data_9B4R
# 
_entry.id   9B4R 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9B4R         pdb_00009b4r 10.2210/pdb9b4r/pdb 
WWPDB D_1000282588 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-22 
# 
_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                        9B4R 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              dhirendra.simanshu@nih.gov 
_pdbx_contact_author.name_first         Dhirendra 
_pdbx_contact_author.name_last          Simanshu 
_pdbx_contact_author.name_mi            K 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9717-4618 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Czyzyk, D.J.'   1 ? 
'Simanshu, D.K.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                525 
_citation.page_last                 525 
_citation.title                     
'Structural insights into isoform-specific RAS-PI3K alpha interactions and the role of RAS in PI3K alpha activation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-55766-x 
_citation.pdbx_database_id_PubMed   39788953 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Czyzyk, D.'     1  0000-0002-2398-5784 
primary 'Yan, W.'        2  ?                   
primary 'Messing, S.'    3  0000-0001-8991-2097 
primary 'Gillette, W.'   4  ?                   
primary 'Tsuji, T.'      5  ?                   
primary 'Yamaguchi, M.'  6  ?                   
primary 'Furuzono, S.'   7  ?                   
primary 'Turner, D.M.'   8  ?                   
primary 'Esposito, D.'   9  0000-0002-9987-1687 
primary 'Nissley, D.V.'  10 0000-0001-7523-116X 
primary 'McCormick, F.'  11 0000-0002-6619-7120 
primary 'Simanshu, D.K.' 12 0000-0002-9717-4618 
# 
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 'Ras-related protein M-Ras'                   19467.254 1   3.6.5.2 ? ? ? 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' 522.196   1   ?       ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                               24.305    1   ?       ? ? ? 
4 non-polymer syn 'ZINC ION'                                    65.409    2   ?       ? ? ? 
5 water       nat water                                         18.015    170 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Ras-related protein R-Ras3' 
# 
_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       
;GLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTAGQEEFSAMREQYMRTGDGFL
IVYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFH
DLVRVIRQQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTAGQEEFSAMREQYMRTGDGFL
IVYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFH
DLVRVIRQQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' GNP 
3 'MAGNESIUM ION'                               MG  
4 'ZINC ION'                                    ZN  
5 water                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   LEU n 
1 3   PRO n 
1 4   THR n 
1 5   TYR n 
1 6   LYS n 
1 7   LEU n 
1 8   VAL n 
1 9   VAL n 
1 10  VAL n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  GLY n 
1 15  VAL n 
1 16  GLY n 
1 17  LYS n 
1 18  SER n 
1 19  ALA n 
1 20  LEU n 
1 21  THR n 
1 22  ILE n 
1 23  GLN n 
1 24  PHE n 
1 25  PHE n 
1 26  GLN n 
1 27  LYS n 
1 28  ILE n 
1 29  PHE n 
1 30  VAL n 
1 31  PRO n 
1 32  ASP n 
1 33  TYR n 
1 34  ASP n 
1 35  PRO n 
1 36  THR n 
1 37  ILE n 
1 38  GLU n 
1 39  ASP n 
1 40  SER n 
1 41  TYR n 
1 42  LEU n 
1 43  LYS n 
1 44  HIS n 
1 45  THR n 
1 46  GLU n 
1 47  ILE n 
1 48  ASP n 
1 49  ASN n 
1 50  GLN n 
1 51  TRP n 
1 52  ALA n 
1 53  ILE n 
1 54  LEU n 
1 55  ASP n 
1 56  VAL n 
1 57  LEU n 
1 58  ASP n 
1 59  THR n 
1 60  ALA n 
1 61  GLY n 
1 62  GLN n 
1 63  GLU n 
1 64  GLU n 
1 65  PHE n 
1 66  SER n 
1 67  ALA n 
1 68  MET n 
1 69  ARG n 
1 70  GLU n 
1 71  GLN n 
1 72  TYR n 
1 73  MET n 
1 74  ARG n 
1 75  THR n 
1 76  GLY n 
1 77  ASP n 
1 78  GLY n 
1 79  PHE n 
1 80  LEU n 
1 81  ILE n 
1 82  VAL n 
1 83  TYR n 
1 84  SER n 
1 85  VAL n 
1 86  THR n 
1 87  ASP n 
1 88  LYS n 
1 89  ALA n 
1 90  SER n 
1 91  PHE n 
1 92  GLU n 
1 93  HIS n 
1 94  VAL n 
1 95  ASP n 
1 96  ARG n 
1 97  PHE n 
1 98  HIS n 
1 99  GLN n 
1 100 LEU n 
1 101 ILE n 
1 102 LEU n 
1 103 ARG n 
1 104 VAL n 
1 105 LYS n 
1 106 ASP n 
1 107 ARG n 
1 108 GLU n 
1 109 SER n 
1 110 PHE n 
1 111 PRO n 
1 112 MET n 
1 113 ILE n 
1 114 LEU n 
1 115 VAL n 
1 116 ALA n 
1 117 ASN n 
1 118 LYS n 
1 119 VAL n 
1 120 ASP n 
1 121 LEU n 
1 122 MET n 
1 123 HIS n 
1 124 LEU n 
1 125 ARG n 
1 126 LYS n 
1 127 ILE n 
1 128 THR n 
1 129 ARG n 
1 130 GLU n 
1 131 GLN n 
1 132 GLY n 
1 133 LYS n 
1 134 GLU n 
1 135 MET n 
1 136 ALA n 
1 137 THR n 
1 138 LYS n 
1 139 HIS n 
1 140 ASN n 
1 141 ILE n 
1 142 PRO n 
1 143 TYR n 
1 144 ILE n 
1 145 GLU n 
1 146 THR n 
1 147 SER n 
1 148 ALA n 
1 149 LYS n 
1 150 ASP n 
1 151 PRO n 
1 152 PRO n 
1 153 LEU n 
1 154 ASN n 
1 155 VAL n 
1 156 ASP n 
1 157 LYS n 
1 158 ALA n 
1 159 PHE n 
1 160 HIS n 
1 161 ASP n 
1 162 LEU n 
1 163 VAL n 
1 164 ARG n 
1 165 VAL n 
1 166 ILE n 
1 167 ARG n 
1 168 GLN n 
1 169 GLN 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                   169 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MRAS, RRAS3' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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  
GNP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' ? 'C10 H17 N6 O13 P3' 522.196 
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 
MG  non-polymer         . 'MAGNESIUM ION'                               ? 'Mg 2'              24.305  
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 
ZN  non-polymer         . 'ZINC ION'                                    ? 'Zn 2'              65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   10  10  GLY GLY A . n 
A 1 2   LEU 2   11  11  LEU LEU A . n 
A 1 3   PRO 3   12  12  PRO PRO A . n 
A 1 4   THR 4   13  13  THR THR A . n 
A 1 5   TYR 5   14  14  TYR TYR A . n 
A 1 6   LYS 6   15  15  LYS LYS A . n 
A 1 7   LEU 7   16  16  LEU LEU A . n 
A 1 8   VAL 8   17  17  VAL VAL A . n 
A 1 9   VAL 9   18  18  VAL VAL A . n 
A 1 10  VAL 10  19  19  VAL VAL A . n 
A 1 11  GLY 11  20  20  GLY GLY A . n 
A 1 12  ASP 12  21  21  ASP ASP A . n 
A 1 13  GLY 13  22  22  GLY GLY A . n 
A 1 14  GLY 14  23  23  GLY GLY A . n 
A 1 15  VAL 15  24  24  VAL VAL A . n 
A 1 16  GLY 16  25  25  GLY GLY A . n 
A 1 17  LYS 17  26  26  LYS LYS A . n 
A 1 18  SER 18  27  27  SER SER A . n 
A 1 19  ALA 19  28  28  ALA ALA A . n 
A 1 20  LEU 20  29  29  LEU LEU A . n 
A 1 21  THR 21  30  30  THR THR A . n 
A 1 22  ILE 22  31  31  ILE ILE A . n 
A 1 23  GLN 23  32  32  GLN GLN A . n 
A 1 24  PHE 24  33  33  PHE PHE A . n 
A 1 25  PHE 25  34  34  PHE PHE A . n 
A 1 26  GLN 26  35  35  GLN GLN A . n 
A 1 27  LYS 27  36  36  LYS LYS A . n 
A 1 28  ILE 28  37  37  ILE ILE A . n 
A 1 29  PHE 29  38  38  PHE PHE A . n 
A 1 30  VAL 30  39  39  VAL VAL A . n 
A 1 31  PRO 31  40  40  PRO PRO A . n 
A 1 32  ASP 32  41  ?   ?   ?   A . n 
A 1 33  TYR 33  42  ?   ?   ?   A . n 
A 1 34  ASP 34  43  ?   ?   ?   A . n 
A 1 35  PRO 35  44  ?   ?   ?   A . n 
A 1 36  THR 36  45  ?   ?   ?   A . n 
A 1 37  ILE 37  46  46  ILE ILE A . n 
A 1 38  GLU 38  47  47  GLU GLU A . n 
A 1 39  ASP 39  48  48  ASP ASP A . n 
A 1 40  SER 40  49  49  SER SER A . n 
A 1 41  TYR 41  50  50  TYR TYR A . n 
A 1 42  LEU 42  51  51  LEU LEU A . n 
A 1 43  LYS 43  52  52  LYS LYS A . n 
A 1 44  HIS 44  53  53  HIS HIS A . n 
A 1 45  THR 45  54  54  THR THR A . n 
A 1 46  GLU 46  55  55  GLU GLU A . n 
A 1 47  ILE 47  56  56  ILE ILE A . n 
A 1 48  ASP 48  57  57  ASP ASP A . n 
A 1 49  ASN 49  58  58  ASN ASN A . n 
A 1 50  GLN 50  59  59  GLN GLN A . n 
A 1 51  TRP 51  60  60  TRP TRP A . n 
A 1 52  ALA 52  61  61  ALA ALA A . n 
A 1 53  ILE 53  62  62  ILE ILE A . n 
A 1 54  LEU 54  63  63  LEU LEU A . n 
A 1 55  ASP 55  64  64  ASP ASP A . n 
A 1 56  VAL 56  65  65  VAL VAL A . n 
A 1 57  LEU 57  66  66  LEU LEU A . n 
A 1 58  ASP 58  67  67  ASP ASP A . n 
A 1 59  THR 59  68  68  THR THR A . n 
A 1 60  ALA 60  69  69  ALA ALA A . n 
A 1 61  GLY 61  70  70  GLY GLY A . n 
A 1 62  GLN 62  71  71  GLN GLN A . n 
A 1 63  GLU 63  72  72  GLU GLU A . n 
A 1 64  GLU 64  73  73  GLU GLU A . n 
A 1 65  PHE 65  74  74  PHE PHE A . n 
A 1 66  SER 66  75  75  SER SER A . n 
A 1 67  ALA 67  76  76  ALA ALA A . n 
A 1 68  MET 68  77  77  MET MET A . n 
A 1 69  ARG 69  78  78  ARG ARG A . n 
A 1 70  GLU 70  79  79  GLU GLU A . n 
A 1 71  GLN 71  80  80  GLN GLN A . n 
A 1 72  TYR 72  81  81  TYR TYR A . n 
A 1 73  MET 73  82  82  MET MET A . n 
A 1 74  ARG 74  83  83  ARG ARG A . n 
A 1 75  THR 75  84  84  THR THR A . n 
A 1 76  GLY 76  85  85  GLY GLY A . n 
A 1 77  ASP 77  86  86  ASP ASP A . n 
A 1 78  GLY 78  87  87  GLY GLY A . n 
A 1 79  PHE 79  88  88  PHE PHE A . n 
A 1 80  LEU 80  89  89  LEU LEU A . n 
A 1 81  ILE 81  90  90  ILE ILE A . n 
A 1 82  VAL 82  91  91  VAL VAL A . n 
A 1 83  TYR 83  92  92  TYR TYR A . n 
A 1 84  SER 84  93  93  SER SER A . n 
A 1 85  VAL 85  94  94  VAL VAL A . n 
A 1 86  THR 86  95  95  THR THR A . n 
A 1 87  ASP 87  96  96  ASP ASP A . n 
A 1 88  LYS 88  97  97  LYS LYS A . n 
A 1 89  ALA 89  98  98  ALA ALA A . n 
A 1 90  SER 90  99  99  SER SER A . n 
A 1 91  PHE 91  100 100 PHE PHE A . n 
A 1 92  GLU 92  101 101 GLU GLU A . n 
A 1 93  HIS 93  102 102 HIS HIS A . n 
A 1 94  VAL 94  103 103 VAL VAL A . n 
A 1 95  ASP 95  104 104 ASP ASP A . n 
A 1 96  ARG 96  105 105 ARG ARG A . n 
A 1 97  PHE 97  106 106 PHE PHE A . n 
A 1 98  HIS 98  107 107 HIS HIS A . n 
A 1 99  GLN 99  108 108 GLN GLN A . n 
A 1 100 LEU 100 109 109 LEU LEU A . n 
A 1 101 ILE 101 110 110 ILE ILE A . n 
A 1 102 LEU 102 111 111 LEU LEU A . n 
A 1 103 ARG 103 112 112 ARG ARG A . n 
A 1 104 VAL 104 113 113 VAL VAL A . n 
A 1 105 LYS 105 114 114 LYS LYS A . n 
A 1 106 ASP 106 115 115 ASP ASP A . n 
A 1 107 ARG 107 116 116 ARG ARG A . n 
A 1 108 GLU 108 117 117 GLU GLU A . n 
A 1 109 SER 109 118 118 SER SER A . n 
A 1 110 PHE 110 119 119 PHE PHE A . n 
A 1 111 PRO 111 120 120 PRO PRO A . n 
A 1 112 MET 112 121 121 MET MET A . n 
A 1 113 ILE 113 122 122 ILE ILE A . n 
A 1 114 LEU 114 123 123 LEU LEU A . n 
A 1 115 VAL 115 124 124 VAL VAL A . n 
A 1 116 ALA 116 125 125 ALA ALA A . n 
A 1 117 ASN 117 126 126 ASN ASN A . n 
A 1 118 LYS 118 127 127 LYS LYS A . n 
A 1 119 VAL 119 128 128 VAL VAL A . n 
A 1 120 ASP 120 129 129 ASP ASP A . n 
A 1 121 LEU 121 130 130 LEU LEU A . n 
A 1 122 MET 122 131 131 MET MET A . n 
A 1 123 HIS 123 132 132 HIS HIS A . n 
A 1 124 LEU 124 133 133 LEU LEU A . n 
A 1 125 ARG 125 134 134 ARG ARG A . n 
A 1 126 LYS 126 135 135 LYS LYS A . n 
A 1 127 ILE 127 136 136 ILE ILE A . n 
A 1 128 THR 128 137 137 THR THR A . n 
A 1 129 ARG 129 138 138 ARG ARG A . n 
A 1 130 GLU 130 139 139 GLU GLU A . n 
A 1 131 GLN 131 140 140 GLN GLN A . n 
A 1 132 GLY 132 141 141 GLY GLY A . n 
A 1 133 LYS 133 142 142 LYS LYS A . n 
A 1 134 GLU 134 143 143 GLU GLU A . n 
A 1 135 MET 135 144 144 MET MET A . n 
A 1 136 ALA 136 145 145 ALA ALA A . n 
A 1 137 THR 137 146 146 THR THR A . n 
A 1 138 LYS 138 147 147 LYS LYS A . n 
A 1 139 HIS 139 148 148 HIS HIS A . n 
A 1 140 ASN 140 149 149 ASN ASN A . n 
A 1 141 ILE 141 150 150 ILE ILE A . n 
A 1 142 PRO 142 151 151 PRO PRO A . n 
A 1 143 TYR 143 152 152 TYR TYR A . n 
A 1 144 ILE 144 153 153 ILE ILE A . n 
A 1 145 GLU 145 154 154 GLU GLU A . n 
A 1 146 THR 146 155 155 THR THR A . n 
A 1 147 SER 147 156 156 SER SER A . n 
A 1 148 ALA 148 157 157 ALA ALA A . n 
A 1 149 LYS 149 158 158 LYS LYS A . n 
A 1 150 ASP 150 159 159 ASP ASP A . n 
A 1 151 PRO 151 160 160 PRO PRO A . n 
A 1 152 PRO 152 161 161 PRO PRO A . n 
A 1 153 LEU 153 162 162 LEU LEU A . n 
A 1 154 ASN 154 163 163 ASN ASN A . n 
A 1 155 VAL 155 164 164 VAL VAL A . n 
A 1 156 ASP 156 165 165 ASP ASP A . n 
A 1 157 LYS 157 166 166 LYS LYS A . n 
A 1 158 ALA 158 167 167 ALA ALA A . n 
A 1 159 PHE 159 168 168 PHE PHE A . n 
A 1 160 HIS 160 169 169 HIS HIS A . n 
A 1 161 ASP 161 170 170 ASP ASP A . n 
A 1 162 LEU 162 171 171 LEU LEU A . n 
A 1 163 VAL 163 172 172 VAL VAL A . n 
A 1 164 ARG 164 173 173 ARG ARG A . n 
A 1 165 VAL 165 174 174 VAL VAL A . n 
A 1 166 ILE 166 175 175 ILE ILE A . n 
A 1 167 ARG 167 176 176 ARG ARG A . n 
A 1 168 GLN 168 177 177 GLN GLN A . n 
A 1 169 GLN 169 178 178 GLN GLN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        GNP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   GNP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 GNP 1   201 500 GNP GNP A . 
C 3 MG  1   202 1   MG  MG  A . 
D 4 ZN  1   203 1   ZN  ZN  A . 
E 4 ZN  1   204 2   ZN  ZN  A . 
F 5 HOH 1   301 169 HOH HOH A . 
F 5 HOH 2   302 170 HOH HOH A . 
F 5 HOH 3   303 164 HOH HOH A . 
F 5 HOH 4   304 52  HOH HOH A . 
F 5 HOH 5   305 93  HOH HOH A . 
F 5 HOH 6   306 161 HOH HOH A . 
F 5 HOH 7   307 27  HOH HOH A . 
F 5 HOH 8   308 163 HOH HOH A . 
F 5 HOH 9   309 3   HOH HOH A . 
F 5 HOH 10  310 127 HOH HOH A . 
F 5 HOH 11  311 166 HOH HOH A . 
F 5 HOH 12  312 11  HOH HOH A . 
F 5 HOH 13  313 165 HOH HOH A . 
F 5 HOH 14  314 29  HOH HOH A . 
F 5 HOH 15  315 159 HOH HOH A . 
F 5 HOH 16  316 65  HOH HOH A . 
F 5 HOH 17  317 14  HOH HOH A . 
F 5 HOH 18  318 21  HOH HOH A . 
F 5 HOH 19  319 40  HOH HOH A . 
F 5 HOH 20  320 160 HOH HOH A . 
F 5 HOH 21  321 18  HOH HOH A . 
F 5 HOH 22  322 92  HOH HOH A . 
F 5 HOH 23  323 53  HOH HOH A . 
F 5 HOH 24  324 61  HOH HOH A . 
F 5 HOH 25  325 66  HOH HOH A . 
F 5 HOH 26  326 55  HOH HOH A . 
F 5 HOH 27  327 7   HOH HOH A . 
F 5 HOH 28  328 74  HOH HOH A . 
F 5 HOH 29  329 30  HOH HOH A . 
F 5 HOH 30  330 152 HOH HOH A . 
F 5 HOH 31  331 42  HOH HOH A . 
F 5 HOH 32  332 31  HOH HOH A . 
F 5 HOH 33  333 86  HOH HOH A . 
F 5 HOH 34  334 25  HOH HOH A . 
F 5 HOH 35  335 72  HOH HOH A . 
F 5 HOH 36  336 24  HOH HOH A . 
F 5 HOH 37  337 94  HOH HOH A . 
F 5 HOH 38  338 15  HOH HOH A . 
F 5 HOH 39  339 63  HOH HOH A . 
F 5 HOH 40  340 73  HOH HOH A . 
F 5 HOH 41  341 6   HOH HOH A . 
F 5 HOH 42  342 149 HOH HOH A . 
F 5 HOH 43  343 19  HOH HOH A . 
F 5 HOH 44  344 13  HOH HOH A . 
F 5 HOH 45  345 79  HOH HOH A . 
F 5 HOH 46  346 50  HOH HOH A . 
F 5 HOH 47  347 8   HOH HOH A . 
F 5 HOH 48  348 77  HOH HOH A . 
F 5 HOH 49  349 113 HOH HOH A . 
F 5 HOH 50  350 100 HOH HOH A . 
F 5 HOH 51  351 20  HOH HOH A . 
F 5 HOH 52  352 41  HOH HOH A . 
F 5 HOH 53  353 67  HOH HOH A . 
F 5 HOH 54  354 4   HOH HOH A . 
F 5 HOH 55  355 58  HOH HOH A . 
F 5 HOH 56  356 49  HOH HOH A . 
F 5 HOH 57  357 5   HOH HOH A . 
F 5 HOH 58  358 56  HOH HOH A . 
F 5 HOH 59  359 134 HOH HOH A . 
F 5 HOH 60  360 9   HOH HOH A . 
F 5 HOH 61  361 35  HOH HOH A . 
F 5 HOH 62  362 46  HOH HOH A . 
F 5 HOH 63  363 126 HOH HOH A . 
F 5 HOH 64  364 75  HOH HOH A . 
F 5 HOH 65  365 32  HOH HOH A . 
F 5 HOH 66  366 23  HOH HOH A . 
F 5 HOH 67  367 12  HOH HOH A . 
F 5 HOH 68  368 57  HOH HOH A . 
F 5 HOH 69  369 44  HOH HOH A . 
F 5 HOH 70  370 36  HOH HOH A . 
F 5 HOH 71  371 47  HOH HOH A . 
F 5 HOH 72  372 62  HOH HOH A . 
F 5 HOH 73  373 59  HOH HOH A . 
F 5 HOH 74  374 68  HOH HOH A . 
F 5 HOH 75  375 83  HOH HOH A . 
F 5 HOH 76  376 98  HOH HOH A . 
F 5 HOH 77  377 37  HOH HOH A . 
F 5 HOH 78  378 102 HOH HOH A . 
F 5 HOH 79  379 26  HOH HOH A . 
F 5 HOH 80  380 16  HOH HOH A . 
F 5 HOH 81  381 96  HOH HOH A . 
F 5 HOH 82  382 48  HOH HOH A . 
F 5 HOH 83  383 80  HOH HOH A . 
F 5 HOH 84  384 137 HOH HOH A . 
F 5 HOH 85  385 107 HOH HOH A . 
F 5 HOH 86  386 45  HOH HOH A . 
F 5 HOH 87  387 85  HOH HOH A . 
F 5 HOH 88  388 71  HOH HOH A . 
F 5 HOH 89  389 10  HOH HOH A . 
F 5 HOH 90  390 76  HOH HOH A . 
F 5 HOH 91  391 54  HOH HOH A . 
F 5 HOH 92  392 120 HOH HOH A . 
F 5 HOH 93  393 64  HOH HOH A . 
F 5 HOH 94  394 38  HOH HOH A . 
F 5 HOH 95  395 51  HOH HOH A . 
F 5 HOH 96  396 70  HOH HOH A . 
F 5 HOH 97  397 60  HOH HOH A . 
F 5 HOH 98  398 33  HOH HOH A . 
F 5 HOH 99  399 171 HOH HOH A . 
F 5 HOH 100 400 123 HOH HOH A . 
F 5 HOH 101 401 115 HOH HOH A . 
F 5 HOH 102 402 99  HOH HOH A . 
F 5 HOH 103 403 95  HOH HOH A . 
F 5 HOH 104 404 81  HOH HOH A . 
F 5 HOH 105 405 139 HOH HOH A . 
F 5 HOH 106 406 121 HOH HOH A . 
F 5 HOH 107 407 158 HOH HOH A . 
F 5 HOH 108 408 141 HOH HOH A . 
F 5 HOH 109 409 176 HOH HOH A . 
F 5 HOH 110 410 116 HOH HOH A . 
F 5 HOH 111 411 117 HOH HOH A . 
F 5 HOH 112 412 39  HOH HOH A . 
F 5 HOH 113 413 84  HOH HOH A . 
F 5 HOH 114 414 119 HOH HOH A . 
F 5 HOH 115 415 34  HOH HOH A . 
F 5 HOH 116 416 105 HOH HOH A . 
F 5 HOH 117 417 1   HOH HOH A . 
F 5 HOH 118 418 108 HOH HOH A . 
F 5 HOH 119 419 2   HOH HOH A . 
F 5 HOH 120 420 114 HOH HOH A . 
F 5 HOH 121 421 132 HOH HOH A . 
F 5 HOH 122 422 97  HOH HOH A . 
F 5 HOH 123 423 104 HOH HOH A . 
F 5 HOH 124 424 138 HOH HOH A . 
F 5 HOH 125 425 143 HOH HOH A . 
F 5 HOH 126 426 78  HOH HOH A . 
F 5 HOH 127 427 177 HOH HOH A . 
F 5 HOH 128 428 156 HOH HOH A . 
F 5 HOH 129 429 69  HOH HOH A . 
F 5 HOH 130 430 122 HOH HOH A . 
F 5 HOH 131 431 135 HOH HOH A . 
F 5 HOH 132 432 87  HOH HOH A . 
F 5 HOH 133 433 175 HOH HOH A . 
F 5 HOH 134 434 157 HOH HOH A . 
F 5 HOH 135 435 111 HOH HOH A . 
F 5 HOH 136 436 89  HOH HOH A . 
F 5 HOH 137 437 136 HOH HOH A . 
F 5 HOH 138 438 133 HOH HOH A . 
F 5 HOH 139 439 118 HOH HOH A . 
F 5 HOH 140 440 91  HOH HOH A . 
F 5 HOH 141 441 154 HOH HOH A . 
F 5 HOH 142 442 168 HOH HOH A . 
F 5 HOH 143 443 144 HOH HOH A . 
F 5 HOH 144 444 128 HOH HOH A . 
F 5 HOH 145 445 22  HOH HOH A . 
F 5 HOH 146 446 125 HOH HOH A . 
F 5 HOH 147 447 145 HOH HOH A . 
F 5 HOH 148 448 110 HOH HOH A . 
F 5 HOH 149 449 155 HOH HOH A . 
F 5 HOH 150 450 101 HOH HOH A . 
F 5 HOH 151 451 140 HOH HOH A . 
F 5 HOH 152 452 146 HOH HOH A . 
F 5 HOH 153 453 112 HOH HOH A . 
F 5 HOH 154 454 148 HOH HOH A . 
F 5 HOH 155 455 17  HOH HOH A . 
F 5 HOH 156 456 103 HOH HOH A . 
F 5 HOH 157 457 28  HOH HOH A . 
F 5 HOH 158 458 167 HOH HOH A . 
F 5 HOH 159 459 172 HOH HOH A . 
F 5 HOH 160 460 90  HOH HOH A . 
F 5 HOH 161 461 88  HOH HOH A . 
F 5 HOH 162 462 131 HOH HOH A . 
F 5 HOH 163 463 142 HOH HOH A . 
F 5 HOH 164 464 150 HOH HOH A . 
F 5 HOH 165 465 130 HOH HOH A . 
F 5 HOH 166 466 147 HOH HOH A . 
F 5 HOH 167 467 43  HOH HOH A . 
F 5 HOH 168 468 174 HOH HOH A . 
F 5 HOH 169 469 153 HOH HOH A . 
F 5 HOH 170 470 124 HOH HOH A . 
# 
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 VAL 39 ? CG1 ? A VAL 30 CG1 
2  1 Y 1 A VAL 39 ? CG2 ? A VAL 30 CG2 
3  1 Y 1 A ILE 46 ? CG1 ? A ILE 37 CG1 
4  1 Y 1 A ILE 46 ? CG2 ? A ILE 37 CG2 
5  1 Y 1 A ILE 46 ? CD1 ? A ILE 37 CD1 
6  1 Y 1 A GLN 71 ? CG  ? A GLN 62 CG  
7  1 Y 1 A GLN 71 ? CD  ? A GLN 62 CD  
8  1 Y 1 A GLN 71 ? OE1 ? A GLN 62 OE1 
9  1 Y 1 A GLN 71 ? NE2 ? A GLN 62 NE2 
10 1 Y 1 A GLU 72 ? CG  ? A GLU 63 CG  
11 1 Y 1 A GLU 72 ? CD  ? A GLU 63 CD  
12 1 Y 1 A GLU 72 ? OE1 ? A GLU 63 OE1 
13 1 Y 1 A GLU 72 ? OE2 ? A GLU 63 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       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.21_5207: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9B4R 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     65.481 
_cell.length_a_esd                 ? 
_cell.length_b                     65.481 
_cell.length_b_esd                 ? 
_cell.length_c                     107.806 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9B4R 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                94 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 42 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9B4R 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.81 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56 
_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              7.4 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.002 M divalent II mix, 50%v/v(30%w/v PEG 3000, 40%v/v 1,2,4-butanetriol, and 2%w/v NDSB 256)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.19556 
_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                        'SSRL BEAMLINE BL14-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.19556 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL14-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9B4R 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1 
_reflns.d_resolution_low                               42.54 
_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                                     14328 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.17 
_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                                0.109 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9990000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.102 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.10 2.22  ? ? ? ? ? ? 2214 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.8059999999999999   ? ? 1 1 0.768              ? ? ? ? 0.747 ? ? ? ? ? 
? ? ? ? 
2.22 2.38  ? ? ? ? ? ? 2098 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.546                ? ? 2 1 0.9420000000000001 ? ? ? ? 0.513 ? ? ? ? ? 
? ? ? ? 
2.38 2.57  ? ? ? ? ? ? 2004 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.366                ? ? 3 1 0.9690000000000001 ? ? ? ? 
0.34299999999999997 ? ? ? ? ? ? ? ? ? 
2.57 2.81  ? ? ? ? ? ? 1849 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.239                ? ? 4 1 0.9840000000000001 ? ? ? ? 0.225 ? ? ? ? ? 
? ? ? ? 
2.81 3.14  ? ? ? ? ? ? 1680 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.14300000000000002  ? ? 5 1 0.993              ? ? ? ? 0.134 ? ? ? ? ? 
? ? ? ? 
3.14 3.62  ? ? ? ? ? ? 1512 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.08199999999999999  ? ? 6 1 0.998              ? ? ? ? 0.077 ? ? ? ? ? 
? ? ? ? 
3.62 4.43  ? ? ? ? ? ? 1290 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.055999999999999994 ? ? 7 1 0.998              ? ? ? ? 0.053 ? ? ? ? ? 
? ? ? ? 
4.43 6.24  ? ? ? ? ? ? 1034 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.05                 ? ? 8 1 0.9990000000000001 ? ? ? ? 0.047 ? ? ? ? ? 
? ? ? ? 
6.24 42.54 ? ? ? ? ? ? 647  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.040999999999999995 ? ? 9 1 0.9990000000000001 ? ? ? ? 0.038 ? ? ? ? ? 
? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9B4R 
_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                            2.10 
_refine.ls_d_res_low                             42.54 
_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                     14321 
_refine.ls_number_reflns_R_free                  716 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.51 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2015 
_refine.ls_R_factor_R_free                       0.2498 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1990 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.34 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.32 
_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                       2.10 
_refine_hist.d_res_low                        42.54 
_refine_hist.number_atoms_solvent             170 
_refine_hist.number_atoms_total               1521 
_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        1316 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_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' ? 0.003  ? 1376 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.533  ? 1865 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.072 ? 533  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.043  ? 207  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 234  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.10 2.26  . . 138 2618 98.00  . . . . 0.3111 . . . . . . . . . . . 0.3713 
'X-RAY DIFFRACTION' 2.26 2.49  . . 140 2661 100.00 . . . . 0.2320 . . . . . . . . . . . 0.2750 
'X-RAY DIFFRACTION' 2.49 2.84  . . 142 2705 100.00 . . . . 0.2210 . . . . . . . . . . . 0.2480 
'X-RAY DIFFRACTION' 2.85 3.58  . . 144 2726 100.00 . . . . 0.1823 . . . . . . . . . . . 0.2618 
'X-RAY DIFFRACTION' 3.58 42.54 . . 152 2895 100.00 . . . . 0.1747 . . . . . . . . . . . 0.2157 
# 
_struct.entry_id                     9B4R 
_struct.title                        'Crystal structure of MRAS bound to GMPPNP' 
_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        9B4R 
_struct_keywords.text            'RAS, RRAS3, MRAS, ONCOPROTEIN' 
_struct_keywords.pdbx_keywords   ONCOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RASM_HUMAN 
_struct_ref.pdbx_db_accession          O14807 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTAGQEEFSAMREQYMRTGDGFLI
VYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHD
LVRVIRQQ
;
_struct_ref.pdbx_align_begin           11 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9B4R 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 169 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O14807 
_struct_ref_seq.db_align_beg                  11 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  178 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       11 
_struct_ref_seq.pdbx_auth_seq_align_end       178 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9B4R 
_struct_ref_seq_dif.mon_id                       GLY 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   O14807 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'expression tag' 
_struct_ref_seq_dif.pdbx_auth_seq_num            10 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 16  ? LYS A 27  ? GLY A 25  LYS A 36  1 ? 12 
HELX_P HELX_P2 AA2 PHE A 65  ? THR A 75  ? PHE A 74  THR A 84  1 ? 11 
HELX_P HELX_P3 AA3 ASP A 87  ? HIS A 93  ? ASP A 96  HIS A 102 1 ? 7  
HELX_P HELX_P4 AA4 HIS A 93  ? ASP A 106 ? HIS A 102 ASP A 115 1 ? 14 
HELX_P HELX_P5 AA5 THR A 128 ? HIS A 139 ? THR A 137 HIS A 148 1 ? 12 
HELX_P HELX_P6 AA6 ASN A 154 ? GLN A 168 ? ASN A 163 GLN A 177 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A SER 18  OG  ? ? ? 1_555 C MG  . MG ? ? A SER 27  A MG  202 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
metalc2  metalc ? ? A ASP 39  OD2 ? ? ? 1_555 D ZN  . ZN ? ? A ASP 48  A ZN  203 5_545 ? ? ? ? ? ? ? 2.070 ? ? 
metalc3  metalc ? ? A HIS 44  ND1 ? ? ? 1_555 D ZN  . ZN ? ? A HIS 53  A ZN  203 6_445 ? ? ? ? ? ? ? 2.107 ? ? 
metalc4  metalc ? ? A HIS 98  ND1 ? ? ? 1_555 E ZN  . ZN ? ? A HIS 107 A ZN  204 1_555 ? ? ? ? ? ? ? 1.998 ? ? 
metalc5  metalc ? ? A GLU 108 OE2 ? ? ? 1_555 E ZN  . ZN ? ? A GLU 117 A ZN  204 8_555 ? ? ? ? ? ? ? 1.962 ? ? 
metalc6  metalc ? ? A HIS 123 NE2 ? ? ? 1_555 D ZN  . ZN ? ? A HIS 132 A ZN  203 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
metalc7  metalc ? ? A HIS 139 ND1 ? ? ? 1_555 E ZN  . ZN ? ? A HIS 148 A ZN  204 1_555 ? ? ? ? ? ? ? 2.193 ? ? 
metalc8  metalc ? ? B GNP .   O2G ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 1.913 ? ? 
metalc9  metalc ? ? B GNP .   O2B ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
metalc10 metalc ? ? C MG  .   MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 309 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc11 metalc ? ? C MG  .   MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 341 1_555 ? ? ? ? ? ? ? 1.963 ? ? 
metalc12 metalc ? ? C MG  .   MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 345 1_555 ? ? ? ? ? ? ? 1.930 ? ? 
metalc13 metalc ? ? D ZN  .   ZN  ? ? ? 1_555 F HOH . O  ? ? A ZN  203 A HOH 417 1_555 ? ? ? ? ? ? ? 2.235 ? ? 
metalc14 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F HOH . O  ? ? A ZN  204 A HOH 419 1_555 ? ? ? ? ? ? ? 2.207 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG  ? A SER 18  ? A SER 27  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O2G ? B GNP .   ? A GNP 201 ? 1_555 175.5 ? 
2  OG  ? A SER 18  ? A SER 27  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O2B ? B GNP .   ? A GNP 201 ? 1_555 90.0  ? 
3  O2G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O2B ? B GNP .   ? A GNP 201 ? 1_555 93.9  ? 
4  OG  ? A SER 18  ? A SER 27  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 309 ? 1_555 85.1  ? 
5  O2G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 309 ? 1_555 97.0  ? 
6  O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 309 ? 1_555 93.0  ? 
7  OG  ? A SER 18  ? A SER 27  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 341 ? 1_555 84.3  ? 
8  O2G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 341 ? 1_555 91.7  ? 
9  O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 341 ? 1_555 174.1 ? 
10 O   ? F HOH .   ? A HOH 309 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 341 ? 1_555 88.1  ? 
11 OG  ? A SER 18  ? A SER 27  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 345 ? 1_555 85.8  ? 
12 O2G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 345 ? 1_555 91.9  ? 
13 O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 345 ? 1_555 90.5  ? 
14 O   ? F HOH .   ? A HOH 309 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 345 ? 1_555 170.3 ? 
15 O   ? F HOH .   ? A HOH 341 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 345 ? 1_555 87.5  ? 
16 OD2 ? A ASP 39  ? A ASP 48  ? 1_555 ZN ? D ZN . ? A ZN 203 ? 5_545 ND1 ? A HIS 44  ? A HIS 53  ? 1_555 103.6 ? 
17 OD2 ? A ASP 39  ? A ASP 48  ? 1_555 ZN ? D ZN . ? A ZN 203 ? 5_545 NE2 ? A HIS 123 ? A HIS 132 ? 1_555 38.5  ? 
18 ND1 ? A HIS 44  ? A HIS 53  ? 1_555 ZN ? D ZN . ? A ZN 203 ? 5_545 NE2 ? A HIS 123 ? A HIS 132 ? 1_555 74.9  ? 
19 OD2 ? A ASP 39  ? A ASP 48  ? 1_555 ZN ? D ZN . ? A ZN 203 ? 5_545 O   ? F HOH .   ? A HOH 417 ? 1_555 40.4  ? 
20 ND1 ? A HIS 44  ? A HIS 53  ? 1_555 ZN ? D ZN . ? A ZN 203 ? 5_545 O   ? F HOH .   ? A HOH 417 ? 1_555 74.8  ? 
21 NE2 ? A HIS 123 ? A HIS 132 ? 1_555 ZN ? D ZN . ? A ZN 203 ? 5_545 O   ? F HOH .   ? A HOH 417 ? 1_555 2.6   ? 
22 ND1 ? A HIS 98  ? A HIS 107 ? 1_555 ZN ? E ZN . ? A ZN 204 ? 1_555 OE2 ? A GLU 108 ? A GLU 117 ? 1_555 92.3  ? 
23 ND1 ? A HIS 98  ? A HIS 107 ? 1_555 ZN ? E ZN . ? A ZN 204 ? 1_555 ND1 ? A HIS 139 ? A HIS 148 ? 1_555 103.2 ? 
24 OE2 ? A GLU 108 ? A GLU 117 ? 1_555 ZN ? E ZN . ? A ZN 204 ? 1_555 ND1 ? A HIS 139 ? A HIS 148 ? 1_555 147.4 ? 
25 ND1 ? A HIS 98  ? A HIS 107 ? 1_555 ZN ? E ZN . ? A ZN 204 ? 1_555 O   ? F HOH .   ? A HOH 419 ? 1_555 112.1 ? 
26 OE2 ? A GLU 108 ? A GLU 117 ? 1_555 ZN ? E ZN . ? A ZN 204 ? 1_555 O   ? F HOH .   ? A HOH 419 ? 1_555 85.8  ? 
27 ND1 ? A HIS 139 ? A HIS 148 ? 1_555 ZN ? E ZN . ? A ZN 204 ? 1_555 O   ? F HOH .   ? A HOH 419 ? 1_555 113.5 ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ASP 
_struct_mon_prot_cis.label_seq_id           150 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ASP 
_struct_mon_prot_cis.auth_seq_id            159 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    151 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     160 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.09 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   6 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? 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 TYR A 41  ? ILE A 47  ? TYR A 50  ILE A 56  
AA1 2 GLN A 50  ? ASP A 58  ? GLN A 59  ASP A 67  
AA1 3 THR A 4   ? GLY A 11  ? THR A 13  GLY A 20  
AA1 4 GLY A 78  ? SER A 84  ? GLY A 87  SER A 93  
AA1 5 MET A 112 ? ASN A 117 ? MET A 121 ASN A 126 
AA1 6 TYR A 143 ? GLU A 145 ? TYR A 152 GLU A 154 
# 
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 TYR A 41  ? N TYR A 50  O VAL A 56  ? O VAL A 65  
AA1 2 3 O LEU A 57  ? O LEU A 66  N LEU A 7   ? N LEU A 16  
AA1 3 4 N VAL A 10  ? N VAL A 19  O VAL A 82  ? O VAL A 91  
AA1 4 5 N ILE A 81  ? N ILE A 90  O VAL A 115 ? O VAL A 124 
AA1 5 6 N ALA A 116 ? N ALA A 125 O ILE A 144 ? O ILE A 153 
# 
_pdbx_entry_details.entry_id                   9B4R 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    351 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    426 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    GLU 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     73 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             55.33 
_pdbx_validate_torsion.psi             -160.42 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 374 ? F HOH . 
2 1 A HOH 434 ? F HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         17.3125 
_pdbx_refine_tls.origin_y         -25.0908 
_pdbx_refine_tls.origin_z         16.6752 
_pdbx_refine_tls.T[1][1]          0.1853 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0235 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0072 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2295 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0003 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2194 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          3.9109 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          1.3636 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          1.0224 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.1453 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.6033 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.7473 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0021 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.2315 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0114 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0885 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0116 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.1349 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0272 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1694 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0157 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 467 ? .    6.21 
2 1 O ? A HOH 468 ? 6.72 .    
3 1 O ? A HOH 469 ? 7.40 .    
4 1 O ? A HOH 470 ? 8.10 .    
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ASP 41 ? A ASP 32 
2 1 Y 1 A TYR 42 ? A TYR 33 
3 1 Y 1 A ASP 43 ? A ASP 34 
4 1 Y 1 A PRO 44 ? A PRO 35 
5 1 Y 1 A THR 45 ? A THR 36 
6 1 Y 0 A GLU 72 ? A GLU 63 
# 
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 
GNP PG     P  N N 123 
GNP O1G    O  N N 124 
GNP O2G    O  N N 125 
GNP O3G    O  N N 126 
GNP N3B    N  N N 127 
GNP PB     P  N R 128 
GNP O1B    O  N N 129 
GNP O2B    O  N N 130 
GNP O3A    O  N N 131 
GNP PA     P  N S 132 
GNP O1A    O  N N 133 
GNP O2A    O  N N 134 
GNP "O5'"  O  N N 135 
GNP "C5'"  C  N N 136 
GNP "C4'"  C  N R 137 
GNP "O4'"  O  N N 138 
GNP "C3'"  C  N S 139 
GNP "O3'"  O  N N 140 
GNP "C2'"  C  N R 141 
GNP "O2'"  O  N N 142 
GNP "C1'"  C  N R 143 
GNP N9     N  Y N 144 
GNP C8     C  Y N 145 
GNP N7     N  Y N 146 
GNP C5     C  Y N 147 
GNP C6     C  Y N 148 
GNP O6     O  N N 149 
GNP N1     N  Y N 150 
GNP C2     C  Y N 151 
GNP N2     N  N N 152 
GNP N3     N  Y N 153 
GNP C4     C  Y N 154 
GNP HOG2   H  N N 155 
GNP HOG3   H  N N 156 
GNP HNB3   H  N N 157 
GNP HOB2   H  N N 158 
GNP HOA2   H  N N 159 
GNP "H5'2" H  N N 160 
GNP "H5'1" H  N N 161 
GNP "H4'"  H  N N 162 
GNP "H3'"  H  N N 163 
GNP "HO3'" H  N N 164 
GNP "H2'"  H  N N 165 
GNP "HO2'" H  N N 166 
GNP "H1'"  H  N N 167 
GNP H8     H  N N 168 
GNP HN1    H  N N 169 
GNP HN21   H  N N 170 
GNP HN22   H  N N 171 
HIS N      N  N N 172 
HIS CA     C  N S 173 
HIS C      C  N N 174 
HIS O      O  N N 175 
HIS CB     C  N N 176 
HIS CG     C  Y N 177 
HIS ND1    N  Y N 178 
HIS CD2    C  Y N 179 
HIS CE1    C  Y N 180 
HIS NE2    N  Y N 181 
HIS OXT    O  N N 182 
HIS H      H  N N 183 
HIS H2     H  N N 184 
HIS HA     H  N N 185 
HIS HB2    H  N N 186 
HIS HB3    H  N N 187 
HIS HD1    H  N N 188 
HIS HD2    H  N N 189 
HIS HE1    H  N N 190 
HIS HE2    H  N N 191 
HIS HXT    H  N N 192 
HOH O      O  N N 193 
HOH H1     H  N N 194 
HOH H2     H  N N 195 
ILE N      N  N N 196 
ILE CA     C  N S 197 
ILE C      C  N N 198 
ILE O      O  N N 199 
ILE CB     C  N S 200 
ILE CG1    C  N N 201 
ILE CG2    C  N N 202 
ILE CD1    C  N N 203 
ILE OXT    O  N N 204 
ILE H      H  N N 205 
ILE H2     H  N N 206 
ILE HA     H  N N 207 
ILE HB     H  N N 208 
ILE HG12   H  N N 209 
ILE HG13   H  N N 210 
ILE HG21   H  N N 211 
ILE HG22   H  N N 212 
ILE HG23   H  N N 213 
ILE HD11   H  N N 214 
ILE HD12   H  N N 215 
ILE HD13   H  N N 216 
ILE HXT    H  N N 217 
LEU N      N  N N 218 
LEU CA     C  N S 219 
LEU C      C  N N 220 
LEU O      O  N N 221 
LEU CB     C  N N 222 
LEU CG     C  N N 223 
LEU CD1    C  N N 224 
LEU CD2    C  N N 225 
LEU OXT    O  N N 226 
LEU H      H  N N 227 
LEU H2     H  N N 228 
LEU HA     H  N N 229 
LEU HB2    H  N N 230 
LEU HB3    H  N N 231 
LEU HG     H  N N 232 
LEU HD11   H  N N 233 
LEU HD12   H  N N 234 
LEU HD13   H  N N 235 
LEU HD21   H  N N 236 
LEU HD22   H  N N 237 
LEU HD23   H  N N 238 
LEU HXT    H  N N 239 
LYS N      N  N N 240 
LYS CA     C  N S 241 
LYS C      C  N N 242 
LYS O      O  N N 243 
LYS CB     C  N N 244 
LYS CG     C  N N 245 
LYS CD     C  N N 246 
LYS CE     C  N N 247 
LYS NZ     N  N N 248 
LYS OXT    O  N N 249 
LYS H      H  N N 250 
LYS H2     H  N N 251 
LYS HA     H  N N 252 
LYS HB2    H  N N 253 
LYS HB3    H  N N 254 
LYS HG2    H  N N 255 
LYS HG3    H  N N 256 
LYS HD2    H  N N 257 
LYS HD3    H  N N 258 
LYS HE2    H  N N 259 
LYS HE3    H  N N 260 
LYS HZ1    H  N N 261 
LYS HZ2    H  N N 262 
LYS HZ3    H  N N 263 
LYS HXT    H  N N 264 
MET N      N  N N 265 
MET CA     C  N S 266 
MET C      C  N N 267 
MET O      O  N N 268 
MET CB     C  N N 269 
MET CG     C  N N 270 
MET SD     S  N N 271 
MET CE     C  N N 272 
MET OXT    O  N N 273 
MET H      H  N N 274 
MET H2     H  N N 275 
MET HA     H  N N 276 
MET HB2    H  N N 277 
MET HB3    H  N N 278 
MET HG2    H  N N 279 
MET HG3    H  N N 280 
MET HE1    H  N N 281 
MET HE2    H  N N 282 
MET HE3    H  N N 283 
MET HXT    H  N N 284 
MG  MG     MG N N 285 
PHE N      N  N N 286 
PHE CA     C  N S 287 
PHE C      C  N N 288 
PHE O      O  N N 289 
PHE CB     C  N N 290 
PHE CG     C  Y N 291 
PHE CD1    C  Y N 292 
PHE CD2    C  Y N 293 
PHE CE1    C  Y N 294 
PHE CE2    C  Y N 295 
PHE CZ     C  Y N 296 
PHE OXT    O  N N 297 
PHE H      H  N N 298 
PHE H2     H  N N 299 
PHE HA     H  N N 300 
PHE HB2    H  N N 301 
PHE HB3    H  N N 302 
PHE HD1    H  N N 303 
PHE HD2    H  N N 304 
PHE HE1    H  N N 305 
PHE HE2    H  N N 306 
PHE HZ     H  N N 307 
PHE HXT    H  N N 308 
PRO N      N  N N 309 
PRO CA     C  N S 310 
PRO C      C  N N 311 
PRO O      O  N N 312 
PRO CB     C  N N 313 
PRO CG     C  N N 314 
PRO CD     C  N N 315 
PRO OXT    O  N N 316 
PRO H      H  N N 317 
PRO HA     H  N N 318 
PRO HB2    H  N N 319 
PRO HB3    H  N N 320 
PRO HG2    H  N N 321 
PRO HG3    H  N N 322 
PRO HD2    H  N N 323 
PRO HD3    H  N N 324 
PRO HXT    H  N N 325 
SER N      N  N N 326 
SER CA     C  N S 327 
SER C      C  N N 328 
SER O      O  N N 329 
SER CB     C  N N 330 
SER OG     O  N N 331 
SER OXT    O  N N 332 
SER H      H  N N 333 
SER H2     H  N N 334 
SER HA     H  N N 335 
SER HB2    H  N N 336 
SER HB3    H  N N 337 
SER HG     H  N N 338 
SER HXT    H  N N 339 
THR N      N  N N 340 
THR CA     C  N S 341 
THR C      C  N N 342 
THR O      O  N N 343 
THR CB     C  N R 344 
THR OG1    O  N N 345 
THR CG2    C  N N 346 
THR OXT    O  N N 347 
THR H      H  N N 348 
THR H2     H  N N 349 
THR HA     H  N N 350 
THR HB     H  N N 351 
THR HG1    H  N N 352 
THR HG21   H  N N 353 
THR HG22   H  N N 354 
THR HG23   H  N N 355 
THR HXT    H  N N 356 
TRP N      N  N N 357 
TRP CA     C  N S 358 
TRP C      C  N N 359 
TRP O      O  N N 360 
TRP CB     C  N N 361 
TRP CG     C  Y N 362 
TRP CD1    C  Y N 363 
TRP CD2    C  Y N 364 
TRP NE1    N  Y N 365 
TRP CE2    C  Y N 366 
TRP CE3    C  Y N 367 
TRP CZ2    C  Y N 368 
TRP CZ3    C  Y N 369 
TRP CH2    C  Y N 370 
TRP OXT    O  N N 371 
TRP H      H  N N 372 
TRP H2     H  N N 373 
TRP HA     H  N N 374 
TRP HB2    H  N N 375 
TRP HB3    H  N N 376 
TRP HD1    H  N N 377 
TRP HE1    H  N N 378 
TRP HE3    H  N N 379 
TRP HZ2    H  N N 380 
TRP HZ3    H  N N 381 
TRP HH2    H  N N 382 
TRP HXT    H  N N 383 
TYR N      N  N N 384 
TYR CA     C  N S 385 
TYR C      C  N N 386 
TYR O      O  N N 387 
TYR CB     C  N N 388 
TYR CG     C  Y N 389 
TYR CD1    C  Y N 390 
TYR CD2    C  Y N 391 
TYR CE1    C  Y N 392 
TYR CE2    C  Y N 393 
TYR CZ     C  Y N 394 
TYR OH     O  N N 395 
TYR OXT    O  N N 396 
TYR H      H  N N 397 
TYR H2     H  N N 398 
TYR HA     H  N N 399 
TYR HB2    H  N N 400 
TYR HB3    H  N N 401 
TYR HD1    H  N N 402 
TYR HD2    H  N N 403 
TYR HE1    H  N N 404 
TYR HE2    H  N N 405 
TYR HH     H  N N 406 
TYR HXT    H  N N 407 
VAL N      N  N N 408 
VAL CA     C  N S 409 
VAL C      C  N N 410 
VAL O      O  N N 411 
VAL CB     C  N N 412 
VAL CG1    C  N N 413 
VAL CG2    C  N N 414 
VAL OXT    O  N N 415 
VAL H      H  N N 416 
VAL H2     H  N N 417 
VAL HA     H  N N 418 
VAL HB     H  N N 419 
VAL HG11   H  N N 420 
VAL HG12   H  N N 421 
VAL HG13   H  N N 422 
VAL HG21   H  N N 423 
VAL HG22   H  N N 424 
VAL HG23   H  N N 425 
VAL HXT    H  N N 426 
ZN  ZN     ZN N N 427 
# 
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 
GNP PG    O1G    doub N N 116 
GNP PG    O2G    sing N N 117 
GNP PG    O3G    sing N N 118 
GNP PG    N3B    sing N N 119 
GNP O2G   HOG2   sing N N 120 
GNP O3G   HOG3   sing N N 121 
GNP N3B   PB     sing N N 122 
GNP N3B   HNB3   sing N N 123 
GNP PB    O1B    doub N N 124 
GNP PB    O2B    sing N N 125 
GNP PB    O3A    sing N N 126 
GNP O2B   HOB2   sing N N 127 
GNP O3A   PA     sing N N 128 
GNP PA    O1A    doub N N 129 
GNP PA    O2A    sing N N 130 
GNP PA    "O5'"  sing N N 131 
GNP O2A   HOA2   sing N N 132 
GNP "O5'" "C5'"  sing N N 133 
GNP "C5'" "C4'"  sing N N 134 
GNP "C5'" "H5'2" sing N N 135 
GNP "C5'" "H5'1" sing N N 136 
GNP "C4'" "O4'"  sing N N 137 
GNP "C4'" "C3'"  sing N N 138 
GNP "C4'" "H4'"  sing N N 139 
GNP "O4'" "C1'"  sing N N 140 
GNP "C3'" "O3'"  sing N N 141 
GNP "C3'" "C2'"  sing N N 142 
GNP "C3'" "H3'"  sing N N 143 
GNP "O3'" "HO3'" sing N N 144 
GNP "C2'" "O2'"  sing N N 145 
GNP "C2'" "C1'"  sing N N 146 
GNP "C2'" "H2'"  sing N N 147 
GNP "O2'" "HO2'" sing N N 148 
GNP "C1'" N9     sing N N 149 
GNP "C1'" "H1'"  sing N N 150 
GNP N9    C8     sing Y N 151 
GNP N9    C4     sing Y N 152 
GNP C8    N7     doub Y N 153 
GNP C8    H8     sing N N 154 
GNP N7    C5     sing Y N 155 
GNP C5    C6     sing Y N 156 
GNP C5    C4     doub Y N 157 
GNP C6    O6     doub N N 158 
GNP C6    N1     sing Y N 159 
GNP N1    C2     sing Y N 160 
GNP N1    HN1    sing N N 161 
GNP C2    N2     sing N N 162 
GNP C2    N3     doub Y N 163 
GNP N2    HN21   sing N N 164 
GNP N2    HN22   sing N N 165 
GNP N3    C4     sing Y N 166 
HIS N     CA     sing N N 167 
HIS N     H      sing N N 168 
HIS N     H2     sing N N 169 
HIS CA    C      sing N N 170 
HIS CA    CB     sing N N 171 
HIS CA    HA     sing N N 172 
HIS C     O      doub N N 173 
HIS C     OXT    sing N N 174 
HIS CB    CG     sing N N 175 
HIS CB    HB2    sing N N 176 
HIS CB    HB3    sing N N 177 
HIS CG    ND1    sing Y N 178 
HIS CG    CD2    doub Y N 179 
HIS ND1   CE1    doub Y N 180 
HIS ND1   HD1    sing N N 181 
HIS CD2   NE2    sing Y N 182 
HIS CD2   HD2    sing N N 183 
HIS CE1   NE2    sing Y N 184 
HIS CE1   HE1    sing N N 185 
HIS NE2   HE2    sing N N 186 
HIS OXT   HXT    sing N N 187 
HOH O     H1     sing N N 188 
HOH O     H2     sing N N 189 
ILE N     CA     sing N N 190 
ILE N     H      sing N N 191 
ILE N     H2     sing N N 192 
ILE CA    C      sing N N 193 
ILE CA    CB     sing N N 194 
ILE CA    HA     sing N N 195 
ILE C     O      doub N N 196 
ILE C     OXT    sing N N 197 
ILE CB    CG1    sing N N 198 
ILE CB    CG2    sing N N 199 
ILE CB    HB     sing N N 200 
ILE CG1   CD1    sing N N 201 
ILE CG1   HG12   sing N N 202 
ILE CG1   HG13   sing N N 203 
ILE CG2   HG21   sing N N 204 
ILE CG2   HG22   sing N N 205 
ILE CG2   HG23   sing N N 206 
ILE CD1   HD11   sing N N 207 
ILE CD1   HD12   sing N N 208 
ILE CD1   HD13   sing N N 209 
ILE OXT   HXT    sing N N 210 
LEU N     CA     sing N N 211 
LEU N     H      sing N N 212 
LEU N     H2     sing N N 213 
LEU CA    C      sing N N 214 
LEU CA    CB     sing N N 215 
LEU CA    HA     sing N N 216 
LEU C     O      doub N N 217 
LEU C     OXT    sing N N 218 
LEU CB    CG     sing N N 219 
LEU CB    HB2    sing N N 220 
LEU CB    HB3    sing N N 221 
LEU CG    CD1    sing N N 222 
LEU CG    CD2    sing N N 223 
LEU CG    HG     sing N N 224 
LEU CD1   HD11   sing N N 225 
LEU CD1   HD12   sing N N 226 
LEU CD1   HD13   sing N N 227 
LEU CD2   HD21   sing N N 228 
LEU CD2   HD22   sing N N 229 
LEU CD2   HD23   sing N N 230 
LEU OXT   HXT    sing N N 231 
LYS N     CA     sing N N 232 
LYS N     H      sing N N 233 
LYS N     H2     sing N N 234 
LYS CA    C      sing N N 235 
LYS CA    CB     sing N N 236 
LYS CA    HA     sing N N 237 
LYS C     O      doub N N 238 
LYS C     OXT    sing N N 239 
LYS CB    CG     sing N N 240 
LYS CB    HB2    sing N N 241 
LYS CB    HB3    sing N N 242 
LYS CG    CD     sing N N 243 
LYS CG    HG2    sing N N 244 
LYS CG    HG3    sing N N 245 
LYS CD    CE     sing N N 246 
LYS CD    HD2    sing N N 247 
LYS CD    HD3    sing N N 248 
LYS CE    NZ     sing N N 249 
LYS CE    HE2    sing N N 250 
LYS CE    HE3    sing N N 251 
LYS NZ    HZ1    sing N N 252 
LYS NZ    HZ2    sing N N 253 
LYS NZ    HZ3    sing N N 254 
LYS OXT   HXT    sing N N 255 
MET N     CA     sing N N 256 
MET N     H      sing N N 257 
MET N     H2     sing N N 258 
MET CA    C      sing N N 259 
MET CA    CB     sing N N 260 
MET CA    HA     sing N N 261 
MET C     O      doub N N 262 
MET C     OXT    sing N N 263 
MET CB    CG     sing N N 264 
MET CB    HB2    sing N N 265 
MET CB    HB3    sing N N 266 
MET CG    SD     sing N N 267 
MET CG    HG2    sing N N 268 
MET CG    HG3    sing N N 269 
MET SD    CE     sing N N 270 
MET CE    HE1    sing N N 271 
MET CE    HE2    sing N N 272 
MET CE    HE3    sing N N 273 
MET OXT   HXT    sing N N 274 
PHE N     CA     sing N N 275 
PHE N     H      sing N N 276 
PHE N     H2     sing N N 277 
PHE CA    C      sing N N 278 
PHE CA    CB     sing N N 279 
PHE CA    HA     sing N N 280 
PHE C     O      doub N N 281 
PHE C     OXT    sing N N 282 
PHE CB    CG     sing N N 283 
PHE CB    HB2    sing N N 284 
PHE CB    HB3    sing N N 285 
PHE CG    CD1    doub Y N 286 
PHE CG    CD2    sing Y N 287 
PHE CD1   CE1    sing Y N 288 
PHE CD1   HD1    sing N N 289 
PHE CD2   CE2    doub Y N 290 
PHE CD2   HD2    sing N N 291 
PHE CE1   CZ     doub Y N 292 
PHE CE1   HE1    sing N N 293 
PHE CE2   CZ     sing Y N 294 
PHE CE2   HE2    sing N N 295 
PHE CZ    HZ     sing N N 296 
PHE OXT   HXT    sing N N 297 
PRO N     CA     sing N N 298 
PRO N     CD     sing N N 299 
PRO N     H      sing N N 300 
PRO CA    C      sing N N 301 
PRO CA    CB     sing N N 302 
PRO CA    HA     sing N N 303 
PRO C     O      doub N N 304 
PRO C     OXT    sing N N 305 
PRO CB    CG     sing N N 306 
PRO CB    HB2    sing N N 307 
PRO CB    HB3    sing N N 308 
PRO CG    CD     sing N N 309 
PRO CG    HG2    sing N N 310 
PRO CG    HG3    sing N N 311 
PRO CD    HD2    sing N N 312 
PRO CD    HD3    sing N N 313 
PRO OXT   HXT    sing N N 314 
SER N     CA     sing N N 315 
SER N     H      sing N N 316 
SER N     H2     sing N N 317 
SER CA    C      sing N N 318 
SER CA    CB     sing N N 319 
SER CA    HA     sing N N 320 
SER C     O      doub N N 321 
SER C     OXT    sing N N 322 
SER CB    OG     sing N N 323 
SER CB    HB2    sing N N 324 
SER CB    HB3    sing N N 325 
SER OG    HG     sing N N 326 
SER OXT   HXT    sing N N 327 
THR N     CA     sing N N 328 
THR N     H      sing N N 329 
THR N     H2     sing N N 330 
THR CA    C      sing N N 331 
THR CA    CB     sing N N 332 
THR CA    HA     sing N N 333 
THR C     O      doub N N 334 
THR C     OXT    sing N N 335 
THR CB    OG1    sing N N 336 
THR CB    CG2    sing N N 337 
THR CB    HB     sing N N 338 
THR OG1   HG1    sing N N 339 
THR CG2   HG21   sing N N 340 
THR CG2   HG22   sing N N 341 
THR CG2   HG23   sing N N 342 
THR OXT   HXT    sing N N 343 
TRP N     CA     sing N N 344 
TRP N     H      sing N N 345 
TRP N     H2     sing N N 346 
TRP CA    C      sing N N 347 
TRP CA    CB     sing N N 348 
TRP CA    HA     sing N N 349 
TRP C     O      doub N N 350 
TRP C     OXT    sing N N 351 
TRP CB    CG     sing N N 352 
TRP CB    HB2    sing N N 353 
TRP CB    HB3    sing N N 354 
TRP CG    CD1    doub Y N 355 
TRP CG    CD2    sing Y N 356 
TRP CD1   NE1    sing Y N 357 
TRP CD1   HD1    sing N N 358 
TRP CD2   CE2    doub Y N 359 
TRP CD2   CE3    sing Y N 360 
TRP NE1   CE2    sing Y N 361 
TRP NE1   HE1    sing N N 362 
TRP CE2   CZ2    sing Y N 363 
TRP CE3   CZ3    doub Y N 364 
TRP CE3   HE3    sing N N 365 
TRP CZ2   CH2    doub Y N 366 
TRP CZ2   HZ2    sing N N 367 
TRP CZ3   CH2    sing Y N 368 
TRP CZ3   HZ3    sing N N 369 
TRP CH2   HH2    sing N N 370 
TRP OXT   HXT    sing N N 371 
TYR N     CA     sing N N 372 
TYR N     H      sing N N 373 
TYR N     H2     sing N N 374 
TYR CA    C      sing N N 375 
TYR CA    CB     sing N N 376 
TYR CA    HA     sing N N 377 
TYR C     O      doub N N 378 
TYR C     OXT    sing N N 379 
TYR CB    CG     sing N N 380 
TYR CB    HB2    sing N N 381 
TYR CB    HB3    sing N N 382 
TYR CG    CD1    doub Y N 383 
TYR CG    CD2    sing Y N 384 
TYR CD1   CE1    sing Y N 385 
TYR CD1   HD1    sing N N 386 
TYR CD2   CE2    doub Y N 387 
TYR CD2   HD2    sing N N 388 
TYR CE1   CZ     doub Y N 389 
TYR CE1   HE1    sing N N 390 
TYR CE2   CZ     sing Y N 391 
TYR CE2   HE2    sing N N 392 
TYR CZ    OH     sing N N 393 
TYR OH    HH     sing N N 394 
TYR OXT   HXT    sing N N 395 
VAL N     CA     sing N N 396 
VAL N     H      sing N N 397 
VAL N     H2     sing N N 398 
VAL CA    C      sing N N 399 
VAL CA    CB     sing N N 400 
VAL CA    HA     sing N N 401 
VAL C     O      doub N N 402 
VAL C     OXT    sing N N 403 
VAL CB    CG1    sing N N 404 
VAL CB    CG2    sing N N 405 
VAL CB    HB     sing N N 406 
VAL CG1   HG11   sing N N 407 
VAL CG1   HG12   sing N N 408 
VAL CG1   HG13   sing N N 409 
VAL CG2   HG21   sing N N 410 
VAL CG2   HG22   sing N N 411 
VAL CG2   HG23   sing N N 412 
VAL OXT   HXT    sing N N 413 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Cancer Institute (NIH/NCI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           75N91019D00024 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   7TVF 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    9B4R 
_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]   0.015272 
_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]   0.015272 
_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]   0.009276 
_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  
MG 
N  
O  
P  
S  
ZN 
# 
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     . GLY A 1 1   ? -5.727 -32.526 7.891  1.00 28.43 ? 10  GLY A N     1 
ATOM   2    C  CA    . GLY A 1 1   ? -5.659 -31.550 8.961  1.00 27.78 ? 10  GLY A CA    1 
ATOM   3    C  C     . GLY A 1 1   ? -4.727 -30.389 8.674  1.00 27.86 ? 10  GLY A C     1 
ATOM   4    O  O     . GLY A 1 1   ? -4.366 -30.131 7.527  1.00 29.35 ? 10  GLY A O     1 
ATOM   5    N  N     . LEU A 1 2   ? -4.339 -29.684 9.732  1.00 29.53 ? 11  LEU A N     1 
ATOM   6    C  CA    . LEU A 1 2   ? -3.446 -28.549 9.585  1.00 27.35 ? 11  LEU A CA    1 
ATOM   7    C  C     . LEU A 1 2   ? -2.083 -29.005 9.071  1.00 30.48 ? 11  LEU A C     1 
ATOM   8    O  O     . LEU A 1 2   ? -1.666 -30.142 9.314  1.00 30.11 ? 11  LEU A O     1 
ATOM   9    C  CB    . LEU A 1 2   ? -3.269 -27.832 10.921 1.00 27.90 ? 11  LEU A CB    1 
ATOM   10   C  CG    . LEU A 1 2   ? -4.481 -27.148 11.545 1.00 31.37 ? 11  LEU A CG    1 
ATOM   11   C  CD1   . LEU A 1 2   ? -4.100 -26.635 12.921 1.00 30.90 ? 11  LEU A CD1   1 
ATOM   12   C  CD2   . LEU A 1 2   ? -4.972 -26.013 10.659 1.00 27.67 ? 11  LEU A CD2   1 
ATOM   13   N  N     . PRO A 1 3   ? -1.367 -28.138 8.359  1.00 30.57 ? 12  PRO A N     1 
ATOM   14   C  CA    . PRO A 1 3   ? 0.012  -28.461 7.980  1.00 22.80 ? 12  PRO A CA    1 
ATOM   15   C  C     . PRO A 1 3   ? 0.839  -28.806 9.208  1.00 23.29 ? 12  PRO A C     1 
ATOM   16   O  O     . PRO A 1 3   ? 0.739  -28.154 10.249 1.00 25.01 ? 12  PRO A O     1 
ATOM   17   C  CB    . PRO A 1 3   ? 0.506  -27.175 7.309  1.00 30.97 ? 12  PRO A CB    1 
ATOM   18   C  CG    . PRO A 1 3   ? -0.741 -26.497 6.830  1.00 26.65 ? 12  PRO A CG    1 
ATOM   19   C  CD    . PRO A 1 3   ? -1.796 -26.826 7.843  1.00 31.06 ? 12  PRO A CD    1 
ATOM   20   N  N     . THR A 1 4   ? 1.647  -29.851 9.085  1.00 22.94 ? 13  THR A N     1 
ATOM   21   C  CA    . THR A 1 4   ? 2.481  -30.331 10.177 1.00 25.82 ? 13  THR A CA    1 
ATOM   22   C  C     . THR A 1 4   ? 3.945  -30.137 9.818  1.00 22.89 ? 13  THR A C     1 
ATOM   23   O  O     . THR A 1 4   ? 4.376  -30.531 8.729  1.00 28.06 ? 13  THR A O     1 
ATOM   24   C  CB    . THR A 1 4   ? 2.211  -31.807 10.470 1.00 30.70 ? 13  THR A CB    1 
ATOM   25   O  OG1   . THR A 1 4   ? 0.837  -31.978 10.829 1.00 40.16 ? 13  THR A OG1   1 
ATOM   26   C  CG2   . THR A 1 4   ? 3.086  -32.281 11.616 1.00 36.59 ? 13  THR A CG2   1 
ATOM   27   N  N     . TYR A 1 5   ? 4.704  -29.535 10.731 1.00 25.24 ? 14  TYR A N     1 
ATOM   28   C  CA    . TYR A 1 5   ? 6.137  -29.334 10.561 1.00 19.76 ? 14  TYR A CA    1 
ATOM   29   C  C     . TYR A 1 5   ? 6.875  -30.109 11.645 1.00 25.89 ? 14  TYR A C     1 
ATOM   30   O  O     . TYR A 1 5   ? 6.651  -29.879 12.839 1.00 26.60 ? 14  TYR A O     1 
ATOM   31   C  CB    . TYR A 1 5   ? 6.498  -27.848 10.616 1.00 21.86 ? 14  TYR A CB    1 
ATOM   32   C  CG    . TYR A 1 5   ? 5.756  -27.007 9.596  1.00 30.01 ? 14  TYR A CG    1 
ATOM   33   C  CD1   . TYR A 1 5   ? 6.255  -26.834 8.308  1.00 31.34 ? 14  TYR A CD1   1 
ATOM   34   C  CD2   . TYR A 1 5   ? 4.552  -26.396 9.918  1.00 21.37 ? 14  TYR A CD2   1 
ATOM   35   C  CE1   . TYR A 1 5   ? 5.571  -26.071 7.369  1.00 27.83 ? 14  TYR A CE1   1 
ATOM   36   C  CE2   . TYR A 1 5   ? 3.865  -25.635 8.992  1.00 27.01 ? 14  TYR A CE2   1 
ATOM   37   C  CZ    . TYR A 1 5   ? 4.376  -25.477 7.721  1.00 23.11 ? 14  TYR A CZ    1 
ATOM   38   O  OH    . TYR A 1 5   ? 3.687  -24.719 6.809  1.00 26.27 ? 14  TYR A OH    1 
ATOM   39   N  N     . LYS A 1 6   ? 7.743  -31.028 11.227 1.00 20.94 ? 15  LYS A N     1 
ATOM   40   C  CA    . LYS A 1 6   ? 8.603  -31.776 12.140 1.00 21.32 ? 15  LYS A CA    1 
ATOM   41   C  C     . LYS A 1 6   ? 9.897  -30.990 12.323 1.00 24.08 ? 15  LYS A C     1 
ATOM   42   O  O     . LYS A 1 6   ? 10.711 -30.898 11.397 1.00 26.53 ? 15  LYS A O     1 
ATOM   43   C  CB    . LYS A 1 6   ? 8.878  -33.179 11.603 1.00 20.36 ? 15  LYS A CB    1 
ATOM   44   C  CG    . LYS A 1 6   ? 9.779  -34.044 12.487 1.00 20.64 ? 15  LYS A CG    1 
ATOM   45   C  CD    . LYS A 1 6   ? 9.118  -34.380 13.820 1.00 26.87 ? 15  LYS A CD    1 
ATOM   46   C  CE    . LYS A 1 6   ? 9.947  -35.370 14.631 1.00 23.47 ? 15  LYS A CE    1 
ATOM   47   N  NZ    . LYS A 1 6   ? 10.022 -36.708 13.977 1.00 30.82 ? 15  LYS A NZ    1 
ATOM   48   N  N     . LEU A 1 7   ? 10.079 -30.416 13.509 1.00 23.45 ? 16  LEU A N     1 
ATOM   49   C  CA    . LEU A 1 7   ? 11.242 -29.597 13.831 1.00 23.24 ? 16  LEU A CA    1 
ATOM   50   C  C     . LEU A 1 7   ? 12.153 -30.368 14.778 1.00 24.35 ? 16  LEU A C     1 
ATOM   51   O  O     . LEU A 1 7   ? 11.686 -30.929 15.775 1.00 26.58 ? 16  LEU A O     1 
ATOM   52   C  CB    . LEU A 1 7   ? 10.814 -28.271 14.465 1.00 19.10 ? 16  LEU A CB    1 
ATOM   53   C  CG    . LEU A 1 7   ? 9.696  -27.515 13.736 1.00 20.75 ? 16  LEU A CG    1 
ATOM   54   C  CD1   . LEU A 1 7   ? 9.395  -26.178 14.409 1.00 17.93 ? 16  LEU A CD1   1 
ATOM   55   C  CD2   . LEU A 1 7   ? 10.052 -27.319 12.273 1.00 17.86 ? 16  LEU A CD2   1 
ATOM   56   N  N     . VAL A 1 8   ? 13.447 -30.393 14.470 1.00 29.81 ? 17  VAL A N     1 
ATOM   57   C  CA    . VAL A 1 8   ? 14.423 -31.161 15.236 1.00 19.18 ? 17  VAL A CA    1 
ATOM   58   C  C     . VAL A 1 8   ? 15.453 -30.204 15.813 1.00 23.09 ? 17  VAL A C     1 
ATOM   59   O  O     . VAL A 1 8   ? 16.044 -29.401 15.081 1.00 24.31 ? 17  VAL A O     1 
ATOM   60   C  CB    . VAL A 1 8   ? 15.100 -32.243 14.375 1.00 22.65 ? 17  VAL A CB    1 
ATOM   61   C  CG1   . VAL A 1 8   ? 16.113 -33.023 15.203 1.00 21.53 ? 17  VAL A CG1   1 
ATOM   62   C  CG2   . VAL A 1 8   ? 14.051 -33.181 13.785 1.00 26.86 ? 17  VAL A CG2   1 
ATOM   63   N  N     . VAL A 1 9   ? 15.667 -30.297 17.121 1.00 24.16 ? 18  VAL A N     1 
ATOM   64   C  CA    . VAL A 1 9   ? 16.608 -29.444 17.838 1.00 23.10 ? 18  VAL A CA    1 
ATOM   65   C  C     . VAL A 1 9   ? 17.879 -30.243 18.091 1.00 28.25 ? 18  VAL A C     1 
ATOM   66   O  O     . VAL A 1 9   ? 17.852 -31.261 18.795 1.00 28.98 ? 18  VAL A O     1 
ATOM   67   C  CB    . VAL A 1 9   ? 15.999 -28.932 19.153 1.00 27.07 ? 18  VAL A CB    1 
ATOM   68   C  CG1   . VAL A 1 9   ? 16.972 -28.024 19.878 1.00 21.90 ? 18  VAL A CG1   1 
ATOM   69   C  CG2   . VAL A 1 9   ? 14.678 -28.206 18.881 1.00 21.57 ? 18  VAL A CG2   1 
ATOM   70   N  N     . VAL A 1 10  ? 18.995 -29.786 17.518 1.00 23.84 ? 19  VAL A N     1 
ATOM   71   C  CA    . VAL A 1 10  ? 20.277 -30.467 17.644 1.00 25.15 ? 19  VAL A CA    1 
ATOM   72   C  C     . VAL A 1 10  ? 21.310 -29.506 18.221 1.00 30.02 ? 19  VAL A C     1 
ATOM   73   O  O     . VAL A 1 10  ? 21.148 -28.282 18.201 1.00 26.01 ? 19  VAL A O     1 
ATOM   74   C  CB    . VAL A 1 10  ? 20.774 -31.039 16.301 1.00 32.89 ? 19  VAL A CB    1 
ATOM   75   C  CG1   . VAL A 1 10  ? 19.740 -31.985 15.705 1.00 28.41 ? 19  VAL A CG1   1 
ATOM   76   C  CG2   . VAL A 1 10  ? 21.109 -29.911 15.333 1.00 27.28 ? 19  VAL A CG2   1 
ATOM   77   N  N     . GLY A 1 11  ? 22.386 -30.080 18.731 1.00 31.36 ? 20  GLY A N     1 
ATOM   78   C  CA    . GLY A 1 11  ? 23.447 -29.304 19.343 1.00 27.49 ? 20  GLY A CA    1 
ATOM   79   C  C     . GLY A 1 11  ? 24.165 -30.115 20.399 1.00 33.50 ? 20  GLY A C     1 
ATOM   80   O  O     . GLY A 1 11  ? 23.684 -31.147 20.865 1.00 29.53 ? 20  GLY A O     1 
ATOM   81   N  N     . ASP A 1 12  ? 25.344 -29.620 20.774 1.00 28.17 ? 21  ASP A N     1 
ATOM   82   C  CA    . ASP A 1 12  ? 26.157 -30.270 21.794 1.00 31.88 ? 21  ASP A CA    1 
ATOM   83   C  C     . ASP A 1 12  ? 25.404 -30.371 23.119 1.00 34.10 ? 21  ASP A C     1 
ATOM   84   O  O     . ASP A 1 12  ? 24.418 -29.673 23.364 1.00 32.86 ? 21  ASP A O     1 
ATOM   85   C  CB    . ASP A 1 12  ? 27.462 -29.504 22.012 1.00 31.34 ? 21  ASP A CB    1 
ATOM   86   C  CG    . ASP A 1 12  ? 28.586 -30.010 21.139 1.00 42.42 ? 21  ASP A CG    1 
ATOM   87   O  OD1   . ASP A 1 12  ? 28.310 -30.791 20.204 1.00 45.35 ? 21  ASP A OD1   1 
ATOM   88   O  OD2   . ASP A 1 12  ? 29.749 -29.632 21.395 1.00 43.80 ? 21  ASP A OD2   1 
ATOM   89   N  N     . GLY A 1 13  ? 25.891 -31.256 23.984 1.00 38.10 ? 22  GLY A N     1 
ATOM   90   C  CA    . GLY A 1 13  ? 25.311 -31.378 25.307 1.00 35.57 ? 22  GLY A CA    1 
ATOM   91   C  C     . GLY A 1 13  ? 25.478 -30.094 26.100 1.00 32.01 ? 22  GLY A C     1 
ATOM   92   O  O     . GLY A 1 13  ? 26.516 -29.432 26.043 1.00 38.66 ? 22  GLY A O     1 
ATOM   93   N  N     . GLY A 1 14  ? 24.428 -29.730 26.832 1.00 31.06 ? 23  GLY A N     1 
ATOM   94   C  CA    . GLY A 1 14  ? 24.457 -28.572 27.697 1.00 30.59 ? 23  GLY A CA    1 
ATOM   95   C  C     . GLY A 1 14  ? 24.218 -27.236 27.023 1.00 32.87 ? 23  GLY A C     1 
ATOM   96   O  O     . GLY A 1 14  ? 24.276 -26.206 27.703 1.00 34.92 ? 23  GLY A O     1 
ATOM   97   N  N     . VAL A 1 15  ? 23.951 -27.206 25.715 1.00 28.66 ? 24  VAL A N     1 
ATOM   98   C  CA    . VAL A 1 15  ? 23.779 -25.917 25.049 1.00 25.73 ? 24  VAL A CA    1 
ATOM   99   C  C     . VAL A 1 15  ? 22.405 -25.318 25.302 1.00 34.61 ? 24  VAL A C     1 
ATOM   100  O  O     . VAL A 1 15  ? 22.222 -24.109 25.096 1.00 28.82 ? 24  VAL A O     1 
ATOM   101  C  CB    . VAL A 1 15  ? 24.049 -26.023 23.538 1.00 29.00 ? 24  VAL A CB    1 
ATOM   102  C  CG1   . VAL A 1 15  ? 25.450 -26.552 23.295 1.00 29.30 ? 24  VAL A CG1   1 
ATOM   103  C  CG2   . VAL A 1 15  ? 23.006 -26.901 22.853 1.00 23.59 ? 24  VAL A CG2   1 
ATOM   104  N  N     . GLY A 1 16  ? 21.441 -26.121 25.749 1.00 28.92 ? 25  GLY A N     1 
ATOM   105  C  CA    . GLY A 1 16  ? 20.134 -25.599 26.094 1.00 29.14 ? 25  GLY A CA    1 
ATOM   106  C  C     . GLY A 1 16  ? 19.015 -26.065 25.186 1.00 30.34 ? 25  GLY A C     1 
ATOM   107  O  O     . GLY A 1 16  ? 17.985 -25.392 25.068 1.00 32.37 ? 25  GLY A O     1 
ATOM   108  N  N     . LYS A 1 17  ? 19.204 -27.222 24.546 1.00 32.81 ? 26  LYS A N     1 
ATOM   109  C  CA    . LYS A 1 17  ? 18.177 -27.761 23.659 1.00 27.19 ? 26  LYS A CA    1 
ATOM   110  C  C     . LYS A 1 17  ? 16.871 -28.001 24.408 1.00 32.27 ? 26  LYS A C     1 
ATOM   111  O  O     . LYS A 1 17  ? 15.802 -27.559 23.970 1.00 29.39 ? 26  LYS A O     1 
ATOM   112  C  CB    . LYS A 1 17  ? 18.668 -29.056 23.011 1.00 31.52 ? 26  LYS A CB    1 
ATOM   113  C  CG    . LYS A 1 17  ? 19.896 -28.888 22.126 1.00 32.83 ? 26  LYS A CG    1 
ATOM   114  C  CD    . LYS A 1 17  ? 20.292 -30.197 21.453 1.00 30.34 ? 26  LYS A CD    1 
ATOM   115  C  CE    . LYS A 1 17  ? 20.640 -31.259 22.476 1.00 34.08 ? 26  LYS A CE    1 
ATOM   116  N  NZ    . LYS A 1 17  ? 21.827 -30.886 23.296 1.00 29.01 ? 26  LYS A NZ    1 
ATOM   117  N  N     . SER A 1 18  ? 16.937 -28.704 25.542 1.00 29.96 ? 27  SER A N     1 
ATOM   118  C  CA    . SER A 1 18  ? 15.727 -28.993 26.306 1.00 36.39 ? 27  SER A CA    1 
ATOM   119  C  C     . SER A 1 18  ? 15.130 -27.725 26.903 1.00 38.78 ? 27  SER A C     1 
ATOM   120  O  O     . SER A 1 18  ? 13.906 -27.539 26.880 1.00 35.44 ? 27  SER A O     1 
ATOM   121  C  CB    . SER A 1 18  ? 16.027 -30.008 27.409 1.00 31.84 ? 27  SER A CB    1 
ATOM   122  O  OG    . SER A 1 18  ? 16.499 -31.226 26.863 1.00 31.73 ? 27  SER A OG    1 
ATOM   123  N  N     . ALA A 1 19  ? 15.978 -26.842 27.438 1.00 33.00 ? 28  ALA A N     1 
ATOM   124  C  CA    . ALA A 1 19  ? 15.481 -25.617 28.056 1.00 31.32 ? 28  ALA A CA    1 
ATOM   125  C  C     . ALA A 1 19  ? 14.740 -24.753 27.046 1.00 27.36 ? 28  ALA A C     1 
ATOM   126  O  O     . ALA A 1 19  ? 13.704 -24.162 27.367 1.00 33.41 ? 28  ALA A O     1 
ATOM   127  C  CB    . ALA A 1 19  ? 16.637 -24.841 28.691 1.00 27.53 ? 28  ALA A CB    1 
ATOM   128  N  N     . LEU A 1 20  ? 15.251 -24.675 25.815 1.00 30.25 ? 29  LEU A N     1 
ATOM   129  C  CA    . LEU A 1 20  ? 14.548 -23.941 24.766 1.00 26.97 ? 29  LEU A CA    1 
ATOM   130  C  C     . LEU A 1 20  ? 13.231 -24.617 24.401 1.00 33.84 ? 29  LEU A C     1 
ATOM   131  O  O     . LEU A 1 20  ? 12.218 -23.942 24.183 1.00 31.04 ? 29  LEU A O     1 
ATOM   132  C  CB    . LEU A 1 20  ? 15.437 -23.814 23.531 1.00 24.48 ? 29  LEU A CB    1 
ATOM   133  C  CG    . LEU A 1 20  ? 16.610 -22.837 23.612 1.00 30.64 ? 29  LEU A CG    1 
ATOM   134  C  CD1   . LEU A 1 20  ? 17.567 -23.066 22.458 1.00 21.21 ? 29  LEU A CD1   1 
ATOM   135  C  CD2   . LEU A 1 20  ? 16.101 -21.406 23.609 1.00 25.00 ? 29  LEU A CD2   1 
ATOM   136  N  N     . THR A 1 21  ? 13.230 -25.948 24.318 1.00 32.33 ? 30  THR A N     1 
ATOM   137  C  CA    . THR A 1 21  ? 12.014 -26.670 23.957 1.00 28.18 ? 30  THR A CA    1 
ATOM   138  C  C     . THR A 1 21  ? 10.948 -26.521 25.036 1.00 29.81 ? 30  THR A C     1 
ATOM   139  O  O     . THR A 1 21  ? 9.779  -26.256 24.736 1.00 30.69 ? 30  THR A O     1 
ATOM   140  C  CB    . THR A 1 21  ? 12.337 -28.145 23.717 1.00 28.24 ? 30  THR A CB    1 
ATOM   141  O  OG1   . THR A 1 21  ? 13.201 -28.262 22.582 1.00 28.51 ? 30  THR A OG1   1 
ATOM   142  C  CG2   . THR A 1 21  ? 11.064 -28.946 23.470 1.00 34.18 ? 30  THR A CG2   1 
ATOM   143  N  N     . ILE A 1 22  ? 11.344 -26.678 26.299 1.00 32.09 ? 31  ILE A N     1 
ATOM   144  C  CA    . ILE A 1 22  ? 10.406 -26.568 27.409 1.00 28.75 ? 31  ILE A CA    1 
ATOM   145  C  C     . ILE A 1 22  ? 9.879  -25.145 27.530 1.00 36.68 ? 31  ILE A C     1 
ATOM   146  O  O     . ILE A 1 22  ? 8.688  -24.928 27.784 1.00 36.71 ? 31  ILE A O     1 
ATOM   147  C  CB    . ILE A 1 22  ? 11.085 -27.046 28.706 1.00 37.12 ? 31  ILE A CB    1 
ATOM   148  C  CG1   . ILE A 1 22  ? 11.339 -28.555 28.630 1.00 36.20 ? 31  ILE A CG1   1 
ATOM   149  C  CG2   . ILE A 1 22  ? 10.256 -26.675 29.929 1.00 34.60 ? 31  ILE A CG2   1 
ATOM   150  C  CD1   . ILE A 1 22  ? 12.154 -29.106 29.779 1.00 43.30 ? 31  ILE A CD1   1 
ATOM   151  N  N     . GLN A 1 23  ? 10.755 -24.152 27.351 1.00 36.32 ? 32  GLN A N     1 
ATOM   152  C  CA    . GLN A 1 23  ? 10.305 -22.764 27.342 1.00 35.92 ? 32  GLN A CA    1 
ATOM   153  C  C     . GLN A 1 23  ? 9.285  -22.528 26.234 1.00 45.80 ? 32  GLN A C     1 
ATOM   154  O  O     . GLN A 1 23  ? 8.295  -21.815 26.432 1.00 39.36 ? 32  GLN A O     1 
ATOM   155  C  CB    . GLN A 1 23  ? 11.504 -21.829 27.183 1.00 38.86 ? 32  GLN A CB    1 
ATOM   156  C  CG    . GLN A 1 23  ? 11.159 -20.347 27.127 1.00 40.08 ? 32  GLN A CG    1 
ATOM   157  C  CD    . GLN A 1 23  ? 10.610 -19.821 28.438 1.00 46.91 ? 32  GLN A CD    1 
ATOM   158  O  OE1   . GLN A 1 23  ? 9.435  -19.470 28.532 1.00 52.70 ? 32  GLN A OE1   1 
ATOM   159  N  NE2   . GLN A 1 23  ? 11.462 -19.757 29.459 1.00 43.89 ? 32  GLN A NE2   1 
ATOM   160  N  N     . PHE A 1 24  ? 9.499  -23.145 25.068 1.00 28.80 ? 33  PHE A N     1 
ATOM   161  C  CA    . PHE A 1 24  ? 8.615  -22.930 23.927 1.00 31.57 ? 33  PHE A CA    1 
ATOM   162  C  C     . PHE A 1 24  ? 7.255  -23.593 24.121 1.00 34.99 ? 33  PHE A C     1 
ATOM   163  O  O     . PHE A 1 24  ? 6.240  -23.063 23.659 1.00 33.71 ? 33  PHE A O     1 
ATOM   164  C  CB    . PHE A 1 24  ? 9.290  -23.447 22.655 1.00 30.92 ? 33  PHE A CB    1 
ATOM   165  C  CG    . PHE A 1 24  ? 8.458  -23.295 21.411 1.00 28.20 ? 33  PHE A CG    1 
ATOM   166  C  CD1   . PHE A 1 24  ? 8.080  -22.041 20.961 1.00 23.71 ? 33  PHE A CD1   1 
ATOM   167  C  CD2   . PHE A 1 24  ? 8.080  -24.410 20.677 1.00 28.99 ? 33  PHE A CD2   1 
ATOM   168  C  CE1   . PHE A 1 24  ? 7.325  -21.901 19.810 1.00 29.47 ? 33  PHE A CE1   1 
ATOM   169  C  CE2   . PHE A 1 24  ? 7.327  -24.278 19.525 1.00 28.04 ? 33  PHE A CE2   1 
ATOM   170  C  CZ    . PHE A 1 24  ? 6.949  -23.022 19.090 1.00 27.53 ? 33  PHE A CZ    1 
ATOM   171  N  N     . PHE A 1 25  ? 7.210  -24.735 24.804 1.00 37.28 ? 34  PHE A N     1 
ATOM   172  C  CA    . PHE A 1 25  ? 5.973  -25.491 24.954 1.00 33.17 ? 34  PHE A CA    1 
ATOM   173  C  C     . PHE A 1 25  ? 5.247  -25.237 26.267 1.00 40.69 ? 34  PHE A C     1 
ATOM   174  O  O     . PHE A 1 25  ? 4.015  -25.312 26.300 1.00 36.31 ? 34  PHE A O     1 
ATOM   175  C  CB    . PHE A 1 25  ? 6.253  -26.991 24.824 1.00 26.69 ? 34  PHE A CB    1 
ATOM   176  C  CG    . PHE A 1 25  ? 6.340  -27.462 23.406 1.00 33.12 ? 34  PHE A CG    1 
ATOM   177  C  CD1   . PHE A 1 25  ? 7.541  -27.424 22.722 1.00 28.98 ? 34  PHE A CD1   1 
ATOM   178  C  CD2   . PHE A 1 25  ? 5.211  -27.927 22.748 1.00 33.88 ? 34  PHE A CD2   1 
ATOM   179  C  CE1   . PHE A 1 25  ? 7.618  -27.849 21.411 1.00 26.89 ? 34  PHE A CE1   1 
ATOM   180  C  CE2   . PHE A 1 25  ? 5.284  -28.352 21.438 1.00 28.30 ? 34  PHE A CE2   1 
ATOM   181  C  CZ    . PHE A 1 25  ? 6.485  -28.311 20.769 1.00 28.26 ? 34  PHE A CZ    1 
ATOM   182  N  N     . GLN A 1 26  ? 5.964  -24.945 27.350 1.00 38.75 ? 35  GLN A N     1 
ATOM   183  C  CA    . GLN A 1 26  ? 5.339  -24.797 28.655 1.00 53.06 ? 35  GLN A CA    1 
ATOM   184  C  C     . GLN A 1 26  ? 5.552  -23.428 29.277 1.00 50.74 ? 35  GLN A C     1 
ATOM   185  O  O     . GLN A 1 26  ? 4.993  -23.164 30.347 1.00 59.57 ? 35  GLN A O     1 
ATOM   186  C  CB    . GLN A 1 26  ? 5.851  -25.880 29.612 1.00 47.64 ? 35  GLN A CB    1 
ATOM   187  C  CG    . GLN A 1 26  ? 5.797  -27.274 29.016 1.00 50.25 ? 35  GLN A CG    1 
ATOM   188  C  CD    . GLN A 1 26  ? 6.193  -28.344 30.004 1.00 60.61 ? 35  GLN A CD    1 
ATOM   189  O  OE1   . GLN A 1 26  ? 6.056  -28.166 31.214 1.00 70.49 ? 35  GLN A OE1   1 
ATOM   190  N  NE2   . GLN A 1 26  ? 6.691  -29.466 29.496 1.00 57.33 ? 35  GLN A NE2   1 
ATOM   191  N  N     . LYS A 1 27  ? 6.334  -22.555 28.641 1.00 55.20 ? 36  LYS A N     1 
ATOM   192  C  CA    . LYS A 1 27  ? 6.604  -21.208 29.148 1.00 60.43 ? 36  LYS A CA    1 
ATOM   193  C  C     . LYS A 1 27  ? 7.163  -21.247 30.569 1.00 65.04 ? 36  LYS A C     1 
ATOM   194  O  O     . LYS A 1 27  ? 6.784  -20.447 31.428 1.00 63.49 ? 36  LYS A O     1 
ATOM   195  C  CB    . LYS A 1 27  ? 5.352  -20.325 29.082 1.00 65.84 ? 36  LYS A CB    1 
ATOM   196  C  CG    . LYS A 1 27  ? 4.697  -20.249 27.710 1.00 58.88 ? 36  LYS A CG    1 
ATOM   197  C  CD    . LYS A 1 27  ? 5.712  -19.952 26.622 1.00 62.38 ? 36  LYS A CD    1 
ATOM   198  C  CE    . LYS A 1 27  ? 6.368  -18.583 26.772 1.00 70.48 ? 36  LYS A CE    1 
ATOM   199  N  NZ    . LYS A 1 27  ? 7.519  -18.428 25.826 1.00 66.09 ? 36  LYS A NZ    1 
ATOM   200  N  N     . ILE A 1 28  ? 8.069  -22.195 30.823 1.00 57.13 ? 37  ILE A N     1 
ATOM   201  C  CA    . ILE A 1 28  ? 8.724  -22.329 32.118 1.00 61.19 ? 37  ILE A CA    1 
ATOM   202  C  C     . ILE A 1 28  ? 10.204 -22.609 31.898 1.00 59.45 ? 37  ILE A C     1 
ATOM   203  O  O     . ILE A 1 28  ? 10.629 -23.035 30.822 1.00 54.74 ? 37  ILE A O     1 
ATOM   204  C  CB    . ILE A 1 28  ? 8.097  -23.441 32.993 1.00 64.22 ? 37  ILE A CB    1 
ATOM   205  C  CG1   . ILE A 1 28  ? 8.101  -24.780 32.251 1.00 57.79 ? 37  ILE A CG1   1 
ATOM   206  C  CG2   . ILE A 1 28  ? 6.688  -23.057 33.438 1.00 59.58 ? 37  ILE A CG2   1 
ATOM   207  C  CD1   . ILE A 1 28  ? 7.543  -25.931 33.067 1.00 62.47 ? 37  ILE A CD1   1 
ATOM   208  N  N     . PHE A 1 29  ? 10.991 -22.360 32.945 1.00 62.85 ? 38  PHE A N     1 
ATOM   209  C  CA    . PHE A 1 29  ? 12.431 -22.619 32.934 1.00 62.19 ? 38  PHE A CA    1 
ATOM   210  C  C     . PHE A 1 29  ? 12.779 -23.280 34.265 1.00 64.71 ? 38  PHE A C     1 
ATOM   211  O  O     . PHE A 1 29  ? 12.906 -22.599 35.287 1.00 62.79 ? 38  PHE A O     1 
ATOM   212  C  CB    . PHE A 1 29  ? 13.227 -21.336 32.718 1.00 58.59 ? 38  PHE A CB    1 
ATOM   213  C  CG    . PHE A 1 29  ? 14.718 -21.510 32.846 1.00 56.91 ? 38  PHE A CG    1 
ATOM   214  C  CD1   . PHE A 1 29  ? 15.459 -22.051 31.809 1.00 48.98 ? 38  PHE A CD1   1 
ATOM   215  C  CD2   . PHE A 1 29  ? 15.379 -21.115 34.001 1.00 60.04 ? 38  PHE A CD2   1 
ATOM   216  C  CE1   . PHE A 1 29  ? 16.832 -22.204 31.924 1.00 47.20 ? 38  PHE A CE1   1 
ATOM   217  C  CE2   . PHE A 1 29  ? 16.750 -21.267 34.121 1.00 58.10 ? 38  PHE A CE2   1 
ATOM   218  C  CZ    . PHE A 1 29  ? 17.477 -21.813 33.080 1.00 48.23 ? 38  PHE A CZ    1 
ATOM   219  N  N     . VAL A 1 30  ? 12.923 -24.602 34.248 1.00 67.47 ? 39  VAL A N     1 
ATOM   220  C  CA    . VAL A 1 30  ? 13.245 -25.361 35.454 1.00 73.87 ? 39  VAL A CA    1 
ATOM   221  C  C     . VAL A 1 30  ? 14.629 -25.979 35.295 1.00 77.29 ? 39  VAL A C     1 
ATOM   222  O  O     . VAL A 1 30  ? 14.777 -26.999 34.606 1.00 74.99 ? 39  VAL A O     1 
ATOM   223  C  CB    . VAL A 1 30  ? 12.186 -26.438 35.738 1.00 71.47 ? 39  VAL A CB    1 
ATOM   224  N  N     . PRO A 1 31  ? 15.674 -25.396 35.906 1.00 77.30 ? 40  PRO A N     1 
ATOM   225  C  CA    . PRO A 1 31  ? 17.042 -25.919 35.830 1.00 74.15 ? 40  PRO A CA    1 
ATOM   226  C  C     . PRO A 1 31  ? 17.259 -27.146 36.716 1.00 77.40 ? 40  PRO A C     1 
ATOM   227  O  O     . PRO A 1 31  ? 17.065 -28.270 36.250 1.00 79.74 ? 40  PRO A O     1 
ATOM   228  C  CB    . PRO A 1 31  ? 17.888 -24.741 36.316 1.00 71.09 ? 40  PRO A CB    1 
ATOM   229  C  CG    . PRO A 1 31  ? 16.991 -24.016 37.260 1.00 67.23 ? 40  PRO A CG    1 
ATOM   230  C  CD    . PRO A 1 31  ? 15.605 -24.145 36.683 1.00 73.40 ? 40  PRO A CD    1 
ATOM   231  N  N     . ILE A 1 37  ? 10.639 -36.490 29.462 1.00 67.64 ? 46  ILE A N     1 
ATOM   232  C  CA    . ILE A 1 37  ? 9.738  -36.598 28.321 1.00 70.95 ? 46  ILE A CA    1 
ATOM   233  C  C     . ILE A 1 37  ? 10.519 -36.971 27.064 1.00 68.77 ? 46  ILE A C     1 
ATOM   234  O  O     . ILE A 1 37  ? 11.122 -36.114 26.418 1.00 66.29 ? 46  ILE A O     1 
ATOM   235  C  CB    . ILE A 1 37  ? 8.949  -35.294 28.108 1.00 66.42 ? 46  ILE A CB    1 
ATOM   236  N  N     . GLU A 1 38  ? 10.496 -38.259 26.719 1.00 72.95 ? 47  GLU A N     1 
ATOM   237  C  CA    . GLU A 1 38  ? 11.249 -38.764 25.579 1.00 64.06 ? 47  GLU A CA    1 
ATOM   238  C  C     . GLU A 1 38  ? 10.504 -38.632 24.256 1.00 58.64 ? 47  GLU A C     1 
ATOM   239  O  O     . GLU A 1 38  ? 11.129 -38.762 23.197 1.00 59.76 ? 47  GLU A O     1 
ATOM   240  C  CB    . GLU A 1 38  ? 11.619 -40.232 25.806 1.00 66.36 ? 47  GLU A CB    1 
ATOM   241  C  CG    . GLU A 1 38  ? 12.296 -40.503 27.135 1.00 69.63 ? 47  GLU A CG    1 
ATOM   242  C  CD    . GLU A 1 38  ? 12.474 -41.985 27.398 1.00 75.37 ? 47  GLU A CD    1 
ATOM   243  O  OE1   . GLU A 1 38  ? 12.061 -42.790 26.536 1.00 73.01 ? 47  GLU A OE1   1 
ATOM   244  O  OE2   . GLU A 1 38  ? 13.022 -42.344 28.462 1.00 71.06 ? 47  GLU A OE2   1 
ATOM   245  N  N     . ASP A 1 39  ? 9.197  -38.386 24.287 1.00 46.35 ? 48  ASP A N     1 
ATOM   246  C  CA    . ASP A 1 39  ? 8.425  -38.204 23.066 1.00 37.85 ? 48  ASP A CA    1 
ATOM   247  C  C     . ASP A 1 39  ? 8.720  -36.836 22.457 1.00 40.12 ? 48  ASP A C     1 
ATOM   248  O  O     . ASP A 1 39  ? 9.171  -35.910 23.136 1.00 42.16 ? 48  ASP A O     1 
ATOM   249  C  CB    . ASP A 1 39  ? 6.927  -38.342 23.363 1.00 34.63 ? 48  ASP A CB    1 
ATOM   250  C  CG    . ASP A 1 39  ? 6.088  -38.584 22.113 1.00 38.43 ? 48  ASP A CG    1 
ATOM   251  O  OD1   . ASP A 1 39  ? 6.657  -38.762 21.015 1.00 37.27 ? 48  ASP A OD1   1 
ATOM   252  O  OD2   . ASP A 1 39  ? 4.844  -38.600 22.236 1.00 31.62 ? 48  ASP A OD2   1 
ATOM   253  N  N     . SER A 1 40  ? 8.475  -36.713 21.155 1.00 28.06 ? 49  SER A N     1 
ATOM   254  C  CA    . SER A 1 40  ? 8.464  -35.383 20.563 1.00 32.85 ? 49  SER A CA    1 
ATOM   255  C  C     . SER A 1 40  ? 7.188  -34.651 20.978 1.00 29.23 ? 49  SER A C     1 
ATOM   256  O  O     . SER A 1 40  ? 6.167  -35.269 21.293 1.00 27.99 ? 49  SER A O     1 
ATOM   257  C  CB    . SER A 1 40  ? 8.591  -35.460 19.039 1.00 28.76 ? 49  SER A CB    1 
ATOM   258  O  OG    . SER A 1 40  ? 7.611  -36.308 18.477 1.00 42.09 ? 49  SER A OG    1 
ATOM   259  N  N     . TYR A 1 41  ? 7.264  -33.322 21.008 1.00 28.50 ? 50  TYR A N     1 
ATOM   260  C  CA    . TYR A 1 41  ? 6.210  -32.477 21.559 1.00 32.93 ? 50  TYR A CA    1 
ATOM   261  C  C     . TYR A 1 41  ? 5.323  -31.906 20.456 1.00 27.03 ? 50  TYR A C     1 
ATOM   262  O  O     . TYR A 1 41  ? 5.819  -31.393 19.448 1.00 24.84 ? 50  TYR A O     1 
ATOM   263  C  CB    . TYR A 1 41  ? 6.810  -31.324 22.366 1.00 34.93 ? 50  TYR A CB    1 
ATOM   264  C  CG    . TYR A 1 41  ? 7.754  -31.720 23.482 1.00 39.34 ? 50  TYR A CG    1 
ATOM   265  C  CD1   . TYR A 1 41  ? 9.100  -31.966 23.229 1.00 40.70 ? 50  TYR A CD1   1 
ATOM   266  C  CD2   . TYR A 1 41  ? 7.308  -31.810 24.792 1.00 48.66 ? 50  TYR A CD2   1 
ATOM   267  C  CE1   . TYR A 1 41  ? 9.968  -32.314 24.246 1.00 37.57 ? 50  TYR A CE1   1 
ATOM   268  C  CE2   . TYR A 1 41  ? 8.169  -32.156 25.816 1.00 57.65 ? 50  TYR A CE2   1 
ATOM   269  C  CZ    . TYR A 1 41  ? 9.497  -32.405 25.536 1.00 45.60 ? 50  TYR A CZ    1 
ATOM   270  O  OH    . TYR A 1 41  ? 10.352 -32.747 26.555 1.00 54.09 ? 50  TYR A OH    1 
ATOM   271  N  N     . LEU A 1 42  ? 4.009  -31.958 20.673 1.00 30.75 ? 51  LEU A N     1 
ATOM   272  C  CA    . LEU A 1 42  ? 3.019  -31.508 19.699 1.00 32.13 ? 51  LEU A CA    1 
ATOM   273  C  C     . LEU A 1 42  ? 2.279  -30.274 20.205 1.00 25.97 ? 51  LEU A C     1 
ATOM   274  O  O     . LEU A 1 42  ? 1.905  -30.206 21.379 1.00 29.17 ? 51  LEU A O     1 
ATOM   275  C  CB    . LEU A 1 42  ? 2.006  -32.616 19.403 1.00 24.79 ? 51  LEU A CB    1 
ATOM   276  C  CG    . LEU A 1 42  ? 2.488  -33.885 18.698 1.00 24.58 ? 51  LEU A CG    1 
ATOM   277  C  CD1   . LEU A 1 42  ? 1.497  -35.017 18.905 1.00 26.32 ? 51  LEU A CD1   1 
ATOM   278  C  CD2   . LEU A 1 42  ? 2.683  -33.620 17.218 1.00 25.47 ? 51  LEU A CD2   1 
ATOM   279  N  N     . LYS A 1 43  ? 2.041  -29.314 19.310 1.00 25.45 ? 52  LYS A N     1 
ATOM   280  C  CA    . LYS A 1 43  ? 1.240  -28.142 19.647 1.00 28.46 ? 52  LYS A CA    1 
ATOM   281  C  C     . LYS A 1 43  ? 0.636  -27.550 18.380 1.00 28.84 ? 52  LYS A C     1 
ATOM   282  O  O     . LYS A 1 43  ? 1.173  -27.719 17.283 1.00 29.82 ? 52  LYS A O     1 
ATOM   283  C  CB    . LYS A 1 43  ? 2.075  -27.068 20.357 1.00 31.02 ? 52  LYS A CB    1 
ATOM   284  C  CG    . LYS A 1 43  ? 3.090  -26.392 19.437 1.00 28.78 ? 52  LYS A CG    1 
ATOM   285  C  CD    . LYS A 1 43  ? 3.366  -24.949 19.837 1.00 28.37 ? 52  LYS A CD    1 
ATOM   286  C  CE    . LYS A 1 43  ? 4.038  -24.863 21.192 1.00 32.88 ? 52  LYS A CE    1 
ATOM   287  N  NZ    . LYS A 1 43  ? 4.303  -23.451 21.583 1.00 33.11 ? 52  LYS A NZ    1 
ATOM   288  N  N     . HIS A 1 44  ? -0.480 -26.847 18.547 1.00 28.33 ? 53  HIS A N     1 
ATOM   289  C  CA    . HIS A 1 44  ? -0.964 -25.938 17.519 1.00 27.80 ? 53  HIS A CA    1 
ATOM   290  C  C     . HIS A 1 44  ? -0.286 -24.587 17.692 1.00 31.05 ? 53  HIS A C     1 
ATOM   291  O  O     . HIS A 1 44  ? 0.047  -24.179 18.807 1.00 35.25 ? 53  HIS A O     1 
ATOM   292  C  CB    . HIS A 1 44  ? -2.481 -25.740 17.592 1.00 27.60 ? 53  HIS A CB    1 
ATOM   293  C  CG    . HIS A 1 44  ? -3.268 -27.006 17.718 1.00 28.87 ? 53  HIS A CG    1 
ATOM   294  N  ND1   . HIS A 1 44  ? -3.715 -27.485 18.930 1.00 30.06 ? 53  HIS A ND1   1 
ATOM   295  C  CD2   . HIS A 1 44  ? -3.720 -27.873 16.781 1.00 29.64 ? 53  HIS A CD2   1 
ATOM   296  C  CE1   . HIS A 1 44  ? -4.398 -28.600 18.736 1.00 31.11 ? 53  HIS A CE1   1 
ATOM   297  N  NE2   . HIS A 1 44  ? -4.415 -28.858 17.441 1.00 29.16 ? 53  HIS A NE2   1 
ATOM   298  N  N     . THR A 1 45  ? -0.089 -23.889 16.578 1.00 27.87 ? 54  THR A N     1 
ATOM   299  C  CA    . THR A 1 45  ? 0.416  -22.526 16.635 1.00 31.62 ? 54  THR A CA    1 
ATOM   300  C  C     . THR A 1 45  ? 0.027  -21.805 15.353 1.00 28.87 ? 54  THR A C     1 
ATOM   301  O  O     . THR A 1 45  ? -0.068 -22.416 14.285 1.00 28.13 ? 54  THR A O     1 
ATOM   302  C  CB    . THR A 1 45  ? 1.937  -22.487 16.842 1.00 37.30 ? 54  THR A CB    1 
ATOM   303  O  OG1   . THR A 1 45  ? 2.350  -21.136 17.087 1.00 41.32 ? 54  THR A OG1   1 
ATOM   304  C  CG2   . THR A 1 45  ? 2.665  -23.019 15.623 1.00 34.77 ? 54  THR A CG2   1 
ATOM   305  N  N     . GLU A 1 46  ? -0.219 -20.503 15.476 1.00 27.60 ? 55  GLU A N     1 
ATOM   306  C  CA    . GLU A 1 46  ? -0.564 -19.656 14.341 1.00 28.42 ? 55  GLU A CA    1 
ATOM   307  C  C     . GLU A 1 46  ? 0.626  -18.767 14.006 1.00 35.01 ? 55  GLU A C     1 
ATOM   308  O  O     . GLU A 1 46  ? 1.028  -17.927 14.819 1.00 35.89 ? 55  GLU A O     1 
ATOM   309  C  CB    . GLU A 1 46  ? -1.799 -18.809 14.638 1.00 32.40 ? 55  GLU A CB    1 
ATOM   310  C  CG    . GLU A 1 46  ? -2.283 -18.026 13.431 1.00 30.82 ? 55  GLU A CG    1 
ATOM   311  C  CD    . GLU A 1 46  ? -3.536 -17.224 13.712 1.00 41.61 ? 55  GLU A CD    1 
ATOM   312  O  OE1   . GLU A 1 46  ? -3.779 -16.887 14.889 1.00 41.03 ? 55  GLU A OE1   1 
ATOM   313  O  OE2   . GLU A 1 46  ? -4.286 -16.939 12.754 1.00 45.87 ? 55  GLU A OE2   1 
ATOM   314  N  N     . ILE A 1 47  ? 1.179  -18.947 12.812 1.00 31.61 ? 56  ILE A N     1 
ATOM   315  C  CA    . ILE A 1 47  ? 2.355  -18.210 12.365 1.00 30.44 ? 56  ILE A CA    1 
ATOM   316  C  C     . ILE A 1 47  ? 1.984  -17.462 11.095 1.00 32.61 ? 56  ILE A C     1 
ATOM   317  O  O     . ILE A 1 47  ? 1.603  -18.083 10.093 1.00 34.30 ? 56  ILE A O     1 
ATOM   318  C  CB    . ILE A 1 47  ? 3.553  -19.139 12.121 1.00 26.39 ? 56  ILE A CB    1 
ATOM   319  C  CG1   . ILE A 1 47  ? 3.867  -19.942 13.385 1.00 32.28 ? 56  ILE A CG1   1 
ATOM   320  C  CG2   . ILE A 1 47  ? 4.763  -18.333 11.681 1.00 35.25 ? 56  ILE A CG2   1 
ATOM   321  C  CD1   . ILE A 1 47  ? 4.909  -21.019 13.187 1.00 23.84 ? 56  ILE A CD1   1 
ATOM   322  N  N     . ASP A 1 48  ? 2.102  -16.134 11.137 1.00 31.41 ? 57  ASP A N     1 
ATOM   323  C  CA    . ASP A 1 48  ? 1.740  -15.269 10.015 1.00 33.99 ? 57  ASP A CA    1 
ATOM   324  C  C     . ASP A 1 48  ? 0.317  -15.564 9.545  1.00 38.92 ? 57  ASP A C     1 
ATOM   325  O  O     . ASP A 1 48  ? 0.046  -15.721 8.352  1.00 39.39 ? 57  ASP A O     1 
ATOM   326  C  CB    . ASP A 1 48  ? 2.746  -15.403 8.868  1.00 31.89 ? 57  ASP A CB    1 
ATOM   327  C  CG    . ASP A 1 48  ? 4.165  -15.076 9.297  1.00 35.87 ? 57  ASP A CG    1 
ATOM   328  O  OD1   . ASP A 1 48  ? 4.333  -14.240 10.208 1.00 36.48 ? 57  ASP A OD1   1 
ATOM   329  O  OD2   . ASP A 1 48  ? 5.116  -15.656 8.731  1.00 36.28 ? 57  ASP A OD2   1 
ATOM   330  N  N     . ASN A 1 49  ? -0.591 -15.664 10.520 1.00 33.31 ? 58  ASN A N     1 
ATOM   331  C  CA    . ASN A 1 49  ? -2.024 -15.856 10.288 1.00 42.45 ? 58  ASN A CA    1 
ATOM   332  C  C     . ASN A 1 49  ? -2.325 -17.177 9.584  1.00 34.53 ? 58  ASN A C     1 
ATOM   333  O  O     . ASN A 1 49  ? -3.348 -17.314 8.912  1.00 36.50 ? 58  ASN A O     1 
ATOM   334  C  CB    . ASN A 1 49  ? -2.622 -14.681 9.507  1.00 39.29 ? 58  ASN A CB    1 
ATOM   335  C  CG    . ASN A 1 49  ? -2.337 -13.348 10.166 1.00 47.07 ? 58  ASN A CG    1 
ATOM   336  O  OD1   . ASN A 1 49  ? -3.019 -12.951 11.109 1.00 46.21 ? 58  ASN A OD1   1 
ATOM   337  N  ND2   . ASN A 1 49  ? -1.312 -12.655 9.681  1.00 49.22 ? 58  ASN A ND2   1 
ATOM   338  N  N     . GLN A 1 50  ? -1.444 -18.161 9.740  1.00 34.71 ? 59  GLN A N     1 
ATOM   339  C  CA    . GLN A 1 50  ? -1.641 -19.496 9.185  1.00 37.03 ? 59  GLN A CA    1 
ATOM   340  C  C     . GLN A 1 50  ? -1.401 -20.504 10.300 1.00 33.48 ? 59  GLN A C     1 
ATOM   341  O  O     . GLN A 1 50  ? -0.276 -20.624 10.797 1.00 29.77 ? 59  GLN A O     1 
ATOM   342  C  CB    . GLN A 1 50  ? -0.702 -19.759 8.006  1.00 35.06 ? 59  GLN A CB    1 
ATOM   343  C  CG    . GLN A 1 50  ? -0.844 -18.785 6.847  1.00 41.25 ? 59  GLN A CG    1 
ATOM   344  C  CD    . GLN A 1 50  ? 0.302  -18.904 5.855  1.00 55.51 ? 59  GLN A CD    1 
ATOM   345  O  OE1   . GLN A 1 50  ? 0.822  -19.997 5.618  1.00 50.48 ? 59  GLN A OE1   1 
ATOM   346  N  NE2   . GLN A 1 50  ? 0.712  -17.775 5.283  1.00 61.79 ? 59  GLN A NE2   1 
ATOM   347  N  N     . TRP A 1 51  ? -2.452 -21.221 10.691 1.00 31.64 ? 60  TRP A N     1 
ATOM   348  C  CA    . TRP A 1 51  ? -2.339 -22.209 11.754 1.00 26.57 ? 60  TRP A CA    1 
ATOM   349  C  C     . TRP A 1 51  ? -1.571 -23.435 11.277 1.00 26.76 ? 60  TRP A C     1 
ATOM   350  O  O     . TRP A 1 51  ? -1.666 -23.845 10.117 1.00 28.37 ? 60  TRP A O     1 
ATOM   351  C  CB    . TRP A 1 51  ? -3.723 -22.627 12.248 1.00 28.13 ? 60  TRP A CB    1 
ATOM   352  C  CG    . TRP A 1 51  ? -4.361 -21.642 13.161 1.00 30.97 ? 60  TRP A CG    1 
ATOM   353  C  CD1   . TRP A 1 51  ? -5.242 -20.659 12.821 1.00 32.11 ? 60  TRP A CD1   1 
ATOM   354  C  CD2   . TRP A 1 51  ? -4.172 -21.544 14.576 1.00 32.37 ? 60  TRP A CD2   1 
ATOM   355  N  NE1   . TRP A 1 51  ? -5.615 -19.952 13.940 1.00 42.04 ? 60  TRP A NE1   1 
ATOM   356  C  CE2   . TRP A 1 51  ? -4.969 -20.476 15.030 1.00 35.87 ? 60  TRP A CE2   1 
ATOM   357  C  CE3   . TRP A 1 51  ? -3.402 -22.255 15.503 1.00 35.51 ? 60  TRP A CE3   1 
ATOM   358  C  CZ2   . TRP A 1 51  ? -5.022 -20.102 16.371 1.00 35.18 ? 60  TRP A CZ2   1 
ATOM   359  C  CZ3   . TRP A 1 51  ? -3.455 -21.882 16.833 1.00 34.97 ? 60  TRP A CZ3   1 
ATOM   360  C  CH2   . TRP A 1 51  ? -4.260 -20.815 17.255 1.00 37.30 ? 60  TRP A CH2   1 
ATOM   361  N  N     . ALA A 1 52  ? -0.807 -24.026 12.192 1.00 25.11 ? 61  ALA A N     1 
ATOM   362  C  CA    . ALA A 1 52  ? -0.026 -25.210 11.873 1.00 26.64 ? 61  ALA A CA    1 
ATOM   363  C  C     . ALA A 1 52  ? 0.148  -26.051 13.126 1.00 25.75 ? 61  ALA A C     1 
ATOM   364  O  O     . ALA A 1 52  ? -0.031 -25.574 14.250 1.00 27.41 ? 61  ALA A O     1 
ATOM   365  C  CB    . ALA A 1 52  ? 1.344  -24.845 11.290 1.00 29.96 ? 61  ALA A CB    1 
ATOM   366  N  N     . ILE A 1 53  ? 0.503  -27.315 12.916 1.00 25.98 ? 62  ILE A N     1 
ATOM   367  C  CA    . ILE A 1 53  ? 0.879  -28.227 13.989 1.00 25.01 ? 62  ILE A CA    1 
ATOM   368  C  C     . ILE A 1 53  ? 2.394  -28.381 13.971 1.00 23.44 ? 62  ILE A C     1 
ATOM   369  O  O     . ILE A 1 53  ? 2.987  -28.684 12.929 1.00 20.85 ? 62  ILE A O     1 
ATOM   370  C  CB    . ILE A 1 53  ? 0.171  -29.585 13.849 1.00 21.98 ? 62  ILE A CB    1 
ATOM   371  C  CG1   . ILE A 1 53  ? -1.332 -29.408 14.088 1.00 23.53 ? 62  ILE A CG1   1 
ATOM   372  C  CG2   . ILE A 1 53  ? 0.765  -30.600 14.811 1.00 22.17 ? 62  ILE A CG2   1 
ATOM   373  C  CD1   . ILE A 1 53  ? -2.149 -30.626 13.810 1.00 24.44 ? 62  ILE A CD1   1 
ATOM   374  N  N     . LEU A 1 54  ? 3.019  -28.149 15.117 1.00 23.49 ? 63  LEU A N     1 
ATOM   375  C  CA    . LEU A 1 54  ? 4.456  -28.316 15.267 1.00 22.38 ? 63  LEU A CA    1 
ATOM   376  C  C     . LEU A 1 54  ? 4.721  -29.621 16.007 1.00 22.81 ? 63  LEU A C     1 
ATOM   377  O  O     . LEU A 1 54  ? 4.068  -29.910 17.015 1.00 25.41 ? 63  LEU A O     1 
ATOM   378  C  CB    . LEU A 1 54  ? 5.068  -27.126 16.010 1.00 24.91 ? 63  LEU A CB    1 
ATOM   379  C  CG    . LEU A 1 54  ? 5.594  -25.954 15.168 1.00 36.98 ? 63  LEU A CG    1 
ATOM   380  C  CD1   . LEU A 1 54  ? 4.654  -25.578 14.037 1.00 20.79 ? 63  LEU A CD1   1 
ATOM   381  C  CD2   . LEU A 1 54  ? 5.885  -24.735 16.041 1.00 31.58 ? 63  LEU A CD2   1 
ATOM   382  N  N     . ASP A 1 55  ? 5.647  -30.416 15.479 1.00 21.92 ? 64  ASP A N     1 
ATOM   383  C  CA    . ASP A 1 55  ? 6.061  -31.698 16.052 1.00 24.08 ? 64  ASP A CA    1 
ATOM   384  C  C     . ASP A 1 55  ? 7.559  -31.567 16.315 1.00 22.70 ? 64  ASP A C     1 
ATOM   385  O  O     . ASP A 1 55  ? 8.364  -31.642 15.383 1.00 25.54 ? 64  ASP A O     1 
ATOM   386  C  CB    . ASP A 1 55  ? 5.737  -32.844 15.089 1.00 25.80 ? 64  ASP A CB    1 
ATOM   387  C  CG    . ASP A 1 55  ? 5.849  -34.219 15.732 1.00 31.06 ? 64  ASP A CG    1 
ATOM   388  O  OD1   . ASP A 1 55  ? 6.192  -34.311 16.930 1.00 28.03 ? 64  ASP A OD1   1 
ATOM   389  O  OD2   . ASP A 1 55  ? 5.580  -35.215 15.026 1.00 29.56 ? 64  ASP A OD2   1 
ATOM   390  N  N     . VAL A 1 56  ? 7.941  -31.340 17.569 1.00 27.13 ? 65  VAL A N     1 
ATOM   391  C  CA    . VAL A 1 56  ? 9.290  -30.889 17.905 1.00 22.60 ? 65  VAL A CA    1 
ATOM   392  C  C     . VAL A 1 56  ? 10.019 -31.994 18.653 1.00 19.93 ? 65  VAL A C     1 
ATOM   393  O  O     . VAL A 1 56  ? 9.580  -32.429 19.726 1.00 22.46 ? 65  VAL A O     1 
ATOM   394  C  CB    . VAL A 1 56  ? 9.265  -29.595 18.728 1.00 27.20 ? 65  VAL A CB    1 
ATOM   395  C  CG1   . VAL A 1 56  ? 10.684 -29.168 19.069 1.00 25.64 ? 65  VAL A CG1   1 
ATOM   396  C  CG2   . VAL A 1 56  ? 8.544  -28.502 17.958 1.00 18.39 ? 65  VAL A CG2   1 
ATOM   397  N  N     . LEU A 1 57  ? 11.144 -32.429 18.095 1.00 24.65 ? 66  LEU A N     1 
ATOM   398  C  CA    . LEU A 1 57  ? 11.974 -33.463 18.693 1.00 23.38 ? 66  LEU A CA    1 
ATOM   399  C  C     . LEU A 1 57  ? 13.147 -32.812 19.414 1.00 22.27 ? 66  LEU A C     1 
ATOM   400  O  O     . LEU A 1 57  ? 13.975 -32.138 18.789 1.00 22.64 ? 66  LEU A O     1 
ATOM   401  C  CB    . LEU A 1 57  ? 12.473 -34.445 17.636 1.00 21.13 ? 66  LEU A CB    1 
ATOM   402  C  CG    . LEU A 1 57  ? 13.408 -35.523 18.177 1.00 29.94 ? 66  LEU A CG    1 
ATOM   403  C  CD1   . LEU A 1 57  ? 12.685 -36.406 19.186 1.00 25.50 ? 66  LEU A CD1   1 
ATOM   404  C  CD2   . LEU A 1 57  ? 13.950 -36.343 17.034 1.00 27.31 ? 66  LEU A CD2   1 
ATOM   405  N  N     . ASP A 1 58  ? 13.209 -33.016 20.725 1.00 22.06 ? 67  ASP A N     1 
ATOM   406  C  CA    . ASP A 1 58  ? 14.314 -32.544 21.554 1.00 28.68 ? 67  ASP A CA    1 
ATOM   407  C  C     . ASP A 1 58  ? 15.340 -33.671 21.647 1.00 36.74 ? 67  ASP A C     1 
ATOM   408  O  O     . ASP A 1 58  ? 15.167 -34.623 22.411 1.00 35.60 ? 67  ASP A O     1 
ATOM   409  C  CB    . ASP A 1 58  ? 13.797 -32.127 22.927 1.00 31.80 ? 67  ASP A CB    1 
ATOM   410  C  CG    . ASP A 1 58  ? 14.901 -31.704 23.869 1.00 27.40 ? 67  ASP A CG    1 
ATOM   411  O  OD1   . ASP A 1 58  ? 15.960 -31.250 23.387 1.00 33.42 ? 67  ASP A OD1   1 
ATOM   412  O  OD2   . ASP A 1 58  ? 14.710 -31.834 25.095 1.00 30.84 ? 67  ASP A OD2   1 
ATOM   413  N  N     . THR A 1 59  ? 16.414 -33.566 20.866 1.00 28.89 ? 68  THR A N     1 
ATOM   414  C  CA    . THR A 1 59  ? 17.400 -34.632 20.783 1.00 39.06 ? 68  THR A CA    1 
ATOM   415  C  C     . THR A 1 59  ? 18.340 -34.601 21.986 1.00 37.66 ? 68  THR A C     1 
ATOM   416  O  O     . THR A 1 59  ? 18.419 -33.618 22.726 1.00 41.68 ? 68  THR A O     1 
ATOM   417  C  CB    . THR A 1 59  ? 18.212 -34.522 19.492 1.00 42.36 ? 68  THR A CB    1 
ATOM   418  O  OG1   . THR A 1 59  ? 18.994 -33.318 19.515 1.00 33.11 ? 68  THR A OG1   1 
ATOM   419  C  CG2   . THR A 1 59  ? 17.293 -34.504 18.282 1.00 30.94 ? 68  THR A CG2   1 
ATOM   420  N  N     . ALA A 1 60  ? 19.067 -35.701 22.166 1.00 40.24 ? 69  ALA A N     1 
ATOM   421  C  CA    . ALA A 1 60  ? 20.076 -35.804 23.211 1.00 51.75 ? 69  ALA A CA    1 
ATOM   422  C  C     . ALA A 1 60  ? 21.445 -35.429 22.658 1.00 55.99 ? 69  ALA A C     1 
ATOM   423  O  O     . ALA A 1 60  ? 21.826 -35.859 21.564 1.00 64.76 ? 69  ALA A O     1 
ATOM   424  C  CB    . ALA A 1 60  ? 20.119 -37.220 23.788 1.00 48.33 ? 69  ALA A CB    1 
ATOM   425  N  N     . GLY A 1 61  ? 22.185 -34.627 23.423 1.00 50.91 ? 70  GLY A N     1 
ATOM   426  C  CA    . GLY A 1 61  ? 23.500 -34.166 23.023 1.00 50.13 ? 70  GLY A CA    1 
ATOM   427  C  C     . GLY A 1 61  ? 24.614 -35.184 23.106 1.00 53.53 ? 70  GLY A C     1 
ATOM   428  O  O     . GLY A 1 61  ? 25.765 -34.848 22.814 1.00 52.06 ? 70  GLY A O     1 
ATOM   429  N  N     . GLN A 1 62  ? 24.312 -36.421 23.494 1.00 64.64 ? 71  GLN A N     1 
ATOM   430  C  CA    . GLN A 1 62  ? 25.317 -37.472 23.540 1.00 67.88 ? 71  GLN A CA    1 
ATOM   431  C  C     . GLN A 1 62  ? 25.653 -37.944 22.125 1.00 64.35 ? 71  GLN A C     1 
ATOM   432  O  O     . GLN A 1 62  ? 25.060 -37.510 21.132 1.00 72.43 ? 71  GLN A O     1 
ATOM   433  C  CB    . GLN A 1 62  ? 24.828 -38.633 24.403 1.00 68.55 ? 71  GLN A CB    1 
ATOM   434  N  N     . GLU A 1 63  ? 26.626 -38.855 22.032 0.00 61.87 ? 72  GLU A N     1 
ATOM   435  C  CA    . GLU A 1 63  ? 27.009 -39.389 20.729 0.00 61.71 ? 72  GLU A CA    1 
ATOM   436  C  C     . GLU A 1 63  ? 25.862 -40.146 20.074 0.00 64.78 ? 72  GLU A C     1 
ATOM   437  O  O     . GLU A 1 63  ? 25.792 -40.217 18.841 0.00 64.66 ? 72  GLU A O     1 
ATOM   438  C  CB    . GLU A 1 63  ? 28.231 -40.297 20.871 0.00 55.01 ? 72  GLU A CB    1 
ATOM   439  N  N     . GLU A 1 64  ? 24.961 -40.714 20.879 1.00 69.92 ? 73  GLU A N     1 
ATOM   440  C  CA    . GLU A 1 64  ? 23.802 -41.455 20.391 1.00 74.76 ? 73  GLU A CA    1 
ATOM   441  C  C     . GLU A 1 64  ? 24.199 -42.584 19.450 1.00 75.79 ? 73  GLU A C     1 
ATOM   442  O  O     . GLU A 1 64  ? 25.351 -43.030 19.448 1.00 72.61 ? 73  GLU A O     1 
ATOM   443  C  CB    . GLU A 1 64  ? 22.816 -40.517 19.690 1.00 74.95 ? 73  GLU A CB    1 
ATOM   444  C  CG    . GLU A 1 64  ? 22.053 -39.607 20.627 1.00 72.70 ? 73  GLU A CG    1 
ATOM   445  C  CD    . GLU A 1 64  ? 20.945 -38.858 19.918 1.00 74.87 ? 73  GLU A CD    1 
ATOM   446  O  OE1   . GLU A 1 64  ? 21.022 -38.719 18.679 1.00 76.57 ? 73  GLU A OE1   1 
ATOM   447  O  OE2   . GLU A 1 64  ? 19.996 -38.414 20.598 1.00 72.81 ? 73  GLU A OE2   1 
ATOM   448  N  N     . PHE A 1 65  ? 23.244 -43.051 18.650 1.00 77.80 ? 74  PHE A N     1 
ATOM   449  C  CA    . PHE A 1 65  ? 23.460 -44.129 17.697 1.00 75.75 ? 74  PHE A CA    1 
ATOM   450  C  C     . PHE A 1 65  ? 23.236 -43.612 16.284 1.00 72.38 ? 74  PHE A C     1 
ATOM   451  O  O     . PHE A 1 65  ? 22.300 -42.844 16.035 1.00 69.59 ? 74  PHE A O     1 
ATOM   452  C  CB    . PHE A 1 65  ? 22.531 -45.314 17.983 1.00 74.55 ? 74  PHE A CB    1 
ATOM   453  C  CG    . PHE A 1 65  ? 22.969 -46.161 19.147 1.00 75.82 ? 74  PHE A CG    1 
ATOM   454  C  CD1   . PHE A 1 65  ? 22.880 -45.681 20.445 1.00 72.04 ? 74  PHE A CD1   1 
ATOM   455  C  CD2   . PHE A 1 65  ? 23.464 -47.440 18.942 1.00 72.44 ? 74  PHE A CD2   1 
ATOM   456  C  CE1   . PHE A 1 65  ? 23.282 -46.460 21.517 1.00 67.05 ? 74  PHE A CE1   1 
ATOM   457  C  CE2   . PHE A 1 65  ? 23.867 -48.222 20.008 1.00 74.15 ? 74  PHE A CE2   1 
ATOM   458  C  CZ    . PHE A 1 65  ? 23.774 -47.733 21.298 1.00 71.17 ? 74  PHE A CZ    1 
ATOM   459  N  N     . SER A 1 66  ? 24.105 -44.041 15.365 1.00 75.06 ? 75  SER A N     1 
ATOM   460  C  CA    . SER A 1 66  ? 24.042 -43.568 13.985 1.00 71.54 ? 75  SER A CA    1 
ATOM   461  C  C     . SER A 1 66  ? 22.698 -43.893 13.344 1.00 66.99 ? 75  SER A C     1 
ATOM   462  O  O     . SER A 1 66  ? 22.136 -43.070 12.612 1.00 60.64 ? 75  SER A O     1 
ATOM   463  C  CB    . SER A 1 66  ? 25.188 -44.179 13.176 1.00 73.53 ? 75  SER A CB    1 
ATOM   464  O  OG    . SER A 1 66  ? 25.168 -43.735 11.831 1.00 79.07 ? 75  SER A OG    1 
ATOM   465  N  N     . ALA A 1 67  ? 22.163 -45.087 13.614 1.00 61.88 ? 76  ALA A N     1 
ATOM   466  C  CA    . ALA A 1 67  ? 20.891 -45.485 13.021 1.00 62.43 ? 76  ALA A CA    1 
ATOM   467  C  C     . ALA A 1 67  ? 19.747 -44.621 13.537 1.00 57.18 ? 76  ALA A C     1 
ATOM   468  O  O     . ALA A 1 67  ? 18.942 -44.106 12.753 1.00 53.96 ? 76  ALA A O     1 
ATOM   469  C  CB    . ALA A 1 67  ? 20.621 -46.964 13.301 1.00 59.33 ? 76  ALA A CB    1 
ATOM   470  N  N     . MET A 1 68  ? 19.661 -44.451 14.860 1.00 65.90 ? 77  MET A N     1 
ATOM   471  C  CA    . MET A 1 68  ? 18.611 -43.617 15.441 1.00 61.71 ? 77  MET A CA    1 
ATOM   472  C  C     . MET A 1 68  ? 18.775 -42.158 15.036 1.00 58.13 ? 77  MET A C     1 
ATOM   473  O  O     . MET A 1 68  ? 17.785 -41.464 14.775 1.00 53.86 ? 77  MET A O     1 
ATOM   474  C  CB    . MET A 1 68  ? 18.624 -43.747 16.965 1.00 71.18 ? 77  MET A CB    1 
ATOM   475  C  CG    . MET A 1 68  ? 18.096 -45.071 17.500 1.00 67.53 ? 77  MET A CG    1 
ATOM   476  S  SD    . MET A 1 68  ? 16.297 -45.180 17.403 1.00 92.42 ? 77  MET A SD    1 
ATOM   477  C  CE    . MET A 1 68  ? 15.823 -43.631 18.173 1.00 68.58 ? 77  MET A CE    1 
ATOM   478  N  N     . ARG A 1 69  ? 20.017 -41.677 14.982 1.00 57.41 ? 78  ARG A N     1 
ATOM   479  C  CA    . ARG A 1 69  ? 20.265 -40.278 14.653 1.00 56.00 ? 78  ARG A CA    1 
ATOM   480  C  C     . ARG A 1 69  ? 19.877 -39.974 13.212 1.00 54.59 ? 78  ARG A C     1 
ATOM   481  O  O     . ARG A 1 69  ? 19.145 -39.014 12.944 1.00 47.72 ? 78  ARG A O     1 
ATOM   482  C  CB    . ARG A 1 69  ? 21.735 -39.942 14.903 1.00 58.66 ? 78  ARG A CB    1 
ATOM   483  C  CG    . ARG A 1 69  ? 22.130 -38.506 14.616 1.00 55.28 ? 78  ARG A CG    1 
ATOM   484  C  CD    . ARG A 1 69  ? 23.645 -38.378 14.631 1.00 57.56 ? 78  ARG A CD    1 
ATOM   485  N  NE    . ARG A 1 69  ? 24.251 -39.255 13.635 1.00 62.40 ? 78  ARG A NE    1 
ATOM   486  C  CZ    . ARG A 1 69  ? 25.521 -39.634 13.637 1.00 64.43 ? 78  ARG A CZ    1 
ATOM   487  N  NH1   . ARG A 1 69  ? 26.359 -39.240 14.583 1.00 67.85 ? 78  ARG A NH1   1 
ATOM   488  N  NH2   . ARG A 1 69  ? 25.961 -40.433 12.669 1.00 65.83 ? 78  ARG A NH2   1 
ATOM   489  N  N     . GLU A 1 70  ? 20.355 -40.786 12.266 1.00 51.78 ? 79  GLU A N     1 
ATOM   490  C  CA    . GLU A 1 70  ? 20.030 -40.540 10.866 1.00 53.75 ? 79  GLU A CA    1 
ATOM   491  C  C     . GLU A 1 70  ? 18.535 -40.657 10.607 1.00 50.90 ? 79  GLU A C     1 
ATOM   492  O  O     . GLU A 1 70  ? 18.006 -39.976 9.721  1.00 39.79 ? 79  GLU A O     1 
ATOM   493  C  CB    . GLU A 1 70  ? 20.805 -41.502 9.968  1.00 50.20 ? 79  GLU A CB    1 
ATOM   494  C  CG    . GLU A 1 70  ? 22.292 -41.204 9.917  1.00 57.66 ? 79  GLU A CG    1 
ATOM   495  C  CD    . GLU A 1 70  ? 23.024 -42.068 8.918  1.00 65.35 ? 79  GLU A CD    1 
ATOM   496  O  OE1   . GLU A 1 70  ? 22.354 -42.831 8.188  1.00 67.72 ? 79  GLU A OE1   1 
ATOM   497  O  OE2   . GLU A 1 70  ? 24.270 -41.984 8.865  1.00 68.53 ? 79  GLU A OE2   1 
ATOM   498  N  N     . GLN A 1 71  ? 17.838 -41.498 11.374 1.00 47.57 ? 80  GLN A N     1 
ATOM   499  C  CA    . GLN A 1 71  ? 16.412 -41.698 11.143 1.00 54.28 ? 80  GLN A CA    1 
ATOM   500  C  C     . GLN A 1 71  ? 15.617 -40.429 11.430 1.00 42.96 ? 80  GLN A C     1 
ATOM   501  O  O     . GLN A 1 71  ? 14.807 -39.996 10.602 1.00 41.79 ? 80  GLN A O     1 
ATOM   502  C  CB    . GLN A 1 71  ? 15.896 -42.861 11.991 1.00 54.32 ? 80  GLN A CB    1 
ATOM   503  C  CG    . GLN A 1 71  ? 14.413 -43.121 11.797 1.00 56.20 ? 80  GLN A CG    1 
ATOM   504  C  CD    . GLN A 1 71  ? 14.033 -43.217 10.329 1.00 59.99 ? 80  GLN A CD    1 
ATOM   505  O  OE1   . GLN A 1 71  ? 14.668 -43.939 9.557  1.00 64.50 ? 80  GLN A OE1   1 
ATOM   506  N  NE2   . GLN A 1 71  ? 12.998 -42.480 9.933  1.00 55.34 ? 80  GLN A NE2   1 
ATOM   507  N  N     . TYR A 1 72  ? 15.834 -39.812 12.595 1.00 41.26 ? 81  TYR A N     1 
ATOM   508  C  CA    . TYR A 1 72  ? 15.083 -38.602 12.905 1.00 44.59 ? 81  TYR A CA    1 
ATOM   509  C  C     . TYR A 1 72  ? 15.554 -37.409 12.086 1.00 41.24 ? 81  TYR A C     1 
ATOM   510  O  O     . TYR A 1 72  ? 14.797 -36.444 11.928 1.00 40.61 ? 81  TYR A O     1 
ATOM   511  C  CB    . TYR A 1 72  ? 15.137 -38.292 14.409 1.00 46.50 ? 81  TYR A CB    1 
ATOM   512  C  CG    . TYR A 1 72  ? 16.477 -37.884 15.008 1.00 41.68 ? 81  TYR A CG    1 
ATOM   513  C  CD1   . TYR A 1 72  ? 17.111 -36.701 14.640 1.00 39.44 ? 81  TYR A CD1   1 
ATOM   514  C  CD2   . TYR A 1 72  ? 17.070 -38.654 15.999 1.00 51.07 ? 81  TYR A CD2   1 
ATOM   515  C  CE1   . TYR A 1 72  ? 18.317 -36.325 15.202 1.00 41.08 ? 81  TYR A CE1   1 
ATOM   516  C  CE2   . TYR A 1 72  ? 18.273 -38.282 16.574 1.00 51.28 ? 81  TYR A CE2   1 
ATOM   517  C  CZ    . TYR A 1 72  ? 18.893 -37.118 16.170 1.00 48.70 ? 81  TYR A CZ    1 
ATOM   518  O  OH    . TYR A 1 72  ? 20.093 -36.745 16.736 1.00 47.85 ? 81  TYR A OH    1 
ATOM   519  N  N     . MET A 1 73  ? 16.780 -37.446 11.565 1.00 35.22 ? 82  MET A N     1 
ATOM   520  C  CA    . MET A 1 73  ? 17.200 -36.401 10.639 1.00 40.39 ? 82  MET A CA    1 
ATOM   521  C  C     . MET A 1 73  ? 16.486 -36.537 9.300  1.00 41.77 ? 82  MET A C     1 
ATOM   522  O  O     . MET A 1 73  ? 16.141 -35.531 8.672  1.00 36.25 ? 82  MET A O     1 
ATOM   523  C  CB    . MET A 1 73  ? 18.715 -36.434 10.443 1.00 37.42 ? 82  MET A CB    1 
ATOM   524  C  CG    . MET A 1 73  ? 19.504 -35.941 11.639 1.00 35.02 ? 82  MET A CG    1 
ATOM   525  S  SD    . MET A 1 73  ? 21.279 -35.925 11.317 1.00 38.11 ? 82  MET A SD    1 
ATOM   526  C  CE    . MET A 1 73  ? 21.884 -35.281 12.873 1.00 39.53 ? 82  MET A CE    1 
ATOM   527  N  N     . ARG A 1 74  ? 16.242 -37.773 8.854  1.00 31.62 ? 83  ARG A N     1 
ATOM   528  C  CA    . ARG A 1 74  ? 15.549 -37.982 7.585  1.00 37.25 ? 83  ARG A CA    1 
ATOM   529  C  C     . ARG A 1 74  ? 14.124 -37.438 7.621  1.00 31.18 ? 83  ARG A C     1 
ATOM   530  O  O     . ARG A 1 74  ? 13.628 -36.916 6.614  1.00 30.97 ? 83  ARG A O     1 
ATOM   531  C  CB    . ARG A 1 74  ? 15.536 -39.469 7.229  1.00 35.77 ? 83  ARG A CB    1 
ATOM   532  C  CG    . ARG A 1 74  ? 16.640 -39.893 6.280  1.00 44.42 ? 83  ARG A CG    1 
ATOM   533  C  CD    . ARG A 1 74  ? 16.357 -41.264 5.684  1.00 54.52 ? 83  ARG A CD    1 
ATOM   534  N  NE    . ARG A 1 74  ? 16.223 -42.290 6.711  1.00 50.70 ? 83  ARG A NE    1 
ATOM   535  C  CZ    . ARG A 1 74  ? 17.223 -43.039 7.158  1.00 63.81 ? 83  ARG A CZ    1 
ATOM   536  N  NH1   . ARG A 1 74  ? 18.455 -42.896 6.695  1.00 60.76 ? 83  ARG A NH1   1 
ATOM   537  N  NH2   . ARG A 1 74  ? 16.979 -43.957 8.090  1.00 57.90 ? 83  ARG A NH2   1 
ATOM   538  N  N     . THR A 1 75  ? 13.451 -37.552 8.766  1.00 33.11 ? 84  THR A N     1 
ATOM   539  C  CA    . THR A 1 75  ? 12.052 -37.159 8.888  1.00 33.01 ? 84  THR A CA    1 
ATOM   540  C  C     . THR A 1 75  ? 11.858 -35.681 9.200  1.00 32.04 ? 84  THR A C     1 
ATOM   541  O  O     . THR A 1 75  ? 10.713 -35.218 9.219  1.00 35.95 ? 84  THR A O     1 
ATOM   542  C  CB    . THR A 1 75  ? 11.360 -37.975 9.985  1.00 34.46 ? 84  THR A CB    1 
ATOM   543  O  OG1   . THR A 1 75  ? 11.865 -37.577 11.266 1.00 41.86 ? 84  THR A OG1   1 
ATOM   544  C  CG2   . THR A 1 75  ? 11.616 -39.455 9.790  1.00 46.62 ? 84  THR A CG2   1 
ATOM   545  N  N     . GLY A 1 76  ? 12.931 -34.934 9.455  1.00 25.62 ? 85  GLY A N     1 
ATOM   546  C  CA    . GLY A 1 76  ? 12.785 -33.552 9.878  1.00 22.06 ? 85  GLY A CA    1 
ATOM   547  C  C     . GLY A 1 76  ? 12.499 -32.624 8.706  1.00 26.82 ? 85  GLY A C     1 
ATOM   548  O  O     . GLY A 1 76  ? 13.081 -32.745 7.628  1.00 23.61 ? 85  GLY A O     1 
ATOM   549  N  N     . ASP A 1 77  ? 11.574 -31.694 8.930  1.00 21.63 ? 86  ASP A N     1 
ATOM   550  C  CA    . ASP A 1 77  ? 11.290 -30.656 7.950  1.00 22.44 ? 86  ASP A CA    1 
ATOM   551  C  C     . ASP A 1 77  ? 12.170 -29.430 8.138  1.00 26.40 ? 86  ASP A C     1 
ATOM   552  O  O     . ASP A 1 77  ? 12.374 -28.674 7.181  1.00 24.74 ? 86  ASP A O     1 
ATOM   553  C  CB    . ASP A 1 77  ? 9.814  -30.251 8.025  1.00 20.94 ? 86  ASP A CB    1 
ATOM   554  C  CG    . ASP A 1 77  ? 8.880  -31.401 7.697  1.00 30.19 ? 86  ASP A CG    1 
ATOM   555  O  OD1   . ASP A 1 77  ? 9.174  -32.153 6.739  1.00 24.49 ? 86  ASP A OD1   1 
ATOM   556  O  OD2   . ASP A 1 77  ? 7.861  -31.557 8.401  1.00 25.27 ? 86  ASP A OD2   1 
ATOM   557  N  N     . GLY A 1 78  ? 12.690 -29.230 9.345  1.00 23.34 ? 87  GLY A N     1 
ATOM   558  C  CA    . GLY A 1 78  ? 13.591 -28.134 9.642  1.00 23.12 ? 87  GLY A CA    1 
ATOM   559  C  C     . GLY A 1 78  ? 14.356 -28.441 10.906 1.00 22.12 ? 87  GLY A C     1 
ATOM   560  O  O     . GLY A 1 78  ? 13.925 -29.253 11.732 1.00 21.86 ? 87  GLY A O     1 
ATOM   561  N  N     . PHE A 1 79  ? 15.506 -27.787 11.052 1.00 21.13 ? 88  PHE A N     1 
ATOM   562  C  CA    . PHE A 1 79  ? 16.397 -28.047 12.173 1.00 16.81 ? 88  PHE A CA    1 
ATOM   563  C  C     . PHE A 1 79  ? 16.838 -26.741 12.817 1.00 23.59 ? 88  PHE A C     1 
ATOM   564  O  O     . PHE A 1 79  ? 17.125 -25.761 12.124 1.00 20.38 ? 88  PHE A O     1 
ATOM   565  C  CB    . PHE A 1 79  ? 17.642 -28.839 11.733 1.00 18.78 ? 88  PHE A CB    1 
ATOM   566  C  CG    . PHE A 1 79  ? 17.338 -30.199 11.171 1.00 26.64 ? 88  PHE A CG    1 
ATOM   567  C  CD1   . PHE A 1 79  ? 16.919 -30.347 9.856  1.00 22.95 ? 88  PHE A CD1   1 
ATOM   568  C  CD2   . PHE A 1 79  ? 17.479 -31.334 11.958 1.00 20.82 ? 88  PHE A CD2   1 
ATOM   569  C  CE1   . PHE A 1 79  ? 16.638 -31.598 9.338  1.00 23.05 ? 88  PHE A CE1   1 
ATOM   570  C  CE2   . PHE A 1 79  ? 17.199 -32.588 11.448 1.00 22.18 ? 88  PHE A CE2   1 
ATOM   571  C  CZ    . PHE A 1 79  ? 16.777 -32.721 10.136 1.00 27.62 ? 88  PHE A CZ    1 
ATOM   572  N  N     . LEU A 1 80  ? 16.896 -26.739 14.146 1.00 19.06 ? 89  LEU A N     1 
ATOM   573  C  CA    . LEU A 1 80  ? 17.584 -25.698 14.901 1.00 23.59 ? 89  LEU A CA    1 
ATOM   574  C  C     . LEU A 1 80  ? 18.941 -26.244 15.327 1.00 17.55 ? 89  LEU A C     1 
ATOM   575  O  O     . LEU A 1 80  ? 19.007 -27.251 16.042 1.00 26.61 ? 89  LEU A O     1 
ATOM   576  C  CB    . LEU A 1 80  ? 16.777 -25.266 16.127 1.00 17.28 ? 89  LEU A CB    1 
ATOM   577  C  CG    . LEU A 1 80  ? 15.421 -24.576 15.949 1.00 21.75 ? 89  LEU A CG    1 
ATOM   578  C  CD1   . LEU A 1 80  ? 14.843 -24.198 17.308 1.00 19.31 ? 89  LEU A CD1   1 
ATOM   579  C  CD2   . LEU A 1 80  ? 15.525 -23.349 15.057 1.00 17.68 ? 89  LEU A CD2   1 
ATOM   580  N  N     . ILE A 1 81  ? 20.013 -25.596 14.877 1.00 26.48 ? 90  ILE A N     1 
ATOM   581  C  CA    . ILE A 1 81  ? 21.369 -25.928 15.311 1.00 23.02 ? 90  ILE A CA    1 
ATOM   582  C  C     . ILE A 1 81  ? 21.722 -24.993 16.460 1.00 24.60 ? 90  ILE A C     1 
ATOM   583  O  O     . ILE A 1 81  ? 21.988 -23.807 16.246 1.00 28.77 ? 90  ILE A O     1 
ATOM   584  C  CB    . ILE A 1 81  ? 22.392 -25.793 14.179 1.00 22.71 ? 90  ILE A CB    1 
ATOM   585  C  CG1   . ILE A 1 81  ? 22.108 -26.763 13.043 1.00 21.80 ? 90  ILE A CG1   1 
ATOM   586  C  CG2   . ILE A 1 81  ? 23.796 -26.066 14.705 1.00 22.35 ? 90  ILE A CG2   1 
ATOM   587  C  CD1   . ILE A 1 81  ? 23.212 -26.736 12.002 1.00 29.00 ? 90  ILE A CD1   1 
ATOM   588  N  N     . VAL A 1 82  ? 21.749 -25.530 17.675 1.00 26.19 ? 91  VAL A N     1 
ATOM   589  C  CA    . VAL A 1 82  ? 21.924 -24.737 18.884 1.00 24.00 ? 91  VAL A CA    1 
ATOM   590  C  C     . VAL A 1 82  ? 23.356 -24.880 19.372 1.00 28.99 ? 91  VAL A C     1 
ATOM   591  O  O     . VAL A 1 82  ? 23.884 -25.996 19.461 1.00 27.55 ? 91  VAL A O     1 
ATOM   592  C  CB    . VAL A 1 82  ? 20.936 -25.171 19.979 1.00 27.42 ? 91  VAL A CB    1 
ATOM   593  C  CG1   . VAL A 1 82  ? 21.048 -24.254 21.191 1.00 21.55 ? 91  VAL A CG1   1 
ATOM   594  C  CG2   . VAL A 1 82  ? 19.515 -25.199 19.432 1.00 18.96 ? 91  VAL A CG2   1 
ATOM   595  N  N     . TYR A 1 83  ? 23.986 -23.755 19.694 1.00 24.36 ? 92  TYR A N     1 
ATOM   596  C  CA    . TYR A 1 83  ? 25.214 -23.764 20.470 1.00 27.99 ? 92  TYR A CA    1 
ATOM   597  C  C     . TYR A 1 83  ? 25.057 -22.794 21.630 1.00 31.29 ? 92  TYR A C     1 
ATOM   598  O  O     . TYR A 1 83  ? 24.098 -22.018 21.699 1.00 34.21 ? 92  TYR A O     1 
ATOM   599  C  CB    . TYR A 1 83  ? 26.447 -23.410 19.622 1.00 24.05 ? 92  TYR A CB    1 
ATOM   600  C  CG    . TYR A 1 83  ? 26.524 -21.972 19.161 1.00 26.26 ? 92  TYR A CG    1 
ATOM   601  C  CD1   . TYR A 1 83  ? 25.915 -21.568 17.978 1.00 29.38 ? 92  TYR A CD1   1 
ATOM   602  C  CD2   . TYR A 1 83  ? 27.228 -21.020 19.895 1.00 28.30 ? 92  TYR A CD2   1 
ATOM   603  C  CE1   . TYR A 1 83  ? 25.992 -20.256 17.543 1.00 28.72 ? 92  TYR A CE1   1 
ATOM   604  C  CE2   . TYR A 1 83  ? 27.307 -19.706 19.472 1.00 28.31 ? 92  TYR A CE2   1 
ATOM   605  C  CZ    . TYR A 1 83  ? 26.688 -19.331 18.293 1.00 31.49 ? 92  TYR A CZ    1 
ATOM   606  O  OH    . TYR A 1 83  ? 26.766 -18.028 17.862 1.00 27.85 ? 92  TYR A OH    1 
ATOM   607  N  N     . SER A 1 84  ? 26.000 -22.868 22.559 1.00 26.21 ? 93  SER A N     1 
ATOM   608  C  CA    . SER A 1 84  ? 26.039 -21.984 23.713 1.00 34.27 ? 93  SER A CA    1 
ATOM   609  C  C     . SER A 1 84  ? 27.139 -20.954 23.508 1.00 38.20 ? 93  SER A C     1 
ATOM   610  O  O     . SER A 1 84  ? 28.278 -21.313 23.188 1.00 32.44 ? 93  SER A O     1 
ATOM   611  C  CB    . SER A 1 84  ? 26.285 -22.772 24.998 1.00 29.52 ? 93  SER A CB    1 
ATOM   612  O  OG    . SER A 1 84  ? 26.598 -21.903 26.073 1.00 31.83 ? 93  SER A OG    1 
ATOM   613  N  N     . VAL A 1 85  ? 26.797 -19.675 23.688 1.00 31.21 ? 94  VAL A N     1 
ATOM   614  C  CA    . VAL A 1 85  ? 27.786 -18.615 23.527 1.00 31.30 ? 94  VAL A CA    1 
ATOM   615  C  C     . VAL A 1 85  ? 28.863 -18.648 24.600 1.00 35.00 ? 94  VAL A C     1 
ATOM   616  O  O     . VAL A 1 85  ? 29.849 -17.910 24.498 1.00 34.50 ? 94  VAL A O     1 
ATOM   617  C  CB    . VAL A 1 85  ? 27.101 -17.234 23.507 1.00 30.26 ? 94  VAL A CB    1 
ATOM   618  C  CG1   . VAL A 1 85  ? 26.206 -17.113 22.283 1.00 26.78 ? 94  VAL A CG1   1 
ATOM   619  C  CG2   . VAL A 1 85  ? 26.308 -17.019 24.781 1.00 29.30 ? 94  VAL A CG2   1 
ATOM   620  N  N     . THR A 1 86  ? 28.702 -19.484 25.625 1.00 32.87 ? 95  THR A N     1 
ATOM   621  C  CA    . THR A 1 86  ? 29.725 -19.698 26.640 1.00 37.91 ? 95  THR A CA    1 
ATOM   622  C  C     . THR A 1 86  ? 30.538 -20.959 26.393 1.00 39.03 ? 95  THR A C     1 
ATOM   623  O  O     . THR A 1 86  ? 31.448 -21.256 27.174 1.00 41.19 ? 95  THR A O     1 
ATOM   624  C  CB    . THR A 1 86  ? 29.093 -19.778 28.032 1.00 38.91 ? 95  THR A CB    1 
ATOM   625  O  OG1   . THR A 1 86  ? 28.336 -20.991 28.141 1.00 43.54 ? 95  THR A OG1   1 
ATOM   626  C  CG2   . THR A 1 86  ? 28.176 -18.588 28.273 1.00 37.84 ? 95  THR A CG2   1 
ATOM   627  N  N     . ASP A 1 87  ? 30.231 -21.706 25.336 1.00 33.64 ? 96  ASP A N     1 
ATOM   628  C  CA    . ASP A 1 87  ? 30.892 -22.972 25.036 1.00 34.40 ? 96  ASP A CA    1 
ATOM   629  C  C     . ASP A 1 87  ? 31.514 -22.868 23.649 1.00 40.02 ? 96  ASP A C     1 
ATOM   630  O  O     . ASP A 1 87  ? 30.801 -22.910 22.640 1.00 34.32 ? 96  ASP A O     1 
ATOM   631  C  CB    . ASP A 1 87  ? 29.897 -24.131 25.120 1.00 35.12 ? 96  ASP A CB    1 
ATOM   632  C  CG    . ASP A 1 87  ? 30.555 -25.492 24.967 1.00 33.33 ? 96  ASP A CG    1 
ATOM   633  O  OD1   . ASP A 1 87  ? 31.746 -25.559 24.613 1.00 43.29 ? 96  ASP A OD1   1 
ATOM   634  O  OD2   . ASP A 1 87  ? 29.872 -26.508 25.208 1.00 42.56 ? 96  ASP A OD2   1 
ATOM   635  N  N     . LYS A 1 88  ? 32.843 -22.729 23.604 1.00 37.76 ? 97  LYS A N     1 
ATOM   636  C  CA    . LYS A 1 88  ? 33.543 -22.659 22.325 1.00 37.38 ? 97  LYS A CA    1 
ATOM   637  C  C     . LYS A 1 88  ? 33.391 -23.953 21.537 1.00 35.57 ? 97  LYS A C     1 
ATOM   638  O  O     . LYS A 1 88  ? 33.141 -23.922 20.326 1.00 40.31 ? 97  LYS A O     1 
ATOM   639  C  CB    . LYS A 1 88  ? 35.027 -22.351 22.547 1.00 44.37 ? 97  LYS A CB    1 
ATOM   640  C  CG    . LYS A 1 88  ? 35.354 -20.895 22.849 1.00 47.49 ? 97  LYS A CG    1 
ATOM   641  C  CD    . LYS A 1 88  ? 36.858 -20.710 23.031 1.00 52.91 ? 97  LYS A CD    1 
ATOM   642  C  CE    . LYS A 1 88  ? 37.233 -19.249 23.260 1.00 60.63 ? 97  LYS A CE    1 
ATOM   643  N  NZ    . LYS A 1 88  ? 36.843 -18.383 22.107 1.00 60.44 ? 97  LYS A NZ    1 
ATOM   644  N  N     . ALA A 1 89  ? 33.547 -25.099 22.203 1.00 35.30 ? 98  ALA A N     1 
ATOM   645  C  CA    . ALA A 1 89  ? 33.464 -26.378 21.506 1.00 37.37 ? 98  ALA A CA    1 
ATOM   646  C  C     . ALA A 1 89  ? 32.096 -26.572 20.864 1.00 31.54 ? 98  ALA A C     1 
ATOM   647  O  O     . ALA A 1 89  ? 31.996 -27.088 19.745 1.00 37.62 ? 98  ALA A O     1 
ATOM   648  C  CB    . ALA A 1 89  ? 33.776 -27.520 22.471 1.00 36.62 ? 98  ALA A CB    1 
ATOM   649  N  N     . SER A 1 90  ? 31.030 -26.159 21.553 1.00 33.91 ? 99  SER A N     1 
ATOM   650  C  CA    . SER A 1 90  ? 29.695 -26.286 20.975 1.00 36.44 ? 99  SER A CA    1 
ATOM   651  C  C     . SER A 1 90  ? 29.538 -25.409 19.739 1.00 32.11 ? 99  SER A C     1 
ATOM   652  O  O     . SER A 1 90  ? 28.795 -25.765 18.818 1.00 31.85 ? 99  SER A O     1 
ATOM   653  C  CB    . SER A 1 90  ? 28.633 -25.942 22.016 1.00 27.54 ? 99  SER A CB    1 
ATOM   654  O  OG    . SER A 1 90  ? 28.489 -24.541 22.175 1.00 33.31 ? 99  SER A OG    1 
ATOM   655  N  N     . PHE A 1 91  ? 30.235 -24.270 19.699 1.00 32.05 ? 100 PHE A N     1 
ATOM   656  C  CA    . PHE A 1 91  ? 30.211 -23.414 18.516 1.00 34.82 ? 100 PHE A CA    1 
ATOM   657  C  C     . PHE A 1 91  ? 30.994 -24.041 17.368 1.00 38.61 ? 100 PHE A C     1 
ATOM   658  O  O     . PHE A 1 91  ? 30.550 -24.009 16.216 1.00 41.46 ? 100 PHE A O     1 
ATOM   659  C  CB    . PHE A 1 91  ? 30.771 -22.034 18.873 1.00 31.43 ? 100 PHE A CB    1 
ATOM   660  C  CG    . PHE A 1 91  ? 30.806 -21.055 17.728 1.00 28.63 ? 100 PHE A CG    1 
ATOM   661  C  CD1   . PHE A 1 91  ? 29.635 -20.617 17.128 1.00 30.02 ? 100 PHE A CD1   1 
ATOM   662  C  CD2   . PHE A 1 91  ? 32.012 -20.538 17.282 1.00 34.07 ? 100 PHE A CD2   1 
ATOM   663  C  CE1   . PHE A 1 91  ? 29.666 -19.700 16.089 1.00 29.69 ? 100 PHE A CE1   1 
ATOM   664  C  CE2   . PHE A 1 91  ? 32.052 -19.620 16.244 1.00 35.10 ? 100 PHE A CE2   1 
ATOM   665  C  CZ    . PHE A 1 91  ? 30.875 -19.199 15.650 1.00 30.62 ? 100 PHE A CZ    1 
ATOM   666  N  N     . GLU A 1 92  ? 32.156 -24.625 17.665 1.00 38.13 ? 101 GLU A N     1 
ATOM   667  C  CA    . GLU A 1 92  ? 32.936 -25.277 16.620 1.00 45.54 ? 101 GLU A CA    1 
ATOM   668  C  C     . GLU A 1 92  ? 32.199 -26.473 16.033 1.00 44.82 ? 101 GLU A C     1 
ATOM   669  O  O     . GLU A 1 92  ? 32.342 -26.762 14.840 1.00 46.64 ? 101 GLU A O     1 
ATOM   670  C  CB    . GLU A 1 92  ? 34.295 -25.707 17.169 1.00 47.60 ? 101 GLU A CB    1 
ATOM   671  C  CG    . GLU A 1 92  ? 35.144 -24.552 17.681 1.00 63.47 ? 101 GLU A CG    1 
ATOM   672  C  CD    . GLU A 1 92  ? 35.560 -23.597 16.577 1.00 71.44 ? 101 GLU A CD    1 
ATOM   673  O  OE1   . GLU A 1 92  ? 35.819 -24.070 15.449 1.00 71.49 ? 101 GLU A OE1   1 
ATOM   674  O  OE2   . GLU A 1 92  ? 35.625 -22.375 16.837 1.00 73.15 ? 101 GLU A OE2   1 
ATOM   675  N  N     . HIS A 1 93  ? 31.398 -27.165 16.841 1.00 40.44 ? 102 HIS A N     1 
ATOM   676  C  CA    . HIS A 1 93  ? 30.677 -28.338 16.369 1.00 35.33 ? 102 HIS A CA    1 
ATOM   677  C  C     . HIS A 1 93  ? 29.493 -27.991 15.476 1.00 33.25 ? 102 HIS A C     1 
ATOM   678  O  O     . HIS A 1 93  ? 28.824 -28.909 14.987 1.00 36.51 ? 102 HIS A O     1 
ATOM   679  C  CB    . HIS A 1 93  ? 30.217 -29.177 17.563 1.00 35.84 ? 102 HIS A CB    1 
ATOM   680  C  CG    . HIS A 1 93  ? 31.345 -29.810 18.319 1.00 45.00 ? 102 HIS A CG    1 
ATOM   681  N  ND1   . HIS A 1 93  ? 31.170 -30.451 19.526 1.00 40.72 ? 102 HIS A ND1   1 
ATOM   682  C  CD2   . HIS A 1 93  ? 32.666 -29.898 18.035 1.00 51.50 ? 102 HIS A CD2   1 
ATOM   683  C  CE1   . HIS A 1 93  ? 32.333 -30.909 19.953 1.00 51.42 ? 102 HIS A CE1   1 
ATOM   684  N  NE2   . HIS A 1 93  ? 33.258 -30.587 19.066 1.00 56.22 ? 102 HIS A NE2   1 
ATOM   685  N  N     . VAL A 1 94  ? 29.222 -26.702 15.248 1.00 29.42 ? 103 VAL A N     1 
ATOM   686  C  CA    . VAL A 1 94  ? 28.167 -26.311 14.315 1.00 29.75 ? 103 VAL A CA    1 
ATOM   687  C  C     . VAL A 1 94  ? 28.467 -26.837 12.917 1.00 32.68 ? 103 VAL A C     1 
ATOM   688  O  O     . VAL A 1 94  ? 27.566 -27.291 12.204 1.00 28.27 ? 103 VAL A O     1 
ATOM   689  C  CB    . VAL A 1 94  ? 27.990 -24.781 14.317 1.00 31.58 ? 103 VAL A CB    1 
ATOM   690  C  CG1   . VAL A 1 94  ? 27.125 -24.335 13.148 1.00 27.59 ? 103 VAL A CG1   1 
ATOM   691  C  CG2   . VAL A 1 94  ? 27.387 -24.316 15.631 1.00 24.76 ? 103 VAL A CG2   1 
ATOM   692  N  N     . ASP A 1 95  ? 29.737 -26.787 12.504 1.00 32.99 ? 104 ASP A N     1 
ATOM   693  C  CA    . ASP A 1 95  ? 30.103 -27.316 11.193 1.00 37.10 ? 104 ASP A CA    1 
ATOM   694  C  C     . ASP A 1 95  ? 29.725 -28.788 11.070 1.00 39.47 ? 104 ASP A C     1 
ATOM   695  O  O     . ASP A 1 95  ? 29.267 -29.235 10.011 1.00 33.85 ? 104 ASP A O     1 
ATOM   696  C  CB    . ASP A 1 95  ? 31.603 -27.130 10.941 1.00 37.46 ? 104 ASP A CB    1 
ATOM   697  C  CG    . ASP A 1 95  ? 32.056 -25.686 11.107 1.00 39.03 ? 104 ASP A CG    1 
ATOM   698  O  OD1   . ASP A 1 95  ? 31.208 -24.774 11.042 1.00 43.63 ? 104 ASP A OD1   1 
ATOM   699  O  OD2   . ASP A 1 95  ? 33.270 -25.463 11.301 1.00 49.40 ? 104 ASP A OD2   1 
ATOM   700  N  N     . ARG A 1 96  ? 29.900 -29.555 12.150 1.00 33.16 ? 105 ARG A N     1 
ATOM   701  C  CA    . ARG A 1 96  ? 29.604 -30.983 12.109 1.00 34.20 ? 105 ARG A CA    1 
ATOM   702  C  C     . ARG A 1 96  ? 28.105 -31.236 11.989 1.00 33.58 ? 105 ARG A C     1 
ATOM   703  O  O     . ARG A 1 96  ? 27.677 -32.088 11.201 1.00 30.53 ? 105 ARG A O     1 
ATOM   704  C  CB    . ARG A 1 96  ? 30.173 -31.662 13.356 1.00 42.05 ? 105 ARG A CB    1 
ATOM   705  C  CG    . ARG A 1 96  ? 30.107 -33.185 13.350 1.00 54.75 ? 105 ARG A CG    1 
ATOM   706  C  CD    . ARG A 1 96  ? 29.374 -33.699 14.584 1.00 66.74 ? 105 ARG A CD    1 
ATOM   707  N  NE    . ARG A 1 96  ? 29.410 -35.153 14.703 1.00 68.37 ? 105 ARG A NE    1 
ATOM   708  C  CZ    . ARG A 1 96  ? 28.660 -35.850 15.548 1.00 66.60 ? 105 ARG A CZ    1 
ATOM   709  N  NH1   . ARG A 1 96  ? 27.797 -35.257 16.357 1.00 62.28 ? 105 ARG A NH1   1 
ATOM   710  N  NH2   . ARG A 1 96  ? 28.774 -37.176 15.575 1.00 67.46 ? 105 ARG A NH2   1 
ATOM   711  N  N     . PHE A 1 97  ? 27.291 -30.507 12.758 1.00 30.67 ? 106 PHE A N     1 
ATOM   712  C  CA    . PHE A 1 97  ? 25.846 -30.711 12.691 1.00 31.64 ? 106 PHE A CA    1 
ATOM   713  C  C     . PHE A 1 97  ? 25.294 -30.334 11.321 1.00 29.32 ? 106 PHE A C     1 
ATOM   714  O  O     . PHE A 1 97  ? 24.455 -31.053 10.767 1.00 30.27 ? 106 PHE A O     1 
ATOM   715  C  CB    . PHE A 1 97  ? 25.141 -29.917 13.792 1.00 29.57 ? 106 PHE A CB    1 
ATOM   716  C  CG    . PHE A 1 97  ? 25.342 -30.480 15.169 1.00 32.54 ? 106 PHE A CG    1 
ATOM   717  C  CD1   . PHE A 1 97  ? 24.853 -31.739 15.495 1.00 32.69 ? 106 PHE A CD1   1 
ATOM   718  C  CD2   . PHE A 1 97  ? 26.014 -29.753 16.140 1.00 26.31 ? 106 PHE A CD2   1 
ATOM   719  C  CE1   . PHE A 1 97  ? 25.039 -32.270 16.760 1.00 31.62 ? 106 PHE A CE1   1 
ATOM   720  C  CE2   . PHE A 1 97  ? 26.205 -30.278 17.412 1.00 30.51 ? 106 PHE A CE2   1 
ATOM   721  C  CZ    . PHE A 1 97  ? 25.714 -31.538 17.722 1.00 30.31 ? 106 PHE A CZ    1 
ATOM   722  N  N     . HIS A 1 98  ? 25.752 -29.218 10.753 1.00 29.43 ? 107 HIS A N     1 
ATOM   723  C  CA    . HIS A 1 98  ? 25.247 -28.805 9.448  1.00 33.00 ? 107 HIS A CA    1 
ATOM   724  C  C     . HIS A 1 98  ? 25.631 -29.808 8.366  1.00 26.81 ? 107 HIS A C     1 
ATOM   725  O  O     . HIS A 1 98  ? 24.790 -30.201 7.550  1.00 29.98 ? 107 HIS A O     1 
ATOM   726  C  CB    . HIS A 1 98  ? 25.763 -27.408 9.095  1.00 31.33 ? 107 HIS A CB    1 
ATOM   727  C  CG    . HIS A 1 98  ? 25.024 -26.763 7.963  1.00 37.56 ? 107 HIS A CG    1 
ATOM   728  N  ND1   . HIS A 1 98  ? 25.644 -26.356 6.801  1.00 31.65 ? 107 HIS A ND1   1 
ATOM   729  C  CD2   . HIS A 1 98  ? 23.711 -26.466 7.812  1.00 34.44 ? 107 HIS A CD2   1 
ATOM   730  C  CE1   . HIS A 1 98  ? 24.747 -25.829 5.987  1.00 32.36 ? 107 HIS A CE1   1 
ATOM   731  N  NE2   . HIS A 1 98  ? 23.565 -25.885 6.575  1.00 30.50 ? 107 HIS A NE2   1 
ATOM   732  N  N     . GLN A 1 99  ? 26.891 -30.245 8.356  1.00 28.68 ? 108 GLN A N     1 
ATOM   733  C  CA    . GLN A 1 99  ? 27.330 -31.214 7.359  1.00 31.50 ? 108 GLN A CA    1 
ATOM   734  C  C     . GLN A 1 99  ? 26.597 -32.539 7.514  1.00 33.60 ? 108 GLN A C     1 
ATOM   735  O  O     . GLN A 1 99  ? 26.200 -33.158 6.520  1.00 32.35 ? 108 GLN A O     1 
ATOM   736  C  CB    . GLN A 1 99  ? 28.839 -31.423 7.468  1.00 32.04 ? 108 GLN A CB    1 
ATOM   737  C  CG    . GLN A 1 99  ? 29.374 -32.476 6.526  1.00 39.65 ? 108 GLN A CG    1 
ATOM   738  C  CD    . GLN A 1 99  ? 30.829 -32.785 6.782  1.00 39.50 ? 108 GLN A CD    1 
ATOM   739  O  OE1   . GLN A 1 99  ? 31.519 -32.033 7.468  1.00 56.39 ? 108 GLN A OE1   1 
ATOM   740  N  NE2   . GLN A 1 99  ? 31.304 -33.897 6.240  1.00 55.50 ? 108 GLN A NE2   1 
ATOM   741  N  N     . LEU A 1 100 ? 26.403 -32.988 8.754  1.00 32.40 ? 109 LEU A N     1 
ATOM   742  C  CA    . LEU A 1 100 ? 25.795 -34.294 8.977  1.00 33.99 ? 109 LEU A CA    1 
ATOM   743  C  C     . LEU A 1 100 ? 24.345 -34.313 8.512  1.00 35.24 ? 109 LEU A C     1 
ATOM   744  O  O     . LEU A 1 100 ? 23.901 -35.280 7.882  1.00 31.34 ? 109 LEU A O     1 
ATOM   745  C  CB    . LEU A 1 100 ? 25.897 -34.663 10.456 1.00 41.33 ? 109 LEU A CB    1 
ATOM   746  C  CG    . LEU A 1 100 ? 25.506 -36.078 10.871 1.00 48.38 ? 109 LEU A CG    1 
ATOM   747  C  CD1   . LEU A 1 100 ? 26.426 -37.100 10.226 1.00 39.94 ? 109 LEU A CD1   1 
ATOM   748  C  CD2   . LEU A 1 100 ? 25.550 -36.191 12.382 1.00 50.43 ? 109 LEU A CD2   1 
ATOM   749  N  N     . ILE A 1 101 ? 23.595 -33.249 8.803  1.00 26.21 ? 110 ILE A N     1 
ATOM   750  C  CA    . ILE A 1 101 ? 22.201 -33.183 8.376  1.00 30.65 ? 110 ILE A CA    1 
ATOM   751  C  C     . ILE A 1 101 ? 22.104 -33.069 6.858  1.00 32.15 ? 110 ILE A C     1 
ATOM   752  O  O     . ILE A 1 101 ? 21.251 -33.708 6.229  1.00 29.56 ? 110 ILE A O     1 
ATOM   753  C  CB    . ILE A 1 101 ? 21.491 -32.023 9.095  1.00 32.14 ? 110 ILE A CB    1 
ATOM   754  C  CG1   . ILE A 1 101 ? 21.410 -32.353 10.587 1.00 34.61 ? 110 ILE A CG1   1 
ATOM   755  C  CG2   . ILE A 1 101 ? 20.118 -31.777 8.489  1.00 28.95 ? 110 ILE A CG2   1 
ATOM   756  C  CD1   . ILE A 1 101 ? 21.018 -31.225 11.474 1.00 25.12 ? 110 ILE A CD1   1 
ATOM   757  N  N     . LEU A 1 102 ? 22.977 -32.269 6.242  1.00 27.56 ? 111 LEU A N     1 
ATOM   758  C  CA    . LEU A 1 102 ? 22.973 -32.183 4.785  1.00 28.04 ? 111 LEU A CA    1 
ATOM   759  C  C     . LEU A 1 102 ? 23.333 -33.523 4.154  1.00 35.34 ? 111 LEU A C     1 
ATOM   760  O  O     . LEU A 1 102 ? 22.760 -33.907 3.128  1.00 35.25 ? 111 LEU A O     1 
ATOM   761  C  CB    . LEU A 1 102 ? 23.928 -31.089 4.313  1.00 28.03 ? 111 LEU A CB    1 
ATOM   762  C  CG    . LEU A 1 102 ? 23.533 -29.646 4.630  1.00 30.95 ? 111 LEU A CG    1 
ATOM   763  C  CD1   . LEU A 1 102 ? 24.517 -28.694 3.969  1.00 34.52 ? 111 LEU A CD1   1 
ATOM   764  C  CD2   . LEU A 1 102 ? 22.103 -29.342 4.188  1.00 25.54 ? 111 LEU A CD2   1 
ATOM   765  N  N     . ARG A 1 103 ? 24.271 -34.254 4.761  1.00 30.80 ? 112 ARG A N     1 
ATOM   766  C  CA    . ARG A 1 103 ? 24.634 -35.570 4.244  1.00 33.20 ? 112 ARG A CA    1 
ATOM   767  C  C     . ARG A 1 103 ? 23.446 -36.524 4.283  1.00 34.50 ? 112 ARG A C     1 
ATOM   768  O  O     . ARG A 1 103 ? 23.171 -37.229 3.306  1.00 41.51 ? 112 ARG A O     1 
ATOM   769  C  CB    . ARG A 1 103 ? 25.806 -36.147 5.037  1.00 34.76 ? 112 ARG A CB    1 
ATOM   770  C  CG    . ARG A 1 103 ? 26.082 -37.606 4.714  1.00 45.80 ? 112 ARG A CG    1 
ATOM   771  C  CD    . ARG A 1 103 ? 27.276 -38.148 5.481  1.00 47.90 ? 112 ARG A CD    1 
ATOM   772  N  NE    . ARG A 1 103 ? 27.482 -39.568 5.217  1.00 58.30 ? 112 ARG A NE    1 
ATOM   773  C  CZ    . ARG A 1 103 ? 28.179 -40.048 4.195  1.00 61.44 ? 112 ARG A CZ    1 
ATOM   774  N  NH1   . ARG A 1 103 ? 28.746 -39.247 3.307  1.00 59.91 ? 112 ARG A NH1   1 
ATOM   775  N  NH2   . ARG A 1 103 ? 28.312 -41.367 4.061  1.00 66.90 ? 112 ARG A NH2   1 
ATOM   776  N  N     . VAL A 1 104 ? 22.737 -36.566 5.414  1.00 31.12 ? 113 VAL A N     1 
ATOM   777  C  CA    . VAL A 1 104 ? 21.574 -37.444 5.535  1.00 39.68 ? 113 VAL A CA    1 
ATOM   778  C  C     . VAL A 1 104 ? 20.520 -37.070 4.502  1.00 35.38 ? 113 VAL A C     1 
ATOM   779  O  O     . VAL A 1 104 ? 19.971 -37.932 3.808  1.00 42.61 ? 113 VAL A O     1 
ATOM   780  C  CB    . VAL A 1 104 ? 21.006 -37.388 6.966  1.00 42.30 ? 113 VAL A CB    1 
ATOM   781  C  CG1   . VAL A 1 104 ? 19.676 -38.123 7.038  1.00 42.35 ? 113 VAL A CG1   1 
ATOM   782  C  CG2   . VAL A 1 104 ? 21.995 -37.984 7.957  1.00 38.30 ? 113 VAL A CG2   1 
ATOM   783  N  N     . LYS A 1 105 ? 20.234 -35.772 4.376  1.00 40.46 ? 114 LYS A N     1 
ATOM   784  C  CA    . LYS A 1 105 ? 19.251 -35.303 3.407  1.00 33.34 ? 114 LYS A CA    1 
ATOM   785  C  C     . LYS A 1 105 ? 19.726 -35.456 1.969  1.00 38.67 ? 114 LYS A C     1 
ATOM   786  O  O     . LYS A 1 105 ? 18.896 -35.416 1.054  1.00 40.05 ? 114 LYS A O     1 
ATOM   787  C  CB    . LYS A 1 105 ? 18.910 -33.838 3.679  1.00 31.27 ? 114 LYS A CB    1 
ATOM   788  C  CG    . LYS A 1 105 ? 18.111 -33.604 4.948  1.00 27.42 ? 114 LYS A CG    1 
ATOM   789  C  CD    . LYS A 1 105 ? 16.724 -34.203 4.820  1.00 33.55 ? 114 LYS A CD    1 
ATOM   790  C  CE    . LYS A 1 105 ? 15.855 -33.863 6.011  1.00 24.94 ? 114 LYS A CE    1 
ATOM   791  N  NZ    . LYS A 1 105 ? 14.447 -34.292 5.775  1.00 30.67 ? 114 LYS A NZ    1 
ATOM   792  N  N     . ASP A 1 106 ? 21.031 -35.635 1.752  1.00 36.97 ? 115 ASP A N     1 
ATOM   793  C  CA    . ASP A 1 106 ? 21.626 -35.626 0.415  1.00 40.65 ? 115 ASP A CA    1 
ATOM   794  C  C     . ASP A 1 106 ? 21.239 -34.350 -0.331 1.00 39.24 ? 115 ASP A C     1 
ATOM   795  O  O     . ASP A 1 106 ? 20.786 -34.374 -1.479 1.00 49.41 ? 115 ASP A O     1 
ATOM   796  C  CB    . ASP A 1 106 ? 21.235 -36.875 -0.379 1.00 38.54 ? 115 ASP A CB    1 
ATOM   797  C  CG    . ASP A 1 106 ? 22.102 -37.081 -1.606 1.00 42.99 ? 115 ASP A CG    1 
ATOM   798  O  OD1   . ASP A 1 106 ? 23.174 -36.449 -1.695 1.00 50.50 ? 115 ASP A OD1   1 
ATOM   799  O  OD2   . ASP A 1 106 ? 21.712 -37.868 -2.489 1.00 52.87 ? 115 ASP A OD2   1 
ATOM   800  N  N     . ARG A 1 107 ? 21.423 -33.220 0.347  1.00 35.93 ? 116 ARG A N     1 
ATOM   801  C  CA    . ARG A 1 107 ? 21.045 -31.912 -0.164 1.00 43.18 ? 116 ARG A CA    1 
ATOM   802  C  C     . ARG A 1 107 ? 22.167 -30.920 0.103  1.00 34.09 ? 116 ARG A C     1 
ATOM   803  O  O     . ARG A 1 107 ? 22.923 -31.065 1.066  1.00 36.47 ? 116 ARG A O     1 
ATOM   804  C  CB    . ARG A 1 107 ? 19.751 -31.413 0.493  1.00 39.47 ? 116 ARG A CB    1 
ATOM   805  C  CG    . ARG A 1 107 ? 18.546 -32.283 0.214  1.00 41.26 ? 116 ARG A CG    1 
ATOM   806  C  CD    . ARG A 1 107 ? 17.902 -31.891 -1.096 1.00 47.85 ? 116 ARG A CD    1 
ATOM   807  N  NE    . ARG A 1 107 ? 17.551 -30.476 -1.085 1.00 53.74 ? 116 ARG A NE    1 
ATOM   808  C  CZ    . ARG A 1 107 ? 16.484 -29.976 -0.477 1.00 43.81 ? 116 ARG A CZ    1 
ATOM   809  N  NH1   . ARG A 1 107 ? 15.627 -30.753 0.166  1.00 46.12 ? 116 ARG A NH1   1 
ATOM   810  N  NH2   . ARG A 1 107 ? 16.273 -28.664 -0.512 1.00 52.93 ? 116 ARG A NH2   1 
ATOM   811  N  N     . GLU A 1 108 ? 22.267 -29.907 -0.760 1.00 36.04 ? 117 GLU A N     1 
ATOM   812  C  CA    . GLU A 1 108 ? 23.215 -28.823 -0.531 1.00 39.75 ? 117 GLU A CA    1 
ATOM   813  C  C     . GLU A 1 108 ? 22.691 -27.790 0.450  1.00 30.94 ? 117 GLU A C     1 
ATOM   814  O  O     . GLU A 1 108 ? 23.492 -27.084 1.070  1.00 37.64 ? 117 GLU A O     1 
ATOM   815  C  CB    . GLU A 1 108 ? 23.561 -28.118 -1.840 1.00 33.90 ? 117 GLU A CB    1 
ATOM   816  C  CG    . GLU A 1 108 ? 24.254 -28.984 -2.839 1.00 36.66 ? 117 GLU A CG    1 
ATOM   817  C  CD    . GLU A 1 108 ? 24.870 -28.172 -3.954 1.00 41.15 ? 117 GLU A CD    1 
ATOM   818  O  OE1   . GLU A 1 108 ? 24.974 -26.934 -3.804 1.00 41.19 ? 117 GLU A OE1   1 
ATOM   819  O  OE2   . GLU A 1 108 ? 25.251 -28.773 -4.977 1.00 47.12 ? 117 GLU A OE2   1 
ATOM   820  N  N     . SER A 1 109 ? 21.373 -27.680 0.591  1.00 33.30 ? 118 SER A N     1 
ATOM   821  C  CA    . SER A 1 109 ? 20.766 -26.771 1.548  1.00 32.59 ? 118 SER A CA    1 
ATOM   822  C  C     . SER A 1 109 ? 19.462 -27.380 2.040  1.00 27.87 ? 118 SER A C     1 
ATOM   823  O  O     . SER A 1 109 ? 18.817 -28.160 1.335  1.00 31.12 ? 118 SER A O     1 
ATOM   824  C  CB    . SER A 1 109 ? 20.509 -25.390 0.937  1.00 28.96 ? 118 SER A CB    1 
ATOM   825  O  OG    . SER A 1 109 ? 19.571 -25.480 -0.121 1.00 43.30 ? 118 SER A OG    1 
ATOM   826  N  N     . PHE A 1 110 ? 19.082 -27.011 3.259  1.00 25.85 ? 119 PHE A N     1 
ATOM   827  C  CA    . PHE A 1 110 ? 17.855 -27.497 3.872  1.00 27.86 ? 119 PHE A CA    1 
ATOM   828  C  C     . PHE A 1 110 ? 17.463 -26.514 4.963  1.00 28.73 ? 119 PHE A C     1 
ATOM   829  O  O     . PHE A 1 110 ? 18.346 -25.922 5.593  1.00 30.60 ? 119 PHE A O     1 
ATOM   830  C  CB    . PHE A 1 110 ? 18.045 -28.908 4.452  1.00 21.61 ? 119 PHE A CB    1 
ATOM   831  C  CG    . PHE A 1 110 ? 16.757 -29.601 4.782  1.00 21.86 ? 119 PHE A CG    1 
ATOM   832  C  CD1   . PHE A 1 110 ? 16.027 -30.236 3.791  1.00 21.57 ? 119 PHE A CD1   1 
ATOM   833  C  CD2   . PHE A 1 110 ? 16.267 -29.603 6.077  1.00 21.00 ? 119 PHE A CD2   1 
ATOM   834  C  CE1   . PHE A 1 110 ? 14.837 -30.867 4.085  1.00 31.30 ? 119 PHE A CE1   1 
ATOM   835  C  CE2   . PHE A 1 110 ? 15.076 -30.232 6.379  1.00 24.18 ? 119 PHE A CE2   1 
ATOM   836  C  CZ    . PHE A 1 110 ? 14.359 -30.862 5.381  1.00 27.48 ? 119 PHE A CZ    1 
ATOM   837  N  N     . PRO A 1 111 ? 16.150 -26.297 5.196  1.00 28.87 ? 120 PRO A N     1 
ATOM   838  C  CA    . PRO A 1 111 ? 15.725 -25.322 6.214  1.00 24.51 ? 120 PRO A CA    1 
ATOM   839  C  C     . PRO A 1 111 ? 16.350 -25.543 7.581  1.00 24.72 ? 120 PRO A C     1 
ATOM   840  O  O     . PRO A 1 111 ? 16.064 -26.535 8.260  1.00 25.86 ? 120 PRO A O     1 
ATOM   841  C  CB    . PRO A 1 111 ? 14.207 -25.519 6.265  1.00 19.03 ? 120 PRO A CB    1 
ATOM   842  C  CG    . PRO A 1 111 ? 13.857 -25.952 4.905  1.00 27.25 ? 120 PRO A CG    1 
ATOM   843  C  CD    . PRO A 1 111 ? 15.001 -26.819 4.437  1.00 31.57 ? 120 PRO A CD    1 
ATOM   844  N  N     . MET A 1 112 ? 17.224 -24.624 7.982  1.00 26.25 ? 121 MET A N     1 
ATOM   845  C  CA    . MET A 1 112 ? 17.885 -24.681 9.278  1.00 24.47 ? 121 MET A CA    1 
ATOM   846  C  C     . MET A 1 112 ? 18.149 -23.260 9.748  1.00 24.90 ? 121 MET A C     1 
ATOM   847  O  O     . MET A 1 112 ? 18.294 -22.338 8.939  1.00 27.94 ? 121 MET A O     1 
ATOM   848  C  CB    . MET A 1 112 ? 19.207 -25.467 9.224  1.00 25.41 ? 121 MET A CB    1 
ATOM   849  C  CG    . MET A 1 112 ? 19.111 -26.824 8.536  1.00 27.70 ? 121 MET A CG    1 
ATOM   850  S  SD    . MET A 1 112 ? 20.649 -27.755 8.491  1.00 40.83 ? 121 MET A SD    1 
ATOM   851  C  CE    . MET A 1 112 ? 20.745 -28.163 10.202 1.00 44.08 ? 121 MET A CE    1 
ATOM   852  N  N     . ILE A 1 113 ? 18.223 -23.093 11.065 1.00 20.51 ? 122 ILE A N     1 
ATOM   853  C  CA    . ILE A 1 113 ? 18.550 -21.817 11.686 1.00 19.03 ? 122 ILE A CA    1 
ATOM   854  C  C     . ILE A 1 113 ? 19.623 -22.064 12.735 1.00 27.07 ? 122 ILE A C     1 
ATOM   855  O  O     . ILE A 1 113 ? 19.545 -23.040 13.490 1.00 25.36 ? 122 ILE A O     1 
ATOM   856  C  CB    . ILE A 1 113 ? 17.308 -21.154 12.313 1.00 25.94 ? 122 ILE A CB    1 
ATOM   857  C  CG1   . ILE A 1 113 ? 16.324 -20.740 11.216 1.00 22.81 ? 122 ILE A CG1   1 
ATOM   858  C  CG2   . ILE A 1 113 ? 17.697 -19.947 13.162 1.00 26.95 ? 122 ILE A CG2   1 
ATOM   859  C  CD1   . ILE A 1 113 ? 15.165 -19.911 11.720 1.00 26.75 ? 122 ILE A CD1   1 
ATOM   860  N  N     . LEU A 1 114 ? 20.636 -21.198 12.762 1.00 23.68 ? 123 LEU A N     1 
ATOM   861  C  CA    . LEU A 1 114 ? 21.677 -21.253 13.780 1.00 23.19 ? 123 LEU A CA    1 
ATOM   862  C  C     . LEU A 1 114 ? 21.217 -20.467 15.002 1.00 24.69 ? 123 LEU A C     1 
ATOM   863  O  O     . LEU A 1 114 ? 20.920 -19.272 14.904 1.00 28.16 ? 123 LEU A O     1 
ATOM   864  C  CB    . LEU A 1 114 ? 22.994 -20.695 13.244 1.00 22.22 ? 123 LEU A CB    1 
ATOM   865  C  CG    . LEU A 1 114 ? 24.165 -20.702 14.226 1.00 23.46 ? 123 LEU A CG    1 
ATOM   866  C  CD1   . LEU A 1 114 ? 24.430 -22.107 14.739 1.00 20.88 ? 123 LEU A CD1   1 
ATOM   867  C  CD2   . LEU A 1 114 ? 25.416 -20.127 13.572 1.00 28.33 ? 123 LEU A CD2   1 
ATOM   868  N  N     . VAL A 1 115 ? 21.173 -21.136 16.150 1.00 22.12 ? 124 VAL A N     1 
ATOM   869  C  CA    . VAL A 1 115 ? 20.643 -20.575 17.386 1.00 23.10 ? 124 VAL A CA    1 
ATOM   870  C  C     . VAL A 1 115 ? 21.796 -20.408 18.366 1.00 25.44 ? 124 VAL A C     1 
ATOM   871  O  O     . VAL A 1 115 ? 22.422 -21.394 18.773 1.00 26.02 ? 124 VAL A O     1 
ATOM   872  C  CB    . VAL A 1 115 ? 19.543 -21.471 17.976 1.00 23.10 ? 124 VAL A CB    1 
ATOM   873  C  CG1   . VAL A 1 115 ? 19.101 -20.961 19.332 1.00 19.88 ? 124 VAL A CG1   1 
ATOM   874  C  CG2   . VAL A 1 115 ? 18.359 -21.575 17.008 1.00 20.44 ? 124 VAL A CG2   1 
ATOM   875  N  N     . ALA A 1 116 ? 22.078 -19.162 18.744 1.00 24.01 ? 125 ALA A N     1 
ATOM   876  C  CA    . ALA A 1 116 ? 23.109 -18.845 19.733 1.00 28.22 ? 125 ALA A CA    1 
ATOM   877  C  C     . ALA A 1 116 ? 22.416 -18.647 21.078 1.00 30.05 ? 125 ALA A C     1 
ATOM   878  O  O     . ALA A 1 116 ? 21.848 -17.585 21.344 1.00 30.78 ? 125 ALA A O     1 
ATOM   879  C  CB    . ALA A 1 116 ? 23.897 -17.606 19.324 1.00 26.88 ? 125 ALA A CB    1 
ATOM   880  N  N     . ASN A 1 117 ? 22.472 -19.665 21.930 1.00 28.17 ? 126 ASN A N     1 
ATOM   881  C  CA    . ASN A 1 117 ? 21.717 -19.646 23.170 1.00 25.00 ? 126 ASN A CA    1 
ATOM   882  C  C     . ASN A 1 117 ? 22.572 -19.125 24.326 1.00 27.69 ? 126 ASN A C     1 
ATOM   883  O  O     . ASN A 1 117 ? 23.785 -18.936 24.206 1.00 33.47 ? 126 ASN A O     1 
ATOM   884  C  CB    . ASN A 1 117 ? 21.176 -21.043 23.482 1.00 28.06 ? 126 ASN A CB    1 
ATOM   885  C  CG    . ASN A 1 117 ? 20.112 -21.026 24.564 1.00 32.43 ? 126 ASN A CG    1 
ATOM   886  O  OD1   . ASN A 1 117 ? 19.254 -20.141 24.589 1.00 29.65 ? 126 ASN A OD1   1 
ATOM   887  N  ND2   . ASN A 1 117 ? 20.180 -21.985 25.478 1.00 25.30 ? 126 ASN A ND2   1 
ATOM   888  N  N     . LYS A 1 118 ? 21.904 -18.882 25.456 1.00 27.12 ? 127 LYS A N     1 
ATOM   889  C  CA    . LYS A 1 118 ? 22.525 -18.450 26.706 1.00 27.28 ? 127 LYS A CA    1 
ATOM   890  C  C     . LYS A 1 118 ? 23.142 -17.058 26.600 1.00 28.39 ? 127 LYS A C     1 
ATOM   891  O  O     . LYS A 1 118 ? 24.113 -16.754 27.295 1.00 31.62 ? 127 LYS A O     1 
ATOM   892  C  CB    . LYS A 1 118 ? 23.578 -19.455 27.194 1.00 32.70 ? 127 LYS A CB    1 
ATOM   893  C  CG    . LYS A 1 118 ? 23.055 -20.869 27.421 1.00 35.06 ? 127 LYS A CG    1 
ATOM   894  C  CD    . LYS A 1 118 ? 24.072 -21.719 28.178 1.00 29.81 ? 127 LYS A CD    1 
ATOM   895  C  CE    . LYS A 1 118 ? 23.554 -23.132 28.411 1.00 29.51 ? 127 LYS A CE    1 
ATOM   896  N  NZ    . LYS A 1 118 ? 24.547 -23.989 29.121 1.00 31.71 ? 127 LYS A NZ    1 
ATOM   897  N  N     . VAL A 1 119 ? 22.584 -16.187 25.753 1.00 30.05 ? 128 VAL A N     1 
ATOM   898  C  CA    . VAL A 1 119 ? 23.115 -14.831 25.636 1.00 28.75 ? 128 VAL A CA    1 
ATOM   899  C  C     . VAL A 1 119 ? 22.860 -13.990 26.877 1.00 36.60 ? 128 VAL A C     1 
ATOM   900  O  O     . VAL A 1 119 ? 23.379 -12.870 26.970 1.00 42.02 ? 128 VAL A O     1 
ATOM   901  C  CB    . VAL A 1 119 ? 22.554 -14.105 24.394 1.00 34.35 ? 128 VAL A CB    1 
ATOM   902  C  CG1   . VAL A 1 119 ? 22.930 -14.859 23.119 1.00 33.48 ? 128 VAL A CG1   1 
ATOM   903  C  CG2   . VAL A 1 119 ? 21.051 -13.921 24.502 1.00 28.57 ? 128 VAL A CG2   1 
ATOM   904  N  N     . ASP A 1 120 ? 22.090 -14.500 27.844 1.00 31.12 ? 129 ASP A N     1 
ATOM   905  C  CA    . ASP A 1 120 ? 21.961 -13.806 29.121 1.00 33.33 ? 129 ASP A CA    1 
ATOM   906  C  C     . ASP A 1 120 ? 23.228 -13.901 29.963 1.00 38.91 ? 129 ASP A C     1 
ATOM   907  O  O     . ASP A 1 120 ? 23.432 -13.066 30.852 1.00 38.28 ? 129 ASP A O     1 
ATOM   908  C  CB    . ASP A 1 120 ? 20.779 -14.360 29.917 1.00 33.73 ? 129 ASP A CB    1 
ATOM   909  C  CG    . ASP A 1 120 ? 20.902 -15.847 30.186 1.00 36.46 ? 129 ASP A CG    1 
ATOM   910  O  OD1   . ASP A 1 120 ? 20.740 -16.638 29.233 1.00 35.67 ? 129 ASP A OD1   1 
ATOM   911  O  OD2   . ASP A 1 120 ? 21.175 -16.222 31.347 1.00 38.00 ? 129 ASP A OD2   1 
ATOM   912  N  N     . LEU A 1 121 ? 24.078 -14.898 29.713 1.00 37.56 ? 130 LEU A N     1 
ATOM   913  C  CA    . LEU A 1 121 ? 25.333 -15.054 30.451 1.00 35.63 ? 130 LEU A CA    1 
ATOM   914  C  C     . LEU A 1 121 ? 26.427 -14.235 29.763 1.00 43.06 ? 130 LEU A C     1 
ATOM   915  O  O     . LEU A 1 121 ? 27.395 -14.755 29.203 1.00 35.90 ? 130 LEU A O     1 
ATOM   916  C  CB    . LEU A 1 121 ? 25.710 -16.527 30.552 1.00 35.29 ? 130 LEU A CB    1 
ATOM   917  C  CG    . LEU A 1 121 ? 24.677 -17.460 31.186 1.00 37.56 ? 130 LEU A CG    1 
ATOM   918  C  CD1   . LEU A 1 121 ? 25.200 -18.888 31.210 1.00 34.25 ? 130 LEU A CD1   1 
ATOM   919  C  CD2   . LEU A 1 121 ? 24.320 -16.991 32.585 1.00 39.20 ? 130 LEU A CD2   1 
ATOM   920  N  N     . MET A 1 122 ? 26.251 -12.913 29.823 1.00 38.17 ? 131 MET A N     1 
ATOM   921  C  CA    . MET A 1 122 ? 27.095 -12.017 29.039 1.00 42.31 ? 131 MET A CA    1 
ATOM   922  C  C     . MET A 1 122 ? 28.525 -11.963 29.564 1.00 43.32 ? 131 MET A C     1 
ATOM   923  O  O     . MET A 1 122 ? 29.456 -11.710 28.791 1.00 43.73 ? 131 MET A O     1 
ATOM   924  C  CB    . MET A 1 122 ? 26.475 -10.617 29.008 1.00 51.18 ? 131 MET A CB    1 
ATOM   925  C  CG    . MET A 1 122 ? 26.072 -10.083 30.376 1.00 49.91 ? 131 MET A CG    1 
ATOM   926  S  SD    . MET A 1 122 ? 24.629 -8.999  30.299 1.00 67.40 ? 131 MET A SD    1 
ATOM   927  C  CE    . MET A 1 122 ? 23.457 -10.053 29.459 1.00 54.49 ? 131 MET A CE    1 
ATOM   928  N  N     . HIS A 1 123 ? 28.726 -12.201 30.859 1.00 40.89 ? 132 HIS A N     1 
ATOM   929  C  CA    . HIS A 1 123 ? 30.072 -12.157 31.416 1.00 43.20 ? 132 HIS A CA    1 
ATOM   930  C  C     . HIS A 1 123 ? 30.835 -13.456 31.206 1.00 45.45 ? 132 HIS A C     1 
ATOM   931  O  O     . HIS A 1 123 ? 32.064 -13.466 31.327 1.00 42.31 ? 132 HIS A O     1 
ATOM   932  C  CB    . HIS A 1 123 ? 30.004 -11.803 32.901 1.00 44.28 ? 132 HIS A CB    1 
ATOM   933  C  CG    . HIS A 1 123 ? 29.393 -10.462 33.157 1.00 45.72 ? 132 HIS A CG    1 
ATOM   934  N  ND1   . HIS A 1 123 ? 28.043 -10.288 33.368 1.00 45.38 ? 132 HIS A ND1   1 
ATOM   935  C  CD2   . HIS A 1 123 ? 29.942 -9.225  33.185 1.00 47.47 ? 132 HIS A CD2   1 
ATOM   936  C  CE1   . HIS A 1 123 ? 27.789 -9.003  33.538 1.00 47.10 ? 132 HIS A CE1   1 
ATOM   937  N  NE2   . HIS A 1 123 ? 28.925 -8.337  33.432 1.00 48.38 ? 132 HIS A NE2   1 
ATOM   938  N  N     . LEU A 1 124 ? 30.138 -14.544 30.892 1.00 40.27 ? 133 LEU A N     1 
ATOM   939  C  CA    . LEU A 1 124 ? 30.767 -15.800 30.515 1.00 42.51 ? 133 LEU A CA    1 
ATOM   940  C  C     . LEU A 1 124 ? 30.835 -15.984 29.007 1.00 38.53 ? 133 LEU A C     1 
ATOM   941  O  O     . LEU A 1 124 ? 31.433 -16.960 28.541 1.00 40.67 ? 133 LEU A O     1 
ATOM   942  C  CB    . LEU A 1 124 ? 30.012 -16.976 31.142 1.00 42.50 ? 133 LEU A CB    1 
ATOM   943  C  CG    . LEU A 1 124 ? 30.006 -17.033 32.670 1.00 43.91 ? 133 LEU A CG    1 
ATOM   944  C  CD1   . LEU A 1 124 ? 29.047 -18.106 33.158 1.00 40.06 ? 133 LEU A CD1   1 
ATOM   945  C  CD2   . LEU A 1 124 ? 31.412 -17.287 33.190 1.00 42.40 ? 133 LEU A CD2   1 
ATOM   946  N  N     . ARG A 1 125 ? 30.245 -15.068 28.240 1.00 37.61 ? 134 ARG A N     1 
ATOM   947  C  CA    . ARG A 1 125 ? 30.132 -15.241 26.798 1.00 35.90 ? 134 ARG A CA    1 
ATOM   948  C  C     . ARG A 1 125 ? 31.503 -15.258 26.137 1.00 39.07 ? 134 ARG A C     1 
ATOM   949  O  O     . ARG A 1 125 ? 32.344 -14.392 26.395 1.00 38.60 ? 134 ARG A O     1 
ATOM   950  C  CB    . ARG A 1 125 ? 29.280 -14.124 26.202 1.00 33.51 ? 134 ARG A CB    1 
ATOM   951  C  CG    . ARG A 1 125 ? 29.114 -14.222 24.701 1.00 33.04 ? 134 ARG A CG    1 
ATOM   952  C  CD    . ARG A 1 125 ? 27.980 -13.344 24.225 1.00 31.52 ? 134 ARG A CD    1 
ATOM   953  N  NE    . ARG A 1 125 ? 27.666 -13.579 22.822 1.00 37.16 ? 134 ARG A NE    1 
ATOM   954  C  CZ    . ARG A 1 125 ? 26.625 -13.053 22.194 1.00 36.73 ? 134 ARG A CZ    1 
ATOM   955  N  NH1   . ARG A 1 125 ? 25.766 -12.267 22.823 1.00 30.21 ? 134 ARG A NH1   1 
ATOM   956  N  NH2   . ARG A 1 125 ? 26.442 -13.320 20.903 1.00 32.40 ? 134 ARG A NH2   1 
ATOM   957  N  N     . LYS A 1 126 ? 31.720 -16.244 25.273 1.00 40.25 ? 135 LYS A N     1 
ATOM   958  C  CA    . LYS A 1 126 ? 32.974 -16.390 24.550 1.00 37.88 ? 135 LYS A CA    1 
ATOM   959  C  C     . LYS A 1 126 ? 32.827 -16.248 23.046 1.00 40.54 ? 135 LYS A C     1 
ATOM   960  O  O     . LYS A 1 126 ? 33.793 -15.866 22.381 1.00 38.37 ? 135 LYS A O     1 
ATOM   961  C  CB    . LYS A 1 126 ? 33.611 -17.750 24.866 1.00 41.93 ? 135 LYS A CB    1 
ATOM   962  C  CG    . LYS A 1 126 ? 33.846 -17.969 26.351 1.00 49.65 ? 135 LYS A CG    1 
ATOM   963  C  CD    . LYS A 1 126 ? 34.430 -19.342 26.632 1.00 54.46 ? 135 LYS A CD    1 
ATOM   964  C  CE    . LYS A 1 126 ? 34.473 -19.610 28.130 1.00 63.39 ? 135 LYS A CE    1 
ATOM   965  N  NZ    . LYS A 1 126 ? 33.114 -19.474 28.748 1.00 53.46 ? 135 LYS A NZ    1 
ATOM   966  N  N     . ILE A 1 127 ? 31.654 -16.538 22.496 1.00 38.17 ? 136 ILE A N     1 
ATOM   967  C  CA    . ILE A 1 127 ? 31.389 -16.389 21.072 1.00 37.71 ? 136 ILE A CA    1 
ATOM   968  C  C     . ILE A 1 127 ? 30.661 -15.067 20.874 1.00 34.71 ? 136 ILE A C     1 
ATOM   969  O  O     . ILE A 1 127 ? 29.541 -14.886 21.368 1.00 33.57 ? 136 ILE A O     1 
ATOM   970  C  CB    . ILE A 1 127 ? 30.566 -17.567 20.528 1.00 28.96 ? 136 ILE A CB    1 
ATOM   971  C  CG1   . ILE A 1 127 ? 31.204 -18.899 20.935 1.00 35.61 ? 136 ILE A CG1   1 
ATOM   972  C  CG2   . ILE A 1 127 ? 30.434 -17.477 19.015 1.00 36.31 ? 136 ILE A CG2   1 
ATOM   973  C  CD1   . ILE A 1 127 ? 32.668 -19.028 20.547 1.00 39.39 ? 136 ILE A CD1   1 
ATOM   974  N  N     . THR A 1 128 ? 31.294 -14.142 20.159 1.00 34.51 ? 137 THR A N     1 
ATOM   975  C  CA    . THR A 1 128 ? 30.683 -12.844 19.924 1.00 38.06 ? 137 THR A CA    1 
ATOM   976  C  C     . THR A 1 128 ? 29.525 -12.970 18.939 1.00 36.41 ? 137 THR A C     1 
ATOM   977  O  O     . THR A 1 128 ? 29.365 -13.977 18.242 1.00 38.88 ? 137 THR A O     1 
ATOM   978  C  CB    . THR A 1 128 ? 31.708 -11.847 19.382 1.00 42.96 ? 137 THR A CB    1 
ATOM   979  O  OG1   . THR A 1 128 ? 32.031 -12.184 18.027 1.00 45.66 ? 137 THR A OG1   1 
ATOM   980  C  CG2   . THR A 1 128 ? 32.976 -11.871 20.220 1.00 41.69 ? 137 THR A CG2   1 
ATOM   981  N  N     . ARG A 1 129 ? 28.704 -11.918 18.891 1.00 39.76 ? 138 ARG A N     1 
ATOM   982  C  CA    . ARG A 1 129 ? 27.655 -11.849 17.881 1.00 41.08 ? 138 ARG A CA    1 
ATOM   983  C  C     . ARG A 1 129 ? 28.242 -11.903 16.477 1.00 43.36 ? 138 ARG A C     1 
ATOM   984  O  O     . ARG A 1 129 ? 27.681 -12.551 15.584 1.00 39.34 ? 138 ARG A O     1 
ATOM   985  C  CB    . ARG A 1 129 ? 26.833 -10.574 18.063 1.00 41.28 ? 138 ARG A CB    1 
ATOM   986  C  CG    . ARG A 1 129 ? 25.889 -10.291 16.906 1.00 48.11 ? 138 ARG A CG    1 
ATOM   987  C  CD    . ARG A 1 129 ? 25.092 -9.026  17.138 1.00 46.41 ? 138 ARG A CD    1 
ATOM   988  N  NE    . ARG A 1 129 ? 24.127 -9.187  18.217 1.00 52.06 ? 138 ARG A NE    1 
ATOM   989  C  CZ    . ARG A 1 129 ? 23.374 -8.207  18.698 1.00 63.15 ? 138 ARG A CZ    1 
ATOM   990  N  NH1   . ARG A 1 129 ? 23.463 -6.973  18.228 1.00 58.02 ? 138 ARG A NH1   1 
ATOM   991  N  NH2   . ARG A 1 129 ? 22.510 -8.472  19.675 1.00 65.15 ? 138 ARG A NH2   1 
ATOM   992  N  N     . GLU A 1 130 ? 29.376 -11.232 16.265 1.00 38.88 ? 139 GLU A N     1 
ATOM   993  C  CA    . GLU A 1 130 ? 29.991 -11.207 14.942 1.00 44.25 ? 139 GLU A CA    1 
ATOM   994  C  C     . GLU A 1 130 ? 30.492 -12.588 14.539 1.00 39.32 ? 139 GLU A C     1 
ATOM   995  O  O     . GLU A 1 130 ? 30.353 -12.989 13.378 1.00 34.98 ? 139 GLU A O     1 
ATOM   996  C  CB    . GLU A 1 130 ? 31.131 -10.188 14.910 1.00 41.09 ? 139 GLU A CB    1 
ATOM   997  C  CG    . GLU A 1 130 ? 30.674 -8.738  15.014 1.00 51.52 ? 139 GLU A CG    1 
ATOM   998  C  CD    . GLU A 1 130 ? 30.187 -8.359  16.408 1.00 63.03 ? 139 GLU A CD    1 
ATOM   999  O  OE1   . GLU A 1 130 ? 30.503 -9.088  17.374 1.00 61.67 ? 139 GLU A OE1   1 
ATOM   1000 O  OE2   . GLU A 1 130 ? 29.485 -7.331  16.534 1.00 65.22 ? 139 GLU A OE2   1 
ATOM   1001 N  N     . GLN A 1 131 ? 31.084 -13.326 15.482 1.00 41.31 ? 140 GLN A N     1 
ATOM   1002 C  CA    . GLN A 1 131 ? 31.480 -14.700 15.198 1.00 35.62 ? 140 GLN A CA    1 
ATOM   1003 C  C     . GLN A 1 131 ? 30.271 -15.554 14.845 1.00 33.93 ? 140 GLN A C     1 
ATOM   1004 O  O     . GLN A 1 131 ? 30.322 -16.359 13.908 1.00 38.40 ? 140 GLN A O     1 
ATOM   1005 C  CB    . GLN A 1 131 ? 32.227 -15.291 16.394 1.00 38.63 ? 140 GLN A CB    1 
ATOM   1006 C  CG    . GLN A 1 131 ? 33.595 -14.676 16.636 1.00 41.04 ? 140 GLN A CG    1 
ATOM   1007 C  CD    . GLN A 1 131 ? 34.283 -15.248 17.860 1.00 44.83 ? 140 GLN A CD    1 
ATOM   1008 O  OE1   . GLN A 1 131 ? 33.762 -15.174 18.972 1.00 42.07 ? 140 GLN A OE1   1 
ATOM   1009 N  NE2   . GLN A 1 131 ? 35.460 -15.827 17.659 1.00 60.16 ? 140 GLN A NE2   1 
ATOM   1010 N  N     . GLY A 1 132 ? 29.168 -15.381 15.576 1.00 38.14 ? 141 GLY A N     1 
ATOM   1011 C  CA    . GLY A 1 132 ? 27.967 -16.140 15.275 1.00 31.92 ? 141 GLY A CA    1 
ATOM   1012 C  C     . GLY A 1 132 ? 27.417 -15.845 13.894 1.00 33.57 ? 141 GLY A C     1 
ATOM   1013 O  O     . GLY A 1 132 ? 27.046 -16.760 13.156 1.00 31.83 ? 141 GLY A O     1 
ATOM   1014 N  N     . LYS A 1 133 ? 27.368 -14.564 13.517 1.00 36.82 ? 142 LYS A N     1 
ATOM   1015 C  CA    . LYS A 1 133 ? 26.849 -14.213 12.198 1.00 36.23 ? 142 LYS A CA    1 
ATOM   1016 C  C     . LYS A 1 133 ? 27.756 -14.726 11.085 1.00 35.30 ? 142 LYS A C     1 
ATOM   1017 O  O     . LYS A 1 133 ? 27.269 -15.150 10.031 1.00 31.93 ? 142 LYS A O     1 
ATOM   1018 C  CB    . LYS A 1 133 ? 26.658 -12.700 12.088 1.00 36.36 ? 142 LYS A CB    1 
ATOM   1019 C  CG    . LYS A 1 133 ? 25.498 -12.169 12.921 1.00 39.16 ? 142 LYS A CG    1 
ATOM   1020 C  CD    . LYS A 1 133 ? 25.223 -10.707 12.626 1.00 45.37 ? 142 LYS A CD    1 
ATOM   1021 C  CE    . LYS A 1 133 ? 24.001 -10.219 13.384 1.00 54.07 ? 142 LYS A CE    1 
ATOM   1022 N  NZ    . LYS A 1 133 ? 23.693 -8.791  13.093 1.00 59.98 ? 142 LYS A NZ    1 
ATOM   1023 N  N     . GLU A 1 134 ? 29.075 -14.695 11.298 1.00 33.24 ? 143 GLU A N     1 
ATOM   1024 C  CA    . GLU A 1 134 ? 29.996 -15.247 10.308 1.00 33.82 ? 143 GLU A CA    1 
ATOM   1025 C  C     . GLU A 1 134 ? 29.765 -16.739 10.120 1.00 30.90 ? 143 GLU A C     1 
ATOM   1026 O  O     . GLU A 1 134 ? 29.760 -17.238 8.988  1.00 31.27 ? 143 GLU A O     1 
ATOM   1027 C  CB    . GLU A 1 134 ? 31.445 -14.984 10.724 1.00 39.64 ? 143 GLU A CB    1 
ATOM   1028 C  CG    . GLU A 1 134 ? 31.854 -13.528 10.688 1.00 44.28 ? 143 GLU A CG    1 
ATOM   1029 C  CD    . GLU A 1 134 ? 33.210 -13.289 11.327 1.00 60.43 ? 143 GLU A CD    1 
ATOM   1030 O  OE1   . GLU A 1 134 ? 33.892 -14.279 11.673 1.00 61.36 ? 143 GLU A OE1   1 
ATOM   1031 O  OE2   . GLU A 1 134 ? 33.591 -12.109 11.488 1.00 68.62 ? 143 GLU A OE2   1 
ATOM   1032 N  N     . MET A 1 135 ? 29.574 -17.466 11.223 1.00 30.22 ? 144 MET A N     1 
ATOM   1033 C  CA    . MET A 1 135 ? 29.303 -18.898 11.148 1.00 30.00 ? 144 MET A CA    1 
ATOM   1034 C  C     . MET A 1 135 ? 28.023 -19.174 10.368 1.00 33.97 ? 144 MET A C     1 
ATOM   1035 O  O     . MET A 1 135 ? 27.984 -20.055 9.500  1.00 33.91 ? 144 MET A O     1 
ATOM   1036 C  CB    . MET A 1 135 ? 29.209 -19.476 12.561 1.00 37.33 ? 144 MET A CB    1 
ATOM   1037 C  CG    . MET A 1 135 ? 28.793 -20.933 12.623 1.00 30.46 ? 144 MET A CG    1 
ATOM   1038 S  SD    . MET A 1 135 ? 30.075 -22.036 12.006 1.00 36.42 ? 144 MET A SD    1 
ATOM   1039 C  CE    . MET A 1 135 ? 31.328 -21.844 13.273 1.00 32.44 ? 144 MET A CE    1 
ATOM   1040 N  N     . ALA A 1 136 ? 26.961 -18.424 10.667 1.00 31.86 ? 145 ALA A N     1 
ATOM   1041 C  CA    . ALA A 1 136 ? 25.703 -18.598 9.949  1.00 33.45 ? 145 ALA A CA    1 
ATOM   1042 C  C     . ALA A 1 136 ? 25.860 -18.255 8.474  1.00 32.00 ? 145 ALA A C     1 
ATOM   1043 O  O     . ALA A 1 136 ? 25.318 -18.948 7.603  1.00 32.90 ? 145 ALA A O     1 
ATOM   1044 C  CB    . ALA A 1 136 ? 24.615 -17.737 10.587 1.00 29.32 ? 145 ALA A CB    1 
ATOM   1045 N  N     . THR A 1 137 ? 26.594 -17.183 8.175  1.00 29.53 ? 146 THR A N     1 
ATOM   1046 C  CA    . THR A 1 137 ? 26.822 -16.810 6.784  1.00 33.55 ? 146 THR A CA    1 
ATOM   1047 C  C     . THR A 1 137 ? 27.607 -17.889 6.051  1.00 39.23 ? 146 THR A C     1 
ATOM   1048 O  O     . THR A 1 137 ? 27.301 -18.213 4.897  1.00 39.03 ? 146 THR A O     1 
ATOM   1049 C  CB    . THR A 1 137 ? 27.552 -15.467 6.716  1.00 32.25 ? 146 THR A CB    1 
ATOM   1050 O  OG1   . THR A 1 137 ? 26.749 -14.458 7.338  1.00 45.35 ? 146 THR A OG1   1 
ATOM   1051 C  CG2   . THR A 1 137 ? 27.822 -15.065 5.274  1.00 34.27 ? 146 THR A CG2   1 
ATOM   1052 N  N     . LYS A 1 138 ? 28.623 -18.461 6.707  1.00 35.39 ? 147 LYS A N     1 
ATOM   1053 C  CA    . LYS A 1 138 ? 29.411 -19.517 6.079  1.00 38.15 ? 147 LYS A CA    1 
ATOM   1054 C  C     . LYS A 1 138 ? 28.534 -20.694 5.669  1.00 32.39 ? 147 LYS A C     1 
ATOM   1055 O  O     . LYS A 1 138 ? 28.702 -21.249 4.577  1.00 41.21 ? 147 LYS A O     1 
ATOM   1056 C  CB    . LYS A 1 138 ? 30.525 -19.980 7.021  1.00 34.18 ? 147 LYS A CB    1 
ATOM   1057 C  CG    . LYS A 1 138 ? 31.433 -21.038 6.413  1.00 37.62 ? 147 LYS A CG    1 
ATOM   1058 C  CD    . LYS A 1 138 ? 32.480 -21.522 7.400  1.00 38.97 ? 147 LYS A CD    1 
ATOM   1059 C  CE    . LYS A 1 138 ? 31.850 -22.276 8.556  1.00 34.83 ? 147 LYS A CE    1 
ATOM   1060 N  NZ    . LYS A 1 138 ? 32.874 -22.795 9.506  1.00 42.12 ? 147 LYS A NZ    1 
ATOM   1061 N  N     . HIS A 1 139 ? 27.582 -21.076 6.517  1.00 31.22 ? 148 HIS A N     1 
ATOM   1062 C  CA    . HIS A 1 139 ? 26.698 -22.200 6.235  1.00 34.35 ? 148 HIS A CA    1 
ATOM   1063 C  C     . HIS A 1 139 ? 25.408 -21.793 5.526  1.00 33.05 ? 148 HIS A C     1 
ATOM   1064 O  O     . HIS A 1 139 ? 24.547 -22.653 5.311  1.00 29.85 ? 148 HIS A O     1 
ATOM   1065 C  CB    . HIS A 1 139 ? 26.354 -22.945 7.534  1.00 33.52 ? 148 HIS A CB    1 
ATOM   1066 C  CG    . HIS A 1 139 ? 27.543 -23.539 8.225  1.00 34.19 ? 148 HIS A CG    1 
ATOM   1067 N  ND1   . HIS A 1 139 ? 28.266 -24.587 7.695  1.00 32.08 ? 148 HIS A ND1   1 
ATOM   1068 C  CD2   . HIS A 1 139 ? 28.132 -23.236 9.406  1.00 32.54 ? 148 HIS A CD2   1 
ATOM   1069 C  CE1   . HIS A 1 139 ? 29.253 -24.899 8.516  1.00 34.11 ? 148 HIS A CE1   1 
ATOM   1070 N  NE2   . HIS A 1 139 ? 29.194 -24.094 9.562  1.00 42.11 ? 148 HIS A NE2   1 
ATOM   1071 N  N     . ASN A 1 140 ? 25.253 -20.512 5.172  1.00 32.58 ? 149 ASN A N     1 
ATOM   1072 C  CA    . ASN A 1 140 ? 24.092 -20.016 4.420  1.00 31.83 ? 149 ASN A CA    1 
ATOM   1073 C  C     . ASN A 1 140 ? 22.778 -20.318 5.146  1.00 27.26 ? 149 ASN A C     1 
ATOM   1074 O  O     . ASN A 1 140 ? 21.819 -20.818 4.557  1.00 36.43 ? 149 ASN A O     1 
ATOM   1075 C  CB    . ASN A 1 140 ? 24.076 -20.591 2.997  1.00 34.52 ? 149 ASN A CB    1 
ATOM   1076 C  CG    . ASN A 1 140 ? 23.183 -19.797 2.045  1.00 36.70 ? 149 ASN A CG    1 
ATOM   1077 O  OD1   . ASN A 1 140 ? 23.012 -18.588 2.193  1.00 34.04 ? 149 ASN A OD1   1 
ATOM   1078 N  ND2   . ASN A 1 140 ? 22.624 -20.482 1.049  1.00 30.78 ? 149 ASN A ND2   1 
ATOM   1079 N  N     . ILE A 1 141 ? 22.740 -20.011 6.441  1.00 31.12 ? 150 ILE A N     1 
ATOM   1080 C  CA    . ILE A 1 141 ? 21.530 -20.181 7.244  1.00 30.62 ? 150 ILE A CA    1 
ATOM   1081 C  C     . ILE A 1 141 ? 21.326 -18.933 8.095  1.00 25.69 ? 150 ILE A C     1 
ATOM   1082 O  O     . ILE A 1 141 ? 22.281 -18.202 8.394  1.00 29.55 ? 150 ILE A O     1 
ATOM   1083 C  CB    . ILE A 1 141 ? 21.605 -21.440 8.141  1.00 25.88 ? 150 ILE A CB    1 
ATOM   1084 C  CG1   . ILE A 1 141 ? 22.862 -21.397 9.017  1.00 25.22 ? 150 ILE A CG1   1 
ATOM   1085 C  CG2   . ILE A 1 141 ? 21.518 -22.712 7.302  1.00 28.18 ? 150 ILE A CG2   1 
ATOM   1086 C  CD1   . ILE A 1 141 ? 22.999 -22.590 9.946  1.00 23.53 ? 150 ILE A CD1   1 
ATOM   1087 N  N     . PRO A 1 142 ? 20.087 -18.668 8.504  1.00 31.54 ? 151 PRO A N     1 
ATOM   1088 C  CA    . PRO A 1 142 ? 19.829 -17.508 9.365  1.00 26.89 ? 151 PRO A CA    1 
ATOM   1089 C  C     . PRO A 1 142 ? 20.422 -17.688 10.753 1.00 25.54 ? 151 PRO A C     1 
ATOM   1090 O  O     . PRO A 1 142 ? 20.712 -18.798 11.206 1.00 26.98 ? 151 PRO A O     1 
ATOM   1091 C  CB    . PRO A 1 142 ? 18.296 -17.436 9.426  1.00 24.24 ? 151 PRO A CB    1 
ATOM   1092 C  CG    . PRO A 1 142 ? 17.821 -18.214 8.230  1.00 27.94 ? 151 PRO A CG    1 
ATOM   1093 C  CD    . PRO A 1 142 ? 18.837 -19.303 8.048  1.00 29.08 ? 151 PRO A CD    1 
ATOM   1094 N  N     . TYR A 1 143 ? 20.584 -16.556 11.436 1.00 28.91 ? 152 TYR A N     1 
ATOM   1095 C  CA    . TYR A 1 143 ? 21.194 -16.477 12.757 1.00 28.75 ? 152 TYR A CA    1 
ATOM   1096 C  C     . TYR A 1 143 ? 20.235 -15.786 13.713 1.00 24.44 ? 152 TYR A C     1 
ATOM   1097 O  O     . TYR A 1 143 ? 19.638 -14.762 13.365 1.00 30.55 ? 152 TYR A O     1 
ATOM   1098 C  CB    . TYR A 1 143 ? 22.517 -15.704 12.694 1.00 23.18 ? 152 TYR A CB    1 
ATOM   1099 C  CG    . TYR A 1 143 ? 23.164 -15.416 14.034 1.00 30.42 ? 152 TYR A CG    1 
ATOM   1100 C  CD1   . TYR A 1 143 ? 23.917 -16.386 14.683 1.00 23.45 ? 152 TYR A CD1   1 
ATOM   1101 C  CD2   . TYR A 1 143 ? 23.046 -14.163 14.634 1.00 28.28 ? 152 TYR A CD2   1 
ATOM   1102 C  CE1   . TYR A 1 143 ? 24.520 -16.128 15.897 1.00 33.18 ? 152 TYR A CE1   1 
ATOM   1103 C  CE2   . TYR A 1 143 ? 23.649 -13.893 15.849 1.00 26.03 ? 152 TYR A CE2   1 
ATOM   1104 C  CZ    . TYR A 1 143 ? 24.385 -14.881 16.475 1.00 34.43 ? 152 TYR A CZ    1 
ATOM   1105 O  OH    . TYR A 1 143 ? 24.991 -14.636 17.682 1.00 30.57 ? 152 TYR A OH    1 
ATOM   1106 N  N     . ILE A 1 144 ? 20.093 -16.336 14.917 1.00 22.20 ? 153 ILE A N     1 
ATOM   1107 C  CA    . ILE A 1 144 ? 19.240 -15.731 15.936 1.00 27.46 ? 153 ILE A CA    1 
ATOM   1108 C  C     . ILE A 1 144 ? 19.833 -16.024 17.309 1.00 32.29 ? 153 ILE A C     1 
ATOM   1109 O  O     . ILE A 1 144 ? 20.345 -17.119 17.564 1.00 27.55 ? 153 ILE A O     1 
ATOM   1110 C  CB    . ILE A 1 144 ? 17.780 -16.230 15.823 1.00 32.70 ? 153 ILE A CB    1 
ATOM   1111 C  CG1   . ILE A 1 144 ? 16.843 -15.370 16.679 1.00 26.67 ? 153 ILE A CG1   1 
ATOM   1112 C  CG2   . ILE A 1 144 ? 17.665 -17.698 16.205 1.00 20.77 ? 153 ILE A CG2   1 
ATOM   1113 C  CD1   . ILE A 1 144 ? 15.371 -15.695 16.481 1.00 23.30 ? 153 ILE A CD1   1 
ATOM   1114 N  N     . GLU A 1 145 ? 19.775 -15.032 18.192 1.00 25.64 ? 154 GLU A N     1 
ATOM   1115 C  CA    . GLU A 1 145 ? 20.271 -15.171 19.554 1.00 27.85 ? 154 GLU A CA    1 
ATOM   1116 C  C     . GLU A 1 145 ? 19.099 -15.406 20.495 1.00 29.12 ? 154 GLU A C     1 
ATOM   1117 O  O     . GLU A 1 145 ? 18.067 -14.734 20.388 1.00 31.90 ? 154 GLU A O     1 
ATOM   1118 C  CB    . GLU A 1 145 ? 21.063 -13.933 19.972 1.00 26.72 ? 154 GLU A CB    1 
ATOM   1119 C  CG    . GLU A 1 145 ? 22.292 -13.723 19.117 1.00 28.37 ? 154 GLU A CG    1 
ATOM   1120 C  CD    . GLU A 1 145 ? 23.221 -12.658 19.652 1.00 37.46 ? 154 GLU A CD    1 
ATOM   1121 O  OE1   . GLU A 1 145 ? 22.795 -11.867 20.517 1.00 51.77 ? 154 GLU A OE1   1 
ATOM   1122 O  OE2   . GLU A 1 145 ? 24.385 -12.614 19.204 1.00 35.79 ? 154 GLU A OE2   1 
ATOM   1123 N  N     . THR A 1 146 ? 19.257 -16.365 21.405 1.00 24.72 ? 155 THR A N     1 
ATOM   1124 C  CA    . THR A 1 146 ? 18.177 -16.776 22.288 1.00 27.22 ? 155 THR A CA    1 
ATOM   1125 C  C     . THR A 1 146 ? 18.645 -16.827 23.733 1.00 33.60 ? 155 THR A C     1 
ATOM   1126 O  O     . THR A 1 146 ? 19.842 -16.844 24.032 1.00 31.20 ? 155 THR A O     1 
ATOM   1127 C  CB    . THR A 1 146 ? 17.619 -18.157 21.917 1.00 30.42 ? 155 THR A CB    1 
ATOM   1128 O  OG1   . THR A 1 146 ? 18.657 -19.139 22.025 1.00 29.68 ? 155 THR A OG1   1 
ATOM   1129 C  CG2   . THR A 1 146 ? 17.053 -18.158 20.504 1.00 24.67 ? 155 THR A CG2   1 
ATOM   1130 N  N     . SER A 1 147 ? 17.663 -16.866 24.628 1.00 31.57 ? 156 SER A N     1 
ATOM   1131 C  CA    . SER A 1 147 ? 17.891 -17.198 26.029 1.00 31.51 ? 156 SER A CA    1 
ATOM   1132 C  C     . SER A 1 147 ? 16.660 -17.930 26.534 1.00 32.89 ? 156 SER A C     1 
ATOM   1133 O  O     . SER A 1 147 ? 15.544 -17.420 26.404 1.00 30.79 ? 156 SER A O     1 
ATOM   1134 C  CB    . SER A 1 147 ? 18.155 -15.949 26.870 1.00 31.67 ? 156 SER A CB    1 
ATOM   1135 O  OG    . SER A 1 147 ? 18.297 -16.289 28.238 1.00 34.84 ? 156 SER A OG    1 
ATOM   1136 N  N     . ALA A 1 148 ? 16.860 -19.122 27.093 1.00 34.72 ? 157 ALA A N     1 
ATOM   1137 C  CA    . ALA A 1 148 ? 15.778 -19.900 27.681 1.00 39.90 ? 157 ALA A CA    1 
ATOM   1138 C  C     . ALA A 1 148 ? 15.501 -19.532 29.133 1.00 39.46 ? 157 ALA A C     1 
ATOM   1139 O  O     . ALA A 1 148 ? 14.482 -19.962 29.682 1.00 37.60 ? 157 ALA A O     1 
ATOM   1140 C  CB    . ALA A 1 148 ? 16.092 -21.397 27.590 1.00 34.57 ? 157 ALA A CB    1 
ATOM   1141 N  N     . LYS A 1 149 ? 16.383 -18.766 29.767 1.00 41.03 ? 158 LYS A N     1 
ATOM   1142 C  CA    . LYS A 1 149 ? 16.147 -18.320 31.132 1.00 42.23 ? 158 LYS A CA    1 
ATOM   1143 C  C     . LYS A 1 149 ? 15.109 -17.203 31.141 1.00 49.91 ? 158 LYS A C     1 
ATOM   1144 O  O     . LYS A 1 149 ? 15.065 -16.370 30.232 1.00 48.37 ? 158 LYS A O     1 
ATOM   1145 C  CB    . LYS A 1 149 ? 17.458 -17.840 31.758 1.00 42.60 ? 158 LYS A CB    1 
ATOM   1146 C  CG    . LYS A 1 149 ? 17.360 -17.412 33.216 1.00 51.43 ? 158 LYS A CG    1 
ATOM   1147 C  CD    . LYS A 1 149 ? 18.640 -16.720 33.661 1.00 51.18 ? 158 LYS A CD    1 
ATOM   1148 C  CE    . LYS A 1 149 ? 18.611 -16.383 35.143 1.00 48.21 ? 158 LYS A CE    1 
ATOM   1149 N  NZ    . LYS A 1 149 ? 18.652 -17.615 35.977 1.00 57.01 ? 158 LYS A NZ    1 
ATOM   1150 N  N     . ASP A 1 150 ? 14.260 -17.196 32.161 1.00 49.68 ? 159 ASP A N     1 
ATOM   1151 C  CA    . ASP A 1 150 ? 13.257 -16.143 32.275 1.00 56.71 ? 159 ASP A CA    1 
ATOM   1152 C  C     . ASP A 1 150 ? 13.940 -14.821 32.604 1.00 57.12 ? 159 ASP A C     1 
ATOM   1153 O  O     . ASP A 1 150 ? 14.781 -14.773 33.510 1.00 61.31 ? 159 ASP A O     1 
ATOM   1154 C  CB    . ASP A 1 150 ? 12.226 -16.482 33.352 1.00 54.68 ? 159 ASP A CB    1 
ATOM   1155 C  CG    . ASP A 1 150 ? 11.265 -17.574 32.923 1.00 62.07 ? 159 ASP A CG    1 
ATOM   1156 O  OD1   . ASP A 1 150 ? 10.911 -17.627 31.726 1.00 59.44 ? 159 ASP A OD1   1 
ATOM   1157 O  OD2   . ASP A 1 150 ? 10.857 -18.376 33.788 1.00 63.81 ? 159 ASP A OD2   1 
ATOM   1158 N  N     . PRO A 1 151 ? 13.614 -13.728 31.902 1.00 57.13 ? 160 PRO A N     1 
ATOM   1159 C  CA    . PRO A 1 151 ? 12.658 -13.617 30.788 1.00 49.34 ? 160 PRO A CA    1 
ATOM   1160 C  C     . PRO A 1 151 ? 13.236 -14.130 29.468 1.00 50.27 ? 160 PRO A C     1 
ATOM   1161 O  O     . PRO A 1 151 ? 14.314 -13.713 29.052 1.00 49.99 ? 160 PRO A O     1 
ATOM   1162 C  CB    . PRO A 1 151 ? 12.364 -12.111 30.747 1.00 50.85 ? 160 PRO A CB    1 
ATOM   1163 C  CG    . PRO A 1 151 ? 13.639 -11.477 31.223 1.00 49.20 ? 160 PRO A CG    1 
ATOM   1164 C  CD    . PRO A 1 151 ? 14.177 -12.416 32.275 1.00 55.13 ? 160 PRO A CD    1 
ATOM   1165 N  N     . PRO A 1 152 ? 12.528 -15.029 28.786 1.00 43.50 ? 161 PRO A N     1 
ATOM   1166 C  CA    . PRO A 1 152 ? 13.094 -15.660 27.588 1.00 43.55 ? 161 PRO A CA    1 
ATOM   1167 C  C     . PRO A 1 152 ? 13.255 -14.678 26.439 1.00 40.89 ? 161 PRO A C     1 
ATOM   1168 O  O     . PRO A 1 152 ? 12.508 -13.705 26.305 1.00 43.90 ? 161 PRO A O     1 
ATOM   1169 C  CB    . PRO A 1 152 ? 12.070 -16.749 27.246 1.00 43.25 ? 161 PRO A CB    1 
ATOM   1170 C  CG    . PRO A 1 152 ? 10.780 -16.226 27.803 1.00 40.30 ? 161 PRO A CG    1 
ATOM   1171 C  CD    . PRO A 1 152 ? 11.156 -15.492 29.062 1.00 48.26 ? 161 PRO A CD    1 
ATOM   1172 N  N     . LEU A 1 153 ? 14.243 -14.956 25.593 1.00 32.91 ? 162 LEU A N     1 
ATOM   1173 C  CA    . LEU A 1 153 ? 14.601 -14.084 24.482 1.00 33.07 ? 162 LEU A CA    1 
ATOM   1174 C  C     . LEU A 1 153 ? 14.547 -14.886 23.190 1.00 39.24 ? 162 LEU A C     1 
ATOM   1175 O  O     . LEU A 1 153 ? 15.294 -15.858 23.031 1.00 28.04 ? 162 LEU A O     1 
ATOM   1176 C  CB    . LEU A 1 153 ? 15.996 -13.484 24.693 1.00 36.16 ? 162 LEU A CB    1 
ATOM   1177 C  CG    . LEU A 1 153 ? 16.468 -12.252 23.912 1.00 43.34 ? 162 LEU A CG    1 
ATOM   1178 C  CD1   . LEU A 1 153 ? 17.581 -12.620 22.939 1.00 41.07 ? 162 LEU A CD1   1 
ATOM   1179 C  CD2   . LEU A 1 153 ? 15.323 -11.543 23.192 1.00 37.77 ? 162 LEU A CD2   1 
ATOM   1180 N  N     . ASN A 1 154 ? 13.652 -14.491 22.283 1.00 27.56 ? 163 ASN A N     1 
ATOM   1181 C  CA    . ASN A 1 154 ? 13.577 -15.026 20.923 1.00 32.31 ? 163 ASN A CA    1 
ATOM   1182 C  C     . ASN A 1 154 ? 13.318 -16.529 20.878 1.00 25.28 ? 163 ASN A C     1 
ATOM   1183 O  O     . ASN A 1 154 ? 13.595 -17.171 19.860 1.00 28.04 ? 163 ASN A O     1 
ATOM   1184 C  CB    . ASN A 1 154 ? 14.849 -14.702 20.130 1.00 30.00 ? 163 ASN A CB    1 
ATOM   1185 C  CG    . ASN A 1 154 ? 14.967 -13.230 19.798 1.00 36.01 ? 163 ASN A CG    1 
ATOM   1186 O  OD1   . ASN A 1 154 ? 13.962 -12.524 19.693 1.00 34.42 ? 163 ASN A OD1   1 
ATOM   1187 N  ND2   . ASN A 1 154 ? 16.197 -12.758 19.624 1.00 25.77 ? 163 ASN A ND2   1 
ATOM   1188 N  N     . VAL A 1 155 ? 12.789 -17.118 21.951 1.00 25.96 ? 164 VAL A N     1 
ATOM   1189 C  CA    . VAL A 1 155 ? 12.497 -18.549 21.926 1.00 28.63 ? 164 VAL A CA    1 
ATOM   1190 C  C     . VAL A 1 155 ? 11.383 -18.847 20.930 1.00 31.29 ? 164 VAL A C     1 
ATOM   1191 O  O     . VAL A 1 155 ? 11.529 -19.700 20.047 1.00 28.28 ? 164 VAL A O     1 
ATOM   1192 C  CB    . VAL A 1 155 ? 12.145 -19.061 23.333 1.00 31.34 ? 164 VAL A CB    1 
ATOM   1193 C  CG1   . VAL A 1 155 ? 11.667 -20.507 23.258 1.00 32.51 ? 164 VAL A CG1   1 
ATOM   1194 C  CG2   . VAL A 1 155 ? 13.347 -18.942 24.256 1.00 25.29 ? 164 VAL A CG2   1 
ATOM   1195 N  N     . ASP A 1 156 ? 10.249 -18.152 21.060 1.00 32.53 ? 165 ASP A N     1 
ATOM   1196 C  CA    . ASP A 1 156 ? 9.175  -18.315 20.086 1.00 27.68 ? 165 ASP A CA    1 
ATOM   1197 C  C     . ASP A 1 156 ? 9.654  -17.980 18.679 1.00 33.16 ? 165 ASP A C     1 
ATOM   1198 O  O     . ASP A 1 156 ? 9.341  -18.698 17.722 1.00 26.92 ? 165 ASP A O     1 
ATOM   1199 C  CB    . ASP A 1 156 ? 7.978  -17.441 20.461 1.00 31.63 ? 165 ASP A CB    1 
ATOM   1200 C  CG    . ASP A 1 156 ? 7.066  -18.098 21.485 1.00 32.56 ? 165 ASP A CG    1 
ATOM   1201 O  OD1   . ASP A 1 156 ? 7.503  -19.035 22.182 1.00 34.69 ? 165 ASP A OD1   1 
ATOM   1202 O  OD2   . ASP A 1 156 ? 5.898  -17.677 21.585 1.00 43.04 ? 165 ASP A OD2   1 
ATOM   1203 N  N     . LYS A 1 157 ? 10.426 -16.897 18.537 1.00 30.41 ? 166 LYS A N     1 
ATOM   1204 C  CA    . LYS A 1 157 ? 10.847 -16.455 17.211 1.00 27.73 ? 166 LYS A CA    1 
ATOM   1205 C  C     . LYS A 1 157 ? 11.700 -17.510 16.518 1.00 27.18 ? 166 LYS A C     1 
ATOM   1206 O  O     . LYS A 1 157 ? 11.563 -17.728 15.309 1.00 29.41 ? 166 LYS A O     1 
ATOM   1207 C  CB    . LYS A 1 157 ? 11.608 -15.133 17.309 1.00 29.18 ? 166 LYS A CB    1 
ATOM   1208 C  CG    . LYS A 1 157 ? 11.852 -14.461 15.964 1.00 30.05 ? 166 LYS A CG    1 
ATOM   1209 C  CD    . LYS A 1 157 ? 12.477 -13.085 16.131 1.00 37.19 ? 166 LYS A CD    1 
ATOM   1210 C  CE    . LYS A 1 157 ? 12.369 -12.264 14.853 1.00 35.90 ? 166 LYS A CE    1 
ATOM   1211 N  NZ    . LYS A 1 157 ? 13.027 -12.937 13.701 1.00 38.34 ? 166 LYS A NZ    1 
ATOM   1212 N  N     . ALA A 1 158 ? 12.582 -18.177 17.268 1.00 22.96 ? 167 ALA A N     1 
ATOM   1213 C  CA    . ALA A 1 158 ? 13.438 -19.201 16.677 1.00 26.71 ? 167 ALA A CA    1 
ATOM   1214 C  C     . ALA A 1 158 ? 12.611 -20.298 16.020 1.00 25.42 ? 167 ALA A C     1 
ATOM   1215 O  O     . ALA A 1 158 ? 12.841 -20.655 14.859 1.00 27.94 ? 167 ALA A O     1 
ATOM   1216 C  CB    . ALA A 1 158 ? 14.365 -19.793 17.740 1.00 21.12 ? 167 ALA A CB    1 
ATOM   1217 N  N     . PHE A 1 159 ? 11.638 -20.846 16.751 1.00 25.62 ? 168 PHE A N     1 
ATOM   1218 C  CA    . PHE A 1 159 ? 10.819 -21.916 16.189 1.00 20.97 ? 168 PHE A CA    1 
ATOM   1219 C  C     . PHE A 1 159 ? 9.930  -21.401 15.064 1.00 27.63 ? 168 PHE A C     1 
ATOM   1220 O  O     . PHE A 1 159 ? 9.820  -22.043 14.014 1.00 25.61 ? 168 PHE A O     1 
ATOM   1221 C  CB    . PHE A 1 159 ? 9.981  -22.573 17.284 1.00 23.06 ? 168 PHE A CB    1 
ATOM   1222 C  CG    . PHE A 1 159 ? 10.775 -23.456 18.208 1.00 28.52 ? 168 PHE A CG    1 
ATOM   1223 C  CD1   . PHE A 1 159 ? 11.053 -24.767 17.862 1.00 20.98 ? 168 PHE A CD1   1 
ATOM   1224 C  CD2   . PHE A 1 159 ? 11.242 -22.974 19.420 1.00 28.08 ? 168 PHE A CD2   1 
ATOM   1225 C  CE1   . PHE A 1 159 ? 11.782 -25.582 18.706 1.00 21.13 ? 168 PHE A CE1   1 
ATOM   1226 C  CE2   . PHE A 1 159 ? 11.971 -23.784 20.270 1.00 27.37 ? 168 PHE A CE2   1 
ATOM   1227 C  CZ    . PHE A 1 159 ? 12.242 -25.092 19.911 1.00 21.87 ? 168 PHE A CZ    1 
ATOM   1228 N  N     . HIS A 1 160 ? 9.299  -20.239 15.260 1.00 23.67 ? 169 HIS A N     1 
ATOM   1229 C  CA    . HIS A 1 160 ? 8.430  -19.685 14.227 1.00 23.07 ? 169 HIS A CA    1 
ATOM   1230 C  C     . HIS A 1 160 ? 9.211  -19.338 12.966 1.00 25.31 ? 169 HIS A C     1 
ATOM   1231 O  O     . HIS A 1 160 ? 8.754  -19.625 11.852 1.00 27.62 ? 169 HIS A O     1 
ATOM   1232 C  CB    . HIS A 1 160 ? 7.699  -18.450 14.755 1.00 26.68 ? 169 HIS A CB    1 
ATOM   1233 C  CG    . HIS A 1 160 ? 6.671  -18.756 15.798 1.00 32.67 ? 169 HIS A CG    1 
ATOM   1234 N  ND1   . HIS A 1 160 ? 5.744  -17.829 16.222 1.00 36.18 ? 169 HIS A ND1   1 
ATOM   1235 C  CD2   . HIS A 1 160 ? 6.424  -19.886 16.503 1.00 25.42 ? 169 HIS A CD2   1 
ATOM   1236 C  CE1   . HIS A 1 160 ? 4.969  -18.375 17.143 1.00 41.99 ? 169 HIS A CE1   1 
ATOM   1237 N  NE2   . HIS A 1 160 ? 5.362  -19.622 17.332 1.00 34.22 ? 169 HIS A NE2   1 
ATOM   1238 N  N     . ASP A 1 161 ? 10.385 -18.715 13.115 1.00 21.90 ? 170 ASP A N     1 
ATOM   1239 C  CA    . ASP A 1 161 ? 11.184 -18.391 11.936 1.00 29.21 ? 170 ASP A CA    1 
ATOM   1240 C  C     . ASP A 1 161 ? 11.582 -19.646 11.172 1.00 22.14 ? 170 ASP A C     1 
ATOM   1241 O  O     . ASP A 1 161 ? 11.636 -19.624 9.938  1.00 29.37 ? 170 ASP A O     1 
ATOM   1242 C  CB    . ASP A 1 161 ? 12.427 -17.586 12.329 1.00 27.95 ? 170 ASP A CB    1 
ATOM   1243 C  CG    . ASP A 1 161 ? 12.118 -16.124 12.590 1.00 33.45 ? 170 ASP A CG    1 
ATOM   1244 O  OD1   . ASP A 1 161 ? 10.951 -15.720 12.398 1.00 32.36 ? 170 ASP A OD1   1 
ATOM   1245 O  OD2   . ASP A 1 161 ? 13.037 -15.378 12.986 1.00 32.67 ? 170 ASP A OD2   1 
ATOM   1246 N  N     . LEU A 1 162 ? 11.844 -20.749 11.880 1.00 22.70 ? 171 LEU A N     1 
ATOM   1247 C  CA    . LEU A 1 162 ? 12.157 -22.003 11.199 1.00 23.15 ? 171 LEU A CA    1 
ATOM   1248 C  C     . LEU A 1 162 ? 10.999 -22.445 10.314 1.00 24.65 ? 171 LEU A C     1 
ATOM   1249 O  O     . LEU A 1 162 ? 11.204 -22.811 9.151  1.00 28.83 ? 171 LEU A O     1 
ATOM   1250 C  CB    . LEU A 1 162 ? 12.507 -23.093 12.217 1.00 21.24 ? 171 LEU A CB    1 
ATOM   1251 C  CG    . LEU A 1 162 ? 12.902 -24.456 11.634 1.00 28.06 ? 171 LEU A CG    1 
ATOM   1252 C  CD1   . LEU A 1 162 ? 14.074 -24.319 10.666 1.00 20.41 ? 171 LEU A CD1   1 
ATOM   1253 C  CD2   . LEU A 1 162 ? 13.227 -25.469 12.732 1.00 20.11 ? 171 LEU A CD2   1 
ATOM   1254 N  N     . VAL A 1 163 ? 9.772  -22.399 10.843 1.00 25.30 ? 172 VAL A N     1 
ATOM   1255 C  CA    . VAL A 1 163 ? 8.598  -22.704 10.028 1.00 25.54 ? 172 VAL A CA    1 
ATOM   1256 C  C     . VAL A 1 163 ? 8.516  -21.757 8.835  1.00 23.32 ? 172 VAL A C     1 
ATOM   1257 O  O     . VAL A 1 163 ? 8.181  -22.173 7.718  1.00 26.66 ? 172 VAL A O     1 
ATOM   1258 C  CB    . VAL A 1 163 ? 7.319  -22.650 10.887 1.00 23.90 ? 172 VAL A CB    1 
ATOM   1259 C  CG1   . VAL A 1 163 ? 6.078  -22.884 10.025 1.00 22.10 ? 172 VAL A CG1   1 
ATOM   1260 C  CG2   . VAL A 1 163 ? 7.388  -23.673 12.009 1.00 24.10 ? 172 VAL A CG2   1 
ATOM   1261 N  N     . ARG A 1 164 ? 8.830  -20.474 9.047  1.00 24.93 ? 173 ARG A N     1 
ATOM   1262 C  CA    . ARG A 1 164 ? 8.825  -19.515 7.942  1.00 24.96 ? 173 ARG A CA    1 
ATOM   1263 C  C     . ARG A 1 164 ? 9.819  -19.909 6.857  1.00 27.94 ? 173 ARG A C     1 
ATOM   1264 O  O     . ARG A 1 164 ? 9.520  -19.797 5.662  1.00 31.37 ? 173 ARG A O     1 
ATOM   1265 C  CB    . ARG A 1 164 ? 9.135  -18.109 8.454  1.00 26.39 ? 173 ARG A CB    1 
ATOM   1266 C  CG    . ARG A 1 164 ? 8.058  -17.511 9.339  1.00 35.07 ? 173 ARG A CG    1 
ATOM   1267 C  CD    . ARG A 1 164 ? 8.374  -16.068 9.717  1.00 26.39 ? 173 ARG A CD    1 
ATOM   1268 N  NE    . ARG A 1 164 ? 7.299  -15.487 10.513 1.00 35.53 ? 173 ARG A NE    1 
ATOM   1269 C  CZ    . ARG A 1 164 ? 7.299  -15.413 11.837 1.00 35.63 ? 173 ARG A CZ    1 
ATOM   1270 N  NH1   . ARG A 1 164 ? 8.333  -15.824 12.554 1.00 32.35 ? 173 ARG A NH1   1 
ATOM   1271 N  NH2   . ARG A 1 164 ? 6.234  -14.915 12.458 1.00 34.29 ? 173 ARG A NH2   1 
ATOM   1272 N  N     . VAL A 1 165 ? 11.013 -20.358 7.250  1.00 27.33 ? 174 VAL A N     1 
ATOM   1273 C  CA    . VAL A 1 165 ? 11.989 -20.816 6.265  1.00 24.38 ? 174 VAL A CA    1 
ATOM   1274 C  C     . VAL A 1 165 ? 11.437 -22.003 5.488  1.00 26.92 ? 174 VAL A C     1 
ATOM   1275 O  O     . VAL A 1 165 ? 11.521 -22.050 4.255  1.00 29.52 ? 174 VAL A O     1 
ATOM   1276 C  CB    . VAL A 1 165 ? 13.324 -21.159 6.951  1.00 26.02 ? 174 VAL A CB    1 
ATOM   1277 C  CG1   . VAL A 1 165 ? 14.290 -21.769 5.953  1.00 28.35 ? 174 VAL A CG1   1 
ATOM   1278 C  CG2   . VAL A 1 165 ? 13.933 -19.918 7.588  1.00 29.64 ? 174 VAL A CG2   1 
ATOM   1279 N  N     . ILE A 1 166 ? 10.854 -22.976 6.195  1.00 25.64 ? 175 ILE A N     1 
ATOM   1280 C  CA    . ILE A 1 166 ? 10.256 -24.135 5.536  1.00 23.88 ? 175 ILE A CA    1 
ATOM   1281 C  C     . ILE A 1 166 ? 9.189  -23.695 4.541  1.00 33.94 ? 175 ILE A C     1 
ATOM   1282 O  O     . ILE A 1 166 ? 9.089  -24.239 3.433  1.00 31.41 ? 175 ILE A O     1 
ATOM   1283 C  CB    . ILE A 1 166 ? 9.680  -25.106 6.585  1.00 24.66 ? 175 ILE A CB    1 
ATOM   1284 C  CG1   . ILE A 1 166 ? 10.793 -25.647 7.486  1.00 28.37 ? 175 ILE A CG1   1 
ATOM   1285 C  CG2   . ILE A 1 166 ? 8.934  -26.250 5.908  1.00 27.93 ? 175 ILE A CG2   1 
ATOM   1286 C  CD1   . ILE A 1 166 ? 10.281 -26.483 8.660  1.00 26.80 ? 175 ILE A CD1   1 
ATOM   1287 N  N     . ARG A 1 167 ? 8.381  -22.699 4.915  1.00 29.37 ? 176 ARG A N     1 
ATOM   1288 C  CA    . ARG A 1 167 ? 7.306  -22.238 4.039  1.00 35.27 ? 176 ARG A CA    1 
ATOM   1289 C  C     . ARG A 1 167 ? 7.850  -21.528 2.805  1.00 35.04 ? 176 ARG A C     1 
ATOM   1290 O  O     . ARG A 1 167 ? 7.266  -21.622 1.719  1.00 40.39 ? 176 ARG A O     1 
ATOM   1291 C  CB    . ARG A 1 167 ? 6.365  -21.314 4.811  1.00 29.53 ? 176 ARG A CB    1 
ATOM   1292 C  CG    . ARG A 1 167 ? 5.454  -22.024 5.795  1.00 31.26 ? 176 ARG A CG    1 
ATOM   1293 C  CD    . ARG A 1 167 ? 4.702  -21.008 6.633  1.00 26.62 ? 176 ARG A CD    1 
ATOM   1294 N  NE    . ARG A 1 167 ? 3.716  -21.624 7.510  1.00 31.94 ? 176 ARG A NE    1 
ATOM   1295 C  CZ    . ARG A 1 167 ? 3.029  -20.968 8.435  1.00 36.37 ? 176 ARG A CZ    1 
ATOM   1296 N  NH1   . ARG A 1 167 ? 3.218  -19.675 8.649  1.00 26.64 ? 176 ARG A NH1   1 
ATOM   1297 N  NH2   . ARG A 1 167 ? 2.131  -21.625 9.164  1.00 33.71 ? 176 ARG A NH2   1 
ATOM   1298 N  N     . GLN A 1 168 ? 8.953  -20.800 2.952  1.00 38.28 ? 177 GLN A N     1 
ATOM   1299 C  CA    . GLN A 1 168 ? 9.548  -20.046 1.857  1.00 42.42 ? 177 GLN A CA    1 
ATOM   1300 C  C     . GLN A 1 168 ? 10.603 -20.844 1.104  1.00 48.07 ? 177 GLN A C     1 
ATOM   1301 O  O     . GLN A 1 168 ? 11.295 -20.284 0.249  1.00 50.91 ? 177 GLN A O     1 
ATOM   1302 C  CB    . GLN A 1 168 ? 10.158 -18.749 2.393  1.00 41.13 ? 177 GLN A CB    1 
ATOM   1303 C  CG    . GLN A 1 168 ? 9.155  -17.848 3.098  1.00 46.68 ? 177 GLN A CG    1 
ATOM   1304 C  CD    . GLN A 1 168 ? 9.805  -16.935 4.123  1.00 55.08 ? 177 GLN A CD    1 
ATOM   1305 O  OE1   . GLN A 1 168 ? 10.964 -17.128 4.497  1.00 51.32 ? 177 GLN A OE1   1 
ATOM   1306 N  NE2   . GLN A 1 168 ? 9.059  -15.935 4.586  1.00 54.00 ? 177 GLN A NE2   1 
ATOM   1307 N  N     . GLN A 1 169 ? 10.730 -22.134 1.400  1.00 47.17 ? 178 GLN A N     1 
ATOM   1308 C  CA    . GLN A 1 169 ? 11.767 -22.996 0.842  1.00 49.37 ? 178 GLN A CA    1 
ATOM   1309 C  C     . GLN A 1 169 ? 11.689 -23.097 -0.679 1.00 62.85 ? 178 GLN A C     1 
ATOM   1310 O  O     . GLN A 1 169 ? 12.716 -23.110 -1.360 1.00 55.74 ? 178 GLN A O     1 
ATOM   1311 C  CB    . GLN A 1 169 ? 11.654 -24.387 1.470  1.00 49.01 ? 178 GLN A CB    1 
ATOM   1312 C  CG    . GLN A 1 169 ? 12.664 -25.411 1.004  1.00 52.33 ? 178 GLN A CG    1 
ATOM   1313 C  CD    . GLN A 1 169 ? 12.463 -26.740 1.706  1.00 47.48 ? 178 GLN A CD    1 
ATOM   1314 O  OE1   . GLN A 1 169 ? 11.562 -26.881 2.537  1.00 42.18 ? 178 GLN A OE1   1 
ATOM   1315 N  NE2   . GLN A 1 169 ? 13.299 -27.719 1.380  1.00 51.93 ? 178 GLN A NE2   1 
ATOM   1316 O  OXT   . GLN A 1 169 ? 10.602 -23.163 -1.258 1.00 58.88 ? 178 GLN A OXT   1 
HETATM 1317 P  PG    . GNP B 2 .   ? 21.623 -32.529 26.754 1.00 34.16 ? 201 GNP A PG    1 
HETATM 1318 O  O1G   . GNP B 2 .   ? 22.495 -33.216 27.809 1.00 34.70 ? 201 GNP A O1G   1 
HETATM 1319 O  O2G   . GNP B 2 .   ? 20.152 -32.946 26.791 1.00 36.26 ? 201 GNP A O2G   1 
HETATM 1320 O  O3G   . GNP B 2 .   ? 22.214 -32.509 25.346 1.00 37.15 ? 201 GNP A O3G   1 
HETATM 1321 N  N3B   . GNP B 2 .   ? 21.650 -30.815 27.276 1.00 29.91 ? 201 GNP A N3B   1 
HETATM 1322 P  PB    . GNP B 2 .   ? 20.665 -29.689 26.524 1.00 31.87 ? 201 GNP A PB    1 
HETATM 1323 O  O1B   . GNP B 2 .   ? 21.264 -29.062 25.292 1.00 31.67 ? 201 GNP A O1B   1 
HETATM 1324 O  O2B   . GNP B 2 .   ? 19.249 -30.207 26.495 1.00 33.58 ? 201 GNP A O2B   1 
HETATM 1325 O  O3A   . GNP B 2 .   ? 20.746 -28.439 27.642 1.00 33.31 ? 201 GNP A O3A   1 
HETATM 1326 P  PA    . GNP B 2 .   ? 19.754 -28.256 28.910 1.00 33.37 ? 201 GNP A PA    1 
HETATM 1327 O  O1A   . GNP B 2 .   ? 18.460 -27.638 28.488 1.00 40.61 ? 201 GNP A O1A   1 
HETATM 1328 O  O2A   . GNP B 2 .   ? 19.787 -29.474 29.778 1.00 31.62 ? 201 GNP A O2A   1 
HETATM 1329 O  "O5'" . GNP B 2 .   ? 20.588 -27.017 29.628 1.00 40.39 ? 201 GNP A "O5'" 1 
HETATM 1330 C  "C5'" . GNP B 2 .   ? 21.814 -27.221 30.285 1.00 36.88 ? 201 GNP A "C5'" 1 
HETATM 1331 C  "C4'" . GNP B 2 .   ? 21.948 -26.270 31.461 1.00 35.49 ? 201 GNP A "C4'" 1 
HETATM 1332 O  "O4'" . GNP B 2 .   ? 22.065 -24.912 31.017 1.00 36.69 ? 201 GNP A "O4'" 1 
HETATM 1333 C  "C3'" . GNP B 2 .   ? 20.786 -26.284 32.456 1.00 34.73 ? 201 GNP A "C3'" 1 
HETATM 1334 O  "O3'" . GNP B 2 .   ? 21.322 -26.031 33.732 1.00 41.46 ? 201 GNP A "O3'" 1 
HETATM 1335 C  "C2'" . GNP B 2 .   ? 19.929 -25.114 31.983 1.00 35.05 ? 201 GNP A "C2'" 1 
HETATM 1336 O  "O2'" . GNP B 2 .   ? 19.129 -24.619 33.013 1.00 41.81 ? 201 GNP A "O2'" 1 
HETATM 1337 C  "C1'" . GNP B 2 .   ? 20.999 -24.131 31.486 1.00 35.75 ? 201 GNP A "C1'" 1 
HETATM 1338 N  N9    . GNP B 2 .   ? 20.542 -23.258 30.424 1.00 33.97 ? 201 GNP A N9    1 
HETATM 1339 C  C8    . GNP B 2 .   ? 19.928 -23.633 29.253 1.00 28.70 ? 201 GNP A C8    1 
HETATM 1340 N  N7    . GNP B 2 .   ? 19.634 -22.620 28.494 1.00 32.91 ? 201 GNP A N7    1 
HETATM 1341 C  C5    . GNP B 2 .   ? 20.075 -21.518 29.186 1.00 33.13 ? 201 GNP A C5    1 
HETATM 1342 C  C6    . GNP B 2 .   ? 20.030 -20.129 28.856 1.00 30.55 ? 201 GNP A C6    1 
HETATM 1343 O  O6    . GNP B 2 .   ? 19.583 -19.590 27.860 1.00 34.36 ? 201 GNP A O6    1 
HETATM 1344 N  N1    . GNP B 2 .   ? 20.604 -19.356 29.875 1.00 30.44 ? 201 GNP A N1    1 
HETATM 1345 C  C2    . GNP B 2 .   ? 21.141 -19.835 31.035 1.00 35.82 ? 201 GNP A C2    1 
HETATM 1346 N  N2    . GNP B 2 .   ? 21.643 -18.933 31.892 1.00 35.55 ? 201 GNP A N2    1 
HETATM 1347 N  N3    . GNP B 2 .   ? 21.179 -21.111 31.336 1.00 35.84 ? 201 GNP A N3    1 
HETATM 1348 C  C4    . GNP B 2 .   ? 20.640 -21.896 30.390 1.00 33.00 ? 201 GNP A C4    1 
HETATM 1349 MG MG    . MG  C 3 .   ? 18.449 -32.075 26.776 1.00 28.87 ? 202 MG  A MG    1 
HETATM 1350 ZN ZN    . ZN  D 4 .   ? 29.226 -6.342  33.179 1.00 51.03 ? 203 ZN  A ZN    1 
HETATM 1351 ZN ZN    . ZN  E 4 .   ? 27.549 -26.085 6.263  1.00 38.26 ? 204 ZN  A ZN    1 
HETATM 1352 O  O     . HOH F 5 .   ? 17.814 -38.192 20.448 1.00 59.44 ? 301 HOH A O     1 
HETATM 1353 O  O     . HOH F 5 .   ? 24.696 -31.000 -5.476 1.00 52.75 ? 302 HOH A O     1 
HETATM 1354 O  O     . HOH F 5 .   ? -5.677 -17.745 11.034 1.00 46.12 ? 303 HOH A O     1 
HETATM 1355 O  O     . HOH F 5 .   ? 35.489 -31.388 19.203 1.00 54.16 ? 304 HOH A O     1 
HETATM 1356 O  O     . HOH F 5 .   ? 35.678 -17.169 20.417 1.00 55.23 ? 305 HOH A O     1 
HETATM 1357 O  O     . HOH F 5 .   ? 5.978  -20.228 23.623 1.00 42.64 ? 306 HOH A O     1 
HETATM 1358 O  O     . HOH F 5 .   ? 30.377 -28.810 23.622 1.00 37.73 ? 307 HOH A O     1 
HETATM 1359 O  O     . HOH F 5 .   ? 12.941 -32.966 26.399 1.00 47.01 ? 308 HOH A O     1 
HETATM 1360 O  O     . HOH F 5 .   ? 18.064 -32.323 24.803 1.00 32.40 ? 309 HOH A O     1 
HETATM 1361 O  O     . HOH F 5 .   ? 9.184  -20.056 34.538 1.00 61.33 ? 310 HOH A O     1 
HETATM 1362 O  O     . HOH F 5 .   ? 13.198 -17.872 3.662  1.00 44.63 ? 311 HOH A O     1 
HETATM 1363 O  O     . HOH F 5 .   ? 27.157 -15.735 18.862 1.00 30.11 ? 312 HOH A O     1 
HETATM 1364 O  O     . HOH F 5 .   ? 10.860 -13.498 11.183 1.00 39.96 ? 313 HOH A O     1 
HETATM 1365 O  O     . HOH F 5 .   ? 8.516  -36.252 8.451  1.00 35.11 ? 314 HOH A O     1 
HETATM 1366 O  O     . HOH F 5 .   ? 26.868 -24.034 27.960 1.00 33.06 ? 315 HOH A O     1 
HETATM 1367 O  O     . HOH F 5 .   ? 24.135 -9.878  21.546 1.00 39.96 ? 316 HOH A O     1 
HETATM 1368 O  O     . HOH F 5 .   ? 13.214 -23.740 29.902 1.00 40.44 ? 317 HOH A O     1 
HETATM 1369 O  O     . HOH F 5 .   ? 11.521 -34.368 22.204 1.00 31.12 ? 318 HOH A O     1 
HETATM 1370 O  O     . HOH F 5 .   ? 16.797 -14.365 29.606 1.00 44.36 ? 319 HOH A O     1 
HETATM 1371 O  O     . HOH F 5 .   ? 1.009  -23.775 8.123  1.00 34.78 ? 320 HOH A O     1 
HETATM 1372 O  O     . HOH F 5 .   ? 2.470  -25.715 24.183 1.00 37.66 ? 321 HOH A O     1 
HETATM 1373 O  O     . HOH F 5 .   ? 3.250  -17.139 4.804  1.00 51.26 ? 322 HOH A O     1 
HETATM 1374 O  O     . HOH F 5 .   ? 15.381 -16.053 11.917 1.00 31.61 ? 323 HOH A O     1 
HETATM 1375 O  O     . HOH F 5 .   ? 16.225 -35.374 1.046  1.00 43.66 ? 324 HOH A O     1 
HETATM 1376 O  O     . HOH F 5 .   ? -3.266 -23.090 8.104  1.00 34.40 ? 325 HOH A O     1 
HETATM 1377 O  O     . HOH F 5 .   ? 10.966 -38.440 15.807 1.00 37.08 ? 326 HOH A O     1 
HETATM 1378 O  O     . HOH F 5 .   ? 23.980 -24.675 2.199  1.00 30.61 ? 327 HOH A O     1 
HETATM 1379 O  O     . HOH F 5 .   ? 21.669 -14.905 33.665 1.00 47.29 ? 328 HOH A O     1 
HETATM 1380 O  O     . HOH F 5 .   ? 27.487 -26.567 26.514 1.00 38.11 ? 329 HOH A O     1 
HETATM 1381 O  O     . HOH F 5 .   ? 21.214 -34.680 29.711 1.00 58.89 ? 330 HOH A O     1 
HETATM 1382 O  O     . HOH F 5 .   ? 22.714 -15.538 8.045  1.00 40.47 ? 331 HOH A O     1 
HETATM 1383 O  O     . HOH F 5 .   ? 2.892  -14.855 13.408 1.00 35.40 ? 332 HOH A O     1 
HETATM 1384 O  O     . HOH F 5 .   ? 19.715 -19.127 4.170  1.00 41.55 ? 333 HOH A O     1 
HETATM 1385 O  O     . HOH F 5 .   ? 4.588  -25.179 4.269  1.00 37.45 ? 334 HOH A O     1 
HETATM 1386 O  O     . HOH F 5 .   ? 20.209 -12.090 13.473 1.00 49.20 ? 335 HOH A O     1 
HETATM 1387 O  O     . HOH F 5 .   ? 19.927 -14.254 10.111 1.00 32.78 ? 336 HOH A O     1 
HETATM 1388 O  O     . HOH F 5 .   ? 29.139 -30.110 25.659 1.00 46.40 ? 337 HOH A O     1 
HETATM 1389 O  O     . HOH F 5 .   ? 19.190 -12.459 17.459 1.00 33.22 ? 338 HOH A O     1 
HETATM 1390 O  O     . HOH F 5 .   ? 28.164 -32.603 23.245 1.00 44.33 ? 339 HOH A O     1 
HETATM 1391 O  O     . HOH F 5 .   ? 20.525 -35.615 27.310 1.00 46.99 ? 340 HOH A O     1 
HETATM 1392 O  O     . HOH F 5 .   ? 17.514 -33.769 27.106 1.00 34.04 ? 341 HOH A O     1 
HETATM 1393 O  O     . HOH F 5 .   ? 12.658 -16.186 6.447  1.00 48.88 ? 342 HOH A O     1 
HETATM 1394 O  O     . HOH F 5 .   ? 6.975  -37.585 14.953 1.00 27.11 ? 343 HOH A O     1 
HETATM 1395 O  O     . HOH F 5 .   ? 11.278 -28.961 4.665  1.00 25.94 ? 344 HOH A O     1 
HETATM 1396 O  O     . HOH F 5 .   ? 18.490 -31.823 28.689 1.00 35.60 ? 345 HOH A O     1 
HETATM 1397 O  O     . HOH F 5 .   ? 20.130 -22.797 34.833 1.00 49.62 ? 346 HOH A O     1 
HETATM 1398 O  O     . HOH F 5 .   ? 26.385 -27.174 19.529 1.00 30.14 ? 347 HOH A O     1 
HETATM 1399 O  O     . HOH F 5 .   ? 16.774 -28.011 30.653 1.00 45.63 ? 348 HOH A O     1 
HETATM 1400 O  O     . HOH F 5 .   ? 0.164  -22.669 5.945  1.00 50.47 ? 349 HOH A O     1 
HETATM 1401 O  O     . HOH F 5 .   ? 1.376  -28.600 23.576 1.00 43.13 ? 350 HOH A O     1 
HETATM 1402 O  O     . HOH F 5 .   ? 8.132  -38.179 12.555 1.00 32.97 ? 351 HOH A O     1 
HETATM 1403 O  O     . HOH F 5 .   ? 25.436 -11.450 25.723 1.00 41.72 ? 352 HOH A O     1 
HETATM 1404 O  O     . HOH F 5 .   ? 6.896  -17.520 5.371  1.00 45.52 ? 353 HOH A O     1 
HETATM 1405 O  O     . HOH F 5 .   ? 17.996 -22.350 6.156  1.00 28.14 ? 354 HOH A O     1 
HETATM 1406 O  O     . HOH F 5 .   ? 34.419 -11.103 17.009 1.00 47.93 ? 355 HOH A O     1 
HETATM 1407 O  O     . HOH F 5 .   ? 13.327 -20.429 2.834  1.00 40.84 ? 356 HOH A O     1 
HETATM 1408 O  O     . HOH F 5 .   ? 21.104 -25.589 5.141  1.00 29.03 ? 357 HOH A O     1 
HETATM 1409 O  O     . HOH F 5 .   ? 27.215 -33.006 3.899  1.00 36.10 ? 358 HOH A O     1 
HETATM 1410 O  O     . HOH F 5 .   ? -3.676 -28.676 5.216  1.00 44.88 ? 359 HOH A O     1 
HETATM 1411 O  O     . HOH F 5 .   ? 3.754  -21.096 19.531 1.00 30.31 ? 360 HOH A O     1 
HETATM 1412 O  O     . HOH F 5 .   ? 10.219 -14.991 20.615 1.00 34.72 ? 361 HOH A O     1 
HETATM 1413 O  O     . HOH F 5 .   ? 1.963  -22.871 23.072 1.00 46.05 ? 362 HOH A O     1 
HETATM 1414 O  O     . HOH F 5 .   ? 7.886  -17.408 29.726 1.00 55.23 ? 363 HOH A O     1 
HETATM 1415 O  O     . HOH F 5 .   ? 0.647  -21.941 20.453 1.00 42.07 ? 364 HOH A O     1 
HETATM 1416 O  O     . HOH F 5 .   ? -4.816 -21.114 9.100  1.00 36.94 ? 365 HOH A O     1 
HETATM 1417 O  O     . HOH F 5 .   ? 4.888  -17.883 6.924  1.00 37.50 ? 366 HOH A O     1 
HETATM 1418 O  O     . HOH F 5 .   ? 5.642  -34.904 12.150 1.00 27.03 ? 367 HOH A O     1 
HETATM 1419 O  O     . HOH F 5 .   ? 11.839 -12.441 23.227 1.00 37.82 ? 368 HOH A O     1 
HETATM 1420 O  O     . HOH F 5 .   ? 25.463 -32.467 0.880  1.00 46.75 ? 369 HOH A O     1 
HETATM 1421 O  O     . HOH F 5 .   ? -2.782 -17.124 17.619 1.00 41.99 ? 370 HOH A O     1 
HETATM 1422 O  O     . HOH F 5 .   ? 25.711 -17.083 2.719  1.00 47.36 ? 371 HOH A O     1 
HETATM 1423 O  O     . HOH F 5 .   ? 29.251 -9.919  20.954 1.00 46.69 ? 372 HOH A O     1 
HETATM 1424 O  O     . HOH F 5 .   ? 33.031 -27.430 26.468 1.00 54.52 ? 373 HOH A O     1 
HETATM 1425 O  O     . HOH F 5 .   ? 23.183 -23.183 0.000  0.50 39.14 ? 374 HOH A O     1 
HETATM 1426 O  O     . HOH F 5 .   ? 21.888 -33.376 18.922 1.00 32.38 ? 375 HOH A O     1 
HETATM 1427 O  O     . HOH F 5 .   ? 22.051 -34.538 16.378 1.00 41.12 ? 376 HOH A O     1 
HETATM 1428 O  O     . HOH F 5 .   ? 12.747 -33.745 3.395  1.00 38.53 ? 377 HOH A O     1 
HETATM 1429 O  O     . HOH F 5 .   ? 6.586  -12.290 10.128 1.00 41.96 ? 378 HOH A O     1 
HETATM 1430 O  O     . HOH F 5 .   ? 19.522 -27.824 -1.963 1.00 36.70 ? 379 HOH A O     1 
HETATM 1431 O  O     . HOH F 5 .   ? 34.558 -22.787 26.044 1.00 41.69 ? 380 HOH A O     1 
HETATM 1432 O  O     . HOH F 5 .   ? 32.845 -17.459 12.757 1.00 41.46 ? 381 HOH A O     1 
HETATM 1433 O  O     . HOH F 5 .   ? 15.577 -35.129 25.329 1.00 52.02 ? 382 HOH A O     1 
HETATM 1434 O  O     . HOH F 5 .   ? 26.993 -13.385 33.007 1.00 41.17 ? 383 HOH A O     1 
HETATM 1435 O  O     . HOH F 5 .   ? 2.667  -21.021 3.481  1.00 41.77 ? 384 HOH A O     1 
HETATM 1436 O  O     . HOH F 5 .   ? 33.036 -7.537  17.825 1.00 58.61 ? 385 HOH A O     1 
HETATM 1437 O  O     . HOH F 5 .   ? 22.299 -23.727 3.586  1.00 37.86 ? 386 HOH A O     1 
HETATM 1438 O  O     . HOH F 5 .   ? 25.637 -26.217 30.875 1.00 44.62 ? 387 HOH A O     1 
HETATM 1439 O  O     . HOH F 5 .   ? 34.723 -25.567 25.265 1.00 53.70 ? 388 HOH A O     1 
HETATM 1440 O  O     . HOH F 5 .   ? 10.596 -15.969 23.730 1.00 34.12 ? 389 HOH A O     1 
HETATM 1441 O  O     . HOH F 5 .   ? 22.765 -15.889 0.782  1.00 50.46 ? 390 HOH A O     1 
HETATM 1442 O  O     . HOH F 5 .   ? 26.513 -27.602 0.905  1.00 35.54 ? 391 HOH A O     1 
HETATM 1443 O  O     . HOH F 5 .   ? 16.717 -25.086 0.941  1.00 44.84 ? 392 HOH A O     1 
HETATM 1444 O  O     . HOH F 5 .   ? 22.379 -19.848 34.733 1.00 49.03 ? 393 HOH A O     1 
HETATM 1445 O  O     . HOH F 5 .   ? 29.339 -23.725 29.216 1.00 40.97 ? 394 HOH A O     1 
HETATM 1446 O  O     . HOH F 5 .   ? 11.131 -40.072 20.360 1.00 49.30 ? 395 HOH A O     1 
HETATM 1447 O  O     . HOH F 5 .   ? 24.367 -14.079 9.583  1.00 38.29 ? 396 HOH A O     1 
HETATM 1448 O  O     . HOH F 5 .   ? -0.140 -15.077 13.559 1.00 38.06 ? 397 HOH A O     1 
HETATM 1449 O  O     . HOH F 5 .   ? 16.920 -24.212 2.973  1.00 34.25 ? 398 HOH A O     1 
HETATM 1450 O  O     . HOH F 5 .   ? 30.952 -5.148  14.741 1.00 58.67 ? 399 HOH A O     1 
HETATM 1451 O  O     . HOH F 5 .   ? 25.017 -34.863 26.746 1.00 58.00 ? 400 HOH A O     1 
HETATM 1452 O  O     . HOH F 5 .   ? 20.140 -30.608 -3.038 1.00 51.84 ? 401 HOH A O     1 
HETATM 1453 O  O     . HOH F 5 .   ? 14.803 -33.613 1.354  1.00 43.78 ? 402 HOH A O     1 
HETATM 1454 O  O     . HOH F 5 .   ? 31.487 -16.092 6.535  1.00 47.37 ? 403 HOH A O     1 
HETATM 1455 O  O     . HOH F 5 .   ? 7.711  -14.893 15.593 1.00 34.31 ? 404 HOH A O     1 
HETATM 1456 O  O     . HOH F 5 .   ? 3.688  -32.313 23.890 1.00 47.58 ? 405 HOH A O     1 
HETATM 1457 O  O     . HOH F 5 .   ? -0.377 -19.103 18.414 1.00 47.78 ? 406 HOH A O     1 
HETATM 1458 O  O     . HOH F 5 .   ? 31.591 -28.502 7.848  1.00 50.39 ? 407 HOH A O     1 
HETATM 1459 O  O     . HOH F 5 .   ? 24.716 -33.574 -1.762 1.00 58.00 ? 408 HOH A O     1 
HETATM 1460 O  O     . HOH F 5 .   ? 24.116 -22.532 32.045 1.00 47.63 ? 409 HOH A O     1 
HETATM 1461 O  O     . HOH F 5 .   ? 17.733 -38.340 0.060  1.00 53.25 ? 410 HOH A O     1 
HETATM 1462 O  O     . HOH F 5 .   ? 16.897 -31.447 -4.187 1.00 51.98 ? 411 HOH A O     1 
HETATM 1463 O  O     . HOH F 5 .   ? 19.408 -23.155 4.064  1.00 43.49 ? 412 HOH A O     1 
HETATM 1464 O  O     . HOH F 5 .   ? 7.293  -39.450 17.357 1.00 50.74 ? 413 HOH A O     1 
HETATM 1465 O  O     . HOH F 5 .   ? 20.824 -18.654 -1.139 1.00 48.25 ? 414 HOH A O     1 
HETATM 1466 O  O     . HOH F 5 .   ? 24.158 -34.312 19.665 1.00 44.23 ? 415 HOH A O     1 
HETATM 1467 O  O     . HOH F 5 .   ? -1.727 -14.152 14.857 1.00 53.70 ? 416 HOH A O     1 
HETATM 1468 O  O     . HOH F 5 .   ? 31.284 -6.005  32.376 1.00 51.65 ? 417 HOH A O     1 
HETATM 1469 O  O     . HOH F 5 .   ? 14.237 -32.805 28.998 1.00 48.11 ? 418 HOH A O     1 
HETATM 1470 O  O     . HOH F 5 .   ? 28.700 -27.968 6.307  1.00 30.41 ? 419 HOH A O     1 
HETATM 1471 O  O     . HOH F 5 .   ? 12.830 -16.520 8.760  1.00 42.26 ? 420 HOH A O     1 
HETATM 1472 O  O     . HOH F 5 .   ? 5.660  -13.430 6.039  1.00 61.24 ? 421 HOH A O     1 
HETATM 1473 O  O     . HOH F 5 .   ? 6.797  -14.761 17.662 1.00 52.63 ? 422 HOH A O     1 
HETATM 1474 O  O     . HOH F 5 .   ? 9.543  -13.024 24.419 1.00 52.30 ? 423 HOH A O     1 
HETATM 1475 O  O     . HOH F 5 .   ? 20.161 -16.423 5.715  1.00 51.90 ? 424 HOH A O     1 
HETATM 1476 O  O     . HOH F 5 .   ? 3.858  -40.550 25.103 1.00 57.32 ? 425 HOH A O     1 
HETATM 1477 O  O     . HOH F 5 .   ? 7.775  -36.549 11.133 1.00 32.72 ? 426 HOH A O     1 
HETATM 1478 O  O     . HOH F 5 .   ? 6.819  -20.447 -1.704 1.00 59.50 ? 427 HOH A O     1 
HETATM 1479 O  O     . HOH F 5 .   ? 23.178 -3.421  19.045 1.00 62.20 ? 428 HOH A O     1 
HETATM 1480 O  O     . HOH F 5 .   ? -2.464 -33.458 6.372  1.00 47.35 ? 429 HOH A O     1 
HETATM 1481 O  O     . HOH F 5 .   ? 33.026 -19.375 10.975 1.00 42.17 ? 430 HOH A O     1 
HETATM 1482 O  O     . HOH F 5 .   ? 30.312 -37.117 11.626 1.00 46.72 ? 431 HOH A O     1 
HETATM 1483 O  O     . HOH F 5 .   ? 10.630 -35.127 4.767  1.00 53.06 ? 432 HOH A O     1 
HETATM 1484 O  O     . HOH F 5 .   ? 30.330 -28.539 28.523 1.00 56.71 ? 433 HOH A O     1 
HETATM 1485 O  O     . HOH F 5 .   ? -0.000 -32.740 23.704 0.50 54.22 ? 434 HOH A O     1 
HETATM 1486 O  O     . HOH F 5 .   ? -8.583 -30.703 5.819  1.00 43.52 ? 435 HOH A O     1 
HETATM 1487 O  O     . HOH F 5 .   ? 27.961 -27.422 29.174 1.00 48.30 ? 436 HOH A O     1 
HETATM 1488 O  O     . HOH F 5 .   ? 29.857 -5.961  12.782 1.00 56.46 ? 437 HOH A O     1 
HETATM 1489 O  O     . HOH F 5 .   ? 16.146 -35.015 -1.866 1.00 52.58 ? 438 HOH A O     1 
HETATM 1490 O  O     . HOH F 5 .   ? 16.408 -11.816 15.626 1.00 43.54 ? 439 HOH A O     1 
HETATM 1491 O  O     . HOH F 5 .   ? 26.933 -30.729 0.560  1.00 46.22 ? 440 HOH A O     1 
HETATM 1492 O  O     . HOH F 5 .   ? 24.081 -35.649 30.646 1.00 69.78 ? 441 HOH A O     1 
HETATM 1493 O  O     . HOH F 5 .   ? 23.449 -33.028 -4.266 1.00 56.46 ? 442 HOH A O     1 
HETATM 1494 O  O     . HOH F 5 .   ? -8.889 -20.148 11.485 1.00 52.50 ? 443 HOH A O     1 
HETATM 1495 O  O     . HOH F 5 .   ? 7.215  -29.175 4.503  1.00 47.02 ? 444 HOH A O     1 
HETATM 1496 O  O     . HOH F 5 .   ? 14.965 -16.186 9.332  1.00 35.39 ? 445 HOH A O     1 
HETATM 1497 O  O     . HOH F 5 .   ? 2.730  -19.426 30.925 1.00 51.51 ? 446 HOH A O     1 
HETATM 1498 O  O     . HOH F 5 .   ? 11.232 -14.702 8.315  1.00 44.64 ? 447 HOH A O     1 
HETATM 1499 O  O     . HOH F 5 .   ? -7.363 -23.603 15.231 1.00 50.52 ? 448 HOH A O     1 
HETATM 1500 O  O     . HOH F 5 .   ? 5.116  -18.041 2.776  1.00 54.26 ? 449 HOH A O     1 
HETATM 1501 O  O     . HOH F 5 .   ? 24.627 -28.324 31.640 1.00 44.67 ? 450 HOH A O     1 
HETATM 1502 O  O     . HOH F 5 .   ? -4.052 -10.244 7.366  1.00 60.35 ? 451 HOH A O     1 
HETATM 1503 O  O     . HOH F 5 .   ? 0.566  -24.640 3.752  1.00 50.59 ? 452 HOH A O     1 
HETATM 1504 O  O     . HOH F 5 .   ? 8.382  -40.235 11.738 1.00 42.22 ? 453 HOH A O     1 
HETATM 1505 O  O     . HOH F 5 .   ? 10.445 -30.999 0.615  1.00 45.74 ? 454 HOH A O     1 
HETATM 1506 O  O     . HOH F 5 .   ? 17.470 -19.846 4.813  1.00 31.76 ? 455 HOH A O     1 
HETATM 1507 O  O     . HOH F 5 .   ? 7.673  -38.347 8.206  1.00 50.30 ? 456 HOH A O     1 
HETATM 1508 O  O     . HOH F 5 .   ? 27.478 -15.163 34.449 1.00 42.55 ? 457 HOH A O     1 
HETATM 1509 O  O     . HOH F 5 .   ? 9.135  -32.438 1.921  1.00 52.29 ? 458 HOH A O     1 
HETATM 1510 O  O     . HOH F 5 .   ? 4.911  -20.474 35.925 1.00 62.87 ? 459 HOH A O     1 
HETATM 1511 O  O     . HOH F 5 .   ? 16.225 -21.481 2.864  1.00 51.28 ? 460 HOH A O     1 
HETATM 1512 O  O     . HOH F 5 .   ? 15.872 -17.528 5.125  1.00 39.43 ? 461 HOH A O     1 
HETATM 1513 O  O     . HOH F 5 .   ? 25.301 -14.171 2.420  1.00 52.68 ? 462 HOH A O     1 
HETATM 1514 O  O     . HOH F 5 .   ? 28.600 -10.334 5.131  1.00 63.25 ? 463 HOH A O     1 
HETATM 1515 O  O     . HOH F 5 .   ? 8.108  -40.841 9.504  1.00 49.88 ? 464 HOH A O     1 
HETATM 1516 O  O     . HOH F 5 .   ? 33.828 -21.021 3.787  1.00 50.79 ? 465 HOH A O     1 
HETATM 1517 O  O     . HOH F 5 .   ? -1.267 -24.711 25.488 1.00 62.43 ? 466 HOH A O     1 
HETATM 1518 O  O     . HOH F 5 .   ? 25.771 -16.403 35.781 1.00 49.59 ? 467 HOH A O     1 
HETATM 1519 O  O     . HOH F 5 .   ? 16.429 -5.907  20.936 1.00 60.18 ? 468 HOH A O     1 
HETATM 1520 O  O     . HOH F 5 .   ? 5.109  -38.893 6.070  1.00 49.98 ? 469 HOH A O     1 
HETATM 1521 O  O     . HOH F 5 .   ? 26.563 -16.592 38.238 1.00 52.49 ? 470 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . GLY A 1   ? 0.2465 0.4410 0.3928 -0.0819 -0.0397 -0.0201 10  GLY A N     
2    C  CA    . GLY A 1   ? 0.2277 0.4381 0.3897 -0.0678 -0.0326 -0.0224 10  GLY A CA    
3    C  C     . GLY A 1   ? 0.2368 0.4289 0.3930 -0.0487 -0.0378 -0.0204 10  GLY A C     
4    O  O     . GLY A 1   ? 0.2646 0.4407 0.4097 -0.0458 -0.0491 -0.0162 10  GLY A O     
5    N  N     . LEU A 2   ? 0.2545 0.4504 0.4170 -0.0378 -0.0294 -0.0234 11  LEU A N     
6    C  CA    . LEU A 2   ? 0.2343 0.4121 0.3930 -0.0212 -0.0340 -0.0218 11  LEU A CA    
7    C  C     . LEU A 2   ? 0.2976 0.4376 0.4230 -0.0241 -0.0331 -0.0142 11  LEU A C     
8    O  O     . LEU A 2   ? 0.3033 0.4297 0.4111 -0.0348 -0.0253 -0.0123 11  LEU A O     
9    C  CB    . LEU A 2   ? 0.2335 0.4228 0.4037 -0.0115 -0.0239 -0.0293 11  LEU A CB    
10   C  CG    . LEU A 2   ? 0.2514 0.4815 0.4589 -0.0045 -0.0226 -0.0421 11  LEU A CG    
11   C  CD1   . LEU A 2   ? 0.2417 0.4805 0.4517 0.0016  -0.0097 -0.0517 11  LEU A CD1   
12   C  CD2   . LEU A 2   ? 0.1945 0.4290 0.4279 0.0108  -0.0402 -0.0434 11  LEU A CD2   
13   N  N     . PRO A 3   ? 0.3066 0.4300 0.4249 -0.0149 -0.0413 -0.0099 12  PRO A N     
14   C  CA    . PRO A 3   ? 0.2274 0.3215 0.3176 -0.0167 -0.0380 -0.0053 12  PRO A CA    
15   C  C     . PRO A 3   ? 0.2390 0.3241 0.3217 -0.0152 -0.0251 -0.0068 12  PRO A C     
16   O  O     . PRO A 3   ? 0.2530 0.3494 0.3481 -0.0082 -0.0206 -0.0104 12  PRO A O     
17   C  CB    . PRO A 3   ? 0.3339 0.4191 0.4235 -0.0075 -0.0483 0.0000  12  PRO A CB    
18   C  CG    . PRO A 3   ? 0.2649 0.3696 0.3780 -0.0038 -0.0621 0.0008  12  PRO A CG    
19   C  CD    . PRO A 3   ? 0.3040 0.4350 0.4412 -0.0034 -0.0552 -0.0084 12  PRO A CD    
20   N  N     . THR A 4   ? 0.2475 0.3134 0.3108 -0.0218 -0.0199 -0.0050 13  THR A N     
21   C  CA    . THR A 4   ? 0.2900 0.3455 0.3453 -0.0212 -0.0107 -0.0037 13  THR A CA    
22   C  C     . THR A 4   ? 0.2643 0.2997 0.3056 -0.0152 -0.0101 -0.0021 13  THR A C     
23   O  O     . THR A 4   ? 0.3371 0.3611 0.3679 -0.0180 -0.0125 -0.0032 13  THR A O     
24   C  CB    . THR A 4   ? 0.3563 0.4047 0.4057 -0.0335 -0.0067 -0.0021 13  THR A CB    
25   O  OG1   . THR A 4   ? 0.4636 0.5354 0.5268 -0.0419 -0.0062 -0.0034 13  THR A OG1   
26   C  CG2   . THR A 4   ? 0.4376 0.4741 0.4786 -0.0328 -0.0006 0.0027  13  THR A CG2   
27   N  N     . TYR A 5   ? 0.2943 0.3287 0.3359 -0.0079 -0.0064 -0.0012 14  TYR A N     
28   C  CA    . TYR A 5   ? 0.2329 0.2531 0.2647 -0.0028 -0.0051 0.0000  14  TYR A CA    
29   C  C     . TYR A 5   ? 0.3146 0.3275 0.3417 -0.0026 0.0001  0.0024  14  TYR A C     
30   O  O     . TYR A 5   ? 0.3193 0.3419 0.3495 -0.0024 0.0028  0.0037  14  TYR A O     
31   C  CB    . TYR A 5   ? 0.2565 0.2806 0.2934 0.0046  -0.0082 0.0000  14  TYR A CB    
32   C  CG    . TYR A 5   ? 0.3563 0.3847 0.3992 0.0048  -0.0171 0.0011  14  TYR A CG    
33   C  CD1   . TYR A 5   ? 0.3796 0.4002 0.4110 0.0011  -0.0218 0.0048  14  TYR A CD1   
34   C  CD2   . TYR A 5   ? 0.2362 0.2790 0.2969 0.0081  -0.0214 -0.0014 14  TYR A CD2   
35   C  CE1   . TYR A 5   ? 0.3330 0.3569 0.3676 -0.0003 -0.0327 0.0094  14  TYR A CE1   
36   C  CE2   . TYR A 5   ? 0.3037 0.3496 0.3731 0.0096  -0.0327 0.0014  14  TYR A CE2   
37   C  CZ    . TYR A 5   ? 0.2629 0.2977 0.3176 0.0049  -0.0394 0.0086  14  TYR A CZ    
38   O  OH    . TYR A 5   ? 0.2999 0.3372 0.3612 0.0049  -0.0534 0.0148  14  TYR A OH    
39   N  N     . LYS A 6   ? 0.2593 0.2567 0.2795 -0.0028 0.0009  0.0024  15  LYS A N     
40   C  CA    . LYS A 6   ? 0.2682 0.2556 0.2864 -0.0007 0.0023  0.0065  15  LYS A CA    
41   C  C     . LYS A 6   ? 0.3024 0.2919 0.3208 0.0076  0.0029  0.0058  15  LYS A C     
42   O  O     . LYS A 6   ? 0.3348 0.3209 0.3525 0.0107  0.0035  0.0011  15  LYS A O     
43   C  CB    . LYS A 6   ? 0.2627 0.2312 0.2796 -0.0029 0.0012  0.0047  15  LYS A CB    
44   C  CG    . LYS A 6   ? 0.2706 0.2248 0.2890 0.0008  -0.0009 0.0107  15  LYS A CG    
45   C  CD    . LYS A 6   ? 0.3499 0.3062 0.3648 -0.0070 -0.0024 0.0226  15  LYS A CD    
46   C  CE    . LYS A 6   ? 0.3128 0.2511 0.3279 -0.0051 -0.0083 0.0324  15  LYS A CE    
47   N  NZ    . LYS A 6   ? 0.4130 0.3243 0.4336 -0.0057 -0.0127 0.0303  15  LYS A NZ    
48   N  N     . LEU A 7   ? 0.2914 0.2894 0.3102 0.0094  0.0032  0.0092  16  LEU A N     
49   C  CA    . LEU A 7   ? 0.2871 0.2891 0.3069 0.0153  0.0028  0.0083  16  LEU A CA    
50   C  C     . LEU A 7   ? 0.3030 0.3007 0.3217 0.0176  0.0008  0.0141  16  LEU A C     
51   O  O     . LEU A 7   ? 0.3326 0.3307 0.3466 0.0130  -0.0005 0.0209  16  LEU A O     
52   C  CB    . LEU A 7   ? 0.2296 0.2445 0.2516 0.0157  0.0031  0.0055  16  LEU A CB    
53   C  CG    . LEU A 7   ? 0.2472 0.2664 0.2748 0.0148  0.0020  0.0015  16  LEU A CG    
54   C  CD1   . LEU A 7   ? 0.2057 0.2348 0.2407 0.0181  0.0012  -0.0042 16  LEU A CD1   
55   C  CD2   . LEU A 7   ? 0.2138 0.2251 0.2398 0.0147  -0.0004 0.0016  16  LEU A CD2   
56   N  N     . VAL A 8   ? 0.3710 0.3669 0.3946 0.0237  -0.0003 0.0122  17  VAL A N     
57   C  CA    . VAL A 8   ? 0.2364 0.2285 0.2638 0.0283  -0.0050 0.0179  17  VAL A CA    
58   C  C     . VAL A 8   ? 0.2804 0.2866 0.3104 0.0313  -0.0065 0.0171  17  VAL A C     
59   O  O     . VAL A 8   ? 0.2920 0.3052 0.3267 0.0328  -0.0036 0.0103  17  VAL A O     
60   C  CB    . VAL A 8   ? 0.2810 0.2609 0.3187 0.0346  -0.0059 0.0137  17  VAL A CB    
61   C  CG1   . VAL A 8   ? 0.2654 0.2406 0.3122 0.0417  -0.0139 0.0205  17  VAL A CG1   
62   C  CG2   . VAL A 8   ? 0.3406 0.3047 0.3751 0.0298  -0.0051 0.0127  17  VAL A CG2   
63   N  N     . VAL A 9   ? 0.2938 0.3049 0.3192 0.0299  -0.0116 0.0247  18  VAL A N     
64   C  CA    . VAL A 9   ? 0.2751 0.3008 0.3017 0.0310  -0.0146 0.0238  18  VAL A CA    
65   C  C     . VAL A 9   ? 0.3367 0.3624 0.3743 0.0383  -0.0224 0.0291  18  VAL A C     
66   O  O     . VAL A 9   ? 0.3494 0.3668 0.3848 0.0387  -0.0300 0.0403  18  VAL A O     
67   C  CB    . VAL A 9   ? 0.3265 0.3626 0.3393 0.0235  -0.0155 0.0264  18  VAL A CB    
68   C  CG1   . VAL A 9   ? 0.2559 0.3070 0.2690 0.0233  -0.0191 0.0231  18  VAL A CG1   
69   C  CG2   . VAL A 9   ? 0.2577 0.2958 0.2663 0.0190  -0.0081 0.0186  18  VAL A CG2   
70   N  N     . VAL A 10  ? 0.2729 0.3088 0.3241 0.0434  -0.0214 0.0219  19  VAL A N     
71   C  CA    . VAL A 10  ? 0.2817 0.3232 0.3506 0.0525  -0.0286 0.0238  19  VAL A CA    
72   C  C     . VAL A 10  ? 0.3345 0.3979 0.4082 0.0510  -0.0320 0.0219  19  VAL A C     
73   O  O     . VAL A 10  ? 0.2838 0.3549 0.3496 0.0433  -0.0271 0.0163  19  VAL A O     
74   C  CB    . VAL A 10  ? 0.3746 0.4140 0.4611 0.0604  -0.0231 0.0134  19  VAL A CB    
75   C  CG1   . VAL A 10  ? 0.3272 0.3440 0.4083 0.0605  -0.0203 0.0132  19  VAL A CG1   
76   C  CG2   . VAL A 10  ? 0.2981 0.3527 0.3856 0.0554  -0.0132 0.0024  19  VAL A CG2   
77   N  N     . GLY A 11  ? 0.3434 0.4159 0.4324 0.0585  -0.0420 0.0265  20  GLY A N     
78   C  CA    . GLY A 11  ? 0.2842 0.3801 0.3802 0.0566  -0.0475 0.0252  20  GLY A CA    
79   C  C     . GLY A 11  ? 0.3556 0.4571 0.4600 0.0629  -0.0638 0.0373  20  GLY A C     
80   O  O     . GLY A 11  ? 0.3132 0.3971 0.4118 0.0657  -0.0718 0.0497  20  GLY A O     
81   N  N     . ASP A 12  ? 0.2752 0.4016 0.3938 0.0638  -0.0703 0.0350  21  ASP A N     
82   C  CA    . ASP A 12  ? 0.3153 0.4517 0.4442 0.0697  -0.0889 0.0473  21  ASP A CA    
83   C  C     . ASP A 12  ? 0.3566 0.4846 0.4545 0.0594  -0.0982 0.0628  21  ASP A C     
84   O  O     . ASP A 12  ? 0.3513 0.4745 0.4226 0.0472  -0.0890 0.0595  21  ASP A O     
85   C  CB    . ASP A 12  ? 0.2913 0.4609 0.4385 0.0688  -0.0937 0.0408  21  ASP A CB    
86   C  CG    . ASP A 12  ? 0.4128 0.5987 0.6001 0.0832  -0.0935 0.0319  21  ASP A CG    
87   O  OD1   . ASP A 12  ? 0.4512 0.6218 0.6501 0.0932  -0.0863 0.0266  21  ASP A OD1   
88   O  OD2   . ASP A 12  ? 0.4130 0.6298 0.6215 0.0842  -0.1004 0.0284  21  ASP A OD2   
89   N  N     . GLY A 13  ? 0.4055 0.5340 0.5081 0.0642  -0.1172 0.0796  22  GLY A N     
90   C  CA    . GLY A 13  ? 0.3849 0.5111 0.4555 0.0514  -0.1274 0.0963  22  GLY A CA    
91   C  C     . GLY A 13  ? 0.3375 0.4897 0.3892 0.0374  -0.1258 0.0886  22  GLY A C     
92   O  O     . GLY A 13  ? 0.4083 0.5832 0.4773 0.0393  -0.1287 0.0794  22  GLY A O     
93   N  N     . GLY A 14  ? 0.3377 0.4878 0.3547 0.0223  -0.1204 0.0902  23  GLY A N     
94   C  CA    . GLY A 14  ? 0.3309 0.5039 0.3275 0.0082  -0.1190 0.0804  23  GLY A CA    
95   C  C     . GLY A 14  ? 0.3577 0.5333 0.3581 0.0056  -0.1017 0.0562  23  GLY A C     
96   O  O     . GLY A 14  ? 0.3826 0.5746 0.3694 -0.0054 -0.1007 0.0447  23  GLY A O     
97   N  N     . VAL A 15  ? 0.3039 0.4632 0.3218 0.0143  -0.0893 0.0482  24  VAL A N     
98   C  CA    . VAL A 15  ? 0.2655 0.4249 0.2874 0.0108  -0.0762 0.0290  24  VAL A CA    
99   C  C     . VAL A 15  ? 0.3882 0.5390 0.3880 0.0027  -0.0651 0.0201  24  VAL A C     
100  O  O     . VAL A 15  ? 0.3145 0.4655 0.3151 -0.0018 -0.0579 0.0040  24  VAL A O     
101  C  CB    . VAL A 15  ? 0.3022 0.4511 0.3484 0.0205  -0.0678 0.0244  24  VAL A CB    
102  C  CG1   . VAL A 15  ? 0.2921 0.4562 0.3649 0.0292  -0.0770 0.0286  24  VAL A CG1   
103  C  CG2   . VAL A 15  ? 0.2425 0.3684 0.2852 0.0263  -0.0606 0.0295  24  VAL A CG2   
104  N  N     . GLY A 16  ? 0.3241 0.4680 0.3069 0.0003  -0.0642 0.0297  25  GLY A N     
105  C  CA    . GLY A 16  ? 0.3330 0.4763 0.2978 -0.0075 -0.0533 0.0197  25  GLY A CA    
106  C  C     . GLY A 16  ? 0.3533 0.4777 0.3218 -0.0028 -0.0431 0.0209  25  GLY A C     
107  O  O     . GLY A 16  ? 0.3805 0.5041 0.3452 -0.0055 -0.0327 0.0081  25  GLY A O     
108  N  N     . LYS A 17  ? 0.3863 0.4960 0.3645 0.0046  -0.0469 0.0350  26  LYS A N     
109  C  CA    . LYS A 17  ? 0.3200 0.4119 0.3013 0.0076  -0.0386 0.0361  26  LYS A CA    
110  C  C     . LYS A 17  ? 0.3894 0.4860 0.3507 -0.0029 -0.0335 0.0386  26  LYS A C     
111  O  O     . LYS A 17  ? 0.3531 0.4481 0.3153 -0.0040 -0.0229 0.0281  26  LYS A O     
112  C  CB    . LYS A 17  ? 0.3759 0.4514 0.3704 0.0164  -0.0451 0.0491  26  LYS A CB    
113  C  CG    . LYS A 17  ? 0.3844 0.4606 0.4023 0.0271  -0.0471 0.0435  26  LYS A CG    
114  C  CD    . LYS A 17  ? 0.3525 0.4134 0.3868 0.0375  -0.0520 0.0512  26  LYS A CD    
115  C  CE    . LYS A 17  ? 0.4021 0.4595 0.4332 0.0380  -0.0674 0.0695  26  LYS A CE    
116  N  NZ    . LYS A 17  ? 0.3294 0.4077 0.3653 0.0389  -0.0789 0.0727  26  LYS A NZ    
117  N  N     . SER A 18  ? 0.3634 0.4681 0.3068 -0.0118 -0.0415 0.0531  27  SER A N     
118  C  CA    . SER A 18  ? 0.4487 0.5629 0.3709 -0.0255 -0.0356 0.0566  27  SER A CA    
119  C  C     . SER A 18  ? 0.4739 0.6122 0.3872 -0.0322 -0.0249 0.0352  27  SER A C     
120  O  O     . SER A 18  ? 0.4300 0.5759 0.3408 -0.0370 -0.0133 0.0259  27  SER A O     
121  C  CB    . SER A 18  ? 0.3967 0.5146 0.2986 -0.0365 -0.0484 0.0800  27  SER A CB    
122  O  OG    . SER A 18  ? 0.3999 0.4915 0.3142 -0.0287 -0.0596 0.0986  27  SER A OG    
123  N  N     . ALA A 19  ? 0.3969 0.5486 0.3082 -0.0323 -0.0290 0.0252  28  ALA A N     
124  C  CA    . ALA A 19  ? 0.3708 0.5436 0.2755 -0.0380 -0.0198 0.0015  28  ALA A CA    
125  C  C     . ALA A 19  ? 0.3170 0.4793 0.2432 -0.0282 -0.0091 -0.0175 28  ALA A C     
126  O  O     . ALA A 19  ? 0.3893 0.5658 0.3144 -0.0314 0.0014  -0.0348 28  ALA A O     
127  C  CB    . ALA A 19  ? 0.3201 0.5047 0.2213 -0.0399 -0.0280 -0.0063 28  ALA A CB    
128  N  N     . LEU A 20  ? 0.3544 0.4939 0.3011 -0.0165 -0.0120 -0.0145 29  LEU A N     
129  C  CA    . LEU A 20  ? 0.3106 0.4379 0.2761 -0.0083 -0.0048 -0.0273 29  LEU A CA    
130  C  C     . LEU A 20  ? 0.3978 0.5238 0.3640 -0.0089 0.0025  -0.0236 29  LEU A C     
131  O  O     . LEU A 20  ? 0.3575 0.4881 0.3337 -0.0064 0.0097  -0.0384 29  LEU A O     
132  C  CB    . LEU A 20  ? 0.2805 0.3872 0.2626 0.0005  -0.0097 -0.0221 29  LEU A CB    
133  C  CG    . LEU A 20  ? 0.3561 0.4638 0.3445 0.0007  -0.0153 -0.0296 29  LEU A CG    
134  C  CD1   . LEU A 20  ? 0.2364 0.3309 0.2385 0.0063  -0.0191 -0.0204 29  LEU A CD1   
135  C  CD2   . LEU A 20  ? 0.2827 0.3882 0.2791 0.0011  -0.0116 -0.0499 29  LEU A CD2   
136  N  N     . THR A 21  ? 0.3836 0.5028 0.3420 -0.0121 -0.0006 -0.0042 30  THR A N     
137  C  CA    . THR A 21  ? 0.3314 0.4489 0.2906 -0.0153 0.0055  0.0003  30  THR A CA    
138  C  C     . THR A 21  ? 0.3467 0.4922 0.2938 -0.0268 0.0142  -0.0081 30  THR A C     
139  O  O     . THR A 21  ? 0.3514 0.5059 0.3088 -0.0264 0.0227  -0.0190 30  THR A O     
140  C  CB    . THR A 21  ? 0.3395 0.4401 0.2933 -0.0174 -0.0014 0.0225  30  THR A CB    
141  O  OG1   . THR A 21  ? 0.3451 0.4242 0.3139 -0.0058 -0.0065 0.0251  30  THR A OG1   
142  C  CG2   . THR A 21  ? 0.4156 0.5150 0.3681 -0.0245 0.0042  0.0278  30  THR A CG2   
143  N  N     . ILE A 22  ? 0.3769 0.5400 0.3024 -0.0379 0.0119  -0.0038 31  ILE A N     
144  C  CA    . ILE A 22  ? 0.3288 0.5248 0.2388 -0.0521 0.0216  -0.0127 31  ILE A CA    
145  C  C     . ILE A 22  ? 0.4185 0.6325 0.3426 -0.0459 0.0313  -0.0440 31  ILE A C     
146  O  O     . ILE A 22  ? 0.4093 0.6471 0.3384 -0.0500 0.0430  -0.0586 31  ILE A O     
147  C  CB    . ILE A 22  ? 0.4400 0.6507 0.3199 -0.0671 0.0148  0.0008  31  ILE A CB    
148  C  CG1   . ILE A 22  ? 0.4384 0.6297 0.3073 -0.0738 0.0043  0.0330  31  ILE A CG1   
149  C  CG2   . ILE A 22  ? 0.4007 0.6524 0.2614 -0.0834 0.0266  -0.0138 31  ILE A CG2   
150  C  CD1   . ILE A 22  ? 0.5348 0.7341 0.3763 -0.0867 -0.0079 0.0524  31  ILE A CD1   
151  N  N     . GLN A 23  ? 0.4143 0.6178 0.3478 -0.0361 0.0260  -0.0557 32  GLN A N     
152  C  CA    . GLN A 23  ? 0.4004 0.6121 0.3522 -0.0281 0.0323  -0.0854 32  GLN A CA    
153  C  C     . GLN A 23  ? 0.5200 0.7213 0.4990 -0.0167 0.0365  -0.0916 32  GLN A C     
154  O  O     . GLN A 23  ? 0.4272 0.6467 0.4215 -0.0131 0.0448  -0.1143 32  GLN A O     
155  C  CB    . GLN A 23  ? 0.4412 0.6360 0.3993 -0.0212 0.0234  -0.0922 32  GLN A CB    
156  C  CG    . GLN A 23  ? 0.4497 0.6441 0.4290 -0.0125 0.0266  -0.1219 32  GLN A CG    
157  C  CD    . GLN A 23  ? 0.5277 0.7567 0.4977 -0.0203 0.0361  -0.1480 32  GLN A CD    
158  O  OE1   . GLN A 23  ? 0.5906 0.8365 0.5752 -0.0166 0.0462  -0.1675 32  GLN A OE1   
159  N  NE2   . GLN A 23  ? 0.4927 0.7356 0.4394 -0.0314 0.0329  -0.1502 32  GLN A NE2   
160  N  N     . PHE A 24  ? 0.3112 0.4856 0.2975 -0.0109 0.0302  -0.0726 33  PHE A N     
161  C  CA    . PHE A 24  ? 0.3419 0.5057 0.3519 -0.0010 0.0314  -0.0760 33  PHE A CA    
162  C  C     . PHE A 24  ? 0.3770 0.5637 0.3889 -0.0076 0.0405  -0.0770 33  PHE A C     
163  O  O     . PHE A 24  ? 0.3504 0.5448 0.3855 -0.0002 0.0439  -0.0905 33  PHE A O     
164  C  CB    . PHE A 24  ? 0.3432 0.4757 0.3561 0.0043  0.0228  -0.0568 33  PHE A CB    
165  C  CG    . PHE A 24  ? 0.3058 0.4272 0.3386 0.0121  0.0218  -0.0574 33  PHE A CG    
166  C  CD1   . PHE A 24  ? 0.2433 0.3601 0.2975 0.0221  0.0193  -0.0723 33  PHE A CD1   
167  C  CD2   . PHE A 24  ? 0.3192 0.4330 0.3494 0.0091  0.0214  -0.0425 33  PHE A CD2   
168  C  CE1   . PHE A 24  ? 0.3136 0.4208 0.3852 0.0287  0.0155  -0.0701 33  PHE A CE1   
169  C  CE2   . PHE A 24  ? 0.3043 0.4104 0.3507 0.0148  0.0191  -0.0428 33  PHE A CE2   
170  C  CZ    . PHE A 24  ? 0.2919 0.3957 0.3584 0.0245  0.0157  -0.0555 33  PHE A CZ    
171  N  N     . PHE A 25  ? 0.4096 0.6081 0.3988 -0.0223 0.0433  -0.0620 34  PHE A N     
172  C  CA    . PHE A 25  ? 0.3504 0.5702 0.3396 -0.0326 0.0517  -0.0593 34  PHE A CA    
173  C  C     . PHE A 25  ? 0.4340 0.6975 0.4146 -0.0448 0.0642  -0.0757 34  PHE A C     
174  O  O     . PHE A 25  ? 0.3653 0.6555 0.3588 -0.0489 0.0740  -0.0855 34  PHE A O     
175  C  CB    . PHE A 25  ? 0.2802 0.4834 0.2506 -0.0440 0.0464  -0.0308 34  PHE A CB    
176  C  CG    . PHE A 25  ? 0.3677 0.5390 0.3516 -0.0349 0.0392  -0.0199 34  PHE A CG    
177  C  CD1   . PHE A 25  ? 0.3252 0.4663 0.3096 -0.0248 0.0295  -0.0121 34  PHE A CD1   
178  C  CD2   . PHE A 25  ? 0.3718 0.5472 0.3682 -0.0378 0.0426  -0.0192 34  PHE A CD2   
179  C  CE1   . PHE A 25  ? 0.3037 0.4198 0.2984 -0.0179 0.0245  -0.0049 34  PHE A CE1   
180  C  CE2   . PHE A 25  ? 0.3070 0.4552 0.3132 -0.0310 0.0359  -0.0111 34  PHE A CE2   
181  C  CZ    . PHE A 25  ? 0.3169 0.4357 0.3211 -0.0212 0.0274  -0.0046 34  PHE A CZ    
182  N  N     . GLN A 26  ? 0.4124 0.6880 0.3718 -0.0518 0.0646  -0.0801 35  GLN A N     
183  C  CA    . GLN A 26  ? 0.5832 0.9044 0.5282 -0.0670 0.0775  -0.0956 35  GLN A CA    
184  C  C     . GLN A 26  ? 0.5459 0.8839 0.4981 -0.0594 0.0819  -0.1277 35  GLN A C     
185  O  O     . GLN A 26  ? 0.6468 1.0273 0.5894 -0.0708 0.0946  -0.1474 35  GLN A O     
186  C  CB    . GLN A 26  ? 0.5255 0.8538 0.4307 -0.0893 0.0744  -0.0703 35  GLN A CB    
187  C  CG    . GLN A 26  ? 0.5691 0.8723 0.4677 -0.0964 0.0669  -0.0375 35  GLN A CG    
188  C  CD    . GLN A 26  ? 0.7111 1.0196 0.5723 -0.1192 0.0617  -0.0107 35  GLN A CD    
189  O  OE1   . GLN A 26  ? 0.8322 1.1768 0.6694 -0.1359 0.0686  -0.0171 35  GLN A OE1   
190  N  NE2   . GLN A 26  ? 0.6834 0.9557 0.5393 -0.1204 0.0485  0.0193  35  GLN A NE2   
191  N  N     . LYS A 27  ? 0.6073 0.9142 0.5758 -0.0421 0.0722  -0.1345 36  LYS A N     
192  C  CA    . LYS A 27  ? 0.6677 0.9825 0.6459 -0.0344 0.0739  -0.1654 36  LYS A CA    
193  C  C     . LYS A 27  ? 0.7283 1.0706 0.6722 -0.0518 0.0772  -0.1708 36  LYS A C     
194  O  O     . LYS A 27  ? 0.6984 1.0678 0.6462 -0.0541 0.0852  -0.1994 36  LYS A O     
195  C  CB    . LYS A 27  ? 0.7173 1.0549 0.7293 -0.0234 0.0847  -0.1985 36  LYS A CB    
196  C  CG    . LYS A 27  ? 0.6253 0.9400 0.6717 -0.0070 0.0796  -0.1930 36  LYS A CG    
197  C  CD    . LYS A 27  ? 0.6843 0.9489 0.7369 0.0047  0.0633  -0.1763 36  LYS A CD    
198  C  CE    . LYS A 27  ? 0.7881 1.0369 0.8531 0.0148  0.0573  -0.1978 36  LYS A CE    
199  N  NZ    . LYS A 27  ? 0.7475 0.9522 0.8112 0.0200  0.0426  -0.1775 36  LYS A NZ    
200  N  N     . ILE A 28  ? 0.6417 0.9733 0.5555 -0.0638 0.0679  -0.1404 37  ILE A N     
201  C  CA    . ILE A 28  ? 0.6974 1.0524 0.5753 -0.0816 0.0666  -0.1390 37  ILE A CA    
202  C  C     . ILE A 28  ? 0.6893 1.0129 0.5566 -0.0793 0.0485  -0.1151 37  ILE A C     
203  O  O     . ILE A 28  ? 0.6365 0.9248 0.5186 -0.0680 0.0393  -0.0951 37  ILE A O     
204  C  CB    . ILE A 28  ? 0.7353 1.1194 0.5856 -0.1046 0.0724  -0.1209 37  ILE A CB    
205  C  CG1   . ILE A 28  ? 0.6638 1.0242 0.5077 -0.1076 0.0655  -0.0843 37  ILE A CG1   
206  C  CG2   . ILE A 28  ? 0.6596 1.0748 0.5295 -0.1075 0.0871  -0.1444 37  ILE A CG2   
207  C  CD1   . ILE A 28  ? 0.7251 1.1057 0.5428 -0.1319 0.0678  -0.0621 37  ILE A CD1   
208  N  N     . PHE A 29  ? 0.7352 1.0758 0.5772 -0.0908 0.0437  -0.1192 38  PHE A N     
209  C  CA    . PHE A 29  ? 0.7370 1.0571 0.5690 -0.0906 0.0258  -0.0982 38  PHE A CA    
210  C  C     . PHE A 29  ? 0.7731 1.1223 0.5635 -0.1133 0.0207  -0.0835 38  PHE A C     
211  O  O     . PHE A 29  ? 0.7441 1.1149 0.5266 -0.1216 0.0234  -0.1017 38  PHE A O     
212  C  CB    . PHE A 29  ? 0.6897 0.9969 0.5396 -0.0795 0.0209  -0.1209 38  PHE A CB    
213  C  CG    . PHE A 29  ? 0.6751 0.9711 0.5161 -0.0815 0.0035  -0.1032 38  PHE A CG    
214  C  CD1   . PHE A 29  ? 0.5797 0.8441 0.4374 -0.0701 -0.0073 -0.0792 38  PHE A CD1   
215  C  CD2   . PHE A 29  ? 0.7145 1.0351 0.5318 -0.0950 -0.0020 -0.1128 38  PHE A CD2   
216  C  CE1   . PHE A 29  ? 0.5598 0.8190 0.4146 -0.0708 -0.0230 -0.0651 38  PHE A CE1   
217  C  CE2   . PHE A 29  ? 0.6937 1.0077 0.5062 -0.0966 -0.0193 -0.0968 38  PHE A CE2   
218  C  CZ    . PHE A 29  ? 0.5717 0.8557 0.4049 -0.0838 -0.0297 -0.0730 38  PHE A CZ    
219  N  N     . VAL A 30  ? 0.8162 1.1559 0.5914 -0.1209 0.0116  -0.0472 39  VAL A N     
220  C  CA    . VAL A 30  ? 0.9021 1.2567 0.6481 -0.1405 0.0029  -0.0248 39  VAL A CA    
221  C  C     . VAL A 30  ? 0.9546 1.2876 0.6945 -0.1368 -0.0202 0.0042  39  VAL A C     
222  O  O     . VAL A 30  ? 0.9323 1.2402 0.6768 -0.1316 -0.0297 0.0321  39  VAL A O     
223  C  CB    . VAL A 30  ? 0.8728 1.2339 0.6090 -0.1548 0.0094  -0.0057 39  VAL A CB    
224  N  N     . PRO A 31  ? 0.9537 1.2943 0.6892 -0.1379 -0.0303 -0.0022 40  PRO A N     
225  C  CA    . PRO A 31  ? 0.9187 1.2439 0.6548 -0.1332 -0.0533 0.0231  40  PRO A CA    
226  C  C     . PRO A 31  ? 0.9667 1.2905 0.6838 -0.1466 -0.0664 0.0574  40  PRO A C     
227  O  O     . PRO A 31  ? 1.0026 1.3044 0.7226 -0.1443 -0.0730 0.0843  40  PRO A O     
228  C  CB    . PRO A 31  ? 0.8743 1.2139 0.6128 -0.1330 -0.0564 -0.0008 40  PRO A CB    
229  C  CG    . PRO A 31  ? 0.8206 1.1865 0.5471 -0.1455 -0.0384 -0.0276 40  PRO A CG    
230  C  CD    . PRO A 31  ? 0.8966 1.2614 0.6310 -0.1426 -0.0203 -0.0363 40  PRO A CD    
231  N  N     . ILE A 37  ? 0.8959 0.9697 0.7043 -0.1407 -0.0551 0.1991  46  ILE A N     
232  C  CA    . ILE A 37  ? 0.9343 0.9968 0.7646 -0.1352 -0.0430 0.1848  46  ILE A CA    
233  C  C     . ILE A 37  ? 0.9102 0.9319 0.7709 -0.1101 -0.0522 0.1812  46  ILE A C     
234  O  O     . ILE A 37  ? 0.8716 0.8969 0.7503 -0.0895 -0.0481 0.1606  46  ILE A O     
235  C  CB    . ILE A 37  ? 0.8620 0.9625 0.6992 -0.1318 -0.0211 0.1525  46  ILE A CB    
236  N  N     . GLU A 38  ? 0.9739 0.9575 0.8403 -0.1132 -0.0644 0.2005  47  GLU A N     
237  C  CA    . GLU A 38  ? 0.8644 0.8100 0.7597 -0.0906 -0.0733 0.1957  47  GLU A CA    
238  C  C     . GLU A 38  ? 0.7913 0.7309 0.7058 -0.0834 -0.0599 0.1740  47  GLU A C     
239  O  O     . GLU A 38  ? 0.8049 0.7230 0.7427 -0.0637 -0.0626 0.1623  47  GLU A O     
240  C  CB    . GLU A 38  ? 0.9072 0.8106 0.8034 -0.0953 -0.0947 0.2242  47  GLU A CB    
241  C  CG    . GLU A 38  ? 0.9545 0.8612 0.8299 -0.1050 -0.1122 0.2514  47  GLU A CG    
242  C  CD    . GLU A 38  ? 1.0372 0.9065 0.9201 -0.1079 -0.1295 0.2691  47  GLU A CD    
243  O  OE1   . GLU A 38  ? 1.0126 0.8493 0.9123 -0.1053 -0.1303 0.2666  47  GLU A OE1   
244  O  OE2   . GLU A 38  ? 0.9851 0.8577 0.8574 -0.1133 -0.1427 0.2849  47  GLU A OE2   
245  N  N     . ASP A 39  ? 0.6313 0.5926 0.5374 -0.0995 -0.0458 0.1678  48  ASP A N     
246  C  CA    . ASP A 39  ? 0.5183 0.4782 0.4418 -0.0940 -0.0347 0.1481  48  ASP A CA    
247  C  C     . ASP A 39  ? 0.5358 0.5172 0.4716 -0.0754 -0.0245 0.1227  48  ASP A C     
248  O  O     . ASP A 39  ? 0.5561 0.5612 0.4845 -0.0719 -0.0218 0.1178  48  ASP A O     
249  C  CB    . ASP A 39  ? 0.4734 0.4550 0.3872 -0.1175 -0.0241 0.1498  48  ASP A CB    
250  C  CG    . ASP A 39  ? 0.5187 0.4910 0.4505 -0.1159 -0.0184 0.1364  48  ASP A CG    
251  O  OD1   . ASP A 39  ? 0.5075 0.4531 0.4557 -0.0986 -0.0231 0.1271  48  ASP A OD1   
252  O  OD2   . ASP A 39  ? 0.4257 0.4207 0.3550 -0.1333 -0.0091 0.1345  48  ASP A OD2   
253  N  N     . SER A 40  ? 0.3802 0.3522 0.3338 -0.0649 -0.0198 0.1069  49  SER A N     
254  C  CA    . SER A 40  ? 0.4306 0.4238 0.3938 -0.0522 -0.0103 0.0855  49  SER A CA    
255  C  C     . SER A 40  ? 0.3743 0.4023 0.3339 -0.0633 0.0016  0.0770  49  SER A C     
256  O  O     . SER A 40  ? 0.3580 0.3932 0.3122 -0.0803 0.0046  0.0840  49  SER A O     
257  C  CB    . SER A 40  ? 0.3792 0.3543 0.3592 -0.0398 -0.0100 0.0731  49  SER A CB    
258  O  OG    . SER A 40  ? 0.5508 0.5147 0.5337 -0.0502 -0.0095 0.0745  49  SER A OG    
259  N  N     . TYR A 41  ? 0.3558 0.4064 0.3206 -0.0538 0.0081  0.0610  50  TYR A N     
260  C  CA    . TYR A 41  ? 0.3997 0.4865 0.3652 -0.0605 0.0190  0.0490  50  TYR A CA    
261  C  C     . TYR A 41  ? 0.3158 0.4095 0.3017 -0.0533 0.0238  0.0336  50  TYR A C     
262  O  O     . TYR A 41  ? 0.2893 0.3684 0.2861 -0.0389 0.0203  0.0265  50  TYR A O     
263  C  CB    . TYR A 41  ? 0.4201 0.5261 0.3810 -0.0543 0.0216  0.0390  50  TYR A CB    
264  C  CG    . TYR A 41  ? 0.4836 0.5875 0.4237 -0.0608 0.0151  0.0533  50  TYR A CG    
265  C  CD1   . TYR A 41  ? 0.5090 0.5878 0.4497 -0.0502 0.0041  0.0617  50  TYR A CD1   
266  C  CD2   . TYR A 41  ? 0.5990 0.7302 0.5197 -0.0783 0.0197  0.0579  50  TYR A CD2   
267  C  CE1   . TYR A 41  ? 0.4749 0.5535 0.3992 -0.0553 -0.0046 0.0758  50  TYR A CE1   
268  C  CE2   . TYR A 41  ? 0.7203 0.8508 0.6195 -0.0857 0.0115  0.0730  50  TYR A CE2   
269  C  CZ    . TYR A 41  ? 0.5757 0.6789 0.4779 -0.0734 -0.0018 0.0826  50  TYR A CZ    
270  O  OH    . TYR A 41  ? 0.6893 0.7934 0.5724 -0.0801 -0.0126 0.0988  50  TYR A OH    
271  N  N     . LEU A 42  ? 0.3527 0.4719 0.3439 -0.0646 0.0313  0.0289  51  LEU A N     
272  C  CA    . LEU A 42  ? 0.3594 0.4893 0.3721 -0.0594 0.0337  0.0161  51  LEU A CA    
273  C  C     . LEU A 42  ? 0.2640 0.4317 0.2912 -0.0547 0.0422  -0.0028 51  LEU A C     
274  O  O     . LEU A 42  ? 0.2973 0.4940 0.3171 -0.0654 0.0506  -0.0060 51  LEU A O     
275  C  CB    . LEU A 42  ? 0.2653 0.3966 0.2798 -0.0755 0.0344  0.0238  51  LEU A CB    
276  C  CG    . LEU A 42  ? 0.2785 0.3703 0.2852 -0.0797 0.0254  0.0381  51  LEU A CG    
277  C  CD1   . LEU A 42  ? 0.3001 0.3959 0.3039 -0.1018 0.0267  0.0479  51  LEU A CD1   
278  C  CD2   . LEU A 42  ? 0.2916 0.3656 0.3105 -0.0658 0.0200  0.0296  51  LEU A CD2   
279  N  N     . LYS A 43  ? 0.2502 0.4182 0.2984 -0.0394 0.0393  -0.0157 52  LYS A N     
280  C  CA    . LYS A 43  ? 0.2703 0.4710 0.3401 -0.0319 0.0450  -0.0357 52  LYS A CA    
281  C  C     . LYS A 43  ? 0.2678 0.4650 0.3631 -0.0195 0.0377  -0.0425 52  LYS A C     
282  O  O     . LYS A 43  ? 0.2915 0.4587 0.3828 -0.0144 0.0284  -0.0335 52  LYS A O     
283  C  CB    . LYS A 43  ? 0.3036 0.5049 0.3701 -0.0219 0.0462  -0.0462 52  LYS A CB    
284  C  CG    . LYS A 43  ? 0.2856 0.4534 0.3545 -0.0069 0.0357  -0.0442 52  LYS A CG    
285  C  CD    . LYS A 43  ? 0.2744 0.4479 0.3556 0.0055  0.0355  -0.0616 52  LYS A CD    
286  C  CE    . LYS A 43  ? 0.3341 0.5187 0.3966 -0.0009 0.0416  -0.0656 52  LYS A CE    
287  N  NZ    . LYS A 43  ? 0.3315 0.5199 0.4065 0.0103  0.0412  -0.0855 52  LYS A NZ    
288  N  N     . HIS A 44  ? 0.2413 0.4718 0.3634 -0.0148 0.0415  -0.0590 53  HIS A N     
289  C  CA    . HIS A 44  ? 0.2261 0.4543 0.3760 0.0009  0.0317  -0.0669 53  HIS A CA    
290  C  C     . HIS A 44  ? 0.2685 0.4851 0.4262 0.0173  0.0276  -0.0776 53  HIS A C     
291  O  O     . HIS A 44  ? 0.3194 0.5479 0.4720 0.0174  0.0359  -0.0885 53  HIS A O     
292  C  CB    . HIS A 44  ? 0.1987 0.4689 0.3811 0.0012  0.0352  -0.0810 53  HIS A CB    
293  C  CG    . HIS A 44  ? 0.2099 0.5004 0.3867 -0.0188 0.0419  -0.0735 53  HIS A CG    
294  N  ND1   . HIS A 44  ? 0.2157 0.5401 0.3863 -0.0344 0.0568  -0.0783 53  HIS A ND1   
295  C  CD2   . HIS A 44  ? 0.2224 0.5052 0.3987 -0.0278 0.0355  -0.0619 53  HIS A CD2   
296  C  CE1   . HIS A 44  ? 0.2268 0.5612 0.3940 -0.0528 0.0588  -0.0681 53  HIS A CE1   
297  N  NE2   . HIS A 44  ? 0.2092 0.5180 0.3806 -0.0485 0.0459  -0.0592 53  HIS A NE2   
298  N  N     . THR A 45  ? 0.2323 0.4254 0.4012 0.0295  0.0141  -0.0742 54  THR A N     
299  C  CA    . THR A 45  ? 0.2803 0.4598 0.4612 0.0443  0.0078  -0.0837 54  THR A CA    
300  C  C     . THR A 45  ? 0.2434 0.4081 0.4455 0.0554  -0.0088 -0.0794 54  THR A C     
301  O  O     . THR A 45  ? 0.2405 0.3943 0.4341 0.0499  -0.0160 -0.0644 54  THR A O     
302  C  CB    . THR A 45  ? 0.3713 0.5218 0.5241 0.0416  0.0078  -0.0751 54  THR A CB    
303  O  OG1   . THR A 45  ? 0.4212 0.5616 0.5873 0.0535  0.0028  -0.0869 54  THR A OG1   
304  C  CG2   . THR A 45  ? 0.3552 0.4757 0.4901 0.0377  -0.0006 -0.0552 54  THR A CG2   
305  N  N     . GLU A 46  ? 0.2182 0.3824 0.4482 0.0707  -0.0159 -0.0930 55  GLU A N     
306  C  CA    . GLU A 46  ? 0.2269 0.3740 0.4788 0.0821  -0.0352 -0.0871 55  GLU A CA    
307  C  C     . GLU A 46  ? 0.3274 0.4351 0.5676 0.0856  -0.0449 -0.0792 55  GLU A C     
308  O  O     . GLU A 46  ? 0.3376 0.4402 0.5859 0.0925  -0.0424 -0.0934 55  GLU A O     
309  C  CB    . GLU A 46  ? 0.2531 0.4260 0.5519 0.0981  -0.0397 -0.1076 55  GLU A CB    
310  C  CG    . GLU A 46  ? 0.2303 0.3864 0.5543 0.1099  -0.0633 -0.0981 55  GLU A CG    
311  C  CD    . GLU A 46  ? 0.3440 0.5233 0.7136 0.1257  -0.0684 -0.1173 55  GLU A CD    
312  O  OE1   . GLU A 46  ? 0.3281 0.5252 0.7056 0.1286  -0.0541 -0.1400 55  GLU A OE1   
313  O  OE2   . GLU A 46  ? 0.3939 0.5693 0.7797 0.1306  -0.0853 -0.1070 55  GLU A OE2   
314  N  N     . ILE A 47  ? 0.2994 0.3815 0.5202 0.0791  -0.0555 -0.0575 56  ILE A N     
315  C  CA    . ILE A 47  ? 0.3010 0.3484 0.5072 0.0778  -0.0640 -0.0466 56  ILE A CA    
316  C  C     . ILE A 47  ? 0.3305 0.3592 0.5492 0.0820  -0.0857 -0.0323 56  ILE A C     
317  O  O     . ILE A 47  ? 0.3538 0.3863 0.5630 0.0752  -0.0916 -0.0186 56  ILE A O     
318  C  CB    . ILE A 47  ? 0.2662 0.3029 0.4336 0.0631  -0.0552 -0.0333 56  ILE A CB    
319  C  CG1   . ILE A 47  ? 0.3389 0.3932 0.4944 0.0587  -0.0370 -0.0439 56  ILE A CG1   
320  C  CG2   . ILE A 47  ? 0.3924 0.3995 0.5474 0.0600  -0.0627 -0.0232 56  ILE A CG2   
321  C  CD1   . ILE A 47  ? 0.2451 0.2917 0.3690 0.0469  -0.0296 -0.0320 56  ILE A CD1   
322  N  N     . ASP A 48  ? 0.3157 0.3231 0.5547 0.0920  -0.0988 -0.0351 57  ASP A N     
323  C  CA    . ASP A 48  ? 0.3507 0.3364 0.6042 0.0964  -0.1233 -0.0193 57  ASP A CA    
324  C  C     . ASP A 48  ? 0.3967 0.4066 0.6753 0.1039  -0.1322 -0.0199 57  ASP A C     
325  O  O     . ASP A 48  ? 0.4074 0.4120 0.6774 0.0977  -0.1469 0.0000  57  ASP A O     
326  C  CB    . ASP A 48  ? 0.3445 0.3061 0.5610 0.0794  -0.1299 0.0070  57  ASP A CB    
327  C  CG    . ASP A 48  ? 0.4085 0.3501 0.6042 0.0713  -0.1218 0.0075  57  ASP A CG    
328  O  OD1   . ASP A 48  ? 0.4130 0.3454 0.6277 0.0804  -0.1215 -0.0075 57  ASP A OD1   
329  O  OD2   . ASP A 48  ? 0.4264 0.3638 0.5883 0.0557  -0.1156 0.0210  57  ASP A OD2   
330  N  N     . ASN A 49  ? 0.3052 0.3461 0.6143 0.1158  -0.1225 -0.0441 58  ASN A N     
331  C  CA    . ASN A 49  ? 0.4007 0.4717 0.7404 0.1238  -0.1284 -0.0498 58  ASN A CA    
332  C  C     . ASN A 49  ? 0.3013 0.3916 0.6191 0.1092  -0.1247 -0.0369 58  ASN A C     
333  O  O     . ASN A 49  ? 0.3140 0.4216 0.6513 0.1121  -0.1374 -0.0323 58  ASN A O     
334  C  CB    . ASN A 49  ? 0.3623 0.4116 0.7187 0.1309  -0.1502 -0.0405 58  ASN A CB    
335  C  CG    . ASN A 49  ? 0.4642 0.4893 0.8350 0.1401  -0.1524 -0.0532 58  ASN A CG    
336  O  OD1   . ASN A 49  ? 0.4383 0.4821 0.8354 0.1508  -0.1438 -0.0781 58  ASN A OD1   
337  N  ND2   . ASN A 49  ? 0.5109 0.4957 0.8638 0.1341  -0.1636 -0.0369 58  ASN A ND2   
338  N  N     . GLN A 50  ? 0.3185 0.4052 0.5953 0.0930  -0.1076 -0.0318 59  GLN A N     
339  C  CA    . GLN A 50  ? 0.3511 0.4520 0.6040 0.0777  -0.1013 -0.0229 59  GLN A CA    
340  C  C     . GLN A 50  ? 0.3050 0.4234 0.5435 0.0699  -0.0770 -0.0350 59  GLN A C     
341  O  O     . GLN A 50  ? 0.2717 0.3736 0.4858 0.0651  -0.0666 -0.0344 59  GLN A O     
342  C  CB    . GLN A 50  ? 0.3480 0.4215 0.5628 0.0641  -0.1082 -0.0011 59  GLN A CB    
343  C  CG    . GLN A 50  ? 0.4305 0.4850 0.6517 0.0670  -0.1335 0.0160  59  GLN A CG    
344  C  CD    . GLN A 50  ? 0.6333 0.6626 0.8131 0.0513  -0.1365 0.0353  59  GLN A CD    
345  O  OE1   . GLN A 50  ? 0.5782 0.6119 0.7277 0.0379  -0.1232 0.0364  59  GLN A OE1   
346  N  NE2   . GLN A 50  ? 0.7216 0.7250 0.9013 0.0524  -0.1539 0.0499  59  GLN A NE2   
347  N  N     . TRP A 51  ? 0.2652 0.4179 0.5191 0.0673  -0.0693 -0.0447 60  TRP A N     
348  C  CA    . TRP A 51  ? 0.2000 0.3700 0.4396 0.0572  -0.0481 -0.0531 60  TRP A CA    
349  C  C     . TRP A 51  ? 0.2214 0.3736 0.4218 0.0405  -0.0427 -0.0387 60  TRP A C     
350  O  O     . TRP A 51  ? 0.2482 0.3914 0.4383 0.0341  -0.0523 -0.0271 60  TRP A O     
351  C  CB    . TRP A 51  ? 0.1958 0.4097 0.4634 0.0559  -0.0418 -0.0662 60  TRP A CB    
352  C  CG    . TRP A 51  ? 0.2105 0.4502 0.5160 0.0712  -0.0387 -0.0880 60  TRP A CG    
353  C  CD1   . TRP A 51  ? 0.2062 0.4589 0.5549 0.0885  -0.0529 -0.0971 60  TRP A CD1   
354  C  CD2   . TRP A 51  ? 0.2224 0.4799 0.5276 0.0711  -0.0205 -0.1055 60  TRP A CD2   
355  N  NE1   . TRP A 51  ? 0.3140 0.5915 0.6921 0.1005  -0.0435 -0.1222 60  TRP A NE1   
356  C  CE2   . TRP A 51  ? 0.2438 0.5259 0.5934 0.0888  -0.0228 -0.1281 60  TRP A CE2   
357  C  CE3   . TRP A 51  ? 0.2741 0.5294 0.5458 0.0575  -0.0038 -0.1042 60  TRP A CE3   
358  C  CZ2   . TRP A 51  ? 0.2251 0.5300 0.5817 0.0915  -0.0067 -0.1511 60  TRP A CZ2   
359  C  CZ3   . TRP A 51  ? 0.2568 0.5366 0.5354 0.0594  0.0105  -0.1244 60  TRP A CZ3   
360  C  CH2   . TRP A 51  ? 0.2632 0.5698 0.5842 0.0760  0.0101  -0.1494 60  TRP A CH2   
361  N  N     . ALA A 52  ? 0.2089 0.3569 0.3882 0.0337  -0.0279 -0.0404 61  ALA A N     
362  C  CA    . ALA A 52  ? 0.2450 0.3750 0.3921 0.0206  -0.0229 -0.0291 61  ALA A CA    
363  C  C     . ALA A 52  ? 0.2342 0.3742 0.3701 0.0120  -0.0077 -0.0325 61  ALA A C     
364  O  O     . ALA A 52  ? 0.2458 0.4038 0.3917 0.0157  -0.0001 -0.0431 61  ALA A O     
365  C  CB    . ALA A 52  ? 0.3047 0.4028 0.4309 0.0227  -0.0274 -0.0202 61  ALA A CB    
366  N  N     . ILE A 53  ? 0.2483 0.3759 0.3628 -0.0002 -0.0043 -0.0235 62  ILE A N     
367  C  CA    . ILE A 53  ? 0.2412 0.3691 0.3400 -0.0100 0.0064  -0.0207 62  ILE A CA    
368  C  C     . ILE A 53  ? 0.2381 0.3368 0.3155 -0.0073 0.0061  -0.0136 62  ILE A C     
369  O  O     . ILE A 53  ? 0.2156 0.2931 0.2836 -0.0069 0.0007  -0.0083 62  ILE A O     
370  C  CB    . ILE A 53  ? 0.2029 0.3352 0.2972 -0.0258 0.0086  -0.0153 62  ILE A CB    
371  C  CG1   . ILE A 53  ? 0.2019 0.3719 0.3204 -0.0300 0.0110  -0.0237 62  ILE A CG1   
372  C  CG2   . ILE A 53  ? 0.2153 0.3374 0.2897 -0.0366 0.0157  -0.0070 62  ILE A CG2   
373  C  CD1   . ILE A 53  ? 0.2115 0.3879 0.3291 -0.0473 0.0115  -0.0189 62  ILE A CD1   
374  N  N     . LEU A 54  ? 0.2402 0.3416 0.3108 -0.0060 0.0119  -0.0149 63  LEU A N     
375  C  CA    . LEU A 54  ? 0.2392 0.3184 0.2929 -0.0036 0.0113  -0.0086 63  LEU A CA    
376  C  C     . LEU A 54  ? 0.2513 0.3251 0.2900 -0.0144 0.0149  0.0008  63  LEU A C     
377  O  O     . LEU A 54  ? 0.2786 0.3713 0.3158 -0.0234 0.0205  0.0011  63  LEU A O     
378  C  CB    . LEU A 54  ? 0.2686 0.3529 0.3249 0.0047  0.0124  -0.0156 63  LEU A CB    
379  C  CG    . LEU A 54  ? 0.4233 0.4949 0.4870 0.0150  0.0053  -0.0186 63  LEU A CG    
380  C  CD1   . LEU A 54  ? 0.2129 0.2860 0.2909 0.0179  -0.0015 -0.0196 63  LEU A CD1   
381  C  CD2   . LEU A 54  ? 0.3502 0.4288 0.4210 0.0216  0.0062  -0.0289 63  LEU A CD2   
382  N  N     . ASP A 55  ? 0.2518 0.3006 0.2805 -0.0141 0.0112  0.0084  64  ASP A N     
383  C  CA    . ASP A 55  ? 0.2875 0.3226 0.3046 -0.0220 0.0107  0.0192  64  ASP A CA    
384  C  C     . ASP A 55  ? 0.2765 0.2984 0.2876 -0.0135 0.0077  0.0224  64  ASP A C     
385  O  O     . ASP A 55  ? 0.3168 0.3234 0.3300 -0.0062 0.0048  0.0202  64  ASP A O     
386  C  CB    . ASP A 55  ? 0.3154 0.3322 0.3328 -0.0278 0.0074  0.0219  64  ASP A CB    
387  C  CG    . ASP A 55  ? 0.3902 0.3905 0.3993 -0.0381 0.0050  0.0340  64  ASP A CG    
388  O  OD1   . ASP A 55  ? 0.3533 0.3576 0.3540 -0.0417 0.0052  0.0429  64  ASP A OD1   
389  O  OD2   . ASP A 55  ? 0.3770 0.3589 0.3873 -0.0436 0.0018  0.0350  64  ASP A OD2   
390  N  N     . VAL A 56  ? 0.3318 0.3636 0.3356 -0.0152 0.0086  0.0263  65  VAL A N     
391  C  CA    . VAL A 56  ? 0.2767 0.3042 0.2777 -0.0070 0.0054  0.0269  65  VAL A CA    
392  C  C     . VAL A 56  ? 0.2500 0.2652 0.2421 -0.0105 -0.0005 0.0410  65  VAL A C     
393  O  O     . VAL A 56  ? 0.2831 0.3064 0.2641 -0.0216 -0.0007 0.0501  65  VAL A O     
394  C  CB    . VAL A 56  ? 0.3280 0.3770 0.3286 -0.0053 0.0089  0.0183  65  VAL A CB    
395  C  CG1   . VAL A 56  ? 0.3102 0.3556 0.3083 0.0011  0.0046  0.0191  65  VAL A CG1   
396  C  CG2   . VAL A 56  ? 0.2095 0.2660 0.2233 0.0001  0.0117  0.0056  65  VAL A CG2   
397  N  N     . LEU A 57  ? 0.3139 0.3112 0.3117 -0.0015 -0.0061 0.0428  66  LEU A N     
398  C  CA    . LEU A 57  ? 0.3033 0.2860 0.2989 -0.0009 -0.0150 0.0559  66  LEU A CA    
399  C  C     . LEU A 57  ? 0.2858 0.2798 0.2807 0.0052  -0.0191 0.0569  66  LEU A C     
400  O  O     . LEU A 57  ? 0.2859 0.2834 0.2909 0.0149  -0.0178 0.0472  66  LEU A O     
401  C  CB    . LEU A 57  ? 0.2789 0.2369 0.2869 0.0068  -0.0190 0.0541  66  LEU A CB    
402  C  CG    . LEU A 57  ? 0.3950 0.3346 0.4078 0.0113  -0.0309 0.0666  66  LEU A CG    
403  C  CD1   . LEU A 57  ? 0.3466 0.2762 0.3462 -0.0031 -0.0373 0.0853  66  LEU A CD1   
404  C  CD2   . LEU A 57  ? 0.3630 0.2813 0.3932 0.0219  -0.0331 0.0578  66  LEU A CD2   
405  N  N     . ASP A 58  ? 0.2850 0.2866 0.2667 -0.0028 -0.0243 0.0691  67  ASP A N     
406  C  CA    . ASP A 58  ? 0.3659 0.3792 0.3447 0.0007  -0.0308 0.0720  67  ASP A CA    
407  C  C     . ASP A 58  ? 0.4713 0.4659 0.4588 0.0076  -0.0446 0.0858  67  ASP A C     
408  O  O     . ASP A 58  ? 0.4636 0.4479 0.4413 -0.0004 -0.0540 0.1040  67  ASP A O     
409  C  CB    . ASP A 58  ? 0.4050 0.4405 0.3628 -0.0131 -0.0293 0.0765  67  ASP A CB    
410  C  CG    . ASP A 58  ? 0.3469 0.3959 0.2985 -0.0121 -0.0377 0.0802  67  ASP A CG    
411  O  OD1   . ASP A 58  ? 0.4182 0.4666 0.3849 -0.0003 -0.0408 0.0731  67  ASP A OD1   
412  O  OD2   . ASP A 58  ? 0.3926 0.4556 0.3235 -0.0250 -0.0414 0.0903  67  ASP A OD2   
413  N  N     . THR A 59  ? 0.3664 0.3575 0.3738 0.0220  -0.0466 0.0774  68  THR A N     
414  C  CA    . THR A 59  ? 0.4951 0.4696 0.5192 0.0326  -0.0594 0.0857  68  THR A CA    
415  C  C     . THR A 59  ? 0.4745 0.4607 0.4957 0.0330  -0.0732 0.0989  68  THR A C     
416  O  O     . THR A 59  ? 0.5222 0.5318 0.5296 0.0261  -0.0710 0.0970  68  THR A O     
417  C  CB    . THR A 59  ? 0.5291 0.5029 0.5777 0.0473  -0.0546 0.0687  68  THR A CB    
418  O  OG1   . THR A 59  ? 0.4023 0.4014 0.4545 0.0500  -0.0507 0.0593  68  THR A OG1   
419  C  CG2   . THR A 59  ? 0.3876 0.3525 0.4355 0.0451  -0.0422 0.0561  68  THR A CG2   
420  N  N     . ALA A 60  ? 0.5080 0.4771 0.5438 0.0415  -0.0889 0.1115  69  ALA A N     
421  C  CA    . ALA A 60  ? 0.6498 0.6291 0.6874 0.0440  -0.1060 0.1258  69  ALA A CA    
422  C  C     . ALA A 60  ? 0.6883 0.6830 0.7561 0.0612  -0.1078 0.1120  69  ALA A C     
423  O  O     . ALA A 60  ? 0.7938 0.7787 0.8880 0.0751  -0.1041 0.0992  69  ALA A O     
424  C  CB    . ALA A 60  ? 0.6152 0.5666 0.6547 0.0438  -0.1259 0.1504  69  ALA A CB    
425  N  N     . GLY A 61  ? 0.6162 0.6380 0.6801 0.0589  -0.1131 0.1132  70  GLY A N     
426  C  CA    . GLY A 61  ? 0.5899 0.6329 0.6819 0.0718  -0.1148 0.1008  70  GLY A CA    
427  C  C     . GLY A 61  ? 0.6238 0.6622 0.7481 0.0887  -0.1338 0.1091  70  GLY A C     
428  O  O     . GLY A 61  ? 0.5882 0.6498 0.7401 0.0996  -0.1356 0.0982  70  GLY A O     
429  N  N     . GLN A 62  ? 0.7741 0.7835 0.8985 0.0910  -0.1488 0.1281  71  GLN A N     
430  C  CA    . GLN A 62  ? 0.8066 0.8059 0.9668 0.1098  -0.1695 0.1361  71  GLN A CA    
431  C  C     . GLN A 62  ? 0.7524 0.7428 0.9498 0.1285  -0.1593 0.1126  71  GLN A C     
432  O  O     . GLN A 62  ? 0.8570 0.8475 1.0475 0.1245  -0.1375 0.0935  71  GLN A O     
433  C  CB    . GLN A 62  ? 0.8317 0.7983 0.9747 0.1027  -0.1859 0.1622  71  GLN A CB    
434  N  N     . GLU A 63  ? 0.7123 0.6979 0.9406 0.1452  -0.1692 0.1094  72  GLU A N     
435  C  CA    . GLU A 63  ? 0.7009 0.6818 0.9619 0.1615  -0.1575 0.0838  72  GLU A CA    
436  C  C     . GLU A 63  ? 0.7564 0.6980 1.0070 0.1577  -0.1506 0.0812  72  GLU A C     
437  O  O     . GLU A 63  ? 0.7499 0.6913 1.0158 0.1646  -0.1351 0.0567  72  GLU A O     
438  C  CB    . GLU A 63  ? 0.6046 0.5876 0.8979 0.1785  -0.1693 0.0815  72  GLU A CB    
439  N  N     . GLU A 64  ? 0.8410 0.7517 1.0641 0.1445  -0.1613 0.1055  73  GLU A N     
440  C  CA    . GLU A 64  ? 0.9187 0.7920 1.1298 0.1371  -0.1566 0.1060  73  GLU A CA    
441  C  C     . GLU A 64  ? 0.9284 0.7812 1.1700 0.1526  -0.1549 0.0868  73  GLU A C     
442  O  O     . GLU A 64  ? 0.8754 0.7372 1.1460 0.1685  -0.1618 0.0797  73  GLU A O     
443  C  CB    . GLU A 64  ? 0.9243 0.8052 1.1182 0.1271  -0.1384 0.0954  73  GLU A CB    
444  C  CG    . GLU A 64  ? 0.9048 0.8011 1.0562 0.1047  -0.1342 0.1118  73  GLU A CG    
445  C  CD    . GLU A 64  ? 0.9379 0.8411 1.0656 0.0911  -0.1111 0.0977  73  GLU A CD    
446  O  OE1   . GLU A 64  ? 0.9535 0.8603 1.0955 0.0987  -0.0972 0.0742  73  GLU A OE1   
447  O  OE2   . GLU A 64  ? 0.9213 0.8284 1.0167 0.0727  -0.1074 0.1097  73  GLU A OE2   
448  N  N     . PHE A 65  ? 0.9646 0.7911 1.2003 0.1476  -0.1459 0.0773  74  PHE A N     
449  C  CA    . PHE A 65  ? 0.9372 0.7430 1.1979 0.1595  -0.1432 0.0566  74  PHE A CA    
450  C  C     . PHE A 65  ? 0.8876 0.7083 1.1541 0.1623  -0.1212 0.0255  74  PHE A C     
451  O  O     . PHE A 65  ? 0.8587 0.6827 1.1028 0.1498  -0.1109 0.0258  74  PHE A O     
452  C  CB    . PHE A 65  ? 0.9415 0.7012 1.1899 0.1488  -0.1535 0.0720  74  PHE A CB    
453  C  CG    . PHE A 65  ? 0.9626 0.7044 1.2138 0.1493  -0.1760 0.0976  74  PHE A CG    
454  C  CD1   . PHE A 65  ? 0.9196 0.6715 1.1460 0.1366  -0.1867 0.1267  74  PHE A CD1   
455  C  CD2   . PHE A 65  ? 0.9196 0.6352 1.1978 0.1616  -0.1870 0.0921  74  PHE A CD2   
456  C  CE1   . PHE A 65  ? 0.8613 0.5981 1.0881 0.1353  -0.2079 0.1507  74  PHE A CE1   
457  C  CE2   . PHE A 65  ? 0.9459 0.6436 1.2277 0.1620  -0.2094 0.1168  74  PHE A CE2   
458  C  CZ    . PHE A 65  ? 0.9135 0.6221 1.1687 0.1483  -0.2199 0.1468  74  PHE A CZ    
459  N  N     . SER A 66  ? 0.9080 0.7395 1.2044 0.1779  -0.1143 -0.0016 75  SER A N     
460  C  CA    . SER A 66  ? 0.8552 0.7072 1.1556 0.1791  -0.0926 -0.0329 75  SER A CA    
461  C  C     . SER A 66  ? 0.8140 0.6370 1.0941 0.1666  -0.0858 -0.0380 75  SER A C     
462  O  O     . SER A 66  ? 0.7333 0.5715 0.9991 0.1587  -0.0703 -0.0504 75  SER A O     
463  C  CB    . SER A 66  ? 0.8639 0.7312 1.1984 0.1959  -0.0876 -0.0602 75  SER A CB    
464  O  OG    . SER A 66  ? 0.9261 0.8177 1.2606 0.1942  -0.0658 -0.0903 75  SER A OG    
465  N  N     . ALA A 67  ? 0.7637 0.5451 1.0424 0.1636  -0.0979 -0.0280 76  ALA A N     
466  C  CA    . ALA A 67  ? 0.7858 0.5393 1.0468 0.1501  -0.0926 -0.0329 76  ALA A CA    
467  C  C     . ALA A 67  ? 0.7305 0.4823 0.9598 0.1316  -0.0912 -0.0123 76  ALA A C     
468  O  O     . ALA A 67  ? 0.6927 0.4487 0.9086 0.1225  -0.0782 -0.0251 76  ALA A O     
469  C  CB    . ALA A 67  ? 0.7589 0.4687 1.0267 0.1494  -0.1074 -0.0244 76  ALA A CB    
470  N  N     . MET A 68  ? 0.8466 0.5940 1.0632 0.1250  -0.1047 0.0193  77  MET A N     
471  C  CA    . MET A 68  ? 0.8027 0.5553 0.9867 0.1054  -0.1020 0.0392  77  MET A CA    
472  C  C     . MET A 68  ? 0.7461 0.5458 0.9166 0.1030  -0.0830 0.0265  77  MET A C     
473  O  O     . MET A 68  ? 0.6969 0.5087 0.8407 0.0869  -0.0704 0.0258  77  MET A O     
474  C  CB    . MET A 68  ? 0.9295 0.6739 1.1009 0.0978  -0.1198 0.0742  77  MET A CB    
475  C  CG    . MET A 68  ? 0.8982 0.6048 1.0628 0.0872  -0.1330 0.0920  77  MET A CG    
476  S  SD    . MET A 68  ? 1.2302 0.9165 1.3647 0.0595  -0.1270 0.1022  77  MET A SD    
477  C  CE    . MET A 68  ? 0.9243 0.6562 1.0252 0.0443  -0.1154 0.1146  77  MET A CE    
478  N  N     . ARG A 69  ? 0.7212 0.5478 0.9121 0.1184  -0.0821 0.0169  78  ARG A N     
479  C  CA    . ARG A 69  ? 0.6932 0.5619 0.8724 0.1144  -0.0662 0.0073  78  ARG A CA    
480  C  C     . ARG A 69  ? 0.6736 0.5526 0.8479 0.1107  -0.0477 -0.0179 78  ARG A C     
481  O  O     . ARG A 69  ? 0.5900 0.4846 0.7386 0.0966  -0.0364 -0.0173 78  ARG A O     
482  C  CB    . ARG A 69  ? 0.7093 0.6048 0.9147 0.1302  -0.0705 0.0027  78  ARG A CB    
483  C  CG    . ARG A 69  ? 0.6558 0.5930 0.8516 0.1249  -0.0561 -0.0058 78  ARG A CG    
484  C  CD    . ARG A 69  ? 0.6644 0.6294 0.8933 0.1409  -0.0592 -0.0155 78  ARG A CD    
485  N  NE    . ARG A 69  ? 0.7152 0.6782 0.9776 0.1571  -0.0557 -0.0401 78  ARG A NE    
486  C  CZ    . ARG A 69  ? 0.7231 0.7033 1.0217 0.1743  -0.0609 -0.0503 78  ARG A CZ    
487  N  NH1   . ARG A 69  ? 0.7568 0.7567 1.0646 0.1780  -0.0718 -0.0365 78  ARG A NH1   
488  N  NH2   . ARG A 69  ? 0.7348 0.7149 1.0515 0.1825  -0.0530 -0.0736 78  ARG A NH2   
489  N  N     . GLU A 70  ? 0.6324 0.5036 0.8316 0.1230  -0.0452 -0.0410 79  GLU A N     
490  C  CA    . GLU A 70  ? 0.6555 0.5396 0.8471 0.1176  -0.0279 -0.0657 79  GLU A CA    
491  C  C     . GLU A 70  ? 0.6355 0.4995 0.7988 0.0998  -0.0254 -0.0599 79  GLU A C     
492  O  O     . GLU A 70  ? 0.4953 0.3768 0.6398 0.0889  -0.0126 -0.0699 79  GLU A O     
493  C  CB    . GLU A 70  ? 0.6010 0.4809 0.8253 0.1340  -0.0257 -0.0947 79  GLU A CB    
494  C  CG    . GLU A 70  ? 0.6741 0.5878 0.9287 0.1505  -0.0229 -0.1076 79  GLU A CG    
495  C  CD    . GLU A 70  ? 0.7620 0.6825 1.0386 0.1604  -0.0160 -0.1363 79  GLU A CD    
496  O  OE1   . GLU A 70  ? 0.8016 0.6997 1.0717 0.1560  -0.0130 -0.1497 79  GLU A OE1   
497  O  OE2   . GLU A 70  ? 0.7850 0.7351 1.0839 0.1708  -0.0135 -0.1452 79  GLU A OE2   
498  N  N     . GLN A 71  ? 0.6060 0.4351 0.7663 0.0952  -0.0385 -0.0423 80  GLN A N     
499  C  CA    . GLN A 71  ? 0.7041 0.5166 0.8416 0.0774  -0.0365 -0.0375 80  GLN A CA    
500  C  C     . GLN A 71  ? 0.5618 0.3996 0.6709 0.0624  -0.0289 -0.0247 80  GLN A C     
501  O  O     . GLN A 71  ? 0.5486 0.3966 0.6425 0.0518  -0.0196 -0.0334 80  GLN A O     
502  C  CB    . GLN A 71  ? 0.7174 0.4887 0.8580 0.0731  -0.0526 -0.0190 80  GLN A CB    
503  C  CG    . GLN A 71  ? 0.7529 0.5099 0.8726 0.0526  -0.0506 -0.0139 80  GLN A CG    
504  C  CD    . GLN A 71  ? 0.8000 0.5610 0.9183 0.0498  -0.0394 -0.0416 80  GLN A CD    
505  O  OE1   . GLN A 71  ? 0.8546 0.6031 0.9931 0.0616  -0.0392 -0.0645 80  GLN A OE1   
506  N  NE2   . GLN A 71  ? 0.7422 0.5227 0.8377 0.0342  -0.0306 -0.0409 80  GLN A NE2   
507  N  N     . TYR A 72  ? 0.5386 0.3876 0.6416 0.0617  -0.0337 -0.0049 81  TYR A N     
508  C  CA    . TYR A 72  ? 0.5807 0.4526 0.6608 0.0493  -0.0268 0.0039  81  TYR A CA    
509  C  C     . TYR A 72  ? 0.5290 0.4309 0.6070 0.0520  -0.0154 -0.0100 81  TYR A C     
510  O  O     . TYR A 72  ? 0.5215 0.4383 0.5833 0.0424  -0.0093 -0.0080 81  TYR A O     
511  C  CB    . TYR A 72  ? 0.6060 0.4824 0.6783 0.0459  -0.0347 0.0261  81  TYR A CB    
512  C  CG    . TYR A 72  ? 0.5363 0.4272 0.6202 0.0580  -0.0395 0.0291  81  TYR A CG    
513  C  CD1   . TYR A 72  ? 0.4980 0.4177 0.5829 0.0618  -0.0309 0.0189  81  TYR A CD1   
514  C  CD2   . TYR A 72  ? 0.6570 0.5332 0.7501 0.0635  -0.0545 0.0444  81  TYR A CD2   
515  C  CE1   . TYR A 72  ? 0.5096 0.4452 0.6062 0.0709  -0.0357 0.0212  81  TYR A CE1   
516  C  CE2   . TYR A 72  ? 0.6502 0.5429 0.7552 0.0740  -0.0607 0.0477  81  TYR A CE2   
517  C  CZ    . TYR A 72  ? 0.6065 0.5300 0.7137 0.0774  -0.0506 0.0350  81  TYR A CZ    
518  O  OH    . TYR A 72  ? 0.5851 0.5275 0.7056 0.0862  -0.0571 0.0374  81  TYR A OH    
519  N  N     . MET A 73  ? 0.4435 0.3554 0.5391 0.0644  -0.0128 -0.0237 82  MET A N     
520  C  CA    . MET A 73  ? 0.5011 0.4410 0.5927 0.0631  -0.0014 -0.0365 82  MET A CA    
521  C  C     . MET A 73  ? 0.5223 0.4614 0.6035 0.0551  0.0066  -0.0511 82  MET A C     
522  O  O     . MET A 73  ? 0.4516 0.4083 0.5174 0.0460  0.0132  -0.0523 82  MET A O     
523  C  CB    . MET A 73  ? 0.4501 0.4071 0.5645 0.0763  0.0005  -0.0482 82  MET A CB    
524  C  CG    . MET A 73  ? 0.4136 0.3814 0.5357 0.0818  -0.0069 -0.0345 82  MET A CG    
525  S  SD    . MET A 73  ? 0.4330 0.4286 0.5865 0.0965  -0.0042 -0.0501 82  MET A SD    
526  C  CE    . MET A 73  ? 0.4467 0.4528 0.6024 0.0983  -0.0160 -0.0296 82  MET A CE    
527  N  N     . ARG A 74  ? 0.3983 0.3157 0.4875 0.0574  0.0045  -0.0617 83  ARG A N     
528  C  CA    . ARG A 74  ? 0.4734 0.3906 0.5513 0.0484  0.0111  -0.0772 83  ARG A CA    
529  C  C     . ARG A 74  ? 0.4042 0.3208 0.4599 0.0331  0.0098  -0.0644 83  ARG A C     
530  O  O     . ARG A 74  ? 0.4017 0.3322 0.4429 0.0237  0.0151  -0.0714 83  ARG A O     
531  C  CB    . ARG A 74  ? 0.4588 0.3488 0.5515 0.0537  0.0075  -0.0923 83  ARG A CB    
532  C  CG    . ARG A 74  ? 0.5586 0.4602 0.6691 0.0646  0.0153  -0.1202 83  ARG A CG    
533  C  CD    . ARG A 74  ? 0.6919 0.5659 0.8135 0.0669  0.0130  -0.1403 83  ARG A CD    
534  N  NE    . ARG A 74  ? 0.6511 0.4859 0.7895 0.0739  -0.0019 -0.1273 83  ARG A NE    
535  C  CZ    . ARG A 74  ? 0.8115 0.6320 0.9811 0.0925  -0.0093 -0.1323 83  ARG A CZ    
536  N  NH1   . ARG A 74  ? 0.7573 0.6033 0.9481 0.1072  -0.0018 -0.1528 83  ARG A NH1   
537  N  NH2   . ARG A 74  ? 0.7459 0.5270 0.9269 0.0956  -0.0256 -0.1157 83  ARG A NH2   
538  N  N     . THR A 75  ? 0.4337 0.3372 0.4873 0.0299  0.0023  -0.0457 84  THR A N     
539  C  CA    . THR A 75  ? 0.4366 0.3423 0.4752 0.0164  0.0012  -0.0356 84  THR A CA    
540  C  C     . THR A 75  ? 0.4195 0.3489 0.4489 0.0141  0.0037  -0.0262 84  THR A C     
541  O  O     . THR A 75  ? 0.4696 0.4056 0.4907 0.0051  0.0029  -0.0205 84  THR A O     
542  C  CB    . THR A 75  ? 0.4613 0.3464 0.5017 0.0113  -0.0065 -0.0210 84  THR A CB    
543  O  OG1   . THR A 75  ? 0.5528 0.4426 0.5950 0.0161  -0.0099 -0.0058 84  THR A OG1   
544  C  CG2   . THR A 75  ? 0.6215 0.4760 0.6739 0.0142  -0.0120 -0.0281 84  THR A CG2   
545  N  N     . GLY A 76  ? 0.3325 0.2749 0.3660 0.0219  0.0059  -0.0255 85  GLY A N     
546  C  CA    . GLY A 76  ? 0.2839 0.2435 0.3109 0.0198  0.0066  -0.0170 85  GLY A CA    
547  C  C     . GLY A 76  ? 0.3427 0.3158 0.3603 0.0138  0.0099  -0.0221 85  GLY A C     
548  O  O     . GLY A 76  ? 0.3011 0.2795 0.3165 0.0131  0.0142  -0.0328 85  GLY A O     
549  N  N     . ASP A 77  ? 0.2765 0.2564 0.2890 0.0090  0.0073  -0.0144 86  ASP A N     
550  C  CA    . ASP A 77  ? 0.2860 0.2763 0.2905 0.0036  0.0065  -0.0144 86  ASP A CA    
551  C  C     . ASP A 77  ? 0.3329 0.3318 0.3382 0.0059  0.0070  -0.0105 86  ASP A C     
552  O  O     . ASP A 77  ? 0.3122 0.3179 0.3098 0.0003  0.0065  -0.0099 86  ASP A O     
553  C  CB    . ASP A 77  ? 0.2661 0.2590 0.2704 -0.0010 0.0011  -0.0090 86  ASP A CB    
554  C  CG    . ASP A 77  ? 0.3857 0.3725 0.3889 -0.0068 0.0001  -0.0128 86  ASP A CG    
555  O  OD1   . ASP A 77  ? 0.3171 0.2991 0.3142 -0.0102 0.0020  -0.0216 86  ASP A OD1   
556  O  OD2   . ASP A 77  ? 0.3209 0.3094 0.3299 -0.0091 -0.0020 -0.0086 86  ASP A OD2   
557  N  N     . GLY A 78  ? 0.2917 0.2905 0.3045 0.0121  0.0070  -0.0071 87  GLY A N     
558  C  CA    . GLY A 78  ? 0.2857 0.2920 0.3008 0.0133  0.0069  -0.0047 87  GLY A CA    
559  C  C     . GLY A 78  ? 0.2702 0.2773 0.2932 0.0200  0.0071  -0.0037 87  GLY A C     
560  O  O     . GLY A 78  ? 0.2684 0.2693 0.2930 0.0225  0.0056  -0.0012 87  GLY A O     
561  N  N     . PHE A 79  ? 0.2533 0.2692 0.2804 0.0209  0.0079  -0.0042 88  PHE A N     
562  C  CA    . PHE A 79  ? 0.1945 0.2147 0.2296 0.0268  0.0062  -0.0031 88  PHE A CA    
563  C  C     . PHE A 79  ? 0.2775 0.3052 0.3135 0.0243  0.0038  -0.0012 88  PHE A C     
564  O  O     . PHE A 79  ? 0.2362 0.2673 0.2707 0.0185  0.0046  -0.0018 88  PHE A O     
565  C  CB    . PHE A 79  ? 0.2136 0.2408 0.2594 0.0319  0.0091  -0.0091 88  PHE A CB    
566  C  CG    . PHE A 79  ? 0.3157 0.3326 0.3640 0.0358  0.0107  -0.0143 88  PHE A CG    
567  C  CD1   . PHE A 79  ? 0.2714 0.2878 0.3128 0.0306  0.0158  -0.0215 88  PHE A CD1   
568  C  CD2   . PHE A 79  ? 0.2425 0.2490 0.2995 0.0435  0.0058  -0.0117 88  PHE A CD2   
569  C  CE1   . PHE A 79  ? 0.2754 0.2812 0.3194 0.0334  0.0171  -0.0293 88  PHE A CE1   
570  C  CE2   . PHE A 79  ? 0.2631 0.2552 0.3245 0.0467  0.0059  -0.0173 88  PHE A CE2   
571  C  CZ    . PHE A 79  ? 0.3340 0.3259 0.3894 0.0419  0.0122  -0.0278 88  PHE A CZ    
572  N  N     . LEU A 80  ? 0.2192 0.2490 0.2561 0.0268  0.0002  0.0013  89  LEU A N     
573  C  CA    . LEU A 80  ? 0.2729 0.3115 0.3121 0.0248  -0.0027 0.0004  89  LEU A CA    
574  C  C     . LEU A 80  ? 0.1894 0.2395 0.2379 0.0288  -0.0049 0.0010  89  LEU A C     
575  O  O     . LEU A 80  ? 0.3041 0.3530 0.3538 0.0339  -0.0086 0.0053  89  LEU A O     
576  C  CB    . LEU A 80  ? 0.1949 0.2333 0.2281 0.0237  -0.0052 0.0001  89  LEU A CB    
577  C  CG    . LEU A 80  ? 0.2547 0.2867 0.2852 0.0219  -0.0040 -0.0033 89  LEU A CG    
578  C  CD1   . LEU A 80  ? 0.2224 0.2619 0.2495 0.0211  -0.0045 -0.0080 89  LEU A CD1   
579  C  CD2   . LEU A 80  ? 0.2037 0.2296 0.2383 0.0189  -0.0057 -0.0054 89  LEU A CD2   
580  N  N     . ILE A 81  ? 0.2960 0.3578 0.3523 0.0258  -0.0038 -0.0023 90  ILE A N     
581  C  CA    . ILE A 81  ? 0.2420 0.3207 0.3120 0.0295  -0.0068 -0.0031 90  ILE A CA    
582  C  C     . ILE A 81  ? 0.2602 0.3464 0.3281 0.0248  -0.0129 -0.0026 90  ILE A C     
583  O  O     . ILE A 81  ? 0.3121 0.4011 0.3798 0.0164  -0.0121 -0.0058 90  ILE A O     
584  C  CB    . ILE A 81  ? 0.2289 0.3231 0.3108 0.0270  -0.0008 -0.0089 90  ILE A CB    
585  C  CG1   . ILE A 81  ? 0.2183 0.3083 0.3016 0.0312  0.0060  -0.0133 90  ILE A CG1   
586  C  CG2   . ILE A 81  ? 0.2103 0.3273 0.3117 0.0317  -0.0046 -0.0112 90  ILE A CG2   
587  C  CD1   . ILE A 81  ? 0.2978 0.4107 0.3936 0.0283  0.0137  -0.0220 90  ILE A CD1   
588  N  N     . VAL A 82  ? 0.2803 0.3692 0.3457 0.0286  -0.0198 0.0018  91  VAL A N     
589  C  CA    . VAL A 82  ? 0.2519 0.3491 0.3108 0.0230  -0.0257 0.0007  91  VAL A CA    
590  C  C     . VAL A 82  ? 0.3036 0.4217 0.3762 0.0244  -0.0332 0.0018  91  VAL A C     
591  O  O     . VAL A 82  ? 0.2800 0.4034 0.3634 0.0332  -0.0380 0.0076  91  VAL A O     
592  C  CB    . VAL A 82  ? 0.3027 0.3941 0.3452 0.0227  -0.0286 0.0051  91  VAL A CB    
593  C  CG1   . VAL A 82  ? 0.2278 0.3304 0.2608 0.0152  -0.0330 -0.0002 91  VAL A CG1   
594  C  CG2   . VAL A 82  ? 0.2036 0.2788 0.2378 0.0225  -0.0212 0.0036  91  VAL A CG2   
595  N  N     . TYR A 83  ? 0.2404 0.3700 0.3152 0.0159  -0.0354 -0.0040 92  TYR A N     
596  C  CA    . TYR A 83  ? 0.2750 0.4279 0.3605 0.0150  -0.0449 -0.0032 92  TYR A CA    
597  C  C     . TYR A 83  ? 0.3205 0.4767 0.3915 0.0051  -0.0502 -0.0083 92  TYR A C     
598  O  O     . TYR A 83  ? 0.3671 0.5081 0.4246 -0.0001 -0.0454 -0.0149 92  TYR A O     
599  C  CB    . TYR A 83  ? 0.2114 0.3831 0.3192 0.0124  -0.0423 -0.0077 92  TYR A CB    
600  C  CG    . TYR A 83  ? 0.2412 0.4101 0.3466 -0.0017 -0.0377 -0.0147 92  TYR A CG    
601  C  CD1   . TYR A 83  ? 0.2879 0.4400 0.3886 -0.0056 -0.0283 -0.0154 92  TYR A CD1   
602  C  CD2   . TYR A 83  ? 0.2619 0.4437 0.3697 -0.0125 -0.0444 -0.0196 92  TYR A CD2   
603  C  CE1   . TYR A 83  ? 0.2824 0.4276 0.3811 -0.0196 -0.0267 -0.0185 92  TYR A CE1   
604  C  CE2   . TYR A 83  ? 0.2649 0.4390 0.3717 -0.0266 -0.0419 -0.0250 92  TYR A CE2   
605  C  CZ    . TYR A 83  ? 0.3132 0.4676 0.4157 -0.0299 -0.0335 -0.0232 92  TYR A CZ    
606  O  OH    . TYR A 83  ? 0.2713 0.4140 0.3729 -0.0449 -0.0337 -0.0254 92  TYR A OH    
607  N  N     . SER A 84  ? 0.2476 0.4253 0.3229 0.0030  -0.0611 -0.0065 93  SER A N     
608  C  CA    . SER A 84  ? 0.3515 0.5375 0.4130 -0.0079 -0.0672 -0.0137 93  SER A CA    
609  C  C     . SER A 84  ? 0.3914 0.5919 0.4682 -0.0175 -0.0696 -0.0222 93  SER A C     
610  O  O     . SER A 84  ? 0.3043 0.5256 0.4026 -0.0150 -0.0738 -0.0183 93  SER A O     
611  C  CB    . SER A 84  ? 0.2896 0.4914 0.3406 -0.0069 -0.0800 -0.0043 93  SER A CB    
612  O  OG    . SER A 84  ? 0.3178 0.5347 0.3570 -0.0192 -0.0869 -0.0133 93  SER A OG    
613  N  N     . VAL A 85  ? 0.3091 0.4993 0.3775 -0.0285 -0.0673 -0.0347 94  VAL A N     
614  C  CA    . VAL A 85  ? 0.3025 0.5026 0.3842 -0.0411 -0.0704 -0.0426 94  VAL A CA    
615  C  C     . VAL A 85  ? 0.3380 0.5686 0.4233 -0.0470 -0.0834 -0.0438 94  VAL A C     
616  O  O     . VAL A 85  ? 0.3220 0.5671 0.4218 -0.0583 -0.0873 -0.0492 94  VAL A O     
617  C  CB    . VAL A 85  ? 0.3003 0.4757 0.3736 -0.0509 -0.0671 -0.0562 94  VAL A CB    
618  C  CG1   . VAL A 85  ? 0.2652 0.4129 0.3395 -0.0461 -0.0572 -0.0525 94  VAL A CG1   
619  C  CG2   . VAL A 85  ? 0.2960 0.4688 0.3487 -0.0517 -0.0699 -0.0672 94  VAL A CG2   
620  N  N     . THR A 86  ? 0.3117 0.5535 0.3838 -0.0415 -0.0913 -0.0375 95  THR A N     
621  C  CA    . THR A 86  ? 0.3641 0.6373 0.4391 -0.0460 -0.1066 -0.0347 95  THR A CA    
622  C  C     . THR A 86  ? 0.3646 0.6571 0.4613 -0.0329 -0.1143 -0.0188 95  THR A C     
623  O  O     . THR A 86  ? 0.3802 0.7006 0.4841 -0.0342 -0.1297 -0.0136 95  THR A O     
624  C  CB    . THR A 86  ? 0.3860 0.6624 0.4300 -0.0511 -0.1133 -0.0366 95  THR A CB    
625  O  OG1   . THR A 86  ? 0.4517 0.7191 0.4837 -0.0398 -0.1124 -0.0215 95  THR A OG1   
626  C  CG2   . THR A 86  ? 0.3847 0.6422 0.4109 -0.0608 -0.1043 -0.0567 95  THR A CG2   
627  N  N     . ASP A 87  ? 0.2970 0.5756 0.4056 -0.0199 -0.1050 -0.0120 96  ASP A N     
628  C  CA    . ASP A 87  ? 0.2941 0.5864 0.4265 -0.0044 -0.1114 -0.0001 96  ASP A CA    
629  C  C     . ASP A 87  ? 0.3529 0.6529 0.5148 -0.0011 -0.1002 -0.0062 96  ASP A C     
630  O  O     . ASP A 87  ? 0.2894 0.5673 0.4474 0.0019  -0.0860 -0.0083 96  ASP A O     
631  C  CB    . ASP A 87  ? 0.3160 0.5846 0.4339 0.0076  -0.1110 0.0122  96  ASP A CB    
632  C  CG    . ASP A 87  ? 0.2817 0.5593 0.4253 0.0246  -0.1213 0.0245  96  ASP A CG    
633  O  OD1   . ASP A 87  ? 0.3881 0.6922 0.5647 0.0298  -0.1258 0.0212  96  ASP A OD1   
634  O  OD2   . ASP A 87  ? 0.4087 0.6668 0.5414 0.0328  -0.1253 0.0371  96  ASP A OD2   
635  N  N     . LYS A 88  ? 0.3030 0.6379 0.4939 -0.0030 -0.1067 -0.0093 97  LYS A N     
636  C  CA    . LYS A 88  ? 0.2830 0.6344 0.5031 -0.0021 -0.0951 -0.0162 97  LYS A CA    
637  C  C     . LYS A 88  ? 0.2565 0.6025 0.4927 0.0179  -0.0896 -0.0128 97  LYS A C     
638  O  O     . LYS A 88  ? 0.3178 0.6562 0.5575 0.0179  -0.0736 -0.0187 97  LYS A O     
639  C  CB    . LYS A 88  ? 0.3457 0.7426 0.5974 -0.0080 -0.1039 -0.0209 97  LYS A CB    
640  C  CG    . LYS A 88  ? 0.3858 0.7899 0.6288 -0.0320 -0.1044 -0.0289 97  LYS A CG    
641  C  CD    . LYS A 88  ? 0.4261 0.8801 0.7042 -0.0382 -0.1134 -0.0332 97  LYS A CD    
642  C  CE    . LYS A 88  ? 0.5242 0.9840 0.7956 -0.0647 -0.1141 -0.0418 97  LYS A CE    
643  N  NZ    . LYS A 88  ? 0.5317 0.9696 0.7952 -0.0790 -0.0962 -0.0463 97  LYS A NZ    
644  N  N     . ALA A 89  ? 0.2489 0.5978 0.4947 0.0342  -0.1040 -0.0031 98  ALA A N     
645  C  CA    . ALA A 89  ? 0.2711 0.6123 0.5364 0.0543  -0.1011 -0.0016 98  ALA A CA    
646  C  C     . ALA A 89  ? 0.2199 0.5207 0.4579 0.0547  -0.0873 -0.0008 98  ALA A C     
647  O  O     . ALA A 89  ? 0.2940 0.5904 0.5450 0.0629  -0.0752 -0.0079 98  ALA A O     
648  C  CB    . ALA A 89  ? 0.2567 0.6003 0.5345 0.0702  -0.1230 0.0121  98  ALA A CB    
649  N  N     . SER A 90  ? 0.2709 0.5454 0.4721 0.0454  -0.0885 0.0059  99  SER A N     
650  C  CA    . SER A 90  ? 0.3225 0.5623 0.5000 0.0451  -0.0762 0.0063  99  SER A CA    
651  C  C     . SER A 90  ? 0.2685 0.5064 0.4450 0.0357  -0.0589 -0.0050 99  SER A C     
652  O  O     . SER A 90  ? 0.2736 0.4924 0.4440 0.0392  -0.0481 -0.0068 99  SER A O     
653  C  CB    . SER A 90  ? 0.2281 0.4478 0.3703 0.0364  -0.0804 0.0132  99  SER A CB    
654  O  OG    . SER A 90  ? 0.3053 0.5270 0.4333 0.0208  -0.0755 0.0044  99  SER A OG    
655  N  N     . PHE A 91  ? 0.2597 0.5169 0.4412 0.0220  -0.0573 -0.0114 100 PHE A N     
656  C  CA    . PHE A 91  ? 0.2952 0.5516 0.4760 0.0102  -0.0431 -0.0187 100 PHE A CA    
657  C  C     . PHE A 91  ? 0.3265 0.6065 0.5342 0.0165  -0.0339 -0.0252 100 PHE A C     
658  O  O     . PHE A 91  ? 0.3678 0.6385 0.5690 0.0133  -0.0208 -0.0286 100 PHE A O     
659  C  CB    . PHE A 91  ? 0.2490 0.5171 0.4282 -0.0084 -0.0459 -0.0225 100 PHE A CB    
660  C  CG    . PHE A 91  ? 0.2152 0.4804 0.3922 -0.0243 -0.0342 -0.0261 100 PHE A CG    
661  C  CD1   . PHE A 91  ? 0.2517 0.4830 0.4060 -0.0285 -0.0275 -0.0237 100 PHE A CD1   
662  C  CD2   . PHE A 91  ? 0.2663 0.5640 0.4640 -0.0367 -0.0314 -0.0305 100 PHE A CD2   
663  C  CE1   . PHE A 91  ? 0.2505 0.4769 0.4009 -0.0447 -0.0198 -0.0233 100 PHE A CE1   
664  C  CE2   . PHE A 91  ? 0.2823 0.5767 0.4748 -0.0551 -0.0218 -0.0306 100 PHE A CE2   
665  C  CZ    . PHE A 91  ? 0.2463 0.5032 0.4140 -0.0591 -0.0169 -0.0258 100 PHE A CZ    
666  N  N     . GLU A 92  ? 0.2988 0.6120 0.5379 0.0257  -0.0408 -0.0282 101 GLU A N     
667  C  CA    . GLU A 92  ? 0.3732 0.7142 0.6430 0.0338  -0.0312 -0.0388 101 GLU A CA    
668  C  C     . GLU A 92  ? 0.3722 0.6903 0.6403 0.0503  -0.0261 -0.0404 101 GLU A C     
669  O  O     . GLU A 92  ? 0.3883 0.7175 0.6664 0.0514  -0.0118 -0.0517 101 GLU A O     
670  C  CB    . GLU A 92  ? 0.3723 0.7547 0.6816 0.0434  -0.0421 -0.0426 101 GLU A CB    
671  C  CG    . GLU A 92  ? 0.5621 0.9727 0.8768 0.0252  -0.0471 -0.0430 101 GLU A CG    
672  C  CD    . GLU A 92  ? 0.6555 1.0865 0.9724 0.0046  -0.0302 -0.0516 101 GLU A CD    
673  O  OE1   . GLU A 92  ? 0.6449 1.0937 0.9776 0.0085  -0.0157 -0.0615 101 GLU A OE1   
674  O  OE2   . GLU A 92  ? 0.6830 1.1117 0.9849 -0.0168 -0.0315 -0.0486 101 GLU A OE2   
675  N  N     . HIS A 93  ? 0.3317 0.6190 0.5858 0.0611  -0.0372 -0.0298 102 HIS A N     
676  C  CA    . HIS A 93  ? 0.2757 0.5379 0.5287 0.0753  -0.0344 -0.0306 102 HIS A CA    
677  C  C     . HIS A 93  ? 0.2680 0.5039 0.4913 0.0654  -0.0205 -0.0319 102 HIS A C     
678  O  O     . HIS A 93  ? 0.3173 0.5323 0.5376 0.0746  -0.0172 -0.0339 102 HIS A O     
679  C  CB    . HIS A 93  ? 0.2922 0.5306 0.5388 0.0863  -0.0520 -0.0159 102 HIS A CB    
680  C  CG    . HIS A 93  ? 0.3897 0.6510 0.6691 0.1000  -0.0689 -0.0127 102 HIS A CG    
681  N  ND1   . HIS A 93  ? 0.3424 0.5885 0.6164 0.1067  -0.0886 0.0042  102 HIS A ND1   
682  C  CD2   . HIS A 93  ? 0.4454 0.7462 0.7649 0.1076  -0.0699 -0.0237 102 HIS A CD2   
683  C  CE1   . HIS A 93  ? 0.4573 0.7298 0.7668 0.1191  -0.1032 0.0050  102 HIS A CE1   
684  N  NE2   . HIS A 93  ? 0.4963 0.8036 0.8362 0.1208  -0.0918 -0.0131 102 HIS A NE2   
685  N  N     . VAL A 94  ? 0.2267 0.4618 0.4295 0.0470  -0.0141 -0.0306 103 VAL A N     
686  C  CA    . VAL A 94  ? 0.2465 0.4594 0.4243 0.0376  -0.0031 -0.0309 103 VAL A CA    
687  C  C     . VAL A 94  ? 0.2751 0.5026 0.4642 0.0394  0.0105  -0.0432 103 VAL A C     
688  O  O     . VAL A 94  ? 0.2307 0.4381 0.4054 0.0408  0.0165  -0.0449 103 VAL A O     
689  C  CB    . VAL A 94  ? 0.2769 0.4865 0.4366 0.0181  -0.0015 -0.0268 103 VAL A CB    
690  C  CG1   . VAL A 94  ? 0.2387 0.4315 0.3782 0.0079  0.0084  -0.0263 103 VAL A CG1   
691  C  CG2   . VAL A 94  ? 0.2019 0.3925 0.3462 0.0170  -0.0127 -0.0188 103 VAL A CG2   
692  N  N     . ASP A 95  ? 0.2573 0.5236 0.4725 0.0382  0.0159  -0.0537 104 ASP A N     
693  C  CA    . ASP A 95  ? 0.2983 0.5857 0.5255 0.0393  0.0307  -0.0693 104 ASP A CA    
694  C  C     . ASP A 95  ? 0.3298 0.6014 0.5684 0.0603  0.0292  -0.0772 104 ASP A C     
695  O  O     . ASP A 95  ? 0.2631 0.5297 0.4935 0.0595  0.0402  -0.0873 104 ASP A O     
696  C  CB    . ASP A 95  ? 0.2749 0.6135 0.5348 0.0366  0.0365  -0.0815 104 ASP A CB    
697  C  CG    . ASP A 95  ? 0.2928 0.6466 0.5437 0.0136  0.0366  -0.0732 104 ASP A CG    
698  O  OD1   . ASP A 95  ? 0.3713 0.6966 0.5896 -0.0017 0.0357  -0.0611 104 ASP A OD1   
699  O  OD2   . ASP A 95  ? 0.4014 0.7955 0.6803 0.0109  0.0366  -0.0795 104 ASP A OD2   
700  N  N     . ARG A 96  ? 0.2473 0.5090 0.5036 0.0778  0.0143  -0.0719 105 ARG A N     
701  C  CA    . ARG A 96  ? 0.2623 0.5043 0.5327 0.0975  0.0099  -0.0776 105 ARG A CA    
702  C  C     . ARG A 96  ? 0.2802 0.4788 0.5170 0.0936  0.0099  -0.0690 105 ARG A C     
703  O  O     . ARG A 96  ? 0.2452 0.4312 0.4835 0.0998  0.0160  -0.0801 105 ARG A O     
704  C  CB    . ARG A 96  ? 0.3539 0.5942 0.6496 0.1147  -0.0095 -0.0691 105 ARG A CB    
705  C  CG    . ARG A 96  ? 0.5136 0.7338 0.8327 0.1367  -0.0174 -0.0747 105 ARG A CG    
706  C  CD    . ARG A 96  ? 0.6835 0.8649 0.9875 0.1411  -0.0368 -0.0516 105 ARG A CD    
707  N  NE    . ARG A 96  ? 0.7035 0.8618 1.0325 0.1614  -0.0486 -0.0530 105 ARG A NE    
708  C  CZ    . ARG A 96  ? 0.6985 0.8180 1.0139 0.1640  -0.0642 -0.0335 105 ARG A CZ    
709  N  NH1   . ARG A 96  ? 0.6618 0.7656 0.9388 0.1481  -0.0681 -0.0133 105 ARG A NH1   
710  N  NH2   . ARG A 96  ? 0.7108 0.8058 1.0467 0.1796  -0.0746 -0.0340 105 ARG A NH2   
711  N  N     . PHE A 97  ? 0.2597 0.4374 0.4680 0.0832  0.0034  -0.0514 106 PHE A N     
712  C  CA    . PHE A 97  ? 0.2934 0.4353 0.4734 0.0791  0.0034  -0.0437 106 PHE A CA    
713  C  C     . PHE A 97  ? 0.2695 0.4119 0.4326 0.0677  0.0178  -0.0526 106 PHE A C     
714  O  O     . PHE A 97  ? 0.2912 0.4135 0.4454 0.0699  0.0206  -0.0564 106 PHE A O     
715  C  CB    . PHE A 97  ? 0.2800 0.4070 0.4366 0.0703  -0.0049 -0.0269 106 PHE A CB    
716  C  CG    . PHE A 97  ? 0.3175 0.4380 0.4810 0.0791  -0.0203 -0.0153 106 PHE A CG    
717  C  CD1   . PHE A 97  ? 0.3266 0.4230 0.4926 0.0891  -0.0282 -0.0094 106 PHE A CD1   
718  C  CD2   . PHE A 97  ? 0.2321 0.3698 0.3979 0.0753  -0.0283 -0.0092 106 PHE A CD2   
719  C  CE1   . PHE A 97  ? 0.3140 0.4038 0.4835 0.0947  -0.0443 0.0049  106 PHE A CE1   
720  C  CE2   . PHE A 97  ? 0.2855 0.4196 0.4542 0.0813  -0.0440 0.0031  106 PHE A CE2   
721  C  CZ    . PHE A 97  ? 0.2907 0.4007 0.4603 0.0908  -0.0523 0.0115  106 PHE A CZ    
722  N  N     . HIS A 98  ? 0.2652 0.4302 0.4226 0.0537  0.0259  -0.0549 107 HIS A N     
723  C  CA    . HIS A 98  ? 0.3165 0.4829 0.4545 0.0402  0.0375  -0.0598 107 HIS A CA    
724  C  C     . HIS A 98  ? 0.2287 0.4100 0.3800 0.0464  0.0481  -0.0795 107 HIS A C     
725  O  O     . HIS A 98  ? 0.2789 0.4464 0.4139 0.0430  0.0529  -0.0842 107 HIS A O     
726  C  CB    . HIS A 98  ? 0.2913 0.4780 0.4211 0.0218  0.0421  -0.0555 107 HIS A CB    
727  C  CG    . HIS A 98  ? 0.3814 0.5616 0.4841 0.0050  0.0486  -0.0521 107 HIS A CG    
728  N  ND1   . HIS A 98  ? 0.2986 0.5066 0.3973 -0.0101 0.0600  -0.0586 107 HIS A ND1   
729  C  CD2   . HIS A 98  ? 0.3595 0.5107 0.4382 0.0002  0.0441  -0.0420 107 HIS A CD2   
730  C  CE1   . HIS A 98  ? 0.3216 0.5154 0.3924 -0.0240 0.0607  -0.0504 107 HIS A CE1   
731  N  NE2   . HIS A 98  ? 0.3130 0.4724 0.3735 -0.0168 0.0506  -0.0409 107 HIS A NE2   
732  N  N     . GLN A 99  ? 0.2317 0.4433 0.4147 0.0559  0.0515  -0.0933 108 GLN A N     
733  C  CA    . GLN A 99  ? 0.2555 0.4850 0.4563 0.0638  0.0627  -0.1172 108 GLN A CA    
734  C  C     . GLN A 99  ? 0.2920 0.4872 0.4977 0.0801  0.0560  -0.1219 108 GLN A C     
735  O  O     . GLN A 99  ? 0.2791 0.4710 0.4789 0.0793  0.0648  -0.1377 108 GLN A O     
736  C  CB    . GLN A 99  ? 0.2350 0.5062 0.4761 0.0737  0.0661  -0.1321 108 GLN A CB    
737  C  CG    . GLN A 99  ? 0.3155 0.6087 0.5824 0.0853  0.0779  -0.1618 108 GLN A CG    
738  C  CD    . GLN A 99  ? 0.2914 0.6143 0.5952 0.0963  0.0760  -0.1710 108 GLN A CD    
739  O  OE1   . GLN A 99  ? 0.4946 0.8385 0.8093 0.0926  0.0711  -0.1608 108 GLN A OE1   
740  N  NE2   . GLN A 99  ? 0.4881 0.8109 0.8099 0.1088  0.0786  -0.1899 108 GLN A NE2   
741  N  N     . LEU A 100 ? 0.2823 0.4518 0.4971 0.0927  0.0400  -0.1079 109 LEU A N     
742  C  CA    . LEU A 100 ? 0.3114 0.4466 0.5334 0.1068  0.0317  -0.1100 109 LEU A CA    
743  C  C     . LEU A 100 ? 0.3485 0.4543 0.5363 0.0949  0.0341  -0.1044 109 LEU A C     
744  O  O     . LEU A 100 ? 0.3037 0.3934 0.4937 0.0995  0.0365  -0.1176 109 LEU A O     
745  C  CB    . LEU A 100 ? 0.4069 0.5227 0.6409 0.1183  0.0128  -0.0913 109 LEU A CB    
746  C  CG    . LEU A 100 ? 0.5037 0.5833 0.7511 0.1333  0.0002  -0.0895 109 LEU A CG    
747  C  CD1   . LEU A 100 ? 0.3796 0.4704 0.6676 0.1520  0.0028  -0.1151 109 LEU A CD1   
748  C  CD2   . LEU A 100 ? 0.5342 0.5983 0.7837 0.1382  -0.0190 -0.0651 109 LEU A CD2   
749  N  N     . ILE A 101 ? 0.2459 0.3454 0.4045 0.0800  0.0327  -0.0864 110 ILE A N     
750  C  CA    . ILE A 101 ? 0.3195 0.3958 0.4492 0.0691  0.0338  -0.0807 110 ILE A CA    
751  C  C     . ILE A 101 ? 0.3373 0.4292 0.4551 0.0587  0.0471  -0.0969 110 ILE A C     
752  O  O     . ILE A 101 ? 0.3137 0.3892 0.4203 0.0561  0.0486  -0.1036 110 ILE A O     
753  C  CB    . ILE A 101 ? 0.3483 0.4172 0.4559 0.0581  0.0283  -0.0599 110 ILE A CB    
754  C  CG1   . ILE A 101 ? 0.3825 0.4353 0.4971 0.0666  0.0156  -0.0457 110 ILE A CG1   
755  C  CG2   . ILE A 101 ? 0.3217 0.3749 0.4035 0.0466  0.0299  -0.0557 110 ILE A CG2   
756  C  CD1   . ILE A 101 ? 0.2674 0.3201 0.3669 0.0584  0.0110  -0.0305 110 ILE A CD1   
757  N  N     . LEU A 102 ? 0.2677 0.3932 0.3862 0.0504  0.0568  -0.1032 111 LEU A N     
758  C  CA    . LEU A 102 ? 0.2719 0.4173 0.3763 0.0379  0.0700  -0.1183 111 LEU A CA    
759  C  C     . LEU A 102 ? 0.3562 0.5064 0.4801 0.0497  0.0769  -0.1456 111 LEU A C     
760  O  O     . LEU A 102 ? 0.3609 0.5098 0.4685 0.0420  0.0835  -0.1583 111 LEU A O     
761  C  CB    . LEU A 102 ? 0.2601 0.4430 0.3620 0.0242  0.0791  -0.1183 111 LEU A CB    
762  C  CG    . LEU A 102 ? 0.3066 0.4831 0.3862 0.0087  0.0729  -0.0940 111 LEU A CG    
763  C  CD1   . LEU A 102 ? 0.3405 0.5538 0.4172 -0.0082 0.0826  -0.0953 111 LEU A CD1   
764  C  CD2   . LEU A 102 ? 0.2568 0.4078 0.3057 -0.0018 0.0677  -0.0821 111 LEU A CD2   
765  N  N     . ARG A 103 ? 0.2847 0.4403 0.4451 0.0690  0.0743  -0.1558 112 ARG A N     
766  C  CA    . ARG A 103 ? 0.3065 0.4626 0.4923 0.0839  0.0789  -0.1839 112 ARG A CA    
767  C  C     . ARG A 103 ? 0.3410 0.4529 0.5169 0.0873  0.0706  -0.1830 112 ARG A C     
768  O  O     . ARG A 103 ? 0.4312 0.5418 0.6041 0.0858  0.0782  -0.2056 112 ARG A O     
769  C  CB    . ARG A 103 ? 0.3080 0.4736 0.5392 0.1064  0.0728  -0.1910 112 ARG A CB    
770  C  CG    . ARG A 103 ? 0.4457 0.5949 0.6995 0.1214  0.0697  -0.2100 112 ARG A CG    
771  C  CD    . ARG A 103 ? 0.4581 0.6123 0.7496 0.1398  0.0594  -0.2087 112 ARG A CD    
772  N  NE    . ARG A 103 ? 0.5898 0.7232 0.9023 0.1538  0.0543  -0.2244 112 ARG A NE    
773  C  CZ    . ARG A 103 ? 0.6174 0.7745 0.9423 0.1549  0.0653  -0.2507 112 ARG A CZ    
774  N  NH1   . ARG A 103 ? 0.5857 0.7887 0.9017 0.1411  0.0824  -0.2632 112 ARG A NH1   
775  N  NH2   . ARG A 103 ? 0.6869 0.8212 1.0337 0.1690  0.0587  -0.2647 112 ARG A NH2   
776  N  N     . VAL A 104 ? 0.3116 0.3890 0.4820 0.0903  0.0552  -0.1579 113 VAL A N     
777  C  CA    . VAL A 104 ? 0.4367 0.4732 0.5977 0.0905  0.0468  -0.1541 113 VAL A CA    
778  C  C     . VAL A 104 ? 0.3936 0.4308 0.5201 0.0713  0.0541  -0.1567 113 VAL A C     
779  O  O     . VAL A 104 ? 0.4910 0.5136 0.6143 0.0698  0.0559  -0.1728 113 VAL A O     
780  C  CB    . VAL A 104 ? 0.4807 0.4884 0.6380 0.0927  0.0309  -0.1247 113 VAL A CB    
781  C  CG1   . VAL A 104 ? 0.4986 0.4692 0.6413 0.0869  0.0239  -0.1182 113 VAL A CG1   
782  C  CG2   . VAL A 104 ? 0.4204 0.4234 0.6114 0.1117  0.0201  -0.1216 113 VAL A CG2   
783  N  N     . LYS A 105 ? 0.4608 0.5144 0.5621 0.0561  0.0570  -0.1410 114 LYS A N     
784  C  CA    . LYS A 105 ? 0.3804 0.4366 0.4496 0.0377  0.0608  -0.1398 114 LYS A CA    
785  C  C     . LYS A 105 ? 0.4406 0.5254 0.5032 0.0298  0.0750  -0.1655 114 LYS A C     
786  O  O     . LYS A 105 ? 0.4667 0.5514 0.5037 0.0154  0.0769  -0.1690 114 LYS A O     
787  C  CB    . LYS A 105 ? 0.3584 0.4225 0.4071 0.0254  0.0577  -0.1157 114 LYS A CB    
788  C  CG    . LYS A 105 ? 0.3184 0.3571 0.3664 0.0289  0.0453  -0.0929 114 LYS A CG    
789  C  CD    . LYS A 105 ? 0.4081 0.4228 0.4441 0.0242  0.0396  -0.0903 114 LYS A CD    
790  C  CE    . LYS A 105 ? 0.3056 0.3029 0.3391 0.0246  0.0297  -0.0690 114 LYS A CE    
791  N  NZ    . LYS A 105 ? 0.3873 0.3688 0.4092 0.0167  0.0252  -0.0664 114 LYS A NZ    
792  N  N     . ASP A 106 ? 0.4023 0.5148 0.4875 0.0380  0.0849  -0.1843 115 ASP A N     
793  C  CA    . ASP A 106 ? 0.4386 0.5888 0.5169 0.0280  0.1014  -0.2098 115 ASP A CA    
794  C  C     . ASP A 106 ? 0.4271 0.5971 0.4667 0.0026  0.1050  -0.1940 115 ASP A C     
795  O  O     . ASP A 106 ? 0.5607 0.7425 0.5740 -0.0134 0.1112  -0.2041 115 ASP A O     
796  C  CB    . ASP A 106 ? 0.4148 0.5546 0.4951 0.0312  0.1056  -0.2388 115 ASP A CB    
797  C  CG    . ASP A 106 ? 0.4581 0.6366 0.5389 0.0241  0.1200  -0.2639 115 ASP A CG    
798  O  OD1   . ASP A 106 ? 0.5389 0.7519 0.6280 0.0214  0.1273  -0.2626 115 ASP A OD1   
799  O  OD2   . ASP A 106 ? 0.5876 0.7613 0.6599 0.0193  0.1220  -0.2814 115 ASP A OD2   
800  N  N     . ARG A 107 ? 0.3856 0.5577 0.4218 -0.0016 0.0994  -0.1684 116 ARG A N     
801  C  CA    . ARG A 107 ? 0.4849 0.6673 0.4885 -0.0240 0.0982  -0.1479 116 ARG A CA    
802  C  C     . ARG A 107 ? 0.3581 0.5674 0.3700 -0.0293 0.1028  -0.1395 116 ARG A C     
803  O  O     . ARG A 107 ? 0.3780 0.5882 0.4196 -0.0138 0.1012  -0.1405 116 ARG A O     
804  C  CB    . ARG A 107 ? 0.4546 0.6011 0.4441 -0.0252 0.0819  -0.1211 116 ARG A CB    
805  C  CG    . ARG A 107 ? 0.4885 0.6109 0.4684 -0.0239 0.0763  -0.1265 116 ARG A CG    
806  C  CD    . ARG A 107 ? 0.5790 0.7140 0.5251 -0.0453 0.0775  -0.1257 116 ARG A CD    
807  N  NE    . ARG A 107 ? 0.6598 0.7949 0.5873 -0.0585 0.0690  -0.0981 116 ARG A NE    
808  C  CZ    . ARG A 107 ? 0.5434 0.6533 0.4680 -0.0565 0.0546  -0.0771 116 ARG A CZ    
809  N  NH1   . ARG A 107 ? 0.5770 0.6627 0.5126 -0.0448 0.0482  -0.0788 116 ARG A NH1   
810  N  NH2   . ARG A 107 ? 0.6632 0.7726 0.5752 -0.0670 0.0464  -0.0545 116 ARG A NH2   
811  N  N     . GLU A 108 ? 0.3844 0.6156 0.3693 -0.0531 0.1072  -0.1300 117 GLU A N     
812  C  CA    . GLU A 108 ? 0.4226 0.6759 0.4118 -0.0630 0.1099  -0.1180 117 GLU A CA    
813  C  C     . GLU A 108 ? 0.3223 0.5450 0.3080 -0.0629 0.0937  -0.0885 117 GLU A C     
814  O  O     . GLU A 108 ? 0.3996 0.6317 0.3988 -0.0640 0.0930  -0.0806 117 GLU A O     
815  C  CB    . GLU A 108 ? 0.3467 0.6347 0.3068 -0.0919 0.1201  -0.1169 117 GLU A CB    
816  C  CG    . GLU A 108 ? 0.3670 0.6956 0.3305 -0.0952 0.1393  -0.1493 117 GLU A CG    
817  C  CD    . GLU A 108 ? 0.4214 0.7794 0.3627 -0.1229 0.1432  -0.1418 117 GLU A CD    
818  O  OE1   . GLU A 108 ? 0.4268 0.7844 0.3540 -0.1400 0.1376  -0.1158 117 GLU A OE1   
819  O  OE2   . GLU A 108 ? 0.4904 0.8710 0.4291 -0.1284 0.1511  -0.1619 117 GLU A OE2   
820  N  N     . SER A 109 ? 0.3689 0.5578 0.3386 -0.0620 0.0811  -0.0743 118 SER A N     
821  C  CA    . SER A 109 ? 0.3695 0.5296 0.3391 -0.0593 0.0663  -0.0510 118 SER A CA    
822  C  C     . SER A 109 ? 0.3204 0.4487 0.2899 -0.0465 0.0565  -0.0484 118 SER A C     
823  O  O     . SER A 109 ? 0.3657 0.4917 0.3248 -0.0476 0.0583  -0.0578 118 SER A O     
824  C  CB    . SER A 109 ? 0.3321 0.4912 0.2771 -0.0814 0.0596  -0.0295 118 SER A CB    
825  O  OG    . SER A 109 ? 0.5237 0.6790 0.4423 -0.0929 0.0563  -0.0258 118 SER A OG    
826  N  N     . PHE A 110 ? 0.2983 0.4049 0.2792 -0.0360 0.0466  -0.0366 119 PHE A N     
827  C  CA    . PHE A 110 ? 0.3319 0.4124 0.3143 -0.0257 0.0381  -0.0329 119 PHE A CA    
828  C  C     . PHE A 110 ? 0.3464 0.4111 0.3341 -0.0222 0.0279  -0.0175 119 PHE A C     
829  O  O     . PHE A 110 ? 0.3647 0.4358 0.3622 -0.0213 0.0285  -0.0149 119 PHE A O     
830  C  CB    . PHE A 110 ? 0.2485 0.3237 0.2490 -0.0097 0.0417  -0.0472 119 PHE A CB    
831  C  CG    . PHE A 110 ? 0.2601 0.3123 0.2584 -0.0044 0.0350  -0.0451 119 PHE A CG    
832  C  CD1   . PHE A 110 ? 0.2613 0.3113 0.2471 -0.0106 0.0362  -0.0530 119 PHE A CD1   
833  C  CD2   . PHE A 110 ? 0.2515 0.2873 0.2591 0.0044  0.0278  -0.0357 119 PHE A CD2   
834  C  CE1   . PHE A 110 ? 0.3909 0.4220 0.3762 -0.0080 0.0299  -0.0509 119 PHE A CE1   
835  C  CE2   . PHE A 110 ? 0.2979 0.3169 0.3037 0.0064  0.0227  -0.0334 119 PHE A CE2   
836  C  CZ    . PHE A 110 ? 0.3440 0.3602 0.3399 0.0002  0.0236  -0.0406 119 PHE A CZ    
837  N  N     . PRO A 111 ? 0.3559 0.4024 0.3385 -0.0207 0.0188  -0.0090 120 PRO A N     
838  C  CA    . PRO A 111 ? 0.3027 0.3366 0.2922 -0.0168 0.0101  0.0015  120 PRO A CA    
839  C  C     . PRO A 111 ? 0.3000 0.3339 0.3052 -0.0059 0.0118  -0.0020 120 PRO A C     
840  O  O     . PRO A 111 ? 0.3139 0.3430 0.3258 0.0034  0.0128  -0.0065 120 PRO A O     
841  C  CB    . PRO A 111 ? 0.2381 0.2593 0.2256 -0.0138 0.0031  0.0048  120 PRO A CB    
842  C  CG    . PRO A 111 ? 0.3455 0.3720 0.3180 -0.0231 0.0040  0.0029  120 PRO A CG    
843  C  CD    . PRO A 111 ? 0.3959 0.4364 0.3671 -0.0242 0.0158  -0.0099 120 PRO A CD    
844  N  N     . MET A 112 ? 0.3160 0.3553 0.3261 -0.0090 0.0110  0.0012  121 MET A N     
845  C  CA    . MET A 112 ? 0.2882 0.3304 0.3113 -0.0009 0.0107  -0.0013 121 MET A CA    
846  C  C     . MET A 112 ? 0.2941 0.3330 0.3189 -0.0066 0.0051  0.0044  121 MET A C     
847  O  O     . MET A 112 ? 0.3353 0.3729 0.3535 -0.0181 0.0030  0.0104  121 MET A O     
848  C  CB    . MET A 112 ? 0.2905 0.3510 0.3241 0.0026  0.0177  -0.0095 121 MET A CB    
849  C  CG    . MET A 112 ? 0.3185 0.3812 0.3529 0.0076  0.0236  -0.0186 121 MET A CG    
850  S  SD    . MET A 112 ? 0.4705 0.5555 0.5255 0.0157  0.0307  -0.0318 121 MET A SD    
851  C  CE    . MET A 112 ? 0.5105 0.5854 0.5788 0.0288  0.0215  -0.0260 121 MET A CE    
852  N  N     . ILE A 113 ? 0.2366 0.2735 0.2692 -0.0001 0.0018  0.0026  122 ILE A N     
853  C  CA    . ILE A 113 ? 0.2178 0.2511 0.2541 -0.0047 -0.0036 0.0039  122 ILE A CA    
854  C  C     . ILE A 113 ? 0.3119 0.3595 0.3571 -0.0014 -0.0029 -0.0007 122 ILE A C     
855  O  O     . ILE A 113 ? 0.2881 0.3398 0.3356 0.0076  -0.0023 -0.0029 122 ILE A O     
856  C  CB    . ILE A 113 ? 0.3107 0.3278 0.3472 -0.0007 -0.0100 0.0034  122 ILE A CB    
857  C  CG1   . ILE A 113 ? 0.2770 0.2812 0.3084 -0.0041 -0.0141 0.0096  122 ILE A CG1   
858  C  CG2   . ILE A 113 ? 0.3229 0.3356 0.3656 -0.0036 -0.0155 0.0000  122 ILE A CG2   
859  C  CD1   . ILE A 113 ? 0.3292 0.3195 0.3677 0.0011  -0.0217 0.0075  122 ILE A CD1   
860  N  N     . LEU A 114 ? 0.2647 0.3201 0.3150 -0.0101 -0.0044 -0.0006 123 LEU A N     
861  C  CA    . LEU A 114 ? 0.2501 0.3212 0.3100 -0.0086 -0.0061 -0.0047 123 LEU A CA    
862  C  C     . LEU A 114 ? 0.2731 0.3340 0.3311 -0.0079 -0.0129 -0.0083 123 LEU A C     
863  O  O     . LEU A 114 ? 0.3220 0.3687 0.3790 -0.0150 -0.0170 -0.0088 123 LEU A O     
864  C  CB    . LEU A 114 ? 0.2292 0.3179 0.2971 -0.0203 -0.0041 -0.0045 123 LEU A CB    
865  C  CG    . LEU A 114 ? 0.2335 0.3432 0.3146 -0.0199 -0.0072 -0.0089 123 LEU A CG    
866  C  CD1   . LEU A 114 ? 0.1937 0.3167 0.2830 -0.0053 -0.0067 -0.0111 123 LEU A CD1   
867  C  CD2   . LEU A 114 ? 0.2849 0.4158 0.3757 -0.0339 -0.0040 -0.0090 123 LEU A CD2   
868  N  N     . VAL A 115 ? 0.2382 0.3064 0.2960 -0.0002 -0.0146 -0.0110 124 VAL A N     
869  C  CA    . VAL A 115 ? 0.2536 0.3176 0.3065 0.0003  -0.0191 -0.0171 124 VAL A CA    
870  C  C     . VAL A 115 ? 0.2758 0.3577 0.3329 -0.0034 -0.0241 -0.0203 124 VAL A C     
871  O  O     . VAL A 115 ? 0.2771 0.3745 0.3370 0.0014  -0.0256 -0.0162 124 VAL A O     
872  C  CB    . VAL A 115 ? 0.2573 0.3187 0.3017 0.0082  -0.0173 -0.0165 124 VAL A CB    
873  C  CG1   . VAL A 115 ? 0.2174 0.2827 0.2554 0.0069  -0.0199 -0.0250 124 VAL A CG1   
874  C  CG2   . VAL A 115 ? 0.2293 0.2756 0.2717 0.0108  -0.0135 -0.0143 124 VAL A CG2   
875  N  N     . ALA A 116 ? 0.2582 0.3368 0.3171 -0.0119 -0.0282 -0.0276 125 ALA A N     
876  C  CA    . ALA A 116 ? 0.3047 0.4009 0.3667 -0.0177 -0.0342 -0.0326 125 ALA A CA    
877  C  C     . ALA A 116 ? 0.3316 0.4281 0.3819 -0.0165 -0.0370 -0.0422 125 ALA A C     
878  O  O     . ALA A 116 ? 0.3459 0.4289 0.3949 -0.0201 -0.0379 -0.0538 125 ALA A O     
879  C  CB    . ALA A 116 ? 0.2857 0.3788 0.3567 -0.0307 -0.0372 -0.0361 125 ALA A CB    
880  N  N     . ASN A 117 ? 0.3053 0.4175 0.3475 -0.0120 -0.0390 -0.0378 126 ASN A N     
881  C  CA    . ASN A 117 ? 0.2688 0.3860 0.2953 -0.0129 -0.0397 -0.0454 126 ASN A CA    
882  C  C     . ASN A 117 ? 0.2982 0.4340 0.3199 -0.0219 -0.0477 -0.0535 126 ASN A C     
883  O  O     . ASN A 117 ? 0.3643 0.5107 0.3967 -0.0264 -0.0537 -0.0511 126 ASN A O     
884  C  CB    . ASN A 117 ? 0.3093 0.4316 0.3252 -0.0067 -0.0383 -0.0333 126 ASN A CB    
885  C  CG    . ASN A 117 ? 0.3687 0.4970 0.3665 -0.0098 -0.0354 -0.0408 126 ASN A CG    
886  O  OD1   . ASN A 117 ? 0.3357 0.4568 0.3339 -0.0106 -0.0299 -0.0558 126 ASN A OD1   
887  N  ND2   . ASN A 117 ? 0.2784 0.4213 0.2614 -0.0123 -0.0397 -0.0306 126 ASN A ND2   
888  N  N     . LYS A 118 ? 0.2940 0.4369 0.2995 -0.0256 -0.0472 -0.0648 127 LYS A N     
889  C  CA    . LYS A 118 ? 0.2928 0.4561 0.2875 -0.0357 -0.0546 -0.0747 127 LYS A CA    
890  C  C     . LYS A 118 ? 0.3052 0.4617 0.3116 -0.0438 -0.0580 -0.0908 127 LYS A C     
891  O  O     . LYS A 118 ? 0.3410 0.5151 0.3455 -0.0531 -0.0667 -0.0952 127 LYS A O     
892  C  CB    . LYS A 118 ? 0.3552 0.5408 0.3465 -0.0369 -0.0651 -0.0577 127 LYS A CB    
893  C  CG    . LYS A 118 ? 0.3880 0.5769 0.3673 -0.0308 -0.0651 -0.0396 127 LYS A CG    
894  C  CD    . LYS A 118 ? 0.3157 0.5262 0.2907 -0.0328 -0.0797 -0.0238 127 LYS A CD    
895  C  CE    . LYS A 118 ? 0.3167 0.5246 0.2801 -0.0281 -0.0823 -0.0034 127 LYS A CE    
896  N  NZ    . LYS A 118 ? 0.3391 0.5644 0.3013 -0.0286 -0.1001 0.0149  127 LYS A NZ    
897  N  N     . VAL A 119 ? 0.3308 0.4612 0.3498 -0.0414 -0.0530 -0.0990 128 VAL A N     
898  C  CA    . VAL A 119 ? 0.3146 0.4323 0.3452 -0.0505 -0.0577 -0.1130 128 VAL A CA    
899  C  C     . VAL A 119 ? 0.4154 0.5389 0.4365 -0.0575 -0.0599 -0.1385 128 VAL A C     
900  O  O     . VAL A 119 ? 0.4844 0.5977 0.5144 -0.0669 -0.0656 -0.1525 128 VAL A O     
901  C  CB    . VAL A 119 ? 0.3916 0.4758 0.4377 -0.0469 -0.0547 -0.1122 128 VAL A CB    
902  C  CG1   . VAL A 119 ? 0.3789 0.4610 0.4322 -0.0433 -0.0522 -0.0893 128 VAL A CG1   
903  C  CG2   . VAL A 119 ? 0.3237 0.3938 0.3681 -0.0368 -0.0485 -0.1238 128 VAL A CG2   
904  N  N     . ASP A 120 ? 0.3463 0.4871 0.3488 -0.0549 -0.0552 -0.1459 129 ASP A N     
905  C  CA    . ASP A 120 ? 0.3738 0.5288 0.3637 -0.0636 -0.0563 -0.1723 129 ASP A CA    
906  C  C     . ASP A 120 ? 0.4394 0.6208 0.4180 -0.0770 -0.0672 -0.1705 129 ASP A C     
907  O  O     . ASP A 120 ? 0.4311 0.6208 0.4028 -0.0875 -0.0708 -0.1944 129 ASP A O     
908  C  CB    . ASP A 120 ? 0.3794 0.5520 0.3502 -0.0600 -0.0467 -0.1803 129 ASP A CB    
909  C  CG    . ASP A 120 ? 0.4127 0.6076 0.3648 -0.0601 -0.0475 -0.1540 129 ASP A CG    
910  O  OD1   . ASP A 120 ? 0.4040 0.5863 0.3650 -0.0507 -0.0454 -0.1321 129 ASP A OD1   
911  O  OD2   . ASP A 120 ? 0.4306 0.6543 0.3588 -0.0704 -0.0514 -0.1550 129 ASP A OD2   
912  N  N     . LEU A 121 ? 0.4176 0.6133 0.3962 -0.0763 -0.0733 -0.1445 130 LEU A N     
913  C  CA    . LEU A 121 ? 0.3859 0.6095 0.3584 -0.0875 -0.0862 -0.1401 130 LEU A CA    
914  C  C     . LEU A 121 ? 0.4749 0.6896 0.4716 -0.0942 -0.0926 -0.1417 130 LEU A C     
915  O  O     . LEU A 121 ? 0.3758 0.6010 0.3871 -0.0932 -0.0980 -0.1231 130 LEU A O     
916  C  CB    . LEU A 121 ? 0.3771 0.6207 0.3428 -0.0819 -0.0916 -0.1122 130 LEU A CB    
917  C  CG    . LEU A 121 ? 0.4116 0.6631 0.3523 -0.0783 -0.0865 -0.1050 130 LEU A CG    
918  C  CD1   . LEU A 121 ? 0.3660 0.6306 0.3046 -0.0730 -0.0958 -0.0749 130 LEU A CD1   
919  C  CD2   . LEU A 121 ? 0.4346 0.7076 0.3471 -0.0918 -0.0871 -0.1253 130 LEU A CD2   
920  N  N     . MET A 122 ? 0.4174 0.6131 0.4199 -0.1019 -0.0918 -0.1656 131 MET A N     
921  C  CA    . MET A 122 ? 0.4675 0.6471 0.4931 -0.1105 -0.0967 -0.1664 131 MET A CA    
922  C  C     . MET A 122 ? 0.4691 0.6789 0.4980 -0.1250 -0.1093 -0.1646 131 MET A C     
923  O  O     . MET A 122 ? 0.4674 0.6771 0.5171 -0.1317 -0.1129 -0.1551 131 MET A O     
924  C  CB    . MET A 122 ? 0.5888 0.7345 0.6211 -0.1148 -0.0950 -0.1921 131 MET A CB    
925  C  CG    . MET A 122 ? 0.5750 0.7312 0.5900 -0.1209 -0.0962 -0.2226 131 MET A CG    
926  S  SD    . MET A 122 ? 0.8068 0.9240 0.8304 -0.1119 -0.0881 -0.2523 131 MET A SD    
927  C  CE    . MET A 122 ? 0.6453 0.7560 0.6691 -0.0911 -0.0759 -0.2303 131 MET A CE    
928  N  N     . HIS A 123 ? 0.4351 0.6745 0.4438 -0.1315 -0.1164 -0.1732 132 HIS A N     
929  C  CA    . HIS A 123 ? 0.4524 0.7240 0.4649 -0.1455 -0.1307 -0.1715 132 HIS A CA    
930  C  C     . HIS A 123 ? 0.4685 0.7694 0.4888 -0.1375 -0.1370 -0.1428 132 HIS A C     
931  O  O     . HIS A 123 ? 0.4152 0.7426 0.4498 -0.1459 -0.1486 -0.1373 132 HIS A O     
932  C  CB    . HIS A 123 ? 0.4710 0.7543 0.4572 -0.1535 -0.1346 -0.1879 132 HIS A CB    
933  C  CG    . HIS A 123 ? 0.5003 0.7529 0.4841 -0.1588 -0.1284 -0.2172 132 HIS A CG    
934  N  ND1   . HIS A 123 ? 0.5058 0.7413 0.4773 -0.1503 -0.1165 -0.2333 132 HIS A ND1   
935  C  CD2   . HIS A 123 ? 0.5246 0.7589 0.5203 -0.1706 -0.1328 -0.2327 132 HIS A CD2   
936  C  CE1   . HIS A 123 ? 0.5346 0.7426 0.5123 -0.1546 -0.1142 -0.2582 132 HIS A CE1   
937  N  NE2   . HIS A 123 ? 0.5476 0.7523 0.5385 -0.1675 -0.1246 -0.2577 132 HIS A NE2   
938  N  N     . LEU A 124 ? 0.4068 0.7027 0.4208 -0.1209 -0.1301 -0.1254 133 LEU A N     
939  C  CA    . LEU A 124 ? 0.4244 0.7396 0.4513 -0.1098 -0.1353 -0.0993 133 LEU A CA    
940  C  C     . LEU A 124 ? 0.3712 0.6685 0.4244 -0.0996 -0.1252 -0.0884 133 LEU A C     
941  O  O     . LEU A 124 ? 0.3873 0.7003 0.4575 -0.0895 -0.1281 -0.0708 133 LEU A O     
942  C  CB    . LEU A 124 ? 0.4304 0.7508 0.4336 -0.0997 -0.1360 -0.0857 133 LEU A CB    
943  C  CG    . LEU A 124 ? 0.4501 0.7959 0.4225 -0.1113 -0.1473 -0.0910 133 LEU A CG    
944  C  CD1   . LEU A 124 ? 0.4103 0.7552 0.3565 -0.1043 -0.1448 -0.0767 133 LEU A CD1   
945  C  CD2   . LEU A 124 ? 0.4174 0.7929 0.4007 -0.1161 -0.1652 -0.0802 133 LEU A CD2   
946  N  N     . ARG A 125 ? 0.3689 0.6341 0.4261 -0.1024 -0.1143 -0.0991 134 ARG A N     
947  C  CA    . ARG A 125 ? 0.3472 0.5944 0.4224 -0.0945 -0.1040 -0.0882 134 ARG A CA    
948  C  C     . ARG A 125 ? 0.3702 0.6413 0.4730 -0.1007 -0.1077 -0.0805 134 ARG A C     
949  O  O     . ARG A 125 ? 0.3572 0.6403 0.4691 -0.1172 -0.1147 -0.0896 134 ARG A O     
950  C  CB    . ARG A 125 ? 0.3305 0.5389 0.4039 -0.0989 -0.0956 -0.1000 134 ARG A CB    
951  C  CG    . ARG A 125 ? 0.3261 0.5159 0.4133 -0.0939 -0.0862 -0.0876 134 ARG A CG    
952  C  CD    . ARG A 125 ? 0.3222 0.4712 0.4042 -0.0935 -0.0805 -0.0956 134 ARG A CD    
953  N  NE    . ARG A 125 ? 0.3966 0.5292 0.4862 -0.0883 -0.0724 -0.0815 134 ARG A NE    
954  C  CZ    . ARG A 125 ? 0.4034 0.5018 0.4904 -0.0849 -0.0684 -0.0825 134 ARG A CZ    
955  N  NH1   . ARG A 125 ? 0.3301 0.4063 0.4113 -0.0837 -0.0708 -0.0989 134 ARG A NH1   
956  N  NH2   . ARG A 125 ? 0.3504 0.4386 0.4419 -0.0824 -0.0625 -0.0681 134 ARG A NH2   
957  N  N     . LYS A 126 ? 0.3774 0.6569 0.4948 -0.0881 -0.1025 -0.0656 135 LYS A N     
958  C  CA    . LYS A 126 ? 0.3280 0.6361 0.4750 -0.0919 -0.1030 -0.0600 135 LYS A CA    
959  C  C     . LYS A 126 ? 0.3632 0.6563 0.5208 -0.0923 -0.0890 -0.0555 135 LYS A C     
960  O  O     . LYS A 126 ? 0.3220 0.6353 0.5006 -0.1040 -0.0868 -0.0554 135 LYS A O     
961  C  CB    . LYS A 126 ? 0.3638 0.7045 0.5249 -0.0765 -0.1108 -0.0489 135 LYS A CB    
962  C  CG    . LYS A 126 ? 0.4593 0.8188 0.6083 -0.0779 -0.1276 -0.0490 135 LYS A CG    
963  C  CD    . LYS A 126 ? 0.5060 0.8924 0.6708 -0.0614 -0.1385 -0.0346 135 LYS A CD    
964  C  CE    . LYS A 126 ? 0.6210 1.0217 0.7659 -0.0640 -0.1567 -0.0306 135 LYS A CE    
965  N  NZ    . LYS A 126 ? 0.5187 0.8890 0.6233 -0.0662 -0.1516 -0.0334 135 LYS A NZ    
966  N  N     . ILE A 127 ? 0.3486 0.6103 0.4916 -0.0818 -0.0796 -0.0516 136 ILE A N     
967  C  CA    . ILE A 127 ? 0.3464 0.5925 0.4940 -0.0835 -0.0673 -0.0465 136 ILE A CA    
968  C  C     . ILE A 127 ? 0.3253 0.5340 0.4597 -0.0964 -0.0663 -0.0520 136 ILE A C     
969  O  O     . ILE A 127 ? 0.3258 0.5071 0.4428 -0.0898 -0.0671 -0.0570 136 ILE A O     
970  C  CB    . ILE A 127 ? 0.2411 0.4765 0.3828 -0.0643 -0.0595 -0.0386 136 ILE A CB    
971  C  CG1   . ILE A 127 ? 0.3105 0.5760 0.4663 -0.0493 -0.0643 -0.0338 136 ILE A CG1   
972  C  CG2   . ILE A 127 ? 0.3357 0.5624 0.4816 -0.0679 -0.0475 -0.0338 136 ILE A CG2   
973  C  CD1   . ILE A 127 ? 0.3346 0.6410 0.5210 -0.0537 -0.0652 -0.0348 136 ILE A CD1   
974  N  N     . THR A 128 ? 0.3195 0.5277 0.4639 -0.1151 -0.0652 -0.0511 137 THR A N     
975  C  CA    . THR A 128 ? 0.3807 0.5492 0.5162 -0.1279 -0.0674 -0.0544 137 THR A CA    
976  C  C     . THR A 128 ? 0.3740 0.5108 0.4986 -0.1193 -0.0600 -0.0459 137 THR A C     
977  O  O     . THR A 128 ? 0.4016 0.5496 0.5260 -0.1081 -0.0515 -0.0374 137 THR A O     
978  C  CB    . THR A 128 ? 0.4363 0.6113 0.5848 -0.1535 -0.0696 -0.0521 137 THR A CB    
979  O  OG1   . THR A 128 ? 0.4645 0.6517 0.6189 -0.1585 -0.0594 -0.0388 137 THR A OG1   
980  C  CG2   . THR A 128 ? 0.4016 0.6172 0.5651 -0.1624 -0.0766 -0.0595 137 THR A CG2   
981  N  N     . ARG A 129 ? 0.4323 0.5285 0.5497 -0.1243 -0.0645 -0.0494 138 ARG A N     
982  C  CA    . ARG A 129 ? 0.4619 0.5275 0.5715 -0.1189 -0.0606 -0.0398 138 ARG A CA    
983  C  C     . ARG A 129 ? 0.4866 0.5618 0.5990 -0.1321 -0.0546 -0.0236 138 ARG A C     
984  O  O     . ARG A 129 ? 0.4387 0.5118 0.5441 -0.1241 -0.0475 -0.0143 138 ARG A O     
985  C  CB    . ARG A 129 ? 0.4799 0.5009 0.5878 -0.1229 -0.0697 -0.0466 138 ARG A CB    
986  C  CG    . ARG A 129 ? 0.5787 0.5672 0.6821 -0.1211 -0.0699 -0.0335 138 ARG A CG    
987  C  CD    . ARG A 129 ? 0.5708 0.5139 0.6788 -0.1221 -0.0814 -0.0412 138 ARG A CD    
988  N  NE    . ARG A 129 ? 0.6441 0.5824 0.7517 -0.1027 -0.0813 -0.0609 138 ARG A NE    
989  C  CZ    . ARG A 129 ? 0.7928 0.6983 0.9084 -0.0983 -0.0898 -0.0759 138 ARG A CZ    
990  N  NH1   . ARG A 129 ? 0.7369 0.6051 0.8624 -0.1111 -0.1017 -0.0723 138 ARG A NH1   
991  N  NH2   . ARG A 129 ? 0.8167 0.7273 0.9314 -0.0813 -0.0865 -0.0955 138 ARG A NH2   
992  N  N     . GLU A 130 ? 0.4222 0.5110 0.5441 -0.1544 -0.0569 -0.0210 139 GLU A N     
993  C  CA    . GLU A 130 ? 0.4849 0.5883 0.6080 -0.1713 -0.0499 -0.0063 139 GLU A CA    
994  C  C     . GLU A 130 ? 0.4057 0.5538 0.5346 -0.1601 -0.0371 -0.0059 139 GLU A C     
995  O  O     . GLU A 130 ? 0.3508 0.5049 0.4733 -0.1625 -0.0280 0.0035  139 GLU A O     
996  C  CB    . GLU A 130 ? 0.4383 0.5508 0.5719 -0.2000 -0.0548 -0.0045 139 GLU A CB    
997  C  CG    . GLU A 130 ? 0.5889 0.6503 0.7182 -0.2148 -0.0684 -0.0024 139 GLU A CG    
998  C  CD    . GLU A 130 ? 0.7410 0.7810 0.8727 -0.2022 -0.0783 -0.0217 139 GLU A CD    
999  O  OE1   . GLU A 130 ? 0.7122 0.7831 0.8480 -0.1893 -0.0760 -0.0347 139 GLU A OE1   
1000 O  OE2   . GLU A 130 ? 0.7852 0.7778 0.9149 -0.2052 -0.0890 -0.0243 139 GLU A OE2   
1001 N  N     . GLN A 131 ? 0.4162 0.5958 0.5577 -0.1481 -0.0374 -0.0165 140 GLN A N     
1002 C  CA    . GLN A 131 ? 0.3285 0.5452 0.4797 -0.1330 -0.0278 -0.0178 140 GLN A CA    
1003 C  C     . GLN A 131 ? 0.3190 0.5144 0.4557 -0.1129 -0.0229 -0.0149 140 GLN A C     
1004 O  O     . GLN A 131 ? 0.3700 0.5811 0.5081 -0.1081 -0.0126 -0.0123 140 GLN A O     
1005 C  CB    . GLN A 131 ? 0.3508 0.5986 0.5184 -0.1223 -0.0338 -0.0272 140 GLN A CB    
1006 C  CG    . GLN A 131 ? 0.3634 0.6450 0.5508 -0.1417 -0.0375 -0.0309 140 GLN A CG    
1007 C  CD    . GLN A 131 ? 0.3960 0.7083 0.5990 -0.1308 -0.0467 -0.0388 140 GLN A CD    
1008 O  OE1   . GLN A 131 ? 0.3710 0.6653 0.5621 -0.1231 -0.0567 -0.0430 140 GLN A OE1   
1009 N  NE2   . GLN A 131 ? 0.5645 0.9263 0.7949 -0.1304 -0.0438 -0.0411 140 GLN A NE2   
1010 N  N     . GLY A 132 ? 0.3880 0.5497 0.5116 -0.1020 -0.0297 -0.0172 141 GLY A N     
1011 C  CA    . GLY A 132 ? 0.3198 0.4623 0.4308 -0.0849 -0.0257 -0.0145 141 GLY A CA    
1012 C  C     . GLY A 132 ? 0.3501 0.4751 0.4504 -0.0932 -0.0206 -0.0044 141 GLY A C     
1013 O  O     . GLY A 132 ? 0.3278 0.4583 0.4235 -0.0844 -0.0128 -0.0018 141 GLY A O     
1014 N  N     . LYS A 133 ? 0.4001 0.5029 0.4958 -0.1112 -0.0263 0.0018  142 LYS A N     
1015 C  CA    . LYS A 133 ? 0.4028 0.4879 0.4858 -0.1216 -0.0245 0.0150  142 LYS A CA    
1016 C  C     . LYS A 133 ? 0.3787 0.4998 0.4626 -0.1336 -0.0125 0.0198  142 LYS A C     
1017 O  O     . LYS A 133 ? 0.3405 0.4608 0.4119 -0.1340 -0.0065 0.0264  142 LYS A O     
1018 C  CB    . LYS A 133 ? 0.4172 0.4673 0.4970 -0.1392 -0.0364 0.0228  142 LYS A CB    
1019 C  CG    . LYS A 133 ? 0.4657 0.4771 0.5451 -0.1253 -0.0472 0.0160  142 LYS A CG    
1020 C  CD    . LYS A 133 ? 0.5578 0.5289 0.6372 -0.1407 -0.0607 0.0243  142 LYS A CD    
1021 C  CE    . LYS A 133 ? 0.6783 0.6137 0.7622 -0.1238 -0.0705 0.0138  142 LYS A CE    
1022 N  NZ    . LYS A 133 ? 0.7664 0.6574 0.8551 -0.1358 -0.0861 0.0209  142 LYS A NZ    
1023 N  N     . GLU A 134 ? 0.3356 0.4922 0.4351 -0.1441 -0.0087 0.0148  143 GLU A N     
1024 C  CA    . GLU A 134 ? 0.3269 0.5263 0.4320 -0.1542 0.0050  0.0147  143 GLU A CA    
1025 C  C     . GLU A 134 ? 0.2822 0.5005 0.3913 -0.1311 0.0147  0.0054  143 GLU A C     
1026 O  O     . GLU A 134 ? 0.2839 0.5181 0.3859 -0.1353 0.0257  0.0061  143 GLU A O     
1027 C  CB    . GLU A 134 ? 0.3800 0.6187 0.5075 -0.1671 0.0066  0.0084  143 GLU A CB    
1028 C  CG    . GLU A 134 ? 0.4445 0.6690 0.5690 -0.1960 -0.0014 0.0180  143 GLU A CG    
1029 C  CD    . GLU A 134 ? 0.6281 0.8910 0.7769 -0.2071 -0.0020 0.0098  143 GLU A CD    
1030 O  OE1   . GLU A 134 ? 0.6190 0.9240 0.7885 -0.1923 0.0042  -0.0024 143 GLU A OE1   
1031 O  OE2   . GLU A 134 ? 0.7360 0.9860 0.8850 -0.2308 -0.0102 0.0157  143 GLU A OE2   
1032 N  N     . MET A 135 ? 0.2709 0.4872 0.3903 -0.1081 0.0101  -0.0035 144 MET A N     
1033 C  CA    . MET A 135 ? 0.2629 0.4897 0.3873 -0.0859 0.0164  -0.0112 144 MET A CA    
1034 C  C     . MET A 135 ? 0.3301 0.5283 0.4324 -0.0815 0.0188  -0.0057 144 MET A C     
1035 O  O     . MET A 135 ? 0.3249 0.5374 0.4260 -0.0768 0.0288  -0.0103 144 MET A O     
1036 C  CB    . MET A 135 ? 0.3538 0.5764 0.4884 -0.0659 0.0074  -0.0166 144 MET A CB    
1037 C  CG    . MET A 135 ? 0.2651 0.4884 0.4037 -0.0432 0.0102  -0.0214 144 MET A CG    
1038 S  SD    . MET A 135 ? 0.3148 0.5862 0.4830 -0.0358 0.0205  -0.0335 144 MET A SD    
1039 C  CE    . MET A 135 ? 0.2456 0.5463 0.4407 -0.0340 0.0099  -0.0365 144 MET A CE    
1040 N  N     . ALA A 136 ? 0.3216 0.4807 0.4082 -0.0826 0.0094  0.0024  145 ALA A N     
1041 C  CA    . ALA A 136 ? 0.3564 0.4900 0.4245 -0.0790 0.0095  0.0085  145 ALA A CA    
1042 C  C     . ALA A 136 ? 0.3398 0.4815 0.3945 -0.0985 0.0157  0.0167  145 ALA A C     
1043 O  O     . ALA A 136 ? 0.3545 0.4977 0.3979 -0.0954 0.0217  0.0164  145 ALA A O     
1044 C  CB    . ALA A 136 ? 0.3198 0.4144 0.3799 -0.0762 -0.0027 0.0138  145 ALA A CB    
1045 N  N     . THR A 137 ? 0.3069 0.4542 0.3609 -0.1209 0.0139  0.0245  146 THR A N     
1046 C  CA    . THR A 137 ? 0.3594 0.5178 0.3974 -0.1442 0.0197  0.0349  146 THR A CA    
1047 C  C     . THR A 137 ? 0.4140 0.6189 0.4575 -0.1440 0.0371  0.0224  146 THR A C     
1048 O  O     . THR A 137 ? 0.4147 0.6278 0.4405 -0.1521 0.0443  0.0247  146 THR A O     
1049 C  CB    . THR A 137 ? 0.3438 0.4999 0.3817 -0.1707 0.0139  0.0466  146 THR A CB    
1050 O  OG1   . THR A 137 ? 0.5266 0.6353 0.5613 -0.1692 -0.0032 0.0556  146 THR A OG1   
1051 C  CG2   . THR A 137 ? 0.3715 0.5414 0.3892 -0.1991 0.0195  0.0605  146 THR A CG2   
1052 N  N     . LYS A 138 ? 0.3459 0.5832 0.4154 -0.1344 0.0433  0.0077  147 LYS A N     
1053 C  CA    . LYS A 138 ? 0.3613 0.6445 0.4438 -0.1305 0.0595  -0.0084 147 LYS A CA    
1054 C  C     . LYS A 138 ? 0.2942 0.5676 0.3688 -0.1117 0.0638  -0.0167 147 LYS A C     
1055 O  O     . LYS A 138 ? 0.3997 0.6982 0.4678 -0.1177 0.0768  -0.0253 147 LYS A O     
1056 C  CB    . LYS A 138 ? 0.2890 0.6037 0.4062 -0.1178 0.0608  -0.0223 147 LYS A CB    
1057 C  CG    . LYS A 138 ? 0.3084 0.6735 0.4474 -0.1113 0.0768  -0.0419 147 LYS A CG    
1058 C  CD    . LYS A 138 ? 0.3028 0.6975 0.4805 -0.0955 0.0744  -0.0543 147 LYS A CD    
1059 C  CE    . LYS A 138 ? 0.2586 0.6217 0.4432 -0.0670 0.0614  -0.0548 147 LYS A CE    
1060 N  NZ    . LYS A 138 ? 0.3289 0.7209 0.5505 -0.0516 0.0560  -0.0642 147 LYS A NZ    
1061 N  N     . HIS A 139 ? 0.2913 0.5296 0.3653 -0.0911 0.0535  -0.0153 148 HIS A N     
1062 C  CA    . HIS A 139 ? 0.3372 0.5629 0.4050 -0.0743 0.0560  -0.0224 148 HIS A CA    
1063 C  C     . HIS A 139 ? 0.3408 0.5357 0.3791 -0.0826 0.0509  -0.0097 148 HIS A C     
1064 O  O     . HIS A 139 ? 0.3068 0.4888 0.3385 -0.0705 0.0513  -0.0145 148 HIS A O     
1065 C  CB    . HIS A 139 ? 0.3275 0.5354 0.4107 -0.0493 0.0477  -0.0267 148 HIS A CB    
1066 C  CG    . HIS A 139 ? 0.3161 0.5532 0.4299 -0.0378 0.0497  -0.0383 148 HIS A CG    
1067 N  ND1   . HIS A 139 ? 0.2726 0.5404 0.4058 -0.0289 0.0602  -0.0551 148 HIS A ND1   
1068 C  CD2   . HIS A 139 ? 0.2884 0.5296 0.4185 -0.0331 0.0411  -0.0363 148 HIS A CD2   
1069 C  CE1   . HIS A 139 ? 0.2812 0.5707 0.4441 -0.0180 0.0569  -0.0615 148 HIS A CE1   
1070 N  NE2   . HIS A 139 ? 0.3886 0.6631 0.5483 -0.0213 0.0451  -0.0494 148 HIS A NE2   
1071 N  N     . ASN A 140 ? 0.3446 0.5267 0.3668 -0.1030 0.0443  0.0070  149 ASN A N     
1072 C  CA    . ASN A 140 ? 0.3528 0.5074 0.3491 -0.1121 0.0365  0.0216  149 ASN A CA    
1073 C  C     . ASN A 140 ? 0.3062 0.4262 0.3032 -0.0919 0.0262  0.0226  149 ASN A C     
1074 O  O     . ASN A 140 ? 0.4301 0.5402 0.4140 -0.0883 0.0252  0.0233  149 ASN A O     
1075 C  CB    . ASN A 140 ? 0.3855 0.5628 0.3632 -0.1237 0.0475  0.0178  149 ASN A CB    
1076 C  CG    . ASN A 140 ? 0.4299 0.5864 0.3780 -0.1418 0.0376  0.0379  149 ASN A CG    
1077 O  OD1   . ASN A 140 ? 0.4057 0.5389 0.3487 -0.1533 0.0248  0.0566  149 ASN A OD1   
1078 N  ND2   . ASN A 140 ? 0.3586 0.5230 0.2881 -0.1446 0.0423  0.0341  149 ASN A ND2   
1079 N  N     . ILE A 141 ? 0.3551 0.4601 0.3671 -0.0802 0.0188  0.0216  150 ILE A N     
1080 C  CA    . ILE A 141 ? 0.3576 0.4347 0.3712 -0.0635 0.0102  0.0217  150 ILE A CA    
1081 C  C     . ILE A 141 ? 0.3010 0.3553 0.3198 -0.0654 -0.0016 0.0283  150 ILE A C     
1082 O  O     . ILE A 141 ? 0.3453 0.4066 0.3709 -0.0756 -0.0026 0.0294  150 ILE A O     
1083 C  CB    . ILE A 141 ? 0.2902 0.3755 0.3176 -0.0437 0.0150  0.0086  150 ILE A CB    
1084 C  CG1   . ILE A 141 ? 0.2696 0.3739 0.3148 -0.0417 0.0168  0.0025  150 ILE A CG1   
1085 C  CG2   . ILE A 141 ? 0.3162 0.4145 0.3400 -0.0390 0.0243  0.0002  150 ILE A CG2   
1086 C  CD1   . ILE A 141 ? 0.2416 0.3521 0.3004 -0.0231 0.0178  -0.0066 150 ILE A CD1   
1087 N  N     . PRO A 142 ? 0.3840 0.4126 0.4019 -0.0560 -0.0106 0.0306  151 PRO A N     
1088 C  CA    . PRO A 142 ? 0.3295 0.3364 0.3556 -0.0553 -0.0214 0.0319  151 PRO A CA    
1089 C  C     . PRO A 142 ? 0.3050 0.3216 0.3437 -0.0468 -0.0191 0.0200  151 PRO A C     
1090 O  O     . PRO A 142 ? 0.3161 0.3507 0.3582 -0.0371 -0.0119 0.0125  151 PRO A O     
1091 C  CB    . PRO A 142 ? 0.3033 0.2886 0.3291 -0.0442 -0.0290 0.0331  151 PRO A CB    
1092 C  CG    . PRO A 142 ? 0.3523 0.3443 0.3648 -0.0466 -0.0254 0.0389  151 PRO A CG    
1093 C  CD    . PRO A 142 ? 0.3584 0.3779 0.3686 -0.0477 -0.0118 0.0316  151 PRO A CD    
1094 N  N     . TYR A 143 ? 0.3501 0.3526 0.3957 -0.0512 -0.0272 0.0185  152 TYR A N     
1095 C  CA    . TYR A 143 ? 0.3419 0.3535 0.3970 -0.0471 -0.0274 0.0074  152 TYR A CA    
1096 C  C     . TYR A 143 ? 0.2928 0.2830 0.3528 -0.0387 -0.0351 -0.0010 152 TYR A C     
1097 O  O     . TYR A 143 ? 0.3778 0.3425 0.4405 -0.0421 -0.0438 0.0024  152 TYR A O     
1098 C  CB    . TYR A 143 ? 0.2665 0.2872 0.3269 -0.0640 -0.0289 0.0094  152 TYR A CB    
1099 C  CG    . TYR A 143 ? 0.3523 0.3815 0.4221 -0.0630 -0.0320 -0.0020 152 TYR A CG    
1100 C  CD1   . TYR A 143 ? 0.2525 0.3112 0.3273 -0.0564 -0.0268 -0.0079 152 TYR A CD1   
1101 C  CD2   . TYR A 143 ? 0.3311 0.3383 0.4053 -0.0690 -0.0416 -0.0071 152 TYR A CD2   
1102 C  CE1   . TYR A 143 ? 0.3702 0.4392 0.4514 -0.0570 -0.0314 -0.0169 152 TYR A CE1   
1103 C  CE2   . TYR A 143 ? 0.2971 0.3142 0.3777 -0.0700 -0.0446 -0.0193 152 TYR A CE2   
1104 C  CZ    . TYR A 143 ? 0.3921 0.4416 0.4746 -0.0646 -0.0396 -0.0233 152 TYR A CZ    
1105 O  OH    . TYR A 143 ? 0.3376 0.3996 0.4243 -0.0668 -0.0443 -0.0341 152 TYR A OH    
1106 N  N     . ILE A 144 ? 0.2600 0.2616 0.3218 -0.0281 -0.0324 -0.0123 153 ILE A N     
1107 C  CA    . ILE A 144 ? 0.3293 0.3186 0.3955 -0.0209 -0.0369 -0.0248 153 ILE A CA    
1108 C  C     . ILE A 144 ? 0.3844 0.3931 0.4495 -0.0194 -0.0352 -0.0359 153 ILE A C     
1109 O  O     . ILE A 144 ? 0.3187 0.3488 0.3793 -0.0166 -0.0304 -0.0325 153 ILE A O     
1110 C  CB    . ILE A 144 ? 0.3980 0.3815 0.4631 -0.0085 -0.0349 -0.0260 153 ILE A CB    
1111 C  CG1   . ILE A 144 ? 0.3223 0.2942 0.3970 -0.0016 -0.0394 -0.0413 153 ILE A CG1   
1112 C  CG2   . ILE A 144 ? 0.2426 0.2469 0.2998 -0.0015 -0.0266 -0.0252 153 ILE A CG2   
1113 C  CD1   . ILE A 144 ? 0.2790 0.2481 0.3580 0.0096  -0.0382 -0.0432 153 ILE A CD1   
1114 N  N     . GLU A 145 ? 0.3011 0.3020 0.3710 -0.0216 -0.0404 -0.0496 154 GLU A N     
1115 C  CA    . GLU A 145 ? 0.3240 0.3442 0.3899 -0.0224 -0.0403 -0.0614 154 GLU A CA    
1116 C  C     . GLU A 145 ? 0.3403 0.3648 0.4014 -0.0127 -0.0368 -0.0743 154 GLU A C     
1117 O  O     . GLU A 145 ? 0.3786 0.3862 0.4475 -0.0072 -0.0378 -0.0834 154 GLU A O     
1118 C  CB    . GLU A 145 ? 0.3100 0.3227 0.3827 -0.0341 -0.0477 -0.0713 154 GLU A CB    
1119 C  CG    . GLU A 145 ? 0.3285 0.3436 0.4060 -0.0471 -0.0501 -0.0585 154 GLU A CG    
1120 C  CD    . GLU A 145 ? 0.4420 0.4552 0.5260 -0.0613 -0.0575 -0.0676 154 GLU A CD    
1121 O  OE1   . GLU A 145 ? 0.6269 0.6276 0.7126 -0.0607 -0.0622 -0.0853 154 GLU A OE1   
1122 O  OE2   . GLU A 145 ? 0.4151 0.4411 0.5036 -0.0738 -0.0584 -0.0589 154 GLU A OE2   
1123 N  N     . THR A 146 ? 0.2804 0.3290 0.3298 -0.0111 -0.0332 -0.0745 155 THR A N     
1124 C  CA    . THR A 146 ? 0.3114 0.3705 0.3524 -0.0053 -0.0281 -0.0839 155 THR A CA    
1125 C  C     . THR A 146 ? 0.3889 0.4708 0.4171 -0.0115 -0.0293 -0.0942 155 THR A C     
1126 O  O     . THR A 146 ? 0.3559 0.4480 0.3817 -0.0185 -0.0350 -0.0902 155 THR A O     
1127 C  CB    . THR A 146 ? 0.3521 0.4179 0.3860 0.0007  -0.0225 -0.0691 155 THR A CB    
1128 O  OG1   . THR A 146 ? 0.3404 0.4195 0.3677 -0.0017 -0.0246 -0.0555 155 THR A OG1   
1129 C  CG2   . THR A 146 ? 0.2824 0.3289 0.3260 0.0057  -0.0214 -0.0603 155 THR A CG2   
1130 N  N     . SER A 147 ? 0.3619 0.4556 0.3820 -0.0098 -0.0239 -0.1077 156 SER A N     
1131 C  CA    . SER A 147 ? 0.3585 0.4793 0.3593 -0.0173 -0.0237 -0.1144 156 SER A CA    
1132 C  C     . SER A 147 ? 0.3748 0.5108 0.3641 -0.0153 -0.0147 -0.1158 156 SER A C     
1133 O  O     . SER A 147 ? 0.3460 0.4781 0.3457 -0.0095 -0.0081 -0.1310 156 SER A O     
1134 C  CB    . SER A 147 ? 0.3592 0.4835 0.3608 -0.0238 -0.0266 -0.1400 156 SER A CB    
1135 O  OG    . SER A 147 ? 0.3969 0.5513 0.3757 -0.0330 -0.0261 -0.1471 156 SER A OG    
1136 N  N     . ALA A 148 ? 0.3984 0.5522 0.3684 -0.0204 -0.0154 -0.0994 157 ALA A N     
1137 C  CA    . ALA A 148 ? 0.4632 0.6344 0.4185 -0.0234 -0.0073 -0.0977 157 ALA A CA    
1138 C  C     . ALA A 148 ? 0.4543 0.6551 0.3899 -0.0345 -0.0033 -0.1167 157 ALA A C     
1139 O  O     . ALA A 148 ? 0.4280 0.6485 0.3520 -0.0393 0.0060  -0.1204 157 ALA A O     
1140 C  CB    . ALA A 148 ? 0.3995 0.5715 0.3427 -0.0254 -0.0117 -0.0688 157 ALA A CB    
1141 N  N     . LYS A 149 ? 0.4736 0.6811 0.4044 -0.0405 -0.0096 -0.1293 158 LYS A N     
1142 C  CA    . LYS A 149 ? 0.4853 0.7229 0.3961 -0.0523 -0.0054 -0.1516 158 LYS A CA    
1143 C  C     . LYS A 149 ? 0.5769 0.8141 0.5052 -0.0460 0.0056  -0.1857 158 LYS A C     
1144 O  O     . LYS A 149 ? 0.5576 0.7664 0.5140 -0.0343 0.0037  -0.1943 158 LYS A O     
1145 C  CB    . LYS A 149 ? 0.4909 0.7353 0.3924 -0.0613 -0.0172 -0.1556 158 LYS A CB    
1146 C  CG    . LYS A 149 ? 0.5999 0.8783 0.4758 -0.0762 -0.0144 -0.1789 158 LYS A CG    
1147 C  CD    . LYS A 149 ? 0.5968 0.8779 0.4698 -0.0841 -0.0270 -0.1870 158 LYS A CD    
1148 C  CE    . LYS A 149 ? 0.5571 0.8697 0.4048 -0.0993 -0.0244 -0.2050 158 LYS A CE    
1149 N  NZ    . LYS A 149 ? 0.6705 1.0083 0.4875 -0.1108 -0.0273 -0.1775 158 LYS A NZ    
1150 N  N     . ASP A 150 ? 0.5683 0.8383 0.4810 -0.0539 0.0167  -0.2049 159 ASP A N     
1151 C  CA    . ASP A 150 ? 0.6488 0.9238 0.5821 -0.0463 0.0276  -0.2420 159 ASP A CA    
1152 C  C     . ASP A 150 ? 0.6543 0.9180 0.5982 -0.0462 0.0214  -0.2681 159 ASP A C     
1153 O  O     . ASP A 150 ? 0.7096 0.9875 0.6324 -0.0593 0.0162  -0.2669 159 ASP A O     
1154 C  CB    . ASP A 150 ? 0.6142 0.9289 0.5344 -0.0558 0.0417  -0.2511 159 ASP A CB    
1155 C  CG    . ASP A 150 ? 0.7055 1.0304 0.6226 -0.0554 0.0499  -0.2335 159 ASP A CG    
1156 O  OD1   . ASP A 150 ? 0.6726 0.9720 0.6136 -0.0409 0.0487  -0.2265 159 ASP A OD1   
1157 O  OD2   . ASP A 150 ? 0.7252 1.0797 0.6195 -0.0705 0.0560  -0.2219 159 ASP A OD2   
1158 N  N     . PRO A 151 ? 0.6523 0.8869 0.6314 -0.0317 0.0201  -0.2867 160 PRO A N     
1159 C  CA    . PRO A 151 ? 0.5506 0.7642 0.5600 -0.0147 0.0229  -0.2867 160 PRO A CA    
1160 C  C     . PRO A 151 ? 0.5711 0.7510 0.5877 -0.0095 0.0126  -0.2495 160 PRO A C     
1161 O  O     . PRO A 151 ? 0.5747 0.7302 0.5944 -0.0117 0.0013  -0.2406 160 PRO A O     
1162 C  CB    . PRO A 151 ? 0.5656 0.7572 0.6092 -0.0041 0.0200  -0.3130 160 PRO A CB    
1163 C  CG    . PRO A 151 ? 0.5518 0.7332 0.5845 -0.0147 0.0104  -0.3183 160 PRO A CG    
1164 C  CD    . PRO A 151 ? 0.6276 0.8468 0.6202 -0.0322 0.0139  -0.3079 160 PRO A CD    
1165 N  N     . PRO A 152 ? 0.4843 0.6645 0.5038 -0.0039 0.0170  -0.2291 161 PRO A N     
1166 C  CA    . PRO A 152 ? 0.4930 0.6468 0.5150 -0.0008 0.0088  -0.1955 161 PRO A CA    
1167 C  C     . PRO A 152 ? 0.4628 0.5781 0.5128 0.0093  -0.0002 -0.1960 161 PRO A C     
1168 O  O     . PRO A 152 ? 0.4964 0.6009 0.5706 0.0189  -0.0003 -0.2176 161 PRO A O     
1169 C  CB    . PRO A 152 ? 0.4860 0.6517 0.5057 0.0021  0.0168  -0.1809 161 PRO A CB    
1170 C  CG    . PRO A 152 ? 0.4369 0.6245 0.4699 0.0067  0.0276  -0.2104 161 PRO A CG    
1171 C  CD    . PRO A 152 ? 0.5348 0.7420 0.5569 -0.0011 0.0301  -0.2380 161 PRO A CD    
1172 N  N     . LEU A 153 ? 0.3693 0.4645 0.4166 0.0067  -0.0086 -0.1713 162 LEU A N     
1173 C  CA    . LEU A 153 ? 0.3763 0.4363 0.4439 0.0109  -0.0181 -0.1662 162 LEU A CA    
1174 C  C     . LEU A 153 ? 0.4582 0.5060 0.5268 0.0143  -0.0193 -0.1383 162 LEU A C     
1175 O  O     . LEU A 153 ? 0.3185 0.3747 0.3721 0.0089  -0.0188 -0.1190 162 LEU A O     
1176 C  CB    . LEU A 153 ? 0.4197 0.4712 0.4830 0.0004  -0.0265 -0.1665 162 LEU A CB    
1177 C  CG    . LEU A 153 ? 0.5159 0.5323 0.5986 -0.0009 -0.0372 -0.1678 162 LEU A CG    
1178 C  CD1   . LEU A 153 ? 0.4914 0.4990 0.5698 -0.0087 -0.0423 -0.1406 162 LEU A CD1   
1179 C  CD2   . LEU A 153 ? 0.4458 0.4367 0.5526 0.0115  -0.0402 -0.1743 162 LEU A CD2   
1180 N  N     . ASN A 154 ? 0.3100 0.3394 0.3975 0.0236  -0.0217 -0.1375 163 ASN A N     
1181 C  CA    . ASN A 154 ? 0.3745 0.3896 0.4636 0.0256  -0.0246 -0.1135 163 ASN A CA    
1182 C  C     . ASN A 154 ? 0.2841 0.3190 0.3576 0.0250  -0.0165 -0.0992 163 ASN A C     
1183 O  O     . ASN A 154 ? 0.3230 0.3499 0.3925 0.0239  -0.0179 -0.0800 163 ASN A O     
1184 C  CB    . ASN A 154 ? 0.3523 0.3487 0.4387 0.0171  -0.0323 -0.0980 163 ASN A CB    
1185 C  CG    . ASN A 154 ? 0.4323 0.3998 0.5360 0.0162  -0.0430 -0.1054 163 ASN A CG    
1186 O  OD1   . ASN A 154 ? 0.4106 0.3645 0.5329 0.0257  -0.0472 -0.1165 163 ASN A OD1   
1187 N  ND2   . ASN A 154 ? 0.3069 0.2649 0.4073 0.0046  -0.0485 -0.0992 163 ASN A ND2   
1188 N  N     . VAL A 155 ? 0.2872 0.3479 0.3513 0.0242  -0.0082 -0.1085 164 VAL A N     
1189 C  CA    . VAL A 155 ? 0.3210 0.3960 0.3709 0.0220  -0.0023 -0.0933 164 VAL A CA    
1190 C  C     . VAL A 155 ? 0.3529 0.4212 0.4148 0.0286  -0.0012 -0.0874 164 VAL A C     
1191 O  O     . VAL A 155 ? 0.3191 0.3797 0.3758 0.0277  -0.0022 -0.0696 164 VAL A O     
1192 C  CB    . VAL A 155 ? 0.3505 0.4551 0.3851 0.0160  0.0055  -0.1023 164 VAL A CB    
1193 C  CG1   . VAL A 155 ? 0.3661 0.4808 0.3883 0.0124  0.0103  -0.0853 164 VAL A CG1   
1194 C  CG2   . VAL A 155 ? 0.2764 0.3891 0.2953 0.0077  0.0021  -0.1039 164 VAL A CG2   
1195 N  N     . ASP A 156 ? 0.3609 0.4342 0.4411 0.0357  0.0003  -0.1041 165 ASP A N     
1196 C  CA    . ASP A 156 ? 0.2959 0.3645 0.3911 0.0424  -0.0012 -0.0990 165 ASP A CA    
1197 C  C     . ASP A 156 ? 0.3735 0.4130 0.4734 0.0440  -0.0119 -0.0831 165 ASP A C     
1198 O  O     . ASP A 156 ? 0.2968 0.3324 0.3937 0.0434  -0.0130 -0.0684 165 ASP A O     
1199 C  CB    . ASP A 156 ? 0.3338 0.4133 0.4547 0.0522  0.0000  -0.1220 165 ASP A CB    
1200 C  CG    . ASP A 156 ? 0.3342 0.4510 0.4518 0.0489  0.0131  -0.1342 165 ASP A CG    
1201 O  OD1   . ASP A 156 ? 0.3649 0.4964 0.4568 0.0376  0.0201  -0.1263 165 ASP A OD1   
1202 O  OD2   . ASP A 156 ? 0.4537 0.5863 0.5955 0.0572  0.0159  -0.1512 165 ASP A OD2   
1203 N  N     . LYS A 157 ? 0.3435 0.3631 0.4489 0.0439  -0.0198 -0.0858 166 LYS A N     
1204 C  CA    . LYS A 157 ? 0.3173 0.3107 0.4257 0.0422  -0.0302 -0.0699 166 LYS A CA    
1205 C  C     . LYS A 157 ? 0.3166 0.3113 0.4047 0.0338  -0.0271 -0.0507 166 LYS A C     
1206 O  O     . LYS A 157 ? 0.3486 0.3338 0.4350 0.0322  -0.0311 -0.0369 166 LYS A O     
1207 C  CB    . LYS A 157 ? 0.3400 0.3122 0.4565 0.0399  -0.0390 -0.0756 166 LYS A CB    
1208 C  CG    . LYS A 157 ? 0.3589 0.3029 0.4800 0.0363  -0.0516 -0.0587 166 LYS A CG    
1209 C  CD    . LYS A 157 ? 0.4541 0.3734 0.5857 0.0327  -0.0618 -0.0645 166 LYS A CD    
1210 C  CE    . LYS A 157 ? 0.4453 0.3338 0.5851 0.0296  -0.0773 -0.0473 166 LYS A CE    
1211 N  NZ    . LYS A 157 ? 0.4825 0.3733 0.6008 0.0170  -0.0759 -0.0231 166 LYS A NZ    
1212 N  N     . ALA A 158 ? 0.2635 0.2715 0.3373 0.0287  -0.0206 -0.0505 167 ALA A N     
1213 C  CA    . ALA A 158 ? 0.3147 0.3252 0.3749 0.0233  -0.0179 -0.0357 167 ALA A CA    
1214 C  C     . ALA A 158 ? 0.2984 0.3126 0.3549 0.0255  -0.0143 -0.0279 167 ALA A C     
1215 O  O     . ALA A 158 ? 0.3341 0.3410 0.3866 0.0228  -0.0157 -0.0174 167 ALA A O     
1216 C  CB    . ALA A 158 ? 0.2424 0.2680 0.2922 0.0200  -0.0138 -0.0373 167 ALA A CB    
1217 N  N     . PHE A 159 ? 0.2963 0.3237 0.3534 0.0284  -0.0094 -0.0339 168 PHE A N     
1218 C  CA    . PHE A 159 ? 0.2372 0.2680 0.2915 0.0284  -0.0065 -0.0271 168 PHE A CA    
1219 C  C     . PHE A 159 ? 0.3208 0.3429 0.3863 0.0314  -0.0125 -0.0252 168 PHE A C     
1220 O  O     . PHE A 159 ? 0.2986 0.3157 0.3586 0.0287  -0.0137 -0.0159 168 PHE A O     
1221 C  CB    . PHE A 159 ? 0.2582 0.3077 0.3103 0.0274  0.0002  -0.0329 168 PHE A CB    
1222 C  CG    . PHE A 159 ? 0.3301 0.3868 0.3667 0.0222  0.0036  -0.0278 168 PHE A CG    
1223 C  CD1   . PHE A 159 ? 0.2393 0.2909 0.2669 0.0192  0.0042  -0.0155 168 PHE A CD1   
1224 C  CD2   . PHE A 159 ? 0.3225 0.3902 0.3543 0.0203  0.0047  -0.0356 168 PHE A CD2   
1225 C  CE1   . PHE A 159 ? 0.2437 0.2991 0.2599 0.0156  0.0040  -0.0086 168 PHE A CE1   
1226 C  CE2   . PHE A 159 ? 0.3161 0.3910 0.3330 0.0149  0.0049  -0.0282 168 PHE A CE2   
1227 C  CZ    . PHE A 159 ? 0.2509 0.3187 0.2611 0.0132  0.0037  -0.0134 168 PHE A CZ    
1228 N  N     . HIS A 160 ? 0.2657 0.2856 0.3479 0.0372  -0.0176 -0.0347 169 HIS A N     
1229 C  CA    . HIS A 160 ? 0.2566 0.2676 0.3525 0.0413  -0.0269 -0.0312 169 HIS A CA    
1230 C  C     . HIS A 160 ? 0.2944 0.2858 0.3815 0.0354  -0.0349 -0.0165 169 HIS A C     
1231 O  O     . HIS A 160 ? 0.3258 0.3139 0.4099 0.0329  -0.0400 -0.0066 169 HIS A O     
1232 C  CB    . HIS A 160 ? 0.2944 0.3047 0.4148 0.0509  -0.0325 -0.0457 169 HIS A CB    
1233 C  CG    . HIS A 160 ? 0.3576 0.3943 0.4895 0.0559  -0.0238 -0.0620 169 HIS A CG    
1234 N  ND1   . HIS A 160 ? 0.3903 0.4343 0.5500 0.0668  -0.0269 -0.0795 169 HIS A ND1   
1235 C  CD2   . HIS A 160 ? 0.2623 0.3213 0.3823 0.0504  -0.0119 -0.0637 169 HIS A CD2   
1236 C  CE1   . HIS A 160 ? 0.4524 0.5270 0.6161 0.0669  -0.0153 -0.0927 169 HIS A CE1   
1237 N  NE2   . HIS A 160 ? 0.3598 0.4428 0.4978 0.0557  -0.0065 -0.0817 169 HIS A NE2   
1238 N  N     . ASP A 161 ? 0.2565 0.2373 0.3383 0.0311  -0.0362 -0.0151 170 ASP A N     
1239 C  CA    . ASP A 161 ? 0.3570 0.3239 0.4288 0.0220  -0.0421 -0.0008 170 ASP A CA    
1240 C  C     . ASP A 161 ? 0.2702 0.2465 0.3244 0.0156  -0.0349 0.0071  170 ASP A C     
1241 O  O     . ASP A 161 ? 0.3664 0.3377 0.4119 0.0084  -0.0394 0.0180  170 ASP A O     
1242 C  CB    . ASP A 161 ? 0.3444 0.3030 0.4147 0.0163  -0.0432 -0.0017 170 ASP A CB    
1243 C  CG    . ASP A 161 ? 0.4147 0.3540 0.5024 0.0197  -0.0547 -0.0066 170 ASP A CG    
1244 O  OD1   . ASP A 161 ? 0.3979 0.3306 0.5008 0.0283  -0.0626 -0.0088 170 ASP A OD1   
1245 O  OD2   . ASP A 161 ? 0.4074 0.3379 0.4960 0.0142  -0.0568 -0.0092 170 ASP A OD2   
1246 N  N     . LEU A 162 ? 0.2747 0.2644 0.3235 0.0175  -0.0247 0.0016  171 LEU A N     
1247 C  CA    . LEU A 162 ? 0.2823 0.2782 0.3189 0.0136  -0.0186 0.0059  171 LEU A CA    
1248 C  C     . LEU A 162 ? 0.3018 0.2976 0.3371 0.0130  -0.0217 0.0092  171 LEU A C     
1249 O  O     . LEU A 162 ? 0.3587 0.3538 0.3830 0.0063  -0.0220 0.0147  171 LEU A O     
1250 C  CB    . LEU A 162 ? 0.2556 0.2612 0.2902 0.0170  -0.0106 0.0009  171 LEU A CB    
1251 C  CG    . LEU A 162 ? 0.3438 0.3520 0.3705 0.0152  -0.0052 0.0028  171 LEU A CG    
1252 C  CD1   . LEU A 162 ? 0.2480 0.2577 0.2697 0.0099  -0.0036 0.0049  171 LEU A CD1   
1253 C  CD2   . LEU A 162 ? 0.2414 0.2542 0.2683 0.0190  -0.0012 0.0010  171 LEU A CD2   
1254 N  N     . VAL A 163 ? 0.3049 0.3047 0.3516 0.0190  -0.0238 0.0046  172 VAL A N     
1255 C  CA    . VAL A 163 ? 0.3063 0.3088 0.3555 0.0182  -0.0288 0.0074  172 VAL A CA    
1256 C  C     . VAL A 163 ? 0.2820 0.2742 0.3298 0.0143  -0.0409 0.0172  172 VAL A C     
1257 O  O     . VAL A 163 ? 0.3271 0.3207 0.3651 0.0079  -0.0447 0.0236  172 VAL A O     
1258 C  CB    . VAL A 163 ? 0.2758 0.2898 0.3426 0.0252  -0.0288 -0.0008 172 VAL A CB    
1259 C  CG1   . VAL A 163 ? 0.2487 0.2688 0.3221 0.0243  -0.0358 0.0021  172 VAL A CG1   
1260 C  CG2   . VAL A 163 ? 0.2760 0.3008 0.3387 0.0245  -0.0175 -0.0067 172 VAL A CG2   
1261 N  N     . ARG A 164 ? 0.3033 0.2842 0.3597 0.0166  -0.0482 0.0192  173 ARG A N     
1262 C  CA    . ARG A 164 ? 0.3091 0.2761 0.3630 0.0108  -0.0621 0.0325  173 ARG A CA    
1263 C  C     . ARG A 164 ? 0.3551 0.3228 0.3839 -0.0036 -0.0587 0.0423  173 ARG A C     
1264 O  O     . ARG A 164 ? 0.4028 0.3688 0.4204 -0.0123 -0.0673 0.0538  173 ARG A O     
1265 C  CB    . ARG A 164 ? 0.3283 0.2783 0.3963 0.0145  -0.0706 0.0325  173 ARG A CB    
1266 C  CG    . ARG A 164 ? 0.4287 0.3786 0.5251 0.0294  -0.0760 0.0204  173 ARG A CG    
1267 C  CD    . ARG A 164 ? 0.3209 0.2490 0.4327 0.0330  -0.0864 0.0188  173 ARG A CD    
1268 N  NE    . ARG A 164 ? 0.4255 0.3559 0.5683 0.0490  -0.0912 0.0030  173 ARG A NE    
1269 C  CZ    . ARG A 164 ? 0.4197 0.3605 0.5737 0.0566  -0.0811 -0.0175 173 ARG A CZ    
1270 N  NH1   . ARG A 164 ? 0.3818 0.3289 0.5186 0.0500  -0.0683 -0.0224 173 ARG A NH1   
1271 N  NH2   . ARG A 164 ? 0.3903 0.3384 0.5741 0.0710  -0.0843 -0.0343 173 ARG A NH2   
1272 N  N     . VAL A 165 ? 0.3483 0.3216 0.3686 -0.0069 -0.0464 0.0372  174 VAL A N     
1273 C  CA    . VAL A 165 ? 0.3151 0.2958 0.3154 -0.0196 -0.0402 0.0418  174 VAL A CA    
1274 C  C     . VAL A 165 ? 0.3474 0.3386 0.3367 -0.0221 -0.0363 0.0389  174 VAL A C     
1275 O  O     . VAL A 165 ? 0.3847 0.3803 0.3568 -0.0341 -0.0387 0.0456  174 VAL A O     
1276 C  CB    . VAL A 165 ? 0.3331 0.3219 0.3337 -0.0193 -0.0282 0.0340  174 VAL A CB    
1277 C  CG1   . VAL A 165 ? 0.3631 0.3661 0.3480 -0.0305 -0.0195 0.0339  174 VAL A CG1   
1278 C  CG2   . VAL A 165 ? 0.3793 0.3583 0.3886 -0.0206 -0.0332 0.0367  174 VAL A CG2   
1279 N  N     . ILE A 166 ? 0.3271 0.3227 0.3246 -0.0127 -0.0305 0.0288  175 ILE A N     
1280 C  CA    . ILE A 166 ? 0.3051 0.3077 0.2944 -0.0156 -0.0277 0.0246  175 ILE A CA    
1281 C  C     . ILE A 166 ? 0.4341 0.4363 0.4190 -0.0213 -0.0406 0.0335  175 ILE A C     
1282 O  O     . ILE A 166 ? 0.4055 0.4142 0.3738 -0.0312 -0.0409 0.0341  175 ILE A O     
1283 C  CB    . ILE A 166 ? 0.3106 0.3149 0.3114 -0.0066 -0.0219 0.0155  175 ILE A CB    
1284 C  CG1   . ILE A 166 ? 0.3567 0.3613 0.3598 -0.0019 -0.0118 0.0094  175 ILE A CG1   
1285 C  CG2   . ILE A 166 ? 0.3529 0.3611 0.3473 -0.0111 -0.0210 0.0113  175 ILE A CG2   
1286 C  CD1   . ILE A 166 ? 0.3339 0.3386 0.3459 0.0046  -0.0081 0.0047  175 ILE A CD1   
1287 N  N     . ARG A 167 ? 0.3732 0.3688 0.3741 -0.0149 -0.0524 0.0396  176 ARG A N     
1288 C  CA    . ARG A 167 ? 0.4475 0.4431 0.4495 -0.0180 -0.0682 0.0494  176 ARG A CA    
1289 C  C     . ARG A 167 ? 0.4532 0.4435 0.4347 -0.0322 -0.0774 0.0648  176 ARG A C     
1290 O  O     . ARG A 167 ? 0.5234 0.5190 0.4923 -0.0414 -0.0873 0.0731  176 ARG A O     
1291 C  CB    . ARG A 167 ? 0.3670 0.3576 0.3975 -0.0049 -0.0789 0.0497  176 ARG A CB    
1292 C  CG    . ARG A 167 ? 0.3783 0.3819 0.4277 0.0052  -0.0719 0.0361  176 ARG A CG    
1293 C  CD    . ARG A 167 ? 0.3096 0.3125 0.3892 0.0188  -0.0797 0.0318  176 ARG A CD    
1294 N  NE    . ARG A 167 ? 0.3646 0.3865 0.4625 0.0259  -0.0726 0.0188  176 ARG A NE    
1295 C  CZ    . ARG A 167 ? 0.4087 0.4385 0.5347 0.0380  -0.0740 0.0086  176 ARG A CZ    
1296 N  NH1   . ARG A 167 ? 0.2850 0.3010 0.4261 0.0465  -0.0832 0.0085  176 ARG A NH1   
1297 N  NH2   . ARG A 167 ? 0.3627 0.4156 0.5026 0.0407  -0.0658 -0.0028 176 ARG A NH2   
1298 N  N     . GLN A 168 ? 0.4987 0.4803 0.4754 -0.0364 -0.0749 0.0697  177 GLN A N     
1299 C  CA    . GLN A 168 ? 0.5595 0.5367 0.5156 -0.0532 -0.0831 0.0865  177 GLN A CA    
1300 C  C     . GLN A 168 ? 0.6341 0.6286 0.5638 -0.0679 -0.0679 0.0815  177 GLN A C     
1301 O  O     . GLN A 168 ? 0.6760 0.6727 0.5856 -0.0852 -0.0705 0.0938  177 GLN A O     
1302 C  CB    . GLN A 168 ? 0.5457 0.5043 0.5125 -0.0525 -0.0895 0.0949  177 GLN A CB    
1303 C  CG    . GLN A 168 ? 0.6122 0.5532 0.6084 -0.0369 -0.1051 0.0967  177 GLN A CG    
1304 C  CD    . GLN A 168 ? 0.7185 0.6433 0.7312 -0.0309 -0.1044 0.0926  177 GLN A CD    
1305 O  OE1   . GLN A 168 ? 0.6717 0.6019 0.6762 -0.0363 -0.0908 0.0868  177 GLN A OE1   
1306 N  NE2   . GLN A 168 ? 0.7022 0.6087 0.7407 -0.0191 -0.1197 0.0939  177 GLN A NE2   
1307 N  N     . GLN A 169 ? 0.6182 0.6253 0.5486 -0.0621 -0.0527 0.0634  178 GLN A N     
1308 C  CA    . GLN A 169 ? 0.6460 0.6704 0.5594 -0.0713 -0.0366 0.0524  178 GLN A CA    
1309 C  C     . GLN A 169 ? 0.8220 0.8599 0.7062 -0.0908 -0.0396 0.0582  178 GLN A C     
1310 O  O     . GLN A 169 ? 0.7327 0.7862 0.5991 -0.1050 -0.0301 0.0564  178 GLN A O     
1311 C  CB    . GLN A 169 ? 0.6364 0.6652 0.5606 -0.0590 -0.0244 0.0327  178 GLN A CB    
1312 C  CG    . GLN A 169 ? 0.6762 0.7210 0.5910 -0.0635 -0.0083 0.0166  178 GLN A CG    
1313 C  CD    . GLN A 169 ? 0.6113 0.6524 0.5402 -0.0502 -0.0006 0.0002  178 GLN A CD    
1314 O  OE1   . GLN A 169 ? 0.5437 0.5728 0.4862 -0.0404 -0.0063 0.0023  178 GLN A OE1   
1315 N  NE2   . GLN A 169 ? 0.6648 0.7165 0.5919 -0.0503 0.0121  -0.0165 178 GLN A NE2   
1316 O  OXT   . GLN A 169 ? 0.7743 0.8111 0.6519 -0.0938 -0.0517 0.0643  178 GLN A OXT   
1317 P  PG    . GNP B .   ? 0.4107 0.4929 0.3943 0.0152  -0.1182 0.1276  201 GNP A PG    
1318 O  O1G   . GNP B .   ? 0.4166 0.5040 0.3979 0.0143  -0.1428 0.1507  201 GNP A O1G   
1319 O  O2G   . GNP B .   ? 0.4496 0.5167 0.4111 0.0031  -0.1084 0.1329  201 GNP A O2G   
1320 O  O3G   . GNP B .   ? 0.4396 0.5134 0.4586 0.0333  -0.1115 0.1121  201 GNP A O3G   
1321 N  N3B   . GNP B .   ? 0.3513 0.4665 0.3187 0.0044  -0.1073 0.1071  201 GNP A N3B   
1322 P  PB    . GNP B .   ? 0.3769 0.4924 0.3415 0.0016  -0.0841 0.0825  201 GNP A PB    
1323 O  O1B   . GNP B .   ? 0.3663 0.4791 0.3579 0.0136  -0.0768 0.0664  201 GNP A O1B   
1324 O  O2B   . GNP B .   ? 0.4082 0.5108 0.3567 -0.0060 -0.0752 0.0872  201 GNP A O2B   
1325 O  O3A   . GNP B .   ? 0.3925 0.5369 0.3362 -0.0116 -0.0829 0.0706  201 GNP A O3A   
1326 P  PA    . GNP B .   ? 0.3997 0.5607 0.3076 -0.0303 -0.0791 0.0711  201 GNP A PA    
1327 O  O1A   . GNP B .   ? 0.4931 0.6519 0.3981 -0.0328 -0.0600 0.0532  201 GNP A O1A   
1328 O  O2A   . GNP B .   ? 0.3839 0.5441 0.2733 -0.0387 -0.0937 0.0985  201 GNP A O2A   
1329 O  "O5'" . GNP B .   ? 0.4815 0.6685 0.3847 -0.0358 -0.0827 0.0549  201 GNP A "O5'" 
1330 C  "C5'" . GNP B .   ? 0.4325 0.6332 0.3357 -0.0370 -0.1009 0.0663  201 GNP A "C5'" 
1331 C  "C4'" . GNP B .   ? 0.4132 0.6428 0.2926 -0.0523 -0.1023 0.0531  201 GNP A "C4'" 
1332 O  "O4'" . GNP B .   ? 0.4231 0.6552 0.3159 -0.0500 -0.0917 0.0253  201 GNP A "O4'" 
1333 C  "C3'" . GNP B .   ? 0.4107 0.6549 0.2539 -0.0697 -0.0943 0.0509  201 GNP A "C3'" 
1334 O  "O3'" . GNP B .   ? 0.4949 0.7678 0.3126 -0.0847 -0.1056 0.0521  201 GNP A "O3'" 
1335 C  "C2'" . GNP B .   ? 0.4128 0.6556 0.2632 -0.0678 -0.0736 0.0198  201 GNP A "C2'" 
1336 O  "O2'" . GNP B .   ? 0.4996 0.7671 0.3220 -0.0835 -0.0647 0.0047  201 GNP A "O2'" 
1337 C  "C1'" . GNP B .   ? 0.4144 0.6551 0.2888 -0.0596 -0.0775 0.0048  201 GNP A "C1'" 
1338 N  N9    . GNP B .   ? 0.3904 0.6133 0.2871 -0.0501 -0.0636 -0.0152 201 GNP A N9    
1339 C  C8    . GNP B .   ? 0.3258 0.5250 0.2396 -0.0388 -0.0551 -0.0108 201 GNP A C8    
1340 N  N7    . GNP B .   ? 0.3775 0.5650 0.3078 -0.0333 -0.0460 -0.0295 201 GNP A N7    
1341 C  C5    . GNP B .   ? 0.3772 0.5784 0.3031 -0.0408 -0.0481 -0.0482 201 GNP A C5    
1342 C  C6    . GNP B .   ? 0.3427 0.5355 0.2823 -0.0399 -0.0432 -0.0721 201 GNP A C6    
1343 O  O6    . GNP B .   ? 0.3919 0.5637 0.3498 -0.0321 -0.0367 -0.0791 201 GNP A O6    
1344 N  N1    . GNP B .   ? 0.3388 0.5499 0.2678 -0.0507 -0.0487 -0.0876 201 GNP A N1    
1345 C  C2    . GNP B .   ? 0.4059 0.6430 0.3122 -0.0615 -0.0579 -0.0805 201 GNP A C2    
1346 N  N2    . GNP B .   ? 0.3999 0.6534 0.2974 -0.0724 -0.0625 -0.0996 201 GNP A N2    
1347 N  N3    . GNP B .   ? 0.4079 0.6530 0.3007 -0.0624 -0.0637 -0.0557 201 GNP A N3    
1348 C  C4    . GNP B .   ? 0.3748 0.5998 0.2791 -0.0516 -0.0584 -0.0410 201 GNP A C4    
1349 MG MG    . MG  C .   ? 0.3612 0.4380 0.2977 -0.0126 -0.0843 0.1166  202 MG  A MG    
1350 ZN ZN    . ZN  D .   ? 0.5903 0.7461 0.6025 -0.1803 -0.1297 -0.2825 203 ZN  A ZN    
1351 ZN ZN    . ZN  E .   ? 0.3541 0.6213 0.4783 -0.0199 0.0735  -0.0729 204 ZN  A ZN    
1352 O  O     . HOH F .   ? 0.7679 0.6663 0.8244 0.0464  -0.0897 0.1112  301 HOH A O     
1353 O  O     . HOH F .   ? 0.5596 0.9285 0.5162 -0.1028 0.1567  -0.2062 302 HOH A O     
1354 O  O     . HOH F .   ? 0.3853 0.5822 0.7848 0.1255  -0.1059 -0.0844 303 HOH A O     
1355 O  O     . HOH F .   ? 0.4279 0.7899 0.8401 0.1428  -0.1058 -0.0214 304 HOH A O     
1356 O  O     . HOH F .   ? 0.4924 0.8768 0.7293 -0.0975 -0.0720 -0.0469 305 HOH A O     
1357 O  O     . HOH F .   ? 0.4491 0.6408 0.5301 0.0247  0.0406  -0.1373 306 HOH A O     
1358 O  O     . HOH F .   ? 0.3340 0.5778 0.5219 0.0688  -0.1260 0.0439  307 HOH A O     
1359 O  O     . HOH F .   ? 0.6061 0.6788 0.5012 -0.0566 -0.0382 0.1123  308 HOH A O     
1360 O  O     . HOH F .   ? 0.4049 0.4541 0.3721 0.0038  -0.0712 0.1017  309 HOH A O     
1361 O  O     . HOH F .   ? 0.6855 1.0855 0.5593 -0.0916 0.0720  -0.1989 310 HOH A O     
1362 O  O     . HOH F .   ? 0.5907 0.5463 0.5586 -0.0625 -0.0679 0.0879  311 HOH A O     
1363 O  O     . HOH F .   ? 0.3054 0.4322 0.4065 -0.0686 -0.0461 -0.0379 312 HOH A O     
1364 O  O     . HOH F .   ? 0.5048 0.3876 0.6257 0.0238  -0.0927 0.0086  313 HOH A O     
1365 O  O     . HOH F .   ? 0.4644 0.3906 0.4791 -0.0147 -0.0011 -0.0237 314 HOH A O     
1366 O  O     . HOH F .   ? 0.3330 0.5723 0.3507 -0.0148 -0.1128 0.0188  315 HOH A O     
1367 O  O     . HOH F .   ? 0.4776 0.4655 0.5751 -0.0866 -0.0774 -0.1085 316 HOH A O     
1368 O  O     . HOH F .   ? 0.4730 0.7072 0.3561 -0.0571 0.0089  -0.0535 317 HOH A O     
1369 O  O     . HOH F .   ? 0.4088 0.4112 0.3624 -0.0322 -0.0260 0.0941  318 HOH A O     
1370 O  O     . HOH F .   ? 0.5118 0.6768 0.4968 -0.0334 -0.0147 -0.2110 319 HOH A O     
1371 O  O     . HOH F .   ? 0.3736 0.4494 0.4983 0.0230  -0.0625 0.0013  320 HOH A O     
1372 O  O     . HOH F .   ? 0.3724 0.6478 0.4109 -0.0361 0.0707  -0.0811 321 HOH A O     
1373 O  O     . HOH F .   ? 0.6206 0.5797 0.7472 0.0316  -0.1483 0.0697  322 HOH A O     
1374 O  O     . HOH F .   ? 0.3993 0.3424 0.4593 -0.0099 -0.0480 0.0103  323 HOH A O     
1375 O  O     . HOH F .   ? 0.5388 0.5812 0.5388 -0.0017 0.0589  -0.1435 324 HOH A O     
1376 O  O     . HOH F .   ? 0.3094 0.4655 0.5322 0.0402  -0.0870 -0.0161 325 HOH A O     
1377 O  O     . HOH F .   ? 0.5037 0.3792 0.5261 -0.0065 -0.0304 0.0581  326 HOH A O     
1378 O  O     . HOH F .   ? 0.3151 0.5346 0.3132 -0.0812 0.0775  -0.0421 327 HOH A O     
1379 O  O     . HOH F .   ? 0.5451 0.8114 0.4402 -0.0969 -0.0574 -0.2012 328 HOH A O     
1380 O  O     . HOH F .   ? 0.3878 0.6091 0.4509 0.0173  -0.1206 0.0473  329 HOH A O     
1381 O  O     . HOH F .   ? 0.7470 0.8199 0.6706 -0.0173 -0.1620 0.1984  330 HOH A O     
1382 O  O     . HOH F .   ? 0.4959 0.5249 0.5169 -0.1091 -0.0206 0.0513  331 HOH A O     
1383 O  O     . HOH F .   ? 0.3613 0.3642 0.6196 0.1043  -0.0845 -0.0734 332 HOH A O     
1384 O  O     . HOH F .   ? 0.5214 0.5736 0.4837 -0.0966 -0.0029 0.0540  333 HOH A O     
1385 O  O     . HOH F .   ? 0.4595 0.4868 0.4766 -0.0158 -0.0608 0.0269  334 HOH A O     
1386 O  O     . HOH F .   ? 0.6243 0.5436 0.7013 -0.0635 -0.0647 0.0038  335 HOH A O     
1387 O  O     . HOH F .   ? 0.4174 0.3698 0.4584 -0.0731 -0.0485 0.0410  336 HOH A O     
1388 O  O     . HOH F .   ? 0.4708 0.6817 0.6105 0.0641  -0.1522 0.0807  337 HOH A O     
1389 O  O     . HOH F .   ? 0.4095 0.3532 0.4994 -0.0298 -0.0576 -0.0548 338 HOH A O     
1390 O  O     . HOH F .   ? 0.4530 0.5991 0.6321 0.0978  -0.1370 0.0775  339 HOH A O     
1391 O  O     . HOH F .   ? 0.5983 0.6190 0.5680 0.0071  -0.1438 0.1809  340 HOH A O     
1392 O  O     . HOH F .   ? 0.4405 0.4907 0.3623 -0.0240 -0.0924 0.1451  341 HOH A O     
1393 O  O     . HOH F .   ? 0.6382 0.5573 0.6618 -0.0317 -0.0797 0.0710  342 HOH A O     
1394 O  O     . HOH F .   ? 0.3675 0.2874 0.3752 -0.0435 -0.0113 0.0476  343 HOH A O     
1395 O  O     . HOH F .   ? 0.3333 0.3457 0.3065 -0.0176 0.0030  -0.0144 344 HOH A O     
1396 O  O     . HOH F .   ? 0.4491 0.5562 0.3474 -0.0339 -0.0939 0.1293  345 HOH A O     
1397 O  O     . HOH F .   ? 0.5915 0.9083 0.3856 -0.1049 -0.0715 -0.0325 346 HOH A O     
1398 O  O     . HOH F .   ? 0.2844 0.4459 0.4148 0.0488  -0.0516 0.0095  347 HOH A O     
1399 O  O     . HOH F .   ? 0.5640 0.7599 0.4100 -0.0670 -0.0529 0.0600  348 HOH A O     
1400 O  O     . HOH F .   ? 0.5717 0.6423 0.7035 0.0226  -0.0966 0.0206  349 HOH A O     
1401 O  O     . HOH F .   ? 0.4502 0.7187 0.4698 -0.0692 0.0704  -0.0379 350 HOH A O     
1402 O  O     . HOH F .   ? 0.4473 0.3368 0.4684 -0.0253 -0.0133 0.0211  351 HOH A O     
1403 O  O     . HOH F .   ? 0.4770 0.5705 0.5378 -0.0893 -0.0792 -0.1441 352 HOH A O     
1404 O  O     . HOH F .   ? 0.5745 0.5147 0.6404 0.0059  -0.1114 0.0686  353 HOH A O     
1405 O  O     . HOH F .   ? 0.3445 0.3904 0.3343 -0.0404 0.0065  0.0187  354 HOH A O     
1406 O  O     . HOH F .   ? 0.4655 0.7053 0.6503 -0.2076 -0.0570 -0.0316 355 HOH A O     
1407 O  O     . HOH F .   ? 0.5367 0.5328 0.4820 -0.0639 -0.0428 0.0674  356 HOH A O     
1408 O  O     . HOH F .   ? 0.3226 0.4440 0.3362 -0.0313 0.0448  -0.0271 357 HOH A O     
1409 O  O     . HOH F .   ? 0.3029 0.5679 0.5007 0.0597  0.1005  -0.1819 358 HOH A O     
1410 O  O     . HOH F .   ? 0.4746 0.6280 0.6025 -0.0345 -0.0771 -0.0039 359 HOH A O     
1411 O  O     . HOH F .   ? 0.2877 0.4430 0.4210 0.0432  0.0210  -0.1022 360 HOH A O     
1412 O  O     . HOH F .   ? 0.3878 0.4165 0.5150 0.0504  -0.0185 -0.1340 361 HOH A O     
1413 O  O     . HOH F .   ? 0.4584 0.7273 0.5641 0.0065  0.0631  -0.1263 362 HOH A O     
1414 O  O     . HOH F .   ? 0.5964 0.8874 0.6147 -0.0074 0.0648  -0.2423 363 HOH A O     
1415 O  O     . HOH F .   ? 0.3954 0.6384 0.5648 0.0358  0.0421  -0.1273 364 HOH A O     
1416 O  O     . HOH F .   ? 0.3022 0.4936 0.6079 0.0737  -0.0994 -0.0395 365 HOH A O     
1417 O  O     . HOH F .   ? 0.4484 0.4129 0.5638 0.0337  -0.1081 0.0410  366 HOH A O     
1418 O  O     . HOH F .   ? 0.3457 0.3169 0.3644 -0.0331 -0.0008 0.0130  367 HOH A O     
1419 O  O     . HOH F .   ? 0.4273 0.4509 0.5586 0.0418  -0.0224 -0.1932 368 HOH A O     
1420 O  O     . HOH F .   ? 0.4643 0.7382 0.5740 0.0111  0.1240  -0.1932 369 HOH A O     
1421 O  O     . HOH F .   ? 0.3405 0.5676 0.6874 0.1167  -0.0144 -0.1755 370 HOH A O     
1422 O  O     . HOH F .   ? 0.5532 0.7271 0.5190 -0.1874 0.0330  0.0607  371 HOH A O     
1423 O  O     . HOH F .   ? 0.5244 0.6035 0.6460 -0.1460 -0.0847 -0.0814 372 HOH A O     
1424 O  O     . HOH F .   ? 0.5129 0.8463 0.7124 0.0484  -0.1725 0.0524  373 HOH A O     
1425 O  O     . HOH F .   ? 0.5542 0.5542 0.3786 -0.1294 0.0299  0.0299  374 HOH A O     
1426 O  O     . HOH F .   ? 0.3675 0.3917 0.4710 0.0755  -0.0601 0.0464  375 HOH A O     
1427 O  O     . HOH F .   ? 0.4726 0.4804 0.6092 0.0918  -0.0452 0.0179  376 HOH A O     
1428 O  O     . HOH F .   ? 0.4946 0.4915 0.4778 -0.0103 0.0256  -0.0732 377 HOH A O     
1429 O  O     . HOH F .   ? 0.5089 0.3769 0.7083 0.0655  -0.1357 0.0071  378 HOH A O     
1430 O  O     . HOH F .   ? 0.4335 0.6243 0.3367 -0.0952 0.0787  -0.0725 379 HOH A O     
1431 O  O     . HOH F .   ? 0.3295 0.7236 0.5309 -0.0100 -0.1475 -0.0010 380 HOH A O     
1432 O  O     . HOH F .   ? 0.3602 0.6724 0.5426 -0.1171 0.0069  -0.0221 381 HOH A O     
1433 O  O     . HOH F .   ? 0.6790 0.6825 0.6150 -0.0246 -0.0766 0.1434  382 HOH A O     
1434 O  O     . HOH F .   ? 0.4480 0.7211 0.3953 -0.1262 -0.1096 -0.1841 383 HOH A O     
1435 O  O     . HOH F .   ? 0.5007 0.5155 0.5708 0.0030  -0.1193 0.0604  384 HOH A O     
1436 O  O     . HOH F .   ? 0.6531 0.7586 0.8154 -0.2430 -0.0877 -0.0401 385 HOH A O     
1437 O  O     . HOH F .   ? 0.4305 0.5857 0.4221 -0.0704 0.0514  -0.0145 386 HOH A O     
1438 O  O     . HOH F .   ? 0.5005 0.7497 0.4452 -0.0307 -0.1392 0.0633  387 HOH A O     
1439 O  O     . HOH F .   ? 0.4692 0.8573 0.7138 0.0343  -0.1552 0.0197  388 HOH A O     
1440 O  O     . HOH F .   ? 0.3711 0.4676 0.4578 0.0341  0.0046  -0.1624 389 HOH A O     
1441 O  O     . HOH F .   ? 0.6395 0.7355 0.5424 -0.2069 -0.0020 0.1102  390 HOH A O     
1442 O  O     . HOH F .   ? 0.3250 0.6469 0.3786 -0.0604 0.1215  -0.1194 391 HOH A O     
1443 O  O     . HOH F .   ? 0.5652 0.6550 0.4836 -0.0753 0.0246  0.0002  392 HOH A O     
1444 O  O     . HOH F .   ? 0.5702 0.8912 0.4014 -0.1040 -0.0832 -0.0869 393 HOH A O     
1445 O  O     . HOH F .   ? 0.4078 0.7035 0.4456 -0.0229 -0.1447 0.0228  394 HOH A O     
1446 O  O     . HOH F .   ? 0.6773 0.5345 0.6611 -0.0403 -0.0631 0.1364  395 HOH A O     
1447 O  O     . HOH F .   ? 0.4598 0.4905 0.5045 -0.1240 -0.0277 0.0442  396 HOH A O     
1448 O  O     . HOH F .   ? 0.3504 0.4163 0.6794 0.1286  -0.0875 -0.0997 397 HOH A O     
1449 O  O     . HOH F .   ? 0.4286 0.4956 0.3772 -0.0575 0.0166  0.0097  398 HOH A O     
1450 O  O     . HOH F .   ? 0.7108 0.6721 0.8461 -0.2747 -0.1019 0.0103  399 HOH A O     
1451 O  O     . HOH F .   ? 0.6888 0.7594 0.7554 0.0589  -0.1753 0.1597  400 HOH A O     
1452 O  O     . HOH F .   ? 0.6090 0.8313 0.5293 -0.0803 0.1056  -0.1397 401 HOH A O     
1453 O  O     . HOH F .   ? 0.5508 0.5904 0.5224 -0.0176 0.0455  -0.1041 402 HOH A O     
1454 O  O     . HOH F .   ? 0.4706 0.7683 0.5611 -0.1990 0.0465  0.0194  403 HOH A O     
1455 O  O     . HOH F .   ? 0.3867 0.3587 0.5582 0.0689  -0.0544 -0.0759 404 HOH A O     
1456 O  O     . HOH F .   ? 0.5616 0.7362 0.5102 -0.1011 0.0433  0.0421  405 HOH A O     
1457 O  O     . HOH F .   ? 0.4497 0.6602 0.7055 0.0821  0.0082  -0.1476 406 HOH A O     
1458 O  O     . HOH F .   ? 0.4253 0.7991 0.6901 0.0364  0.0747  -0.1228 407 HOH A O     
1459 O  O     . HOH F .   ? 0.6157 0.9036 0.6843 -0.0106 0.1403  -0.2299 408 HOH A O     
1460 O  O     . HOH F .   ? 0.5460 0.8193 0.4443 -0.0646 -0.1055 -0.0111 409 HOH A O     
1461 O  O     . HOH F .   ? 0.6458 0.6840 0.6934 0.0229  0.0752  -0.2168 410 HOH A O     
1462 O  O     . HOH F .   ? 0.6433 0.8187 0.5129 -0.0946 0.0816  -0.1325 411 HOH A O     
1463 O  O     . HOH F .   ? 0.5305 0.6196 0.5024 -0.0611 0.0254  0.0089  412 HOH A O     
1464 O  O     . HOH F .   ? 0.6829 0.5700 0.6750 -0.0638 -0.0267 0.0886  413 HOH A O     
1465 O  O     . HOH F .   ? 0.6148 0.7402 0.4785 -0.1889 0.0120  0.0871  414 HOH A O     
1466 O  O     . HOH F .   ? 0.4968 0.5377 0.6461 0.0978  -0.0852 0.0537  415 HOH A O     
1467 O  O     . HOH F .   ? 0.5229 0.6234 0.8940 0.1428  -0.0786 -0.1382 416 HOH A O     
1468 O  O     . HOH F .   ? 0.5862 0.7508 0.6255 -0.2028 -0.1463 -0.2604 417 HOH A O     
1469 O  O     . HOH F .   ? 0.6229 0.7315 0.4735 -0.0767 -0.0582 0.1351  418 HOH A O     
1470 O  O     . HOH F .   ? 0.2268 0.5279 0.4006 0.0095  0.0813  -0.1043 419 HOH A O     
1471 O  O     . HOH F .   ? 0.5433 0.4716 0.5907 -0.0111 -0.0653 0.0414  420 HOH A O     
1472 O  O     . HOH F .   ? 0.7689 0.6401 0.9177 0.0361  -0.1672 0.0773  421 HOH A O     
1473 O  O     . HOH F .   ? 0.5995 0.6102 0.7901 0.0796  -0.0383 -0.1171 422 HOH A O     
1474 O  O     . HOH F .   ? 0.5872 0.6683 0.7315 0.0544  -0.0012 -0.2275 423 HOH A O     
1475 O  O     . HOH F .   ? 0.6600 0.6677 0.6442 -0.1049 -0.0261 0.0702  424 HOH A O     
1476 O  O     . HOH F .   ? 0.7671 0.7716 0.6392 -0.2036 -0.0182 0.1976  425 HOH A O     
1477 O  O     . HOH F .   ? 0.4341 0.3566 0.4526 -0.0210 -0.0052 0.0043  426 HOH A O     
1478 O  O     . HOH F .   ? 0.7832 0.7824 0.6953 -0.0828 -0.1262 0.1190  427 HOH A O     
1479 O  O     . HOH F .   ? 0.8127 0.5731 0.9776 -0.1283 -0.1385 -0.1069 428 HOH A O     
1480 O  O     . HOH F .   ? 0.5424 0.6409 0.6158 -0.0777 -0.0388 -0.0157 429 HOH A O     
1481 O  O     . HOH F .   ? 0.3512 0.7059 0.5452 -0.1003 0.0317  -0.0334 430 HOH A O     
1482 O  O     . HOH F .   ? 0.4104 0.5803 0.7843 0.1811  -0.0155 -0.1163 431 HOH A O     
1483 O  O     . HOH F .   ? 0.6874 0.6469 0.6817 -0.0112 0.0125  -0.0617 432 HOH A O     
1484 O  O     . HOH F .   ? 0.5930 0.8664 0.6954 0.0328  -0.1840 0.0894  433 HOH A O     
1485 O  O     . HOH F .   ? 0.6082 0.8623 0.5894 -0.1337 0.0000  0.0000  434 HOH A O     
1486 O  O     . HOH F .   ? 0.3866 0.6637 0.6032 -0.0704 -0.0816 -0.0250 435 HOH A O     
1487 O  O     . HOH F .   ? 0.5196 0.7678 0.5478 0.0047  -0.1578 0.0777  436 HOH A O     
1488 O  O     . HOH F .   ? 0.6932 0.6470 0.8049 -0.2658 -0.0916 0.0414  437 HOH A O     
1489 O  O     . HOH F .   ? 0.6516 0.7448 0.6012 -0.0359 0.0747  -0.1713 438 HOH A O     
1490 O  O     . HOH F .   ? 0.5508 0.4452 0.6584 -0.0106 -0.0705 -0.0414 439 HOH A O     
1491 O  O     . HOH F .   ? 0.4382 0.7734 0.5445 -0.0153 0.1363  -0.1827 440 HOH A O     
1492 O  O     . HOH F .   ? 0.8699 0.9468 0.8346 0.0065  -0.2087 0.2216  441 HOH A O     
1493 O  O     . HOH F .   ? 0.6163 0.9230 0.6060 -0.0586 0.1474  -0.2289 442 HOH A O     
1494 O  O     . HOH F .   ? 0.4095 0.7338 0.8513 0.1055  -0.0819 -0.1056 443 HOH A O     
1495 O  O     . HOH F .   ? 0.5974 0.6101 0.5790 -0.0252 -0.0191 -0.0047 444 HOH A O     
1496 O  O     . HOH F .   ? 0.4565 0.3912 0.4970 -0.0248 -0.0557 0.0388  445 HOH A O     
1497 O  O     . HOH F .   ? 0.4974 0.9176 0.5420 -0.0326 0.1070  -0.2508 446 HOH A O     
1498 O  O     . HOH F .   ? 0.5769 0.4679 0.6512 -0.0026 -0.0955 0.0515  447 HOH A O     
1499 O  O     . HOH F .   ? 0.3969 0.7753 0.7471 0.0434  0.0023  -0.1234 448 HOH A O     
1500 O  O     . HOH F .   ? 0.6865 0.6412 0.7340 -0.0085 -0.1403 0.0961  449 HOH A O     
1501 O  O     . HOH F .   ? 0.5177 0.7473 0.4324 -0.0341 -0.1521 0.1049  450 HOH A O     
1502 O  O     . HOH F .   ? 0.6385 0.5966 1.0579 0.1541  -0.2276 -0.0103 451 HOH A O     
1503 O  O     . HOH F .   ? 0.5934 0.6619 0.6671 -0.0088 -0.0963 0.0309  452 HOH A O     
1504 O  O     . HOH F .   ? 0.5774 0.4178 0.6090 -0.0271 -0.0219 0.0127  453 HOH A O     
1505 O  O     . HOH F .   ? 0.5936 0.6267 0.5176 -0.0509 0.0068  -0.0459 454 HOH A O     
1506 O  O     . HOH F .   ? 0.4054 0.4273 0.3740 -0.0688 -0.0140 0.0498  455 HOH A O     
1507 O  O     . HOH F .   ? 0.6667 0.5588 0.6856 -0.0273 -0.0067 -0.0298 456 HOH A O     
1508 O  O     . HOH F .   ? 0.4610 0.7833 0.3723 -0.1289 -0.1222 -0.1521 457 HOH A O     
1509 O  O     . HOH F .   ? 0.6771 0.6850 0.6248 -0.0410 0.0026  -0.0497 458 HOH A O     
1510 O  O     . HOH F .   ? 0.6595 1.1618 0.5675 -0.1129 0.1123  -0.2346 459 HOH A O     
1511 O  O     . HOH F .   ? 0.6573 0.6946 0.5966 -0.0741 -0.0093 0.0461  460 HOH A O     
1512 O  O     . HOH F .   ? 0.5171 0.4855 0.4957 -0.0681 -0.0468 0.0734  461 HOH A O     
1513 O  O     . HOH F .   ? 0.6503 0.7577 0.5936 -0.2295 -0.0003 0.1099  462 HOH A O     
1514 O  O     . HOH F .   ? 0.7727 0.8546 0.7761 -0.2840 -0.0244 0.1198  463 HOH A O     
1515 O  O     . HOH F .   ? 0.6766 0.5070 0.7116 -0.0285 -0.0186 -0.0197 464 HOH A O     
1516 O  O     . HOH F .   ? 0.4358 0.9124 0.5814 -0.1526 0.1148  -0.0651 465 HOH A O     
1517 O  O     . HOH F .   ? 0.6194 1.0319 0.7210 -0.0433 0.1077  -0.1459 466 HOH A O     
1518 O  O     . HOH F .   ? 0.5618 0.9001 0.4222 -0.1280 -0.1097 -0.1430 467 HOH A O     
1519 O  O     . HOH F .   ? 0.7609 0.5742 0.9515 -0.0029 -0.1025 -0.1817 468 HOH A O     
1520 O  O     . HOH F .   ? 0.6624 0.5673 0.6694 -0.0580 -0.0117 -0.0475 469 HOH A O     
1521 O  O     . HOH F .   ? 0.5995 0.9785 0.4162 -0.1498 -0.1223 -0.1376 470 HOH A O     
# 
