ASP B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 ASP 117 117 117 ASP ASP B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 GLY 119 119 119 GLY GLY B . n 
B 1 120 LYS 120 120 120 LYS LYS B . n 
B 1 121 PRO 121 121 121 PRO PRO B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 ASN 123 123 123 ASN ASN B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 MET 125 125 125 MET MET B . n 
B 1 126 SER 126 126 126 SER SER B . n 
B 1 127 TRP 127 127 127 TRP TRP B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 VAL 129 129 129 VAL VAL B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 ASP 131 131 131 ASP ASP B . n 
B 1 132 ASN 132 132 132 ASN ASN B . n 
B 1 133 VAL 133 133 133 VAL VAL B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 MET 136 136 136 MET MET B . n 
B 1 137 SER 137 137 137 SER SER B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 LYS 140 140 140 LYS LYS B . n 
B 1 141 ASP 141 141 141 ASP ASP B . n 
B 1 142 PHE 142 142 142 PHE PHE B . n 
B 1 143 ASN 143 143 143 ASN ASN B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 ASN 145 145 145 ASN ASN B . n 
B 1 146 LYS 146 146 146 LYS LYS B . n 
B 1 147 PRO 147 147 147 PRO PRO B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 PHE 149 149 149 PHE PHE B . n 
B 1 150 ASP 150 150 150 ASP ASP B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 GLU 153 153 153 GLU GLU B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 ALA 155 155 155 ALA ALA B . n 
B 1 156 VAL 156 156 156 VAL VAL B . n 
B 1 157 TYR 157 157 157 TYR TYR B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1 201 3  HOH HOH A . 
C 2 HOH 2 202 1  HOH HOH A . 
C 2 HOH 3 203 7  HOH HOH A . 
C 2 HOH 4 204 4  HOH HOH A . 
C 2 HOH 5 205 8  HOH HOH A . 
C 2 HOH 6 206 2  HOH HOH A . 
C 2 HOH 7 207 6  HOH HOH A . 
D 2 HOH 1 201 11 HOH HOH B . 
D 2 HOH 2 202 10 HOH HOH B . 
D 2 HOH 3 203 5  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 22  ? CG  ? A LYS 22  CG  
2  1 Y 1 A LYS 22  ? CD  ? A LYS 22  CD  
3  1 Y 1 A LYS 22  ? CE  ? A LYS 22  CE  
4  1 Y 1 A LYS 22  ? NZ  ? A LYS 22  NZ  
5  1 Y 1 A LYS 29  ? CE  ? A LYS 29  CE  
6  1 Y 1 A LYS 29  ? NZ  ? A LYS 29  NZ  
7  1 Y 1 A GLU 30  ? OE1 ? A GLU 30  OE1 
8  1 Y 1 A GLU 30  ? OE2 ? A GLU 30  OE2 
9  1 Y 1 A GLU 37  ? OE1 ? A GLU 37  OE1 
10 1 Y 1 A GLU 37  ? OE2 ? A GLU 37  OE2 
11 1 Y 1 A LYS 135 ? CE  ? A LYS 135 CE  
12 1 Y 1 A LYS 135 ? NZ  ? A LYS 135 NZ  
13 1 Y 1 B LYS 3   ? CD  ? B LYS 3   CD  
14 1 Y 1 B LYS 3   ? CE  ? B LYS 3   CE  
15 1 Y 1 B LYS 3   ? NZ  ? B LYS 3   NZ  
16 1 Y 1 B LYS 4   ? CE  ? B LYS 4   CE  
17 1 Y 1 B LYS 4   ? NZ  ? B LYS 4   NZ  
18 1 Y 1 B LYS 19  ? CD  ? B LYS 19  CD  
19 1 Y 1 B LYS 19  ? CE  ? B LYS 19  CE  
20 1 Y 1 B LYS 19  ? NZ  ? B LYS 19  NZ  
21 1 Y 1 B LYS 29  ? CG  ? B LYS 29  CG  
22 1 Y 1 B LYS 29  ? CD  ? B LYS 29  CD  
23 1 Y 1 B LYS 29  ? CE  ? B LYS 29  CE  
24 1 Y 1 B LYS 29  ? NZ  ? B LYS 29  NZ  
25 1 Y 1 B GLU 30  ? CG  ? B GLU 30  CG  
26 1 Y 1 B GLU 30  ? CD  ? B GLU 30  CD  
27 1 Y 1 B GLU 30  ? OE1 ? B GLU 30  OE1 
28 1 Y 1 B GLU 30  ? OE2 ? B GLU 30  OE2 
29 1 Y 1 B ARG 51  ? CG  ? B ARG 51  CG  
30 1 Y 1 B ARG 51  ? CD  ? B ARG 51  CD  
31 1 Y 1 B ARG 51  ? NE  ? B ARG 51  NE  
32 1 Y 1 B ARG 51  ? CZ  ? B ARG 51  CZ  
33 1 Y 1 B ARG 51  ? NH1 ? B ARG 51  NH1 
34 1 Y 1 B ARG 51  ? NH2 ? B ARG 51  NH2 
35 1 Y 1 B LYS 135 ? CE  ? B LYS 135 CE  
36 1 Y 1 B LYS 135 ? NZ  ? B LYS 135 NZ  
37 1 Y 1 B LYS 140 ? CG  ? B LYS 140 CG  
38 1 Y 1 B LYS 140 ? CD  ? B LYS 140 CD  
39 1 Y 1 B LYS 140 ? CE  ? B LYS 140 CE  
40 1 Y 1 B LYS 140 ? NZ  ? B LYS 140 NZ  
41 1 Y 1 B GLU 153 ? CG  ? B GLU 153 CG  
42 1 Y 1 B GLU 153 ? CD  ? B GLU 153 CD  
43 1 Y 1 B GLU 153 ? OE1 ? B GLU 153 OE1 
44 1 Y 1 B GLU 153 ? OE2 ? B GLU 153 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EZK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     149.270 
_cell.length_a_esd                 ? 
_cell.length_b                     149.270 
_cell.length_b_esd                 ? 
_cell.length_c                     149.270 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_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                         9EZK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                199 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 21 3' 
_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                   9EZK 
_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             3.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          67.87 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_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    '20 mM NaH2PO4 buffer; 0.2M sodium citrate; 20% (w/v) PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     120 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-20 
_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   0.976277 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976277 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          75 
_reflns.entry_id                                       9EZK 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.79 
_reflns.d_resolution_low                               60.94 
_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                                     13954 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                40.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.03 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.00 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.15 
_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                                    2.79 
_reflns_shell.d_res_low                                     2.94 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2028 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.49 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.82 
_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                                  2.20 
_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]                            0.000 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.000 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               77.264 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.937 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_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                                 9EZK 
_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                            2.790 
_refine.ls_d_res_low                             52.831 
_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                     13951 
_refine.ls_number_reflns_R_free                  723 
_refine.ls_number_reflns_R_work                  13228 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.971 
_refine.ls_percent_reflns_R_free                 5.182 
_refine.ls_R_factor_all                          0.175 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2374 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1717 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'MASK BULK SOLVENT' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.433 
_refine.pdbx_overall_ESU_R_Free                  0.294 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             12.347 
_refine.overall_SU_ML                            0.230 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.790 
_refine_hist.d_res_low                        52.831 
_refine_hist.number_atoms_solvent             10 
_refine_hist.number_atoms_total               2510 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2500 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  0.012  2566 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  2308 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.838  1.818  3490 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 0.635  1.752  5322 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 6.382  5.000  311  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 10.252 5.000  5    ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 17.396 10.000 400  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 13.954 10.000 129  ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.087  0.200  365  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.038  0.200  1    ? r_chiral_restr_other           ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  3027 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  585  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.216  0.200  484  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.202  0.200  2052 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.192  0.200  1235 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.084  0.200  1274 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.161  0.200  52   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.098  0.200  12   ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.251  0.200  65   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.043  0.200  1    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 6.963  7.742  1250 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 6.963  7.742  1250 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 8.882  13.947 1559 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 8.882  13.947 1560 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 8.388  8.199  1316 ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 8.388  8.199  1316 ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 10.688 14.913 1931 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 10.686 14.911 1932 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 11.357 74.717 2792 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 11.355 74.728 2793 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.080  0.050  4953 ? r_ncsr_local_group_1           ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.07976 ? 0.05009 1 'Local ncs' ? A ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.07976 ? 0.05009 2 'Local ncs' ? A ? ? ? 1 
# 
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' 2.790  2.862  1026 . 54 972 100.0000 . 0.271 . . 0.262 . . . . . 0.239 . 20 . 0.957 0.900 0.439 
'X-RAY DIFFRACTION' 2.862  2.941  993  . 41 952 100.0000 . 0.286 . . 0.282 . . . . . 0.254 . 20 . 0.954 0.909 0.385 
'X-RAY DIFFRACTION' 2.941  3.026  971  . 45 926 100.0000 . 0.268 . . 0.264 . . . . . 0.235 . 20 . 0.958 0.941 0.330 
'X-RAY DIFFRACTION' 3.026  3.118  936  . 53 883 100.0000 . 0.256 . . 0.253 . . . . . 0.220 . 20 . 0.958 0.941 0.300 
'X-RAY DIFFRACTION' 3.118  3.220  906  . 30 876 100.0000 . 0.260 . . 0.254 . . . . . 0.223 . 20 . 0.961 0.913 0.405 
'X-RAY DIFFRACTION' 3.220  3.333  885  . 53 832 100.0000 . 0.225 . . 0.220 . . . . . 0.194 . 20 . 0.969 0.946 0.297 
'X-RAY DIFFRACTION' 3.333  3.458  833  . 52 781 100.0000 . 0.200 . . 0.198 . . . . . 0.171 . 20 . 0.979 0.966 0.240 
'X-RAY DIFFRACTION' 3.458  3.599  820  . 54 765 99.8781  . 0.168 . . 0.164 . . . . . 0.142 . 20 . 0.984 0.971 0.223 
'X-RAY DIFFRACTION' 3.599  3.758  792  . 32 760 100.0000 . 0.165 . . 0.163 . . . . . 0.142 . 20 . 0.984 0.975 0.226 
'X-RAY DIFFRACTION' 3.758  3.940  751  . 30 721 100.0000 . 0.164 . . 0.160 . . . . . 0.141 . 20 . 0.983 0.966 0.241 
'X-RAY DIFFRACTION' 3.940  4.152  725  . 47 678 100.0000 . 0.143 . . 0.140 . . . . . 0.123 . 20 . 0.988 0.981 0.186 
'X-RAY DIFFRACTION' 4.152  4.403  691  . 32 659 100.0000 . 0.121 . . 0.118 . . . . . 0.109 . 20 . 0.991 0.986 0.168 
'X-RAY DIFFRACTION' 4.403  4.704  626  . 31 595 100.0000 . 0.112 . . 0.108 . . . . . 0.103 . 20 . 0.993 0.988 0.178 
'X-RAY DIFFRACTION' 4.704  5.078  609  . 26 583 100.0000 . 0.141 . . 0.139 . . . . . 0.135 . 20 . 0.990 0.974 0.193 
'X-RAY DIFFRACTION' 5.078  5.557  556  . 31 525 100.0000 . 0.143 . . 0.137 . . . . . 0.133 . 20 . 0.990 0.972 0.265 
'X-RAY DIFFRACTION' 5.557  6.205  503  . 36 467 100.0000 . 0.151 . . 0.147 . . . . . 0.143 . 20 . 0.987 0.979 0.201 
'X-RAY DIFFRACTION' 6.205  7.148  443  . 22 421 100.0000 . 0.165 . . 0.161 . . . . . 0.159 . 20 . 0.984 0.946 0.275 
'X-RAY DIFFRACTION' 7.148  8.715  390  . 23 367 100.0000 . 0.166 . . 0.161 . . . . . 0.165 . 20 . 0.983 0.964 0.247 
'X-RAY DIFFRACTION' 8.715  12.160 302  . 20 282 100.0000 . 0.178 . . 0.174 . . . . . 0.188 . 20 . 0.987 0.977 0.230 
'X-RAY DIFFRACTION' 12.160 52.831 194  . 11 183 100.0000 . 0.269 . . 0.273 . . . . . 0.290 . 20 . 0.961 0.976 0.223 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 A 
2 1 A 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1 1 A PRO 2 . A VAL 156 . A PRO 2 A VAL 156 ? ? 
1 2 1 A PRO 2 . A VAL 156 . A PRO 2 A VAL 156 ? ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   'Local NCS retraints between domains:       1       2' 
# 
_struct.entry_id                     9EZK 
_struct.title                        
;Nucleoside-2'-deoxyribosyltransferase from Lactobacillus leichmannii (apo).
;
_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        9EZK 
_struct_keywords.text            
;Nucleoside-2'-deoxyribosyltransferase, TRANSFERASE
;
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NTD_LACLE 
_struct_ref.pdbx_db_accession          Q9R5V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPKKTIYFGAGWFTDRQNKAYKEAMEALKENPTIDLENSYVPLDNQYKGIRVDEHPEYLHDKVWATATYNNDLNGIKTND
IMLGVYIPDEEDVGLGMELGYALSQGKYVLLVIPDEDYGKPINLMSWGVSDNVIKMSQLKDFNFNKPRFDFYEGAVY
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EZK A 1 ? 157 ? Q9R5V5 1 ? 157 ? 1 157 
2 1 9EZK B 1 ? 157 ? Q9R5V5 1 ? 157 ? 1 157 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
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)' 17080 ? 
1 MORE         -127  ? 
1 'SSA (A^2)'  33270 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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' 5_555 z,x,y 0.0000000000 0.0000000000 1.0000000000 0.0000000000 1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 
3 'crystal symmetry operation' 9_555 y,z,x 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 
1.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 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 THR A 14  ? GLU A 30  ? THR A 14  GLU A 30  1 ? 17 
HELX_P HELX_P2  AA2 ASP A 35  ? SER A 39  ? ASP A 35  SER A 39  5 ? 5  
HELX_P HELX_P3  AA3 VAL A 41  ? ILE A 50  ? VAL A 41  ILE A 50  5 ? 10 
HELX_P HELX_P4  AA4 HIS A 55  ? HIS A 60  ? HIS A 55  HIS A 60  5 ? 6  
HELX_P HELX_P5  AA5 ASP A 61  ? THR A 78  ? ASP A 61  THR A 78  1 ? 18 
HELX_P HELX_P6  AA6 ASP A 92  ? GLN A 105 ? ASP A 92  GLN A 105 1 ? 14 
HELX_P HELX_P7  AA7 ASN A 123 ? SER A 130 ? ASN A 123 SER A 130 1 ? 8  
HELX_P HELX_P8  AA8 SER A 137 ? PHE A 142 ? SER A 137 PHE A 142 5 ? 6  
HELX_P HELX_P9  AA9 THR B 14  ? GLU B 30  ? THR B 14  GLU B 30  1 ? 17 
HELX_P HELX_P10 AB1 ASP B 35  ? SER B 39  ? ASP B 35  SER B 39  5 ? 5  
HELX_P HELX_P11 AB2 VAL B 41  ? ILE B 50  ? VAL B 41  ILE B 50  5 ? 10 
HELX_P HELX_P12 AB3 HIS B 55  ? HIS B 60  ? HIS B 55  HIS B 60  5 ? 6  
HELX_P HELX_P13 AB4 ASP B 61  ? THR B 78  ? ASP B 61  THR B 78  1 ? 18 
HELX_P HELX_P14 AB5 ASP B 92  ? GLN B 105 ? ASP B 92  GLN B 105 1 ? 14 
HELX_P HELX_P15 AB6 ASN B 123 ? SER B 130 ? ASN B 123 SER B 130 1 ? 8  
HELX_P HELX_P16 AB7 SER B 137 ? PHE B 142 ? SER B 137 PHE B 142 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
# 
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 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? 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 ILE A 6   ? GLY A 9   ? ILE A 6   GLY A 9   
AA1 2 ILE A 81  ? VAL A 85  ? ILE A 81  VAL A 85  
AA1 3 TYR A 108 ? ILE A 113 ? TYR A 108 ILE A 113 
AA1 4 ASN A 132 ? LYS A 135 ? ASN A 132 LYS A 135 
AA2 1 ILE B 6   ? GLY B 9   ? ILE B 6   GLY B 9   
AA2 2 ILE B 81  ? VAL B 85  ? ILE B 81  VAL B 85  
AA2 3 TYR B 108 ? ILE B 113 ? TYR B 108 ILE B 113 
AA2 4 ASN B 132 ? LYS B 135 ? ASN B 132 LYS B 135 
# 
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 GLY A 9   ? N GLY A 9   O VAL A 85  ? O VAL A 85  
AA1 2 3 N GLY A 84  ? N GLY A 84  O LEU A 110 ? O LEU A 110 
AA1 3 4 N LEU A 111 ? N LEU A 111 O ILE A 134 ? O ILE A 134 
AA2 1 2 N GLY B 9   ? N GLY B 9   O VAL B 85  ? O VAL B 85  
AA2 2 3 N MET B 82  ? N MET B 82  O LEU B 110 ? O LEU B 110 
AA2 3 4 N LEU B 111 ? N LEU B 111 O ILE B 134 ? O ILE B 134 
# 
_pdbx_entry_details.entry_id                   9EZK 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 56  ? ? -59.98  -5.29 
2 1 GLU B 153 ? ? -100.21 72.63 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     16 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.095 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     MET 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    MET 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
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  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
THR N    N N N 290 
THR CA   C N S 291 
THR C    C N N 292 
THR O    O N N 293 
THR CB   C N R 294 
THR OG1  O N N 295 
THR CG2  C N N 296 
THR OXT  O N N 297 
THR H    H N N 298 
THR H2   H N N 299 
THR HA   H N N 300 
THR HB   H N N 301 
THR HG1  H N N 302 
THR HG21 H N N 303 
THR HG22 H N N 304 
THR HG23 H N N 305 
THR HXT  H N N 306 
TRP N    N N N 307 
TRP CA   C N S 308 
TRP C    C N N 309 
TRP O    O N N 310 
TRP CB   C N N 311 
TRP CG   C Y N 312 
TRP CD1  C Y N 313 
TRP CD2  C Y N 314 
TRP NE1  N Y N 315 
TRP CE2  C Y N 316 
TRP CE3  C Y N 317 
TRP CZ2  C Y N 318 
TRP CZ3  C Y N 319 
TRP CH2  C Y N 320 
TRP OXT  O N N 321 
TRP H    H N N 322 
TRP H2   H N N 323 
TRP HA   H N N 324 
TRP HB2  H N N 325 
TRP HB3  H N N 326 
TRP HD1  H N N 327 
TRP HE1  H N N 328 
TRP HE3  H N N 329 
TRP HZ2  H N N 330 
TRP HZ3  H N N 331 
TRP HH2  H N N 332 
TRP HXT  H N N 333 
TYR N    N N N 334 
TYR CA   C N S 335 
TYR C    C N N 336 
TYR O    O N N 337 
TYR CB   C N N 338 
TYR CG   C Y N 339 
TYR CD1  C Y N 340 
TYR CD2  C Y N 341 
TYR CE1  C Y N 342 
TYR CE2  C Y N 343 
TYR CZ   C Y N 344 
TYR OH   O N N 345 
TYR OXT  O N N 346 
TYR H    H N N 347 
TYR H2   H N N 348 
TYR HA   H N N 349 
TYR HB2  H N N 350 
TYR HB3  H N N 351 
TYR HD1  H N N 352 
TYR HD2  H N N 353 
TYR HE1  H N N 354 
TYR HE2  H N N 355 
TYR HH   H N N 356 
TYR HXT  H N N 357 
VAL N    N N N 358 
VAL CA   C N S 359 
VAL C    C N N 360 
VAL O    O N N 361 
VAL CB   C N N 362 
VAL CG1  C N N 363 
VAL CG2  C N N 364 
VAL OXT  O N N 365 
VAL H    H N N 366 
VAL H2   H N N 367 
VAL HA   H N N 368 
VAL HB   H N N 369 
VAL HG11 H N N 370 
VAL HG12 H N N 371 
VAL HG13 H N N 372 
VAL HG21 H N N 373 
VAL HG22 H N N 374 
VAL HG23 H N N 375 
VAL HXT  H N N 376 
# 
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  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TRP N   CA   sing N N 293 
TRP N   H    sing N N 294 
TRP N   H2   sing N N 295 
TRP CA  C    sing N N 296 
TRP CA  CB   sing N N 297 
TRP CA  HA   sing N N 298 
TRP C   O    doub N N 299 
TRP C   OXT  sing N N 300 
TRP CB  CG   sing N N 301 
TRP CB  HB2  sing N N 302 
TRP CB  HB3  sing N N 303 
TRP CG  CD1  doub Y N 304 
TRP CG  CD2  sing Y N 305 
TRP CD1 NE1  sing Y N 306 
TRP CD1 HD1  sing N N 307 
TRP CD2 CE2  doub Y N 308 
TRP CD2 CE3  sing Y N 309 
TRP NE1 CE2  sing Y N 310 
TRP NE1 HE1  sing N N 311 
TRP CE2 CZ2  sing Y N 312 
TRP CE3 CZ3  doub Y N 313 
TRP CE3 HE3  sing N N 314 
TRP CZ2 CH2  doub Y N 315 
TRP CZ2 HZ2  sing N N 316 
TRP CZ3 CH2  sing Y N 317 
TRP CZ3 HZ3  sing N N 318 
TRP CH2 HH2  sing N N 319 
TRP OXT HXT  sing N N 320 
TYR N   CA   sing N N 321 
TYR N   H    sing N N 322 
TYR N   H2   sing N N 323 
TYR CA  C    sing N N 324 
TYR CA  CB   sing N N 325 
TYR CA  HA   sing N N 326 
TYR C   O    doub N N 327 
TYR C   OXT  sing N N 328 
TYR CB  CG   sing N N 329 
TYR CB  HB2  sing N N 330 
TYR CB  HB3  sing N N 331 
TYR CG  CD1  doub Y N 332 
TYR CG  CD2  sing Y N 333 
TYR CD1 CE1  sing Y N 334 
TYR CD1 HD1  sing N N 335 
TYR CD2 CE2  doub Y N 336 
TYR CD2 HD2  sing N N 337 
TYR CE1 CZ   doub Y N 338 
TYR CE1 HE1  sing N N 339 
TYR CE2 CZ   sing Y N 340 
TYR CE2 HE2  sing N N 341 
TYR CZ  OH   sing N N 342 
TYR OH  HH   sing N N 343 
TYR OXT HXT  sing N N 344 
VAL N   CA   sing N N 345 
VAL N   H    sing N N 346 
VAL N   H2   sing N N 347 
VAL CA  C    sing N N 348 
VAL CA  CB   sing N N 349 
VAL CA  HA   sing N N 350 
VAL C   O    doub N N 351 
VAL C   OXT  sing N N 352 
VAL CB  CG1  sing N N 353 
VAL CB  CG2  sing N N 354 
VAL CB  HB   sing N N 355 
VAL CG1 HG11 sing N N 356 
VAL CG1 HG12 sing N N 357 
VAL CG1 HG13 sing N N 358 
VAL CG2 HG21 sing N N 359 
VAL CG2 HG22 sing N N 360 
VAL CG2 HG23 sing N N 361 
VAL OXT HXT  sing N N 362 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1F8Y 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EZK 
_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]   0.006699 
_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]   0.006699 
_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]   0.006699 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
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   . MET A 1 1   ? 21.971  32.066  20.907  1.000 128.571 0 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 22.612  30.933  21.622  1.000 121.647 0 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 22.295  29.614  20.909  1.000 112.684 0 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 23.219  28.902  20.548  1.000 111.817 0 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 22.204  30.888  23.102  1.000 124.232 0 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 23.294  31.348  24.062  1.000 134.507 0 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 22.854  31.191  25.809  1.000 152.833 0 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 21.811  29.723  25.782  1.000 131.662 0 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 2   ? 21.019  29.204  20.696  1.000 97.808  0 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 2   ? 20.720  27.895  20.104  1.000 78.353  0 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 2   ? 20.946  27.926  18.598  1.000 70.664  0 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 2   ? 20.538  28.875  17.938  1.000 76.541  0 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 2   ? 19.260  27.637  20.469  1.000 69.206  0 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 2   ? 18.922  28.736  21.438  1.000 79.543  0 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 2   ? 19.788  29.930  21.032  1.000 96.194  0 2   PRO A CD  1 
ATOM   16   N N   . LYS A 1 3   ? 21.644  26.911  18.074  1.000 69.957  0 3   LYS A N   1 
ATOM   17   C CA  . LYS A 1 3   ? 22.073  26.879  16.678  1.000 72.843  0 3   LYS A CA  1 
ATOM   18   C C   . LYS A 1 3   ? 21.509  25.627  15.987  1.000 69.529  0 3   LYS A C   1 
ATOM   19   O O   . LYS A 1 3   ? 21.343  24.593  16.608  1.000 60.981  0 3   LYS A O   1 
ATOM   20   C CB  . LYS A 1 3   ? 23.602  26.975  16.647  1.000 68.004  0 3   LYS A CB  1 
ATOM   21   C CG  . LYS A 1 3   ? 24.180  28.367  16.638  1.000 78.514  0 3   LYS A CG  1 
ATOM   22   C CD  . LYS A 1 3   ? 25.467  28.562  17.451  1.000 94.891  0 3   LYS A CD  1 
ATOM   23   C CE  . LYS A 1 3   ? 26.700  29.110  16.740  1.000 98.168  0 3   LYS A CE  1 
ATOM   24   N NZ  . LYS A 1 3   ? 26.453  30.173  15.763  1.000 101.453 0 3   LYS A NZ  1 
ATOM   25   N N   . LYS A 1 4   ? 21.135  25.714  14.704  1.000 74.809  0 4   LYS A N   1 
ATOM   26   C CA  . LYS A 1 4   ? 20.668  24.540  13.970  1.000 71.299  0 4   LYS A CA  1 
ATOM   27   C C   . LYS A 1 4   ? 21.701  24.175  12.893  1.000 64.536  0 4   LYS A C   1 
ATOM   28   O O   . LYS A 1 4   ? 22.462  25.018  12.428  1.000 78.775  0 4   LYS A O   1 
ATOM   29   C CB  . LYS A 1 4   ? 19.287  24.805  13.348  1.000 66.350  0 4   LYS A CB  1 
ATOM   30   C CG  . LYS A 1 4   ? 18.066  25.030  14.235  1.000 72.680  0 4   LYS A CG  1 
ATOM   31   C CD  . LYS A 1 4   ? 17.629  23.907  15.185  1.000 77.235  0 4   LYS A CD  1 
ATOM   32   C CE  . LYS A 1 4   ? 16.151  23.610  15.166  1.000 95.453  0 4   LYS A CE  1 
ATOM   33   N NZ  . LYS A 1 4   ? 15.269  24.782  15.025  1.000 104.987 0 4   LYS A NZ  1 
ATOM   34   N N   . THR A 1 5   ? 21.708  22.926  12.442  1.000 61.839  0 5   THR A N   1 
ATOM   35   C CA  . THR A 1 5   ? 22.547  22.547  11.307  1.000 65.228  0 5   THR A CA  1 
ATOM   36   C C   . THR A 1 5   ? 21.668  22.367  10.088  1.000 58.449  0 5   THR A C   1 
ATOM   37   O O   . THR A 1 5   ? 20.474  22.120  10.230  1.000 64.199  0 5   THR A O   1 
ATOM   38   C CB  . THR A 1 5   ? 23.340  21.270  11.561  1.000 65.347  0 5   THR A CB  1 
ATOM   39   O OG1 . THR A 1 5   ? 22.354  20.246  11.674  1.000 61.252  0 5   THR A OG1 1 
ATOM   40   C CG2 . THR A 1 5   ? 24.207  21.421  12.797  1.000 63.882  0 5   THR A CG2 1 
ATOM   41   N N   . ILE A 1 6   ? 22.291  22.514  8.910   1.000 64.554  0 6   ILE A N   1 
ATOM   42   C CA  . ILE A 1 6   ? 21.581  22.395  7.645   1.000 71.175  0 6   ILE A CA  1 
ATOM   43   C C   . ILE A 1 6   ? 22.248  21.394  6.700   1.000 72.064  0 6   ILE A C   1 
ATOM   44   O O   . ILE A 1 6   ? 23.352  20.917  6.948   1.000 67.533  0 6   ILE A O   1 
ATOM   45   C CB  . ILE A 1 6   ? 21.439  23.756  6.960   1.000 65.156  0 6   ILE A CB  1 
ATOM   46   C CG1 . ILE A 1 6   ? 22.768  24.401  6.668   1.000 80.983  0 6   ILE A CG1 1 
ATOM   47   C CG2 . ILE A 1 6   ? 20.545  24.664  7.768   1.000 73.520  0 6   ILE A CG2 1 
ATOM   48   C CD1 . ILE A 1 6   ? 23.125  24.409  5.189   1.000 82.139  0 6   ILE A CD1 1 
ATOM   49   N N   . TYR A 1 7   ? 21.502  21.069  5.634   1.000 64.670  0 7   TYR A N   1 
ATOM   50   C CA  . TYR A 1 7   ? 21.997  20.375  4.463   1.000 62.980  0 7   TYR A CA  1 
ATOM   51   C C   . TYR A 1 7   ? 21.977  21.380  3.323   1.000 67.088  0 7   TYR A C   1 
ATOM   52   O O   . TYR A 1 7   ? 20.928  21.953  3.016   1.000 72.079  0 7   TYR A O   1 
ATOM   53   C CB  . TYR A 1 7   ? 21.118  19.169  4.119   1.000 66.606  0 7   TYR A CB  1 
ATOM   54   C CG  . TYR A 1 7   ? 21.444  18.448  2.817   1.000 62.432  0 7   TYR A CG  1 
ATOM   55   C CD1 . TYR A 1 7   ? 20.908  18.849  1.593   1.000 70.289  0 7   TYR A CD1 1 
ATOM   56   C CD2 . TYR A 1 7   ? 22.303  17.368  2.812   1.000 61.562  0 7   TYR A CD2 1 
ATOM   57   C CE1 . TYR A 1 7   ? 21.241  18.203  0.407   1.000 67.796  0 7   TYR A CE1 1 
ATOM   58   C CE2 . TYR A 1 7   ? 22.635  16.711  1.637   1.000 67.420  0 7   TYR A CE2 1 
ATOM   59   C CZ  . TYR A 1 7   ? 22.108  17.128  0.431   1.000 62.738  0 7   TYR A CZ  1 
ATOM   60   O OH  . TYR A 1 7   ? 22.453  16.417  -0.677  1.000 60.384  0 7   TYR A OH  1 
ATOM   61   N N   . PHE A 1 8   ? 23.144  21.551  2.693   1.000 69.457  0 8   PHE A N   1 
ATOM   62   C CA  . PHE A 1 8   ? 23.356  22.607  1.723   1.000 63.922  0 8   PHE A CA  1 
ATOM   63   C C   . PHE A 1 8   ? 22.953  22.100  0.352   1.000 65.074  0 8   PHE A C   1 
ATOM   64   O O   . PHE A 1 8   ? 23.794  21.690  -0.434  1.000 68.538  0 8   PHE A O   1 
ATOM   65   C CB  . PHE A 1 8   ? 24.814  23.059  1.773   1.000 63.138  0 8   PHE A CB  1 
ATOM   66   C CG  . PHE A 1 8   ? 25.042  24.351  1.019   1.000 65.500  0 8   PHE A CG  1 
ATOM   67   C CD1 . PHE A 1 8   ? 24.809  25.566  1.642   1.000 64.421  0 8   PHE A CD1 1 
ATOM   68   C CD2 . PHE A 1 8   ? 25.452  24.343  -0.310  1.000 67.890  0 8   PHE A CD2 1 
ATOM   69   C CE1 . PHE A 1 8   ? 25.005  26.747  0.958   1.000 64.615  0 8   PHE A CE1 1 
ATOM   70   C CE2 . PHE A 1 8   ? 25.638  25.525  -0.992  1.000 73.123  0 8   PHE A CE2 1 
ATOM   71   C CZ  . PHE A 1 8   ? 25.401  26.722  -0.353  1.000 80.955  0 8   PHE A CZ  1 
ATOM   72   N N   . GLY A 1 9   ? 21.649  22.161  0.075   1.000 70.436  0 9   GLY A N   1 
ATOM   73   C CA  . GLY A 1 9   ? 21.123  21.754  -1.211  1.000 69.967  0 9   GLY A CA  1 
ATOM   74   C C   . GLY A 1 9   ? 21.310  22.844  -2.261  1.000 64.505  0 9   GLY A C   1 
ATOM   75   O O   . GLY A 1 9   ? 20.682  23.886  -2.178  1.000 69.730  0 9   GLY A O   1 
ATOM   76   N N   . ALA A 1 10  ? 22.130  22.553  -3.275  1.000 70.304  0 10  ALA A N   1 
ATOM   77   C CA  . ALA A 1 10  ? 22.549  23.535  -4.270  1.000 59.696  0 10  ALA A CA  1 
ATOM   78   C C   . ALA A 1 10  ? 23.245  22.835  -5.429  1.000 60.154  0 10  ALA A C   1 
ATOM   79   O O   . ALA A 1 10  ? 24.092  21.982  -5.208  1.000 83.693  0 10  ALA A O   1 
ATOM   80   C CB  . ALA A 1 10  ? 23.507  24.519  -3.662  1.000 69.439  0 10  ALA A CB  1 
ATOM   81   N N   . GLY A 1 11  ? 22.906  23.232  -6.651  1.000 69.258  0 11  GLY A N   1 
ATOM   82   C CA  . GLY A 1 11  ? 23.624  22.812  -7.842  1.000 79.239  0 11  GLY A CA  1 
ATOM   83   C C   . GLY A 1 11  ? 24.943  23.570  -8.009  1.000 73.342  0 11  GLY A C   1 
ATOM   84   O O   . GLY A 1 11  ? 25.140  24.621  -7.395  1.000 65.641  0 11  GLY A O   1 
ATOM   85   N N   . TRP A 1 12  ? 25.845  22.992  -8.828  1.000 80.716  0 12  TRP A N   1 
ATOM   86   C CA  . TRP A 1 12  ? 27.132  23.596  -9.161  1.000 73.968  0 12  TRP A CA  1 
ATOM   87   C C   . TRP A 1 12  ? 27.460  23.408  -10.642 1.000 77.538  0 12  TRP A C   1 
ATOM   88   O O   . TRP A 1 12  ? 28.624  23.357  -11.012 1.000 72.784  0 12  TRP A O   1 
ATOM   89   C CB  . TRP A 1 12  ? 28.237  23.005  -8.286  1.000 70.160  0 12  TRP A CB  1 
ATOM   90   C CG  . TRP A 1 12  ? 28.298  21.502  -8.316  1.000 79.451  0 12  TRP A CG  1 
ATOM   91   C CD1 . TRP A 1 12  ? 28.909  20.749  -9.265  1.000 80.546  0 12  TRP A CD1 1 
ATOM   92   C CD2 . TRP A 1 12  ? 27.755  20.568  -7.359  1.000 83.844  0 12  TRP A CD2 1 
ATOM   93   N NE1 . TRP A 1 12  ? 28.760  19.417  -8.992  1.000 80.243  0 12  TRP A NE1 1 
ATOM   94   C CE2 . TRP A 1 12  ? 28.081  19.276  -7.819  1.000 79.453  0 12  TRP A CE2 1 
ATOM   95   C CE3 . TRP A 1 12  ? 27.031  20.690  -6.171  1.000 79.313  0 12  TRP A CE3 1 
ATOM   96   C CZ2 . TRP A 1 12  ? 27.716  18.126  -7.134  1.000 77.443  0 12  TRP A CZ2 1 
ATOM   97   C CZ3 . TRP A 1 12  ? 26.668  19.551  -5.491  1.000 83.772  0 12  TRP A CZ3 1 
ATOM   98   C CH2 . TRP A 1 12  ? 27.022  18.288  -5.959  1.000 80.369  0 12  TRP A CH2 1 
ATOM   99   N N   . PHE A 1 13  ? 26.423  23.385  -11.492 1.000 87.495  0 13  PHE A N   1 
ATOM   100  C CA  . PHE A 1 13  ? 26.526  22.914  -12.863 1.000 87.667  0 13  PHE A CA  1 
ATOM   101  C C   . PHE A 1 13  ? 26.534  24.086  -13.837 1.000 91.810  0 13  PHE A C   1 
ATOM   102  O O   . PHE A 1 13  ? 26.806  23.857  -15.007 1.000 104.590 0 13  PHE A O   1 
ATOM   103  C CB  . PHE A 1 13  ? 25.372  21.963  -13.212 1.000 89.798  0 13  PHE A CB  1 
ATOM   104  C CG  . PHE A 1 13  ? 25.144  20.830  -12.209 1.000 114.991 0 13  PHE A CG  1 
ATOM   105  C CD1 . PHE A 1 13  ? 26.149  19.880  -11.968 1.000 109.346 0 13  PHE A CD1 1 
ATOM   106  C CD2 . PHE A 1 13  ? 23.924  20.709  -11.525 1.000 102.103 0 13  PHE A CD2 1 
ATOM   107  C CE1 . PHE A 1 13  ? 25.959  18.880  -11.031 1.000 105.068 0 13  PHE A CE1 1 
ATOM   108  C CE2 . PHE A 1 13  ? 23.739  19.710  -10.586 1.000 100.952 0 13  PHE A CE2 1 
ATOM   109  C CZ  . PHE A 1 13  ? 24.753  18.796  -10.344 1.000 118.822 0 13  PHE A CZ  1 
ATOM   110  N N   . THR A 1 14  ? 26.189  25.301  -13.375 1.000 88.896  0 14  THR A N   1 
ATOM   111  C CA  . THR A 1 14  ? 26.085  26.480  -14.227 1.000 77.479  0 14  THR A CA  1 
ATOM   112  C C   . THR A 1 14  ? 26.719  27.671  -13.516 1.000 79.379  0 14  THR A C   1 
ATOM   113  O O   . THR A 1 14  ? 27.118  27.583  -12.350 1.000 91.012  0 14  THR A O   1 
ATOM   114  C CB  . THR A 1 14  ? 24.637  26.809  -14.589 1.000 71.656  0 14  THR A CB  1 
ATOM   115  O OG1 . THR A 1 14  ? 24.160  27.489  -13.440 1.000 88.260  0 14  THR A OG1 1 
ATOM   116  C CG2 . THR A 1 14  ? 23.751  25.616  -14.904 1.000 69.166  0 14  THR A CG2 1 
ATOM   117  N N   . ASP A 1 15  ? 26.784  28.805  -14.225 1.000 86.891  0 15  ASP A N   1 
ATOM   118  C CA  . ASP A 1 15  ? 27.428  29.990  -13.683 1.000 91.324  0 15  ASP A CA  1 
ATOM   119  C C   . ASP A 1 15  ? 26.550  30.653  -12.634 1.000 82.886  0 15  ASP A C   1 
ATOM   120  O O   . ASP A 1 15  ? 27.056  31.131  -11.622 1.000 88.343  0 15  ASP A O   1 
ATOM   121  C CB  . ASP A 1 15  ? 27.768  30.975  -14.779 1.000 92.116  0 15  ASP A CB  1 
ATOM   122  C CG  . ASP A 1 15  ? 28.857  30.478  -15.703 1.000 93.625  0 15  ASP A CG  1 
ATOM   123  O OD1 . ASP A 1 15  ? 29.624  29.572  -15.271 1.000 87.488  0 15  ASP A OD1 1 
ATOM   124  O OD2 . ASP A 1 15  ? 28.892  30.988  -16.834 1.000 88.293  0 15  ASP A OD2 1 
ATOM   125  N N   . ARG A 1 16  ? 25.241  30.658  -12.881 1.000 83.195  0 16  ARG A N   1 
ATOM   126  C CA  . ARG A 1 16  ? 24.304  31.296  -11.967 1.000 87.987  0 16  ARG A CA  1 
ATOM   127  C C   . ARG A 1 16  ? 24.183  30.472  -10.699 1.000 84.010  0 16  ARG A C   1 
ATOM   128  O O   . ARG A 1 16  ? 24.041  31.017  -9.609  1.000 92.853  0 16  ARG A O   1 
ATOM   129  C CB  . ARG A 1 16  ? 22.905  31.434  -12.552 1.000 79.933  0 16  ARG A CB  1 
ATOM   130  C CG  . ARG A 1 16  ? 22.975  31.692  -14.049 1.000 100.295 0 16  ARG A CG  1 
ATOM   131  C CD  . ARG A 1 16  ? 22.209  32.943  -14.421 1.000 95.566  0 16  ARG A CD  1 
ATOM   132  N NE  . ARG A 1 16  ? 20.953  33.123  -13.684 1.000 92.130  0 16  ARG A NE  1 
ATOM   133  C CZ  . ARG A 1 16  ? 19.753  32.963  -14.205 1.000 89.884  0 16  ARG A CZ  1 
ATOM   134  N NH1 . ARG A 1 16  ? 19.624  32.340  -15.369 1.000 77.785  0 16  ARG A NH1 1 
ATOM   135  N NH2 . ARG A 1 16  ? 18.713  33.372  -13.500 1.000 105.422 0 16  ARG A NH2 1 
ATOM   136  N N   . GLN A 1 17  ? 24.248  29.155  -10.877 1.000 77.365  0 17  GLN A N   1 
ATOM   137  C CA  . GLN A 1 17  ? 24.236  28.222  -9.769  1.000 75.469  0 17  GLN A CA  1 
ATOM   138  C C   . GLN A 1 17  ? 25.465  28.414  -8.908  1.000 73.514  0 17  GLN A C   1 
ATOM   139  O O   . GLN A 1 17  ? 25.350  28.452  -7.688  1.000 83.065  0 17  GLN A O   1 
ATOM   140  C CB  . GLN A 1 17  ? 24.194  26.768  -10.218 1.000 68.834  0 17  GLN A CB  1 
ATOM   141  C CG  . GLN A 1 17  ? 22.807  26.320  -10.667 1.000 68.651  0 17  GLN A CG  1 
ATOM   142  C CD  . GLN A 1 17  ? 22.812  24.884  -11.132 1.000 74.184  0 17  GLN A CD  1 
ATOM   143  O OE1 . GLN A 1 17  ? 23.816  24.173  -10.995 1.000 68.142  0 17  GLN A OE1 1 
ATOM   144  N NE2 . GLN A 1 17  ? 21.699  24.469  -11.718 1.000 71.694  0 17  GLN A NE2 1 
ATOM   145  N N   . ASN A 1 18  ? 26.631  28.490  -9.547  1.000 68.819  0 18  ASN A N   1 
ATOM   146  C CA  . ASN A 1 18  ? 27.868  28.618  -8.791  1.000 80.484  0 18  ASN A CA  1 
ATOM   147  C C   . ASN A 1 18  ? 27.900  29.960  -8.049  1.000 73.114  0 18  ASN A C   1 
ATOM   148  O O   . ASN A 1 18  ? 28.484  30.077  -6.975  1.000 77.296  0 18  ASN A O   1 
ATOM   149  C CB  . ASN A 1 18  ? 29.096  28.359  -9.662  1.000 73.455  0 18  ASN A CB  1 
ATOM   150  C CG  . ASN A 1 18  ? 29.330  26.887  -9.876  1.000 75.455  0 18  ASN A CG  1 
ATOM   151  O OD1 . ASN A 1 18  ? 29.567  26.152  -8.909  1.000 83.421  0 18  ASN A OD1 1 
ATOM   152  N ND2 . ASN A 1 18  ? 29.262  26.439  -11.120 1.000 79.552  0 18  ASN A ND2 1 
ATOM   153  N N   . LYS A 1 19  ? 27.284  30.982  -8.637  1.000 76.030  0 19  LYS A N   1 
ATOM   154  C CA  . LYS A 1 19  ? 27.264  32.299  -8.033  1.000 74.648  0 19  LYS A CA  1 
ATOM   155  C C   . LYS A 1 19  ? 26.410  32.228  -6.767  1.000 74.534  0 19  LYS A C   1 
ATOM   156  O O   . LYS A 1 19  ? 26.847  32.647  -5.699  1.000 84.637  0 19  LYS A O   1 
ATOM   157  C CB  . LYS A 1 19  ? 26.745  33.313  -9.063  1.000 82.818  0 19  LYS A CB  1 
ATOM   158  C CG  . LYS A 1 19  ? 26.926  34.796  -8.720  1.000 90.699  0 19  LYS A CG  1 
ATOM   159  C CD  . LYS A 1 19  ? 25.665  35.627  -8.910  1.000 104.047 0 19  LYS A CD  1 
ATOM   160  C CE  . LYS A 1 19  ? 25.949  37.085  -8.761  1.000 111.430 0 19  LYS A CE  1 
ATOM   161  N NZ  . LYS A 1 19  ? 26.215  37.683  -10.069 1.000 108.020 0 19  LYS A NZ  1 
ATOM   162  N N   . ALA A 1 20  ? 25.206  31.654  -6.908  1.000 73.051  0 20  ALA A N   1 
ATOM   163  C CA  . ALA A 1 20  ? 24.225  31.501  -5.836  1.000 72.769  0 20  ALA A CA  1 
ATOM   164  C C   . ALA A 1 20  ? 24.788  30.703  -4.657  1.000 64.320  0 20  ALA A C   1 
ATOM   165  O O   . ALA A 1 20  ? 24.558  31.021  -3.493  1.000 70.010  0 20  ALA A O   1 
ATOM   166  C CB  . ALA A 1 20  ? 22.995  30.821  -6.408  1.000 64.556  0 20  ALA A CB  1 
ATOM   167  N N   . TYR A 1 21  ? 25.514  29.648  -5.003  1.000 62.152  0 21  TYR A N   1 
ATOM   168  C CA  . TYR A 1 21  ? 26.220  28.811  -4.061  1.000 58.754  0 21  TYR A CA  1 
ATOM   169  C C   . TYR A 1 21  ? 27.121  29.682  -3.190  1.000 63.294  0 21  TYR A C   1 
ATOM   170  O O   . TYR A 1 21  ? 27.001  29.608  -1.967  1.000 65.770  0 21  TYR A O   1 
ATOM   171  C CB  . TYR A 1 21  ? 26.902  27.769  -4.956  1.000 63.224  0 21  TYR A CB  1 
ATOM   172  C CG  . TYR A 1 21  ? 27.621  26.681  -4.185  1.000 66.060  0 21  TYR A CG  1 
ATOM   173  C CD1 . TYR A 1 21  ? 28.674  27.001  -3.350  1.000 69.243  0 21  TYR A CD1 1 
ATOM   174  C CD2 . TYR A 1 21  ? 27.262  25.347  -4.294  1.000 67.069  0 21  TYR A CD2 1 
ATOM   175  C CE1 . TYR A 1 21  ? 29.309  26.030  -2.595  1.000 81.977  0 21  TYR A CE1 1 
ATOM   176  C CE2 . TYR A 1 21  ? 27.916  24.363  -3.568  1.000 61.776  0 21  TYR A CE2 1 
ATOM   177  C CZ  . TYR A 1 21  ? 28.924  24.708  -2.696  1.000 67.199  0 21  TYR A CZ  1 
ATOM   178  O OH  . TYR A 1 21  ? 29.626  23.791  -1.974  1.000 71.472  0 21  TYR A OH  1 
ATOM   179  N N   . LYS A 1 22  ? 27.989  30.517  -3.813  1.000 71.084  0 22  LYS A N   1 
ATOM   180  C CA  . LYS A 1 22  ? 29.012  31.270  -3.082  1.000 74.922  0 22  LYS A CA  1 
ATOM   181  C C   . LYS A 1 22  ? 28.303  32.258  -2.149  1.000 73.477  0 22  LYS A C   1 
ATOM   182  O O   . LYS A 1 22  ? 28.695  32.386  -0.980  1.000 81.232  0 22  LYS A O   1 
ATOM   183  C CB  . LYS A 1 22  ? 30.135  31.887  -3.948  1.000 61.216  0 22  LYS A CB  1 
ATOM   184  N N   . GLU A 1 23  ? 27.223  32.886  -2.657  1.000 71.423  0 23  GLU A N   1 
ATOM   185  C CA  . GLU A 1 23  ? 26.471  33.884  -1.910  1.000 72.340  0 23  GLU A CA  1 
ATOM   186  C C   . GLU A 1 23  ? 25.806  33.277  -0.668  1.000 73.174  0 23  GLU A C   1 
ATOM   187  O O   . GLU A 1 23  ? 25.781  33.889  0.409   1.000 81.995  0 23  GLU A O   1 
ATOM   188  C CB  . GLU A 1 23  ? 25.415  34.521  -2.811  1.000 67.179  0 23  GLU A CB  1 
ATOM   189  C CG  . GLU A 1 23  ? 26.001  35.377  -3.924  1.000 70.605  0 23  GLU A CG  1 
ATOM   190  C CD  . GLU A 1 23  ? 25.013  36.178  -4.781  1.000 89.601  0 23  GLU A CD  1 
ATOM   191  O OE1 . GLU A 1 23  ? 25.391  37.354  -5.032  1.000 85.387  0 23  GLU A OE1 1 
ATOM   192  O OE2 . GLU A 1 23  ? 23.920  35.700  -5.224  1.000 92.212  0 23  GLU A OE2 1 
ATOM   193  N N   . ALA A 1 24  ? 25.237  32.079  -0.840  1.000 70.013  0 24  ALA A N   1 
ATOM   194  C CA  . ALA A 1 24  ? 24.470  31.440  0.217   1.000 76.560  0 24  ALA A CA  1 
ATOM   195  C C   . ALA A 1 24  ? 25.398  30.950  1.329   1.000 74.287  0 24  ALA A C   1 
ATOM   196  O O   . ALA A 1 24  ? 25.052  30.899  2.516   1.000 78.539  0 24  ALA A O   1 
ATOM   197  C CB  . ALA A 1 24  ? 23.682  30.306  -0.379  1.000 76.730  0 24  ALA A CB  1 
ATOM   198  N N   . MET A 1 25  ? 26.600  30.573  0.928   1.000 69.697  0 25  MET A N   1 
ATOM   199  C CA  . MET A 1 25  ? 27.553  30.048  1.873   1.000 68.540  0 25  MET A CA  1 
ATOM   200  C C   . MET A 1 25  ? 28.077  31.216  2.721   1.000 75.519  0 25  MET A C   1 
ATOM   201  O O   . MET A 1 25  ? 28.249  31.080  3.941   1.000 88.638  0 25  MET A O   1 
ATOM   202  C CB  . MET A 1 25  ? 28.605  29.249  1.090   1.000 61.986  0 25  MET A CB  1 
ATOM   203  C CG  . MET A 1 25  ? 29.465  28.364  1.966   1.000 70.376  0 25  MET A CG  1 
ATOM   204  S SD  . MET A 1 25  ? 28.752  26.836  2.617   1.000 78.377  0 25  MET A SD  1 
ATOM   205  C CE  . MET A 1 25  ? 28.654  25.771  1.178   1.000 78.265  0 25  MET A CE  1 
ATOM   206  N N   . GLU A 1 26  ? 28.304  32.380  2.091   1.000 84.253  0 26  GLU A N   1 
ATOM   207  C CA  . GLU A 1 26  ? 28.751  33.560  2.825   1.000 89.723  0 26  GLU A CA  1 
ATOM   208  C C   . GLU A 1 26  ? 27.668  34.005  3.807   1.000 83.905  0 26  GLU A C   1 
ATOM   209  O O   . GLU A 1 26  ? 27.969  34.382  4.948   1.000 91.124  0 26  GLU A O   1 
ATOM   210  C CB  . GLU A 1 26  ? 29.129  34.710  1.898   1.000 97.494  0 26  GLU A CB  1 
ATOM   211  C CG  . GLU A 1 26  ? 30.504  34.553  1.247   1.000 99.214  0 26  GLU A CG  1 
ATOM   212  C CD  . GLU A 1 26  ? 30.615  35.376  -0.040  1.000 118.325 0 26  GLU A CD  1 
ATOM   213  O OE1 . GLU A 1 26  ? 29.600  35.980  -0.515  1.000 99.113  0 26  GLU A OE1 1 
ATOM   214  O OE2 . GLU A 1 26  ? 31.746  35.429  -0.581  1.000 122.696 0 26  GLU A OE2 1 
ATOM   215  N N   . ALA A 1 27  ? 26.408  33.925  3.353   1.000 68.182  0 27  ALA A N   1 
ATOM   216  C CA  . ALA A 1 27  ? 25.240  34.197  4.174   1.000 66.581  0 27  ALA A CA  1 
ATOM   217  C C   . ALA A 1 27  ? 25.222  33.376  5.469   1.000 72.680  0 27  ALA A C   1 
ATOM   218  O O   . ALA A 1 27  ? 24.993  33.905  6.561   1.000 77.962  0 27  ALA A O   1 
ATOM   219  C CB  . ALA A 1 27  ? 24.021  33.941  3.342   1.000 63.777  0 27  ALA A CB  1 
ATOM   220  N N   . LEU A 1 28  ? 25.474  32.068  5.352   1.000 71.708  0 28  LEU A N   1 
ATOM   221  C CA  . LEU A 1 28  ? 25.365  31.174  6.495   1.000 68.186  0 28  LEU A CA  1 
ATOM   222  C C   . LEU A 1 28  ? 26.488  31.424  7.495   1.000 72.385  0 28  LEU A C   1 
ATOM   223  O O   . LEU A 1 28  ? 26.242  31.410  8.707   1.000 78.479  0 28  LEU A O   1 
ATOM   224  C CB  . LEU A 1 28  ? 25.339  29.736  5.989   1.000 69.086  0 28  LEU A CB  1 
ATOM   225  C CG  . LEU A 1 28  ? 24.099  29.373  5.158   1.000 68.708  0 28  LEU A CG  1 
ATOM   226  C CD1 . LEU A 1 28  ? 24.349  28.047  4.516   1.000 63.969  0 28  LEU A CD1 1 
ATOM   227  C CD2 . LEU A 1 28  ? 22.752  29.361  5.920   1.000 62.079  0 28  LEU A CD2 1 
ATOM   228  N N   . LYS A 1 29  ? 27.696  31.697  6.975   1.000 74.815  0 29  LYS A N   1 
ATOM   229  C CA  . LYS A 1 29  ? 28.850  32.034  7.800   1.000 71.984  0 29  LYS A CA  1 
ATOM   230  C C   . LYS A 1 29  ? 28.455  33.148  8.781   1.000 77.387  0 29  LYS A C   1 
ATOM   231  O O   . LYS A 1 29  ? 28.857  33.090  9.946   1.000 75.617  0 29  LYS A O   1 
ATOM   232  C CB  . LYS A 1 29  ? 30.122  32.298  6.959   1.000 75.039  0 29  LYS A CB  1 
ATOM   233  C CG  . LYS A 1 29  ? 30.868  31.073  6.279   1.000 89.115  0 29  LYS A CG  1 
ATOM   234  C CD  . LYS A 1 29  ? 31.890  31.185  5.128   1.000 69.334  0 29  LYS A CD  1 
ATOM   235  N N   . GLU A 1 30  ? 27.607  34.102  8.335   1.000 77.644  0 30  GLU A N   1 
ATOM   236  C CA  . GLU A 1 30  ? 27.255  35.290  9.116   1.000 75.634  0 30  GLU A CA  1 
ATOM   237  C C   . GLU A 1 30  ? 25.945  35.099  9.893   1.000 73.204  0 30  GLU A C   1 
ATOM   238  O O   . GLU A 1 30  ? 25.528  36.002  10.614  1.000 71.857  0 30  GLU A O   1 
ATOM   239  C CB  . GLU A 1 30  ? 27.126  36.557  8.250   1.000 87.948  0 30  GLU A CB  1 
ATOM   240  C CG  . GLU A 1 30  ? 28.410  37.303  7.870   1.000 88.558  0 30  GLU A CG  1 
ATOM   241  C CD  . GLU A 1 30  ? 28.143  38.235  6.687   1.000 88.169  0 30  GLU A CD  1 
ATOM   242  N N   . ASN A 1 31  ? 25.285  33.934  9.798   1.000 79.320  0 31  ASN A N   1 
ATOM   243  C CA  . ASN A 1 31  ? 23.998  33.754  10.458  1.000 69.909  0 31  ASN A CA  1 
ATOM   244  C C   . ASN A 1 31  ? 24.220  33.163  11.844  1.000 70.983  0 31  ASN A C   1 
ATOM   245  O O   . ASN A 1 31  ? 24.701  32.049  11.962  1.000 80.217  0 31  ASN A O   1 
ATOM   246  C CB  . ASN A 1 31  ? 23.057  32.854  9.665   1.000 64.748  0 31  ASN A CB  1 
ATOM   247  C CG  . ASN A 1 31  ? 21.680  32.738  10.286  1.000 67.711  0 31  ASN A CG  1 
ATOM   248  O OD1 . ASN A 1 31  ? 21.536  32.471  11.485  1.000 73.276  0 31  ASN A OD1 1 
ATOM   249  N ND2 . ASN A 1 31  ? 20.644  32.926  9.485   1.000 70.267  0 31  ASN A ND2 1 
ATOM   250  N N   . PRO A 1 32  ? 23.825  33.850  12.939  1.000 72.930  0 32  PRO A N   1 
ATOM   251  C CA  . PRO A 1 32  ? 24.107  33.352  14.284  1.000 68.245  0 32  PRO A CA  1 
ATOM   252  C C   . PRO A 1 32  ? 23.234  32.188  14.763  1.000 76.213  0 32  PRO A C   1 
ATOM   253  O O   . PRO A 1 32  ? 23.437  31.714  15.882  1.000 69.316  0 32  PRO A O   1 
ATOM   254  C CB  . PRO A 1 32  ? 23.913  34.628  15.119  1.000 66.488  0 32  PRO A CB  1 
ATOM   255  C CG  . PRO A 1 32  ? 22.782  35.360  14.397  1.000 70.954  0 32  PRO A CG  1 
ATOM   256  C CD  . PRO A 1 32  ? 23.098  35.130  12.937  1.000 78.210  0 32  PRO A CD  1 
ATOM   257  N N   . THR A 1 33  ? 22.278  31.713  13.936  1.000 76.407  0 33  THR A N   1 
ATOM   258  C CA  . THR A 1 33  ? 21.410  30.608  14.349  1.000 74.805  0 33  THR A CA  1 
ATOM   259  C C   . THR A 1 33  ? 21.878  29.299  13.717  1.000 69.178  0 33  THR A C   1 
ATOM   260  O O   . THR A 1 33  ? 21.309  28.243  13.980  1.000 74.498  0 33  THR A O   1 
ATOM   261  C CB  . THR A 1 33  ? 19.925  30.883  14.080  1.000 69.124  0 33  THR A CB  1 
ATOM   262  O OG1 . THR A 1 33  ? 19.714  31.086  12.691  1.000 64.817  0 33  THR A OG1 1 
ATOM   263  C CG2 . THR A 1 33  ? 19.418  32.088  14.858  1.000 79.764  0 33  THR A CG2 1 
ATOM   264  N N   . ILE A 1 34  ? 22.961  29.358  12.946  1.000 66.945  0 34  ILE A N   1 
ATOM   265  C CA  . ILE A 1 34  ? 23.436  28.211  12.188  1.000 65.753  0 34  ILE A CA  1 
ATOM   266  C C   . ILE A 1 34  ? 24.788  27.731  12.712  1.000 63.914  0 34  ILE A C   1 
ATOM   267  O O   . ILE A 1 34  ? 25.672  28.544  12.899  1.000 69.837  0 34  ILE A O   1 
ATOM   268  C CB  . ILE A 1 34  ? 23.568  28.624  10.720  1.000 64.247  0 34  ILE A CB  1 
ATOM   269  C CG1 . ILE A 1 34  ? 22.224  28.783  10.024  1.000 77.042  0 34  ILE A CG1 1 
ATOM   270  C CG2 . ILE A 1 34  ? 24.468  27.640  9.990   1.000 80.120  0 34  ILE A CG2 1 
ATOM   271  C CD1 . ILE A 1 34  ? 21.375  27.523  9.983   1.000 81.311  0 34  ILE A CD1 1 
ATOM   272  N N   . ASP A 1 35  ? 24.973  26.411  12.849  1.000 72.940  0 35  ASP A N   1 
ATOM   273  C CA  . ASP A 1 35  ? 26.293  25.812  13.031  1.000 69.035  0 35  ASP A CA  1 
ATOM   274  C C   . ASP A 1 35  ? 26.787  25.276  11.683  1.000 65.414  0 35  ASP A C   1 
ATOM   275  O O   . ASP A 1 35  ? 26.489  24.140  11.318  1.000 64.525  0 35  ASP A O   1 
ATOM   276  C CB  . ASP A 1 35  ? 26.290  24.763  14.143  1.000 72.105  0 35  ASP A CB  1 
ATOM   277  C CG  . ASP A 1 35  ? 27.550  23.901  14.319  1.000 77.760  0 35  ASP A CG  1 
ATOM   278  O OD1 . ASP A 1 35  ? 28.513  24.083  13.541  1.000 68.396  0 35  ASP A OD1 1 
ATOM   279  O OD2 . ASP A 1 35  ? 27.579  23.045  15.248  1.000 68.062  0 35  ASP A OD2 1 
ATOM   280  N N   . LEU A 1 36  ? 27.555  26.082  10.937  1.000 65.169  0 36  LEU A N   1 
ATOM   281  C CA  . LEU A 1 36  ? 27.960  25.690  9.591   1.000 63.630  0 36  LEU A CA  1 
ATOM   282  C C   . LEU A 1 36  ? 29.078  24.657  9.629   1.000 58.661  0 36  LEU A C   1 
ATOM   283  O O   . LEU A 1 36  ? 29.218  23.868  8.712   1.000 66.693  0 36  LEU A O   1 
ATOM   284  C CB  . LEU A 1 36  ? 28.374  26.890  8.749   1.000 69.451  0 36  LEU A CB  1 
ATOM   285  C CG  . LEU A 1 36  ? 28.574  26.636  7.244   1.000 69.230  0 36  LEU A CG  1 
ATOM   286  C CD1 . LEU A 1 36  ? 27.381  26.018  6.527   1.000 64.947  0 36  LEU A CD1 1 
ATOM   287  C CD2 . LEU A 1 36  ? 28.946  27.930  6.538   1.000 73.865  0 36  LEU A CD2 1 
ATOM   288  N N   . GLU A 1 37  ? 29.877  24.658  10.690  1.000 68.800  0 37  GLU A N   1 
ATOM   289  C CA  . GLU A 1 37  ? 31.003  23.745  10.801  1.000 78.839  0 37  GLU A CA  1 
ATOM   290  C C   . GLU A 1 37  ? 30.483  22.309  10.909  1.000 66.009  0 37  GLU A C   1 
ATOM   291  O O   . GLU A 1 37  ? 31.186  21.399  10.534  1.000 71.262  0 37  GLU A O   1 
ATOM   292  C CB  . GLU A 1 37  ? 31.900  24.194  11.963  1.000 99.601  0 37  GLU A CB  1 
ATOM   293  C CG  . GLU A 1 37  ? 33.175  23.387  12.217  1.000 103.861 0 37  GLU A CG  1 
ATOM   294  C CD  . GLU A 1 37  ? 33.654  23.568  13.660  1.000 95.383  0 37  GLU A CD  1 
ATOM   295  N N   . ASN A 1 38  ? 29.266  22.098  11.419  1.000 70.827  0 38  ASN A N   1 
ATOM   296  C CA  . ASN A 1 38  ? 28.747  20.749  11.620  1.000 68.284  0 38  ASN A CA  1 
ATOM   297  C C   . ASN A 1 38  ? 27.599  20.443  10.664  1.000 71.210  0 38  ASN A C   1 
ATOM   298  O O   . ASN A 1 38  ? 26.862  19.471  10.861  1.000 74.025  0 38  ASN A O   1 
ATOM   299  C CB  . ASN A 1 38  ? 28.271  20.530  13.049  1.000 58.687  0 38  ASN A CB  1 
ATOM   300  C CG  . ASN A 1 38  ? 29.419  20.428  14.024  1.000 62.395  0 38  ASN A CG  1 
ATOM   301  O OD1 . ASN A 1 38  ? 29.367  21.062  15.084  1.000 64.751  0 38  ASN A OD1 1 
ATOM   302  N ND2 . ASN A 1 38  ? 30.451  19.656  13.693  1.000 62.459  0 38  ASN A ND2 1 
ATOM   303  N N   . SER A 1 39  ? 27.444  21.310  9.656   1.000 69.463  0 39  SER A N   1 
ATOM   304  C CA  . SER A 1 39  ? 26.430  21.157  8.635   1.000 61.186  0 39  SER A CA  1 
ATOM   305  C C   . SER A 1 39  ? 26.972  20.231  7.549   1.000 61.406  0 39  SER A C   1 
ATOM   306  O O   . SER A 1 39  ? 28.164  19.905  7.540   1.000 64.652  0 39  SER A O   1 
ATOM   307  C CB  . SER A 1 39  ? 25.998  22.505  8.094   1.000 70.093  0 39  SER A CB  1 
ATOM   308  O OG  . SER A 1 39  ? 25.291  23.253  9.078   1.000 64.833  0 39  SER A OG  1 
ATOM   309  N N   . TYR A 1 40  ? 26.067  19.731  6.698   1.000 58.443  0 40  TYR A N   1 
ATOM   310  C CA  . TYR A 1 40  ? 26.459  18.829  5.636   1.000 62.925  0 40  TYR A CA  1 
ATOM   311  C C   . TYR A 1 40  ? 26.501  19.599  4.329   1.000 65.751  0 40  TYR A C   1 
ATOM   312  O O   . TYR A 1 40  ? 25.457  20.025  3.828   1.000 63.311  0 40  TYR A O   1 
ATOM   313  C CB  . TYR A 1 40  ? 25.539  17.623  5.448   1.000 64.269  0 40  TYR A CB  1 
ATOM   314  C CG  . TYR A 1 40  ? 26.017  16.563  4.453   1.000 56.731  0 40  TYR A CG  1 
ATOM   315  C CD1 . TYR A 1 40  ? 25.614  16.614  3.142   1.000 57.487  0 40  TYR A CD1 1 
ATOM   316  C CD2 . TYR A 1 40  ? 26.785  15.466  4.838   1.000 64.859  0 40  TYR A CD2 1 
ATOM   317  C CE1 . TYR A 1 40  ? 25.985  15.646  2.230   1.000 72.884  0 40  TYR A CE1 1 
ATOM   318  C CE2 . TYR A 1 40  ? 27.159  14.478  3.940   1.000 69.153  0 40  TYR A CE2 1 
ATOM   319  C CZ  . TYR A 1 40  ? 26.748  14.570  2.625   1.000 69.250  0 40  TYR A CZ  1 
ATOM   320  O OH  . TYR A 1 40  ? 27.110  13.697  1.651   1.000 70.941  0 40  TYR A OH  1 
ATOM   321  N N   . VAL A 1 41  ? 27.723  19.745  3.815   1.000 68.857  0 41  VAL A N   1 
ATOM   322  C CA  . VAL A 1 41  ? 27.925  20.288  2.487   1.000 66.283  0 41  VAL A CA  1 
ATOM   323  C C   . VAL A 1 41  ? 28.278  19.155  1.540   1.000 58.718  0 41  VAL A C   1 
ATOM   324  O O   . VAL A 1 41  ? 29.336  18.563  1.672   1.000 62.037  0 41  VAL A O   1 
ATOM   325  C CB  . VAL A 1 41  ? 29.045  21.341  2.520   1.000 70.959  0 41  VAL A CB  1 
ATOM   326  C CG1 . VAL A 1 41  ? 29.336  21.857  1.119   1.000 76.589  0 41  VAL A CG1 1 
ATOM   327  C CG2 . VAL A 1 41  ? 28.696  22.499  3.462   1.000 64.877  0 41  VAL A CG2 1 
ATOM   328  N N   . PRO A 1 42  ? 27.418  18.835  0.560   1.000 61.983  0 42  PRO A N   1 
ATOM   329  C CA  . PRO A 1 42  ? 27.667  17.729  -0.362  1.000 67.595  0 42  PRO A CA  1 
ATOM   330  C C   . PRO A 1 42  ? 29.035  17.712  -1.033  1.000 75.783  0 42  PRO A C   1 
ATOM   331  O O   . PRO A 1 42  ? 29.694  16.668  -1.079  1.000 67.471  0 42  PRO A O   1 
ATOM   332  C CB  . PRO A 1 42  ? 26.534  17.935  -1.382  1.000 64.702  0 42  PRO A CB  1 
ATOM   333  C CG  . PRO A 1 42  ? 25.432  18.410  -0.500  1.000 67.140  0 42  PRO A CG  1 
ATOM   334  C CD  . PRO A 1 42  ? 26.121  19.477  0.323   1.000 70.041  0 42  PRO A CD  1 
ATOM   335  N N   . LEU A 1 43  ? 29.458  18.872  -1.549  1.000 74.440  0 43  LEU A N   1 
ATOM   336  C CA  . LEU A 1 43  ? 30.655  18.915  -2.367  1.000 70.525  0 43  LEU A CA  1 
ATOM   337  C C   . LEU A 1 43  ? 31.879  18.521  -1.543  1.000 67.884  0 43  LEU A C   1 
ATOM   338  O O   . LEU A 1 43  ? 32.827  17.979  -2.085  1.000 81.311  0 43  LEU A O   1 
ATOM   339  C CB  . LEU A 1 43  ? 30.715  20.310  -2.976  1.000 71.350  0 43  LEU A CB  1 
ATOM   340  C CG  . LEU A 1 43  ? 31.061  20.442  -4.462  1.000 80.852  0 43  LEU A CG  1 
ATOM   341  C CD1 . LEU A 1 43  ? 30.545  19.343  -5.351  1.000 83.748  0 43  LEU A CD1 1 
ATOM   342  C CD2 . LEU A 1 43  ? 30.500  21.764  -4.947  1.000 89.145  0 43  LEU A CD2 1 
ATOM   343  N N   . ASP A 1 44  ? 31.820  18.698  -0.220  1.000 80.740  0 44  ASP A N   1 
ATOM   344  C CA  . ASP A 1 44  ? 32.898  18.287  0.679   1.000 87.270  0 44  ASP A CA  1 
ATOM   345  C C   . ASP A 1 44  ? 32.713  16.848  1.164   1.000 70.954  0 44  ASP A C   1 
ATOM   346  O O   . ASP A 1 44  ? 33.476  16.401  1.999   1.000 85.770  0 44  ASP A O   1 
ATOM   347  C CB  . ASP A 1 44  ? 33.027  19.176  1.919   1.000 84.145  0 44  ASP A CB  1 
ATOM   348  C CG  . ASP A 1 44  ? 32.980  20.686  1.687   1.000 87.038  0 44  ASP A CG  1 
ATOM   349  O OD1 . ASP A 1 44  ? 33.370  21.111  0.573   1.000 90.949  0 44  ASP A OD1 1 
ATOM   350  O OD2 . ASP A 1 44  ? 32.484  21.430  2.585   1.000 79.704  0 44  ASP A OD2 1 
ATOM   351  N N   . ASN A 1 45  ? 31.724  16.113  0.658   1.000 73.408  0 45  ASN A N   1 
ATOM   352  C CA  . ASN A 1 45  ? 31.385  14.802  1.198   1.000 72.062  0 45  ASN A CA  1 
ATOM   353  C C   . ASN A 1 45  ? 31.123  13.770  0.093   1.000 67.194  0 45  ASN A C   1 
ATOM   354  O O   . ASN A 1 45  ? 30.474  12.761  0.342   1.000 66.940  0 45  ASN A O   1 
ATOM   355  C CB  . ASN A 1 45  ? 30.153  14.886  2.104   1.000 79.570  0 45  ASN A CB  1 
ATOM   356  C CG  . ASN A 1 45  ? 30.418  15.644  3.382   1.000 75.877  0 45  ASN A CG  1 
ATOM   357  O OD1 . ASN A 1 45  ? 30.045  16.820  3.502   1.000 83.386  0 45  ASN A OD1 1 
ATOM   358  N ND2 . ASN A 1 45  ? 31.078  15.000  4.332   1.000 78.848  0 45  ASN A ND2 1 
ATOM   359  N N   . GLN A 1 46  ? 31.615  14.005  -1.130  1.000 81.685  0 46  GLN A N   1 
ATOM   360  C CA  . GLN A 1 46  ? 31.525  13.009  -2.191  1.000 71.341  0 46  GLN A CA  1 
ATOM   361  C C   . GLN A 1 46  ? 32.411  11.839  -1.780  1.000 62.951  0 46  GLN A C   1 
ATOM   362  O O   . GLN A 1 46  ? 33.303  12.015  -0.964  1.000 64.203  0 46  GLN A O   1 
ATOM   363  C CB  . GLN A 1 46  ? 31.923  13.595  -3.546  1.000 76.121  0 46  GLN A CB  1 
ATOM   364  C CG  . GLN A 1 46  ? 31.219  14.905  -3.882  1.000 85.423  0 46  GLN A CG  1 
ATOM   365  C CD  . GLN A 1 46  ? 29.798  14.696  -4.355  1.000 96.979  0 46  GLN A CD  1 
ATOM   366  O OE1 . GLN A 1 46  ? 29.574  14.457  -5.551  1.000 96.660  0 46  GLN A OE1 1 
ATOM   367  N NE2 . GLN A 1 46  ? 28.841  14.789  -3.427  1.000 93.602  0 46  GLN A NE2 1 
ATOM   368  N N   . TYR A 1 47  ? 32.103  10.644  -2.266  1.000 63.002  0 47  TYR A N   1 
ATOM   369  C CA  . TYR A 1 47  ? 32.854  9.435   -1.952  1.000 74.115  0 47  TYR A CA  1 
ATOM   370  C C   . TYR A 1 47  ? 34.330  9.603   -2.318  1.000 72.925  0 47  TYR A C   1 
ATOM   371  O O   . TYR A 1 47  ? 34.662  10.002  -3.440  1.000 65.291  0 47  TYR A O   1 
ATOM   372  C CB  . TYR A 1 47  ? 32.316  8.210   -2.713  1.000 78.682  0 47  TYR A CB  1 
ATOM   373  C CG  . TYR A 1 47  ? 32.866  6.873   -2.226  1.000 79.380  0 47  TYR A CG  1 
ATOM   374  C CD1 . TYR A 1 47  ? 32.862  6.551   -0.866  1.000 78.189  0 47  TYR A CD1 1 
ATOM   375  C CD2 . TYR A 1 47  ? 33.384  5.923   -3.112  1.000 86.513  0 47  TYR A CD2 1 
ATOM   376  C CE1 . TYR A 1 47  ? 33.353  5.338   -0.399  1.000 81.333  0 47  TYR A CE1 1 
ATOM   377  C CE2 . TYR A 1 47  ? 33.854  4.689   -2.661  1.000 79.246  0 47  TYR A CE2 1 
ATOM   378  C CZ  . TYR A 1 47  ? 33.864  4.416   -1.298  1.000 77.564  0 47  TYR A CZ  1 
ATOM   379  O OH  . TYR A 1 47  ? 34.330  3.260   -0.760  1.000 81.833  0 47  TYR A OH  1 
ATOM   380  N N   . LYS A 1 48  ? 35.211  9.283   -1.354  1.000 81.069  0 48  LYS A N   1 
ATOM   381  C CA  . LYS A 1 48  ? 36.653  9.339   -1.553  1.000 86.705  0 48  LYS A CA  1 
ATOM   382  C C   . LYS A 1 48  ? 37.098  10.744  -1.944  1.000 92.868  0 48  LYS A C   1 
ATOM   383  O O   . LYS A 1 48  ? 38.082  10.899  -2.641  1.000 106.985 0 48  LYS A O   1 
ATOM   384  C CB  . LYS A 1 48  ? 37.061  8.318   -2.626  1.000 82.422  0 48  LYS A CB  1 
ATOM   385  C CG  . LYS A 1 48  ? 37.253  6.898   -2.114  1.000 82.884  0 48  LYS A CG  1 
ATOM   386  C CD  . LYS A 1 48  ? 37.462  5.866   -3.222  1.000 85.952  0 48  LYS A CD  1 
ATOM   387  C CE  . LYS A 1 48  ? 37.918  4.540   -2.688  1.000 91.605  0 48  LYS A CE  1 
ATOM   388  N NZ  . LYS A 1 48  ? 37.632  3.517   -3.682  1.000 95.253  0 48  LYS A NZ  1 
ATOM   389  N N   . GLY A 1 49  ? 36.344  11.770  -1.555  1.000 100.905 0 49  GLY A N   1 
ATOM   390  C CA  . GLY A 1 49  ? 36.681  13.153  -1.857  1.000 93.044  0 49  GLY A CA  1 
ATOM   391  C C   . GLY A 1 49  ? 36.748  13.474  -3.349  1.000 86.359  0 49  GLY A C   1 
ATOM   392  O O   . GLY A 1 49  ? 37.259  14.529  -3.722  1.000 106.169 0 49  GLY A O   1 
ATOM   393  N N   . ILE A 1 50  ? 36.199  12.623  -4.215  1.000 86.826  0 50  ILE A N   1 
ATOM   394  C CA  . ILE A 1 50  ? 36.422  12.799  -5.642  1.000 96.656  0 50  ILE A CA  1 
ATOM   395  C C   . ILE A 1 50  ? 35.101  13.173  -6.305  1.000 86.219  0 50  ILE A C   1 
ATOM   396  O O   . ILE A 1 50  ? 34.111  12.485  -6.085  1.000 83.013  0 50  ILE A O   1 
ATOM   397  C CB  . ILE A 1 50  ? 37.070  11.539  -6.282  1.000 111.642 0 50  ILE A CB  1 
ATOM   398  C CG1 . ILE A 1 50  ? 36.055  10.445  -6.665  1.000 103.209 0 50  ILE A CG1 1 
ATOM   399  C CG2 . ILE A 1 50  ? 38.231  10.976  -5.448  1.000 98.652  0 50  ILE A CG2 1 
ATOM   400  C CD1 . ILE A 1 50  ? 35.470  10.640  -8.052  1.000 104.139 0 50  ILE A CD1 1 
ATOM   401  N N   . ARG A 1 51  ? 35.121  14.198  -7.175  1.000 97.693  0 51  ARG A N   1 
ATOM   402  C CA  . ARG A 1 51  ? 33.956  14.618  -7.959  1.000 103.215 0 51  ARG A CA  1 
ATOM   403  C C   . ARG A 1 51  ? 34.090  14.259  -9.444  1.000 90.151  0 51  ARG A C   1 
ATOM   404  O O   . ARG A 1 51  ? 35.156  14.446  -10.018 1.000 107.940 0 51  ARG A O   1 
ATOM   405  C CB  . ARG A 1 51  ? 33.853  16.147  -7.948  1.000 119.186 0 51  ARG A CB  1 
ATOM   406  C CG  . ARG A 1 51  ? 34.300  16.877  -6.688  1.000 129.529 0 51  ARG A CG  1 
ATOM   407  C CD  . ARG A 1 51  ? 34.610  18.345  -6.976  1.000 131.556 0 51  ARG A CD  1 
ATOM   408  N NE  . ARG A 1 51  ? 33.736  18.960  -7.992  1.000 121.635 0 51  ARG A NE  1 
ATOM   409  C CZ  . ARG A 1 51  ? 33.465  20.264  -8.072  1.000 90.658  0 51  ARG A CZ  1 
ATOM   410  N NH1 . ARG A 1 51  ? 34.012  21.089  -7.190  1.000 89.070  0 51  ARG A NH1 1 
ATOM   411  N NH2 . ARG A 1 51  ? 32.633  20.722  -8.998  1.000 73.239  0 51  ARG A NH2 1 
ATOM   412  N N   . VAL A 1 52  ? 32.994  13.836  -10.093 1.000 90.460  0 52  VAL A N   1 
ATOM   413  C CA  . VAL A 1 52  ? 33.044  13.263  -11.439 1.000 105.392 0 52  VAL A CA  1 
ATOM   414  C C   . VAL A 1 52  ? 33.227  14.341  -12.512 1.000 101.547 0 52  VAL A C   1 
ATOM   415  O O   . VAL A 1 52  ? 33.339  14.037  -13.706 1.000 87.940  0 52  VAL A O   1 
ATOM   416  C CB  . VAL A 1 52  ? 31.825  12.391  -11.808 1.000 109.565 0 52  VAL A CB  1 
ATOM   417  C CG1 . VAL A 1 52  ? 31.632  11.279  -10.797 1.000 111.208 0 52  VAL A CG1 1 
ATOM   418  C CG2 . VAL A 1 52  ? 30.541  13.197  -11.972 1.000 116.804 0 52  VAL A CG2 1 
ATOM   419  N N   . ASP A 1 53  ? 33.197  15.616  -12.130 1.000 93.840  0 53  ASP A N   1 
ATOM   420  C CA  . ASP A 1 53  ? 33.555  16.646  -13.099 1.000 108.701 0 53  ASP A CA  1 
ATOM   421  C C   . ASP A 1 53  ? 35.083  16.586  -13.256 1.000 105.633 0 53  ASP A C   1 
ATOM   422  O O   . ASP A 1 53  ? 35.582  16.714  -14.369 1.000 85.552  0 53  ASP A O   1 
ATOM   423  C CB  . ASP A 1 53  ? 32.834  17.977  -12.843 1.000 85.533  0 53  ASP A CB  1 
ATOM   424  C CG  . ASP A 1 53  ? 33.054  18.607  -11.477 1.000 87.407  0 53  ASP A CG  1 
ATOM   425  O OD1 . ASP A 1 53  ? 32.566  18.057  -10.457 1.000 94.101  0 53  ASP A OD1 1 
ATOM   426  O OD2 . ASP A 1 53  ? 33.784  19.608  -11.427 1.000 109.262 0 53  ASP A OD2 1 
ATOM   427  N N   . GLU A 1 54  ? 35.800  16.306  -12.152 1.000 90.324  0 54  GLU A N   1 
ATOM   428  C CA  . GLU A 1 54  ? 37.256  16.372  -12.123 1.000 93.537  0 54  GLU A CA  1 
ATOM   429  C C   . GLU A 1 54  ? 37.865  15.005  -12.459 1.000 95.974  0 54  GLU A C   1 
ATOM   430  O O   . GLU A 1 54  ? 39.039  14.932  -12.836 1.000 83.803  0 54  GLU A O   1 
ATOM   431  C CB  . GLU A 1 54  ? 37.797  16.905  -10.790 1.000 76.146  0 54  GLU A CB  1 
ATOM   432  C CG  . GLU A 1 54  ? 36.927  18.018  -10.217 1.000 89.060  0 54  GLU A CG  1 
ATOM   433  C CD  . GLU A 1 54  ? 37.559  19.117  -9.396  1.000 97.278  0 54  GLU A CD  1 
ATOM   434  O OE1 . GLU A 1 54  ? 38.303  18.737  -8.475  1.000 90.162  0 54  GLU A OE1 1 
ATOM   435  O OE2 . GLU A 1 54  ? 37.247  20.318  -9.647  1.000 98.836  0 54  GLU A OE2 1 
ATOM   436  N N   . HIS A 1 55  ? 37.082  13.929  -12.301 1.000 78.277  0 55  HIS A N   1 
ATOM   437  C CA  . HIS A 1 55  ? 37.569  12.577  -12.544 1.000 69.327  0 55  HIS A CA  1 
ATOM   438  C C   . HIS A 1 55  ? 36.478  11.790  -13.266 1.000 61.383  0 55  HIS A C   1 
ATOM   439  O O   . HIS A 1 55  ? 35.834  10.948  -12.672 1.000 65.955  0 55  HIS A O   1 
ATOM   440  C CB  . HIS A 1 55  ? 38.055  11.907  -11.249 1.000 64.658  0 55  HIS A CB  1 
ATOM   441  C CG  . HIS A 1 55  ? 39.049  12.689  -10.448 1.000 74.140  0 55  HIS A CG  1 
ATOM   442  N ND1 . HIS A 1 55  ? 40.412  12.655  -10.653 1.000 79.080  0 55  HIS A ND1 1 
ATOM   443  C CD2 . HIS A 1 55  ? 38.872  13.523  -9.402  1.000 86.991  0 55  HIS A CD2 1 
ATOM   444  C CE1 . HIS A 1 55  ? 41.025  13.441  -9.759  1.000 74.360  0 55  HIS A CE1 1 
ATOM   445  N NE2 . HIS A 1 55  ? 40.113  13.979  -8.987  1.000 82.866  0 55  HIS A NE2 1 
ATOM   446  N N   . PRO A 1 56  ? 36.231  12.044  -14.566 1.000 63.801  0 56  PRO A N   1 
ATOM   447  C CA  . PRO A 1 56  ? 35.143  11.399  -15.307 1.000 75.946  0 56  PRO A CA  1 
ATOM   448  C C   . PRO A 1 56  ? 35.173  9.880   -15.411 1.000 86.650  0 56  PRO A C   1 
ATOM   449  O O   . PRO A 1 56  ? 34.247  9.276   -15.971 1.000 82.846  0 56  PRO A O   1 
ATOM   450  C CB  . PRO A 1 56  ? 35.219  12.032  -16.728 1.000 82.503  0 56  PRO A CB  1 
ATOM   451  C CG  . PRO A 1 56  ? 35.970  13.333  -16.535 1.000 83.837  0 56  PRO A CG  1 
ATOM   452  C CD  . PRO A 1 56  ? 36.912  13.066  -15.363 1.000 72.230  0 56  PRO A CD  1 
ATOM   453  N N   . GLU A 1 57  ? 36.251  9.268   -14.909 1.000 82.942  0 57  GLU A N   1 
ATOM   454  C CA  . GLU A 1 57  ? 36.335  7.819   -14.875 1.000 77.536  0 57  GLU A CA  1 
ATOM   455  C C   . GLU A 1 57  ? 35.284  7.262   -13.923 1.000 78.310  0 57  GLU A C   1 
ATOM   456  O O   . GLU A 1 57  ? 34.968  6.078   -13.990 1.000 80.615  0 57  GLU A O   1 
ATOM   457  C CB  . GLU A 1 57  ? 37.731  7.309   -14.499 1.000 85.024  0 57  GLU A CB  1 
ATOM   458  C CG  . GLU A 1 57  ? 38.301  7.735   -13.143 1.000 76.252  0 57  GLU A CG  1 
ATOM   459  C CD  . GLU A 1 57  ? 39.222  8.956   -13.132 1.000 76.970  0 57  GLU A CD  1 
ATOM   460  O OE1 . GLU A 1 57  ? 39.102  9.846   -13.998 1.000 83.191  0 57  GLU A OE1 1 
ATOM   461  O OE2 . GLU A 1 57  ? 40.109  9.001   -12.265 1.000 71.394  0 57  GLU A OE2 1 
ATOM   462  N N   . TYR A 1 58  ? 34.760  8.112   -13.020 1.000 77.420  0 58  TYR A N   1 
ATOM   463  C CA  . TYR A 1 58  ? 33.844  7.644   -11.992 1.000 81.701  0 58  TYR A CA  1 
ATOM   464  C C   . TYR A 1 58  ? 32.384  7.703   -12.448 1.000 78.926  0 58  TYR A C   1 
ATOM   465  O O   . TYR A 1 58  ? 31.497  7.284   -11.710 1.000 74.710  0 58  TYR A O   1 
ATOM   466  C CB  . TYR A 1 58  ? 34.119  8.438   -10.724 1.000 69.855  0 58  TYR A CB  1 
ATOM   467  C CG  . TYR A 1 58  ? 35.326  7.944   -9.949  1.000 85.847  0 58  TYR A CG  1 
ATOM   468  C CD1 . TYR A 1 58  ? 35.229  6.899   -9.034  1.000 94.792  0 58  TYR A CD1 1 
ATOM   469  C CD2 . TYR A 1 58  ? 36.553  8.560   -10.103 1.000 87.752  0 58  TYR A CD2 1 
ATOM   470  C CE1 . TYR A 1 58  ? 36.327  6.479   -8.299  1.000 96.269  0 58  TYR A CE1 1 
ATOM   471  C CE2 . TYR A 1 58  ? 37.646  8.173   -9.351  1.000 90.165  0 58  TYR A CE2 1 
ATOM   472  C CZ  . TYR A 1 58  ? 37.541  7.122   -8.461  1.000 90.368  0 58  TYR A CZ  1 
ATOM   473  O OH  . TYR A 1 58  ? 38.665  6.754   -7.775  1.000 93.668  0 58  TYR A OH  1 
ATOM   474  N N   . LEU A 1 59  ? 32.157  8.155   -13.680 1.000 82.690  0 59  LEU A N   1 
ATOM   475  C CA  . LEU A 1 59  ? 30.830  8.260   -14.269 1.000 97.301  0 59  LEU A CA  1 
ATOM   476  C C   . LEU A 1 59  ? 30.131  6.907   -14.321 1.000 85.918  0 59  LEU A C   1 
ATOM   477  O O   . LEU A 1 59  ? 28.905  6.866   -14.406 1.000 84.488  0 59  LEU A O   1 
ATOM   478  C CB  . LEU A 1 59  ? 30.851  8.828   -15.696 1.000 101.523 0 59  LEU A CB  1 
ATOM   479  C CG  . LEU A 1 59  ? 31.058  10.340  -15.855 1.000 105.563 0 59  LEU A CG  1 
ATOM   480  C CD1 . LEU A 1 59  ? 31.212  10.692  -17.322 1.000 91.103  0 59  LEU A CD1 1 
ATOM   481  C CD2 . LEU A 1 59  ? 29.945  11.170  -15.230 1.000 108.236 0 59  LEU A CD2 1 
ATOM   482  N N   . HIS A 1 60  ? 30.897  5.812   -14.417 1.000 106.666 0 60  HIS A N   1 
ATOM   483  C CA  . HIS A 1 60  ? 30.263  4.516   -14.587 1.000 101.167 0 60  HIS A CA  1 
ATOM   484  C C   . HIS A 1 60  ? 30.512  3.644   -13.359 1.000 83.305  0 60  HIS A C   1 
ATOM   485  O O   . HIS A 1 60  ? 30.036  2.517   -13.384 1.000 93.838  0 60  HIS A O   1 
ATOM   486  C CB  . HIS A 1 60  ? 30.596  3.892   -15.956 1.000 97.871  0 60  HIS A CB  1 
ATOM   487  C CG  . HIS A 1 60  ? 29.887  4.484   -17.161 1.000 99.530  0 60  HIS A CG  1 
ATOM   488  N ND1 . HIS A 1 60  ? 30.445  5.475   -17.957 1.000 108.142 0 60  HIS A ND1 1 
ATOM   489  C CD2 . HIS A 1 60  ? 28.679  4.216   -17.735 1.000 94.411  0 60  HIS A CD2 1 
ATOM   490  C CE1 . HIS A 1 60  ? 29.618  5.787   -18.970 1.000 85.349  0 60  HIS A CE1 1 
ATOM   491  N NE2 . HIS A 1 60  ? 28.531  5.045   -18.849 1.000 83.518  0 60  HIS A NE2 1 
ATOM   492  N N   . ASP A 1 61  ? 31.144  4.196   -12.297 1.000 76.913  0 61  ASP A N   1 
ATOM   493  C CA  . ASP A 1 61  ? 31.478  3.499   -11.051 1.000 69.862  0 61  ASP A CA  1 
ATOM   494  C C   . ASP A 1 61  ? 30.276  3.457   -10.089 1.000 70.187  0 61  ASP A C   1 
ATOM   495  O O   . ASP A 1 61  ? 29.842  4.491   -9.601  1.000 93.055  0 61  ASP A O   1 
ATOM   496  C CB  . ASP A 1 61  ? 32.726  4.090   -10.400 1.000 65.488  0 61  ASP A CB  1 
ATOM   497  C CG  . ASP A 1 61  ? 33.176  3.442   -9.085  1.000 75.137  0 61  ASP A CG  1 
ATOM   498  O OD1 . ASP A 1 61  ? 32.455  2.555   -8.629  1.000 68.355  0 61  ASP A OD1 1 
ATOM   499  O OD2 . ASP A 1 61  ? 34.239  3.825   -8.485  1.000 76.538  0 61  ASP A OD2 1 
ATOM   500  N N   . LYS A 1 62  ? 29.765  2.254   -9.782  1.000 67.838  0 62  LYS A N   1 
ATOM   501  C CA  . LYS A 1 62  ? 28.525  2.081   -9.032  1.000 72.663  0 62  LYS A CA  1 
ATOM   502  C C   . LYS A 1 62  ? 28.776  2.143   -7.525  1.000 67.911  0 62  LYS A C   1 
ATOM   503  O O   . LYS A 1 62  ? 27.881  2.436   -6.730  1.000 64.188  0 62  LYS A O   1 
ATOM   504  C CB  . LYS A 1 62  ? 27.822  0.750   -9.320  1.000 67.544  0 62  LYS A CB  1 
ATOM   505  C CG  . LYS A 1 62  ? 27.276  0.633   -10.735 1.000 69.801  0 62  LYS A CG  1 
ATOM   506  C CD  . LYS A 1 62  ? 26.593  -0.722  -10.900 1.000 76.532  0 62  LYS A CD  1 
ATOM   507  C CE  . LYS A 1 62  ? 25.880  -0.971  -12.184 1.000 72.792  0 62  LYS A CE  1 
ATOM   508  N NZ  . LYS A 1 62  ? 26.812  -0.885  -13.301 1.000 80.489  0 62  LYS A NZ  1 
ATOM   509  N N   . VAL A 1 63  ? 30.001  1.858   -7.120  1.000 67.525  0 63  VAL A N   1 
ATOM   510  C CA  . VAL A 1 63  ? 30.373  2.016   -5.727  1.000 71.050  0 63  VAL A CA  1 
ATOM   511  C C   . VAL A 1 63  ? 30.381  3.508   -5.386  1.000 76.129  0 63  VAL A C   1 
ATOM   512  O O   . VAL A 1 63  ? 29.808  3.920   -4.375  1.000 84.217  0 63  VAL A O   1 
ATOM   513  C CB  . VAL A 1 63  ? 31.729  1.319   -5.468  1.000 74.774  0 63  VAL A CB  1 
ATOM   514  C CG1 . VAL A 1 63  ? 32.267  1.578   -4.069  1.000 80.025  0 63  VAL A CG1 1 
ATOM   515  C CG2 . VAL A 1 63  ? 31.648  -0.183  -5.727  1.000 73.455  0 63  VAL A CG2 1 
ATOM   516  N N   . TRP A 1 64  ? 31.013  4.315   -6.249  1.000 76.528  0 64  TRP A N   1 
ATOM   517  C CA  . TRP A 1 64  ? 31.087  5.740   -6.008  1.000 79.328  0 64  TRP A CA  1 
ATOM   518  C C   . TRP A 1 64  ? 29.675  6.340   -5.920  1.000 73.490  0 64  TRP A C   1 
ATOM   519  O O   . TRP A 1 64  ? 29.405  7.132   -5.028  1.000 71.997  0 64  TRP A O   1 
ATOM   520  C CB  . TRP A 1 64  ? 31.957  6.437   -7.069  1.000 78.029  0 64  TRP A CB  1 
ATOM   521  C CG  . TRP A 1 64  ? 31.914  7.932   -6.911  1.000 72.578  0 64  TRP A CG  1 
ATOM   522  C CD1 . TRP A 1 64  ? 32.667  8.718   -6.082  1.000 72.909  0 64  TRP A CD1 1 
ATOM   523  C CD2 . TRP A 1 64  ? 30.936  8.795   -7.523  1.000 55.312  0 64  TRP A CD2 1 
ATOM   524  N NE1 . TRP A 1 64  ? 32.255  10.026  -6.177  1.000 66.851  0 64  TRP A NE1 1 
ATOM   525  C CE2 . TRP A 1 64  ? 31.187  10.093  -7.040  1.000 58.360  0 64  TRP A CE2 1 
ATOM   526  C CE3 . TRP A 1 64  ? 29.879  8.576   -8.414  1.000 65.998  0 64  TRP A CE3 1 
ATOM   527  C CZ2 . TRP A 1 64  ? 30.403  11.168  -7.427  1.000 71.002  0 64  TRP A CZ2 1 
ATOM   528  C CZ3 . TRP A 1 64  ? 29.081  9.635   -8.776  1.000 73.555  0 64  TRP A CZ3 1 
ATOM   529  C CH2 . TRP A 1 64  ? 29.345  10.913  -8.280  1.000 79.021  0 64  TRP A CH2 1 
ATOM   530  N N   . ALA A 1 65  ? 28.790  5.964   -6.849  1.000 60.719  0 65  ALA A N   1 
ATOM   531  C CA  . ALA A 1 65  ? 27.419  6.451   -6.878  1.000 68.853  0 65  ALA A CA  1 
ATOM   532  C C   . ALA A 1 65  ? 26.602  6.029   -5.639  1.000 77.236  0 65  ALA A C   1 
ATOM   533  O O   . ALA A 1 65  ? 25.864  6.834   -5.071  1.000 74.051  0 65  ALA A O   1 
ATOM   534  C CB  . ALA A 1 65  ? 26.759  5.975   -8.150  1.000 56.176  0 65  ALA A CB  1 
ATOM   535  N N   . THR A 1 66  ? 26.698  4.756   -5.251  1.000 68.016  0 66  THR A N   1 
ATOM   536  C CA  . THR A 1 66  ? 25.992  4.228   -4.092  1.000 70.276  0 66  THR A CA  1 
ATOM   537  C C   . THR A 1 66  ? 26.374  4.997   -2.824  1.000 66.101  0 66  THR A C   1 
ATOM   538  O O   . THR A 1 66  ? 25.504  5.482   -2.095  1.000 72.389  0 66  THR A O   1 
ATOM   539  C CB  . THR A 1 66  ? 26.288  2.732   -3.953  1.000 69.376  0 66  THR A CB  1 
ATOM   540  O OG1 . THR A 1 66  ? 25.657  2.088   -5.056  1.000 58.559  0 66  THR A OG1 1 
ATOM   541  C CG2 . THR A 1 66  ? 25.717  2.118   -2.690  1.000 64.102  0 66  THR A CG2 1 
ATOM   542  N N   . ALA A 1 67  ? 27.677  5.130   -2.570  1.000 64.138  0 67  ALA A N   1 
ATOM   543  C CA  . ALA A 1 67  ? 28.138  5.778   -1.345  1.000 64.036  0 67  ALA A CA  1 
ATOM   544  C C   . ALA A 1 67  ? 27.822  7.275   -1.345  1.000 65.062  0 67  ALA A C   1 
ATOM   545  O O   . ALA A 1 67  ? 27.431  7.844   -0.328  1.000 66.662  0 67  ALA A O   1 
ATOM   546  C CB  . ALA A 1 67  ? 29.608  5.558   -1.174  1.000 59.301  0 67  ALA A CB  1 
ATOM   547  N N   . THR A 1 68  ? 27.984  7.935   -2.493  1.000 59.765  0 68  THR A N   1 
ATOM   548  C CA  . THR A 1 68  ? 27.733  9.360   -2.549  1.000 61.865  0 68  THR A CA  1 
ATOM   549  C C   . THR A 1 68  ? 26.234  9.564   -2.342  1.000 65.445  0 68  THR A C   1 
ATOM   550  O O   . THR A 1 68  ? 25.831  10.396  -1.545  1.000 78.305  0 68  THR A O   1 
ATOM   551  C CB  . THR A 1 68  ? 28.241  9.964   -3.860  1.000 59.670  0 68  THR A CB  1 
ATOM   552  O OG1 . THR A 1 68  ? 29.648  9.812   -3.906  1.000 61.770  0 68  THR A OG1 1 
ATOM   553  C CG2 . THR A 1 68  ? 28.078  11.467  -3.945  1.000 61.365  0 68  THR A CG2 1 
ATOM   554  N N   . TYR A 1 69  ? 25.418  8.799   -3.058  1.000 64.159  0 69  TYR A N   1 
ATOM   555  C CA  . TYR A 1 69  ? 23.980  8.911   -2.914  1.000 68.711  0 69  TYR A CA  1 
ATOM   556  C C   . TYR A 1 69  ? 23.618  8.665   -1.451  1.000 64.212  0 69  TYR A C   1 
ATOM   557  O O   . TYR A 1 69  ? 22.865  9.431   -0.865  1.000 57.968  0 69  TYR A O   1 
ATOM   558  C CB  . TYR A 1 69  ? 23.259  7.974   -3.884  1.000 60.734  0 69  TYR A CB  1 
ATOM   559  C CG  . TYR A 1 69  ? 21.764  7.905   -3.636  1.000 65.480  0 69  TYR A CG  1 
ATOM   560  C CD1 . TYR A 1 69  ? 20.925  8.934   -4.043  1.000 67.358  0 69  TYR A CD1 1 
ATOM   561  C CD2 . TYR A 1 69  ? 21.197  6.817   -2.979  1.000 57.842  0 69  TYR A CD2 1 
ATOM   562  C CE1 . TYR A 1 69  ? 19.557  8.876   -3.816  1.000 74.628  0 69  TYR A CE1 1 
ATOM   563  C CE2 . TYR A 1 69  ? 19.835  6.759   -2.738  1.000 70.591  0 69  TYR A CE2 1 
ATOM   564  C CZ  . TYR A 1 69  ? 19.007  7.781   -3.170  1.000 77.601  0 69  TYR A CZ  1 
ATOM   565  O OH  . TYR A 1 69  ? 17.667  7.703   -2.918  1.000 73.439  0 69  TYR A OH  1 
ATOM   566  N N   . ASN A 1 70  ? 24.173  7.622   -0.844  1.000 56.145  0 70  ASN A N   1 
ATOM   567  C CA  . ASN A 1 70  ? 23.838  7.344   0.539   1.000 64.690  0 70  ASN A CA  1 
ATOM   568  C C   . ASN A 1 70  ? 24.272  8.464   1.482   1.000 70.895  0 70  ASN A C   1 
ATOM   569  O O   . ASN A 1 70  ? 23.576  8.804   2.434   1.000 76.386  0 70  ASN A O   1 
ATOM   570  C CB  . ASN A 1 70  ? 24.477  6.051   1.004   1.000 77.580  0 70  ASN A CB  1 
ATOM   571  C CG  . ASN A 1 70  ? 23.745  4.849   0.472   1.000 68.279  0 70  ASN A CG  1 
ATOM   572  O OD1 . ASN A 1 70  ? 22.675  4.968   -0.122  1.000 60.820  0 70  ASN A OD1 1 
ATOM   573  N ND2 . ASN A 1 70  ? 24.326  3.687   0.683   1.000 82.337  0 70  ASN A ND2 1 
ATOM   574  N N   . ASN A 1 71  ? 25.442  9.037   1.236   1.000 74.383  0 71  ASN A N   1 
ATOM   575  C CA  . ASN A 1 71  ? 25.980  10.034  2.145   1.000 63.813  0 71  ASN A CA  1 
ATOM   576  C C   . ASN A 1 71  ? 25.148  11.327  2.088   1.000 65.062  0 71  ASN A C   1 
ATOM   577  O O   . ASN A 1 71  ? 24.978  12.005  3.101   1.000 60.970  0 71  ASN A O   1 
ATOM   578  C CB  . ASN A 1 71  ? 27.459  10.229  1.831   1.000 67.305  0 71  ASN A CB  1 
ATOM   579  C CG  . ASN A 1 71  ? 28.284  10.695  3.005   1.000 69.268  0 71  ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 71  ? 29.335  11.286  2.768   1.000 68.734  0 71  ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 71  ? 27.783  10.605  4.231   1.000 78.307  0 71  ASN A ND2 1 
ATOM   582  N N   . ASP A 1 72  ? 24.612  11.651  0.900   1.000 60.728  0 72  ASP A N   1 
ATOM   583  C CA  . ASP A 1 72  ? 23.772  12.816  0.689   1.000 61.690  0 72  ASP A CA  1 
ATOM   584  C C   . ASP A 1 72  ? 22.451  12.640  1.450   1.000 61.943  0 72  ASP A C   1 
ATOM   585  O O   . ASP A 1 72  ? 22.019  13.530  2.183   1.000 66.660  0 72  ASP A O   1 
ATOM   586  C CB  . ASP A 1 72  ? 23.704  13.204  -0.787  1.000 62.618  0 72  ASP A CB  1 
ATOM   587  C CG  . ASP A 1 72  ? 24.940  13.877  -1.392  1.000 76.472  0 72  ASP A CG  1 
ATOM   588  O OD1 . ASP A 1 72  ? 25.982  14.038  -0.714  1.000 81.494  0 72  ASP A OD1 1 
ATOM   589  O OD2 . ASP A 1 72  ? 24.874  14.260  -2.560  1.000 95.095  0 72  ASP A OD2 1 
ATOM   590  N N   . LEU A 1 73  ? 21.829  11.470  1.330   1.000 61.252  0 73  LEU A N   1 
ATOM   591  C CA  . LEU A 1 73  ? 20.663  11.144  2.135   1.000 54.911  0 73  LEU A CA  1 
ATOM   592  C C   . LEU A 1 73  ? 20.994  11.252  3.613   1.000 60.734  0 73  LEU A C   1 
ATOM   593  O O   . LEU A 1 73  ? 20.252  11.868  4.374   1.000 69.498  0 73  LEU A O   1 
ATOM   594  C CB  . LEU A 1 73  ? 20.140  9.750   1.831   1.000 61.241  0 73  LEU A CB  1 
ATOM   595  C CG  . LEU A 1 73  ? 19.651  9.526   0.394   1.000 75.494  0 73  LEU A CG  1 
ATOM   596  C CD1 . LEU A 1 73  ? 18.724  8.316   0.408   1.000 73.264  0 73  LEU A CD1 1 
ATOM   597  C CD2 . LEU A 1 73  ? 18.976  10.754  -0.279  1.000 68.916  0 73  LEU A CD2 1 
ATOM   598  N N   . ASN A 1 74  ? 22.123  10.666  4.016   1.000 63.918  0 74  ASN A N   1 
ATOM   599  C CA  . ASN A 1 74  ? 22.526  10.709  5.411   1.000 60.766  0 74  ASN A CA  1 
ATOM   600  C C   . ASN A 1 74  ? 22.706  12.154  5.890   1.000 69.683  0 74  ASN A C   1 
ATOM   601  O O   . ASN A 1 74  ? 22.364  12.514  7.029   1.000 58.930  0 74  ASN A O   1 
ATOM   602  C CB  . ASN A 1 74  ? 23.796  9.922   5.572   1.000 63.378  0 74  ASN A CB  1 
ATOM   603  C CG  . ASN A 1 74  ? 24.249  9.915   6.996   1.000 68.092  0 74  ASN A CG  1 
ATOM   604  O OD1 . ASN A 1 74  ? 25.336  10.430  7.309   1.000 79.875  0 74  ASN A OD1 1 
ATOM   605  N ND2 . ASN A 1 74  ? 23.423  9.301   7.822   1.000 72.281  0 74  ASN A ND2 1 
ATOM   606  N N   . GLY A 1 75  ? 23.228  12.989  4.994   1.000 64.978  0 75  GLY A N   1 
ATOM   607  C CA  . GLY A 1 75  ? 23.330  14.409  5.265   1.000 74.514  0 75  GLY A CA  1 
ATOM   608  C C   . GLY A 1 75  ? 21.981  15.063  5.559   1.000 71.599  0 75  GLY A C   1 
ATOM   609  O O   . GLY A 1 75  ? 21.874  15.866  6.476   1.000 74.467  0 75  GLY A O   1 
ATOM   610  N N   . ILE A 1 76  ? 20.947  14.701  4.799   1.000 67.917  0 76  ILE A N   1 
ATOM   611  C CA  . ILE A 1 76  ? 19.635  15.309  4.980   1.000 74.909  0 76  ILE A CA  1 
ATOM   612  C C   . ILE A 1 76  ? 19.020  14.861  6.305   1.000 71.692  0 76  ILE A C   1 
ATOM   613  O O   . ILE A 1 76  ? 18.546  15.697  7.084   1.000 71.257  0 76  ILE A O   1 
ATOM   614  C CB  . ILE A 1 76  ? 18.727  15.013  3.773   1.000 63.874  0 76  ILE A CB  1 
ATOM   615  C CG1 . ILE A 1 76  ? 19.333  15.588  2.505   1.000 67.430  0 76  ILE A CG1 1 
ATOM   616  C CG2 . ILE A 1 76  ? 17.320  15.554  3.991   1.000 65.196  0 76  ILE A CG2 1 
ATOM   617  C CD1 . ILE A 1 76  ? 18.632  15.182  1.227   1.000 67.736  0 76  ILE A CD1 1 
ATOM   618  N N   . LYS A 1 77  ? 19.086  13.553  6.568   1.000 68.257  0 77  LYS A N   1 
ATOM   619  C CA  . LYS A 1 77  ? 18.342  12.979  7.672   1.000 73.012  0 77  LYS A CA  1 
ATOM   620  C C   . LYS A 1 77  ? 18.979  13.302  9.023   1.000 63.422  0 77  LYS A C   1 
ATOM   621  O O   . LYS A 1 77  ? 18.261  13.348  10.006  1.000 75.539  0 77  LYS A O   1 
ATOM   622  C CB  . LYS A 1 77  ? 18.082  11.487  7.458   1.000 78.759  0 77  LYS A CB  1 
ATOM   623  C CG  . LYS A 1 77  ? 19.050  10.543  8.097   1.000 74.848  0 77  LYS A CG  1 
ATOM   624  C CD  . LYS A 1 77  ? 18.885  9.112   7.611   1.000 70.656  0 77  LYS A CD  1 
ATOM   625  C CE  . LYS A 1 77  ? 20.035  8.355   8.199   1.000 74.560  0 77  LYS A CE  1 
ATOM   626  N NZ  . LYS A 1 77  ? 20.255  7.020   7.669   1.000 71.534  0 77  LYS A NZ  1 
ATOM   627  N N   . THR A 1 78  ? 20.285  13.553  9.082   1.000 61.993  0 78  THR A N   1 
ATOM   628  C CA  . THR A 1 78  ? 20.933  13.828  10.358  1.000 66.253  0 78  THR A CA  1 
ATOM   629  C C   . THR A 1 78  ? 21.152  15.327  10.608  1.000 68.468  0 78  THR A C   1 
ATOM   630  O O   . THR A 1 78  ? 21.887  15.667  11.526  1.000 63.175  0 78  THR A O   1 
ATOM   631  C CB  . THR A 1 78  ? 22.280  13.101  10.427  1.000 61.530  0 78  THR A CB  1 
ATOM   632  O OG1 . THR A 1 78  ? 23.103  13.648  9.398   1.000 65.118  0 78  THR A OG1 1 
ATOM   633  C CG2 . THR A 1 78  ? 22.110  11.598  10.337  1.000 62.546  0 78  THR A CG2 1 
ATOM   634  N N   . ASN A 1 79  ? 20.592  16.214  9.780   1.000 70.816  0 79  ASN A N   1 
ATOM   635  C CA  . ASN A 1 79  ? 20.653  17.647  10.041  1.000 70.698  0 79  ASN A CA  1 
ATOM   636  C C   . ASN A 1 79  ? 19.234  18.184  10.232  1.000 68.973  0 79  ASN A C   1 
ATOM   637  O O   . ASN A 1 79  ? 18.255  17.530  9.882   1.000 94.554  0 79  ASN A O   1 
ATOM   638  C CB  . ASN A 1 79  ? 21.473  18.374  8.978   1.000 71.648  0 79  ASN A CB  1 
ATOM   639  C CG  . ASN A 1 79  ? 22.946  18.037  9.098   1.000 74.005  0 79  ASN A CG  1 
ATOM   640  O OD1 . ASN A 1 79  ? 23.659  18.552  9.964   1.000 76.610  0 79  ASN A OD1 1 
ATOM   641  N ND2 . ASN A 1 79  ? 23.446  17.170  8.247   1.000 75.317  0 79  ASN A ND2 1 
ATOM   642  N N   . ASP A 1 80  ? 19.138  19.394  10.781  1.000 68.376  0 80  ASP A N   1 
ATOM   643  C CA  . ASP A 1 80  ? 17.879  19.932  11.289  1.000 68.169  0 80  ASP A CA  1 
ATOM   644  C C   . ASP A 1 80  ? 17.054  20.591  10.176  1.000 61.583  0 80  ASP A C   1 
ATOM   645  O O   . ASP A 1 80  ? 15.844  20.442  10.142  1.000 78.551  0 80  ASP A O   1 
ATOM   646  C CB  . ASP A 1 80  ? 18.159  20.891  12.440  1.000 78.097  0 80  ASP A CB  1 
ATOM   647  C CG  . ASP A 1 80  ? 18.991  20.329  13.595  1.000 86.375  0 80  ASP A CG  1 
ATOM   648  O OD1 . ASP A 1 80  ? 18.588  19.268  14.159  1.000 77.222  0 80  ASP A OD1 1 
ATOM   649  O OD2 . ASP A 1 80  ? 20.022  20.965  13.936  1.000 68.366  0 80  ASP A OD2 1 
ATOM   650  N N   . ILE A 1 81  ? 17.693  21.326  9.257   1.000 60.033  0 81  ILE A N   1 
ATOM   651  C CA  . ILE A 1 81  ? 16.986  22.047  8.218   1.000 62.136  0 81  ILE A CA  1 
ATOM   652  C C   . ILE A 1 81  ? 17.460  21.622  6.820   1.000 60.335  0 81  ILE A C   1 
ATOM   653  O O   . ILE A 1 81  ? 18.635  21.419  6.603   1.000 58.781  0 81  ILE A O   1 
ATOM   654  C CB  . ILE A 1 81  ? 17.128  23.570  8.434   1.000 63.244  0 81  ILE A CB  1 
ATOM   655  C CG1 . ILE A 1 81  ? 16.034  24.139  9.335   1.000 63.109  0 81  ILE A CG1 1 
ATOM   656  C CG2 . ILE A 1 81  ? 17.076  24.295  7.087   1.000 68.595  0 81  ILE A CG2 1 
ATOM   657  C CD1 . ILE A 1 81  ? 16.338  24.156  10.800  1.000 60.695  0 81  ILE A CD1 1 
ATOM   658  N N   . MET A 1 82  ? 16.516  21.561  5.866   1.000 60.114  0 82  MET A N   1 
ATOM   659  C CA  . MET A 1 82  ? 16.778  21.356  4.453   1.000 60.682  0 82  MET A CA  1 
ATOM   660  C C   . MET A 1 82  ? 16.783  22.705  3.752   1.000 65.379  0 82  MET A C   1 
ATOM   661  O O   . MET A 1 82  ? 15.752  23.367  3.655   1.000 66.210  0 82  MET A O   1 
ATOM   662  C CB  . MET A 1 82  ? 15.693  20.530  3.743   1.000 65.017  0 82  MET A CB  1 
ATOM   663  C CG  . MET A 1 82  ? 15.917  20.317  2.230   1.000 60.322  0 82  MET A CG  1 
ATOM   664  S SD  . MET A 1 82  ? 17.479  19.477  1.864   1.000 68.872  0 82  MET A SD  1 
ATOM   665  C CE  . MET A 1 82  ? 17.692  19.953  0.150   1.000 75.015  0 82  MET A CE  1 
ATOM   666  N N   . LEU A 1 83  ? 17.949  23.058  3.224   1.000 61.767  0 83  LEU A N   1 
ATOM   667  C CA  . LEU A 1 83  ? 18.120  24.305  2.532   1.000 69.541  0 83  LEU A CA  1 
ATOM   668  C C   . LEU A 1 83  ? 18.254  23.994  1.057   1.000 63.373  0 83  LEU A C   1 
ATOM   669  O O   . LEU A 1 83  ? 19.085  23.193  0.686   1.000 54.982  0 83  LEU A O   1 
ATOM   670  C CB  . LEU A 1 83  ? 19.365  25.023  3.048   1.000 74.515  0 83  LEU A CB  1 
ATOM   671  C CG  . LEU A 1 83  ? 19.520  26.465  2.564   1.000 75.802  0 83  LEU A CG  1 
ATOM   672  C CD1 . LEU A 1 83  ? 18.550  27.354  3.303   1.000 91.264  0 83  LEU A CD1 1 
ATOM   673  C CD2 . LEU A 1 83  ? 20.913  26.985  2.733   1.000 74.397  0 83  LEU A CD2 1 
ATOM   674  N N   . GLY A 1 84  ? 17.488  24.700  0.234   1.000 64.855  0 84  GLY A N   1 
ATOM   675  C CA  . GLY A 1 84  ? 17.597  24.541  -1.204  1.000 60.371  0 84  GLY A CA  1 
ATOM   676  C C   . GLY A 1 84  ? 17.848  25.869  -1.909  1.000 58.131  0 84  GLY A C   1 
ATOM   677  O O   . GLY A 1 84  ? 16.924  26.650  -2.103  1.000 63.689  0 84  GLY A O   1 
ATOM   678  N N   . VAL A 1 85  ? 19.097  26.085  -2.325  1.000 63.112  0 85  VAL A N   1 
ATOM   679  C CA  . VAL A 1 85  ? 19.455  27.166  -3.229  1.000 63.106  0 85  VAL A CA  1 
ATOM   680  C C   . VAL A 1 85  ? 18.859  26.882  -4.603  1.000 62.398  0 85  VAL A C   1 
ATOM   681  O O   . VAL A 1 85  ? 19.259  25.940  -5.267  1.000 74.035  0 85  VAL A O   1 
ATOM   682  C CB  . VAL A 1 85  ? 20.980  27.325  -3.332  1.000 59.420  0 85  VAL A CB  1 
ATOM   683  C CG1 . VAL A 1 85  ? 21.356  28.509  -4.207  1.000 62.948  0 85  VAL A CG1 1 
ATOM   684  C CG2 . VAL A 1 85  ? 21.642  27.488  -1.972  1.000 64.474  0 85  VAL A CG2 1 
ATOM   685  N N   . TYR A 1 86  ? 17.925  27.730  -5.029  1.000 66.439  0 86  TYR A N   1 
ATOM   686  C CA  . TYR A 1 86  ? 17.024  27.423  -6.125  1.000 68.555  0 86  TYR A CA  1 
ATOM   687  C C   . TYR A 1 86  ? 17.059  28.537  -7.172  1.000 74.762  0 86  TYR A C   1 
ATOM   688  O O   . TYR A 1 86  ? 16.705  29.683  -6.867  1.000 74.777  0 86  TYR A O   1 
ATOM   689  C CB  . TYR A 1 86  ? 15.660  27.251  -5.455  1.000 67.683  0 86  TYR A CB  1 
ATOM   690  C CG  . TYR A 1 86  ? 14.611  26.602  -6.330  1.000 65.938  0 86  TYR A CG  1 
ATOM   691  C CD1 . TYR A 1 86  ? 13.956  27.333  -7.303  1.000 68.192  0 86  TYR A CD1 1 
ATOM   692  C CD2 . TYR A 1 86  ? 14.241  25.287  -6.143  1.000 67.547  0 86  TYR A CD2 1 
ATOM   693  C CE1 . TYR A 1 86  ? 12.987  26.757  -8.107  1.000 73.749  0 86  TYR A CE1 1 
ATOM   694  C CE2 . TYR A 1 86  ? 13.300  24.689  -6.962  1.000 76.867  0 86  TYR A CE2 1 
ATOM   695  C CZ  . TYR A 1 86  ? 12.675  25.422  -7.953  1.000 77.499  0 86  TYR A CZ  1 
ATOM   696  O OH  . TYR A 1 86  ? 11.722  24.856  -8.758  1.000 68.537  0 86  TYR A OH  1 
ATOM   697  N N   . ILE A 1 87  ? 17.470  28.186  -8.408  1.000 73.598  0 87  ILE A N   1 
ATOM   698  C CA  . ILE A 1 87  ? 17.392  29.101  -9.541  1.000 72.742  0 87  ILE A CA  1 
ATOM   699  C C   . ILE A 1 87  ? 16.158  28.769  -10.366 1.000 64.266  0 87  ILE A C   1 
ATOM   700  O O   . ILE A 1 87  ? 16.093  27.691  -10.929 1.000 68.939  0 87  ILE A O   1 
ATOM   701  C CB  . ILE A 1 87  ? 18.685  29.079  -10.384 1.000 71.167  0 87  ILE A CB  1 
ATOM   702  C CG1 . ILE A 1 87  ? 19.814  29.833  -9.702  1.000 71.434  0 87  ILE A CG1 1 
ATOM   703  C CG2 . ILE A 1 87  ? 18.455  29.685  -11.757 1.000 71.396  0 87  ILE A CG2 1 
ATOM   704  C CD1 . ILE A 1 87  ? 20.590  29.004  -8.720  1.000 83.391  0 87  ILE A CD1 1 
ATOM   705  N N   . PRO A 1 88  ? 15.150  29.667  -10.469 1.000 70.177  0 88  PRO A N   1 
ATOM   706  C CA  . PRO A 1 88  ? 13.934  29.374  -11.256 1.000 67.085  0 88  PRO A CA  1 
ATOM   707  C C   . PRO A 1 88  ? 14.070  29.051  -12.759 1.000 72.964  0 88  PRO A C   1 
ATOM   708  O O   . PRO A 1 88  ? 13.223  28.365  -13.337 1.000 82.369  0 88  PRO A O   1 
ATOM   709  C CB  . PRO A 1 88  ? 13.083  30.640  -11.020 1.000 66.816  0 88  PRO A CB  1 
ATOM   710  C CG  . PRO A 1 88  ? 13.631  31.237  -9.746  1.000 75.744  0 88  PRO A CG  1 
ATOM   711  C CD  . PRO A 1 88  ? 15.118  30.967  -9.783  1.000 70.349  0 88  PRO A CD  1 
ATOM   712  N N   . ASP A 1 89  ? 15.129  29.534  -13.412 1.000 74.757  0 89  ASP A N   1 
ATOM   713  C CA  . ASP A 1 89  ? 15.315  29.280  -14.836 1.000 84.123  0 89  ASP A CA  1 
ATOM   714  C C   . ASP A 1 89  ? 16.253  28.094  -15.038 1.000 75.750  0 89  ASP A C   1 
ATOM   715  O O   . ASP A 1 89  ? 16.494  27.715  -16.172 1.000 70.535  0 89  ASP A O   1 
ATOM   716  C CB  . ASP A 1 89  ? 15.969  30.437  -15.584 1.000 90.520  0 89  ASP A CB  1 
ATOM   717  C CG  . ASP A 1 89  ? 15.802  31.815  -14.977 1.000 95.047  0 89  ASP A CG  1 
ATOM   718  O OD1 . ASP A 1 89  ? 16.441  32.097  -13.925 1.000 105.248 0 89  ASP A OD1 1 
ATOM   719  O OD2 . ASP A 1 89  ? 15.014  32.569  -15.550 1.000 95.503  0 89  ASP A OD2 1 
ATOM   720  N N   . GLU A 1 90  ? 16.832  27.575  -13.953 1.000 71.655  0 90  GLU A N   1 
ATOM   721  C CA  . GLU A 1 90  ? 17.759  26.458  -14.011 1.000 72.644  0 90  GLU A CA  1 
ATOM   722  C C   . GLU A 1 90  ? 17.452  25.527  -12.839 1.000 78.213  0 90  GLU A C   1 
ATOM   723  O O   . GLU A 1 90  ? 18.212  25.430  -11.877 1.000 82.015  0 90  GLU A O   1 
ATOM   724  C CB  . GLU A 1 90  ? 19.207  26.935  -13.941 1.000 79.795  0 90  GLU A CB  1 
ATOM   725  C CG  . GLU A 1 90  ? 19.650  27.904  -15.040 1.000 81.945  0 90  GLU A CG  1 
ATOM   726  C CD  . GLU A 1 90  ? 21.104  28.346  -14.872 1.000 76.270  0 90  GLU A CD  1 
ATOM   727  O OE1 . GLU A 1 90  ? 21.627  29.110  -15.682 1.000 88.974  0 90  GLU A OE1 1 
ATOM   728  O OE2 . GLU A 1 90  ? 21.746  27.913  -13.910 1.000 94.732  0 90  GLU A OE2 1 
ATOM   729  N N   . GLU A 1 91  ? 16.276  24.899  -12.896 1.000 76.452  0 91  GLU A N   1 
ATOM   730  C CA  . GLU A 1 91  ? 15.787  24.095  -11.788 1.000 81.930  0 91  GLU A CA  1 
ATOM   731  C C   . GLU A 1 91  ? 16.481  22.742  -11.878 1.000 74.754  0 91  GLU A C   1 
ATOM   732  O O   . GLU A 1 91  ? 16.730  22.295  -12.983 1.000 72.225  0 91  GLU A O   1 
ATOM   733  C CB  . GLU A 1 91  ? 14.257  24.060  -11.838 1.000 95.278  0 91  GLU A CB  1 
ATOM   734  C CG  . GLU A 1 91  ? 13.586  25.401  -11.529 1.000 96.683  0 91  GLU A CG  1 
ATOM   735  C CD  . GLU A 1 91  ? 12.089  25.525  -11.825 1.000 98.814  0 91  GLU A CD  1 
ATOM   736  O OE1 . GLU A 1 91  ? 11.710  25.316  -13.002 1.000 79.007  0 91  GLU A OE1 1 
ATOM   737  O OE2 . GLU A 1 91  ? 11.288  25.834  -10.894 1.000 82.029  0 91  GLU A OE2 1 
ATOM   738  N N   . ASP A 1 92  ? 16.806  22.120  -10.729 1.000 78.585  0 92  ASP A N   1 
ATOM   739  C CA  . ASP A 1 92  ? 17.646  20.922  -10.671 1.000 65.192  0 92  ASP A CA  1 
ATOM   740  C C   . ASP A 1 92  ? 16.817  19.703  -10.251 1.000 69.061  0 92  ASP A C   1 
ATOM   741  O O   . ASP A 1 92  ? 16.235  19.671  -9.162  1.000 77.328  0 92  ASP A O   1 
ATOM   742  C CB  . ASP A 1 92  ? 18.809  21.136  -9.705  1.000 67.866  0 92  ASP A CB  1 
ATOM   743  C CG  . ASP A 1 92  ? 19.870  20.047  -9.591  1.000 80.708  0 92  ASP A CG  1 
ATOM   744  O OD1 . ASP A 1 92  ? 19.905  19.137  -10.450 1.000 105.329 0 92  ASP A OD1 1 
ATOM   745  O OD2 . ASP A 1 92  ? 20.675  20.128  -8.645  1.000 100.520 0 92  ASP A OD2 1 
ATOM   746  N N   . VAL A 1 93  ? 16.823  18.664  -11.094 1.000 60.780  0 93  VAL A N   1 
ATOM   747  C CA  . VAL A 1 93  ? 16.137  17.425  -10.762 1.000 69.423  0 93  VAL A CA  1 
ATOM   748  C C   . VAL A 1 93  ? 16.694  16.795  -9.473  1.000 67.274  0 93  VAL A C   1 
ATOM   749  O O   . VAL A 1 93  ? 15.970  16.137  -8.735  1.000 64.273  0 93  VAL A O   1 
ATOM   750  C CB  . VAL A 1 93  ? 16.234  16.440  -11.937 1.000 70.093  0 93  VAL A CB  1 
ATOM   751  C CG1 . VAL A 1 93  ? 17.659  15.939  -12.125 1.000 67.353  0 93  VAL A CG1 1 
ATOM   752  C CG2 . VAL A 1 93  ? 15.280  15.265  -11.756 1.000 68.799  0 93  VAL A CG2 1 
ATOM   753  N N   . GLY A 1 94  ? 17.989  16.974  -9.209  1.000 78.167  0 94  GLY A N   1 
ATOM   754  C CA  . GLY A 1 94  ? 18.629  16.398  -8.037  1.000 77.800  0 94  GLY A CA  1 
ATOM   755  C C   . GLY A 1 94  ? 18.066  17.023  -6.774  1.000 78.463  0 94  GLY A C   1 
ATOM   756  O O   . GLY A 1 94  ? 17.682  16.336  -5.838  1.000 67.078  0 94  GLY A O   1 
ATOM   757  N N   . LEU A 1 95  ? 17.977  18.349  -6.800  1.000 82.950  0 95  LEU A N   1 
ATOM   758  C CA  . LEU A 1 95  ? 17.488  19.073  -5.647  1.000 72.603  0 95  LEU A CA  1 
ATOM   759  C C   . LEU A 1 95  ? 16.009  18.770  -5.473  1.000 70.176  0 95  LEU A C   1 
ATOM   760  O O   . LEU A 1 95  ? 15.529  18.678  -4.356  1.000 66.742  0 95  LEU A O   1 
ATOM   761  C CB  . LEU A 1 95  ? 17.737  20.558  -5.879  1.000 72.690  0 95  LEU A CB  1 
ATOM   762  C CG  . LEU A 1 95  ? 17.185  21.483  -4.799  1.000 72.290  0 95  LEU A CG  1 
ATOM   763  C CD1 . LEU A 1 95  ? 17.870  21.146  -3.501  1.000 72.602  0 95  LEU A CD1 1 
ATOM   764  C CD2 . LEU A 1 95  ? 17.417  22.930  -5.214  1.000 82.510  0 95  LEU A CD2 1 
ATOM   765  N N   . GLY A 1 96  ? 15.291  18.645  -6.589  1.000 70.432  0 96  GLY A N   1 
ATOM   766  C CA  . GLY A 1 96  ? 13.894  18.248  -6.530  1.000 83.539  0 96  GLY A CA  1 
ATOM   767  C C   . GLY A 1 96  ? 13.689  17.010  -5.657  1.000 79.200  0 96  GLY A C   1 
ATOM   768  O O   . GLY A 1 96  ? 12.841  17.011  -4.765  1.000 70.241  0 96  GLY A O   1 
ATOM   769  N N   . MET A 1 97  ? 14.509  15.978  -5.905  1.000 67.908  0 97  MET A N   1 
ATOM   770  C CA  . MET A 1 97  ? 14.418  14.727  -5.177  1.000 69.223  0 97  MET A CA  1 
ATOM   771  C C   . MET A 1 97  ? 14.724  14.915  -3.688  1.000 64.841  0 97  MET A C   1 
ATOM   772  O O   . MET A 1 97  ? 14.023  14.401  -2.828  1.000 59.859  0 97  MET A O   1 
ATOM   773  C CB  . MET A 1 97  ? 15.383  13.700  -5.777  1.000 72.189  0 97  MET A CB  1 
ATOM   774  C CG  . MET A 1 97  ? 15.305  12.327  -5.125  1.000 64.810  0 97  MET A CG  1 
ATOM   775  S SD  . MET A 1 97  ? 16.550  12.202  -3.833  1.000 68.269  0 97  MET A SD  1 
ATOM   776  C CE  . MET A 1 97  ? 16.022  10.886  -2.741  1.000 59.278  0 97  MET A CE  1 
ATOM   777  N N   . GLU A 1 98  ? 15.814  15.619  -3.400  1.000 71.518  0 98  GLU A N   1 
ATOM   778  C CA  . GLU A 1 98  ? 16.224  15.950  -2.046  1.000 68.618  0 98  GLU A CA  1 
ATOM   779  C C   . GLU A 1 98  ? 15.097  16.635  -1.275  1.000 64.915  0 98  GLU A C   1 
ATOM   780  O O   . GLU A 1 98  ? 14.923  16.377  -0.080  1.000 70.338  0 98  GLU A O   1 
ATOM   781  C CB  . GLU A 1 98  ? 17.485  16.811  -2.086  1.000 66.959  0 98  GLU A CB  1 
ATOM   782  C CG  . GLU A 1 98  ? 18.728  16.000  -2.447  1.000 70.996  0 98  GLU A CG  1 
ATOM   783  C CD  . GLU A 1 98  ? 19.921  16.762  -2.999  1.000 69.123  0 98  GLU A CD  1 
ATOM   784  O OE1 . GLU A 1 98  ? 20.920  16.071  -3.229  1.000 71.444  0 98  GLU A OE1 1 
ATOM   785  O OE2 . GLU A 1 98  ? 19.876  17.987  -3.195  1.000 75.687  0 98  GLU A OE2 1 
ATOM   786  N N   . LEU A 1 99  ? 14.315  17.477  -1.950  1.000 61.174  0 99  LEU A N   1 
ATOM   787  C CA  . LEU A 1 99  ? 13.254  18.196  -1.257  1.000 64.706  0 99  LEU A CA  1 
ATOM   788  C C   . LEU A 1 99  ? 12.200  17.190  -0.810  1.000 63.462  0 99  LEU A C   1 
ATOM   789  O O   . LEU A 1 99  ? 11.695  17.262  0.301   1.000 68.704  0 99  LEU A O   1 
ATOM   790  C CB  . LEU A 1 99  ? 12.646  19.333  -2.082  1.000 63.565  0 99  LEU A CB  1 
ATOM   791  C CG  . LEU A 1 99  ? 13.610  20.442  -2.539  1.000 68.057  0 99  LEU A CG  1 
ATOM   792  C CD1 . LEU A 1 99  ? 12.929  21.367  -3.538  1.000 67.899  0 99  LEU A CD1 1 
ATOM   793  C CD2 . LEU A 1 99  ? 14.191  21.269  -1.411  1.000 72.310  0 99  LEU A CD2 1 
ATOM   794  N N   . GLY A 1 100 ? 11.877  16.246  -1.691  1.000 71.424  0 100 GLY A N   1 
ATOM   795  C CA  . GLY A 1 100 ? 10.956  15.178  -1.354  1.000 67.004  0 100 GLY A CA  1 
ATOM   796  C C   . GLY A 1 100 ? 11.466  14.328  -0.196  1.000 62.681  0 100 GLY A C   1 
ATOM   797  O O   . GLY A 1 100 ? 10.716  13.970  0.702   1.000 64.870  0 100 GLY A O   1 
ATOM   798  N N   . TYR A 1 101 ? 12.758  14.013  -0.208  1.000 69.268  0 101 TYR A N   1 
ATOM   799  C CA  . TYR A 1 101 ? 13.302  13.137  0.814   1.000 69.832  0 101 TYR A CA  1 
ATOM   800  C C   . TYR A 1 101 ? 13.258  13.870  2.155   1.000 70.782  0 101 TYR A C   1 
ATOM   801  O O   . TYR A 1 101 ? 12.807  13.301  3.155   1.000 60.633  0 101 TYR A O   1 
ATOM   802  C CB  . TYR A 1 101 ? 14.681  12.662  0.354   1.000 62.068  0 101 TYR A CB  1 
ATOM   803  C CG  . TYR A 1 101 ? 15.305  11.735  1.376   1.000 65.175  0 101 TYR A CG  1 
ATOM   804  C CD1 . TYR A 1 101 ? 14.945  10.398  1.466   1.000 62.814  0 101 TYR A CD1 1 
ATOM   805  C CD2 . TYR A 1 101 ? 16.221  12.227  2.292   1.000 62.298  0 101 TYR A CD2 1 
ATOM   806  C CE1 . TYR A 1 101 ? 15.491  9.576   2.442   1.000 63.566  0 101 TYR A CE1 1 
ATOM   807  C CE2 . TYR A 1 101 ? 16.763  11.413  3.269   1.000 59.242  0 101 TYR A CE2 1 
ATOM   808  C CZ  . TYR A 1 101 ? 16.404  10.086  3.345   1.000 61.123  0 101 TYR A CZ  1 
ATOM   809  O OH  . TYR A 1 101 ? 16.965  9.360   4.355   1.000 71.493  0 101 TYR A OH  1 
ATOM   810  N N   . ALA A 1 102 ? 13.676  15.144  2.156   1.000 64.307  0 102 ALA A N   1 
ATOM   811  C CA  . ALA A 1 102 ? 13.572  15.994  3.341   1.000 67.734  0 102 ALA A CA  1 
ATOM   812  C C   . ALA A 1 102 ? 12.153  16.023  3.916   1.000 66.000  0 102 ALA A C   1 
ATOM   813  O O   . ALA A 1 102 ? 12.010  15.947  5.126   1.000 62.382  0 102 ALA A O   1 
ATOM   814  C CB  . ALA A 1 102 ? 14.042  17.395  3.025   1.000 65.584  0 102 ALA A CB  1 
ATOM   815  N N   . LEU A 1 103 ? 11.123  16.167  3.065   1.000 66.005  0 103 LEU A N   1 
ATOM   816  C CA  . LEU A 1 103 ? 9.736   16.090  3.488   1.000 70.990  0 103 LEU A CA  1 
ATOM   817  C C   . LEU A 1 103 ? 9.466   14.778  4.227   1.000 72.064  0 103 LEU A C   1 
ATOM   818  O O   . LEU A 1 103 ? 8.858   14.751  5.308   1.000 75.565  0 103 LEU A O   1 
ATOM   819  C CB  . LEU A 1 103 ? 8.773   16.219  2.310   1.000 87.751  0 103 LEU A CB  1 
ATOM   820  C CG  . LEU A 1 103 ? 7.285   16.192  2.704   1.000 90.938  0 103 LEU A CG  1 
ATOM   821  C CD1 . LEU A 1 103 ? 6.953   17.551  3.322   1.000 91.925  0 103 LEU A CD1 1 
ATOM   822  C CD2 . LEU A 1 103 ? 6.306   15.808  1.593   1.000 86.174  0 103 LEU A CD2 1 
ATOM   823  N N   . SER A 1 104 ? 9.905   13.675  3.634   1.000 66.284  0 104 SER A N   1 
ATOM   824  C CA  . SER A 1 104 ? 9.656   12.374  4.230   1.000 70.304  0 104 SER A CA  1 
ATOM   825  C C   . SER A 1 104 ? 10.367  12.216  5.584   1.000 69.721  0 104 SER A C   1 
ATOM   826  O O   . SER A 1 104 ? 9.912   11.430  6.405   1.000 68.922  0 104 SER A O   1 
ATOM   827  C CB  . SER A 1 104 ? 10.027  11.281  3.273   1.000 71.565  0 104 SER A CB  1 
ATOM   828  O OG  . SER A 1 104 ? 11.429  11.085  3.188   1.000 75.343  0 104 SER A OG  1 
ATOM   829  N N   . GLN A 1 105 ? 11.471  12.947  5.825   1.000 61.839  0 105 GLN A N   1 
ATOM   830  C CA  . GLN A 1 105 ? 12.206  12.861  7.081   1.000 65.397  0 105 GLN A CA  1 
ATOM   831  C C   . GLN A 1 105 ? 11.832  14.007  8.026   1.000 64.199  0 105 GLN A C   1 
ATOM   832  O O   . GLN A 1 105 ? 12.485  14.199  9.066   1.000 69.584  0 105 GLN A O   1 
ATOM   833  C CB  . GLN A 1 105 ? 13.727  12.973  6.935   1.000 69.314  0 105 GLN A CB  1 
ATOM   834  C CG  . GLN A 1 105 ? 14.361  11.964  5.991   1.000 69.469  0 105 GLN A CG  1 
ATOM   835  C CD  . GLN A 1 105 ? 14.014  10.552  6.380   1.000 67.705  0 105 GLN A CD  1 
ATOM   836  O OE1 . GLN A 1 105 ? 14.425  10.088  7.428   1.000 63.094  0 105 GLN A OE1 1 
ATOM   837  N NE2 . GLN A 1 105 ? 13.249  9.864   5.551   1.000 80.924  0 105 GLN A NE2 1 
ATOM   838  N N   . GLY A 1 106 ? 10.810  14.787  7.661   1.000 55.464  0 106 GLY A N   1 
ATOM   839  C CA  . GLY A 1 106 ? 10.184  15.731  8.586   1.000 56.460  0 106 GLY A CA  1 
ATOM   840  C C   . GLY A 1 106 ? 11.026  16.982  8.848   1.000 57.775  0 106 GLY A C   1 
ATOM   841  O O   . GLY A 1 106 ? 10.885  17.587  9.895   1.000 63.703  0 106 GLY A O   1 
ATOM   842  N N   . LYS A 1 107 ? 11.810  17.413  7.855   1.000 57.808  0 107 LYS A N   1 
ATOM   843  C CA  . LYS A 1 107 ? 12.634  18.602  7.969   1.000 59.095  0 107 LYS A CA  1 
ATOM   844  C C   . LYS A 1 107 ? 11.914  19.833  7.431   1.000 60.018  0 107 LYS A C   1 
ATOM   845  O O   . LYS A 1 107 ? 11.139  19.741  6.483   1.000 66.714  0 107 LYS A O   1 
ATOM   846  C CB  . LYS A 1 107 ? 13.895  18.431  7.124   1.000 60.000  0 107 LYS A CB  1 
ATOM   847  C CG  . LYS A 1 107 ? 14.619  17.101  7.316   1.000 61.835  0 107 LYS A CG  1 
ATOM   848  C CD  . LYS A 1 107 ? 15.167  16.958  8.718   1.000 58.553  0 107 LYS A CD  1 
ATOM   849  C CE  . LYS A 1 107 ? 15.850  15.648  8.864   1.000 61.718  0 107 LYS A CE  1 
ATOM   850  N NZ  . LYS A 1 107 ? 16.416  15.533  10.208  1.000 61.787  0 107 LYS A NZ  1 
ATOM   851  N N   . TYR A 1 108 ? 12.187  20.983  8.050   1.000 64.244  0 108 TYR A N   1 
ATOM   852  C CA  . TYR A 1 108 ? 11.832  22.261  7.461   1.000 68.476  0 108 TYR A CA  1 
ATOM   853  C C   . TYR A 1 108 ? 12.515  22.389  6.106   1.000 66.686  0 108 TYR A C   1 
ATOM   854  O O   . TYR A 1 108 ? 13.724  22.272  6.024   1.000 56.259  0 108 TYR A O   1 
ATOM   855  C CB  . TYR A 1 108 ? 12.277  23.401  8.378   1.000 62.180  0 108 TYR A CB  1 
ATOM   856  C CG  . TYR A 1 108 ? 11.755  24.786  8.013   1.000 63.004  0 108 TYR A CG  1 
ATOM   857  C CD1 . TYR A 1 108 ? 10.402  25.097  8.086   1.000 65.881  0 108 TYR A CD1 1 
ATOM   858  C CD2 . TYR A 1 108 ? 12.632  25.815  7.668   1.000 65.587  0 108 TYR A CD2 1 
ATOM   859  C CE1 . TYR A 1 108 ? 9.936   26.374  7.796   1.000 62.875  0 108 TYR A CE1 1 
ATOM   860  C CE2 . TYR A 1 108 ? 12.180  27.091  7.379   1.000 59.750  0 108 TYR A CE2 1 
ATOM   861  C CZ  . TYR A 1 108 ? 10.828  27.375  7.462   1.000 62.764  0 108 TYR A CZ  1 
ATOM   862  O OH  . TYR A 1 108 ? 10.368  28.626  7.184   1.000 65.951  0 108 TYR A OH  1 
ATOM   863  N N   . VAL A 1 109 ? 11.740  22.660  5.054   1.000 70.991  0 109 VAL A N   1 
ATOM   864  C CA  . VAL A 1 109 ? 12.299  22.874  3.729   1.000 67.751  0 109 VAL A CA  1 
ATOM   865  C C   . VAL A 1 109 ? 12.227  24.361  3.395   1.000 64.410  0 109 VAL A C   1 
ATOM   866  O O   . VAL A 1 109 ? 11.136  24.905  3.256   1.000 71.407  0 109 VAL A O   1 
ATOM   867  C CB  . VAL A 1 109 ? 11.540  22.022  2.697   1.000 72.118  0 109 VAL A CB  1 
ATOM   868  C CG1 . VAL A 1 109 ? 12.042  22.252  1.284   1.000 70.729  0 109 VAL A CG1 1 
ATOM   869  C CG2 . VAL A 1 109 ? 11.626  20.550  3.050   1.000 67.190  0 109 VAL A CG2 1 
ATOM   870  N N   . LEU A 1 110 ? 13.402  24.996  3.309   1.000 67.307  0 110 LEU A N   1 
ATOM   871  C CA  . LEU A 1 110 ? 13.570  26.416  3.009   1.000 67.485  0 110 LEU A CA  1 
ATOM   872  C C   . LEU A 1 110 ? 14.245  26.549  1.648   1.000 68.093  0 110 LEU A C   1 
ATOM   873  O O   . LEU A 1 110 ? 15.349  26.018  1.434   1.000 58.788  0 110 LEU A O   1 
ATOM   874  C CB  . LEU A 1 110 ? 14.463  27.069  4.065   1.000 66.250  0 110 LEU A CB  1 
ATOM   875  C CG  . LEU A 1 110 ? 14.217  28.533  4.449   1.000 70.706  0 110 LEU A CG  1 
ATOM   876  C CD1 . LEU A 1 110 ? 15.549  29.207  4.661   1.000 72.654  0 110 LEU A CD1 1 
ATOM   877  C CD2 . LEU A 1 110 ? 13.343  29.362  3.557   1.000 67.993  0 110 LEU A CD2 1 
ATOM   878  N N   . LEU A 1 111 ? 13.584  27.262  0.730   1.000 65.845  0 111 LEU A N   1 
ATOM   879  C CA  . LEU A 1 111 ? 14.246  27.616  -0.516  1.000 69.030  0 111 LEU A CA  1 
ATOM   880  C C   . LEU A 1 111 ? 14.829  29.033  -0.433  1.000 61.720  0 111 LEU A C   1 
ATOM   881  O O   . LEU A 1 111 ? 14.231  29.917  0.148   1.000 64.484  0 111 LEU A O   1 
ATOM   882  C CB  . LEU A 1 111 ? 13.243  27.496  -1.654  1.000 72.007  0 111 LEU A CB  1 
ATOM   883  C CG  . LEU A 1 111 ? 12.565  26.146  -1.866  1.000 65.733  0 111 LEU A CG  1 
ATOM   884  C CD1 . LEU A 1 111 ? 11.657  26.301  -3.097  1.000 69.600  0 111 LEU A CD1 1 
ATOM   885  C CD2 . LEU A 1 111 ? 13.599  25.048  -2.054  1.000 76.421  0 111 LEU A CD2 1 
ATOM   886  N N   . VAL A 1 112 ? 15.989  29.247  -1.054  1.000 68.908  0 112 VAL A N   1 
ATOM   887  C CA  . VAL A 1 112 ? 16.622  30.556  -1.162  1.000 69.360  0 112 VAL A CA  1 
ATOM   888  C C   . VAL A 1 112 ? 16.836  30.871  -2.636  1.000 68.630  0 112 VAL A C   1 
ATOM   889  O O   . VAL A 1 112 ? 17.594  30.179  -3.302  1.000 69.816  0 112 VAL A O   1 
ATOM   890  C CB  . VAL A 1 112 ? 17.995  30.617  -0.484  1.000 76.402  0 112 VAL A CB  1 
ATOM   891  C CG1 . VAL A 1 112 ? 18.501  32.039  -0.489  1.000 75.057  0 112 VAL A CG1 1 
ATOM   892  C CG2 . VAL A 1 112 ? 17.970  30.056  0.924   1.000 92.127  0 112 VAL A CG2 1 
ATOM   893  N N   . ILE A 1 113 ? 16.208  31.941  -3.110  1.000 70.167  0 113 ILE A N   1 
ATOM   894  C CA  . ILE A 1 113 ? 16.320  32.381  -4.487  1.000 60.979  0 113 ILE A CA  1 
ATOM   895  C C   . ILE A 1 113 ? 17.119  33.674  -4.511  1.000 68.221  0 113 ILE A C   1 
ATOM   896  O O   . ILE A 1 113 ? 16.954  34.538  -3.646  1.000 73.705  0 113 ILE A O   1 
ATOM   897  C CB  . ILE A 1 113 ? 14.932  32.580  -5.094  1.000 64.729  0 113 ILE A CB  1 
ATOM   898  C CG1 . ILE A 1 113 ? 14.115  31.311  -5.004  1.000 70.566  0 113 ILE A CG1 1 
ATOM   899  C CG2 . ILE A 1 113 ? 15.041  33.093  -6.522  1.000 71.938  0 113 ILE A CG2 1 
ATOM   900  C CD1 . ILE A 1 113 ? 12.678  31.467  -5.477  1.000 74.434  0 113 ILE A CD1 1 
ATOM   901  N N   . PRO A 1 114 ? 18.055  33.821  -5.471  1.000 71.505  0 114 PRO A N   1 
ATOM   902  C CA  . PRO A 1 114 ? 18.765  35.083  -5.647  1.000 75.910  0 114 PRO A CA  1 
ATOM   903  C C   . PRO A 1 114 ? 17.794  36.243  -5.833  1.000 79.265  0 114 PRO A C   1 
ATOM   904  O O   . PRO A 1 114 ? 16.771  36.073  -6.505  1.000 73.780  0 114 PRO A O   1 
ATOM   905  C CB  . PRO A 1 114 ? 19.567  34.777  -6.888  1.000 75.055  0 114 PRO A CB  1 
ATOM   906  C CG  . PRO A 1 114 ? 19.893  33.323  -6.726  1.000 81.254  0 114 PRO A CG  1 
ATOM   907  C CD  . PRO A 1 114 ? 18.546  32.761  -6.361  1.000 77.404  0 114 PRO A CD  1 
ATOM   908  N N   . ASP A 1 115 ? 18.142  37.401  -5.241  1.000 70.979  0 115 ASP A N   1 
ATOM   909  C CA  . ASP A 1 115 ? 17.257  38.554  -5.183  1.000 70.434  0 115 ASP A CA  1 
ATOM   910  C C   . ASP A 1 115 ? 16.829  38.966  -6.590  1.000 73.663  0 115 ASP A C   1 
ATOM   911  O O   . ASP A 1 115 ? 15.655  39.290  -6.816  1.000 73.374  0 115 ASP A O   1 
ATOM   912  C CB  . ASP A 1 115 ? 17.935  39.717  -4.478  1.000 68.633  0 115 ASP A CB  1 
ATOM   913  C CG  . ASP A 1 115 ? 18.390  39.479  -3.046  1.000 74.249  0 115 ASP A CG  1 
ATOM   914  O OD1 . ASP A 1 115 ? 19.288  38.639  -2.861  1.000 94.883  0 115 ASP A OD1 1 
ATOM   915  O OD2 . ASP A 1 115 ? 17.842  40.133  -2.136  1.000 76.789  0 115 ASP A OD2 1 
ATOM   916  N N   . GLU A 1 116 ? 17.806  38.910  -7.522  1.000 77.035  0 116 GLU A N   1 
ATOM   917  C CA  . GLU A 1 116 ? 17.613  39.252  -8.930  1.000 79.716  0 116 GLU A CA  1 
ATOM   918  C C   . GLU A 1 116 ? 16.523  38.394  -9.570  1.000 76.875  0 116 GLU A C   1 
ATOM   919  O O   . GLU A 1 116 ? 15.988  38.816  -10.590 1.000 73.431  0 116 GLU A O   1 
ATOM   920  C CB  . GLU A 1 116 ? 18.880  39.231  -9.798  1.000 80.669  0 116 GLU A CB  1 
ATOM   921  C CG  . GLU A 1 116 ? 19.756  37.981  -9.682  1.000 103.194 0 116 GLU A CG  1 
ATOM   922  C CD  . GLU A 1 116 ? 20.808  37.987  -8.560  1.000 117.378 0 116 GLU A CD  1 
ATOM   923  O OE1 . GLU A 1 116 ? 20.494  38.548  -7.458  1.000 89.699  0 116 GLU A OE1 1 
ATOM   924  O OE2 . GLU A 1 116 ? 21.930  37.399  -8.748  1.000 93.874  0 116 GLU A OE2 1 
ATOM   925  N N   . ASP A 1 117 ? 16.176  37.241  -8.958  1.000 78.350  0 117 ASP A N   1 
ATOM   926  C CA  . ASP A 1 117 ? 15.209  36.299  -9.514  1.000 72.307  0 117 ASP A CA  1 
ATOM   927  C C   . ASP A 1 117 ? 13.989  36.096  -8.607  1.000 76.690  0 117 ASP A C   1 
ATOM   928  O O   . ASP A 1 117 ? 13.007  35.477  -9.049  1.000 76.807  0 117 ASP A O   1 
ATOM   929  C CB  . ASP A 1 117 ? 15.825  34.935  -9.787  1.000 81.384  0 117 ASP A CB  1 
ATOM   930  C CG  . ASP A 1 117 ? 17.054  34.898  -10.695 1.000 92.029  0 117 ASP A CG  1 
ATOM   931  O OD1 . ASP A 1 117 ? 17.073  35.670  -11.693 1.000 83.514  0 117 ASP A OD1 1 
ATOM   932  O OD2 . ASP A 1 117 ? 17.982  34.090  -10.412 1.000 81.149  0 117 ASP A OD2 1 
ATOM   933  N N   . TYR A 1 118 ? 14.021  36.586  -7.349  1.000 69.421  0 118 TYR A N   1 
ATOM   934  C CA  . TYR A 1 118 ? 12.900  36.367  -6.441  1.000 75.320  0 118 TYR A CA  1 
ATOM   935  C C   . TYR A 1 118 ? 11.656  37.013  -7.036  1.000 73.419  0 118 TYR A C   1 
ATOM   936  O O   . TYR A 1 118 ? 11.737  38.154  -7.480  1.000 68.647  0 118 TYR A O   1 
ATOM   937  C CB  . TYR A 1 118 ? 13.107  36.948  -5.043  1.000 81.757  0 118 TYR A CB  1 
ATOM   938  C CG  . TYR A 1 118 ? 12.057  36.568  -4.008  1.000 83.572  0 118 TYR A CG  1 
ATOM   939  C CD1 . TYR A 1 118 ? 10.945  37.368  -3.767  1.000 80.272  0 118 TYR A CD1 1 
ATOM   940  C CD2 . TYR A 1 118 ? 12.212  35.427  -3.234  1.000 83.012  0 118 TYR A CD2 1 
ATOM   941  C CE1 . TYR A 1 118 ? 10.018  37.043  -2.784  1.000 84.676  0 118 TYR A CE1 1 
ATOM   942  C CE2 . TYR A 1 118 ? 11.285  35.078  -2.270  1.000 84.159  0 118 TYR A CE2 1 
ATOM   943  C CZ  . TYR A 1 118 ? 10.173  35.874  -2.051  1.000 90.724  0 118 TYR A CZ  1 
ATOM   944  O OH  . TYR A 1 118 ? 9.264   35.457  -1.113  1.000 93.748  0 118 TYR A OH  1 
ATOM   945  N N   . GLY A 1 119 ? 10.538  36.268  -7.067  1.000 79.045  0 119 GLY A N   1 
ATOM   946  C CA  . GLY A 1 119 ? 9.323   36.717  -7.741  1.000 77.612  0 119 GLY A CA  1 
ATOM   947  C C   . GLY A 1 119 ? 9.024   35.939  -9.019  1.000 75.319  0 119 GLY A C   1 
ATOM   948  O O   . GLY A 1 119 ? 7.847   35.805  -9.407  1.000 76.317  0 119 GLY A O   1 
ATOM   949  N N   . LYS A 1 120 ? 10.087  35.401  -9.653  1.000 70.856  0 120 LYS A N   1 
ATOM   950  C CA  . LYS A 1 120 ? 9.932   34.659  -10.893 1.000 72.002  0 120 LYS A CA  1 
ATOM   951  C C   . LYS A 1 120 ? 9.205   33.343  -10.642 1.000 78.896  0 120 LYS A C   1 
ATOM   952  O O   . LYS A 1 120 ? 9.312   32.767  -9.567  1.000 75.703  0 120 LYS A O   1 
ATOM   953  C CB  . LYS A 1 120 ? 11.248  34.287  -11.573 1.000 79.162  0 120 LYS A CB  1 
ATOM   954  C CG  . LYS A 1 120 ? 12.070  35.419  -12.177 1.000 80.229  0 120 LYS A CG  1 
ATOM   955  C CD  . LYS A 1 120 ? 12.885  35.007  -13.406 1.000 90.519  0 120 LYS A CD  1 
ATOM   956  C CE  . LYS A 1 120 ? 14.360  35.316  -13.361 1.000 88.446  0 120 LYS A CE  1 
ATOM   957  N NZ  . LYS A 1 120 ? 14.642  36.717  -13.099 1.000 82.207  0 120 LYS A NZ  1 
ATOM   958  N N   . PRO A 1 121 ? 8.469   32.797  -11.637 1.000 82.655  0 121 PRO A N   1 
ATOM   959  C CA  . PRO A 1 121 ? 7.618   31.630  -11.411 1.000 86.351  0 121 PRO A CA  1 
ATOM   960  C C   . PRO A 1 121 ? 8.497   30.433  -11.085 1.000 82.513  0 121 PRO A C   1 
ATOM   961  O O   . PRO A 1 121 ? 9.548   30.286  -11.712 1.000 77.606  0 121 PRO A O   1 
ATOM   962  C CB  . PRO A 1 121 ? 6.875   31.449  -12.748 1.000 84.214  0 121 PRO A CB  1 
ATOM   963  C CG  . PRO A 1 121 ? 7.036   32.783  -13.435 1.000 76.482  0 121 PRO A CG  1 
ATOM   964  C CD  . PRO A 1 121 ? 8.424   33.250  -13.028 1.000 78.399  0 121 PRO A CD  1 
ATOM   965  N N   . ILE A 1 122 ? 8.060   29.606  -10.112 1.000 80.442  0 122 ILE A N   1 
ATOM   966  C CA  . ILE A 1 122 ? 8.748   28.358  -9.776  1.000 71.843  0 122 ILE A CA  1 
ATOM   967  C C   . ILE A 1 122 ? 7.821   27.173  -10.033 1.000 62.339  0 122 ILE A C   1 
ATOM   968  O O   . ILE A 1 122 ? 6.601   27.290  -10.055 1.000 69.967  0 122 ILE A O   1 
ATOM   969  C CB  . ILE A 1 122 ? 9.266   28.345  -8.323  1.000 74.542  0 122 ILE A CB  1 
ATOM   970  C CG1 . ILE A 1 122 ? 8.130   28.337  -7.319  1.000 84.149  0 122 ILE A CG1 1 
ATOM   971  C CG2 . ILE A 1 122 ? 10.237  29.502  -8.063  1.000 75.237  0 122 ILE A CG2 1 
ATOM   972  C CD1 . ILE A 1 122 ? 8.597   28.244  -5.885  1.000 83.804  0 122 ILE A CD1 1 
ATOM   973  N N   . ASN A 1 123 ? 8.414   26.010  -10.220 1.000 59.285  0 123 ASN A N   1 
ATOM   974  C CA  . ASN A 1 123 ? 7.646   24.792  -10.421 1.000 74.600  0 123 ASN A CA  1 
ATOM   975  C C   . ASN A 1 123 ? 6.642   24.550  -9.284  1.000 67.577  0 123 ASN A C   1 
ATOM   976  O O   . ASN A 1 123 ? 6.985   24.655  -8.105  1.000 63.852  0 123 ASN A O   1 
ATOM   977  C CB  . ASN A 1 123 ? 8.605   23.618  -10.577 1.000 74.949  0 123 ASN A CB  1 
ATOM   978  C CG  . ASN A 1 123 ? 7.886   22.353  -10.939 1.000 74.931  0 123 ASN A CG  1 
ATOM   979  O OD1 . ASN A 1 123 ? 7.220   21.747  -10.094 1.000 79.021  0 123 ASN A OD1 1 
ATOM   980  N ND2 . ASN A 1 123 ? 8.044   21.933  -12.176 1.000 79.287  0 123 ASN A ND2 1 
ATOM   981  N N   . LEU A 1 124 ? 5.414   24.141  -9.646  1.000 72.350  0 124 LEU A N   1 
ATOM   982  C CA  . LEU A 1 124 ? 4.360   23.839  -8.679  1.000 70.597  0 124 LEU A CA  1 
ATOM   983  C C   . LEU A 1 124 ? 4.864   22.936  -7.546  1.000 67.532  0 124 LEU A C   1 
ATOM   984  O O   . LEU A 1 124 ? 4.608   23.230  -6.377  1.000 67.188  0 124 LEU A O   1 
ATOM   985  C CB  . LEU A 1 124 ? 3.113   23.221  -9.311  1.000 59.965  0 124 LEU A CB  1 
ATOM   986  C CG  . LEU A 1 124 ? 2.014   22.851  -8.306  1.000 74.918  0 124 LEU A CG  1 
ATOM   987  C CD1 . LEU A 1 124 ? 1.429   24.076  -7.552  1.000 70.494  0 124 LEU A CD1 1 
ATOM   988  C CD2 . LEU A 1 124 ? 0.874   22.072  -8.955  1.000 73.372  0 124 LEU A CD2 1 
ATOM   989  N N   . MET A 1 125 ? 5.520   21.817  -7.882  1.000 65.307  0 125 MET A N   1 
ATOM   990  C CA  . MET A 1 125 ? 5.863   20.829  -6.866  1.000 69.634  0 125 MET A CA  1 
ATOM   991  C C   . MET A 1 125 ? 6.941   21.368  -5.918  1.000 69.371  0 125 MET A C   1 
ATOM   992  O O   . MET A 1 125 ? 6.949   20.980  -4.747  1.000 75.031  0 125 MET A O   1 
ATOM   993  C CB  . MET A 1 125 ? 6.313   19.492  -7.464  1.000 65.149  0 125 MET A CB  1 
ATOM   994  C CG  . MET A 1 125 ? 5.452   18.999  -8.595  1.000 59.081  0 125 MET A CG  1 
ATOM   995  S SD  . MET A 1 125 ? 3.695   18.990  -8.196  1.000 69.486  0 125 MET A SD  1 
ATOM   996  C CE  . MET A 1 125 ? 3.574   17.394  -7.391  1.000 71.655  0 125 MET A CE  1 
ATOM   997  N N   . SER A 1 126 ? 7.797   22.287  -6.393  1.000 64.848  0 126 SER A N   1 
ATOM   998  C CA  . SER A 1 126 ? 8.798   22.937  -5.546  1.000 63.357  0 126 SER A CA  1 
ATOM   999  C C   . SER A 1 126 ? 8.129   23.870  -4.545  1.000 67.810  0 126 SER A C   1 
ATOM   1000 O O   . SER A 1 126 ? 8.430   23.835  -3.363  1.000 79.498  0 126 SER A O   1 
ATOM   1001 C CB  . SER A 1 126 ? 9.820   23.703  -6.337  1.000 64.088  0 126 SER A CB  1 
ATOM   1002 O OG  . SER A 1 126 ? 10.564  22.839  -7.181  1.000 72.397  0 126 SER A OG  1 
ATOM   1003 N N   . TRP A 1 127 ? 7.207   24.689  -5.051  1.000 70.713  0 127 TRP A N   1 
ATOM   1004 C CA  . TRP A 1 127 ? 6.327   25.511  -4.240  1.000 69.627  0 127 TRP A CA  1 
ATOM   1005 C C   . TRP A 1 127 ? 5.679   24.698  -3.107  1.000 69.071  0 127 TRP A C   1 
ATOM   1006 O O   . TRP A 1 127 ? 5.654   25.130  -1.955  1.000 78.162  0 127 TRP A O   1 
ATOM   1007 C CB  . TRP A 1 127 ? 5.295   26.122  -5.199  1.000 69.972  0 127 TRP A CB  1 
ATOM   1008 C CG  . TRP A 1 127 ? 4.254   26.982  -4.557  1.000 70.393  0 127 TRP A CG  1 
ATOM   1009 C CD1 . TRP A 1 127 ? 4.370   28.310  -4.299  1.000 78.626  0 127 TRP A CD1 1 
ATOM   1010 C CD2 . TRP A 1 127 ? 2.949   26.590  -4.093  1.000 65.454  0 127 TRP A CD2 1 
ATOM   1011 N NE1 . TRP A 1 127 ? 3.225   28.781  -3.721  1.000 82.861  0 127 TRP A NE1 1 
ATOM   1012 C CE2 . TRP A 1 127 ? 2.331   27.754  -3.586  1.000 72.561  0 127 TRP A CE2 1 
ATOM   1013 C CE3 . TRP A 1 127 ? 2.240   25.391  -4.055  1.000 64.169  0 127 TRP A CE3 1 
ATOM   1014 C CZ2 . TRP A 1 127 ? 1.052   27.747  -3.033  1.000 67.646  0 127 TRP A CZ2 1 
ATOM   1015 C CZ3 . TRP A 1 127 ? 0.967   25.385  -3.517  1.000 66.289  0 127 TRP A CZ3 1 
ATOM   1016 C CH2 . TRP A 1 127 ? 0.382   26.545  -3.016  1.000 71.079  0 127 TRP A CH2 1 
ATOM   1017 N N   . GLY A 1 128 ? 5.186   23.506  -3.450  1.000 65.573  0 128 GLY A N   1 
ATOM   1018 C CA  . GLY A 1 128 ? 4.390   22.677  -2.565  1.000 75.644  0 128 GLY A CA  1 
ATOM   1019 C C   . GLY A 1 128 ? 5.219   21.997  -1.481  1.000 76.820  0 128 GLY A C   1 
ATOM   1020 O O   . GLY A 1 128 ? 4.799   22.031  -0.333  1.000 68.909  0 128 GLY A O   1 
ATOM   1021 N N   . VAL A 1 129 ? 6.378   21.407  -1.827  1.000 69.979  0 129 VAL A N   1 
ATOM   1022 C CA  . VAL A 1 129 ? 7.206   20.757  -0.811  1.000 75.501  0 129 VAL A CA  1 
ATOM   1023 C C   . VAL A 1 129 ? 7.716   21.772  0.215   1.000 68.495  0 129 VAL A C   1 
ATOM   1024 O O   . VAL A 1 129 ? 7.952   21.425  1.372   1.000 80.718  0 129 VAL A O   1 
ATOM   1025 C CB  . VAL A 1 129 ? 8.425   19.974  -1.332  1.000 70.253  0 129 VAL A CB  1 
ATOM   1026 C CG1 . VAL A 1 129 ? 8.083   18.567  -1.722  1.000 79.902  0 129 VAL A CG1 1 
ATOM   1027 C CG2 . VAL A 1 129 ? 9.126   20.690  -2.469  1.000 70.471  0 129 VAL A CG2 1 
ATOM   1028 N N   . SER A 1 130 ? 8.035   22.968  -0.270  1.000 67.427  0 130 SER A N   1 
ATOM   1029 C CA  . SER A 1 130 ? 8.530   24.069  0.532   1.000 67.681  0 130 SER A CA  1 
ATOM   1030 C C   . SER A 1 130 ? 7.558   24.411  1.638   1.000 74.579  0 130 SER A C   1 
ATOM   1031 O O   . SER A 1 130 ? 6.332   24.503  1.425   1.000 89.690  0 130 SER A O   1 
ATOM   1032 C CB  . SER A 1 130 ? 8.723   25.296  -0.292  1.000 70.916  0 130 SER A CB  1 
ATOM   1033 O OG  . SER A 1 130 ? 9.612   24.953  -1.332  1.000 99.354  0 130 SER A OG  1 
ATOM   1034 N N   . ASP A 1 131 ? 8.203   24.667  2.780   1.000 64.881  0 131 ASP A N   1 
ATOM   1035 C CA  . ASP A 1 131 ? 7.602   25.314  3.928   1.000 73.056  0 131 ASP A CA  1 
ATOM   1036 C C   . ASP A 1 131 ? 7.634   26.833  3.762   1.000 73.642  0 131 ASP A C   1 
ATOM   1037 O O   . ASP A 1 131 ? 6.742   27.513  4.263   1.000 72.885  0 131 ASP A O   1 
ATOM   1038 C CB  . ASP A 1 131 ? 8.230   24.760  5.192   1.000 73.698  0 131 ASP A CB  1 
ATOM   1039 C CG  . ASP A 1 131 ? 7.878   23.296  5.428   1.000 70.930  0 131 ASP A CG  1 
ATOM   1040 O OD1 . ASP A 1 131 ? 6.681   22.990  5.661   1.000 74.038  0 131 ASP A OD1 1 
ATOM   1041 O OD2 . ASP A 1 131 ? 8.793   22.471  5.341   1.000 66.783  0 131 ASP A OD2 1 
ATOM   1042 N N   . ASN A 1 132 ? 8.625   27.356  3.021   1.000 62.954  0 132 ASN A N   1 
ATOM   1043 C CA  . ASN A 1 132 ? 8.869   28.791  2.973   1.000 64.662  0 132 ASN A CA  1 
ATOM   1044 C C   . ASN A 1 132 ? 9.922   29.060  1.898   1.000 63.271  0 132 ASN A C   1 
ATOM   1045 O O   . ASN A 1 132 ? 10.691  28.172  1.536   1.000 60.632  0 132 ASN A O   1 
ATOM   1046 C CB  . ASN A 1 132 ? 9.208   29.288  4.380   1.000 68.602  0 132 ASN A CB  1 
ATOM   1047 C CG  . ASN A 1 132 ? 9.535   30.756  4.507   1.000 69.729  0 132 ASN A CG  1 
ATOM   1048 O OD1 . ASN A 1 132 ? 10.351  31.127  5.364   1.000 76.919  0 132 ASN A OD1 1 
ATOM   1049 N ND2 . ASN A 1 132 ? 8.872   31.608  3.742   1.000 62.440  0 132 ASN A ND2 1 
ATOM   1050 N N   . VAL A 1 133 ? 9.925   30.279  1.342   1.000 66.609  0 133 VAL A N   1 
ATOM   1051 C CA  . VAL A 1 133 ? 10.947  30.663  0.383   1.000 69.826  0 133 VAL A CA  1 
ATOM   1052 C C   . VAL A 1 133 ? 11.309  32.141  0.528   1.000 65.047  0 133 VAL A C   1 
ATOM   1053 O O   . VAL A 1 133 ? 10.443  33.006  0.652   1.000 74.663  0 133 VAL A O   1 
ATOM   1054 C CB  . VAL A 1 133 ? 10.576  30.274  -1.060  1.000 72.723  0 133 VAL A CB  1 
ATOM   1055 C CG1 . VAL A 1 133 ? 9.129   29.838  -1.237  1.000 74.501  0 133 VAL A CG1 1 
ATOM   1056 C CG2 . VAL A 1 133 ? 10.998  31.331  -2.066  1.000 68.750  0 133 VAL A CG2 1 
ATOM   1057 N N   . ILE A 1 134 ? 12.626  32.415  0.480   1.000 63.115  0 134 ILE A N   1 
ATOM   1058 C CA  . ILE A 1 134 ? 13.189  33.700  0.863   1.000 65.084  0 134 ILE A CA  1 
ATOM   1059 C C   . ILE A 1 134 ? 14.195  34.208  -0.165  1.000 65.010  0 134 ILE A C   1 
ATOM   1060 O O   . ILE A 1 134 ? 14.625  33.445  -1.013  1.000 65.330  0 134 ILE A O   1 
ATOM   1061 C CB  . ILE A 1 134 ? 13.826  33.617  2.254   1.000 68.334  0 134 ILE A CB  1 
ATOM   1062 C CG1 . ILE A 1 134 ? 15.031  32.710  2.290   1.000 63.169  0 134 ILE A CG1 1 
ATOM   1063 C CG2 . ILE A 1 134 ? 12.761  33.219  3.283   1.000 79.800  0 134 ILE A CG2 1 
ATOM   1064 C CD1 . ILE A 1 134 ? 15.889  32.907  3.533   1.000 73.153  0 134 ILE A CD1 1 
ATOM   1065 N N   . LYS A 1 135 ? 14.533  35.512  -0.088  1.000 80.373  0 135 LYS A N   1 
ATOM   1066 C CA  . LYS A 1 135 ? 15.526  36.108  -0.974  1.000 76.321  0 135 LYS A CA  1 
ATOM   1067 C C   . LYS A 1 135 ? 16.885  35.870  -0.318  1.000 72.790  0 135 LYS A C   1 
ATOM   1068 O O   . LYS A 1 135 ? 16.951  35.692  0.902   1.000 78.998  0 135 LYS A O   1 
ATOM   1069 C CB  . LYS A 1 135 ? 15.286  37.554  -1.472  1.000 75.734  0 135 LYS A CB  1 
ATOM   1070 C CG  . LYS A 1 135 ? 14.583  38.648  -0.653  1.000 80.485  0 135 LYS A CG  1 
ATOM   1071 C CD  . LYS A 1 135 ? 13.892  39.804  -1.420  1.000 71.542  0 135 LYS A CD  1 
ATOM   1072 N N   . MET A 1 136 ? 17.945  35.817  -1.145  1.000 70.230  0 136 MET A N   1 
ATOM   1073 C CA  . MET A 1 136 ? 19.296  35.514  -0.683  1.000 66.392  0 136 MET A CA  1 
ATOM   1074 C C   . MET A 1 136 ? 19.769  36.508  0.378   1.000 67.971  0 136 MET A C   1 
ATOM   1075 O O   . MET A 1 136 ? 20.470  36.140  1.327   1.000 76.505  0 136 MET A O   1 
ATOM   1076 C CB  . MET A 1 136 ? 20.272  35.508  -1.858  1.000 63.720  0 136 MET A CB  1 
ATOM   1077 C CG  . MET A 1 136 ? 21.706  35.139  -1.512  1.000 67.224  0 136 MET A CG  1 
ATOM   1078 S SD  . MET A 1 136 ? 22.047  33.372  -1.432  1.000 76.424  0 136 MET A SD  1 
ATOM   1079 C CE  . MET A 1 136 ? 21.447  32.781  -3.025  1.000 71.554  0 136 MET A CE  1 
ATOM   1080 N N   . SER A 1 137 ? 19.352  37.762  0.246   1.000 68.592  0 137 SER A N   1 
ATOM   1081 C CA  . SER A 1 137 ? 19.687  38.785  1.231   1.000 77.657  0 137 SER A CA  1 
ATOM   1082 C C   . SER A 1 137 ? 18.988  38.588  2.578   1.000 73.202  0 137 SER A C   1 
ATOM   1083 O O   . SER A 1 137 ? 19.423  39.211  3.544   1.000 83.823  0 137 SER A O   1 
ATOM   1084 C CB  . SER A 1 137 ? 19.417  40.153  0.704   1.000 65.549  0 137 SER A CB  1 
ATOM   1085 O OG  . SER A 1 137 ? 18.089  40.241  0.239   1.000 80.126  0 137 SER A OG  1 
ATOM   1086 N N   . GLN A 1 138 ? 17.969  37.711  2.670   1.000 65.354  0 138 GLN A N   1 
ATOM   1087 C CA  . GLN A 1 138 ? 17.343  37.392  3.957   1.000 75.562  0 138 GLN A CA  1 
ATOM   1088 C C   . GLN A 1 138 ? 18.093  36.273  4.706   1.000 75.929  0 138 GLN A C   1 
ATOM   1089 O O   . GLN A 1 138 ? 17.854  36.035  5.892   1.000 77.859  0 138 GLN A O   1 
ATOM   1090 C CB  . GLN A 1 138 ? 15.859  37.040  3.819   1.000 64.171  0 138 GLN A CB  1 
ATOM   1091 C CG  . GLN A 1 138 ? 14.966  38.144  3.264   1.000 64.411  0 138 GLN A CG  1 
ATOM   1092 C CD  . GLN A 1 138 ? 13.540  37.688  3.009   1.000 72.966  0 138 GLN A CD  1 
ATOM   1093 O OE1 . GLN A 1 138 ? 13.239  37.089  1.976   1.000 73.770  0 138 GLN A OE1 1 
ATOM   1094 N NE2 . GLN A 1 138 ? 12.629  37.986  3.925   1.000 72.864  0 138 GLN A NE2 1 
ATOM   1095 N N   . LEU A 1 139 ? 19.033  35.599  4.045   1.000 67.207  0 139 LEU A N   1 
ATOM   1096 C CA  . LEU A 1 139 ? 19.555  34.355  4.579   1.000 68.060  0 139 LEU A CA  1 
ATOM   1097 C C   . LEU A 1 139 ? 20.536  34.598  5.725   1.000 73.509  0 139 LEU A C   1 
ATOM   1098 O O   . LEU A 1 139 ? 20.534  33.835  6.686   1.000 69.035  0 139 LEU A O   1 
ATOM   1099 C CB  . LEU A 1 139 ? 20.164  33.503  3.472   1.000 67.900  0 139 LEU A CB  1 
ATOM   1100 C CG  . LEU A 1 139 ? 20.683  32.124  3.905   1.000 68.093  0 139 LEU A CG  1 
ATOM   1101 C CD1 . LEU A 1 139 ? 19.593  31.279  4.515   1.000 74.730  0 139 LEU A CD1 1 
ATOM   1102 C CD2 . LEU A 1 139 ? 21.325  31.358  2.779   1.000 61.084  0 139 LEU A CD2 1 
ATOM   1103 N N   . LYS A 1 140 ? 21.360  35.648  5.640   1.000 88.670  0 140 LYS A N   1 
ATOM   1104 C CA  . LYS A 1 140 ? 22.246  36.030  6.744   1.000 83.595  0 140 LYS A CA  1 
ATOM   1105 C C   . LYS A 1 140 ? 21.478  36.192  8.060   1.000 67.186  0 140 LYS A C   1 
ATOM   1106 O O   . LYS A 1 140 ? 22.065  36.002  9.109   1.000 74.087  0 140 LYS A O   1 
ATOM   1107 C CB  . LYS A 1 140 ? 23.094  37.293  6.482   1.000 85.205  0 140 LYS A CB  1 
ATOM   1108 C CG  . LYS A 1 140 ? 22.399  38.668  6.548   1.000 105.670 0 140 LYS A CG  1 
ATOM   1109 C CD  . LYS A 1 140 ? 22.898  39.794  5.635   1.000 101.739 0 140 LYS A CD  1 
ATOM   1110 C CE  . LYS A 1 140 ? 24.338  40.177  5.826   1.000 114.284 0 140 LYS A CE  1 
ATOM   1111 N NZ  . LYS A 1 140 ? 24.732  40.371  7.225   1.000 117.774 0 140 LYS A NZ  1 
ATOM   1112 N N   . ASP A 1 141 ? 20.182  36.520  8.027   1.000 73.846  0 141 ASP A N   1 
ATOM   1113 C CA  . ASP A 1 141 ? 19.471  36.981  9.216   1.000 81.818  0 141 ASP A CA  1 
ATOM   1114 C C   . ASP A 1 141 ? 18.324  36.057  9.618   1.000 72.708  0 141 ASP A C   1 
ATOM   1115 O O   . ASP A 1 141 ? 17.678  36.300  10.633  1.000 73.689  0 141 ASP A O   1 
ATOM   1116 C CB  . ASP A 1 141 ? 18.955  38.402  9.034   1.000 81.303  0 141 ASP A CB  1 
ATOM   1117 C CG  . ASP A 1 141 ? 20.040  39.459  8.839   1.000 89.800  0 141 ASP A CG  1 
ATOM   1118 O OD1 . ASP A 1 141 ? 21.027  39.478  9.633   1.000 80.857  0 141 ASP A OD1 1 
ATOM   1119 O OD2 . ASP A 1 141 ? 19.888  40.267  7.899   1.000 90.447  0 141 ASP A OD2 1 
ATOM   1120 N N   . PHE A 1 142 ? 18.081  34.990  8.846   1.000 76.064  0 142 PHE A N   1 
ATOM   1121 C CA  . PHE A 1 142 ? 16.900  34.177  9.074   1.000 72.678  0 142 PHE A CA  1 
ATOM   1122 C C   . PHE A 1 142 ? 16.994  33.476  10.429  1.000 72.139  0 142 PHE A C   1 
ATOM   1123 O O   . PHE A 1 142 ? 18.033  32.931  10.763  1.000 72.009  0 142 PHE A O   1 
ATOM   1124 C CB  . PHE A 1 142 ? 16.783  33.212  7.904   1.000 68.743  0 142 PHE A CB  1 
ATOM   1125 C CG  . PHE A 1 142 ? 15.528  32.354  7.933   1.000 65.587  0 142 PHE A CG  1 
ATOM   1126 C CD1 . PHE A 1 142 ? 15.459  31.213  8.711   1.000 72.194  0 142 PHE A CD1 1 
ATOM   1127 C CD2 . PHE A 1 142 ? 14.456  32.650  7.118   1.000 56.713  0 142 PHE A CD2 1 
ATOM   1128 C CE1 . PHE A 1 142 ? 14.317  30.427  8.694   1.000 85.694  0 142 PHE A CE1 1 
ATOM   1129 C CE2 . PHE A 1 142 ? 13.312  31.876  7.135   1.000 62.495  0 142 PHE A CE2 1 
ATOM   1130 C CZ  . PHE A 1 142 ? 13.241  30.760  7.904   1.000 66.777  0 142 PHE A CZ  1 
ATOM   1131 N N   . ASN A 1 143 ? 15.913  33.493  11.214  1.000 71.347  0 143 ASN A N   1 
ATOM   1132 C CA  . ASN A 1 143 ? 15.917  32.842  12.520  1.000 69.504  0 143 ASN A CA  1 
ATOM   1133 C C   . ASN A 1 143 ? 15.470  31.389  12.397  1.000 65.152  0 143 ASN A C   1 
ATOM   1134 O O   . ASN A 1 143 ? 14.275  31.084  12.338  1.000 63.466  0 143 ASN A O   1 
ATOM   1135 C CB  . ASN A 1 143 ? 15.054  33.588  13.529  1.000 70.843  0 143 ASN A CB  1 
ATOM   1136 C CG  . ASN A 1 143 ? 15.130  32.989  14.904  1.000 72.560  0 143 ASN A CG  1 
ATOM   1137 O OD1 . ASN A 1 143 ? 15.938  32.095  15.150  1.000 76.521  0 143 ASN A OD1 1 
ATOM   1138 N ND2 . ASN A 1 143 ? 14.281  33.455  15.805  1.000 100.583 0 143 ASN A ND2 1 
ATOM   1139 N N   . PHE A 1 144 ? 16.468  30.503  12.415  1.000 71.300  0 144 PHE A N   1 
ATOM   1140 C CA  . PHE A 1 144 ? 16.270  29.085  12.178  1.000 68.780  0 144 PHE A CA  1 
ATOM   1141 C C   . PHE A 1 144 ? 15.752  28.383  13.430  1.000 71.967  0 144 PHE A C   1 
ATOM   1142 O O   . PHE A 1 144 ? 15.428  27.190  13.373  1.000 68.243  0 144 PHE A O   1 
ATOM   1143 C CB  . PHE A 1 144 ? 17.590  28.460  11.723  1.000 69.940  0 144 PHE A CB  1 
ATOM   1144 C CG  . PHE A 1 144 ? 17.880  28.679  10.248  1.000 68.110  0 144 PHE A CG  1 
ATOM   1145 C CD1 . PHE A 1 144 ? 17.243  27.909  9.281   1.000 59.413  0 144 PHE A CD1 1 
ATOM   1146 C CD2 . PHE A 1 144 ? 18.819  29.617  9.833   1.000 66.057  0 144 PHE A CD2 1 
ATOM   1147 C CE1 . PHE A 1 144 ? 17.494  28.114  7.936   1.000 66.209  0 144 PHE A CE1 1 
ATOM   1148 C CE2 . PHE A 1 144 ? 19.078  29.805  8.486   1.000 62.986  0 144 PHE A CE2 1 
ATOM   1149 C CZ  . PHE A 1 144 ? 18.401  29.068  7.540   1.000 63.856  0 144 PHE A CZ  1 
ATOM   1150 N N   . ASN A 1 145 ? 15.656  29.123  14.547  1.000 67.949  0 145 ASN A N   1 
ATOM   1151 C CA  . ASN A 1 145 ? 15.132  28.526  15.762  1.000 70.509  0 145 ASN A CA  1 
ATOM   1152 C C   . ASN A 1 145 ? 13.620  28.637  15.823  1.000 67.419  0 145 ASN A C   1 
ATOM   1153 O O   . ASN A 1 145 ? 13.025  27.954  16.657  1.000 72.556  0 145 ASN A O   1 
ATOM   1154 C CB  . ASN A 1 145 ? 15.742  29.107  17.024  1.000 70.899  0 145 ASN A CB  1 
ATOM   1155 C CG  . ASN A 1 145 ? 17.204  28.789  17.102  1.000 71.134  0 145 ASN A CG  1 
ATOM   1156 O OD1 . ASN A 1 145 ? 17.578  27.608  17.106  1.000 71.123  0 145 ASN A OD1 1 
ATOM   1157 N ND2 . ASN A 1 145 ? 18.014  29.838  17.117  1.000 74.373  0 145 ASN A ND2 1 
ATOM   1158 N N   . LYS A 1 146 ? 13.046  29.505  14.964  1.000 71.913  0 146 LYS A N   1 
ATOM   1159 C CA  . LYS A 1 146 ? 11.612  29.755  14.911  1.000 67.230  0 146 LYS A CA  1 
ATOM   1160 C C   . LYS A 1 146 ? 11.173  29.728  13.440  1.000 66.318  0 146 LYS A C   1 
ATOM   1161 O O   . LYS A 1 146 ? 10.662  30.709  12.907  1.000 75.937  0 146 LYS A O   1 
ATOM   1162 C CB  . LYS A 1 146 ? 11.266  31.083  15.608  1.000 74.356  0 146 LYS A CB  1 
ATOM   1163 C CG  . LYS A 1 146 ? 11.898  31.359  17.000  1.000 93.437  0 146 LYS A CG  1 
ATOM   1164 C CD  . LYS A 1 146 ? 11.346  32.498  17.863  1.000 94.131  0 146 LYS A CD  1 
ATOM   1165 C CE  . LYS A 1 146 ? 10.020  32.018  18.410  1.000 102.936 0 146 LYS A CE  1 
ATOM   1166 N NZ  . LYS A 1 146 ? 9.264   33.025  19.150  1.000 120.945 0 146 LYS A NZ  1 
ATOM   1167 N N   . PRO A 1 147 ? 11.350  28.600  12.718  1.000 62.154  0 147 PRO A N   1 
ATOM   1168 C CA  . PRO A 1 147 ? 11.012  28.530  11.294  1.000 60.228  0 147 PRO A CA  1 
ATOM   1169 C C   . PRO A 1 147 ? 9.519   28.335  11.046  1.000 63.039  0 147 PRO A C   1 
ATOM   1170 O O   . PRO A 1 147 ? 8.890   27.550  11.744  1.000 54.544  0 147 PRO A O   1 
ATOM   1171 C CB  . PRO A 1 147 ? 11.816  27.315  10.859  1.000 60.981  0 147 PRO A CB  1 
ATOM   1172 C CG  . PRO A 1 147 ? 11.765  26.394  12.067  1.000 64.339  0 147 PRO A CG  1 
ATOM   1173 C CD  . PRO A 1 147 ? 11.826  27.313  13.257  1.000 63.883  0 147 PRO A CD  1 
ATOM   1174 N N   . ARG A 1 148 ? 8.955   29.068  10.074  1.000 71.695  0 148 ARG A N   1 
ATOM   1175 C CA  . ARG A 1 148 ? 7.511   29.148  9.929   1.000 71.696  0 148 ARG A CA  1 
ATOM   1176 C C   . ARG A 1 148 ? 7.107   28.796  8.499   1.000 68.668  0 148 ARG A C   1 
ATOM   1177 O O   . ARG A 1 148 ? 7.882   28.980  7.570   1.000 62.942  0 148 ARG A O   1 
ATOM   1178 C CB  . ARG A 1 148 ? 7.064   30.553  10.359  1.000 75.846  0 148 ARG A CB  1 
ATOM   1179 C CG  . ARG A 1 148 ? 7.372   31.024  11.776  1.000 88.110  0 148 ARG A CG  1 
ATOM   1180 C CD  . ARG A 1 148 ? 6.712   30.179  12.873  1.000 108.185 0 148 ARG A CD  1 
ATOM   1181 N NE  . ARG A 1 148 ? 7.169   30.381  14.259  1.000 119.182 0 148 ARG A NE  1 
ATOM   1182 C CZ  . ARG A 1 148 ? 7.832   29.506  15.037  1.000 106.825 0 148 ARG A CZ  1 
ATOM   1183 N NH1 . ARG A 1 148 ? 7.999   29.735  16.330  1.000 118.636 0 148 ARG A NH1 1 
ATOM   1184 N NH2 . ARG A 1 148 ? 8.320   28.384  14.542  1.000 100.255 0 148 ARG A NH2 1 
ATOM   1185 N N   . PHE A 1 149 ? 5.883   28.292  8.319   1.000 66.063  0 149 PHE A N   1 
ATOM   1186 C CA  . PHE A 1 149 ? 5.302   28.167  6.997   1.000 60.592  0 149 PHE A CA  1 
ATOM   1187 C C   . PHE A 1 149 ? 4.906   29.537  6.436   1.000 67.229  0 149 PHE A C   1 
ATOM   1188 O O   . PHE A 1 149 ? 4.267   30.343  7.098   1.000 74.659  0 149 PHE A O   1 
ATOM   1189 C CB  . PHE A 1 149 ? 4.056   27.288  7.023   1.000 66.704  0 149 PHE A CB  1 
ATOM   1190 C CG  . PHE A 1 149 ? 3.401   27.282  5.650   1.000 74.652  0 149 PHE A CG  1 
ATOM   1191 C CD1 . PHE A 1 149 ? 2.504   28.285  5.271   1.000 71.789  0 149 PHE A CD1 1 
ATOM   1192 C CD2 . PHE A 1 149 ? 3.741   26.305  4.721   1.000 71.471  0 149 PHE A CD2 1 
ATOM   1193 C CE1 . PHE A 1 149 ? 1.940   28.288  4.007   1.000 77.861  0 149 PHE A CE1 1 
ATOM   1194 C CE2 . PHE A 1 149 ? 3.187   26.323  3.457   1.000 71.690  0 149 PHE A CE2 1 
ATOM   1195 C CZ  . PHE A 1 149 ? 2.289   27.311  3.104   1.000 74.423  0 149 PHE A CZ  1 
ATOM   1196 N N   . ASP A 1 150 ? 5.261   29.789  5.180   1.000 75.571  0 150 ASP A N   1 
ATOM   1197 C CA  . ASP A 1 150 ? 4.706   30.920  4.463   1.000 81.347  0 150 ASP A CA  1 
ATOM   1198 C C   . ASP A 1 150 ? 4.634   30.594  2.979   1.000 74.976  0 150 ASP A C   1 
ATOM   1199 O O   . ASP A 1 150 ? 5.350   29.695  2.527   1.000 76.407  0 150 ASP A O   1 
ATOM   1200 C CB  . ASP A 1 150 ? 5.520   32.182  4.688   1.000 81.771  0 150 ASP A CB  1 
ATOM   1201 C CG  . ASP A 1 150 ? 4.784   33.478  4.392   1.000 86.387  0 150 ASP A CG  1 
ATOM   1202 O OD1 . ASP A 1 150 ? 3.553   33.447  4.113   1.000 89.121  0 150 ASP A OD1 1 
ATOM   1203 O OD2 . ASP A 1 150 ? 5.460   34.507  4.403   1.000 101.873 0 150 ASP A OD2 1 
ATOM   1204 N N   . PHE A 1 151 ? 3.767   31.348  2.269   1.000 70.015  0 151 PHE A N   1 
ATOM   1205 C CA  . PHE A 1 151 ? 3.579   31.224  0.831   1.000 66.298  0 151 PHE A CA  1 
ATOM   1206 C C   . PHE A 1 151 ? 4.595   32.093  0.090   1.000 71.511  0 151 PHE A C   1 
ATOM   1207 O O   . PHE A 1 151 ? 4.899   33.207  0.513   1.000 68.077  0 151 PHE A O   1 
ATOM   1208 C CB  . PHE A 1 151 ? 2.170   31.667  0.446   1.000 65.308  0 151 PHE A CB  1 
ATOM   1209 C CG  . PHE A 1 151 ? 1.002   30.737  0.781   1.000 58.664  0 151 PHE A CG  1 
ATOM   1210 C CD1 . PHE A 1 151 ? 0.829   29.532  0.122   1.000 57.255  0 151 PHE A CD1 1 
ATOM   1211 C CD2 . PHE A 1 151 ? 0.015   31.121  1.667   1.000 60.012  0 151 PHE A CD2 1 
ATOM   1212 C CE1 . PHE A 1 151 ? -0.262  28.722  0.386   1.000 63.281  0 151 PHE A CE1 1 
ATOM   1213 C CE2 . PHE A 1 151 ? -1.070  30.296  1.936   1.000 67.994  0 151 PHE A CE2 1 
ATOM   1214 C CZ  . PHE A 1 151 ? -1.215  29.105  1.286   1.000 64.288  0 151 PHE A CZ  1 
ATOM   1215 N N   . TYR A 1 152 ? 5.144   31.565  -1.013  1.000 77.485  0 152 TYR A N   1 
ATOM   1216 C CA  . TYR A 1 152 ? 6.021   32.349  -1.876  1.000 75.535  0 152 TYR A CA  1 
ATOM   1217 C C   . TYR A 1 152 ? 5.293   33.581  -2.421  1.000 80.381  0 152 TYR A C   1 
ATOM   1218 O O   . TYR A 1 152 ? 4.123   33.503  -2.795  1.000 68.877  0 152 TYR A O   1 
ATOM   1219 C CB  . TYR A 1 152 ? 6.419   31.448  -3.047  1.000 76.284  0 152 TYR A CB  1 
ATOM   1220 C CG  . TYR A 1 152 ? 7.325   32.022  -4.133  1.000 67.802  0 152 TYR A CG  1 
ATOM   1221 C CD1 . TYR A 1 152 ? 8.477   32.758  -3.830  1.000 67.062  0 152 TYR A CD1 1 
ATOM   1222 C CD2 . TYR A 1 152 ? 7.066   31.746  -5.470  1.000 63.238  0 152 TYR A CD2 1 
ATOM   1223 C CE1 . TYR A 1 152 ? 9.327   33.215  -4.829  1.000 63.955  0 152 TYR A CE1 1 
ATOM   1224 C CE2 . TYR A 1 152 ? 7.889   32.214  -6.482  1.000 61.968  0 152 TYR A CE2 1 
ATOM   1225 C CZ  . TYR A 1 152 ? 9.010   32.956  -6.156  1.000 63.163  0 152 TYR A CZ  1 
ATOM   1226 O OH  . TYR A 1 152 ? 9.786   33.409  -7.164  1.000 73.466  0 152 TYR A OH  1 
ATOM   1227 N N   . GLU A 1 153 ? 6.019   34.703  -2.490  1.000 80.182  0 153 GLU A N   1 
ATOM   1228 C CA  . GLU A 1 153 ? 5.526   35.945  -3.067  1.000 81.476  0 153 GLU A CA  1 
ATOM   1229 C C   . GLU A 1 153 ? 5.972   35.967  -4.531  1.000 83.835  0 153 GLU A C   1 
ATOM   1230 O O   . GLU A 1 153 ? 6.916   36.671  -4.903  1.000 94.418  0 153 GLU A O   1 
ATOM   1231 C CB  . GLU A 1 153 ? 6.030   37.076  -2.156  1.000 91.516  0 153 GLU A CB  1 
ATOM   1232 C CG  . GLU A 1 153 ? 5.297   38.415  -2.243  1.000 96.668  0 153 GLU A CG  1 
ATOM   1233 C CD  . GLU A 1 153 ? 3.821   38.448  -1.865  1.000 100.466 0 153 GLU A CD  1 
ATOM   1234 O OE1 . GLU A 1 153 ? 3.235   37.521  -1.259  1.000 92.147  0 153 GLU A OE1 1 
ATOM   1235 O OE2 . GLU A 1 153 ? 3.237   39.469  -2.249  1.000 103.904 0 153 GLU A OE2 1 
ATOM   1236 N N   . GLY A 1 154 ? 5.310   35.127  -5.342  1.000 78.111  0 154 GLY A N   1 
ATOM   1237 C CA  . GLY A 1 154 ? 5.635   34.972  -6.752  1.000 79.402  0 154 GLY A CA  1 
ATOM   1238 C C   . GLY A 1 154 ? 4.707   33.962  -7.423  1.000 69.569  0 154 GLY A C   1 
ATOM   1239 O O   . GLY A 1 154 ? 3.883   33.353  -6.769  1.000 60.093  0 154 GLY A O   1 
ATOM   1240 N N   . ALA A 1 155 ? 4.866   33.742  -8.730  1.000 85.172  0 155 ALA A N   1 
ATOM   1241 C CA  . ALA A 1 155 ? 3.977   32.830  -9.433  1.000 87.963  0 155 ALA A CA  1 
ATOM   1242 C C   . ALA A 1 155 ? 4.450   31.380  -9.305  1.000 76.347  0 155 ALA A C   1 
ATOM   1243 O O   . ALA A 1 155 ? 5.550   31.084  -8.860  1.000 80.210  0 155 ALA A O   1 
ATOM   1244 C CB  . ALA A 1 155 ? 3.903   33.242  -10.888 1.000 105.114 0 155 ALA A CB  1 
ATOM   1245 N N   . VAL A 1 156 ? 3.637   30.477  -9.840  1.000 78.890  0 156 VAL A N   1 
ATOM   1246 C CA  . VAL A 1 156 ? 4.027   29.097  -10.050 1.000 75.294  0 156 VAL A CA  1 
ATOM   1247 C C   . VAL A 1 156 ? 3.568   28.679  -11.438 1.000 75.105  0 156 VAL A C   1 
ATOM   1248 O O   . VAL A 1 156 ? 2.437   28.944  -11.790 1.000 101.814 0 156 VAL A O   1 
ATOM   1249 C CB  . VAL A 1 156 ? 3.436   28.225  -8.930  1.000 83.499  0 156 VAL A CB  1 
ATOM   1250 C CG1 . VAL A 1 156 ? 2.524   29.003  -8.004  1.000 115.172 0 156 VAL A CG1 1 
ATOM   1251 C CG2 . VAL A 1 156 ? 2.692   27.020  -9.469  1.000 91.121  0 156 VAL A CG2 1 
ATOM   1252 N N   . TYR A 1 157 ? 4.439   28.021  -12.210 1.000 85.225  0 157 TYR A N   1 
ATOM   1253 C CA  . TYR A 1 157 ? 4.071   27.524  -13.530 1.000 78.821  0 157 TYR A CA  1 
ATOM   1254 C C   . TYR A 1 157 ? 3.744   26.008  -13.519 1.000 88.866  0 157 TYR A C   1 
ATOM   1255 O O   . TYR A 1 157 ? 3.049   25.671  -14.493 1.000 96.594  0 157 TYR A O   1 
ATOM   1256 C CB  . TYR A 1 157 ? 5.217   27.772  -14.501 1.000 69.995  0 157 TYR A CB  1 
ATOM   1257 C CG  . TYR A 1 157 ? 6.420   26.863  -14.308 1.000 68.609  0 157 TYR A CG  1 
ATOM   1258 C CD1 . TYR A 1 157 ? 6.412   25.544  -14.767 1.000 72.360  0 157 TYR A CD1 1 
ATOM   1259 C CD2 . TYR A 1 157 ? 7.577   27.329  -13.679 1.000 71.564  0 157 TYR A CD2 1 
ATOM   1260 C CE1 . TYR A 1 157 ? 7.513   24.717  -14.588 1.000 80.090  0 157 TYR A CE1 1 
ATOM   1261 C CE2 . TYR A 1 157 ? 8.695   26.519  -13.509 1.000 64.726  0 157 TYR A CE2 1 
ATOM   1262 C CZ  . TYR A 1 157 ? 8.661   25.212  -13.972 1.000 79.016  0 157 TYR A CZ  1 
ATOM   1263 O OH  . TYR A 1 157 ? 9.739   24.403  -13.766 1.000 71.521  0 157 TYR A OH  1 
ATOM   1264 O OXT . TYR A 1 157 ? 4.177   25.207  -12.643 1.000 81.407  0 157 TYR A OXT 1 
ATOM   1265 N N   . PRO B 1 2   ? -3.906  -10.238 -13.269 1.000 93.844  0 2   PRO B N   1 
ATOM   1266 C CA  . PRO B 1 2   ? -3.738  -9.223  -12.221 1.000 92.208  0 2   PRO B CA  1 
ATOM   1267 C C   . PRO B 1 2   ? -3.086  -7.964  -12.796 1.000 94.069  0 2   PRO B C   1 
ATOM   1268 O O   . PRO B 1 2   ? -2.055  -8.052  -13.468 1.000 88.980  0 2   PRO B O   1 
ATOM   1269 C CB  . PRO B 1 2   ? -2.860  -9.840  -11.078 1.000 81.460  0 2   PRO B CB  1 
ATOM   1270 C CG  . PRO B 1 2   ? -2.410  -11.193 -11.635 1.000 93.015  0 2   PRO B CG  1 
ATOM   1271 C CD  . PRO B 1 2   ? -2.900  -11.294 -13.124 1.000 98.772  0 2   PRO B CD  1 
ATOM   1272 N N   . LYS B 1 3   ? -3.693  -6.797  -12.526 1.000 90.631  0 3   LYS B N   1 
ATOM   1273 C CA  . LYS B 1 3   ? -3.241  -5.533  -13.102 1.000 93.458  0 3   LYS B CA  1 
ATOM   1274 C C   . LYS B 1 3   ? -2.797  -4.576  -11.977 1.000 85.277  0 3   LYS B C   1 
ATOM   1275 O O   . LYS B 1 3   ? -3.361  -4.586  -10.893 1.000 76.822  0 3   LYS B O   1 
ATOM   1276 C CB  . LYS B 1 3   ? -4.357  -4.983  -14.014 1.000 98.585  0 3   LYS B CB  1 
ATOM   1277 C CG  . LYS B 1 3   ? -4.921  -5.801  -15.226 1.000 83.155  0 3   LYS B CG  1 
ATOM   1278 N N   . LYS B 1 4   ? -1.762  -3.753  -12.199 1.000 85.787  0 4   LYS B N   1 
ATOM   1279 C CA  . LYS B 1 4   ? -1.396  -2.722  -11.229 1.000 81.683  0 4   LYS B CA  1 
ATOM   1280 C C   . LYS B 1 4   ? -1.717  -1.349  -11.817 1.000 78.503  0 4   LYS B C   1 
ATOM   1281 O O   . LYS B 1 4   ? -1.748  -1.188  -13.035 1.000 85.814  0 4   LYS B O   1 
ATOM   1282 C CB  . LYS B 1 4   ? 0.081   -2.787  -10.820 1.000 80.202  0 4   LYS B CB  1 
ATOM   1283 C CG  . LYS B 1 4   ? 0.599   -4.017  -10.015 1.000 91.137  0 4   LYS B CG  1 
ATOM   1284 C CD  . LYS B 1 4   ? -0.018  -4.401  -8.668  1.000 66.543  0 4   LYS B CD  1 
ATOM   1285 N N   . THR B 1 5   ? -1.981  -0.346  -10.969 1.000 84.262  0 5   THR B N   1 
ATOM   1286 C CA  . THR B 1 5   ? -2.181  1.014   -11.470 1.000 83.734  0 5   THR B CA  1 
ATOM   1287 C C   . THR B 1 5   ? -0.921  1.834   -11.241 1.000 80.392  0 5   THR B C   1 
ATOM   1288 O O   . THR B 1 5   ? -0.111  1.502   -10.364 1.000 75.660  0 5   THR B O   1 
ATOM   1289 C CB  . THR B 1 5   ? -3.364  1.688   -10.799 1.000 77.083  0 5   THR B CB  1 
ATOM   1290 O OG1 . THR B 1 5   ? -2.961  1.848   -9.444  1.000 80.758  0 5   THR B OG1 1 
ATOM   1291 C CG2 . THR B 1 5   ? -4.608  0.826   -10.878 1.000 88.462  0 5   THR B CG2 1 
ATOM   1292 N N   . ILE B 1 6   ? -0.779  2.891   -12.051 1.000 79.051  0 6   ILE B N   1 
ATOM   1293 C CA  . ILE B 1 6   ? 0.388   3.762   -11.986 1.000 82.916  0 6   ILE B CA  1 
ATOM   1294 C C   . ILE B 1 6   ? 0.003   5.241   -11.864 1.000 80.802  0 6   ILE B C   1 
ATOM   1295 O O   . ILE B 1 6   ? -1.157  5.627   -11.972 1.000 83.094  0 6   ILE B O   1 
ATOM   1296 C CB  . ILE B 1 6   ? 1.302   3.540   -13.199 1.000 74.686  0 6   ILE B CB  1 
ATOM   1297 C CG1 . ILE B 1 6   ? 0.591   3.808   -14.513 1.000 89.279  0 6   ILE B CG1 1 
ATOM   1298 C CG2 . ILE B 1 6   ? 1.912   2.158   -13.161 1.000 80.574  0 6   ILE B CG2 1 
ATOM   1299 C CD1 . ILE B 1 6   ? 1.032   5.081   -15.214 1.000 88.254  0 6   ILE B CD1 1 
ATOM   1300 N N   . TYR B 1 7   ? 1.031   6.054   -11.590 1.000 72.593  0 7   TYR B N   1 
ATOM   1301 C CA  . TYR B 1 7   ? 0.977   7.493   -11.712 1.000 69.663  0 7   TYR B CA  1 
ATOM   1302 C C   . TYR B 1 7   ? 1.885   7.864   -12.878 1.000 78.439  0 7   TYR B C   1 
ATOM   1303 O O   . TYR B 1 7   ? 3.065   7.486   -12.913 1.000 63.481  0 7   TYR B O   1 
ATOM   1304 C CB  . TYR B 1 7   ? 1.447   8.168   -10.415 1.000 80.479  0 7   TYR B CB  1 
ATOM   1305 C CG  . TYR B 1 7   ? 1.599   9.688   -10.474 1.000 76.239  0 7   TYR B CG  1 
ATOM   1306 C CD1 . TYR B 1 7   ? 2.775   10.301  -10.923 1.000 65.630  0 7   TYR B CD1 1 
ATOM   1307 C CD2 . TYR B 1 7   ? 0.556   10.510  -10.064 1.000 72.282  0 7   TYR B CD2 1 
ATOM   1308 C CE1 . TYR B 1 7   ? 2.895   11.686  -10.983 1.000 68.190  0 7   TYR B CE1 1 
ATOM   1309 C CE2 . TYR B 1 7   ? 0.677   11.887  -10.097 1.000 68.185  0 7   TYR B CE2 1 
ATOM   1310 C CZ  . TYR B 1 7   ? 1.843   12.482  -10.556 1.000 69.376  0 7   TYR B CZ  1 
ATOM   1311 O OH  . TYR B 1 7   ? 1.882   13.850  -10.606 1.000 71.904  0 7   TYR B OH  1 
ATOM   1312 N N   . PHE B 1 8   ? 1.315   8.619   -13.820 1.000 84.097  0 8   PHE B N   1 
ATOM   1313 C CA  . PHE B 1 8   ? 1.981   8.900   -15.078 1.000 82.179  0 8   PHE B CA  1 
ATOM   1314 C C   . PHE B 1 8   ? 2.823   10.159  -14.924 1.000 72.629  0 8   PHE B C   1 
ATOM   1315 O O   . PHE B 1 8   ? 2.387   11.250  -15.286 1.000 84.802  0 8   PHE B O   1 
ATOM   1316 C CB  . PHE B 1 8   ? 0.929   9.004   -16.195 1.000 92.274  0 8   PHE B CB  1 
ATOM   1317 C CG  . PHE B 1 8   ? 1.576   8.986   -17.572 1.000 81.145  0 8   PHE B CG  1 
ATOM   1318 C CD1 . PHE B 1 8   ? 1.961   7.787   -18.155 1.000 72.898  0 8   PHE B CD1 1 
ATOM   1319 C CD2 . PHE B 1 8   ? 1.848   10.172  -18.249 1.000 78.909  0 8   PHE B CD2 1 
ATOM   1320 C CE1 . PHE B 1 8   ? 2.637   7.786   -19.360 1.000 80.143  0 8   PHE B CE1 1 
ATOM   1321 C CE2 . PHE B 1 8   ? 2.476   10.155  -19.479 1.000 74.132  0 8   PHE B CE2 1 
ATOM   1322 C CZ  . PHE B 1 8   ? 2.882   8.965   -20.025 1.000 80.340  0 8   PHE B CZ  1 
ATOM   1323 N N   . GLY B 1 9   ? 4.020   9.992   -14.378 1.000 72.237  0 9   GLY B N   1 
ATOM   1324 C CA  . GLY B 1 9   ? 4.942   11.107  -14.209 1.000 78.474  0 9   GLY B CA  1 
ATOM   1325 C C   . GLY B 1 9   ? 5.723   11.407  -15.486 1.000 76.524  0 9   GLY B C   1 
ATOM   1326 O O   . GLY B 1 9   ? 6.629   10.657  -15.856 1.000 82.901  0 9   GLY B O   1 
ATOM   1327 N N   . ALA B 1 10  ? 5.387   12.542  -16.116 1.000 84.888  0 10  ALA B N   1 
ATOM   1328 C CA  . ALA B 1 10  ? 5.886   12.924  -17.427 1.000 73.964  0 10  ALA B CA  1 
ATOM   1329 C C   . ALA B 1 10  ? 5.614   14.398  -17.673 1.000 73.585  0 10  ALA B C   1 
ATOM   1330 O O   . ALA B 1 10  ? 4.492   14.851  -17.430 1.000 88.435  0 10  ALA B O   1 
ATOM   1331 C CB  . ALA B 1 10  ? 5.191   12.114  -18.477 1.000 75.223  0 10  ALA B CB  1 
ATOM   1332 N N   . GLY B 1 11  ? 6.631   15.109  -18.188 1.000 87.494  0 11  GLY B N   1 
ATOM   1333 C CA  . GLY B 1 11  ? 6.505   16.503  -18.611 1.000 88.493  0 11  GLY B CA  1 
ATOM   1334 C C   . GLY B 1 11  ? 5.773   16.629  -19.947 1.000 84.677  0 11  GLY B C   1 
ATOM   1335 O O   . GLY B 1 11  ? 5.691   15.647  -20.699 1.000 99.703  0 11  GLY B O   1 
ATOM   1336 N N   . TRP B 1 12  ? 5.231   17.832  -20.221 1.000 96.717  0 12  TRP B N   1 
ATOM   1337 C CA  . TRP B 1 12  ? 4.544   18.114  -21.481 1.000 103.422 0 12  TRP B CA  1 
ATOM   1338 C C   . TRP B 1 12  ? 4.929   19.489  -22.030 1.000 94.039  0 12  TRP B C   1 
ATOM   1339 O O   . TRP B 1 12  ? 4.135   20.075  -22.746 1.000 98.045  0 12  TRP B O   1 
ATOM   1340 C CB  . TRP B 1 12  ? 3.016   18.000  -21.319 1.000 102.684 0 12  TRP B CB  1 
ATOM   1341 C CG  . TRP B 1 12  ? 2.486   18.805  -20.162 1.000 111.594 0 12  TRP B CG  1 
ATOM   1342 C CD1 . TRP B 1 12  ? 2.280   20.149  -20.133 1.000 120.794 0 12  TRP B CD1 1 
ATOM   1343 C CD2 . TRP B 1 12  ? 2.134   18.326  -18.846 1.000 125.358 0 12  TRP B CD2 1 
ATOM   1344 N NE1 . TRP B 1 12  ? 1.839   20.540  -18.902 1.000 117.400 0 12  TRP B NE1 1 
ATOM   1345 C CE2 . TRP B 1 12  ? 1.732   19.448  -18.092 1.000 126.645 0 12  TRP B CE2 1 
ATOM   1346 C CE3 . TRP B 1 12  ? 2.132   17.072  -18.227 1.000 128.181 0 12  TRP B CE3 1 
ATOM   1347 C CZ2 . TRP B 1 12  ? 1.326   19.355  -16.763 1.000 121.279 0 12  TRP B CZ2 1 
ATOM   1348 C CZ3 . TRP B 1 12  ? 1.716   16.975  -16.917 1.000 127.763 0 12  TRP B CZ3 1 
ATOM   1349 C CH2 . TRP B 1 12  ? 1.331   18.105  -16.193 1.000 126.511 0 12  TRP B CH2 1 
ATOM   1350 N N   . PHE B 1 13  ? 6.166   19.939  -21.775 1.000 101.164 0 13  PHE B N   1 
ATOM   1351 C CA  . PHE B 1 13  ? 6.566   21.318  -22.021 1.000 119.982 0 13  PHE B CA  1 
ATOM   1352 C C   . PHE B 1 13  ? 7.396   21.447  -23.299 1.000 110.713 0 13  PHE B C   1 
ATOM   1353 O O   . PHE B 1 13  ? 7.515   22.545  -23.811 1.000 130.560 0 13  PHE B O   1 
ATOM   1354 C CB  . PHE B 1 13  ? 7.350   21.904  -20.837 1.000 138.265 0 13  PHE B CB  1 
ATOM   1355 C CG  . PHE B 1 13  ? 6.706   21.715  -19.461 1.000 170.102 0 13  PHE B CG  1 
ATOM   1356 C CD1 . PHE B 1 13  ? 5.450   22.262  -19.168 1.000 151.455 0 13  PHE B CD1 1 
ATOM   1357 C CD2 . PHE B 1 13  ? 7.377   21.021  -18.446 1.000 151.530 0 13  PHE B CD2 1 
ATOM   1358 C CE1 . PHE B 1 13  ? 4.872   22.091  -17.914 1.000 139.641 0 13  PHE B CE1 1 
ATOM   1359 C CE2 . PHE B 1 13  ? 6.803   20.866  -17.187 1.000 142.499 0 13  PHE B CE2 1 
ATOM   1360 C CZ  . PHE B 1 13  ? 5.555   21.404  -16.923 1.000 145.117 0 13  PHE B CZ  1 
ATOM   1361 N N   . THR B 1 14  ? 7.967   20.350  -23.815 1.000 112.193 0 14  THR B N   1 
ATOM   1362 C CA  . THR B 1 14  ? 8.917   20.399  -24.929 1.000 98.279  0 14  THR B CA  1 
ATOM   1363 C C   . THR B 1 14  ? 8.552   19.332  -25.963 1.000 105.810 0 14  THR B C   1 
ATOM   1364 O O   . THR B 1 14  ? 7.643   18.527  -25.743 1.000 95.528  0 14  THR B O   1 
ATOM   1365 C CB  . THR B 1 14  ? 10.364  20.183  -24.466 1.000 90.082  0 14  THR B CB  1 
ATOM   1366 O OG1 . THR B 1 14  ? 10.515  18.767  -24.337 1.000 91.967  0 14  THR B OG1 1 
ATOM   1367 C CG2 . THR B 1 14  ? 10.710  20.915  -23.183 1.000 84.737  0 14  THR B CG2 1 
ATOM   1368 N N   . ASP B 1 15  ? 9.310   19.311  -27.069 1.000 101.762 0 15  ASP B N   1 
ATOM   1369 C CA  . ASP B 1 15  ? 9.029   18.401  -28.171 1.000 105.956 0 15  ASP B CA  1 
ATOM   1370 C C   . ASP B 1 15  ? 9.425   16.983  -27.796 1.000 91.212  0 15  ASP B C   1 
ATOM   1371 O O   . ASP B 1 15  ? 8.696   16.041  -28.093 1.000 104.303 0 15  ASP B O   1 
ATOM   1372 C CB  . ASP B 1 15  ? 9.696   18.821  -29.472 1.000 96.997  0 15  ASP B CB  1 
ATOM   1373 C CG  . ASP B 1 15  ? 9.203   20.172  -29.964 1.000 104.128 0 15  ASP B CG  1 
ATOM   1374 O OD1 . ASP B 1 15  ? 7.999   20.445  -29.732 1.000 92.635  0 15  ASP B OD1 1 
ATOM   1375 O OD2 . ASP B 1 15  ? 10.023  20.941  -30.528 1.000 106.433 0 15  ASP B OD2 1 
ATOM   1376 N N   . ARG B 1 16  ? 10.565  16.855  -27.119 1.000 89.277  0 16  ARG B N   1 
ATOM   1377 C CA  . ARG B 1 16  ? 11.112  15.546  -26.789 1.000 92.433  0 16  ARG B CA  1 
ATOM   1378 C C   . ARG B 1 16  ? 10.271  14.929  -25.681 1.000 94.335  0 16  ARG B C   1 
ATOM   1379 O O   . ARG B 1 16  ? 10.035  13.710  -25.680 1.000 97.842  0 16  ARG B O   1 
ATOM   1380 C CB  . ARG B 1 16  ? 12.571  15.620  -26.332 1.000 90.003  0 16  ARG B CB  1 
ATOM   1381 C CG  . ARG B 1 16  ? 13.285  16.846  -26.894 1.000 102.128 0 16  ARG B CG  1 
ATOM   1382 C CD  . ARG B 1 16  ? 14.782  16.894  -26.646 1.000 102.336 0 16  ARG B CD  1 
ATOM   1383 N NE  . ARG B 1 16  ? 15.359  15.558  -26.778 1.000 88.240  0 16  ARG B NE  1 
ATOM   1384 C CZ  . ARG B 1 16  ? 16.626  15.361  -26.606 1.000 101.066 0 16  ARG B CZ  1 
ATOM   1385 N NH1 . ARG B 1 16  ? 17.077  14.142  -26.345 1.000 113.907 0 16  ARG B NH1 1 
ATOM   1386 N NH2 . ARG B 1 16  ? 17.409  16.421  -26.581 1.000 101.237 0 16  ARG B NH2 1 
ATOM   1387 N N   . GLN B 1 17  ? 9.832   15.808  -24.765 1.000 84.609  0 17  GLN B N   1 
ATOM   1388 C CA  . GLN B 1 17  ? 8.932   15.427  -23.691 1.000 83.691  0 17  GLN B CA  1 
ATOM   1389 C C   . GLN B 1 17  ? 7.614   14.923  -24.253 1.000 84.949  0 17  GLN B C   1 
ATOM   1390 O O   . GLN B 1 17  ? 7.127   13.882  -23.807 1.000 87.658  0 17  GLN B O   1 
ATOM   1391 C CB  . GLN B 1 17  ? 8.615   16.581  -22.746 1.000 89.737  0 17  GLN B CB  1 
ATOM   1392 C CG  . GLN B 1 17  ? 9.725   16.858  -21.745 1.000 100.175 0 17  GLN B CG  1 
ATOM   1393 C CD  . GLN B 1 17  ? 9.415   18.011  -20.825 1.000 93.731  0 17  GLN B CD  1 
ATOM   1394 O OE1 . GLN B 1 17  ? 8.290   18.518  -20.780 1.000 102.789 0 17  GLN B OE1 1 
ATOM   1395 N NE2 . GLN B 1 17  ? 10.424  18.439  -20.085 1.000 97.872  0 17  GLN B NE2 1 
ATOM   1396 N N   . ASN B 1 18  ? 7.026   15.690  -25.186 1.000 86.875  0 18  ASN B N   1 
ATOM   1397 C CA  . ASN B 1 18  ? 5.713   15.334  -25.697 1.000 93.033  0 18  ASN B CA  1 
ATOM   1398 C C   . ASN B 1 18  ? 5.791   14.061  -26.538 1.000 99.199  0 18  ASN B C   1 
ATOM   1399 O O   . ASN B 1 18  ? 4.821   13.288  -26.579 1.000 87.042  0 18  ASN B O   1 
ATOM   1400 C CB  . ASN B 1 18  ? 5.045   16.487  -26.423 1.000 95.736  0 18  ASN B CB  1 
ATOM   1401 C CG  . ASN B 1 18  ? 4.421   17.460  -25.453 1.000 98.599  0 18  ASN B CG  1 
ATOM   1402 O OD1 . ASN B 1 18  ? 3.517   17.094  -24.680 1.000 83.568  0 18  ASN B OD1 1 
ATOM   1403 N ND2 . ASN B 1 18  ? 4.889   18.700  -25.509 1.000 91.932  0 18  ASN B ND2 1 
ATOM   1404 N N   . LYS B 1 19  ? 6.946   13.837  -27.183 1.000 80.520  0 19  LYS B N   1 
ATOM   1405 C CA  . LYS B 1 19  ? 7.138   12.630  -27.974 1.000 87.663  0 19  LYS B CA  1 
ATOM   1406 C C   . LYS B 1 19  ? 7.131   11.427  -27.029 1.000 86.371  0 19  LYS B C   1 
ATOM   1407 O O   . LYS B 1 19  ? 6.377   10.469  -27.242 1.000 87.652  0 19  LYS B O   1 
ATOM   1408 C CB  . LYS B 1 19  ? 8.425   12.747  -28.808 1.000 92.141  0 19  LYS B CB  1 
ATOM   1409 C CG  . LYS B 1 19  ? 8.633   11.728  -29.941 1.000 85.962  0 19  LYS B CG  1 
ATOM   1410 N N   . ALA B 1 20  ? 7.959   11.522  -25.972 1.000 79.069  0 20  ALA B N   1 
ATOM   1411 C CA  . ALA B 1 20  ? 8.137   10.465  -24.979 1.000 78.412  0 20  ALA B CA  1 
ATOM   1412 C C   . ALA B 1 20  ? 6.823   10.115  -24.283 1.000 73.935  0 20  ALA B C   1 
ATOM   1413 O O   . ALA B 1 20  ? 6.531   8.952   -24.015 1.000 74.192  0 20  ALA B O   1 
ATOM   1414 C CB  . ALA B 1 20  ? 9.150   10.914  -23.959 1.000 81.360  0 20  ALA B CB  1 
ATOM   1415 N N   . TYR B 1 21  ? 6.055   11.160  -23.980 1.000 79.055  0 21  TYR B N   1 
ATOM   1416 C CA  . TYR B 1 21  ? 4.737   11.038  -23.398 1.000 79.136  0 21  TYR B CA  1 
ATOM   1417 C C   . TYR B 1 21  ? 3.891   10.111  -24.264 1.000 87.545  0 21  TYR B C   1 
ATOM   1418 O O   . TYR B 1 21  ? 3.361   9.140   -23.732 1.000 81.704  0 21  TYR B O   1 
ATOM   1419 C CB  . TYR B 1 21  ? 4.235   12.479  -23.253 1.000 80.470  0 21  TYR B CB  1 
ATOM   1420 C CG  . TYR B 1 21  ? 2.942   12.615  -22.460 1.000 78.893  0 21  TYR B CG  1 
ATOM   1421 C CD1 . TYR B 1 21  ? 1.790   11.905  -22.789 1.000 80.034  0 21  TYR B CD1 1 
ATOM   1422 C CD2 . TYR B 1 21  ? 2.888   13.439  -21.343 1.000 80.294  0 21  TYR B CD2 1 
ATOM   1423 C CE1 . TYR B 1 21  ? 0.627   12.030  -22.046 1.000 90.427  0 21  TYR B CE1 1 
ATOM   1424 C CE2 . TYR B 1 21  ? 1.722   13.587  -20.605 1.000 78.104  0 21  TYR B CE2 1 
ATOM   1425 C CZ  . TYR B 1 21  ? 0.582   12.891  -20.962 1.000 82.864  0 21  TYR B CZ  1 
ATOM   1426 O OH  . TYR B 1 21  ? -0.560  12.971  -20.218 1.000 92.330  0 21  TYR B OH  1 
ATOM   1427 N N   . LYS B 1 22  ? 3.783   10.402  -25.580 1.000 100.469 0 22  LYS B N   1 
ATOM   1428 C CA  . LYS B 1 22  ? 2.857   9.681   -26.456 1.000 102.815 0 22  LYS B CA  1 
ATOM   1429 C C   . LYS B 1 22  ? 3.303   8.230   -26.573 1.000 103.008 0 22  LYS B C   1 
ATOM   1430 O O   . LYS B 1 22  ? 2.454   7.341   -26.519 1.000 84.616  0 22  LYS B O   1 
ATOM   1431 C CB  . LYS B 1 22  ? 2.581   10.322  -27.822 1.000 109.361 0 22  LYS B CB  1 
ATOM   1432 C CG  . LYS B 1 22  ? 1.678   11.531  -27.613 1.000 144.691 0 22  LYS B CG  1 
ATOM   1433 C CD  . LYS B 1 22  ? 1.457   12.526  -28.744 1.000 150.009 0 22  LYS B CD  1 
ATOM   1434 C CE  . LYS B 1 22  ? 0.907   13.784  -28.134 1.000 151.612 0 22  LYS B CE  1 
ATOM   1435 N NZ  . LYS B 1 22  ? 0.197   14.607  -29.112 1.000 163.266 0 22  LYS B NZ  1 
ATOM   1436 N N   . GLU B 1 23  ? 4.628   8.011   -26.629 1.000 80.457  0 23  GLU B N   1 
ATOM   1437 C CA  . GLU B 1 23  ? 5.187   6.675   -26.752 1.000 79.919  0 23  GLU B CA  1 
ATOM   1438 C C   . GLU B 1 23  ? 4.905   5.827   -25.516 1.000 85.081  0 23  GLU B C   1 
ATOM   1439 O O   . GLU B 1 23  ? 4.610   4.637   -25.625 1.000 93.077  0 23  GLU B O   1 
ATOM   1440 C CB  . GLU B 1 23  ? 6.689   6.760   -27.014 1.000 90.103  0 23  GLU B CB  1 
ATOM   1441 C CG  . GLU B 1 23  ? 6.988   7.353   -28.385 1.000 101.899 0 23  GLU B CG  1 
ATOM   1442 C CD  . GLU B 1 23  ? 8.432   7.715   -28.608 1.000 107.005 0 23  GLU B CD  1 
ATOM   1443 O OE1 . GLU B 1 23  ? 8.631   8.369   -29.654 1.000 114.933 0 23  GLU B OE1 1 
ATOM   1444 O OE2 . GLU B 1 23  ? 9.303   7.360   -27.768 1.000 99.162  0 23  GLU B OE2 1 
ATOM   1445 N N   . ALA B 1 24  ? 5.027   6.441   -24.341 1.000 83.454  0 24  ALA B N   1 
ATOM   1446 C CA  . ALA B 1 24  ? 4.886   5.723   -23.086 1.000 84.032  0 24  ALA B CA  1 
ATOM   1447 C C   . ALA B 1 24  ? 3.418   5.383   -22.842 1.000 83.698  0 24  ALA B C   1 
ATOM   1448 O O   . ALA B 1 24  ? 3.070   4.392   -22.212 1.000 74.114  0 24  ALA B O   1 
ATOM   1449 C CB  . ALA B 1 24  ? 5.453   6.569   -21.967 1.000 84.178  0 24  ALA B CB  1 
ATOM   1450 N N   . MET B 1 25  ? 2.537   6.244   -23.329 1.000 89.894  0 25  MET B N   1 
ATOM   1451 C CA  . MET B 1 25  ? 1.120   6.038   -23.135 1.000 80.962  0 25  MET B CA  1 
ATOM   1452 C C   . MET B 1 25  ? 0.673   4.934   -24.100 1.000 92.290  0 25  MET B C   1 
ATOM   1453 O O   . MET B 1 25  ? -0.130  4.087   -23.734 1.000 93.457  0 25  MET B O   1 
ATOM   1454 C CB  . MET B 1 25  ? 0.424   7.392   -23.308 1.000 86.362  0 25  MET B CB  1 
ATOM   1455 C CG  . MET B 1 25  ? -1.003  7.421   -22.821 1.000 96.783  0 25  MET B CG  1 
ATOM   1456 S SD  . MET B 1 25  ? -1.254  7.212   -21.046 1.000 100.319 0 25  MET B SD  1 
ATOM   1457 C CE  . MET B 1 25  ? -0.914  8.913   -20.541 1.000 97.559  0 25  MET B CE  1 
ATOM   1458 N N   . GLU B 1 26  ? 1.234   4.904   -25.321 1.000 99.365  0 26  GLU B N   1 
ATOM   1459 C CA  . GLU B 1 26  ? 0.929   3.851   -26.280 1.000 105.466 0 26  GLU B CA  1 
ATOM   1460 C C   . GLU B 1 26  ? 1.404   2.515   -25.720 1.000 102.295 0 26  GLU B C   1 
ATOM   1461 O O   . GLU B 1 26  ? 0.675   1.527   -25.817 1.000 98.215  0 26  GLU B O   1 
ATOM   1462 C CB  . GLU B 1 26  ? 1.569   4.082   -27.652 1.000 104.826 0 26  GLU B CB  1 
ATOM   1463 C CG  . GLU B 1 26  ? 0.858   5.139   -28.493 1.000 120.141 0 26  GLU B CG  1 
ATOM   1464 C CD  . GLU B 1 26  ? 1.740   5.804   -29.546 1.000 118.823 0 26  GLU B CD  1 
ATOM   1465 O OE1 . GLU B 1 26  ? 2.880   5.350   -29.713 1.000 96.257  0 26  GLU B OE1 1 
ATOM   1466 O OE2 . GLU B 1 26  ? 1.336   6.803   -30.178 1.000 117.177 0 26  GLU B OE2 1 
ATOM   1467 N N   . ALA B 1 27  ? 2.615   2.532   -25.133 1.000 92.311  0 27  ALA B N   1 
ATOM   1468 C CA  . ALA B 1 27  ? 3.221   1.372   -24.484 1.000 96.447  0 27  ALA B CA  1 
ATOM   1469 C C   . ALA B 1 27  ? 2.325   0.784   -23.393 1.000 89.298  0 27  ALA B C   1 
ATOM   1470 O O   . ALA B 1 27  ? 2.180   -0.427  -23.304 1.000 95.697  0 27  ALA B O   1 
ATOM   1471 C CB  . ALA B 1 27  ? 4.568   1.743   -23.909 1.000 98.204  0 27  ALA B CB  1 
ATOM   1472 N N   . LEU B 1 28  ? 1.734   1.640   -22.559 1.000 92.060  0 28  LEU B N   1 
ATOM   1473 C CA  . LEU B 1 28  ? 0.933   1.187   -21.437 1.000 98.035  0 28  LEU B CA  1 
ATOM   1474 C C   . LEU B 1 28  ? -0.378  0.595   -21.928 1.000 102.869 0 28  LEU B C   1 
ATOM   1475 O O   . LEU B 1 28  ? -0.801  -0.433  -21.401 1.000 100.536 0 28  LEU B O   1 
ATOM   1476 C CB  . LEU B 1 28  ? 0.711   2.344   -20.465 1.000 105.512 0 28  LEU B CB  1 
ATOM   1477 C CG  . LEU B 1 28  ? 1.982   2.871   -19.780 1.000 100.653 0 28  LEU B CG  1 
ATOM   1478 C CD1 . LEU B 1 28  ? 1.650   4.108   -18.987 1.000 97.924  0 28  LEU B CD1 1 
ATOM   1479 C CD2 . LEU B 1 28  ? 2.662   1.866   -18.866 1.000 98.440  0 28  LEU B CD2 1 
ATOM   1480 N N   . LYS B 1 29  ? -0.992  1.241   -22.939 1.000 99.448  0 29  LYS B N   1 
ATOM   1481 C CA  . LYS B 1 29  ? -2.237  0.760   -23.525 1.000 91.819  0 29  LYS B CA  1 
ATOM   1482 C C   . LYS B 1 29  ? -2.053  -0.708  -23.940 1.000 92.430  0 29  LYS B C   1 
ATOM   1483 O O   . LYS B 1 29  ? -2.995  -1.485  -23.774 1.000 74.855  0 29  LYS B O   1 
ATOM   1484 C CB  . LYS B 1 29  ? -2.759  1.723   -24.602 1.000 79.392  0 29  LYS B CB  1 
ATOM   1485 N N   . GLU B 1 30  ? -0.829  -1.091  -24.383 1.000 89.008  0 30  GLU B N   1 
ATOM   1486 C CA  . GLU B 1 30  ? -0.515  -2.439  -24.860 1.000 99.859  0 30  GLU B CA  1 
ATOM   1487 C C   . GLU B 1 30  ? 0.058   -3.349  -23.753 1.000 91.531  0 30  GLU B C   1 
ATOM   1488 O O   . GLU B 1 30  ? 0.390   -4.495  -24.018 1.000 99.236  0 30  GLU B O   1 
ATOM   1489 C CB  . GLU B 1 30  ? 0.407   -2.369  -26.091 1.000 88.297  0 30  GLU B CB  1 
ATOM   1490 N N   . ASN B 1 31  ? 0.212   -2.873  -22.510 1.000 99.218  0 31  ASN B N   1 
ATOM   1491 C CA  . ASN B 1 31  ? 0.826   -3.689  -21.465 1.000 88.821  0 31  ASN B CA  1 
ATOM   1492 C C   . ASN B 1 31  ? -0.269  -4.390  -20.666 1.000 92.597  0 31  ASN B C   1 
ATOM   1493 O O   . ASN B 1 31  ? -1.073  -3.742  -19.995 1.000 97.249  0 31  ASN B O   1 
ATOM   1494 C CB  . ASN B 1 31  ? 1.717   -2.879  -20.525 1.000 80.931  0 31  ASN B CB  1 
ATOM   1495 C CG  . ASN B 1 31  ? 2.421   -3.740  -19.493 1.000 85.788  0 31  ASN B CG  1 
ATOM   1496 O OD1 . ASN B 1 31  ? 1.790   -4.534  -18.769 1.000 71.865  0 31  ASN B OD1 1 
ATOM   1497 N ND2 . ASN B 1 31  ? 3.734   -3.588  -19.386 1.000 84.873  0 31  ASN B ND2 1 
ATOM   1498 N N   . PRO B 1 32  ? -0.304  -5.737  -20.649 1.000 98.491  0 32  PRO B N   1 
ATOM   1499 C CA  . PRO B 1 32  ? -1.375  -6.454  -19.945 1.000 92.093  0 32  PRO B CA  1 
ATOM   1500 C C   . PRO B 1 32  ? -1.357  -6.436  -18.418 1.000 91.284  0 32  PRO B C   1 
ATOM   1501 O O   . PRO B 1 32  ? -2.287  -6.969  -17.816 1.000 80.083  0 32  PRO B O   1 
ATOM   1502 C CB  . PRO B 1 32  ? -1.169  -7.897  -20.468 1.000 83.429  0 32  PRO B CB  1 
ATOM   1503 C CG  . PRO B 1 32  ? 0.328   -8.002  -20.704 1.000 81.791  0 32  PRO B CG  1 
ATOM   1504 C CD  . PRO B 1 32  ? 0.688   -6.631  -21.283 1.000 80.382  0 32  PRO B CD  1 
ATOM   1505 N N   . THR B 1 33  ? -0.297  -5.871  -17.797 1.000 100.508 0 33  THR B N   1 
ATOM   1506 C CA  . THR B 1 33  ? -0.162  -5.918  -16.339 1.000 101.198 0 33  THR B CA  1 
ATOM   1507 C C   . THR B 1 33  ? -0.634  -4.600  -15.721 1.000 83.662  0 33  THR B C   1 
ATOM   1508 O O   . THR B 1 33  ? -0.643  -4.446  -14.506 1.000 84.574  0 33  THR B O   1 
ATOM   1509 C CB  . THR B 1 33  ? 1.256   -6.295  -15.883 1.000 92.267  0 33  THR B CB  1 
ATOM   1510 O OG1 . THR B 1 33  ? 2.226   -5.380  -16.393 1.000 80.894  0 33  THR B OG1 1 
ATOM   1511 C CG2 . THR B 1 33  ? 1.653   -7.701  -16.294 1.000 85.853  0 33  THR B CG2 1 
ATOM   1512 N N   . ILE B 1 34  ? -1.109  -3.681  -16.562 1.000 89.490  0 34  ILE B N   1 
ATOM   1513 C CA  . ILE B 1 34  ? -1.458  -2.334  -16.142 1.000 90.430  0 34  ILE B CA  1 
ATOM   1514 C C   . ILE B 1 34  ? -2.962  -2.102  -16.262 1.000 83.021  0 34  ILE B C   1 
ATOM   1515 O O   . ILE B 1 34  ? -3.531  -2.410  -17.292 1.000 81.805  0 34  ILE B O   1 
ATOM   1516 C CB  . ILE B 1 34  ? -0.708  -1.326  -17.028 1.000 86.531  0 34  ILE B CB  1 
ATOM   1517 C CG1 . ILE B 1 34  ? 0.788   -1.266  -16.706 1.000 84.900  0 34  ILE B CG1 1 
ATOM   1518 C CG2 . ILE B 1 34  ? -1.373  0.045   -16.941 1.000 100.280 0 34  ILE B CG2 1 
ATOM   1519 C CD1 . ILE B 1 34  ? 1.100   -0.789  -15.303 1.000 94.165  0 34  ILE B CD1 1 
ATOM   1520 N N   . ASP B 1 35  ? -3.575  -1.468  -15.257 1.000 80.174  0 35  ASP B N   1 
ATOM   1521 C CA  . ASP B 1 35  ? -4.924  -0.927  -15.381 1.000 81.268  0 35  ASP B CA  1 
ATOM   1522 C C   . ASP B 1 35  ? -4.826  0.577   -15.640 1.000 81.450  0 35  ASP B C   1 
ATOM   1523 O O   . ASP B 1 35  ? -4.792  1.365   -14.703 1.000 86.268  0 35  ASP B O   1 
ATOM   1524 C CB  . ASP B 1 35  ? -5.795  -1.302  -14.183 1.000 73.710  0 35  ASP B CB  1 
ATOM   1525 C CG  . ASP B 1 35  ? -7.155  -0.623  -14.053 1.000 79.892  0 35  ASP B CG  1 
ATOM   1526 O OD1 . ASP B 1 35  ? -7.509  0.167   -14.968 1.000 84.196  0 35  ASP B OD1 1 
ATOM   1527 O OD2 . ASP B 1 35  ? -7.855  -0.887  -13.028 1.000 72.689  0 35  ASP B OD2 1 
ATOM   1528 N N   . LEU B 1 36  ? -4.821  0.979   -16.919 1.000 80.395  0 36  LEU B N   1 
ATOM   1529 C CA  . LEU B 1 36  ? -4.627  2.378   -17.278 1.000 78.514  0 36  LEU B CA  1 
ATOM   1530 C C   . LEU B 1 36  ? -5.869  3.209   -16.990 1.000 75.123  0 36  LEU B C   1 
ATOM   1531 O O   . LEU B 1 36  ? -5.761  4.413   -16.775 1.000 78.478  0 36  LEU B O   1 
ATOM   1532 C CB  . LEU B 1 36  ? -4.232  2.481   -18.748 1.000 83.222  0 36  LEU B CB  1 
ATOM   1533 C CG  . LEU B 1 36  ? -3.749  3.841   -19.255 1.000 94.823  0 36  LEU B CG  1 
ATOM   1534 C CD1 . LEU B 1 36  ? -2.626  4.447   -18.438 1.000 106.294 0 36  LEU B CD1 1 
ATOM   1535 C CD2 . LEU B 1 36  ? -3.260  3.656   -20.690 1.000 111.625 0 36  LEU B CD2 1 
ATOM   1536 N N   . GLU B 1 37  ? -7.040  2.568   -17.004 1.000 84.844  0 37  GLU B N   1 
ATOM   1537 C CA  . GLU B 1 37  ? -8.293  3.286   -16.853 1.000 95.764  0 37  GLU B CA  1 
ATOM   1538 C C   . GLU B 1 37  ? -8.387  3.820   -15.425 1.000 85.827  0 37  GLU B C   1 
ATOM   1539 O O   . GLU B 1 37  ? -9.024  4.840   -15.188 1.000 82.441  0 37  GLU B O   1 
ATOM   1540 C CB  . GLU B 1 37  ? -9.476  2.399   -17.261 1.000 115.799 0 37  GLU B CB  1 
ATOM   1541 C CG  . GLU B 1 37  ? -10.436 3.059   -18.254 1.000 120.339 0 37  GLU B CG  1 
ATOM   1542 C CD  . GLU B 1 37  ? -11.266 4.216   -17.717 1.000 111.432 0 37  GLU B CD  1 
ATOM   1543 O OE1 . GLU B 1 37  ? -12.047 3.984   -16.772 1.000 103.592 0 37  GLU B OE1 1 
ATOM   1544 O OE2 . GLU B 1 37  ? -11.153 5.340   -18.249 1.000 93.428  0 37  GLU B OE2 1 
ATOM   1545 N N   . ASN B 1 38  ? -7.755  3.136   -14.469 1.000 82.561  0 38  ASN B N   1 
ATOM   1546 C CA  . ASN B 1 38  ? -7.881  3.512   -13.066 1.000 85.353  0 38  ASN B CA  1 
ATOM   1547 C C   . ASN B 1 38  ? -6.561  4.065   -12.526 1.000 87.422  0 38  ASN B C   1 
ATOM   1548 O O   . ASN B 1 38  ? -6.411  4.215   -11.305 1.000 76.147  0 38  ASN B O   1 
ATOM   1549 C CB  . ASN B 1 38  ? -8.328  2.352   -12.185 1.000 81.469  0 38  ASN B CB  1 
ATOM   1550 C CG  . ASN B 1 38  ? -9.740  1.912   -12.467 1.000 80.140  0 38  ASN B CG  1 
ATOM   1551 O OD1 . ASN B 1 38  ? -9.979  0.704   -12.593 1.000 90.112  0 38  ASN B OD1 1 
ATOM   1552 N ND2 . ASN B 1 38  ? -10.672 2.855   -12.523 1.000 75.440  0 38  ASN B ND2 1 
ATOM   1553 N N   . SER B 1 39  ? -5.645  4.377   -13.458 1.000 81.519  0 39  SER B N   1 
ATOM   1554 C CA  . SER B 1 39  ? -4.386  5.033   -13.160 1.000 72.869  0 39  SER B CA  1 
ATOM   1555 C C   . SER B 1 39  ? -4.611  6.538   -13.049 1.000 76.423  0 39  SER B C   1 
ATOM   1556 O O   . SER B 1 39  ? -5.684  7.042   -13.389 1.000 70.389  0 39  SER B O   1 
ATOM   1557 C CB  . SER B 1 39  ? -3.348  4.697   -14.205 1.000 72.484  0 39  SER B CB  1 
ATOM   1558 O OG  . SER B 1 39  ? -2.993  3.319   -14.144 1.000 81.147  0 39  SER B OG  1 
ATOM   1559 N N   . TYR B 1 40  ? -3.615  7.246   -12.505 1.000 87.264  0 40  TYR B N   1 
ATOM   1560 C CA  . TYR B 1 40  ? -3.712  8.690   -12.354 1.000 79.394  0 40  TYR B CA  1 
ATOM   1561 C C   . TYR B 1 40  ? -2.824  9.307   -13.418 1.000 82.091  0 40  TYR B C   1 
ATOM   1562 O O   . TYR B 1 40  ? -1.596  9.200   -13.384 1.000 71.910  0 40  TYR B O   1 
ATOM   1563 C CB  . TYR B 1 40  ? -3.329  9.291   -11.002 1.000 71.835  0 40  TYR B CB  1 
ATOM   1564 C CG  . TYR B 1 40  ? -3.520  10.800  -10.827 1.000 69.104  0 40  TYR B CG  1 
ATOM   1565 C CD1 . TYR B 1 40  ? -2.501  11.698  -11.124 1.000 67.737  0 40  TYR B CD1 1 
ATOM   1566 C CD2 . TYR B 1 40  ? -4.693  11.327  -10.283 1.000 63.375  0 40  TYR B CD2 1 
ATOM   1567 C CE1 . TYR B 1 40  ? -2.649  13.063  -10.914 1.000 71.646  0 40  TYR B CE1 1 
ATOM   1568 C CE2 . TYR B 1 40  ? -4.873  12.690  -10.091 1.000 62.881  0 40  TYR B CE2 1 
ATOM   1569 C CZ  . TYR B 1 40  ? -3.845  13.569  -10.420 1.000 80.765  0 40  TYR B CZ  1 
ATOM   1570 O OH  . TYR B 1 40  ? -3.952  14.929  -10.248 1.000 69.857  0 40  TYR B OH  1 
ATOM   1571 N N   . VAL B 1 41  ? -3.507  9.913   -14.385 1.000 86.741  0 41  VAL B N   1 
ATOM   1572 C CA  . VAL B 1 41  ? -2.873  10.680  -15.431 1.000 81.488  0 41  VAL B CA  1 
ATOM   1573 C C   . VAL B 1 41  ? -3.129  12.143  -15.115 1.000 87.539  0 41  VAL B C   1 
ATOM   1574 O O   . VAL B 1 41  ? -4.282  12.587  -15.166 1.000 79.802  0 41  VAL B O   1 
ATOM   1575 C CB  . VAL B 1 41  ? -3.494  10.331  -16.789 1.000 82.112  0 41  VAL B CB  1 
ATOM   1576 C CG1 . VAL B 1 41  ? -2.840  11.174  -17.889 1.000 87.836  0 41  VAL B CG1 1 
ATOM   1577 C CG2 . VAL B 1 41  ? -3.453  8.831   -17.044 1.000 76.565  0 41  VAL B CG2 1 
ATOM   1578 N N   . PRO B 1 42  ? -2.081  12.925  -14.791 1.000 81.519  0 42  PRO B N   1 
ATOM   1579 C CA  . PRO B 1 42  ? -2.274  14.320  -14.393 1.000 77.732  0 42  PRO B CA  1 
ATOM   1580 C C   . PRO B 1 42  ? -3.113  15.167  -15.347 1.000 85.192  0 42  PRO B C   1 
ATOM   1581 O O   . PRO B 1 42  ? -4.034  15.869  -14.919 1.000 78.601  0 42  PRO B O   1 
ATOM   1582 C CB  . PRO B 1 42  ? -0.828  14.791  -14.310 1.000 79.356  0 42  PRO B CB  1 
ATOM   1583 C CG  . PRO B 1 42  ? -0.095  13.560  -13.846 1.000 76.365  0 42  PRO B CG  1 
ATOM   1584 C CD  . PRO B 1 42  ? -0.681  12.476  -14.712 1.000 83.885  0 42  PRO B CD  1 
ATOM   1585 N N   . LEU B 1 43  ? -2.815  15.073  -16.643 1.000 89.938  0 43  LEU B N   1 
ATOM   1586 C CA  . LEU B 1 43  ? -3.415  15.999  -17.592 1.000 87.663  0 43  LEU B CA  1 
ATOM   1587 C C   . LEU B 1 43  ? -4.923  15.748  -17.694 1.000 87.769  0 43  LEU B C   1 
ATOM   1588 O O   . LEU B 1 43  ? -5.670  16.668  -18.001 1.000 99.825  0 43  LEU B O   1 
ATOM   1589 C CB  . LEU B 1 43  ? -2.693  15.857  -18.926 1.000 91.504  0 43  LEU B CB  1 
ATOM   1590 C CG  . LEU B 1 43  ? -2.090  17.129  -19.538 1.000 99.075  0 43  LEU B CG  1 
ATOM   1591 C CD1 . LEU B 1 43  ? -1.538  18.183  -18.579 1.000 90.564  0 43  LEU B CD1 1 
ATOM   1592 C CD2 . LEU B 1 43  ? -0.941  16.652  -20.474 1.000 101.267 0 43  LEU B CD2 1 
ATOM   1593 N N   . ASP B 1 44  ? -5.388  14.541  -17.336 1.000 89.583  0 44  ASP B N   1 
ATOM   1594 C CA  . ASP B 1 44  ? -6.814  14.236  -17.295 1.000 94.449  0 44  ASP B CA  1 
ATOM   1595 C C   . ASP B 1 44  ? -7.433  14.560  -15.937 1.000 90.824  0 44  ASP B C   1 
ATOM   1596 O O   . ASP B 1 44  ? -8.589  14.231  -15.718 1.000 80.985  0 44  ASP B O   1 
ATOM   1597 C CB  . ASP B 1 44  ? -7.091  12.763  -17.576 1.000 102.043 0 44  ASP B CB  1 
ATOM   1598 C CG  . ASP B 1 44  ? -6.475  12.180  -18.844 1.000 109.342 0 44  ASP B CG  1 
ATOM   1599 O OD1 . ASP B 1 44  ? -6.160  12.964  -19.777 1.000 108.623 0 44  ASP B OD1 1 
ATOM   1600 O OD2 . ASP B 1 44  ? -6.284  10.942  -18.871 1.000 92.121  0 44  ASP B OD2 1 
ATOM   1601 N N   . ASN B 1 45  ? -6.679  15.192  -15.027 1.000 96.686  0 45  ASN B N   1 
ATOM   1602 C CA  . ASN B 1 45  ? -7.126  15.407  -13.654 1.000 91.640  0 45  ASN B CA  1 
ATOM   1603 C C   . ASN B 1 45  ? -6.794  16.832  -13.202 1.000 96.050  0 45  ASN B C   1 
ATOM   1604 O O   . ASN B 1 45  ? -6.450  17.066  -12.042 1.000 111.572 0 45  ASN B O   1 
ATOM   1605 C CB  . ASN B 1 45  ? -6.500  14.403  -12.694 1.000 80.912  0 45  ASN B CB  1 
ATOM   1606 C CG  . ASN B 1 45  ? -6.975  12.991  -12.929 1.000 78.824  0 45  ASN B CG  1 
ATOM   1607 O OD1 . ASN B 1 45  ? -6.284  12.183  -13.556 1.000 86.018  0 45  ASN B OD1 1 
ATOM   1608 N ND2 . ASN B 1 45  ? -8.155  12.661  -12.449 1.000 70.479  0 45  ASN B ND2 1 
ATOM   1609 N N   . GLN B 1 46  ? -6.902  17.783  -14.133 1.000 88.643  0 46  GLN B N   1 
ATOM   1610 C CA  . GLN B 1 46  ? -6.681  19.195  -13.863 1.000 95.992  0 46  GLN B CA  1 
ATOM   1611 C C   . GLN B 1 46  ? -7.803  19.670  -12.945 1.000 82.031  0 46  GLN B C   1 
ATOM   1612 O O   . GLN B 1 46  ? -8.934  19.280  -13.176 1.000 83.852  0 46  GLN B O   1 
ATOM   1613 C CB  . GLN B 1 46  ? -6.724  20.058  -15.133 1.000 103.728 0 46  GLN B CB  1 
ATOM   1614 C CG  . GLN B 1 46  ? -6.361  19.340  -16.437 1.000 103.345 0 46  GLN B CG  1 
ATOM   1615 C CD  . GLN B 1 46  ? -5.839  20.216  -17.563 1.000 101.838 0 46  GLN B CD  1 
ATOM   1616 O OE1 . GLN B 1 46  ? -5.848  19.794  -18.719 1.000 100.574 0 46  GLN B OE1 1 
ATOM   1617 N NE2 . GLN B 1 46  ? -5.364  21.425  -17.289 1.000 105.000 0 46  GLN B NE2 1 
ATOM   1618 N N   . TYR B 1 47  ? -7.505  20.514  -11.946 1.000 78.546  0 47  TYR B N   1 
ATOM   1619 C CA  . TYR B 1 47  ? -8.483  20.829  -10.912 1.000 85.145  0 47  TYR B CA  1 
ATOM   1620 C C   . TYR B 1 47  ? -9.634  21.612  -11.545 1.000 86.406  0 47  TYR B C   1 
ATOM   1621 O O   . TYR B 1 47  ? -9.366  22.605  -12.227 1.000 79.563  0 47  TYR B O   1 
ATOM   1622 C CB  . TYR B 1 47  ? -7.856  21.660  -9.780  1.000 89.116  0 47  TYR B CB  1 
ATOM   1623 C CG  . TYR B 1 47  ? -8.774  21.936  -8.592  1.000 85.874  0 47  TYR B CG  1 
ATOM   1624 C CD1 . TYR B 1 47  ? -9.417  20.883  -7.938  1.000 91.701  0 47  TYR B CD1 1 
ATOM   1625 C CD2 . TYR B 1 47  ? -9.030  23.238  -8.144  1.000 81.049  0 47  TYR B CD2 1 
ATOM   1626 C CE1 . TYR B 1 47  ? -10.263 21.106  -6.861  1.000 82.827  0 47  TYR B CE1 1 
ATOM   1627 C CE2 . TYR B 1 47  ? -9.900  23.476  -7.083  1.000 81.704  0 47  TYR B CE2 1 
ATOM   1628 C CZ  . TYR B 1 47  ? -10.500 22.405  -6.427  1.000 85.468  0 47  TYR B CZ  1 
ATOM   1629 O OH  . TYR B 1 47  ? -11.362 22.590  -5.376  1.000 88.240  0 47  TYR B OH  1 
ATOM   1630 N N   . LYS B 1 48  ? -10.882 21.162  -11.298 1.000 89.973  0 48  LYS B N   1 
ATOM   1631 C CA  . LYS B 1 48  ? -12.096 21.782  -11.833 1.000 92.975  0 48  LYS B CA  1 
ATOM   1632 C C   . LYS B 1 48  ? -12.012 22.013  -13.345 1.000 99.402  0 48  LYS B C   1 
ATOM   1633 O O   . LYS B 1 48  ? -12.527 23.002  -13.854 1.000 96.121  0 48  LYS B O   1 
ATOM   1634 C CB  . LYS B 1 48  ? -12.378 23.095  -11.093 1.000 96.841  0 48  LYS B CB  1 
ATOM   1635 C CG  . LYS B 1 48  ? -12.989 22.853  -9.719  1.000 120.593 0 48  LYS B CG  1 
ATOM   1636 C CD  . LYS B 1 48  ? -13.346 24.057  -8.852  1.000 126.095 0 48  LYS B CD  1 
ATOM   1637 C CE  . LYS B 1 48  ? -14.259 23.608  -7.738  1.000 127.795 0 48  LYS B CE  1 
ATOM   1638 N NZ  . LYS B 1 48  ? -14.391 24.645  -6.711  1.000 142.957 0 48  LYS B NZ  1 
ATOM   1639 N N   . GLY B 1 49  ? -11.322 21.106  -14.044 1.000 106.419 0 49  GLY B N   1 
ATOM   1640 C CA  . GLY B 1 49  ? -11.164 21.148  -15.487 1.000 101.931 0 49  GLY B CA  1 
ATOM   1641 C C   . GLY B 1 49  ? -10.560 22.443  -16.039 1.000 97.993  0 49  GLY B C   1 
ATOM   1642 O O   . GLY B 1 49  ? -10.602 22.643  -17.245 1.000 127.219 0 49  GLY B O   1 
ATOM   1643 N N   . ILE B 1 50  ? -9.962  23.314  -15.218 1.000 100.108 0 50  ILE B N   1 
ATOM   1644 C CA  . ILE B 1 50  ? -9.534  24.605  -15.747 1.000 109.929 0 50  ILE B CA  1 
ATOM   1645 C C   . ILE B 1 50  ? -8.200  24.407  -16.468 1.000 101.179 0 50  ILE B C   1 
ATOM   1646 O O   . ILE B 1 50  ? -7.280  23.835  -15.886 1.000 104.357 0 50  ILE B O   1 
ATOM   1647 C CB  . ILE B 1 50  ? -9.480  25.725  -14.677 1.000 118.041 0 50  ILE B CB  1 
ATOM   1648 C CG1 . ILE B 1 50  ? -8.129  25.818  -13.961 1.000 135.236 0 50  ILE B CG1 1 
ATOM   1649 C CG2 . ILE B 1 50  ? -10.632 25.643  -13.668 1.000 97.072  0 50  ILE B CG2 1 
ATOM   1650 C CD1 . ILE B 1 50  ? -7.108  26.691  -14.673 1.000 134.888 0 50  ILE B CD1 1 
ATOM   1651 N N   . ARG B 1 51  ? -8.112  24.898  -17.717 1.000 107.893 0 51  ARG B N   1 
ATOM   1652 C CA  . ARG B 1 51  ? -6.918  24.765  -18.540 1.000 120.384 0 51  ARG B CA  1 
ATOM   1653 C C   . ARG B 1 51  ? -6.080  26.041  -18.342 1.000 123.369 0 51  ARG B C   1 
ATOM   1654 O O   . ARG B 1 51  ? -6.474  27.130  -18.766 1.000 109.429 0 51  ARG B O   1 
ATOM   1655 C CB  . ARG B 1 51  ? -7.345  24.330  -19.961 1.000 94.586  0 51  ARG B CB  1 
ATOM   1656 N N   . VAL B 1 52  ? -4.923  25.885  -17.666 1.000 125.288 0 52  VAL B N   1 
ATOM   1657 C CA  . VAL B 1 52  ? -4.025  26.975  -17.283 1.000 121.678 0 52  VAL B CA  1 
ATOM   1658 C C   . VAL B 1 52  ? -3.336  27.613  -18.490 1.000 121.403 0 52  VAL B C   1 
ATOM   1659 O O   . VAL B 1 52  ? -2.682  28.647  -18.349 1.000 117.982 0 52  VAL B O   1 
ATOM   1660 C CB  . VAL B 1 52  ? -2.935  26.493  -16.302 1.000 126.128 0 52  VAL B CB  1 
ATOM   1661 C CG1 . VAL B 1 52  ? -3.367  26.614  -14.850 1.000 129.272 0 52  VAL B CG1 1 
ATOM   1662 C CG2 . VAL B 1 52  ? -2.451  25.081  -16.627 1.000 121.475 0 52  VAL B CG2 1 
ATOM   1663 N N   . ASP B 1 53  ? -3.400  26.954  -19.647 1.000 135.795 0 53  ASP B N   1 
ATOM   1664 C CA  . ASP B 1 53  ? -2.937  27.559  -20.885 1.000 129.142 0 53  ASP B CA  1 
ATOM   1665 C C   . ASP B 1 53  ? -3.877  28.716  -21.236 1.000 120.613 0 53  ASP B C   1 
ATOM   1666 O O   . ASP B 1 53  ? -3.427  29.804  -21.604 1.000 99.885  0 53  ASP B O   1 
ATOM   1667 C CB  . ASP B 1 53  ? -2.721  26.541  -22.003 1.000 121.901 0 53  ASP B CB  1 
ATOM   1668 C CG  . ASP B 1 53  ? -3.423  25.193  -21.878 1.000 129.009 0 53  ASP B CG  1 
ATOM   1669 O OD1 . ASP B 1 53  ? -2.916  24.348  -21.108 1.000 155.748 0 53  ASP B OD1 1 
ATOM   1670 O OD2 . ASP B 1 53  ? -4.465  24.988  -22.540 1.000 109.414 0 53  ASP B OD2 1 
ATOM   1671 N N   . GLU B 1 54  ? -5.183  28.497  -21.047 1.000 121.886 0 54  GLU B N   1 
ATOM   1672 C CA  . GLU B 1 54  ? -6.201  29.425  -21.509 1.000 117.187 0 54  GLU B CA  1 
ATOM   1673 C C   . GLU B 1 54  ? -6.545  30.442  -20.422 1.000 126.244 0 54  GLU B C   1 
ATOM   1674 O O   . GLU B 1 54  ? -7.185  31.451  -20.730 1.000 106.173 0 54  GLU B O   1 
ATOM   1675 C CB  . GLU B 1 54  ? -7.456  28.657  -21.932 1.000 137.517 0 54  GLU B CB  1 
ATOM   1676 C CG  . GLU B 1 54  ? -7.187  27.522  -22.918 1.000 142.940 0 54  GLU B CG  1 
ATOM   1677 C CD  . GLU B 1 54  ? -8.351  26.549  -23.056 1.000 141.601 0 54  GLU B CD  1 
ATOM   1678 O OE1 . GLU B 1 54  ? -8.206  25.487  -23.699 1.000 132.975 0 54  GLU B OE1 1 
ATOM   1679 O OE2 . GLU B 1 54  ? -9.420  26.842  -22.488 1.000 140.150 0 54  GLU B OE2 1 
ATOM   1680 N N   . HIS B 1 55  ? -6.150  30.174  -19.159 1.000 128.110 0 55  HIS B N   1 
ATOM   1681 C CA  . HIS B 1 55  ? -6.440  31.092  -18.069 1.000 117.149 0 55  HIS B CA  1 
ATOM   1682 C C   . HIS B 1 55  ? -5.227  31.243  -17.145 1.000 116.380 0 55  HIS B C   1 
ATOM   1683 O O   . HIS B 1 55  ? -5.268  30.860  -15.979 1.000 127.086 0 55  HIS B O   1 
ATOM   1684 C CB  . HIS B 1 55  ? -7.712  30.676  -17.314 1.000 118.091 0 55  HIS B CB  1 
ATOM   1685 C CG  . HIS B 1 55  ? -8.910  30.309  -18.146 1.000 135.771 0 55  HIS B CG  1 
ATOM   1686 N ND1 . HIS B 1 55  ? -9.860  31.212  -18.587 1.000 128.342 0 55  HIS B ND1 1 
ATOM   1687 C CD2 . HIS B 1 55  ? -9.317  29.098  -18.582 1.000 132.429 0 55  HIS B CD2 1 
ATOM   1688 C CE1 . HIS B 1 55  ? -10.794 30.563  -19.273 1.000 129.454 0 55  HIS B CE1 1 
ATOM   1689 N NE2 . HIS B 1 55  ? -10.499 29.275  -19.259 1.000 133.786 0 55  HIS B NE2 1 
ATOM   1690 N N   . PRO B 1 56  ? -4.109  31.856  -17.596 1.000 112.123 0 56  PRO B N   1 
ATOM   1691 C CA  . PRO B 1 56  ? -2.902  31.976  -16.762 1.000 116.892 0 56  PRO B CA  1 
ATOM   1692 C C   . PRO B 1 56  ? -3.033  32.823  -15.492 1.000 113.467 0 56  PRO B C   1 
ATOM   1693 O O   . PRO B 1 56  ? -2.063  32.963  -14.750 1.000 91.484  0 56  PRO B O   1 
ATOM   1694 C CB  . PRO B 1 56  ? -1.820  32.583  -17.679 1.000 113.303 0 56  PRO B CB  1 
ATOM   1695 C CG  . PRO B 1 56  ? -2.428  32.566  -19.059 1.000 121.205 0 56  PRO B CG  1 
ATOM   1696 C CD  . PRO B 1 56  ? -3.945  32.469  -18.918 1.000 110.851 0 56  PRO B CD  1 
ATOM   1697 N N   . GLU B 1 57  ? -4.216  33.420  -15.271 1.000 116.048 0 57  GLU B N   1 
ATOM   1698 C CA  . GLU B 1 57  ? -4.471  34.151  -14.040 1.000 99.912  0 57  GLU B CA  1 
ATOM   1699 C C   . GLU B 1 57  ? -4.454  33.188  -12.850 1.000 91.050  0 57  GLU B C   1 
ATOM   1700 O O   . GLU B 1 57  ? -4.334  33.633  -11.719 1.000 91.329  0 57  GLU B O   1 
ATOM   1701 C CB  . GLU B 1 57  ? -5.761  34.981  -14.074 1.000 96.198  0 57  GLU B CB  1 
ATOM   1702 C CG  . GLU B 1 57  ? -7.071  34.204  -14.240 1.000 110.857 0 57  GLU B CG  1 
ATOM   1703 C CD  . GLU B 1 57  ? -7.637  34.036  -15.648 1.000 112.738 0 57  GLU B CD  1 
ATOM   1704 O OE1 . GLU B 1 57  ? -6.888  34.133  -16.654 1.000 89.517  0 57  GLU B OE1 1 
ATOM   1705 O OE2 . GLU B 1 57  ? -8.877  33.816  -15.708 1.000 100.428 0 57  GLU B OE2 1 
ATOM   1706 N N   . TYR B 1 58  ? -4.561  31.877  -13.101 1.000 92.511  0 58  TYR B N   1 
ATOM   1707 C CA  . TYR B 1 58  ? -4.653  30.891  -12.033 1.000 91.080  0 58  TYR B CA  1 
ATOM   1708 C C   . TYR B 1 58  ? -3.269  30.541  -11.475 1.000 87.339  0 58  TYR B C   1 
ATOM   1709 O O   . TYR B 1 58  ? -3.168  29.934  -10.418 1.000 83.214  0 58  TYR B O   1 
ATOM   1710 C CB  . TYR B 1 58  ? -5.444  29.680  -12.549 1.000 89.519  0 58  TYR B CB  1 
ATOM   1711 C CG  . TYR B 1 58  ? -6.953  29.902  -12.531 1.000 101.361 0 58  TYR B CG  1 
ATOM   1712 C CD1 . TYR B 1 58  ? -7.616  30.427  -13.634 1.000 99.029  0 58  TYR B CD1 1 
ATOM   1713 C CD2 . TYR B 1 58  ? -7.720  29.609  -11.403 1.000 110.986 0 58  TYR B CD2 1 
ATOM   1714 C CE1 . TYR B 1 58  ? -8.982  30.669  -13.614 1.000 98.163  0 58  TYR B CE1 1 
ATOM   1715 C CE2 . TYR B 1 58  ? -9.086  29.828  -11.378 1.000 111.124 0 58  TYR B CE2 1 
ATOM   1716 C CZ  . TYR B 1 58  ? -9.718  30.359  -12.487 1.000 102.849 0 58  TYR B CZ  1 
ATOM   1717 O OH  . TYR B 1 58  ? -11.055 30.598  -12.436 1.000 113.402 0 58  TYR B OH  1 
ATOM   1718 N N   . LEU B 1 59  ? -2.206  30.973  -12.156 1.000 84.172  0 59  LEU B N   1 
ATOM   1719 C CA  . LEU B 1 59  ? -0.852  30.806  -11.672 1.000 86.662  0 59  LEU B CA  1 
ATOM   1720 C C   . LEU B 1 59  ? -0.547  31.701  -10.472 1.000 83.975  0 59  LEU B C   1 
ATOM   1721 O O   . LEU B 1 59  ? 0.531   31.580  -9.896  1.000 99.460  0 59  LEU B O   1 
ATOM   1722 C CB  . LEU B 1 59  ? 0.091   31.116  -12.833 1.000 113.719 0 59  LEU B CB  1 
ATOM   1723 C CG  . LEU B 1 59  ? 0.566   29.920  -13.667 1.000 115.620 0 59  LEU B CG  1 
ATOM   1724 C CD1 . LEU B 1 59  ? -0.498  28.917  -14.141 1.000 83.109  0 59  LEU B CD1 1 
ATOM   1725 C CD2 . LEU B 1 59  ? 1.373   30.565  -14.808 1.000 127.994 0 59  LEU B CD2 1 
ATOM   1726 N N   . HIS B 1 60  ? -1.415  32.649  -10.122 1.000 80.086  0 60  HIS B N   1 
ATOM   1727 C CA  . HIS B 1 60  ? -1.159  33.433  -8.919  1.000 81.785  0 60  HIS B CA  1 
ATOM   1728 C C   . HIS B 1 60  ? -2.165  33.098  -7.822  1.000 77.760  0 60  HIS B C   1 
ATOM   1729 O O   . HIS B 1 60  ? -2.011  33.606  -6.726  1.000 81.095  0 60  HIS B O   1 
ATOM   1730 C CB  . HIS B 1 60  ? -1.069  34.936  -9.185  1.000 78.940  0 60  HIS B CB  1 
ATOM   1731 C CG  . HIS B 1 60  ? 0.145   35.430  -9.922  1.000 82.265  0 60  HIS B CG  1 
ATOM   1732 N ND1 . HIS B 1 60  ? 1.273   35.924  -9.285  1.000 91.368  0 60  HIS B ND1 1 
ATOM   1733 C CD2 . HIS B 1 60  ? 0.357   35.606  -11.251 1.000 74.756  0 60  HIS B CD2 1 
ATOM   1734 C CE1 . HIS B 1 60  ? 2.158   36.334  -10.208 1.000 92.497  0 60  HIS B CE1 1 
ATOM   1735 N NE2 . HIS B 1 60  ? 1.622   36.154  -11.416 1.000 73.854  0 60  HIS B NE2 1 
ATOM   1736 N N   . ASP B 1 61  ? -3.093  32.169  -8.111  1.000 78.890  0 61  ASP B N   1 
ATOM   1737 C CA  . ASP B 1 61  ? -4.136  31.701  -7.205  1.000 77.341  0 61  ASP B CA  1 
ATOM   1738 C C   . ASP B 1 61  ? -3.569  30.546  -6.370  1.000 89.182  0 61  ASP B C   1 
ATOM   1739 O O   . ASP B 1 61  ? -3.176  29.513  -6.907  1.000 84.793  0 61  ASP B O   1 
ATOM   1740 C CB  . ASP B 1 61  ? -5.380  31.342  -8.012  1.000 72.844  0 61  ASP B CB  1 
ATOM   1741 C CG  . ASP B 1 61  ? -6.541  30.707  -7.270  1.000 76.787  0 61  ASP B CG  1 
ATOM   1742 O OD1 . ASP B 1 61  ? -6.395  30.440  -6.077  1.000 90.166  0 61  ASP B OD1 1 
ATOM   1743 O OD2 . ASP B 1 61  ? -7.573  30.458  -7.909  1.000 88.325  0 61  ASP B OD2 1 
ATOM   1744 N N   . LYS B 1 62  ? -3.552  30.722  -5.039  1.000 85.980  0 62  LYS B N   1 
ATOM   1745 C CA  . LYS B 1 62  ? -2.926  29.781  -4.121  1.000 77.918  0 62  LYS B CA  1 
ATOM   1746 C C   . LYS B 1 62  ? -3.817  28.573  -3.846  1.000 82.758  0 62  LYS B C   1 
ATOM   1747 O O   . LYS B 1 62  ? -3.321  27.507  -3.455  1.000 77.569  0 62  LYS B O   1 
ATOM   1748 C CB  . LYS B 1 62  ? -2.621  30.451  -2.785  1.000 67.496  0 62  LYS B CB  1 
ATOM   1749 C CG  . LYS B 1 62  ? -1.600  31.577  -2.838  1.000 70.486  0 62  LYS B CG  1 
ATOM   1750 C CD  . LYS B 1 62  ? -1.643  32.359  -1.521  1.000 76.594  0 62  LYS B CD  1 
ATOM   1751 C CE  . LYS B 1 62  ? -0.629  33.457  -1.319  1.000 74.966  0 62  LYS B CE  1 
ATOM   1752 N NZ  . LYS B 1 62  ? -0.446  34.443  -2.394  1.000 74.908  0 62  LYS B NZ  1 
ATOM   1753 N N   . VAL B 1 63  ? -5.131  28.764  -4.006  1.000 75.272  0 63  VAL B N   1 
ATOM   1754 C CA  . VAL B 1 63  ? -6.067  27.670  -3.831  1.000 79.575  0 63  VAL B CA  1 
ATOM   1755 C C   . VAL B 1 63  ? -5.937  26.718  -5.019  1.000 79.411  0 63  VAL B C   1 
ATOM   1756 O O   . VAL B 1 63  ? -5.885  25.510  -4.838  1.000 94.692  0 63  VAL B O   1 
ATOM   1757 C CB  . VAL B 1 63  ? -7.496  28.219  -3.642  1.000 73.949  0 63  VAL B CB  1 
ATOM   1758 C CG1 . VAL B 1 63  ? -8.531  27.102  -3.579  1.000 68.659  0 63  VAL B CG1 1 
ATOM   1759 C CG2 . VAL B 1 63  ? -7.593  29.082  -2.390  1.000 72.777  0 63  VAL B CG2 1 
ATOM   1760 N N   . TRP B 1 64  ? -5.844  27.274  -6.228  1.000 74.033  0 64  TRP B N   1 
ATOM   1761 C CA  . TRP B 1 64  ? -5.636  26.475  -7.428  1.000 80.227  0 64  TRP B CA  1 
ATOM   1762 C C   . TRP B 1 64  ? -4.389  25.604  -7.286  1.000 73.982  0 64  TRP B C   1 
ATOM   1763 O O   . TRP B 1 64  ? -4.437  24.405  -7.561  1.000 79.872  0 64  TRP B O   1 
ATOM   1764 C CB  . TRP B 1 64  ? -5.539  27.338  -8.705  1.000 74.137  0 64  TRP B CB  1 
ATOM   1765 C CG  . TRP B 1 64  ? -5.348  26.463  -9.913  1.000 74.283  0 64  TRP B CG  1 
ATOM   1766 C CD1 . TRP B 1 64  ? -6.296  25.738  -10.587 1.000 85.196  0 64  TRP B CD1 1 
ATOM   1767 C CD2 . TRP B 1 64  ? -4.082  26.073  -10.469 1.000 71.878  0 64  TRP B CD2 1 
ATOM   1768 N NE1 . TRP B 1 64  ? -5.718  25.003  -11.590 1.000 83.810  0 64  TRP B NE1 1 
ATOM   1769 C CE2 . TRP B 1 64  ? -4.359  25.169  -11.519 1.000 74.223  0 64  TRP B CE2 1 
ATOM   1770 C CE3 . TRP B 1 64  ? -2.756  26.394  -10.174 1.000 78.220  0 64  TRP B CE3 1 
ATOM   1771 C CZ2 . TRP B 1 64  ? -3.348  24.582  -12.269 1.000 74.225  0 64  TRP B CZ2 1 
ATOM   1772 C CZ3 . TRP B 1 64  ? -1.755  25.813  -10.924 1.000 76.781  0 64  TRP B CZ3 1 
ATOM   1773 C CH2 . TRP B 1 64  ? -2.051  24.887  -11.928 1.000 73.308  0 64  TRP B CH2 1 
ATOM   1774 N N   . ALA B 1 65  ? -3.278  26.231  -6.880  1.000 63.369  0 65  ALA B N   1 
ATOM   1775 C CA  . ALA B 1 65  ? -1.998  25.559  -6.708  1.000 66.841  0 65  ALA B CA  1 
ATOM   1776 C C   . ALA B 1 65  ? -2.041  24.459  -5.640  1.000 79.016  0 65  ALA B C   1 
ATOM   1777 O O   . ALA B 1 65  ? -1.503  23.372  -5.864  1.000 80.143  0 65  ALA B O   1 
ATOM   1778 C CB  . ALA B 1 65  ? -0.976  26.594  -6.331  1.000 61.150  0 65  ALA B CB  1 
ATOM   1779 N N   . THR B 1 66  ? -2.642  24.767  -4.475  1.000 79.173  0 66  THR B N   1 
ATOM   1780 C CA  . THR B 1 66  ? -2.790  23.833  -3.367  1.000 73.643  0 66  THR B CA  1 
ATOM   1781 C C   . THR B 1 66  ? -3.524  22.577  -3.833  1.000 78.673  0 66  THR B C   1 
ATOM   1782 O O   . THR B 1 66  ? -3.012  21.475  -3.637  1.000 81.889  0 66  THR B O   1 
ATOM   1783 C CB  . THR B 1 66  ? -3.504  24.524  -2.204  1.000 72.387  0 66  THR B CB  1 
ATOM   1784 O OG1 . THR B 1 66  ? -2.580  25.470  -1.676  1.000 68.263  0 66  THR B OG1 1 
ATOM   1785 C CG2 . THR B 1 66  ? -3.855  23.593  -1.060  1.000 70.500  0 66  THR B CG2 1 
ATOM   1786 N N   . ALA B 1 67  ? -4.695  22.742  -4.463  1.000 66.488  0 67  ALA B N   1 
ATOM   1787 C CA  . ALA B 1 67  ? -5.468  21.608  -4.967  1.000 74.957  0 67  ALA B CA  1 
ATOM   1788 C C   . ALA B 1 67  ? -4.721  20.790  -6.033  1.000 76.534  0 67  ALA B C   1 
ATOM   1789 O O   . ALA B 1 67  ? -4.778  19.551  -6.035  1.000 64.480  0 67  ALA B O   1 
ATOM   1790 C CB  . ALA B 1 67  ? -6.787  22.095  -5.510  1.000 68.919  0 67  ALA B CB  1 
ATOM   1791 N N   . THR B 1 68  ? -4.043  21.472  -6.962  1.000 65.816  0 68  THR B N   1 
ATOM   1792 C CA  . THR B 1 68  ? -3.375  20.753  -8.029  1.000 73.799  0 68  THR B CA  1 
ATOM   1793 C C   . THR B 1 68  ? -2.241  19.942  -7.410  1.000 69.702  0 68  THR B C   1 
ATOM   1794 O O   . THR B 1 68  ? -2.083  18.743  -7.656  1.000 69.026  0 68  THR B O   1 
ATOM   1795 C CB  . THR B 1 68  ? -2.860  21.673  -9.139  1.000 73.869  0 68  THR B CB  1 
ATOM   1796 O OG1 . THR B 1 68  ? -3.892  22.491  -9.665  1.000 78.317  0 68  THR B OG1 1 
ATOM   1797 C CG2 . THR B 1 68  ? -2.407  20.881  -10.349 1.000 65.139  0 68  THR B CG2 1 
ATOM   1798 N N   . TYR B 1 69  ? -1.452  20.629  -6.593  1.000 68.066  0 69  TYR B N   1 
ATOM   1799 C CA  . TYR B 1 69  ? -0.332  19.988  -5.930  1.000 65.278  0 69  TYR B CA  1 
ATOM   1800 C C   . TYR B 1 69  ? -0.858  18.819  -5.110  1.000 62.770  0 69  TYR B C   1 
ATOM   1801 O O   . TYR B 1 69  ? -0.317  17.741  -5.201  1.000 67.933  0 69  TYR B O   1 
ATOM   1802 C CB  . TYR B 1 69  ? 0.395   21.031  -5.073  1.000 75.016  0 69  TYR B CB  1 
ATOM   1803 C CG  . TYR B 1 69  ? 1.456   20.446  -4.165  1.000 67.842  0 69  TYR B CG  1 
ATOM   1804 C CD1 . TYR B 1 69  ? 2.674   20.038  -4.683  1.000 77.250  0 69  TYR B CD1 1 
ATOM   1805 C CD2 . TYR B 1 69  ? 1.240   20.286  -2.804  1.000 66.342  0 69  TYR B CD2 1 
ATOM   1806 C CE1 . TYR B 1 69  ? 3.655   19.489  -3.874  1.000 80.035  0 69  TYR B CE1 1 
ATOM   1807 C CE2 . TYR B 1 69  ? 2.209   19.738  -1.977  1.000 70.550  0 69  TYR B CE2 1 
ATOM   1808 C CZ  . TYR B 1 69  ? 3.411   19.327  -2.524  1.000 74.942  0 69  TYR B CZ  1 
ATOM   1809 O OH  . TYR B 1 69  ? 4.407   18.806  -1.787  1.000 69.565  0 69  TYR B OH  1 
ATOM   1810 N N   . ASN B 1 70  ? -1.923  19.032  -4.336  1.000 61.784  0 70  ASN B N   1 
ATOM   1811 C CA  . ASN B 1 70  ? -2.486  17.967  -3.530  1.000 66.406  0 70  ASN B CA  1 
ATOM   1812 C C   . ASN B 1 70  ? -2.993  16.797  -4.364  1.000 71.310  0 70  ASN B C   1 
ATOM   1813 O O   . ASN B 1 70  ? -2.803  15.639  -3.980  1.000 72.326  0 70  ASN B O   1 
ATOM   1814 C CB  . ASN B 1 70  ? -3.640  18.462  -2.675  1.000 70.205  0 70  ASN B CB  1 
ATOM   1815 C CG  . ASN B 1 70  ? -3.139  19.213  -1.471  1.000 61.987  0 70  ASN B CG  1 
ATOM   1816 O OD1 . ASN B 1 70  ? -1.941  19.363  -1.268  1.000 68.589  0 70  ASN B OD1 1 
ATOM   1817 N ND2 . ASN B 1 70  ? -4.038  19.708  -0.653  1.000 87.004  0 70  ASN B ND2 1 
ATOM   1818 N N   . ASN B 1 71  ? -3.629  17.089  -5.498  1.000 72.914  0 71  ASN B N   1 
ATOM   1819 C CA  . ASN B 1 71  ? -4.229  16.031  -6.296  1.000 86.827  0 71  ASN B CA  1 
ATOM   1820 C C   . ASN B 1 71  ? -3.152  15.114  -6.894  1.000 80.000  0 71  ASN B C   1 
ATOM   1821 O O   . ASN B 1 71  ? -3.344  13.890  -6.997  1.000 82.125  0 71  ASN B O   1 
ATOM   1822 C CB  . ASN B 1 71  ? -5.167  16.628  -7.338  1.000 84.371  0 71  ASN B CB  1 
ATOM   1823 C CG  . ASN B 1 71  ? -6.357  15.753  -7.643  1.000 86.778  0 71  ASN B CG  1 
ATOM   1824 O OD1 . ASN B 1 71  ? -7.204  16.220  -8.397  1.000 98.142  0 71  ASN B OD1 1 
ATOM   1825 N ND2 . ASN B 1 71  ? -6.490  14.546  -7.091  1.000 93.732  0 71  ASN B ND2 1 
ATOM   1826 N N   . ASP B 1 72  ? -2.017  15.726  -7.270  1.000 69.981  0 72  ASP B N   1 
ATOM   1827 C CA  . ASP B 1 72  ? -0.917  15.014  -7.892  1.000 78.910  0 72  ASP B CA  1 
ATOM   1828 C C   . ASP B 1 72  ? -0.261  14.096  -6.855  1.000 74.777  0 72  ASP B C   1 
ATOM   1829 O O   . ASP B 1 72  ? -0.007  12.916  -7.117  1.000 87.132  0 72  ASP B O   1 
ATOM   1830 C CB  . ASP B 1 72  ? 0.002   15.971  -8.653  1.000 87.688  0 72  ASP B CB  1 
ATOM   1831 C CG  . ASP B 1 72  ? -0.504  16.508  -9.997  1.000 94.224  0 72  ASP B CG  1 
ATOM   1832 O OD1 . ASP B 1 72  ? -1.660  16.217  -10.411 1.000 80.259  0 72  ASP B OD1 1 
ATOM   1833 O OD2 . ASP B 1 72  ? 0.282   17.215  -10.646 1.000 95.050  0 72  ASP B OD2 1 
ATOM   1834 N N   . LEU B 1 73  ? -0.013  14.610  -5.650  1.000 74.038  0 73  LEU B N   1 
ATOM   1835 C CA  . LEU B 1 73  ? 0.471   13.767  -4.571  1.000 70.059  0 73  LEU B CA  1 
ATOM   1836 C C   . LEU B 1 73  ? -0.527  12.651  -4.294  1.000 76.495  0 73  LEU B C   1 
ATOM   1837 O O   . LEU B 1 73  ? -0.144  11.493  -4.146  1.000 83.776  0 73  LEU B O   1 
ATOM   1838 C CB  . LEU B 1 73  ? 0.714   14.590  -3.316  1.000 79.422  0 73  LEU B CB  1 
ATOM   1839 C CG  . LEU B 1 73  ? 1.801   15.663  -3.427  1.000 78.862  0 73  LEU B CG  1 
ATOM   1840 C CD1 . LEU B 1 73  ? 2.189   16.060  -2.025  1.000 85.522  0 73  LEU B CD1 1 
ATOM   1841 C CD2 . LEU B 1 73  ? 3.014   15.224  -4.216  1.000 76.852  0 73  LEU B CD2 1 
ATOM   1842 N N   . ASN B 1 74  ? -1.812  12.995  -4.238  1.000 70.287  0 74  ASN B N   1 
ATOM   1843 C CA  . ASN B 1 74  ? -2.832  11.995  -3.981  1.000 78.169  0 74  ASN B CA  1 
ATOM   1844 C C   . ASN B 1 74  ? -2.818  10.906  -5.059  1.000 72.609  0 74  ASN B C   1 
ATOM   1845 O O   . ASN B 1 74  ? -3.040  9.725   -4.782  1.000 64.305  0 74  ASN B O   1 
ATOM   1846 C CB  . ASN B 1 74  ? -4.180  12.686  -3.880  1.000 80.754  0 74  ASN B CB  1 
ATOM   1847 C CG  . ASN B 1 74  ? -5.227  11.723  -3.415  1.000 71.887  0 74  ASN B CG  1 
ATOM   1848 O OD1 . ASN B 1 74  ? -6.204  11.498  -4.128  1.000 93.931  0 74  ASN B OD1 1 
ATOM   1849 N ND2 . ASN B 1 74  ? -5.013  11.133  -2.257  1.000 78.607  0 74  ASN B ND2 1 
ATOM   1850 N N   . GLY B 1 75  ? -2.560  11.326  -6.302  1.000 68.681  0 75  GLY B N   1 
ATOM   1851 C CA  . GLY B 1 75  ? -2.361  10.410  -7.415  1.000 70.937  0 75  GLY B CA  1 
ATOM   1852 C C   . GLY B 1 75  ? -1.250  9.395   -7.144  1.000 63.342  0 75  GLY B C   1 
ATOM   1853 O O   . GLY B 1 75  ? -1.403  8.214   -7.420  1.000 76.565  0 75  GLY B O   1 
ATOM   1854 N N   . ILE B 1 76  ? -0.128  9.844   -6.583  1.000 72.227  0 76  ILE B N   1 
ATOM   1855 C CA  . ILE B 1 76  ? 1.017   8.970   -6.326  1.000 69.984  0 76  ILE B CA  1 
ATOM   1856 C C   . ILE B 1 76  ? 0.725   7.977   -5.197  1.000 65.745  0 76  ILE B C   1 
ATOM   1857 O O   . ILE B 1 76  ? 0.999   6.780   -5.308  1.000 68.994  0 76  ILE B O   1 
ATOM   1858 C CB  . ILE B 1 76  ? 2.262   9.818   -6.036  1.000 69.377  0 76  ILE B CB  1 
ATOM   1859 C CG1 . ILE B 1 76  ? 2.560   10.725  -7.236  1.000 67.314  0 76  ILE B CG1 1 
ATOM   1860 C CG2 . ILE B 1 76  ? 3.465   8.945   -5.654  1.000 76.141  0 76  ILE B CG2 1 
ATOM   1861 C CD1 . ILE B 1 76  ? 3.699   11.687  -7.022  1.000 69.011  0 76  ILE B CD1 1 
ATOM   1862 N N   . LYS B 1 77  ? 0.107   8.475   -4.127  1.000 65.534  0 77  LYS B N   1 
ATOM   1863 C CA  . LYS B 1 77  ? -0.041  7.687   -2.918  1.000 77.417  0 77  LYS B CA  1 
ATOM   1864 C C   . LYS B 1 77  ? -1.135  6.635   -3.067  1.000 73.640  0 77  LYS B C   1 
ATOM   1865 O O   . LYS B 1 77  ? -1.062  5.615   -2.384  1.000 75.964  0 77  LYS B O   1 
ATOM   1866 C CB  . LYS B 1 77  ? -0.214  8.568   -1.669  1.000 73.674  0 77  LYS B CB  1 
ATOM   1867 C CG  . LYS B 1 77  ? -1.590  8.764   -1.147  1.000 71.026  0 77  LYS B CG  1 
ATOM   1868 C CD  . LYS B 1 77  ? -1.694  9.856   -0.104  1.000 71.791  0 77  LYS B CD  1 
ATOM   1869 C CE  . LYS B 1 77  ? -3.069  9.878   0.469   1.000 82.873  0 77  LYS B CE  1 
ATOM   1870 N NZ  . LYS B 1 77  ? -3.455  11.196  0.980   1.000 81.015  0 77  LYS B NZ  1 
ATOM   1871 N N   . THR B 1 78  ? -2.138  6.876   -3.924  1.000 76.966  0 78  THR B N   1 
ATOM   1872 C CA  . THR B 1 78  ? -3.250  5.943   -4.043  1.000 70.861  0 78  THR B CA  1 
ATOM   1873 C C   . THR B 1 78  ? -3.072  5.008   -5.234  1.000 71.922  0 78  THR B C   1 
ATOM   1874 O O   . THR B 1 78  ? -3.989  4.256   -5.507  1.000 67.629  0 78  THR B O   1 
ATOM   1875 C CB  . THR B 1 78  ? -4.574  6.687   -4.153  1.000 71.107  0 78  THR B CB  1 
ATOM   1876 O OG1 . THR B 1 78  ? -4.505  7.488   -5.331  1.000 76.019  0 78  THR B OG1 1 
ATOM   1877 C CG2 . THR B 1 78  ? -4.854  7.520   -2.924  1.000 69.851  0 78  THR B CG2 1 
ATOM   1878 N N   . ASN B 1 79  ? -1.915  5.029   -5.926  1.000 81.511  0 79  ASN B N   1 
ATOM   1879 C CA  . ASN B 1 79  ? -1.644  4.062   -6.988  1.000 78.571  0 79  ASN B CA  1 
ATOM   1880 C C   . ASN B 1 79  ? -0.442  3.199   -6.624  1.000 72.316  0 79  ASN B C   1 
ATOM   1881 O O   . ASN B 1 79  ? 0.271   3.511   -5.685  1.000 98.373  0 79  ASN B O   1 
ATOM   1882 C CB  . ASN B 1 79  ? -1.533  4.740   -8.347  1.000 78.336  0 79  ASN B CB  1 
ATOM   1883 C CG  . ASN B 1 79  ? -2.883  5.238   -8.801  1.000 77.382  0 79  ASN B CG  1 
ATOM   1884 O OD1 . ASN B 1 79  ? -3.740  4.453   -9.223  1.000 92.133  0 79  ASN B OD1 1 
ATOM   1885 N ND2 . ASN B 1 79  ? -3.103  6.533   -8.678  1.000 89.765  0 79  ASN B ND2 1 
ATOM   1886 N N   . ASP B 1 80  ? -0.222  2.121   -7.386  1.000 77.145  0 80  ASP B N   1 
ATOM   1887 C CA  . ASP B 1 80  ? 0.690   1.059   -6.992  1.000 74.339  0 80  ASP B CA  1 
ATOM   1888 C C   . ASP B 1 80  ? 2.130   1.401   -7.390  1.000 75.682  0 80  ASP B C   1 
ATOM   1889 O O   . ASP B 1 80  ? 3.067   1.103   -6.649  1.000 74.718  0 80  ASP B O   1 
ATOM   1890 C CB  . ASP B 1 80  ? 0.210   -0.284  -7.530  1.000 78.213  0 80  ASP B CB  1 
ATOM   1891 C CG  . ASP B 1 80  ? -1.201  -0.707  -7.124  1.000 97.283  0 80  ASP B CG  1 
ATOM   1892 O OD1 . ASP B 1 80  ? -1.483  -0.734  -5.902  1.000 95.333  0 80  ASP B OD1 1 
ATOM   1893 O OD2 . ASP B 1 80  ? -2.022  -1.002  -8.031  1.000 104.238 0 80  ASP B OD2 1 
ATOM   1894 N N   . ILE B 1 81  ? 2.324   1.978   -8.579  1.000 74.445  0 81  ILE B N   1 
ATOM   1895 C CA  . ILE B 1 81  ? 3.667   2.178   -9.101  1.000 74.891  0 81  ILE B CA  1 
ATOM   1896 C C   . ILE B 1 81  ? 3.851   3.649   -9.479  1.000 72.246  0 81  ILE B C   1 
ATOM   1897 O O   . ILE B 1 81  ? 2.945   4.300   -10.002 1.000 67.622  0 81  ILE B O   1 
ATOM   1898 C CB  . ILE B 1 81  ? 3.965   1.238   -10.302 1.000 79.828  0 81  ILE B CB  1 
ATOM   1899 C CG1 . ILE B 1 81  ? 4.517   -0.123  -9.899  1.000 73.229  0 81  ILE B CG1 1 
ATOM   1900 C CG2 . ILE B 1 81  ? 4.923   1.886   -11.303 1.000 75.527  0 81  ILE B CG2 1 
ATOM   1901 C CD1 . ILE B 1 81  ? 3.457   -1.175  -9.736  1.000 80.341  0 81  ILE B CD1 1 
ATOM   1902 N N   . MET B 1 82  ? 5.083   4.132   -9.274  1.000 73.895  0 82  MET B N   1 
ATOM   1903 C CA  . MET B 1 82  ? 5.521   5.446   -9.723  1.000 70.342  0 82  MET B CA  1 
ATOM   1904 C C   . MET B 1 82  ? 6.276   5.300   -11.027 1.000 75.371  0 82  MET B C   1 
ATOM   1905 O O   . MET B 1 82  ? 7.366   4.707   -11.030 1.000 73.313  0 82  MET B O   1 
ATOM   1906 C CB  . MET B 1 82  ? 6.520   6.102   -8.759  1.000 70.058  0 82  MET B CB  1 
ATOM   1907 C CG  . MET B 1 82  ? 6.955   7.484   -9.174  1.000 65.943  0 82  MET B CG  1 
ATOM   1908 S SD  . MET B 1 82  ? 5.574   8.643   -9.341  1.000 70.391  0 82  MET B SD  1 
ATOM   1909 C CE  . MET B 1 82  ? 6.428   9.876   -10.346 1.000 64.242  0 82  MET B CE  1 
ATOM   1910 N N   . LEU B 1 83  ? 5.689   5.877   -12.089 1.000 74.881  0 83  LEU B N   1 
ATOM   1911 C CA  . LEU B 1 83  ? 6.305   5.859   -13.398 1.000 72.943  0 83  LEU B CA  1 
ATOM   1912 C C   . LEU B 1 83  ? 6.871   7.238   -13.671 1.000 69.034  0 83  LEU B C   1 
ATOM   1913 O O   . LEU B 1 83  ? 6.141   8.214   -13.590 1.000 70.756  0 83  LEU B O   1 
ATOM   1914 C CB  . LEU B 1 83  ? 5.311   5.479   -14.489 1.000 84.159  0 83  LEU B CB  1 
ATOM   1915 C CG  . LEU B 1 83  ? 5.942   5.193   -15.862 1.000 89.055  0 83  LEU B CG  1 
ATOM   1916 C CD1 . LEU B 1 83  ? 6.611   3.833   -15.843 1.000 85.810  0 83  LEU B CD1 1 
ATOM   1917 C CD2 . LEU B 1 83  ? 4.955   5.281   -17.005 1.000 85.606  0 83  LEU B CD2 1 
ATOM   1918 N N   . GLY B 1 84  ? 8.146   7.289   -14.062 1.000 67.772  0 84  GLY B N   1 
ATOM   1919 C CA  . GLY B 1 84  ? 8.758   8.549   -14.426 1.000 64.244  0 84  GLY B CA  1 
ATOM   1920 C C   . GLY B 1 84  ? 9.369   8.493   -15.820 1.000 73.541  0 84  GLY B C   1 
ATOM   1921 O O   . GLY B 1 84  ? 10.445  7.936   -16.015 1.000 75.634  0 84  GLY B O   1 
ATOM   1922 N N   . VAL B 1 85  ? 8.676   9.113   -16.780 1.000 83.246  0 85  VAL B N   1 
ATOM   1923 C CA  . VAL B 1 85  ? 9.225   9.347   -18.105 1.000 79.616  0 85  VAL B CA  1 
ATOM   1924 C C   . VAL B 1 85  ? 10.327  10.401  -17.979 1.000 76.968  0 85  VAL B C   1 
ATOM   1925 O O   . VAL B 1 85  ? 10.057  11.553  -17.672 1.000 88.462  0 85  VAL B O   1 
ATOM   1926 C CB  . VAL B 1 85  ? 8.102   9.790   -19.065 1.000 73.236  0 85  VAL B CB  1 
ATOM   1927 C CG1 . VAL B 1 85  ? 8.608   10.113  -20.460 1.000 76.552  0 85  VAL B CG1 1 
ATOM   1928 C CG2 . VAL B 1 85  ? 7.017   8.733   -19.162 1.000 82.474  0 85  VAL B CG2 1 
ATOM   1929 N N   . TYR B 1 86  ? 11.562  10.004  -18.276 1.000 75.110  0 86  TYR B N   1 
ATOM   1930 C CA  . TYR B 1 86  ? 12.745  10.759  -17.914 1.000 69.539  0 86  TYR B CA  1 
ATOM   1931 C C   . TYR B 1 86  ? 13.590  11.051  -19.152 1.000 68.897  0 86  TYR B C   1 
ATOM   1932 O O   . TYR B 1 86  ? 14.110  10.137  -19.778 1.000 80.242  0 86  TYR B O   1 
ATOM   1933 C CB  . TYR B 1 86  ? 13.491  9.933   -16.857 1.000 72.384  0 86  TYR B CB  1 
ATOM   1934 C CG  . TYR B 1 86  ? 14.548  10.724  -16.086 1.000 79.688  0 86  TYR B CG  1 
ATOM   1935 C CD1 . TYR B 1 86  ? 15.765  11.081  -16.667 1.000 77.347  0 86  TYR B CD1 1 
ATOM   1936 C CD2 . TYR B 1 86  ? 14.315  11.153  -14.785 1.000 71.269  0 86  TYR B CD2 1 
ATOM   1937 C CE1 . TYR B 1 86  ? 16.708  11.830  -15.982 1.000 71.674  0 86  TYR B CE1 1 
ATOM   1938 C CE2 . TYR B 1 86  ? 15.258  11.889  -14.089 1.000 68.960  0 86  TYR B CE2 1 
ATOM   1939 C CZ  . TYR B 1 86  ? 16.456  12.239  -14.686 1.000 71.403  0 86  TYR B CZ  1 
ATOM   1940 O OH  . TYR B 1 86  ? 17.407  12.921  -13.980 1.000 75.450  0 86  TYR B OH  1 
ATOM   1941 N N   . ILE B 1 87  ? 13.727  12.338  -19.484 1.000 75.190  0 87  ILE B N   1 
ATOM   1942 C CA  . ILE B 1 87  ? 14.580  12.804  -20.562 1.000 78.670  0 87  ILE B CA  1 
ATOM   1943 C C   . ILE B 1 87  ? 15.877  13.348  -19.968 1.000 76.943  0 87  ILE B C   1 
ATOM   1944 O O   . ILE B 1 87  ? 15.863  14.348  -19.254 1.000 95.331  0 87  ILE B O   1 
ATOM   1945 C CB  . ILE B 1 87  ? 13.859  13.872  -21.403 1.000 90.247  0 87  ILE B CB  1 
ATOM   1946 C CG1 . ILE B 1 87  ? 12.714  13.247  -22.223 1.000 88.927  0 87  ILE B CG1 1 
ATOM   1947 C CG2 . ILE B 1 87  ? 14.856  14.646  -22.277 1.000 96.171  0 87  ILE B CG2 1 
ATOM   1948 C CD1 . ILE B 1 87  ? 11.389  13.215  -21.494 1.000 97.836  0 87  ILE B CD1 1 
ATOM   1949 N N   . PRO B 1 88  ? 17.040  12.710  -20.229 1.000 80.697  0 88  PRO B N   1 
ATOM   1950 C CA  . PRO B 1 88  ? 18.324  13.155  -19.664 1.000 83.517  0 88  PRO B CA  1 
ATOM   1951 C C   . PRO B 1 88  ? 18.840  14.564  -19.972 1.000 82.313  0 88  PRO B C   1 
ATOM   1952 O O   . PRO B 1 88  ? 19.649  15.124  -19.224 1.000 84.091  0 88  PRO B O   1 
ATOM   1953 C CB  . PRO B 1 88  ? 19.291  12.066  -20.218 1.000 82.098  0 88  PRO B CB  1 
ATOM   1954 C CG  . PRO B 1 88  ? 18.412  10.848  -20.384 1.000 74.958  0 88  PRO B CG  1 
ATOM   1955 C CD  . PRO B 1 88  ? 17.158  11.454  -20.986 1.000 82.968  0 88  PRO B CD  1 
ATOM   1956 N N   . ASP B 1 89  ? 18.398  15.137  -21.094 1.000 82.570  0 89  ASP B N   1 
ATOM   1957 C CA  . ASP B 1 89  ? 18.857  16.466  -21.473 1.000 100.601 0 89  ASP B CA  1 
ATOM   1958 C C   . ASP B 1 89  ? 17.838  17.507  -21.036 1.000 89.167  0 89  ASP B C   1 
ATOM   1959 O O   . ASP B 1 89  ? 18.073  18.679  -21.233 1.000 95.736  0 89  ASP B O   1 
ATOM   1960 C CB  . ASP B 1 89  ? 19.089  16.619  -22.971 1.000 104.233 0 89  ASP B CB  1 
ATOM   1961 C CG  . ASP B 1 89  ? 19.570  15.360  -23.680 1.000 118.214 0 89  ASP B CG  1 
ATOM   1962 O OD1 . ASP B 1 89  ? 18.676  14.475  -23.987 1.000 104.496 0 89  ASP B OD1 1 
ATOM   1963 O OD2 . ASP B 1 89  ? 20.831  15.247  -23.848 1.000 86.430  0 89  ASP B OD2 1 
ATOM   1964 N N   . GLU B 1 90  ? 16.699  17.071  -20.495 1.000 86.367  0 90  GLU B N   1 
ATOM   1965 C CA  . GLU B 1 90  ? 15.611  17.954  -20.105 1.000 95.221  0 90  GLU B CA  1 
ATOM   1966 C C   . GLU B 1 90  ? 15.037  17.435  -18.783 1.000 88.401  0 90  GLU B C   1 
ATOM   1967 O O   . GLU B 1 90  ? 13.886  16.985  -18.710 1.000 85.624  0 90  GLU B O   1 
ATOM   1968 C CB  . GLU B 1 90  ? 14.538  18.060  -21.200 1.000 109.761 0 90  GLU B CB  1 
ATOM   1969 C CG  . GLU B 1 90  ? 15.019  18.605  -22.548 1.000 102.989 0 90  GLU B CG  1 
ATOM   1970 C CD  . GLU B 1 90  ? 13.922  18.810  -23.593 1.000 100.612 0 90  GLU B CD  1 
ATOM   1971 O OE1 . GLU B 1 90  ? 14.255  19.367  -24.662 1.000 100.076 0 90  GLU B OE1 1 
ATOM   1972 O OE2 . GLU B 1 90  ? 12.757  18.384  -23.381 1.000 97.017  0 90  GLU B OE2 1 
ATOM   1973 N N   . GLU B 1 91  ? 15.879  17.469  -17.748 1.000 85.284  0 91  GLU B N   1 
ATOM   1974 C CA  . GLU B 1 91  ? 15.543  16.871  -16.464 1.000 95.695  0 91  GLU B CA  1 
ATOM   1975 C C   . GLU B 1 91  ? 14.628  17.838  -15.716 1.000 83.340  0 91  GLU B C   1 
ATOM   1976 O O   . GLU B 1 91  ? 14.823  19.037  -15.844 1.000 77.263  0 91  GLU B O   1 
ATOM   1977 C CB  . GLU B 1 91  ? 16.839  16.555  -15.714 1.000 86.241  0 91  GLU B CB  1 
ATOM   1978 C CG  . GLU B 1 91  ? 17.629  15.390  -16.315 1.000 78.854  0 91  GLU B CG  1 
ATOM   1979 C CD  . GLU B 1 91  ? 18.983  15.134  -15.649 1.000 81.494  0 91  GLU B CD  1 
ATOM   1980 O OE1 . GLU B 1 91  ? 19.836  16.026  -15.839 1.000 81.193  0 91  GLU B OE1 1 
ATOM   1981 O OE2 . GLU B 1 91  ? 19.228  14.093  -14.984 1.000 77.101  0 91  GLU B OE2 1 
ATOM   1982 N N   . ASP B 1 92  ? 13.622  17.310  -14.991 1.000 83.872  0 92  ASP B N   1 
ATOM   1983 C CA  . ASP B 1 92  ? 12.497  18.093  -14.478 1.000 86.050  0 92  ASP B CA  1 
ATOM   1984 C C   . ASP B 1 92  ? 12.556  18.145  -12.952 1.000 76.695  0 92  ASP B C   1 
ATOM   1985 O O   . ASP B 1 92  ? 12.462  17.115  -12.283 1.000 78.585  0 92  ASP B O   1 
ATOM   1986 C CB  . ASP B 1 92  ? 11.165  17.539  -14.980 1.000 82.135  0 92  ASP B CB  1 
ATOM   1987 C CG  . ASP B 1 92  ? 9.893   18.299  -14.618 1.000 98.496  0 92  ASP B CG  1 
ATOM   1988 O OD1 . ASP B 1 92  ? 10.000  19.468  -14.179 1.000 101.016 0 92  ASP B OD1 1 
ATOM   1989 O OD2 . ASP B 1 92  ? 8.793   17.711  -14.808 1.000 95.533  0 92  ASP B OD2 1 
ATOM   1990 N N   . VAL B 1 93  ? 12.651  19.353  -12.389 1.000 69.429  0 93  VAL B N   1 
ATOM   1991 C CA  . VAL B 1 93  ? 12.645  19.495  -10.936 1.000 68.257  0 93  VAL B CA  1 
ATOM   1992 C C   . VAL B 1 93  ? 11.322  18.987  -10.337 1.000 70.182  0 93  VAL B C   1 
ATOM   1993 O O   . VAL B 1 93  ? 11.314  18.468  -9.228  1.000 66.247  0 93  VAL B O   1 
ATOM   1994 C CB  . VAL B 1 93  ? 12.908  20.943  -10.512 1.000 60.830  0 93  VAL B CB  1 
ATOM   1995 C CG1 . VAL B 1 93  ? 11.748  21.851  -10.895 1.000 70.179  0 93  VAL B CG1 1 
ATOM   1996 C CG2 . VAL B 1 93  ? 13.175  21.065  -9.032  1.000 65.233  0 93  VAL B CG2 1 
ATOM   1997 N N   . GLY B 1 94  ? 10.203  19.133  -11.061 1.000 75.556  0 94  GLY B N   1 
ATOM   1998 C CA  . GLY B 1 94  ? 8.918   18.660  -10.577 1.000 70.734  0 94  GLY B CA  1 
ATOM   1999 C C   . GLY B 1 94  ? 8.909   17.138  -10.461 1.000 72.483  0 94  GLY B C   1 
ATOM   2000 O O   . GLY B 1 94  ? 8.449   16.601  -9.462  1.000 63.168  0 94  GLY B O   1 
ATOM   2001 N N   . LEU B 1 95  ? 9.455   16.457  -11.474 1.000 68.770  0 95  LEU B N   1 
ATOM   2002 C CA  . LEU B 1 95  ? 9.478   15.007  -11.486 1.000 72.950  0 95  LEU B CA  1 
ATOM   2003 C C   . LEU B 1 95  ? 10.410  14.527  -10.382 1.000 71.719  0 95  LEU B C   1 
ATOM   2004 O O   . LEU B 1 95  ? 10.136  13.535  -9.701  1.000 64.012  0 95  LEU B O   1 
ATOM   2005 C CB  . LEU B 1 95  ? 9.917   14.465  -12.840 1.000 63.130  0 95  LEU B CB  1 
ATOM   2006 C CG  . LEU B 1 95  ? 9.933   12.942  -12.952 1.000 73.280  0 95  LEU B CG  1 
ATOM   2007 C CD1 . LEU B 1 95  ? 8.523   12.364  -12.687 1.000 77.358  0 95  LEU B CD1 1 
ATOM   2008 C CD2 . LEU B 1 95  ? 10.483  12.529  -14.322 1.000 66.247  0 95  LEU B CD2 1 
ATOM   2009 N N   . GLY B 1 96  ? 11.515  15.259  -10.220 1.000 70.815  0 96  GLY B N   1 
ATOM   2010 C CA  . GLY B 1 96  ? 12.447  14.973  -9.142  1.000 75.189  0 96  GLY B CA  1 
ATOM   2011 C C   . GLY B 1 96  ? 11.717  14.845  -7.806  1.000 73.768  0 96  GLY B C   1 
ATOM   2012 O O   . GLY B 1 96  ? 11.927  13.876  -7.092  1.000 66.928  0 96  GLY B O   1 
ATOM   2013 N N   . MET B 1 97  ? 10.844  15.819  -7.510  1.000 64.227  0 97  MET B N   1 
ATOM   2014 C CA  . MET B 1 97  ? 10.144  15.892  -6.244  1.000 61.387  0 97  MET B CA  1 
ATOM   2015 C C   . MET B 1 97  ? 9.179   14.724  -6.076  1.000 62.289  0 97  MET B C   1 
ATOM   2016 O O   . MET B 1 97  ? 9.126   14.094  -5.015  1.000 62.833  0 97  MET B O   1 
ATOM   2017 C CB  . MET B 1 97  ? 9.368   17.205  -6.146  1.000 61.696  0 97  MET B CB  1 
ATOM   2018 C CG  . MET B 1 97  ? 8.661   17.387  -4.827  1.000 59.160  0 97  MET B CG  1 
ATOM   2019 S SD  . MET B 1 97  ? 6.975   16.792  -4.895  1.000 71.023  0 97  MET B SD  1 
ATOM   2020 C CE  . MET B 1 97  ? 6.573   16.351  -3.200  1.000 81.762  0 97  MET B CE  1 
ATOM   2021 N N   . GLU B 1 98  ? 8.413   14.458  -7.136  1.000 68.622  0 98  GLU B N   1 
ATOM   2022 C CA  . GLU B 1 98  ? 7.489   13.339  -7.187  1.000 65.126  0 98  GLU B CA  1 
ATOM   2023 C C   . GLU B 1 98  ? 8.210   12.023  -6.891  1.000 70.445  0 98  GLU B C   1 
ATOM   2024 O O   . GLU B 1 98  ? 7.636   11.145  -6.247  1.000 77.774  0 98  GLU B O   1 
ATOM   2025 C CB  . GLU B 1 98  ? 6.826   13.321  -8.568  1.000 78.058  0 98  GLU B CB  1 
ATOM   2026 C CG  . GLU B 1 98  ? 5.751   14.398  -8.721  1.000 86.687  0 98  GLU B CG  1 
ATOM   2027 C CD  . GLU B 1 98  ? 5.274   14.744  -10.109 1.000 77.992  0 98  GLU B CD  1 
ATOM   2028 O OE1 . GLU B 1 98  ? 4.358   15.583  -10.221 1.000 96.036  0 98  GLU B OE1 1 
ATOM   2029 O OE2 . GLU B 1 98  ? 5.845   14.216  -11.067 1.000 85.077  0 98  GLU B OE2 1 
ATOM   2030 N N   . LEU B 1 99  ? 9.454   11.869  -7.372  1.000 67.540  0 99  LEU B N   1 
ATOM   2031 C CA  . LEU B 1 99  ? 10.165  10.610  -7.172  1.000 74.142  0 99  LEU B CA  1 
ATOM   2032 C C   . LEU B 1 99  ? 10.492  10.457  -5.690  1.000 71.683  0 99  LEU B C   1 
ATOM   2033 O O   . LEU B 1 99  ? 10.399  9.367   -5.138  1.000 71.508  0 99  LEU B O   1 
ATOM   2034 C CB  . LEU B 1 99  ? 11.429  10.474  -8.027  1.000 74.265  0 99  LEU B CB  1 
ATOM   2035 C CG  . LEU B 1 99  ? 11.242  10.547  -9.547  1.000 74.054  0 99  LEU B CG  1 
ATOM   2036 C CD1 . LEU B 1 99  ? 12.596  10.689  -10.220 1.000 72.772  0 99  LEU B CD1 1 
ATOM   2037 C CD2 . LEU B 1 99  ? 10.488  9.349   -10.116 1.000 74.840  0 99  LEU B CD2 1 
ATOM   2038 N N   . GLY B 1 100 ? 10.863  11.566  -5.048  1.000 69.581  0 100 GLY B N   1 
ATOM   2039 C CA  . GLY B 1 100 ? 11.113  11.555  -3.622  1.000 69.943  0 100 GLY B CA  1 
ATOM   2040 C C   . GLY B 1 100 ? 9.850   11.195  -2.851  1.000 66.910  0 100 GLY B C   1 
ATOM   2041 O O   . GLY B 1 100 ? 9.864   10.380  -1.939  1.000 78.076  0 100 GLY B O   1 
ATOM   2042 N N   . TYR B 1 101 ? 8.739   11.792  -3.246  1.000 69.185  0 101 TYR B N   1 
ATOM   2043 C CA  . TYR B 1 101 ? 7.486   11.519  -2.564  1.000 73.548  0 101 TYR B CA  1 
ATOM   2044 C C   . TYR B 1 101 ? 7.103   10.043  -2.719  1.000 68.311  0 101 TYR B C   1 
ATOM   2045 O O   . TYR B 1 101 ? 6.756   9.391   -1.740  1.000 70.344  0 101 TYR B O   1 
ATOM   2046 C CB  . TYR B 1 101 ? 6.446   12.527  -3.062  1.000 63.888  0 101 TYR B CB  1 
ATOM   2047 C CG  . TYR B 1 101 ? 5.130   12.352  -2.340  1.000 65.062  0 101 TYR B CG  1 
ATOM   2048 C CD1 . TYR B 1 101 ? 4.931   12.897  -1.084  1.000 68.585  0 101 TYR B CD1 1 
ATOM   2049 C CD2 . TYR B 1 101 ? 4.106   11.606  -2.904  1.000 69.089  0 101 TYR B CD2 1 
ATOM   2050 C CE1 . TYR B 1 101 ? 3.726   12.738  -0.423  1.000 72.470  0 101 TYR B CE1 1 
ATOM   2051 C CE2 . TYR B 1 101 ? 2.908   11.423  -2.241  1.000 66.338  0 101 TYR B CE2 1 
ATOM   2052 C CZ  . TYR B 1 101 ? 2.717   11.991  -1.000  1.000 66.474  0 101 TYR B CZ  1 
ATOM   2053 O OH  . TYR B 1 101 ? 1.542   11.795  -0.355  1.000 74.821  0 101 TYR B OH  1 
ATOM   2054 N N   . ALA B 1 102 ? 7.198   9.510   -3.942  1.000 68.877  0 102 ALA B N   1 
ATOM   2055 C CA  . ALA B 1 102 ? 6.930   8.103   -4.201  1.000 72.738  0 102 ALA B CA  1 
ATOM   2056 C C   . ALA B 1 102 ? 7.755   7.172   -3.302  1.000 70.442  0 102 ALA B C   1 
ATOM   2057 O O   . ALA B 1 102 ? 7.227   6.202   -2.743  1.000 65.757  0 102 ALA B O   1 
ATOM   2058 C CB  . ALA B 1 102 ? 7.195   7.818   -5.641  1.000 84.888  0 102 ALA B CB  1 
ATOM   2059 N N   . LEU B 1 103 ? 9.054   7.452   -3.170  1.000 65.573  0 103 LEU B N   1 
ATOM   2060 C CA  . LEU B 1 103 ? 9.902   6.717   -2.245  1.000 64.537  0 103 LEU B CA  1 
ATOM   2061 C C   . LEU B 1 103 ? 9.314   6.739   -0.827  1.000 64.418  0 103 LEU B C   1 
ATOM   2062 O O   . LEU B 1 103 ? 9.234   5.724   -0.129  1.000 63.029  0 103 LEU B O   1 
ATOM   2063 C CB  . LEU B 1 103 ? 11.306  7.323   -2.234  1.000 73.989  0 103 LEU B CB  1 
ATOM   2064 C CG  . LEU B 1 103 ? 12.306  6.607   -1.317  1.000 79.997  0 103 LEU B CG  1 
ATOM   2065 C CD1 . LEU B 1 103 ? 12.655  5.230   -1.900  1.000 75.020  0 103 LEU B CD1 1 
ATOM   2066 C CD2 . LEU B 1 103 ? 13.544  7.463   -1.061  1.000 77.080  0 103 LEU B CD2 1 
ATOM   2067 N N   . SER B 1 104 ? 8.937   7.927   -0.369  1.000 62.105  0 104 SER B N   1 
ATOM   2068 C CA  . SER B 1 104 ? 8.450   8.076   0.984   1.000 61.300  0 104 SER B CA  1 
ATOM   2069 C C   . SER B 1 104 ? 7.130   7.319   1.192   1.000 68.301  0 104 SER B C   1 
ATOM   2070 O O   . SER B 1 104 ? 6.828   6.954   2.323   1.000 70.021  0 104 SER B O   1 
ATOM   2071 C CB  . SER B 1 104 ? 8.340   9.541   1.318   1.000 64.589  0 104 SER B CB  1 
ATOM   2072 O OG  . SER B 1 104 ? 7.175   10.151  0.777   1.000 71.541  0 104 SER B OG  1 
ATOM   2073 N N   . GLN B 1 105 ? 6.340   7.085   0.123   1.000 71.466  0 105 GLN B N   1 
ATOM   2074 C CA  . GLN B 1 105 ? 5.086   6.347   0.225   1.000 65.268  0 105 GLN B CA  1 
ATOM   2075 C C   . GLN B 1 105 ? 5.262   4.873   -0.138  1.000 64.147  0 105 GLN B C   1 
ATOM   2076 O O   . GLN B 1 105 ? 4.273   4.153   -0.234  1.000 73.484  0 105 GLN B O   1 
ATOM   2077 C CB  . GLN B 1 105 ? 4.000   6.845   -0.725  1.000 69.497  0 105 GLN B CB  1 
ATOM   2078 C CG  . GLN B 1 105 ? 3.646   8.309   -0.546  1.000 78.264  0 105 GLN B CG  1 
ATOM   2079 C CD  . GLN B 1 105 ? 3.274   8.648   0.874   1.000 70.940  0 105 GLN B CD  1 
ATOM   2080 O OE1 . GLN B 1 105 ? 2.272   8.173   1.401   1.000 63.109  0 105 GLN B OE1 1 
ATOM   2081 N NE2 . GLN B 1 105 ? 4.095   9.469   1.503   1.000 88.728  0 105 GLN B NE2 1 
ATOM   2082 N N   . GLY B 1 106 ? 6.506   4.430   -0.357  1.000 66.172  0 106 GLY B N   1 
ATOM   2083 C CA  . GLY B 1 106 ? 6.815   3.009   -0.459  1.000 77.899  0 106 GLY B CA  1 
ATOM   2084 C C   . GLY B 1 106 ? 6.389   2.377   -1.790  1.000 73.665  0 106 GLY B C   1 
ATOM   2085 O O   . GLY B 1 106 ? 6.050   1.201   -1.857  1.000 78.422  0 106 GLY B O   1 
ATOM   2086 N N   . LYS B 1 107 ? 6.452   3.159   -2.865  1.000 72.011  0 107 LYS B N   1 
ATOM   2087 C CA  . LYS B 1 107 ? 6.101   2.699   -4.195  1.000 71.529  0 107 LYS B CA  1 
ATOM   2088 C C   . LYS B 1 107 ? 7.343   2.237   -4.946  1.000 74.197  0 107 LYS B C   1 
ATOM   2089 O O   . LYS B 1 107 ? 8.427   2.792   -4.749  1.000 67.089  0 107 LYS B O   1 
ATOM   2090 C CB  . LYS B 1 107 ? 5.525   3.888   -4.966  1.000 65.437  0 107 LYS B CB  1 
ATOM   2091 C CG  . LYS B 1 107 ? 4.391   4.586   -4.247  1.000 67.637  0 107 LYS B CG  1 
ATOM   2092 C CD  . LYS B 1 107 ? 3.176   3.702   -3.967  1.000 62.253  0 107 LYS B CD  1 
ATOM   2093 C CE  . LYS B 1 107 ? 2.132   4.528   -3.317  1.000 71.089  0 107 LYS B CE  1 
ATOM   2094 N NZ  . LYS B 1 107 ? 0.971   3.693   -3.078  1.000 76.191  0 107 LYS B NZ  1 
ATOM   2095 N N   . TYR B 1 108 ? 7.150   1.261   -5.847  1.000 78.453  0 108 TYR B N   1 
ATOM   2096 C CA  . TYR B 1 108 ? 8.174   0.962   -6.839  1.000 74.737  0 108 TYR B CA  1 
ATOM   2097 C C   . TYR B 1 108 ? 8.378   2.193   -7.717  1.000 69.118  0 108 TYR B C   1 
ATOM   2098 O O   . TYR B 1 108 ? 7.419   2.739   -8.252  1.000 69.592  0 108 TYR B O   1 
ATOM   2099 C CB  . TYR B 1 108 ? 7.766   -0.233  -7.692  1.000 72.865  0 108 TYR B CB  1 
ATOM   2100 C CG  . TYR B 1 108 ? 8.810   -0.779  -8.660  1.000 70.285  0 108 TYR B CG  1 
ATOM   2101 C CD1 . TYR B 1 108 ? 9.939   -1.436  -8.180  1.000 68.876  0 108 TYR B CD1 1 
ATOM   2102 C CD2 . TYR B 1 108 ? 8.621   -0.747  -10.039 1.000 58.942  0 108 TYR B CD2 1 
ATOM   2103 C CE1 . TYR B 1 108 ? 10.883  -1.991  -9.034  1.000 73.290  0 108 TYR B CE1 1 
ATOM   2104 C CE2 . TYR B 1 108 ? 9.547   -1.317  -10.904 1.000 65.933  0 108 TYR B CE2 1 
ATOM   2105 C CZ  . TYR B 1 108 ? 10.677  -1.949  -10.402 1.000 68.883  0 108 TYR B CZ  1 
ATOM   2106 O OH  . TYR B 1 108 ? 11.612  -2.494  -11.233 1.000 67.996  0 108 TYR B OH  1 
ATOM   2107 N N   . VAL B 1 109 ? 9.631   2.637   -7.870  1.000 73.768  0 109 VAL B N   1 
ATOM   2108 C CA  . VAL B 1 109 ? 9.917   3.761   -8.749  1.000 75.700  0 109 VAL B CA  1 
ATOM   2109 C C   . VAL B 1 109 ? 10.608  3.251   -10.007 1.000 72.041  0 109 VAL B C   1 
ATOM   2110 O O   . VAL B 1 109 ? 11.749  2.794   -9.919  1.000 67.666  0 109 VAL B O   1 
ATOM   2111 C CB  . VAL B 1 109 ? 10.770  4.810   -8.010  1.000 76.971  0 109 VAL B CB  1 
ATOM   2112 C CG1 . VAL B 1 109 ? 11.098  6.003   -8.895  1.000 81.097  0 109 VAL B CG1 1 
ATOM   2113 C CG2 . VAL B 1 109 ? 10.078  5.282   -6.737  1.000 79.931  0 109 VAL B CG2 1 
ATOM   2114 N N   . LEU B 1 110 ? 9.898   3.353   -11.149 1.000 74.251  0 110 LEU B N   1 
ATOM   2115 C CA  . LEU B 1 110 ? 10.407  2.967   -12.462 1.000 71.048  0 110 LEU B CA  1 
ATOM   2116 C C   . LEU B 1 110 ? 10.620  4.202   -13.332 1.000 67.146  0 110 LEU B C   1 
ATOM   2117 O O   . LEU B 1 110 ? 9.683   4.983   -13.541 1.000 62.742  0 110 LEU B O   1 
ATOM   2118 C CB  . LEU B 1 110 ? 9.357   2.071   -13.116 1.000 78.141  0 110 LEU B CB  1 
ATOM   2119 C CG  . LEU B 1 110 ? 9.836   0.938   -14.032 1.000 86.839  0 110 LEU B CG  1 
ATOM   2120 C CD1 . LEU B 1 110 ? 8.947   0.954   -15.255 1.000 81.654  0 110 LEU B CD1 1 
ATOM   2121 C CD2 . LEU B 1 110 ? 11.294  0.940   -14.443 1.000 102.871 0 110 LEU B CD2 1 
ATOM   2122 N N   . LEU B 1 111 ? 11.843  4.367   -13.843 1.000 68.170  0 111 LEU B N   1 
ATOM   2123 C CA  . LEU B 1 111 ? 12.099  5.384   -14.853 1.000 70.577  0 111 LEU B CA  1 
ATOM   2124 C C   . LEU B 1 111 ? 12.107  4.759   -16.252 1.000 78.998  0 111 LEU B C   1 
ATOM   2125 O O   . LEU B 1 111 ? 12.595  3.637   -16.441 1.000 71.980  0 111 LEU B O   1 
ATOM   2126 C CB  . LEU B 1 111 ? 13.437  6.068   -14.603 1.000 70.883  0 111 LEU B CB  1 
ATOM   2127 C CG  . LEU B 1 111 ? 13.633  6.761   -13.259 1.000 74.092  0 111 LEU B CG  1 
ATOM   2128 C CD1 . LEU B 1 111 ? 14.986  7.459   -13.266 1.000 69.112  0 111 LEU B CD1 1 
ATOM   2129 C CD2 . LEU B 1 111 ? 12.510  7.737   -12.938 1.000 70.965  0 111 LEU B CD2 1 
ATOM   2130 N N   . VAL B 1 112 ? 11.610  5.530   -17.238 1.000 91.525  0 112 VAL B N   1 
ATOM   2131 C CA  . VAL B 1 112 ? 11.574  5.123   -18.636 1.000 84.803  0 112 VAL B CA  1 
ATOM   2132 C C   . VAL B 1 112 ? 12.272  6.186   -19.469 1.000 81.919  0 112 VAL B C   1 
ATOM   2133 O O   . VAL B 1 112 ? 11.777  7.303   -19.541 1.000 83.038  0 112 VAL B O   1 
ATOM   2134 C CB  . VAL B 1 112 ? 10.152  4.966   -19.186 1.000 76.622  0 112 VAL B CB  1 
ATOM   2135 C CG1 . VAL B 1 112 ? 10.198  4.395   -20.588 1.000 100.324 0 112 VAL B CG1 1 
ATOM   2136 C CG2 . VAL B 1 112 ? 9.289   4.081   -18.315 1.000 85.526  0 112 VAL B CG2 1 
ATOM   2137 N N   . ILE B 1 113 ? 13.362  5.804   -20.136 1.000 82.492  0 113 ILE B N   1 
ATOM   2138 C CA  . ILE B 1 113 ? 14.114  6.703   -20.994 1.000 87.306  0 113 ILE B CA  1 
ATOM   2139 C C   . ILE B 1 113 ? 13.928  6.298   -22.449 1.000 81.191  0 113 ILE B C   1 
ATOM   2140 O O   . ILE B 1 113 ? 13.969  5.115   -22.778 1.000 93.072  0 113 ILE B O   1 
ATOM   2141 C CB  . ILE B 1 113 ? 15.597  6.693   -20.601 1.000 80.598  0 113 ILE B CB  1 
ATOM   2142 C CG1 . ILE B 1 113 ? 15.732  7.049   -19.117 1.000 76.857  0 113 ILE B CG1 1 
ATOM   2143 C CG2 . ILE B 1 113 ? 16.391  7.623   -21.517 1.000 83.244  0 113 ILE B CG2 1 
ATOM   2144 C CD1 . ILE B 1 113 ? 17.138  7.288   -18.620 1.000 80.814  0 113 ILE B CD1 1 
ATOM   2145 N N   . PRO B 1 114 ? 13.695  7.259   -23.359 1.000 86.101  0 114 PRO B N   1 
ATOM   2146 C CA  . PRO B 1 114 ? 13.656  6.954   -24.790 1.000 91.877  0 114 PRO B CA  1 
ATOM   2147 C C   . PRO B 1 114 ? 14.937  6.276   -25.259 1.000 86.544  0 114 PRO B C   1 
ATOM   2148 O O   . PRO B 1 114 ? 16.018  6.648   -24.807 1.000 82.613  0 114 PRO B O   1 
ATOM   2149 C CB  . PRO B 1 114 ? 13.470  8.354   -25.383 1.000 107.268 0 114 PRO B CB  1 
ATOM   2150 C CG  . PRO B 1 114 ? 12.675  9.090   -24.326 1.000 104.069 0 114 PRO B CG  1 
ATOM   2151 C CD  . PRO B 1 114 ? 13.368  8.660   -23.054 1.000 105.202 0 114 PRO B CD  1 
ATOM   2152 N N   . ASP B 1 115 ? 14.804  5.291   -26.163 1.000 90.346  0 115 ASP B N   1 
ATOM   2153 C CA  . ASP B 1 115 ? 15.924  4.414   -26.498 1.000 87.525  0 115 ASP B CA  1 
ATOM   2154 C C   . ASP B 1 115 ? 17.058  5.236   -27.112 1.000 84.875  0 115 ASP B C   1 
ATOM   2155 O O   . ASP B 1 115 ? 18.233  4.975   -26.822 1.000 72.410  0 115 ASP B O   1 
ATOM   2156 C CB  . ASP B 1 115 ? 15.528  3.243   -27.382 1.000 90.765  0 115 ASP B CB  1 
ATOM   2157 C CG  . ASP B 1 115 ? 14.343  2.391   -26.931 1.000 99.735  0 115 ASP B CG  1 
ATOM   2158 O OD1 . ASP B 1 115 ? 13.214  2.948   -26.764 1.000 81.804  0 115 ASP B OD1 1 
ATOM   2159 O OD2 . ASP B 1 115 ? 14.543  1.163   -26.776 1.000 85.105  0 115 ASP B OD2 1 
ATOM   2160 N N   . GLU B 1 116 ? 16.699  6.264   -27.906 1.000 79.731  0 116 GLU B N   1 
ATOM   2161 C CA  . GLU B 1 116 ? 17.665  7.175   -28.524 1.000 86.416  0 116 GLU B CA  1 
ATOM   2162 C C   . GLU B 1 116 ? 18.547  7.870   -27.476 1.000 90.592  0 116 GLU B C   1 
ATOM   2163 O O   . GLU B 1 116 ? 19.618  8.379   -27.825 1.000 82.693  0 116 GLU B O   1 
ATOM   2164 C CB  . GLU B 1 116 ? 17.085  8.220   -29.496 1.000 87.053  0 116 GLU B CB  1 
ATOM   2165 C CG  . GLU B 1 116 ? 15.901  9.043   -28.978 1.000 93.496  0 116 GLU B CG  1 
ATOM   2166 C CD  . GLU B 1 116 ? 14.515  8.397   -29.094 1.000 112.055 0 116 GLU B CD  1 
ATOM   2167 O OE1 . GLU B 1 116 ? 14.331  7.132   -28.993 1.000 96.926  0 116 GLU B OE1 1 
ATOM   2168 O OE2 . GLU B 1 116 ? 13.591  9.223   -29.267 1.000 91.689  0 116 GLU B OE2 1 
ATOM   2169 N N   . ASP B 1 117 ? 18.100  7.879   -26.207 1.000 92.317  0 117 ASP B N   1 
ATOM   2170 C CA  . ASP B 1 117 ? 18.791  8.559   -25.128 1.000 81.077  0 117 ASP B CA  1 
ATOM   2171 C C   . ASP B 1 117 ? 19.309  7.604   -24.050 1.000 78.636  0 117 ASP B C   1 
ATOM   2172 O O   . ASP B 1 117 ? 20.140  8.027   -23.248 1.000 73.620  0 117 ASP B O   1 
ATOM   2173 C CB  . ASP B 1 117 ? 17.871  9.564   -24.460 1.000 88.787  0 117 ASP B CB  1 
ATOM   2174 C CG  . ASP B 1 117 ? 17.332  10.688  -25.325 1.000 88.092  0 117 ASP B CG  1 
ATOM   2175 O OD1 . ASP B 1 117 ? 18.073  11.132  -26.214 1.000 93.331  0 117 ASP B OD1 1 
ATOM   2176 O OD2 . ASP B 1 117 ? 16.213  11.159  -25.022 1.000 88.174  0 117 ASP B OD2 1 
ATOM   2177 N N   . TYR B 1 118 ? 18.841  6.347   -24.016 1.000 83.806  0 118 TYR B N   1 
ATOM   2178 C CA  . TYR B 1 118 ? 19.235  5.422   -22.956 1.000 82.268  0 118 TYR B CA  1 
ATOM   2179 C C   . TYR B 1 118 ? 20.744  5.228   -23.014 1.000 78.068  0 118 TYR B C   1 
ATOM   2180 O O   . TYR B 1 118 ? 21.281  5.002   -24.077 1.000 78.769  0 118 TYR B O   1 
ATOM   2181 C CB  . TYR B 1 118 ? 18.607  4.031   -23.044 1.000 82.076  0 118 TYR B CB  1 
ATOM   2182 C CG  . TYR B 1 118 ? 18.764  3.171   -21.797 1.000 86.442  0 118 TYR B CG  1 
ATOM   2183 C CD1 . TYR B 1 118 ? 19.892  2.381   -21.572 1.000 88.746  0 118 TYR B CD1 1 
ATOM   2184 C CD2 . TYR B 1 118 ? 17.734  3.103   -20.860 1.000 95.927  0 118 TYR B CD2 1 
ATOM   2185 C CE1 . TYR B 1 118 ? 20.014  1.596   -20.434 1.000 88.773  0 118 TYR B CE1 1 
ATOM   2186 C CE2 . TYR B 1 118 ? 17.839  2.316   -19.722 1.000 83.175  0 118 TYR B CE2 1 
ATOM   2187 C CZ  . TYR B 1 118 ? 18.985  1.568   -19.504 1.000 89.477  0 118 TYR B CZ  1 
ATOM   2188 O OH  . TYR B 1 118 ? 19.050  0.812   -18.365 1.000 76.042  0 118 TYR B OH  1 
ATOM   2189 N N   . GLY B 1 119 ? 21.409  5.337   -21.867 1.000 80.590  0 119 GLY B N   1 
ATOM   2190 C CA  . GLY B 1 119 ? 22.856  5.358   -21.777 1.000 78.940  0 119 GLY B CA  1 
ATOM   2191 C C   . GLY B 1 119 ? 23.401  6.737   -21.397 1.000 79.192  0 119 GLY B C   1 
ATOM   2192 O O   . GLY B 1 119 ? 24.466  6.818   -20.799 1.000 71.493  0 119 GLY B O   1 
ATOM   2193 N N   . LYS B 1 120 ? 22.676  7.815   -21.741 1.000 91.050  0 120 LYS B N   1 
ATOM   2194 C CA  . LYS B 1 120 ? 23.160  9.172   -21.499 1.000 94.799  0 120 LYS B CA  1 
ATOM   2195 C C   . LYS B 1 120 ? 23.171  9.474   -20.002 1.000 88.868  0 120 LYS B C   1 
ATOM   2196 O O   . LYS B 1 120 ? 22.385  8.913   -19.241 1.000 85.069  0 120 LYS B O   1 
ATOM   2197 C CB  . LYS B 1 120 ? 22.346  10.228  -22.262 1.000 93.709  0 120 LYS B CB  1 
ATOM   2198 C CG  . LYS B 1 120 ? 22.774  10.370  -23.724 1.000 97.832  0 120 LYS B CG  1 
ATOM   2199 C CD  . LYS B 1 120 ? 22.382  11.640  -24.482 1.000 99.917  0 120 LYS B CD  1 
ATOM   2200 C CE  . LYS B 1 120 ? 20.995  11.551  -25.044 1.000 94.561  0 120 LYS B CE  1 
ATOM   2201 N NZ  . LYS B 1 120 ? 20.715  12.503  -26.119 1.000 86.064  0 120 LYS B NZ  1 
ATOM   2202 N N   . PRO B 1 121 ? 24.009  10.426  -19.545 1.000 89.249  0 121 PRO B N   1 
ATOM   2203 C CA  . PRO B 1 121 ? 24.177  10.687  -18.117 1.000 87.874  0 121 PRO B CA  1 
ATOM   2204 C C   . PRO B 1 121 ? 22.885  11.197  -17.499 1.000 81.894  0 121 PRO B C   1 
ATOM   2205 O O   . PRO B 1 121 ? 22.223  12.017  -18.126 1.000 86.160  0 121 PRO B O   1 
ATOM   2206 C CB  . PRO B 1 121 ? 25.291  11.756  -18.049 1.000 98.325  0 121 PRO B CB  1 
ATOM   2207 C CG  . PRO B 1 121 ? 25.899  11.793  -19.437 1.000 91.194  0 121 PRO B CG  1 
ATOM   2208 C CD  . PRO B 1 121 ? 24.774  11.377  -20.364 1.000 91.916  0 121 PRO B CD  1 
ATOM   2209 N N   . ILE B 1 122 ? 22.543  10.681  -16.302 1.000 87.183  0 122 ILE B N   1 
ATOM   2210 C CA  . ILE B 1 122 ? 21.423  11.160  -15.503 1.000 83.596  0 122 ILE B CA  1 
ATOM   2211 C C   . ILE B 1 122 ? 21.932  11.619  -14.140 1.000 80.968  0 122 ILE B C   1 
ATOM   2212 O O   . ILE B 1 122 ? 22.961  11.185  -13.644 1.000 82.604  0 122 ILE B O   1 
ATOM   2213 C CB  . ILE B 1 122 ? 20.318  10.098  -15.330 1.000 87.133  0 122 ILE B CB  1 
ATOM   2214 C CG1 . ILE B 1 122 ? 20.782  8.925   -14.482 1.000 94.652  0 122 ILE B CG1 1 
ATOM   2215 C CG2 . ILE B 1 122 ? 19.764  9.627   -16.673 1.000 82.370  0 122 ILE B CG2 1 
ATOM   2216 C CD1 . ILE B 1 122 ? 19.676  7.952   -14.121 1.000 97.990  0 122 ILE B CD1 1 
ATOM   2217 N N   . ASN B 1 123 ? 21.157  12.478  -13.494 1.000 80.876  0 123 ASN B N   1 
ATOM   2218 C CA  . ASN B 1 123 ? 21.509  12.946  -12.165 1.000 77.127  0 123 ASN B CA  1 
ATOM   2219 C C   . ASN B 1 123 ? 21.655  11.793  -11.156 1.000 69.469  0 123 ASN B C   1 
ATOM   2220 O O   . ASN B 1 123 ? 20.838  10.891  -11.092 1.000 66.064  0 123 ASN B O   1 
ATOM   2221 C CB  . ASN B 1 123 ? 20.471  13.967  -11.714 1.000 74.365  0 123 ASN B CB  1 
ATOM   2222 C CG  . ASN B 1 123 ? 20.905  14.635  -10.441 1.000 68.610  0 123 ASN B CG  1 
ATOM   2223 O OD1 . ASN B 1 123 ? 20.759  14.018  -9.383  1.000 65.946  0 123 ASN B OD1 1 
ATOM   2224 N ND2 . ASN B 1 123 ? 21.472  15.838  -10.523 1.000 76.347  0 123 ASN B ND2 1 
ATOM   2225 N N   . LEU B 1 124 ? 22.667  11.878  -10.284 1.000 71.660  0 124 LEU B N   1 
ATOM   2226 C CA  . LEU B 1 124 ? 22.901  10.892  -9.232  1.000 68.948  0 124 LEU B CA  1 
ATOM   2227 C C   . LEU B 1 124 ? 21.652  10.607  -8.409  1.000 69.956  0 124 LEU B C   1 
ATOM   2228 O O   . LEU B 1 124 ? 21.363  9.443   -8.157  1.000 61.718  0 124 LEU B O   1 
ATOM   2229 C CB  . LEU B 1 124 ? 24.040  11.276  -8.296  1.000 71.020  0 124 LEU B CB  1 
ATOM   2230 C CG  . LEU B 1 124 ? 24.239  10.334  -7.106  1.000 69.027  0 124 LEU B CG  1 
ATOM   2231 C CD1 . LEU B 1 124 ? 24.774  9.010   -7.588  1.000 66.994  0 124 LEU B CD1 1 
ATOM   2232 C CD2 . LEU B 1 124 ? 25.149  10.917  -6.042  1.000 68.468  0 124 LEU B CD2 1 
ATOM   2233 N N   . MET B 1 125 ? 20.929  11.641  -7.962  1.000 69.097  0 125 MET B N   1 
ATOM   2234 C CA  . MET B 1 125 ? 19.799  11.394  -7.073  1.000 68.614  0 125 MET B CA  1 
ATOM   2235 C C   . MET B 1 125 ? 18.651  10.708  -7.812  1.000 64.073  0 125 MET B C   1 
ATOM   2236 O O   . MET B 1 125 ? 17.876  9.994   -7.172  1.000 61.643  0 125 MET B O   1 
ATOM   2237 C CB  . MET B 1 125 ? 19.284  12.663  -6.387  1.000 61.484  0 125 MET B CB  1 
ATOM   2238 C CG  . MET B 1 125 ? 20.384  13.521  -5.806  1.000 66.461  0 125 MET B CG  1 
ATOM   2239 S SD  . MET B 1 125 ? 21.532  12.629  -4.744  1.000 71.472  0 125 MET B SD  1 
ATOM   2240 C CE  . MET B 1 125 ? 20.586  12.640  -3.217  1.000 73.032  0 125 MET B CE  1 
ATOM   2241 N N   . SER B 1 126 ? 18.547  10.915  -9.140  1.000 62.701  0 126 SER B N   1 
ATOM   2242 C CA  . SER B 1 126 ? 17.538  10.228  -9.944  1.000 68.028  0 126 SER B CA  1 
ATOM   2243 C C   . SER B 1 126 ? 17.854  8.731   -10.029 1.000 68.556  0 126 SER B C   1 
ATOM   2244 O O   . SER B 1 126 ? 17.009  7.868   -9.805  1.000 63.393  0 126 SER B O   1 
ATOM   2245 C CB  . SER B 1 126 ? 17.428  10.840  -11.315 1.000 70.273  0 126 SER B CB  1 
ATOM   2246 O OG  . SER B 1 126 ? 16.976  12.180  -11.244 1.000 75.300  0 126 SER B OG  1 
ATOM   2247 N N   . TRP B 1 127 ? 19.117  8.448   -10.320 1.000 66.336  0 127 TRP B N   1 
ATOM   2248 C CA  . TRP B 1 127 ? 19.675  7.111   -10.253 1.000 72.603  0 127 TRP B CA  1 
ATOM   2249 C C   . TRP B 1 127 ? 19.342  6.420   -8.926  1.000 61.421  0 127 TRP B C   1 
ATOM   2250 O O   . TRP B 1 127 ? 18.936  5.264   -8.909  1.000 75.000  0 127 TRP B O   1 
ATOM   2251 C CB  . TRP B 1 127 ? 21.186  7.258   -10.481 1.000 82.075  0 127 TRP B CB  1 
ATOM   2252 C CG  . TRP B 1 127 ? 21.965  5.980   -10.387 1.000 83.012  0 127 TRP B CG  1 
ATOM   2253 C CD1 . TRP B 1 127 ? 22.219  5.127   -11.413 1.000 81.904  0 127 TRP B CD1 1 
ATOM   2254 C CD2 . TRP B 1 127 ? 22.627  5.436   -9.226  1.000 68.630  0 127 TRP B CD2 1 
ATOM   2255 N NE1 . TRP B 1 127 ? 22.967  4.077   -10.968 1.000 73.741  0 127 TRP B NE1 1 
ATOM   2256 C CE2 . TRP B 1 127 ? 23.252  4.250   -9.638  1.000 67.241  0 127 TRP B CE2 1 
ATOM   2257 C CE3 . TRP B 1 127 ? 22.767  5.827   -7.896  1.000 74.210  0 127 TRP B CE3 1 
ATOM   2258 C CZ2 . TRP B 1 127 ? 23.996  3.460   -8.763  1.000 67.590  0 127 TRP B CZ2 1 
ATOM   2259 C CZ3 . TRP B 1 127 ? 23.508  5.045   -7.034  1.000 73.009  0 127 TRP B CZ3 1 
ATOM   2260 C CH2 . TRP B 1 127 ? 24.104  3.873   -7.459  1.000 68.940  0 127 TRP B CH2 1 
ATOM   2261 N N   . GLY B 1 128 ? 19.491  7.151   -7.817  1.000 70.212  0 128 GLY B N   1 
ATOM   2262 C CA  . GLY B 1 128 ? 19.354  6.634   -6.457  1.000 70.895  0 128 GLY B CA  1 
ATOM   2263 C C   . GLY B 1 128 ? 17.906  6.307   -6.068  1.000 66.982  0 128 GLY B C   1 
ATOM   2264 O O   . GLY B 1 128 ? 17.623  5.196   -5.592  1.000 63.257  0 128 GLY B O   1 
ATOM   2265 N N   . VAL B 1 129 ? 16.975  7.231   -6.332  1.000 66.207  0 129 VAL B N   1 
ATOM   2266 C CA  . VAL B 1 129 ? 15.573  6.987   -5.992  1.000 78.541  0 129 VAL B CA  1 
ATOM   2267 C C   . VAL B 1 129 ? 15.011  5.782   -6.750  1.000 69.079  0 129 VAL B C   1 
ATOM   2268 O O   . VAL B 1 129 ? 14.122  5.105   -6.217  1.000 70.444  0 129 VAL B O   1 
ATOM   2269 C CB  . VAL B 1 129 ? 14.602  8.156   -6.219  1.000 73.259  0 129 VAL B CB  1 
ATOM   2270 C CG1 . VAL B 1 129 ? 14.593  9.092   -5.037  1.000 76.187  0 129 VAL B CG1 1 
ATOM   2271 C CG2 . VAL B 1 129 ? 14.866  8.873   -7.540  1.000 77.543  0 129 VAL B CG2 1 
ATOM   2272 N N   . SER B 1 130 ? 15.447  5.621   -8.005  1.000 71.077  0 130 SER B N   1 
ATOM   2273 C CA  . SER B 1 130 ? 15.018  4.546   -8.884  1.000 66.866  0 130 SER B CA  1 
ATOM   2274 C C   . SER B 1 130 ? 15.303  3.192   -8.256  1.000 76.086  0 130 SER B C   1 
ATOM   2275 O O   . SER B 1 130 ? 16.432  2.949   -7.767  1.000 71.346  0 130 SER B O   1 
ATOM   2276 C CB  . SER B 1 130 ? 15.719  4.604   -10.189 1.000 65.710  0 130 SER B CB  1 
ATOM   2277 O OG  . SER B 1 130 ? 15.502  5.879   -10.762 1.000 96.093  0 130 SER B OG  1 
ATOM   2278 N N   . ASP B 1 131 ? 14.255  2.349   -8.343  1.000 63.809  0 131 ASP B N   1 
ATOM   2279 C CA  . ASP B 1 131 ? 14.369  0.911   -8.207  1.000 73.872  0 131 ASP B CA  1 
ATOM   2280 C C   . ASP B 1 131 ? 14.883  0.247   -9.492  1.000 68.591  0 131 ASP B C   1 
ATOM   2281 O O   . ASP B 1 131 ? 15.597  -0.757  -9.440  1.000 70.992  0 131 ASP B O   1 
ATOM   2282 C CB  . ASP B 1 131 ? 13.041  0.361   -7.742  1.000 78.683  0 131 ASP B CB  1 
ATOM   2283 C CG  . ASP B 1 131 ? 12.709  0.744   -6.310  1.000 78.359  0 131 ASP B CG  1 
ATOM   2284 O OD1 . ASP B 1 131 ? 13.417  0.234   -5.413  1.000 79.699  0 131 ASP B OD1 1 
ATOM   2285 O OD2 . ASP B 1 131 ? 11.750  1.533   -6.125  1.000 78.675  0 131 ASP B OD2 1 
ATOM   2286 N N   . ASN B 1 132 ? 14.597  0.857   -10.638 1.000 62.707  0 132 ASN B N   1 
ATOM   2287 C CA  . ASN B 1 132 ? 14.985  0.303   -11.913 1.000 71.360  0 132 ASN B CA  1 
ATOM   2288 C C   . ASN B 1 132 ? 14.854  1.405   -12.969 1.000 82.742  0 132 ASN B C   1 
ATOM   2289 O O   . ASN B 1 132 ? 14.055  2.354   -12.818 1.000 70.119  0 132 ASN B O   1 
ATOM   2290 C CB  . ASN B 1 132 ? 14.109  -0.930  -12.108 1.000 82.075  0 132 ASN B CB  1 
ATOM   2291 C CG  . ASN B 1 132 ? 14.314  -1.700  -13.386 1.000 81.622  0 132 ASN B CG  1 
ATOM   2292 O OD1 . ASN B 1 132 ? 13.364  -2.347  -13.831 1.000 93.906  0 132 ASN B OD1 1 
ATOM   2293 N ND2 . ASN B 1 132 ? 15.495  -1.677  -13.980 1.000 75.423  0 132 ASN B ND2 1 
ATOM   2294 N N   . VAL B 1 133 ? 15.630  1.284   -14.055 1.000 75.916  0 133 VAL B N   1 
ATOM   2295 C CA  . VAL B 1 133 ? 15.384  2.148   -15.203 1.000 76.848  0 133 VAL B CA  1 
ATOM   2296 C C   . VAL B 1 133 ? 15.535  1.381   -16.523 1.000 78.514  0 133 VAL B C   1 
ATOM   2297 O O   . VAL B 1 133 ? 16.486  0.622   -16.720 1.000 70.554  0 133 VAL B O   1 
ATOM   2298 C CB  . VAL B 1 133 ? 16.251  3.420   -15.106 1.000 80.603  0 133 VAL B CB  1 
ATOM   2299 C CG1 . VAL B 1 133 ? 17.368  3.322   -14.091 1.000 73.082  0 133 VAL B CG1 1 
ATOM   2300 C CG2 . VAL B 1 133 ? 16.784  3.875   -16.447 1.000 93.187  0 133 VAL B CG2 1 
ATOM   2301 N N   . ILE B 1 134 ? 14.572  1.616   -17.427 1.000 76.438  0 134 ILE B N   1 
ATOM   2302 C CA  . ILE B 1 134 ? 14.411  0.820   -18.636 1.000 85.594  0 134 ILE B CA  1 
ATOM   2303 C C   . ILE B 1 134 ? 14.283  1.710   -19.872 1.000 88.468  0 134 ILE B C   1 
ATOM   2304 O O   . ILE B 1 134 ? 14.068  2.905   -19.740 1.000 80.344  0 134 ILE B O   1 
ATOM   2305 C CB  . ILE B 1 134 ? 13.203  -0.120  -18.499 1.000 68.250  0 134 ILE B CB  1 
ATOM   2306 C CG1 . ILE B 1 134 ? 11.897  0.654   -18.401 1.000 67.293  0 134 ILE B CG1 1 
ATOM   2307 C CG2 . ILE B 1 134 ? 13.414  -1.033  -17.300 1.000 71.539  0 134 ILE B CG2 1 
ATOM   2308 C CD1 . ILE B 1 134 ? 10.657  -0.210  -18.553 1.000 66.110  0 134 ILE B CD1 1 
ATOM   2309 N N   . LYS B 1 135 ? 14.424  1.081   -21.055 1.000 96.431  0 135 LYS B N   1 
ATOM   2310 C CA  . LYS B 1 135 ? 14.254  1.718   -22.353 1.000 95.169  0 135 LYS B CA  1 
ATOM   2311 C C   . LYS B 1 135 ? 12.749  1.738   -22.628 1.000 88.305  0 135 LYS B C   1 
ATOM   2312 O O   . LYS B 1 135 ? 12.006  0.877   -22.133 1.000 85.406  0 135 LYS B O   1 
ATOM   2313 C CB  . LYS B 1 135 ? 15.072  1.035   -23.475 1.000 101.769 0 135 LYS B CB  1 
ATOM   2314 C CG  . LYS B 1 135 ? 16.509  0.516   -23.164 1.000 106.662 0 135 LYS B CG  1 
ATOM   2315 C CD  . LYS B 1 135 ? 17.432  0.029   -24.292 1.000 87.109  0 135 LYS B CD  1 
ATOM   2316 N N   . MET B 1 136 ? 12.304  2.728   -23.419 1.000 79.066  0 136 MET B N   1 
ATOM   2317 C CA  . MET B 1 136 ? 10.892  2.892   -23.745 1.000 73.876  0 136 MET B CA  1 
ATOM   2318 C C   . MET B 1 136 ? 10.332  1.641   -24.415 1.000 72.114  0 136 MET B C   1 
ATOM   2319 O O   . MET B 1 136 ? 9.186   1.265   -24.161 1.000 86.943  0 136 MET B O   1 
ATOM   2320 C CB  . MET B 1 136 ? 10.691  4.096   -24.655 1.000 75.000  0 136 MET B CB  1 
ATOM   2321 C CG  . MET B 1 136 ? 9.238   4.391   -25.011 1.000 90.218  0 136 MET B CG  1 
ATOM   2322 S SD  . MET B 1 136 ? 8.267   5.331   -23.824 1.000 92.994  0 136 MET B SD  1 
ATOM   2323 C CE  . MET B 1 136 ? 9.367   6.754   -23.660 1.000 87.258  0 136 MET B CE  1 
ATOM   2324 N N   . SER B 1 137 ? 11.159  0.981   -25.236 1.000 80.260  0 137 SER B N   1 
ATOM   2325 C CA  . SER B 1 137 ? 10.755  -0.235  -25.926 1.000 79.944  0 137 SER B CA  1 
ATOM   2326 C C   . SER B 1 137 ? 10.470  -1.403  -24.977 1.000 85.057  0 137 SER B C   1 
ATOM   2327 O O   . SER B 1 137 ? 9.783   -2.331  -25.402 1.000 92.795  0 137 SER B O   1 
ATOM   2328 C CB  . SER B 1 137 ? 11.788  -0.615  -26.930 1.000 80.706  0 137 SER B CB  1 
ATOM   2329 O OG  . SER B 1 137 ? 13.065  -0.717  -26.313 1.000 84.804  0 137 SER B OG  1 
ATOM   2330 N N   . GLN B 1 138 ? 10.986  -1.382  -23.724 1.000 80.693  0 138 GLN B N   1 
ATOM   2331 C CA  . GLN B 1 138 ? 10.733  -2.476  -22.782 1.000 74.159  0 138 GLN B CA  1 
ATOM   2332 C C   . GLN B 1 138 ? 9.433   -2.248  -21.974 1.000 79.069  0 138 GLN B C   1 
ATOM   2333 O O   . GLN B 1 138 ? 8.936   -3.151  -21.276 1.000 79.570  0 138 GLN B O   1 
ATOM   2334 C CB  . GLN B 1 138 ? 11.896  -2.824  -21.845 1.000 63.368  0 138 GLN B CB  1 
ATOM   2335 C CG  . GLN B 1 138 ? 13.295  -2.841  -22.461 1.000 71.885  0 138 GLN B CG  1 
ATOM   2336 C CD  . GLN B 1 138 ? 14.419  -2.760  -21.434 1.000 84.688  0 138 GLN B CD  1 
ATOM   2337 O OE1 . GLN B 1 138 ? 15.004  -1.702  -21.177 1.000 88.115  0 138 GLN B OE1 1 
ATOM   2338 N NE2 . GLN B 1 138 ? 14.733  -3.864  -20.778 1.000 81.633  0 138 GLN B NE2 1 
ATOM   2339 N N   . LEU B 1 139 ? 8.815   -1.071  -22.117 1.000 71.394  0 139 LEU B N   1 
ATOM   2340 C CA  . LEU B 1 139 ? 7.664   -0.724  -21.307 1.000 74.561  0 139 LEU B CA  1 
ATOM   2341 C C   . LEU B 1 139 ? 6.421   -1.500  -21.730 1.000 87.498  0 139 LEU B C   1 
ATOM   2342 O O   . LEU B 1 139 ? 5.636   -1.863  -20.849 1.000 99.048  0 139 LEU B O   1 
ATOM   2343 C CB  . LEU B 1 139 ? 7.412   0.784   -21.351 1.000 84.373  0 139 LEU B CB  1 
ATOM   2344 C CG  . LEU B 1 139 ? 6.253   1.309   -20.486 1.000 83.886  0 139 LEU B CG  1 
ATOM   2345 C CD1 . LEU B 1 139 ? 6.382   0.931   -19.022 1.000 84.434  0 139 LEU B CD1 1 
ATOM   2346 C CD2 . LEU B 1 139 ? 6.132   2.804   -20.596 1.000 78.052  0 139 LEU B CD2 1 
ATOM   2347 N N   . LYS B 1 140 ? 6.210   -1.731  -23.043 1.000 105.410 0 140 LYS B N   1 
ATOM   2348 C CA  . LYS B 1 140 ? 5.045   -2.495  -23.496 1.000 111.131 0 140 LYS B CA  1 
ATOM   2349 C C   . LYS B 1 140 ? 4.967   -3.861  -22.789 1.000 103.156 0 140 LYS B C   1 
ATOM   2350 O O   . LYS B 1 140 ? 3.864   -4.386  -22.637 1.000 97.014  0 140 LYS B O   1 
ATOM   2351 C CB  . LYS B 1 140 ? 4.972   -2.691  -25.020 1.000 98.621  0 140 LYS B CB  1 
ATOM   2352 N N   . ASP B 1 141 ? 6.113   -4.416  -22.331 1.000 88.114  0 141 ASP B N   1 
ATOM   2353 C CA  . ASP B 1 141 ? 6.163   -5.803  -21.887 1.000 94.038  0 141 ASP B CA  1 
ATOM   2354 C C   . ASP B 1 141 ? 6.593   -5.945  -20.428 1.000 96.994  0 141 ASP B C   1 
ATOM   2355 O O   . ASP B 1 141 ? 6.712   -7.066  -19.932 1.000 81.516  0 141 ASP B O   1 
ATOM   2356 C CB  . ASP B 1 141 ? 7.096   -6.644  -22.751 1.000 111.548 0 141 ASP B CB  1 
ATOM   2357 C CG  . ASP B 1 141 ? 7.014   -6.424  -24.255 1.000 118.612 0 141 ASP B CG  1 
ATOM   2358 O OD1 . ASP B 1 141 ? 7.673   -5.483  -24.739 1.000 131.935 0 141 ASP B OD1 1 
ATOM   2359 O OD2 . ASP B 1 141 ? 6.252   -7.146  -24.913 1.000 106.941 0 141 ASP B OD2 1 
ATOM   2360 N N   . PHE B 1 142 ? 6.819   -4.829  -19.726 1.000 99.053  0 142 PHE B N   1 
ATOM   2361 C CA  . PHE B 1 142 ? 7.323   -4.884  -18.361 1.000 88.645  0 142 PHE B CA  1 
ATOM   2362 C C   . PHE B 1 142 ? 6.321   -5.595  -17.447 1.000 88.828  0 142 PHE B C   1 
ATOM   2363 O O   . PHE B 1 142 ? 5.123   -5.279  -17.468 1.000 84.672  0 142 PHE B O   1 
ATOM   2364 C CB  . PHE B 1 142 ? 7.618   -3.460  -17.862 1.000 94.850  0 142 PHE B CB  1 
ATOM   2365 C CG  . PHE B 1 142 ? 8.348   -3.419  -16.522 1.000 82.500  0 142 PHE B CG  1 
ATOM   2366 C CD1 . PHE B 1 142 ? 9.723   -3.631  -16.447 1.000 85.428  0 142 PHE B CD1 1 
ATOM   2367 C CD2 . PHE B 1 142 ? 7.667   -3.217  -15.336 1.000 83.498  0 142 PHE B CD2 1 
ATOM   2368 C CE1 . PHE B 1 142 ? 10.390  -3.660  -15.233 1.000 81.635  0 142 PHE B CE1 1 
ATOM   2369 C CE2 . PHE B 1 142 ? 8.340   -3.267  -14.122 1.000 93.066  0 142 PHE B CE2 1 
ATOM   2370 C CZ  . PHE B 1 142 ? 9.696   -3.499  -14.073 1.000 83.542  0 142 PHE B CZ  1 
ATOM   2371 N N   . ASN B 1 143 ? 6.816   -6.535  -16.621 1.000 73.237  0 143 ASN B N   1 
ATOM   2372 C CA  . ASN B 1 143 ? 5.933   -7.247  -15.710 1.000 79.964  0 143 ASN B CA  1 
ATOM   2373 C C   . ASN B 1 143 ? 5.803   -6.494  -14.384 1.000 85.945  0 143 ASN B C   1 
ATOM   2374 O O   . ASN B 1 143 ? 6.665   -6.595  -13.507 1.000 84.439  0 143 ASN B O   1 
ATOM   2375 C CB  . ASN B 1 143 ? 6.390   -8.683  -15.468 1.000 72.807  0 143 ASN B CB  1 
ATOM   2376 C CG  . ASN B 1 143 ? 5.357   -9.466  -14.676 1.000 76.937  0 143 ASN B CG  1 
ATOM   2377 O OD1 . ASN B 1 143 ? 4.261   -8.967  -14.372 1.000 77.605  0 143 ASN B OD1 1 
ATOM   2378 N ND2 . ASN B 1 143 ? 5.685   -10.699 -14.317 1.000 80.235  0 143 ASN B ND2 1 
ATOM   2379 N N   . PHE B 1 144 ? 4.683   -5.790  -14.224 1.000 77.007  0 144 PHE B N   1 
ATOM   2380 C CA  . PHE B 1 144 ? 4.469   -4.935  -13.067 1.000 74.816  0 144 PHE B CA  1 
ATOM   2381 C C   . PHE B 1 144 ? 3.986   -5.729  -11.855 1.000 88.170  0 144 PHE B C   1 
ATOM   2382 O O   . PHE B 1 144 ? 3.822   -5.166  -10.765 1.000 103.880 0 144 PHE B O   1 
ATOM   2383 C CB  . PHE B 1 144 ? 3.463   -3.833  -13.409 1.000 75.717  0 144 PHE B CB  1 
ATOM   2384 C CG  . PHE B 1 144 ? 4.089   -2.691  -14.195 1.000 80.826  0 144 PHE B CG  1 
ATOM   2385 C CD1 . PHE B 1 144 ? 4.939   -1.777  -13.577 1.000 87.423  0 144 PHE B CD1 1 
ATOM   2386 C CD2 . PHE B 1 144 ? 3.846   -2.540  -15.552 1.000 83.549  0 144 PHE B CD2 1 
ATOM   2387 C CE1 . PHE B 1 144 ? 5.535   -0.763  -14.302 1.000 85.965  0 144 PHE B CE1 1 
ATOM   2388 C CE2 . PHE B 1 144 ? 4.415   -1.490  -16.255 1.000 84.984  0 144 PHE B CE2 1 
ATOM   2389 C CZ  . PHE B 1 144 ? 5.260   -0.616  -15.637 1.000 82.583  0 144 PHE B CZ  1 
ATOM   2390 N N   . ASN B 1 145 ? 3.760   -7.034  -12.036 1.000 82.480  0 145 ASN B N   1 
ATOM   2391 C CA  . ASN B 1 145 ? 3.330   -7.865  -10.927 1.000 82.941  0 145 ASN B CA  1 
ATOM   2392 C C   . ASN B 1 145 ? 4.561   -8.399  -10.196 1.000 78.474  0 145 ASN B C   1 
ATOM   2393 O O   . ASN B 1 145 ? 4.430   -8.857  -9.062  1.000 81.150  0 145 ASN B O   1 
ATOM   2394 C CB  . ASN B 1 145 ? 2.372   -8.979  -11.349 1.000 89.338  0 145 ASN B CB  1 
ATOM   2395 C CG  . ASN B 1 145 ? 1.065   -8.440  -11.905 1.000 99.361  0 145 ASN B CG  1 
ATOM   2396 O OD1 . ASN B 1 145 ? 0.354   -7.683  -11.233 1.000 82.163  0 145 ASN B OD1 1 
ATOM   2397 N ND2 . ASN B 1 145 ? 0.726   -8.799  -13.137 1.000 98.827  0 145 ASN B ND2 1 
ATOM   2398 N N   . LYS B 1 146 ? 5.737   -8.344  -10.849 1.000 79.709  0 146 LYS B N   1 
ATOM   2399 C CA  . LYS B 1 146 ? 6.981   -8.887  -10.311 1.000 76.319  0 146 LYS B CA  1 
ATOM   2400 C C   . LYS B 1 146 ? 8.091   -7.858  -10.543 1.000 87.249  0 146 LYS B C   1 
ATOM   2401 O O   . LYS B 1 146 ? 9.086   -8.137  -11.203 1.000 86.545  0 146 LYS B O   1 
ATOM   2402 C CB  . LYS B 1 146 ? 7.345   -10.262 -10.910 1.000 84.092  0 146 LYS B CB  1 
ATOM   2403 C CG  . LYS B 1 146 ? 6.260   -11.361 -10.908 1.000 99.620  0 146 LYS B CG  1 
ATOM   2404 C CD  . LYS B 1 146 ? 6.701   -12.741 -11.404 1.000 106.294 0 146 LYS B CD  1 
ATOM   2405 C CE  . LYS B 1 146 ? 7.553   -13.449 -10.379 1.000 120.520 0 146 LYS B CE  1 
ATOM   2406 N NZ  . LYS B 1 146 ? 8.278   -14.621 -10.886 1.000 101.041 0 146 LYS B NZ  1 
ATOM   2407 N N   . PRO B 1 147 ? 7.973   -6.625  -9.993  1.000 88.781  0 147 PRO B N   1 
ATOM   2408 C CA  . PRO B 1 147 ? 8.946   -5.566  -10.284 1.000 76.796  0 147 PRO B CA  1 
ATOM   2409 C C   . PRO B 1 147 ? 10.191  -5.705  -9.418  1.000 67.761  0 147 PRO B C   1 
ATOM   2410 O O   . PRO B 1 147 ? 10.064  -5.985  -8.239  1.000 73.531  0 147 PRO B O   1 
ATOM   2411 C CB  . PRO B 1 147 ? 8.119   -4.326  -9.947  1.000 74.941  0 147 PRO B CB  1 
ATOM   2412 C CG  . PRO B 1 147 ? 7.253   -4.763  -8.786  1.000 79.199  0 147 PRO B CG  1 
ATOM   2413 C CD  . PRO B 1 147 ? 6.898   -6.193  -9.081  1.000 80.832  0 147 PRO B CD  1 
ATOM   2414 N N   . ARG B 1 148 ? 11.377  -5.497  -9.992  1.000 64.992  0 148 ARG B N   1 
ATOM   2415 C CA  . ARG B 1 148 ? 12.617  -5.873  -9.327  1.000 74.483  0 148 ARG B CA  1 
ATOM   2416 C C   . ARG B 1 148 ? 13.637  -4.733  -9.386  1.000 74.546  0 148 ARG B C   1 
ATOM   2417 O O   . ARG B 1 148 ? 13.528  -3.797  -10.178 1.000 60.606  0 148 ARG B O   1 
ATOM   2418 C CB  . ARG B 1 148 ? 13.202  -7.147  -9.960  1.000 76.662  0 148 ARG B CB  1 
ATOM   2419 C CG  . ARG B 1 148 ? 12.329  -8.402  -10.001 1.000 80.417  0 148 ARG B CG  1 
ATOM   2420 C CD  . ARG B 1 148 ? 12.003  -8.949  -8.615  1.000 90.763  0 148 ARG B CD  1 
ATOM   2421 N NE  . ARG B 1 148 ? 10.996  -10.020 -8.570  1.000 115.100 0 148 ARG B NE  1 
ATOM   2422 C CZ  . ARG B 1 148 ? 9.783   -9.997  -8.007  1.000 120.234 0 148 ARG B CZ  1 
ATOM   2423 N NH1 . ARG B 1 148 ? 9.124   -11.143 -7.860  1.000 127.981 0 148 ARG B NH1 1 
ATOM   2424 N NH2 . ARG B 1 148 ? 9.251   -8.859  -7.572  1.000 104.280 0 148 ARG B NH2 1 
ATOM   2425 N N   . PHE B 1 149 ? 14.669  -4.858  -8.550  1.000 74.728  0 149 PHE B N   1 
ATOM   2426 C CA  . PHE B 1 149 ? 15.703  -3.848  -8.478  1.000 71.888  0 149 PHE B CA  1 
ATOM   2427 C C   . PHE B 1 149 ? 16.717  -4.090  -9.591  1.000 70.381  0 149 PHE B C   1 
ATOM   2428 O O   . PHE B 1 149 ? 17.208  -5.200  -9.720  1.000 75.141  0 149 PHE B O   1 
ATOM   2429 C CB  . PHE B 1 149 ? 16.453  -3.880  -7.148  1.000 68.083  0 149 PHE B CB  1 
ATOM   2430 C CG  . PHE B 1 149 ? 17.585  -2.867  -7.204  1.000 84.626  0 149 PHE B CG  1 
ATOM   2431 C CD1 . PHE B 1 149 ? 18.832  -3.239  -7.715  1.000 78.791  0 149 PHE B CD1 1 
ATOM   2432 C CD2 . PHE B 1 149 ? 17.372  -1.534  -6.837  1.000 81.160  0 149 PHE B CD2 1 
ATOM   2433 C CE1 . PHE B 1 149 ? 19.858  -2.319  -7.809  1.000 79.147  0 149 PHE B CE1 1 
ATOM   2434 C CE2 . PHE B 1 149 ? 18.399  -0.616  -6.948  1.000 81.639  0 149 PHE B CE2 1 
ATOM   2435 C CZ  . PHE B 1 149 ? 19.641  -1.014  -7.427  1.000 86.638  0 149 PHE B CZ  1 
ATOM   2436 N N   . ASP B 1 150 ? 17.080  -3.049  -10.346 1.000 67.621  0 150 ASP B N   1 
ATOM   2437 C CA  . ASP B 1 150 ? 18.258  -3.136  -11.186 1.000 78.229  0 150 ASP B CA  1 
ATOM   2438 C C   . ASP B 1 150 ? 18.901  -1.761  -11.338 1.000 73.715  0 150 ASP B C   1 
ATOM   2439 O O   . ASP B 1 150 ? 18.264  -0.752  -11.077 1.000 87.595  0 150 ASP B O   1 
ATOM   2440 C CB  . ASP B 1 150 ? 17.919  -3.738  -12.538 1.000 86.812  0 150 ASP B CB  1 
ATOM   2441 C CG  . ASP B 1 150 ? 19.079  -4.355  -13.305 1.000 93.465  0 150 ASP B CG  1 
ATOM   2442 O OD1 . ASP B 1 150 ? 20.239  -4.361  -12.770 1.000 87.744  0 150 ASP B OD1 1 
ATOM   2443 O OD2 . ASP B 1 150 ? 18.791  -4.846  -14.423 1.000 96.352  0 150 ASP B OD2 1 
ATOM   2444 N N   . PHE B 1 151 ? 20.166  -1.750  -11.770 1.000 72.203  0 151 PHE B N   1 
ATOM   2445 C CA  . PHE B 1 151 ? 20.930  -0.536  -11.993 1.000 69.809  0 151 PHE B CA  1 
ATOM   2446 C C   . PHE B 1 151 ? 20.758  -0.057  -13.433 1.000 68.210  0 151 PHE B C   1 
ATOM   2447 O O   . PHE B 1 151 ? 20.707  -0.860  -14.359 1.000 78.408  0 151 PHE B O   1 
ATOM   2448 C CB  . PHE B 1 151 ? 22.408  -0.830  -11.730 1.000 71.812  0 151 PHE B CB  1 
ATOM   2449 C CG  . PHE B 1 151 ? 22.869  -1.022  -10.290 1.000 76.490  0 151 PHE B CG  1 
ATOM   2450 C CD1 . PHE B 1 151 ? 22.916  0.044   -9.396  1.000 81.736  0 151 PHE B CD1 1 
ATOM   2451 C CD2 . PHE B 1 151 ? 23.382  -2.238  -9.862  1.000 77.805  0 151 PHE B CD2 1 
ATOM   2452 C CE1 . PHE B 1 151 ? 23.386  -0.125  -8.099  1.000 77.254  0 151 PHE B CE1 1 
ATOM   2453 C CE2 . PHE B 1 151 ? 23.832  -2.405  -8.557  1.000 84.324  0 151 PHE B CE2 1 
ATOM   2454 C CZ  . PHE B 1 151 ? 23.836  -1.346  -7.680  1.000 76.108  0 151 PHE B CZ  1 
ATOM   2455 N N   . TYR B 1 152 ? 20.684  1.263   -13.623 1.000 84.727  0 152 TYR B N   1 
ATOM   2456 C CA  . TYR B 1 152 ? 20.827  1.886   -14.939 1.000 86.050  0 152 TYR B CA  1 
ATOM   2457 C C   . TYR B 1 152 ? 22.157  1.524   -15.590 1.000 86.588  0 152 TYR B C   1 
ATOM   2458 O O   . TYR B 1 152 ? 23.190  1.619   -14.935 1.000 78.544  0 152 TYR B O   1 
ATOM   2459 C CB  . TYR B 1 152 ? 20.880  3.403   -14.775 1.000 72.849  0 152 TYR B CB  1 
ATOM   2460 C CG  . TYR B 1 152 ? 20.885  4.277   -16.017 1.000 73.315  0 152 TYR B CG  1 
ATOM   2461 C CD1 . TYR B 1 152 ? 20.061  4.020   -17.100 1.000 81.572  0 152 TYR B CD1 1 
ATOM   2462 C CD2 . TYR B 1 152 ? 21.698  5.407   -16.078 1.000 81.608  0 152 TYR B CD2 1 
ATOM   2463 C CE1 . TYR B 1 152 ? 20.037  4.867   -18.206 1.000 76.011  0 152 TYR B CE1 1 
ATOM   2464 C CE2 . TYR B 1 152 ? 21.690  6.252   -17.174 1.000 79.461  0 152 TYR B CE2 1 
ATOM   2465 C CZ  . TYR B 1 152 ? 20.863  5.981   -18.244 1.000 76.100  0 152 TYR B CZ  1 
ATOM   2466 O OH  . TYR B 1 152 ? 20.915  6.849   -19.293 1.000 74.415  0 152 TYR B OH  1 
ATOM   2467 N N   . GLU B 1 153 ? 22.110  1.164   -16.878 1.000 91.602  0 153 GLU B N   1 
ATOM   2468 C CA  . GLU B 1 153 ? 23.298  0.786   -17.626 1.000 98.527  0 153 GLU B CA  1 
ATOM   2469 C C   . GLU B 1 153 ? 23.674  2.028   -18.442 1.000 89.423  0 153 GLU B C   1 
ATOM   2470 O O   . GLU B 1 153 ? 23.432  2.088   -19.646 1.000 107.643 0 153 GLU B O   1 
ATOM   2471 C CB  . GLU B 1 153 ? 23.035  -0.543  -18.357 1.000 80.376  0 153 GLU B CB  1 
ATOM   2472 N N   . GLY B 1 154 ? 24.199  3.047   -17.749 1.000 79.174  0 154 GLY B N   1 
ATOM   2473 C CA  . GLY B 1 154 ? 24.471  4.350   -18.342 1.000 79.194  0 154 GLY B CA  1 
ATOM   2474 C C   . GLY B 1 154 ? 25.201  5.271   -17.366 1.000 70.322  0 154 GLY B C   1 
ATOM   2475 O O   . GLY B 1 154 ? 25.469  4.876   -16.245 1.000 64.664  0 154 GLY B O   1 
ATOM   2476 N N   . ALA B 1 155 ? 25.532  6.500   -17.777 1.000 73.353  0 155 ALA B N   1 
ATOM   2477 C CA  . ALA B 1 155 ? 26.378  7.349   -16.945 1.000 82.678  0 155 ALA B CA  1 
ATOM   2478 C C   . ALA B 1 155 ? 25.549  8.099   -15.903 1.000 90.542  0 155 ALA B C   1 
ATOM   2479 O O   . ALA B 1 155 ? 24.328  8.181   -16.041 1.000 79.345  0 155 ALA B O   1 
ATOM   2480 C CB  . ALA B 1 155 ? 27.156  8.305   -17.811 1.000 89.207  0 155 ALA B CB  1 
ATOM   2481 N N   . VAL B 1 156 ? 26.213  8.626   -14.856 1.000 83.667  0 156 VAL B N   1 
ATOM   2482 C CA  . VAL B 1 156 ? 25.543  9.431   -13.843 1.000 90.117  0 156 VAL B CA  1 
ATOM   2483 C C   . VAL B 1 156 ? 26.482  10.530  -13.334 1.000 84.788  0 156 VAL B C   1 
ATOM   2484 O O   . VAL B 1 156 ? 27.616  10.199  -13.003 1.000 82.212  0 156 VAL B O   1 
ATOM   2485 C CB  . VAL B 1 156 ? 25.012  8.528   -12.706 1.000 89.801  0 156 VAL B CB  1 
ATOM   2486 C CG1 . VAL B 1 156 ? 25.497  7.086   -12.804 1.000 96.595  0 156 VAL B CG1 1 
ATOM   2487 C CG2 . VAL B 1 156 ? 25.309  9.095   -11.333 1.000 90.401  0 156 VAL B CG2 1 
ATOM   2488 N N   . TYR B 1 157 ? 25.991  11.797  -13.223 1.000 81.794  0 157 TYR B N   1 
ATOM   2489 C CA  . TYR B 1 157 ? 26.762  12.957  -12.737 1.000 81.496  0 157 TYR B CA  1 
ATOM   2490 C C   . TYR B 1 157 ? 26.323  13.413  -11.272 1.000 87.881  0 157 TYR B C   1 
ATOM   2491 O O   . TYR B 1 157 ? 27.185  14.060  -10.655 1.000 91.629  0 157 TYR B O   1 
ATOM   2492 C CB  . TYR B 1 157 ? 26.715  14.156  -13.703 1.000 62.387  0 157 TYR B CB  1 
ATOM   2493 C CG  . TYR B 1 157 ? 25.314  14.729  -13.882 1.000 71.768  0 157 TYR B CG  1 
ATOM   2494 C CD1 . TYR B 1 157 ? 24.423  14.231  -14.831 1.000 71.727  0 157 TYR B CD1 1 
ATOM   2495 C CD2 . TYR B 1 157 ? 24.866  15.769  -13.074 1.000 79.700  0 157 TYR B CD2 1 
ATOM   2496 C CE1 . TYR B 1 157 ? 23.142  14.753  -14.960 1.000 71.285  0 157 TYR B CE1 1 
ATOM   2497 C CE2 . TYR B 1 157 ? 23.594  16.305  -13.196 1.000 75.585  0 157 TYR B CE2 1 
ATOM   2498 C CZ  . TYR B 1 157 ? 22.728  15.794  -14.142 1.000 76.049  0 157 TYR B CZ  1 
ATOM   2499 O OH  . TYR B 1 157 ? 21.459  16.303  -14.180 1.000 75.394  0 157 TYR B OH  1 
ATOM   2500 O OXT . TYR B 1 157 ? 25.210  13.157  -10.750 1.000 81.401  0 157 TYR B OXT 1 
HETATM 2501 O O   . HOH C 2 .   ? 30.529  25.655  -6.440  1.000 59.727  0 201 HOH A O   1 
HETATM 2502 O O   . HOH C 2 .   ? 20.941  33.107  18.642  1.000 68.830  0 202 HOH A O   1 
HETATM 2503 O O   . HOH C 2 .   ? 22.086  19.343  -3.971  1.000 63.758  0 203 HOH A O   1 
HETATM 2504 O O   . HOH C 2 .   ? 2.952   23.321  1.205   1.000 75.166  0 204 HOH A O   1 
HETATM 2505 O O   . HOH C 2 .   ? 21.707  17.649  -8.032  1.000 66.020  0 205 HOH A O   1 
HETATM 2506 O O   . HOH C 2 .   ? 5.513   28.197  -0.137  1.000 59.657  0 206 HOH A O   1 
HETATM 2507 O O   . HOH C 2 .   ? 1.443   21.253  -13.322 1.000 62.130  0 207 HOH A O   1 
HETATM 2508 O O   . HOH D 2 .   ? 6.675   18.738  -13.251 1.000 63.085  0 201 HOH B O   1 
HETATM 2509 O O   . HOH D 2 .   ? -4.917  21.196  2.434   1.000 57.236  0 202 HOH B O   1 
HETATM 2510 O O   . HOH D 2 .   ? 25.565  14.758  -7.486  1.000 51.509  0 203 HOH B O   1 
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