data_8YIM
# 
_entry.id   8YIM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YIM         pdb_00008yim 10.2210/pdb8yim/pdb 
WWPDB D_1300045601 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-12-04 
2 'Structure model' 1 1 2024-12-18 
3 'Structure model' 1 2 2025-01-08 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 2 'Structure model' '_citation_author.identifier_ORCID' 
13 3 'Structure model' '_citation.journal_volume'          
14 3 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YIM 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              aikweishen@hkbu.edu.hk 
_pdbx_contact_author.name_first         'Wei Shen' 
_pdbx_contact_author.name_last          Aik 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4414-173X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chau, Y.Y.' 1 ?                   
'Liang, H.'  2 ?                   
'Aik, W.S.'  3 0000-0003-4414-173X 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108036 
_citation.page_last                 108036 
_citation.title                     'Structural basis for Rab23 activation and a loss-of-function mutation in Carpenter syndrome.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2024.108036 
_citation.pdbx_database_id_PubMed   39615683 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chau, Y.Y.'  1 ? 
primary 'Liang, H.'   2 ? 
primary 'Tung, W.L.'  3 ? 
primary 'Hor, C.H.H.' 4 ? 
primary 'Aik, W.S.'   5 ? 
# 
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 Rab-23'                  19089.822 1   ? ? ? 'Truncated to residues 7-172' 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' 522.196   1   ? ? ? ?                             
3 non-polymer nat 'MAGNESIUM ION'                               24.305    1   ? ? ? ?                             
4 water       nat water                                         18.015    193 ? ? ? ?                             
# 
_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       
;SEVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQAC
VLVFSTTDRESFEAVSSWREKVVAEVGDIPTVLVQNKIDLLDDSCIKNEEAEALAKRLKLRFYRTSVKEDLNVNEVFKYL
AEKYLQK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SEVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQAC
VLVFSTTDRESFEAVSSWREKVVAEVGDIPTVLVQNKIDLLDDSCIKNEEAEALAKRLKLRFYRTSVKEDLNVNEVFKYL
AEKYLQK
;
_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 water                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLU n 
1 3   VAL n 
1 4   ALA n 
1 5   ILE n 
1 6   LYS n 
1 7   MET n 
1 8   VAL n 
1 9   VAL n 
1 10  VAL n 
1 11  GLY n 
1 12  ASN n 
1 13  GLY n 
1 14  ALA n 
1 15  VAL n 
1 16  GLY n 
1 17  LYS n 
1 18  SER n 
1 19  SER n 
1 20  MET n 
1 21  ILE n 
1 22  GLN n 
1 23  ARG n 
1 24  TYR n 
1 25  CYS n 
1 26  LYS n 
1 27  GLY n 
1 28  ILE n 
1 29  PHE n 
1 30  THR n 
1 31  LYS n 
1 32  ASP n 
1 33  TYR n 
1 34  LYS n 
1 35  LYS n 
1 36  THR n 
1 37  ILE n 
1 38  GLY n 
1 39  VAL n 
1 40  ASP n 
1 41  PHE n 
1 42  LEU n 
1 43  GLU n 
1 44  ARG n 
1 45  GLN n 
1 46  ILE n 
1 47  GLN n 
1 48  VAL n 
1 49  ASN n 
1 50  ASP n 
1 51  GLU n 
1 52  ASP n 
1 53  VAL n 
1 54  ARG n 
1 55  LEU n 
1 56  MET n 
1 57  LEU n 
1 58  TRP n 
1 59  ASP n 
1 60  THR n 
1 61  ALA n 
1 62  GLY n 
1 63  GLN n 
1 64  GLU n 
1 65  GLU n 
1 66  PHE n 
1 67  ASP n 
1 68  ALA n 
1 69  ILE n 
1 70  THR n 
1 71  LYS n 
1 72  ALA n 
1 73  TYR n 
1 74  TYR n 
1 75  ARG n 
1 76  GLY n 
1 77  ALA n 
1 78  GLN n 
1 79  ALA n 
1 80  CYS n 
1 81  VAL n 
1 82  LEU n 
1 83  VAL n 
1 84  PHE n 
1 85  SER n 
1 86  THR n 
1 87  THR n 
1 88  ASP n 
1 89  ARG n 
1 90  GLU n 
1 91  SER n 
1 92  PHE n 
1 93  GLU n 
1 94  ALA n 
1 95  VAL n 
1 96  SER n 
1 97  SER n 
1 98  TRP n 
1 99  ARG n 
1 100 GLU n 
1 101 LYS n 
1 102 VAL n 
1 103 VAL n 
1 104 ALA n 
1 105 GLU n 
1 106 VAL n 
1 107 GLY n 
1 108 ASP n 
1 109 ILE n 
1 110 PRO n 
1 111 THR n 
1 112 VAL n 
1 113 LEU n 
1 114 VAL n 
1 115 GLN n 
1 116 ASN n 
1 117 LYS n 
1 118 ILE n 
1 119 ASP n 
1 120 LEU n 
1 121 LEU n 
1 122 ASP n 
1 123 ASP n 
1 124 SER n 
1 125 CYS n 
1 126 ILE n 
1 127 LYS n 
1 128 ASN n 
1 129 GLU n 
1 130 GLU n 
1 131 ALA n 
1 132 GLU n 
1 133 ALA n 
1 134 LEU n 
1 135 ALA n 
1 136 LYS n 
1 137 ARG n 
1 138 LEU n 
1 139 LYS n 
1 140 LEU n 
1 141 ARG n 
1 142 PHE n 
1 143 TYR n 
1 144 ARG n 
1 145 THR n 
1 146 SER n 
1 147 VAL n 
1 148 LYS n 
1 149 GLU n 
1 150 ASP n 
1 151 LEU n 
1 152 ASN n 
1 153 VAL n 
1 154 ASN n 
1 155 GLU n 
1 156 VAL n 
1 157 PHE n 
1 158 LYS n 
1 159 TYR n 
1 160 LEU n 
1 161 ALA n 
1 162 GLU n 
1 163 LYS n 
1 164 TYR n 
1 165 LEU n 
1 166 GLN n 
1 167 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   167 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'RAB23, HSPC137' 
_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 
CYS 'L-peptide linking' y CYSTEINE                                      ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                       ? 'C2 H5 N O2'        75.067  
GNP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' ? 'C10 H17 N6 O13 P3' 522.196 
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 
# 
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   SER 1   6   ?   ?   ?   A . n 
A 1 2   GLU 2   7   7   GLU GLU A . n 
A 1 3   VAL 3   8   8   VAL VAL A . n 
A 1 4   ALA 4   9   9   ALA ALA A . n 
A 1 5   ILE 5   10  10  ILE ILE A . n 
A 1 6   LYS 6   11  11  LYS LYS A . n 
A 1 7   MET 7   12  12  MET MET A . n 
A 1 8   VAL 8   13  13  VAL VAL A . n 
A 1 9   VAL 9   14  14  VAL VAL A . n 
A 1 10  VAL 10  15  15  VAL VAL A . n 
A 1 11  GLY 11  16  16  GLY GLY A . n 
A 1 12  ASN 12  17  17  ASN ASN A . n 
A 1 13  GLY 13  18  18  GLY GLY A . n 
A 1 14  ALA 14  19  19  ALA ALA A . n 
A 1 15  VAL 15  20  20  VAL VAL A . n 
A 1 16  GLY 16  21  21  GLY GLY A . n 
A 1 17  LYS 17  22  22  LYS LYS A . n 
A 1 18  SER 18  23  23  SER SER A . n 
A 1 19  SER 19  24  24  SER SER A . n 
A 1 20  MET 20  25  25  MET MET A . n 
A 1 21  ILE 21  26  26  ILE ILE A . n 
A 1 22  GLN 22  27  27  GLN GLN A . n 
A 1 23  ARG 23  28  28  ARG ARG A . n 
A 1 24  TYR 24  29  29  TYR TYR A . n 
A 1 25  CYS 25  30  30  CYS CYS A . n 
A 1 26  LYS 26  31  31  LYS LYS A . n 
A 1 27  GLY 27  32  32  GLY GLY A . n 
A 1 28  ILE 28  33  33  ILE ILE A . n 
A 1 29  PHE 29  34  34  PHE PHE A . n 
A 1 30  THR 30  35  35  THR THR A . n 
A 1 31  LYS 31  36  36  LYS LYS A . n 
A 1 32  ASP 32  37  37  ASP ASP A . n 
A 1 33  TYR 33  38  38  TYR TYR A . n 
A 1 34  LYS 34  39  39  LYS LYS A . n 
A 1 35  LYS 35  40  40  LYS LYS A . n 
A 1 36  THR 36  41  41  THR THR A . n 
A 1 37  ILE 37  42  42  ILE ILE A . n 
A 1 38  GLY 38  43  43  GLY GLY A . n 
A 1 39  VAL 39  44  44  VAL VAL A . n 
A 1 40  ASP 40  45  45  ASP ASP A . n 
A 1 41  PHE 41  46  46  PHE PHE A . n 
A 1 42  LEU 42  47  47  LEU LEU A . n 
A 1 43  GLU 43  48  48  GLU GLU A . n 
A 1 44  ARG 44  49  49  ARG ARG A . n 
A 1 45  GLN 45  50  50  GLN GLN A . n 
A 1 46  ILE 46  51  51  ILE ILE A . n 
A 1 47  GLN 47  52  52  GLN GLN A . n 
A 1 48  VAL 48  53  53  VAL VAL A . n 
A 1 49  ASN 49  54  54  ASN ASN A . n 
A 1 50  ASP 50  55  55  ASP ASP A . n 
A 1 51  GLU 51  56  56  GLU GLU A . n 
A 1 52  ASP 52  57  57  ASP ASP A . n 
A 1 53  VAL 53  58  58  VAL VAL A . n 
A 1 54  ARG 54  59  59  ARG ARG A . n 
A 1 55  LEU 55  60  60  LEU LEU A . n 
A 1 56  MET 56  61  61  MET MET A . n 
A 1 57  LEU 57  62  62  LEU LEU A . n 
A 1 58  TRP 58  63  63  TRP TRP A . n 
A 1 59  ASP 59  64  64  ASP ASP A . n 
A 1 60  THR 60  65  65  THR THR A . n 
A 1 61  ALA 61  66  66  ALA ALA A . n 
A 1 62  GLY 62  67  67  GLY GLY A . n 
A 1 63  GLN 63  68  68  GLN GLN A . n 
A 1 64  GLU 64  69  ?   ?   ?   A . n 
A 1 65  GLU 65  70  ?   ?   ?   A . n 
A 1 66  PHE 66  71  ?   ?   ?   A . n 
A 1 67  ASP 67  72  ?   ?   ?   A . n 
A 1 68  ALA 68  73  ?   ?   ?   A . n 
A 1 69  ILE 69  74  74  ILE ILE A . n 
A 1 70  THR 70  75  75  THR THR A . n 
A 1 71  LYS 71  76  76  LYS LYS A . n 
A 1 72  ALA 72  77  77  ALA ALA A . n 
A 1 73  TYR 73  78  78  TYR TYR A . n 
A 1 74  TYR 74  79  79  TYR TYR A . n 
A 1 75  ARG 75  80  80  ARG ARG A . n 
A 1 76  GLY 76  81  81  GLY GLY A . n 
A 1 77  ALA 77  82  82  ALA ALA A . n 
A 1 78  GLN 78  83  83  GLN GLN A . n 
A 1 79  ALA 79  84  84  ALA ALA A . n 
A 1 80  CYS 80  85  85  CYS CYS A . n 
A 1 81  VAL 81  86  86  VAL VAL A . n 
A 1 82  LEU 82  87  87  LEU LEU A . n 
A 1 83  VAL 83  88  88  VAL VAL A . n 
A 1 84  PHE 84  89  89  PHE PHE A . n 
A 1 85  SER 85  90  90  SER SER A . n 
A 1 86  THR 86  91  91  THR THR A . n 
A 1 87  THR 87  92  92  THR THR A . n 
A 1 88  ASP 88  93  93  ASP ASP A . n 
A 1 89  ARG 89  94  94  ARG ARG A . n 
A 1 90  GLU 90  95  95  GLU GLU A . n 
A 1 91  SER 91  96  96  SER SER A . n 
A 1 92  PHE 92  97  97  PHE PHE A . n 
A 1 93  GLU 93  98  98  GLU GLU A . n 
A 1 94  ALA 94  99  99  ALA ALA A . n 
A 1 95  VAL 95  100 100 VAL VAL A . n 
A 1 96  SER 96  101 101 SER SER A . n 
A 1 97  SER 97  102 102 SER SER A . n 
A 1 98  TRP 98  103 103 TRP TRP A . n 
A 1 99  ARG 99  104 104 ARG ARG A . n 
A 1 100 GLU 100 105 105 GLU GLU A . n 
A 1 101 LYS 101 106 106 LYS LYS A . n 
A 1 102 VAL 102 107 107 VAL VAL A . n 
A 1 103 VAL 103 108 108 VAL VAL A . n 
A 1 104 ALA 104 109 109 ALA ALA A . n 
A 1 105 GLU 105 110 110 GLU GLU A . n 
A 1 106 VAL 106 111 111 VAL VAL A . n 
A 1 107 GLY 107 112 112 GLY GLY A . n 
A 1 108 ASP 108 113 113 ASP ASP A . n 
A 1 109 ILE 109 114 114 ILE ILE A . n 
A 1 110 PRO 110 115 115 PRO PRO A . n 
A 1 111 THR 111 116 116 THR THR A . n 
A 1 112 VAL 112 117 117 VAL VAL A . n 
A 1 113 LEU 113 118 118 LEU LEU A . n 
A 1 114 VAL 114 119 119 VAL VAL A . n 
A 1 115 GLN 115 120 120 GLN GLN A . n 
A 1 116 ASN 116 121 121 ASN ASN A . n 
A 1 117 LYS 117 122 122 LYS LYS A . n 
A 1 118 ILE 118 123 123 ILE ILE A . n 
A 1 119 ASP 119 124 124 ASP ASP A . n 
A 1 120 LEU 120 125 125 LEU LEU A . n 
A 1 121 LEU 121 126 126 LEU LEU A . n 
A 1 122 ASP 122 127 127 ASP ASP A . n 
A 1 123 ASP 123 128 128 ASP ASP A . n 
A 1 124 SER 124 129 129 SER SER A . n 
A 1 125 CYS 125 130 130 CYS CYS A . n 
A 1 126 ILE 126 131 131 ILE ILE A . n 
A 1 127 LYS 127 132 132 LYS LYS A . n 
A 1 128 ASN 128 133 133 ASN ASN A . n 
A 1 129 GLU 129 134 134 GLU GLU A . n 
A 1 130 GLU 130 135 135 GLU GLU A . n 
A 1 131 ALA 131 136 136 ALA ALA A . n 
A 1 132 GLU 132 137 137 GLU GLU A . n 
A 1 133 ALA 133 138 138 ALA ALA A . n 
A 1 134 LEU 134 139 139 LEU LEU A . n 
A 1 135 ALA 135 140 140 ALA ALA A . n 
A 1 136 LYS 136 141 141 LYS LYS A . n 
A 1 137 ARG 137 142 142 ARG ARG A . n 
A 1 138 LEU 138 143 143 LEU LEU A . n 
A 1 139 LYS 139 144 144 LYS LYS A . n 
A 1 140 LEU 140 145 145 LEU LEU A . n 
A 1 141 ARG 141 146 146 ARG ARG A . n 
A 1 142 PHE 142 147 147 PHE PHE A . n 
A 1 143 TYR 143 148 148 TYR TYR A . n 
A 1 144 ARG 144 149 149 ARG ARG A . n 
A 1 145 THR 145 150 150 THR THR A . n 
A 1 146 SER 146 151 151 SER SER A . n 
A 1 147 VAL 147 152 152 VAL VAL A . n 
A 1 148 LYS 148 153 153 LYS LYS A . n 
A 1 149 GLU 149 154 154 GLU GLU A . n 
A 1 150 ASP 150 155 155 ASP ASP A . n 
A 1 151 LEU 151 156 156 LEU LEU A . n 
A 1 152 ASN 152 157 157 ASN ASN A . n 
A 1 153 VAL 153 158 158 VAL VAL A . n 
A 1 154 ASN 154 159 159 ASN ASN A . n 
A 1 155 GLU 155 160 160 GLU GLU A . n 
A 1 156 VAL 156 161 161 VAL VAL A . n 
A 1 157 PHE 157 162 162 PHE PHE A . n 
A 1 158 LYS 158 163 163 LYS LYS A . n 
A 1 159 TYR 159 164 164 TYR TYR A . n 
A 1 160 LEU 160 165 165 LEU LEU A . n 
A 1 161 ALA 161 166 166 ALA ALA A . n 
A 1 162 GLU 162 167 167 GLU GLU A . n 
A 1 163 LYS 163 168 168 LYS LYS A . n 
A 1 164 TYR 164 169 169 TYR TYR A . n 
A 1 165 LEU 165 170 170 LEU LEU A . n 
A 1 166 GLN 166 171 171 GLN GLN A . n 
A 1 167 LYS 167 172 ?   ?   ?   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   201 201 GNP LIG A . 
C 3 MG  1   202 1   MG  MG  A . 
D 4 HOH 1   301 77  HOH HOH A . 
D 4 HOH 2   302 64  HOH HOH A . 
D 4 HOH 3   303 124 HOH HOH A . 
D 4 HOH 4   304 57  HOH HOH A . 
D 4 HOH 5   305 150 HOH HOH A . 
D 4 HOH 6   306 93  HOH HOH A . 
D 4 HOH 7   307 99  HOH HOH A . 
D 4 HOH 8   308 111 HOH HOH A . 
D 4 HOH 9   309 70  HOH HOH A . 
D 4 HOH 10  310 165 HOH HOH A . 
D 4 HOH 11  311 31  HOH HOH A . 
D 4 HOH 12  312 193 HOH HOH A . 
D 4 HOH 13  313 8   HOH HOH A . 
D 4 HOH 14  314 148 HOH HOH A . 
D 4 HOH 15  315 122 HOH HOH A . 
D 4 HOH 16  316 174 HOH HOH A . 
D 4 HOH 17  317 56  HOH HOH A . 
D 4 HOH 18  318 89  HOH HOH A . 
D 4 HOH 19  319 12  HOH HOH A . 
D 4 HOH 20  320 203 HOH HOH A . 
D 4 HOH 21  321 9   HOH HOH A . 
D 4 HOH 22  322 13  HOH HOH A . 
D 4 HOH 23  323 16  HOH HOH A . 
D 4 HOH 24  324 6   HOH HOH A . 
D 4 HOH 25  325 112 HOH HOH A . 
D 4 HOH 26  326 95  HOH HOH A . 
D 4 HOH 27  327 131 HOH HOH A . 
D 4 HOH 28  328 3   HOH HOH A . 
D 4 HOH 29  329 58  HOH HOH A . 
D 4 HOH 30  330 22  HOH HOH A . 
D 4 HOH 31  331 146 HOH HOH A . 
D 4 HOH 32  332 2   HOH HOH A . 
D 4 HOH 33  333 38  HOH HOH A . 
D 4 HOH 34  334 97  HOH HOH A . 
D 4 HOH 35  335 84  HOH HOH A . 
D 4 HOH 36  336 11  HOH HOH A . 
D 4 HOH 37  337 18  HOH HOH A . 
D 4 HOH 38  338 43  HOH HOH A . 
D 4 HOH 39  339 128 HOH HOH A . 
D 4 HOH 40  340 36  HOH HOH A . 
D 4 HOH 41  341 118 HOH HOH A . 
D 4 HOH 42  342 82  HOH HOH A . 
D 4 HOH 43  343 68  HOH HOH A . 
D 4 HOH 44  344 32  HOH HOH A . 
D 4 HOH 45  345 62  HOH HOH A . 
D 4 HOH 46  346 26  HOH HOH A . 
D 4 HOH 47  347 173 HOH HOH A . 
D 4 HOH 48  348 69  HOH HOH A . 
D 4 HOH 49  349 44  HOH HOH A . 
D 4 HOH 50  350 7   HOH HOH A . 
D 4 HOH 51  351 147 HOH HOH A . 
D 4 HOH 52  352 5   HOH HOH A . 
D 4 HOH 53  353 28  HOH HOH A . 
D 4 HOH 54  354 164 HOH HOH A . 
D 4 HOH 55  355 48  HOH HOH A . 
D 4 HOH 56  356 171 HOH HOH A . 
D 4 HOH 57  357 152 HOH HOH A . 
D 4 HOH 58  358 219 HOH HOH A . 
D 4 HOH 59  359 157 HOH HOH A . 
D 4 HOH 60  360 159 HOH HOH A . 
D 4 HOH 61  361 74  HOH HOH A . 
D 4 HOH 62  362 92  HOH HOH A . 
D 4 HOH 63  363 42  HOH HOH A . 
D 4 HOH 64  364 54  HOH HOH A . 
D 4 HOH 65  365 52  HOH HOH A . 
D 4 HOH 66  366 101 HOH HOH A . 
D 4 HOH 67  367 130 HOH HOH A . 
D 4 HOH 68  368 19  HOH HOH A . 
D 4 HOH 69  369 191 HOH HOH A . 
D 4 HOH 70  370 4   HOH HOH A . 
D 4 HOH 71  371 1   HOH HOH A . 
D 4 HOH 72  372 41  HOH HOH A . 
D 4 HOH 73  373 24  HOH HOH A . 
D 4 HOH 74  374 47  HOH HOH A . 
D 4 HOH 75  375 154 HOH HOH A . 
D 4 HOH 76  376 88  HOH HOH A . 
D 4 HOH 77  377 49  HOH HOH A . 
D 4 HOH 78  378 72  HOH HOH A . 
D 4 HOH 79  379 166 HOH HOH A . 
D 4 HOH 80  380 160 HOH HOH A . 
D 4 HOH 81  381 39  HOH HOH A . 
D 4 HOH 82  382 135 HOH HOH A . 
D 4 HOH 83  383 17  HOH HOH A . 
D 4 HOH 84  384 53  HOH HOH A . 
D 4 HOH 85  385 20  HOH HOH A . 
D 4 HOH 86  386 37  HOH HOH A . 
D 4 HOH 87  387 162 HOH HOH A . 
D 4 HOH 88  388 65  HOH HOH A . 
D 4 HOH 89  389 60  HOH HOH A . 
D 4 HOH 90  390 25  HOH HOH A . 
D 4 HOH 91  391 15  HOH HOH A . 
D 4 HOH 92  392 115 HOH HOH A . 
D 4 HOH 93  393 156 HOH HOH A . 
D 4 HOH 94  394 94  HOH HOH A . 
D 4 HOH 95  395 121 HOH HOH A . 
D 4 HOH 96  396 50  HOH HOH A . 
D 4 HOH 97  397 10  HOH HOH A . 
D 4 HOH 98  398 169 HOH HOH A . 
D 4 HOH 99  399 178 HOH HOH A . 
D 4 HOH 100 400 23  HOH HOH A . 
D 4 HOH 101 401 46  HOH HOH A . 
D 4 HOH 102 402 136 HOH HOH A . 
D 4 HOH 103 403 45  HOH HOH A . 
D 4 HOH 104 404 113 HOH HOH A . 
D 4 HOH 105 405 100 HOH HOH A . 
D 4 HOH 106 406 155 HOH HOH A . 
D 4 HOH 107 407 96  HOH HOH A . 
D 4 HOH 108 408 76  HOH HOH A . 
D 4 HOH 109 409 105 HOH HOH A . 
D 4 HOH 110 410 86  HOH HOH A . 
D 4 HOH 111 411 108 HOH HOH A . 
D 4 HOH 112 412 210 HOH HOH A . 
D 4 HOH 113 413 132 HOH HOH A . 
D 4 HOH 114 414 66  HOH HOH A . 
D 4 HOH 115 415 151 HOH HOH A . 
D 4 HOH 116 416 168 HOH HOH A . 
D 4 HOH 117 417 117 HOH HOH A . 
D 4 HOH 118 418 27  HOH HOH A . 
D 4 HOH 119 419 14  HOH HOH A . 
D 4 HOH 120 420 176 HOH HOH A . 
D 4 HOH 121 421 140 HOH HOH A . 
D 4 HOH 122 422 109 HOH HOH A . 
D 4 HOH 123 423 204 HOH HOH A . 
D 4 HOH 124 424 33  HOH HOH A . 
D 4 HOH 125 425 102 HOH HOH A . 
D 4 HOH 126 426 63  HOH HOH A . 
D 4 HOH 127 427 21  HOH HOH A . 
D 4 HOH 128 428 116 HOH HOH A . 
D 4 HOH 129 429 153 HOH HOH A . 
D 4 HOH 130 430 29  HOH HOH A . 
D 4 HOH 131 431 35  HOH HOH A . 
D 4 HOH 132 432 34  HOH HOH A . 
D 4 HOH 133 433 110 HOH HOH A . 
D 4 HOH 134 434 90  HOH HOH A . 
D 4 HOH 135 435 123 HOH HOH A . 
D 4 HOH 136 436 107 HOH HOH A . 
D 4 HOH 137 437 78  HOH HOH A . 
D 4 HOH 138 438 73  HOH HOH A . 
D 4 HOH 139 439 51  HOH HOH A . 
D 4 HOH 140 440 67  HOH HOH A . 
D 4 HOH 141 441 215 HOH HOH A . 
D 4 HOH 142 442 30  HOH HOH A . 
D 4 HOH 143 443 197 HOH HOH A . 
D 4 HOH 144 444 134 HOH HOH A . 
D 4 HOH 145 445 200 HOH HOH A . 
D 4 HOH 146 446 184 HOH HOH A . 
D 4 HOH 147 447 194 HOH HOH A . 
D 4 HOH 148 448 213 HOH HOH A . 
D 4 HOH 149 449 91  HOH HOH A . 
D 4 HOH 150 450 103 HOH HOH A . 
D 4 HOH 151 451 119 HOH HOH A . 
D 4 HOH 152 452 179 HOH HOH A . 
D 4 HOH 153 453 143 HOH HOH A . 
D 4 HOH 154 454 211 HOH HOH A . 
D 4 HOH 155 455 75  HOH HOH A . 
D 4 HOH 156 456 106 HOH HOH A . 
D 4 HOH 157 457 40  HOH HOH A . 
D 4 HOH 158 458 161 HOH HOH A . 
D 4 HOH 159 459 202 HOH HOH A . 
D 4 HOH 160 460 141 HOH HOH A . 
D 4 HOH 161 461 129 HOH HOH A . 
D 4 HOH 162 462 163 HOH HOH A . 
D 4 HOH 163 463 139 HOH HOH A . 
D 4 HOH 164 464 186 HOH HOH A . 
D 4 HOH 165 465 192 HOH HOH A . 
D 4 HOH 166 466 189 HOH HOH A . 
D 4 HOH 167 467 81  HOH HOH A . 
D 4 HOH 168 468 188 HOH HOH A . 
D 4 HOH 169 469 85  HOH HOH A . 
D 4 HOH 170 470 142 HOH HOH A . 
D 4 HOH 171 471 185 HOH HOH A . 
D 4 HOH 172 472 175 HOH HOH A . 
D 4 HOH 173 473 144 HOH HOH A . 
D 4 HOH 174 474 190 HOH HOH A . 
D 4 HOH 175 475 133 HOH HOH A . 
D 4 HOH 176 476 126 HOH HOH A . 
D 4 HOH 177 477 71  HOH HOH A . 
D 4 HOH 178 478 212 HOH HOH A . 
D 4 HOH 179 479 120 HOH HOH A . 
D 4 HOH 180 480 114 HOH HOH A . 
D 4 HOH 181 481 198 HOH HOH A . 
D 4 HOH 182 482 87  HOH HOH A . 
D 4 HOH 183 483 214 HOH HOH A . 
D 4 HOH 184 484 199 HOH HOH A . 
D 4 HOH 185 485 218 HOH HOH A . 
D 4 HOH 186 486 59  HOH HOH A . 
D 4 HOH 187 487 61  HOH HOH A . 
D 4 HOH 188 488 104 HOH HOH A . 
D 4 HOH 189 489 207 HOH HOH A . 
D 4 HOH 190 490 181 HOH HOH A . 
D 4 HOH 191 491 195 HOH HOH A . 
D 4 HOH 192 492 80  HOH HOH A . 
D 4 HOH 193 493 145 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 LYS 31  ? CD  ? A LYS 26  CD  
2  1 Y 1 A LYS 31  ? CE  ? A LYS 26  CE  
3  1 Y 1 A LYS 31  ? NZ  ? A LYS 26  NZ  
4  1 Y 1 A LYS 39  ? CD  ? A LYS 34  CD  
5  1 Y 1 A LYS 39  ? CE  ? A LYS 34  CE  
6  1 Y 1 A LYS 39  ? NZ  ? A LYS 34  NZ  
7  1 Y 1 A GLN 50  ? CG  ? A GLN 45  CG  
8  1 Y 1 A GLN 50  ? CD  ? A GLN 45  CD  
9  1 Y 1 A GLN 50  ? OE1 ? A GLN 45  OE1 
10 1 Y 1 A GLN 50  ? NE2 ? A GLN 45  NE2 
11 1 Y 1 A ASN 54  ? CG  ? A ASN 49  CG  
12 1 Y 1 A ASN 54  ? OD1 ? A ASN 49  OD1 
13 1 Y 1 A ASN 54  ? ND2 ? A ASN 49  ND2 
14 1 Y 1 A ASP 55  ? CG  ? A ASP 50  CG  
15 1 Y 1 A ASP 55  ? OD1 ? A ASP 50  OD1 
16 1 Y 1 A ASP 55  ? OD2 ? A ASP 50  OD2 
17 1 Y 1 A GLU 56  ? CG  ? A GLU 51  CG  
18 1 Y 1 A GLU 56  ? CD  ? A GLU 51  CD  
19 1 Y 1 A GLU 56  ? OE1 ? A GLU 51  OE1 
20 1 Y 1 A GLU 56  ? OE2 ? A GLU 51  OE2 
21 1 Y 1 A GLN 68  ? CG  ? A GLN 63  CG  
22 1 Y 1 A GLN 68  ? CD  ? A GLN 63  CD  
23 1 Y 1 A GLN 68  ? OE1 ? A GLN 63  OE1 
24 1 Y 1 A GLN 68  ? NE2 ? A GLN 63  NE2 
25 1 Y 1 A GLU 95  ? CD  ? A GLU 90  CD  
26 1 Y 1 A GLU 95  ? OE1 ? A GLU 90  OE1 
27 1 Y 1 A GLU 95  ? OE2 ? A GLU 90  OE2 
28 1 Y 1 A ASP 113 ? CG  ? A ASP 108 CG  
29 1 Y 1 A ASP 113 ? OD1 ? A ASP 108 OD1 
30 1 Y 1 A ASP 113 ? OD2 ? A ASP 108 OD2 
31 1 Y 1 A LEU 126 ? CG  ? A LEU 121 CG  
32 1 Y 1 A LEU 126 ? CD1 ? A LEU 121 CD1 
33 1 Y 1 A LEU 126 ? CD2 ? A LEU 121 CD2 
34 1 Y 1 A ASP 127 ? CG  ? A ASP 122 CG  
35 1 Y 1 A ASP 127 ? OD1 ? A ASP 122 OD1 
36 1 Y 1 A ASP 127 ? OD2 ? A ASP 122 OD2 
37 1 Y 1 A GLN 171 ? CG  ? A GLN 166 CG  
38 1 Y 1 A GLN 171 ? CD  ? A GLN 166 CD  
39 1 Y 1 A GLN 171 ? OE1 ? A GLN 166 OE1 
40 1 Y 1 A GLN 171 ? NE2 ? A GLN 166 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.18.2_3874 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YIM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.523 
_cell.length_a_esd                 ? 
_cell.length_b                     60.523 
_cell.length_b_esd                 ? 
_cell.length_c                     93.920 
_cell.length_c_esd                 ? 
_cell.volume                       297940.831 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         8YIM 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            
;P 31 2"
;
_symmetry.space_group_name_H-M             'P 31 2 1' 
_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                   8YIM 
_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             2.60 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.71 
_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              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.1M Imidazole pH 8.0, 0.2M NaCl, 0.4M sodium phosphate monobasic/1.6M potassium phosphate dibasic' 
_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                         'RIGAKU HyPix-6000HE' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-17 
_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   1.5418 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU FR-X' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          9.90 
_reflns.entry_id                                       8YIM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.35 
_reflns.d_resolution_low                               22.88 
_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                                     44414 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.50 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.37 
_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                                0.141 
_reflns.pdbx_Rpim_I_all                                0.046 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.133 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.35 
_reflns_shell.d_res_low                                     1.37 
_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                             2185 
_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                               6.8 
_reflns_shell.pdbx_chi_squared                              0.52 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               2.260 
_reflns_shell.pdbx_Rpim_I_all                               0.862 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.724 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.087 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               16.58 
_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                                 8YIM 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.35 
_refine.ls_d_res_low                             22.88 
_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                     44369 
_refine.ls_number_reflns_R_free                  2354 
_refine.ls_number_reflns_R_work                  42015 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_percent_reflns_R_free                 5.31 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1513 
_refine.ls_R_factor_R_free                       0.1794 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1496 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 16.5251 
_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                            0.1110 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.35 
_refine_hist.d_res_low                        22.88 
_refine_hist.number_atoms_solvent             193 
_refine_hist.number_atoms_total               1468 
_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        1242 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_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' ? 0.0027  ? 1348 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6805  ? 1831 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0648  ? 212  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0025  ? 229  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.2101 ? 516  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.35 1.38  . . 161 2438 100.00 . . . . 0.1898 . . . . . . . . . . . 0.2348 
'X-RAY DIFFRACTION' 1.38 1.41  . . 152 2424 100.00 . . . . 0.1743 . . . . . . . . . . . 0.1961 
'X-RAY DIFFRACTION' 1.41 1.44  . . 132 2434 100.00 . . . . 0.1567 . . . . . . . . . . . 0.2009 
'X-RAY DIFFRACTION' 1.44 1.48  . . 130 2438 100.00 . . . . 0.1423 . . . . . . . . . . . 0.2009 
'X-RAY DIFFRACTION' 1.48 1.52  . . 123 2451 100.00 . . . . 0.1346 . . . . . . . . . . . 0.2045 
'X-RAY DIFFRACTION' 1.52 1.56  . . 95  2476 100.00 . . . . 0.1300 . . . . . . . . . . . 0.1625 
'X-RAY DIFFRACTION' 1.56 1.61  . . 141 2417 100.00 . . . . 0.1266 . . . . . . . . . . . 0.1727 
'X-RAY DIFFRACTION' 1.61 1.67  . . 118 2492 100.00 . . . . 0.1281 . . . . . . . . . . . 0.1611 
'X-RAY DIFFRACTION' 1.67 1.74  . . 144 2453 100.00 . . . . 0.1275 . . . . . . . . . . . 0.1825 
'X-RAY DIFFRACTION' 1.74 1.81  . . 123 2459 100.00 . . . . 0.1350 . . . . . . . . . . . 0.1784 
'X-RAY DIFFRACTION' 1.81 1.91  . . 146 2447 100.00 . . . . 0.1391 . . . . . . . . . . . 0.1693 
'X-RAY DIFFRACTION' 1.91 2.03  . . 132 2500 100.00 . . . . 0.1353 . . . . . . . . . . . 0.1637 
'X-RAY DIFFRACTION' 2.03 2.19  . . 141 2468 100.00 . . . . 0.1375 . . . . . . . . . . . 0.1625 
'X-RAY DIFFRACTION' 2.19 2.41  . . 122 2490 100.00 . . . . 0.1477 . . . . . . . . . . . 0.1684 
'X-RAY DIFFRACTION' 2.41 2.75  . . 165 2487 100.00 . . . . 0.1640 . . . . . . . . . . . 0.1947 
'X-RAY DIFFRACTION' 2.75 3.47  . . 140 2523 100.00 . . . . 0.1653 . . . . . . . . . . . 0.1820 
'X-RAY DIFFRACTION' 3.47 22.88 . . 189 2618 99.96  . . . . 0.1592 . . . . . . . . . . . 0.1753 
# 
_struct.entry_id                     8YIM 
_struct.title                        'Crystal Structure of Human Rab23 in complex with GMPPNP (1.35 Angstroms Resolution)' 
_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        8YIM 
_struct_keywords.text            'Small GTPase Rossmann Fold, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RAB23_HUMAN 
_struct_ref.pdbx_db_accession          Q9ULC3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQACV
LVFSTTDRESFEAVSSWREKVVAEVGDIPTVLVQNKIDLLDDSCIKNEEAEALAKRLKLRFYRTSVKEDLNVNEVFKYLA
EKYLQK
;
_struct_ref.pdbx_align_begin           7 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YIM 
_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                 167 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9ULC3 
_struct_ref_seq.db_align_beg                  7 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  172 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       172 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             8YIM 
_struct_ref_seq_dif.mon_id                       SER 
_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   Q9ULC3 
_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            6 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1010 ? 
1 MORE         -14  ? 
1 'SSA (A^2)'  7860 ? 
# 
_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 
# 
_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  ? GLY A 27  ? GLY A 21  GLY A 32  1 ? 12 
HELX_P HELX_P2 AA2 THR A 70  ? ARG A 75  ? THR A 75  ARG A 80  1 ? 6  
HELX_P HELX_P3 AA3 ASP A 88  ? ALA A 94  ? ASP A 93  ALA A 99  1 ? 7  
HELX_P HELX_P4 AA4 ALA A 94  ? GLY A 107 ? ALA A 99  GLY A 112 1 ? 14 
HELX_P HELX_P5 AA5 LYS A 117 ? SER A 124 ? LYS A 122 SER A 129 5 ? 8  
HELX_P HELX_P6 AA6 LYS A 127 ? LYS A 139 ? LYS A 132 LYS A 144 1 ? 13 
HELX_P HELX_P7 AA7 ASN A 152 ? GLN A 166 ? ASN A 157 GLN A 171 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 23  A MG  202 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc2 metalc ? ? A THR 36 OG1 ? ? ? 1_555 C MG  . MG ? ? A THR 41  A MG  202 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
metalc3 metalc ? ? B GNP .  O1G ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.056 ? ? 
metalc4 metalc ? ? B GNP .  O2B ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.115 ? ? 
metalc5 metalc ? ? C MG  .  MG  ? ? ? 1_555 D HOH . O  ? ? A MG  202 A HOH 315 1_555 ? ? ? ? ? ? ? 2.111 ? ? 
metalc6 metalc ? ? C MG  .  MG  ? ? ? 1_555 D HOH . O  ? ? A MG  202 A HOH 331 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
# 
_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 23  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 OG1 ? A THR 36 ? A THR 41  ? 1_555 78.2  ? 
2  OG  ? A SER 18 ? A SER 23  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O1G ? B GNP .  ? A GNP 201 ? 1_555 172.5 ? 
3  OG1 ? A THR 36 ? A THR 41  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O1G ? B GNP .  ? A GNP 201 ? 1_555 94.9  ? 
4  OG  ? A SER 18 ? A SER 23  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O2B ? B GNP .  ? A GNP 201 ? 1_555 90.4  ? 
5  OG1 ? A THR 36 ? A THR 41  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O2B ? B GNP .  ? A GNP 201 ? 1_555 168.4 ? 
6  O1G ? B GNP .  ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O2B ? B GNP .  ? A GNP 201 ? 1_555 96.6  ? 
7  OG  ? A SER 18 ? A SER 23  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? D HOH .  ? A HOH 315 ? 1_555 89.2  ? 
8  OG1 ? A THR 36 ? A THR 41  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? D HOH .  ? A HOH 315 ? 1_555 90.4  ? 
9  O1G ? B GNP .  ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? D HOH .  ? A HOH 315 ? 1_555 93.7  ? 
10 O2B ? B GNP .  ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? D HOH .  ? A HOH 315 ? 1_555 87.5  ? 
11 OG  ? A SER 18 ? A SER 23  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? D HOH .  ? A HOH 331 ? 1_555 85.2  ? 
12 OG1 ? A THR 36 ? A THR 41  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? D HOH .  ? A HOH 331 ? 1_555 91.2  ? 
13 O1G ? B GNP .  ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? D HOH .  ? A HOH 331 ? 1_555 92.1  ? 
14 O2B ? B GNP .  ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? D HOH .  ? A HOH 331 ? 1_555 89.8  ? 
15 O   ? D HOH .  ? A HOH 315 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? D HOH .  ? A HOH 331 ? 1_555 173.8 ? 
# 
_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 VAL A 39  ? GLN A 47  ? VAL A 44  GLN A 52  
AA1 2 ASP A 52  ? THR A 60  ? ASP A 57  THR A 65  
AA1 3 VAL A 3   ? VAL A 10  ? VAL A 8   VAL A 15  
AA1 4 ALA A 79  ? SER A 85  ? ALA A 84  SER A 90  
AA1 5 THR A 111 ? ASN A 116 ? THR A 116 ASN A 121 
AA1 6 ARG A 141 ? ARG A 144 ? ARG A 146 ARG A 149 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 44  ? N ARG A 49  O LEU A 55  ? O LEU A 60  
AA1 2 3 O MET A 56  ? O MET A 61  N ILE A 5   ? N ILE A 10  
AA1 3 4 N VAL A 10  ? N VAL A 15  O VAL A 83  ? O VAL A 88  
AA1 4 5 N LEU A 82  ? N LEU A 87  O VAL A 114 ? O VAL A 119 
AA1 5 6 N LEU A 113 ? N LEU A 118 O ARG A 141 ? O ARG A 146 
# 
_pdbx_entry_details.entry_id                   8YIM 
_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 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 54  ? ? 54.65   -121.96 
2 1 ASP A 55  ? ? -112.73 63.98   
3 1 LEU A 125 ? ? -94.39  35.01   
# 
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 486 ? D HOH . 
2 1 A HOH 492 ? D HOH . 
# 
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 SER 6   ? A SER 1   
2 1 Y 1 A GLU 69  ? A GLU 64  
3 1 Y 1 A GLU 70  ? A GLU 65  
4 1 Y 1 A PHE 71  ? A PHE 66  
5 1 Y 1 A ASP 72  ? A ASP 67  
6 1 Y 1 A ALA 73  ? A ALA 68  
7 1 Y 1 A LYS 172 ? A LYS 167 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
GNP PG     P  N N 137 
GNP O1G    O  N N 138 
GNP O2G    O  N N 139 
GNP O3G    O  N N 140 
GNP N3B    N  N N 141 
GNP PB     P  N R 142 
GNP O1B    O  N N 143 
GNP O2B    O  N N 144 
GNP O3A    O  N N 145 
GNP PA     P  N S 146 
GNP O1A    O  N N 147 
GNP O2A    O  N N 148 
GNP "O5'"  O  N N 149 
GNP "C5'"  C  N N 150 
GNP "C4'"  C  N R 151 
GNP "O4'"  O  N N 152 
GNP "C3'"  C  N S 153 
GNP "O3'"  O  N N 154 
GNP "C2'"  C  N R 155 
GNP "O2'"  O  N N 156 
GNP "C1'"  C  N R 157 
GNP N9     N  Y N 158 
GNP C8     C  Y N 159 
GNP N7     N  Y N 160 
GNP C5     C  Y N 161 
GNP C6     C  Y N 162 
GNP O6     O  N N 163 
GNP N1     N  Y N 164 
GNP C2     C  Y N 165 
GNP N2     N  N N 166 
GNP N3     N  Y N 167 
GNP C4     C  Y N 168 
GNP HOG2   H  N N 169 
GNP HOG3   H  N N 170 
GNP HNB3   H  N N 171 
GNP HOB2   H  N N 172 
GNP HOA2   H  N N 173 
GNP "H5'2" H  N N 174 
GNP "H5'1" H  N N 175 
GNP "H4'"  H  N N 176 
GNP "H3'"  H  N N 177 
GNP "HO3'" H  N N 178 
GNP "H2'"  H  N N 179 
GNP "HO2'" H  N N 180 
GNP "H1'"  H  N N 181 
GNP H8     H  N N 182 
GNP HN1    H  N N 183 
GNP HN21   H  N N 184 
GNP HN22   H  N N 185 
HOH O      O  N N 186 
HOH H1     H  N N 187 
HOH H2     H  N N 188 
ILE N      N  N N 189 
ILE CA     C  N S 190 
ILE C      C  N N 191 
ILE O      O  N N 192 
ILE CB     C  N S 193 
ILE CG1    C  N N 194 
ILE CG2    C  N N 195 
ILE CD1    C  N N 196 
ILE OXT    O  N N 197 
ILE H      H  N N 198 
ILE H2     H  N N 199 
ILE HA     H  N N 200 
ILE HB     H  N N 201 
ILE HG12   H  N N 202 
ILE HG13   H  N N 203 
ILE HG21   H  N N 204 
ILE HG22   H  N N 205 
ILE HG23   H  N N 206 
ILE HD11   H  N N 207 
ILE HD12   H  N N 208 
ILE HD13   H  N N 209 
ILE HXT    H  N N 210 
LEU N      N  N N 211 
LEU CA     C  N S 212 
LEU C      C  N N 213 
LEU O      O  N N 214 
LEU CB     C  N N 215 
LEU CG     C  N N 216 
LEU CD1    C  N N 217 
LEU CD2    C  N N 218 
LEU OXT    O  N N 219 
LEU H      H  N N 220 
LEU H2     H  N N 221 
LEU HA     H  N N 222 
LEU HB2    H  N N 223 
LEU HB3    H  N N 224 
LEU HG     H  N N 225 
LEU HD11   H  N N 226 
LEU HD12   H  N N 227 
LEU HD13   H  N N 228 
LEU HD21   H  N N 229 
LEU HD22   H  N N 230 
LEU HD23   H  N N 231 
LEU HXT    H  N N 232 
LYS N      N  N N 233 
LYS CA     C  N S 234 
LYS C      C  N N 235 
LYS O      O  N N 236 
LYS CB     C  N N 237 
LYS CG     C  N N 238 
LYS CD     C  N N 239 
LYS CE     C  N N 240 
LYS NZ     N  N N 241 
LYS OXT    O  N N 242 
LYS H      H  N N 243 
LYS H2     H  N N 244 
LYS HA     H  N N 245 
LYS HB2    H  N N 246 
LYS HB3    H  N N 247 
LYS HG2    H  N N 248 
LYS HG3    H  N N 249 
LYS HD2    H  N N 250 
LYS HD3    H  N N 251 
LYS HE2    H  N N 252 
LYS HE3    H  N N 253 
LYS HZ1    H  N N 254 
LYS HZ2    H  N N 255 
LYS HZ3    H  N N 256 
LYS HXT    H  N N 257 
MET N      N  N N 258 
MET CA     C  N S 259 
MET C      C  N N 260 
MET O      O  N N 261 
MET CB     C  N N 262 
MET CG     C  N N 263 
MET SD     S  N N 264 
MET CE     C  N N 265 
MET OXT    O  N N 266 
MET H      H  N N 267 
MET H2     H  N N 268 
MET HA     H  N N 269 
MET HB2    H  N N 270 
MET HB3    H  N N 271 
MET HG2    H  N N 272 
MET HG3    H  N N 273 
MET HE1    H  N N 274 
MET HE2    H  N N 275 
MET HE3    H  N N 276 
MET HXT    H  N N 277 
MG  MG     MG N N 278 
PHE N      N  N N 279 
PHE CA     C  N S 280 
PHE C      C  N N 281 
PHE O      O  N N 282 
PHE CB     C  N N 283 
PHE CG     C  Y N 284 
PHE CD1    C  Y N 285 
PHE CD2    C  Y N 286 
PHE CE1    C  Y N 287 
PHE CE2    C  Y N 288 
PHE CZ     C  Y N 289 
PHE OXT    O  N N 290 
PHE H      H  N N 291 
PHE H2     H  N N 292 
PHE HA     H  N N 293 
PHE HB2    H  N N 294 
PHE HB3    H  N N 295 
PHE HD1    H  N N 296 
PHE HD2    H  N N 297 
PHE HE1    H  N N 298 
PHE HE2    H  N N 299 
PHE HZ     H  N N 300 
PHE HXT    H  N N 301 
PRO N      N  N N 302 
PRO CA     C  N S 303 
PRO C      C  N N 304 
PRO O      O  N N 305 
PRO CB     C  N N 306 
PRO CG     C  N N 307 
PRO CD     C  N N 308 
PRO OXT    O  N N 309 
PRO H      H  N N 310 
PRO HA     H  N N 311 
PRO HB2    H  N N 312 
PRO HB3    H  N N 313 
PRO HG2    H  N N 314 
PRO HG3    H  N N 315 
PRO HD2    H  N N 316 
PRO HD3    H  N N 317 
PRO HXT    H  N N 318 
SER N      N  N N 319 
SER CA     C  N S 320 
SER C      C  N N 321 
SER O      O  N N 322 
SER CB     C  N N 323 
SER OG     O  N N 324 
SER OXT    O  N N 325 
SER H      H  N N 326 
SER H2     H  N N 327 
SER HA     H  N N 328 
SER HB2    H  N N 329 
SER HB3    H  N N 330 
SER HG     H  N N 331 
SER HXT    H  N N 332 
THR N      N  N N 333 
THR CA     C  N S 334 
THR C      C  N N 335 
THR O      O  N N 336 
THR CB     C  N R 337 
THR OG1    O  N N 338 
THR CG2    C  N N 339 
THR OXT    O  N N 340 
THR H      H  N N 341 
THR H2     H  N N 342 
THR HA     H  N N 343 
THR HB     H  N N 344 
THR HG1    H  N N 345 
THR HG21   H  N N 346 
THR HG22   H  N N 347 
THR HG23   H  N N 348 
THR HXT    H  N N 349 
TRP N      N  N N 350 
TRP CA     C  N S 351 
TRP C      C  N N 352 
TRP O      O  N N 353 
TRP CB     C  N N 354 
TRP CG     C  Y N 355 
TRP CD1    C  Y N 356 
TRP CD2    C  Y N 357 
TRP NE1    N  Y N 358 
TRP CE2    C  Y N 359 
TRP CE3    C  Y N 360 
TRP CZ2    C  Y N 361 
TRP CZ3    C  Y N 362 
TRP CH2    C  Y N 363 
TRP OXT    O  N N 364 
TRP H      H  N N 365 
TRP H2     H  N N 366 
TRP HA     H  N N 367 
TRP HB2    H  N N 368 
TRP HB3    H  N N 369 
TRP HD1    H  N N 370 
TRP HE1    H  N N 371 
TRP HE3    H  N N 372 
TRP HZ2    H  N N 373 
TRP HZ3    H  N N 374 
TRP HH2    H  N N 375 
TRP HXT    H  N N 376 
TYR N      N  N N 377 
TYR CA     C  N S 378 
TYR C      C  N N 379 
TYR O      O  N N 380 
TYR CB     C  N N 381 
TYR CG     C  Y N 382 
TYR CD1    C  Y N 383 
TYR CD2    C  Y N 384 
TYR CE1    C  Y N 385 
TYR CE2    C  Y N 386 
TYR CZ     C  Y N 387 
TYR OH     O  N N 388 
TYR OXT    O  N N 389 
TYR H      H  N N 390 
TYR H2     H  N N 391 
TYR HA     H  N N 392 
TYR HB2    H  N N 393 
TYR HB3    H  N N 394 
TYR HD1    H  N N 395 
TYR HD2    H  N N 396 
TYR HE1    H  N N 397 
TYR HE2    H  N N 398 
TYR HH     H  N N 399 
TYR HXT    H  N N 400 
VAL N      N  N N 401 
VAL CA     C  N S 402 
VAL C      C  N N 403 
VAL O      O  N N 404 
VAL CB     C  N N 405 
VAL CG1    C  N N 406 
VAL CG2    C  N N 407 
VAL OXT    O  N N 408 
VAL H      H  N N 409 
VAL H2     H  N N 410 
VAL HA     H  N N 411 
VAL HB     H  N N 412 
VAL HG11   H  N N 413 
VAL HG12   H  N N 414 
VAL HG13   H  N N 415 
VAL HG21   H  N N 416 
VAL HG22   H  N N 417 
VAL HG23   H  N N 418 
VAL HXT    H  N N 419 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
GNP PG    O1G    doub N N 129 
GNP PG    O2G    sing N N 130 
GNP PG    O3G    sing N N 131 
GNP PG    N3B    sing N N 132 
GNP O2G   HOG2   sing N N 133 
GNP O3G   HOG3   sing N N 134 
GNP N3B   PB     sing N N 135 
GNP N3B   HNB3   sing N N 136 
GNP PB    O1B    doub N N 137 
GNP PB    O2B    sing N N 138 
GNP PB    O3A    sing N N 139 
GNP O2B   HOB2   sing N N 140 
GNP O3A   PA     sing N N 141 
GNP PA    O1A    doub N N 142 
GNP PA    O2A    sing N N 143 
GNP PA    "O5'"  sing N N 144 
GNP O2A   HOA2   sing N N 145 
GNP "O5'" "C5'"  sing N N 146 
GNP "C5'" "C4'"  sing N N 147 
GNP "C5'" "H5'2" sing N N 148 
GNP "C5'" "H5'1" sing N N 149 
GNP "C4'" "O4'"  sing N N 150 
GNP "C4'" "C3'"  sing N N 151 
GNP "C4'" "H4'"  sing N N 152 
GNP "O4'" "C1'"  sing N N 153 
GNP "C3'" "O3'"  sing N N 154 
GNP "C3'" "C2'"  sing N N 155 
GNP "C3'" "H3'"  sing N N 156 
GNP "O3'" "HO3'" sing N N 157 
GNP "C2'" "O2'"  sing N N 158 
GNP "C2'" "C1'"  sing N N 159 
GNP "C2'" "H2'"  sing N N 160 
GNP "O2'" "HO2'" sing N N 161 
GNP "C1'" N9     sing N N 162 
GNP "C1'" "H1'"  sing N N 163 
GNP N9    C8     sing Y N 164 
GNP N9    C4     sing Y N 165 
GNP C8    N7     doub Y N 166 
GNP C8    H8     sing N N 167 
GNP N7    C5     sing Y N 168 
GNP C5    C6     sing Y N 169 
GNP C5    C4     doub Y N 170 
GNP C6    O6     doub N N 171 
GNP C6    N1     sing Y N 172 
GNP N1    C2     sing Y N 173 
GNP N1    HN1    sing N N 174 
GNP C2    N2     sing N N 175 
GNP C2    N3     doub Y N 176 
GNP N2    HN21   sing N N 177 
GNP N2    HN22   sing N N 178 
GNP N3    C4     sing Y N 179 
HOH O     H1     sing N N 180 
HOH O     H2     sing N N 181 
ILE N     CA     sing N N 182 
ILE N     H      sing N N 183 
ILE N     H2     sing N N 184 
ILE CA    C      sing N N 185 
ILE CA    CB     sing N N 186 
ILE CA    HA     sing N N 187 
ILE C     O      doub N N 188 
ILE C     OXT    sing N N 189 
ILE CB    CG1    sing N N 190 
ILE CB    CG2    sing N N 191 
ILE CB    HB     sing N N 192 
ILE CG1   CD1    sing N N 193 
ILE CG1   HG12   sing N N 194 
ILE CG1   HG13   sing N N 195 
ILE CG2   HG21   sing N N 196 
ILE CG2   HG22   sing N N 197 
ILE CG2   HG23   sing N N 198 
ILE CD1   HD11   sing N N 199 
ILE CD1   HD12   sing N N 200 
ILE CD1   HD13   sing N N 201 
ILE OXT   HXT    sing N N 202 
LEU N     CA     sing N N 203 
LEU N     H      sing N N 204 
LEU N     H2     sing N N 205 
LEU CA    C      sing N N 206 
LEU CA    CB     sing N N 207 
LEU CA    HA     sing N N 208 
LEU C     O      doub N N 209 
LEU C     OXT    sing N N 210 
LEU CB    CG     sing N N 211 
LEU CB    HB2    sing N N 212 
LEU CB    HB3    sing N N 213 
LEU CG    CD1    sing N N 214 
LEU CG    CD2    sing N N 215 
LEU CG    HG     sing N N 216 
LEU CD1   HD11   sing N N 217 
LEU CD1   HD12   sing N N 218 
LEU CD1   HD13   sing N N 219 
LEU CD2   HD21   sing N N 220 
LEU CD2   HD22   sing N N 221 
LEU CD2   HD23   sing N N 222 
LEU OXT   HXT    sing N N 223 
LYS N     CA     sing N N 224 
LYS N     H      sing N N 225 
LYS N     H2     sing N N 226 
LYS CA    C      sing N N 227 
LYS CA    CB     sing N N 228 
LYS CA    HA     sing N N 229 
LYS C     O      doub N N 230 
LYS C     OXT    sing N N 231 
LYS CB    CG     sing N N 232 
LYS CB    HB2    sing N N 233 
LYS CB    HB3    sing N N 234 
LYS CG    CD     sing N N 235 
LYS CG    HG2    sing N N 236 
LYS CG    HG3    sing N N 237 
LYS CD    CE     sing N N 238 
LYS CD    HD2    sing N N 239 
LYS CD    HD3    sing N N 240 
LYS CE    NZ     sing N N 241 
LYS CE    HE2    sing N N 242 
LYS CE    HE3    sing N N 243 
LYS NZ    HZ1    sing N N 244 
LYS NZ    HZ2    sing N N 245 
LYS NZ    HZ3    sing N N 246 
LYS OXT   HXT    sing N N 247 
MET N     CA     sing N N 248 
MET N     H      sing N N 249 
MET N     H2     sing N N 250 
MET CA    C      sing N N 251 
MET CA    CB     sing N N 252 
MET CA    HA     sing N N 253 
MET C     O      doub N N 254 
MET C     OXT    sing N N 255 
MET CB    CG     sing N N 256 
MET CB    HB2    sing N N 257 
MET CB    HB3    sing N N 258 
MET CG    SD     sing N N 259 
MET CG    HG2    sing N N 260 
MET CG    HG3    sing N N 261 
MET SD    CE     sing N N 262 
MET CE    HE1    sing N N 263 
MET CE    HE2    sing N N 264 
MET CE    HE3    sing N N 265 
MET OXT   HXT    sing N N 266 
PHE N     CA     sing N N 267 
PHE N     H      sing N N 268 
PHE N     H2     sing N N 269 
PHE CA    C      sing N N 270 
PHE CA    CB     sing N N 271 
PHE CA    HA     sing N N 272 
PHE C     O      doub N N 273 
PHE C     OXT    sing N N 274 
PHE CB    CG     sing N N 275 
PHE CB    HB2    sing N N 276 
PHE CB    HB3    sing N N 277 
PHE CG    CD1    doub Y N 278 
PHE CG    CD2    sing Y N 279 
PHE CD1   CE1    sing Y N 280 
PHE CD1   HD1    sing N N 281 
PHE CD2   CE2    doub Y N 282 
PHE CD2   HD2    sing N N 283 
PHE CE1   CZ     doub Y N 284 
PHE CE1   HE1    sing N N 285 
PHE CE2   CZ     sing Y N 286 
PHE CE2   HE2    sing N N 287 
PHE CZ    HZ     sing N N 288 
PHE OXT   HXT    sing N N 289 
PRO N     CA     sing N N 290 
PRO N     CD     sing N N 291 
PRO N     H      sing N N 292 
PRO CA    C      sing N N 293 
PRO CA    CB     sing N N 294 
PRO CA    HA     sing N N 295 
PRO C     O      doub N N 296 
PRO C     OXT    sing N N 297 
PRO CB    CG     sing N N 298 
PRO CB    HB2    sing N N 299 
PRO CB    HB3    sing N N 300 
PRO CG    CD     sing N N 301 
PRO CG    HG2    sing N N 302 
PRO CG    HG3    sing N N 303 
PRO CD    HD2    sing N N 304 
PRO CD    HD3    sing N N 305 
PRO OXT   HXT    sing N N 306 
SER N     CA     sing N N 307 
SER N     H      sing N N 308 
SER N     H2     sing N N 309 
SER CA    C      sing N N 310 
SER CA    CB     sing N N 311 
SER CA    HA     sing N N 312 
SER C     O      doub N N 313 
SER C     OXT    sing N N 314 
SER CB    OG     sing N N 315 
SER CB    HB2    sing N N 316 
SER CB    HB3    sing N N 317 
SER OG    HG     sing N N 318 
SER OXT   HXT    sing N N 319 
THR N     CA     sing N N 320 
THR N     H      sing N N 321 
THR N     H2     sing N N 322 
THR CA    C      sing N N 323 
THR CA    CB     sing N N 324 
THR CA    HA     sing N N 325 
THR C     O      doub N N 326 
THR C     OXT    sing N N 327 
THR CB    OG1    sing N N 328 
THR CB    CG2    sing N N 329 
THR CB    HB     sing N N 330 
THR OG1   HG1    sing N N 331 
THR CG2   HG21   sing N N 332 
THR CG2   HG22   sing N N 333 
THR CG2   HG23   sing N N 334 
THR OXT   HXT    sing N N 335 
TRP N     CA     sing N N 336 
TRP N     H      sing N N 337 
TRP N     H2     sing N N 338 
TRP CA    C      sing N N 339 
TRP CA    CB     sing N N 340 
TRP CA    HA     sing N N 341 
TRP C     O      doub N N 342 
TRP C     OXT    sing N N 343 
TRP CB    CG     sing N N 344 
TRP CB    HB2    sing N N 345 
TRP CB    HB3    sing N N 346 
TRP CG    CD1    doub Y N 347 
TRP CG    CD2    sing Y N 348 
TRP CD1   NE1    sing Y N 349 
TRP CD1   HD1    sing N N 350 
TRP CD2   CE2    doub Y N 351 
TRP CD2   CE3    sing Y N 352 
TRP NE1   CE2    sing Y N 353 
TRP NE1   HE1    sing N N 354 
TRP CE2   CZ2    sing Y N 355 
TRP CE3   CZ3    doub Y N 356 
TRP CE3   HE3    sing N N 357 
TRP CZ2   CH2    doub Y N 358 
TRP CZ2   HZ2    sing N N 359 
TRP CZ3   CH2    sing Y N 360 
TRP CZ3   HZ3    sing N N 361 
TRP CH2   HH2    sing N N 362 
TRP OXT   HXT    sing N N 363 
TYR N     CA     sing N N 364 
TYR N     H      sing N N 365 
TYR N     H2     sing N N 366 
TYR CA    C      sing N N 367 
TYR CA    CB     sing N N 368 
TYR CA    HA     sing N N 369 
TYR C     O      doub N N 370 
TYR C     OXT    sing N N 371 
TYR CB    CG     sing N N 372 
TYR CB    HB2    sing N N 373 
TYR CB    HB3    sing N N 374 
TYR CG    CD1    doub Y N 375 
TYR CG    CD2    sing Y N 376 
TYR CD1   CE1    sing Y N 377 
TYR CD1   HD1    sing N N 378 
TYR CD2   CE2    doub Y N 379 
TYR CD2   HD2    sing N N 380 
TYR CE1   CZ     doub Y N 381 
TYR CE1   HE1    sing N N 382 
TYR CE2   CZ     sing Y N 383 
TYR CE2   HE2    sing N N 384 
TYR CZ    OH     sing N N 385 
TYR OH    HH     sing N N 386 
TYR OXT   HXT    sing N N 387 
VAL N     CA     sing N N 388 
VAL N     H      sing N N 389 
VAL N     H2     sing N N 390 
VAL CA    C      sing N N 391 
VAL CA    CB     sing N N 392 
VAL CA    HA     sing N N 393 
VAL C     O      doub N N 394 
VAL C     OXT    sing N N 395 
VAL CB    CG1    sing N N 396 
VAL CB    CG2    sing N N 397 
VAL CB    HB     sing N N 398 
VAL CG1   HG11   sing N N 399 
VAL CG1   HG12   sing N N 400 
VAL CG1   HG13   sing N N 401 
VAL CG2   HG21   sing N N 402 
VAL CG2   HG22   sing N N 403 
VAL CG2   HG23   sing N N 404 
VAL OXT   HXT    sing N N 405 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'Hong Kong' 
_pdbx_audit_support.grant_number           'HKBU Faculty of Science Seed Money' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Structure of human Rab23-GDP complex' 
# 
_atom_sites.entry_id                    8YIM 
_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]   0.016523 
_atom_sites.fract_transf_matrix[1][2]   0.009539 
_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]   0.019079 
_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]   0.010647 
_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  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLU A 1 2   ? -8.88566  -6.15551 -5.12802  1.000 39.14075 ?  7   GLU A N     1 
ATOM   2    C  CA    . GLU A 1 2   ? -9.88932  -5.13496 -4.84373  1.000 37.96725 ?  7   GLU A CA    1 
ATOM   3    C  C     . GLU A 1 2   ? -10.37126 -5.21418 -3.39883  1.000 34.88851 ?  7   GLU A C     1 
ATOM   4    O  O     . GLU A 1 2   ? -10.71123 -6.28819 -2.90418  1.000 37.05272 ?  7   GLU A O     1 
ATOM   5    C  CB    . GLU A 1 2   ? -11.07459 -5.26309 -5.80494  1.000 40.76511 ?  7   GLU A CB    1 
ATOM   6    C  CG    . GLU A 1 2   ? -12.28459 -4.42618 -5.42168  1.000 42.68265 ?  7   GLU A CG    1 
ATOM   7    C  CD    . GLU A 1 2   ? -13.38840 -4.48408 -6.46041  1.000 44.43251 ?  7   GLU A CD    1 
ATOM   8    O  OE1   . GLU A 1 2   ? -13.25914 -3.81360 -7.50647  1.000 45.29466 ?  7   GLU A OE1   1 
ATOM   9    O  OE2   . GLU A 1 2   ? -14.38209 -5.20640 -6.23410  1.000 45.03697 ?  7   GLU A OE2   1 
ATOM   10   N  N     . VAL A 1 3   ? -10.39589 -4.06764 -2.72690  1.000 29.21155 ?  8   VAL A N     1 
ATOM   11   C  CA    . VAL A 1 3   ? -10.84695 -3.96993 -1.34419  1.000 26.82252 ?  8   VAL A CA    1 
ATOM   12   C  C     . VAL A 1 3   ? -12.28802 -3.47917 -1.34945  1.000 24.36596 ?  8   VAL A C     1 
ATOM   13   O  O     . VAL A 1 3   ? -12.59434 -2.43223 -1.93243  1.000 24.15307 ?  8   VAL A O     1 
ATOM   14   C  CB    . VAL A 1 3   ? -9.94660  -3.02878 -0.52864  1.000 27.72029 ?  8   VAL A CB    1 
ATOM   15   C  CG1   . VAL A 1 3   ? -10.47365 -2.88932 0.89249   1.000 28.87992 ?  8   VAL A CG1   1 
ATOM   16   C  CG2   . VAL A 1 3   ? -8.51042  -3.53537 -0.52710  1.000 28.92833 ?  8   VAL A CG2   1 
ATOM   17   N  N     . ALA A 1 4   ? -13.17407 -4.23497 -0.70970  1.000 21.01992 ?  9   ALA A N     1 
ATOM   18   C  CA    . ALA A 1 4   ? -14.57158 -3.85374 -0.57001  1.000 19.27997 ?  9   ALA A CA    1 
ATOM   19   C  C     . ALA A 1 4   ? -14.78961 -3.23617 0.80387   1.000 17.66712 ?  9   ALA A C     1 
ATOM   20   O  O     . ALA A 1 4   ? -14.28009 -3.74127 1.80889   1.000 20.30493 ?  9   ALA A O     1 
ATOM   21   C  CB    . ALA A 1 4   ? -15.48238 -5.07079 -0.74027  1.000 21.41631 ?  9   ALA A CB    1 
ATOM   22   N  N     . ILE A 1 5   ? -15.53775 -2.13422 0.84074   1.000 14.78763 ?  10  ILE A N     1 
ATOM   23   C  CA    . ILE A 1 5   ? -15.82754 -1.41284 2.07605   1.000 13.58514 ?  10  ILE A CA    1 
ATOM   24   C  C     . ILE A 1 5   ? -17.33336 -1.21183 2.16318   1.000 13.13862 ?  10  ILE A C     1 
ATOM   25   O  O     . ILE A 1 5   ? -17.92285 -0.55766 1.29581   1.000 13.57052 ?  10  ILE A O     1 
ATOM   26   C  CB    . ILE A 1 5   ? -15.11768 -0.04869 2.12861   1.000 13.84007 ?  10  ILE A CB    1 
ATOM   27   C  CG1   . ILE A 1 5   ? -13.62550 -0.18674 1.81872   1.000 16.05076 ?  10  ILE A CG1   1 
ATOM   28   C  CG2   . ILE A 1 5   ? -15.32198 0.59616  3.48976   1.000 14.35488 ?  10  ILE A CG2   1 
ATOM   29   C  CD1   . ILE A 1 5   ? -12.91630 1.14746  1.68952   1.000 17.80173 ?  10  ILE A CD1   1 
ATOM   30   N  N     . LYS A 1 6   ? -17.95228 -1.75896 3.20689   1.000 11.93853 ?  11  LYS A N     1 
ATOM   31   C  CA    . LYS A 1 6   ? -19.36299 -1.50090 3.46048   1.000 11.14470 ?  11  LYS A CA    1 
ATOM   32   C  C     . LYS A 1 6   ? -19.51522 -0.17723 4.19572   1.000 10.96572 ?  11  LYS A C     1 
ATOM   33   O  O     . LYS A 1 6   ? -18.88999 0.04224  5.23723   1.000 12.77320 ?  11  LYS A O     1 
ATOM   34   C  CB    . LYS A 1 6   ? -19.98873 -2.61903 4.29517   1.000 12.96646 ?  11  LYS A CB    1 
ATOM   35   C  CG    . LYS A 1 6   ? -21.40000 -2.27046 4.75598   1.000 12.39185 ?  11  LYS A CG    1 
ATOM   36   C  CD    . LYS A 1 6   ? -22.08835 -3.40493 5.48844   1.000 12.69510 ?  11  LYS A CD    1 
ATOM   37   C  CE    . LYS A 1 6   ? -23.40663 -2.92396 6.08070   1.000 13.24449 ?  11  LYS A CE    1 
ATOM   38   N  NZ    . LYS A 1 6   ? -24.23669 -4.02167 6.63679   1.000 13.08165 ?  11  LYS A NZ    1 
ATOM   39   N  N     . MET A 1 7   ? -20.35250 0.70132  3.66220   1.000 10.10857 ?  12  MET A N     1 
ATOM   40   C  CA    . MET A 1 7   ? -20.60908 1.98303  4.29632   1.000 9.13766  ?  12  MET A CA    1 
ATOM   41   C  C     . MET A 1 7   ? -22.10288 2.16327  4.48704   1.000 9.55776  ?  12  MET A C     1 
ATOM   42   O  O     . MET A 1 7   ? -22.89639 1.83187  3.60146   1.000 10.65960 ?  12  MET A O     1 
ATOM   43   C  CB    . MET A 1 7   ? -20.05923 3.14075  3.46658   1.000 10.91509 ?  12  MET A CB    1 
ATOM   44   C  CG    . MET A 1 7   ? -18.57683 3.03856  3.19995   1.000 11.71306 ?  12  MET A CG    1 
ATOM   45   S  SD    . MET A 1 7   ? -17.92960 4.55165  2.48780   1.000 13.40951 ?  12  MET A SD    1 
ATOM   46   C  CE    . MET A 1 7   ? -16.18097 4.17423  2.43513   1.000 14.38063 ?  12  MET A CE    1 
ATOM   47   N  N     . VAL A 1 8   ? -22.47664 2.68165  5.64915   1.000 9.22732  ?  13  VAL A N     1 
ATOM   48   C  CA    . VAL A 1 8   ? -23.85701 3.03446  5.93807   1.000 8.88499  ?  13  VAL A CA    1 
ATOM   49   C  C     . VAL A 1 8   ? -23.98796 4.54923  5.92199   1.000 8.33189  ?  13  VAL A C     1 
ATOM   50   O  O     . VAL A 1 8   ? -23.01918 5.28600  6.13486   1.000 9.06404  ?  13  VAL A O     1 
ATOM   51   C  CB    . VAL A 1 8   ? -24.36365 2.43007  7.26535   1.000 10.30763 ?  13  VAL A CB    1 
ATOM   52   C  CG1   . VAL A 1 8   ? -24.37755 0.91096  7.17087   1.000 12.04778 ?  13  VAL A CG1   1 
ATOM   53   C  CG2   . VAL A 1 8   ? -23.50541 2.89844  8.43755   1.000 10.73783 ?  13  VAL A CG2   1 
ATOM   54   N  N     . VAL A 1 9   ? -25.19901 5.01081  5.63573   1.000 7.50935  ?  14  VAL A N     1 
ATOM   55   C  CA    . VAL A 1 9   ? -25.51964 6.42905  5.56227   1.000 7.41012  ?  14  VAL A CA    1 
ATOM   56   C  C     . VAL A 1 9   ? -26.80482 6.60601  6.35039   1.000 7.12460  ?  14  VAL A C     1 
ATOM   57   O  O     . VAL A 1 9   ? -27.83850 6.03649  5.98307   1.000 8.50655  ?  14  VAL A O     1 
ATOM   58   C  CB    . VAL A 1 9   ? -25.70627 6.88756  4.10398   1.000 8.09321  ?  14  VAL A CB    1 
ATOM   59   C  CG1   . VAL A 1 9   ? -26.12220 8.35023  4.04069   1.000 8.78346  ?  14  VAL A CG1   1 
ATOM   60   C  CG2   . VAL A 1 9   ? -24.42914 6.64898  3.29636   1.000 9.47502  ?  14  VAL A CG2   1 
ATOM   61   N  N     . VAL A 1 10  ? -26.73842 7.35787  7.44886   1.000 6.64609  ?  15  VAL A N     1 
ATOM   62   C  CA    . VAL A 1 10  ? -27.84747 7.43187  8.38924   1.000 6.67346  ?  15  VAL A CA    1 
ATOM   63   C  C     . VAL A 1 10  ? -28.21743 8.88318  8.66241   1.000 6.13223  ?  15  VAL A C     1 
ATOM   64   O  O     . VAL A 1 10  ? -27.40749 9.80117  8.51695   1.000 8.14390  ?  15  VAL A O     1 
ATOM   65   C  CB    . VAL A 1 10  ? -27.58168 6.66870  9.70716   1.000 10.39702 ?  15  VAL A CB    1 
ATOM   66   C  CG1   . VAL A 1 10  ? -27.37918 5.18468  9.42941   1.000 11.67517 ?  15  VAL A CG1   1 
ATOM   67   C  CG2   . VAL A 1 10  ? -26.38189 7.25168  10.42808  1.000 11.13036 ?  15  VAL A CG2   1 
ATOM   68   N  N     . GLY A 1 11  ? -29.45814 9.06912  9.07148   1.000 5.77333  ?  16  GLY A N     1 
ATOM   69   C  CA    . GLY A 1 11  ? -30.01572 10.38885 9.29090   1.000 6.57713  ?  16  GLY A CA    1 
ATOM   70   C  C     . GLY A 1 11  ? -31.51910 10.34354 9.12980   1.000 5.94307  ?  16  GLY A C     1 
ATOM   71   O  O     . GLY A 1 11  ? -32.08765 9.38812  8.60582   1.000 7.30677  ?  16  GLY A O     1 
ATOM   72   N  N     . ASN A 1 12  ? -32.16486 11.41242 9.58471   1.000 6.73948  ?  17  ASN A N     1 
ATOM   73   C  CA    . ASN A 1 12  ? -33.61998 11.45882 9.58895   1.000 6.89374  ?  17  ASN A CA    1 
ATOM   74   C  C     . ASN A 1 12  ? -34.19003 11.33080 8.17798   1.000 6.48015  ?  17  ASN A C     1 
ATOM   75   O  O     . ASN A 1 12  ? -33.50444 11.53295 7.16750   1.000 6.79436  ?  17  ASN A O     1 
ATOM   76   C  CB    . ASN A 1 12  ? -34.10440 12.76249 10.21702  1.000 7.72239  ?  17  ASN A CB    1 
ATOM   77   C  CG    . ASN A 1 12  ? -34.16192 12.68880 11.72576  1.000 8.89298  ?  17  ASN A CG    1 
ATOM   78   O  OD1   . ASN A 1 12  ? -33.55277 11.80557 12.33416  1.000 9.41424  ?  17  ASN A OD1   1 
ATOM   79   N  ND2   . ASN A 1 12  ? -34.89791 13.61269 12.34156  1.000 9.97354  ?  17  ASN A ND2   1 
ATOM   80   N  N     . GLY A 1 13  ? -35.47382 10.99112 8.12013   1.000 7.51963  ?  18  GLY A N     1 
ATOM   81   C  CA    . GLY A 1 13  ? -36.13727 10.88964 6.83284   1.000 7.28662  ?  18  GLY A CA    1 
ATOM   82   C  C     . GLY A 1 13  ? -36.02740 12.18598 6.04989   1.000 7.30501  ?  18  GLY A C     1 
ATOM   83   O  O     . GLY A 1 13  ? -36.10113 13.28280 6.60853   1.000 8.36039  ?  18  GLY A O     1 
ATOM   84   N  N     . ALA A 1 14  ? -35.81411 12.04799 4.74308   1.000 7.40684  ?  19  ALA A N     1 
ATOM   85   C  CA    . ALA A 1 14  ? -35.81831 13.13442 3.76710   1.000 7.09766  ?  19  ALA A CA    1 
ATOM   86   C  C     . ALA A 1 14  ? -34.59432 14.04143 3.81767   1.000 6.56659  ?  19  ALA A C     1 
ATOM   87   O  O     . ALA A 1 14  ? -34.58486 15.07238 3.13595   1.000 8.00685  ?  19  ALA A O     1 
ATOM   88   C  CB    . ALA A 1 14  ? -37.11097 13.96182 3.78704   1.000 10.20824 ?  19  ALA A CB    1 
ATOM   89   N  N     . VAL A 1 15  ? -33.54846 13.68605 4.57329   1.000 6.25770  ?  20  VAL A N     1 
ATOM   90   C  CA    . VAL A 1 15  ? -32.35198 14.53042 4.58663   1.000 6.73089  ?  20  VAL A CA    1 
ATOM   91   C  C     . VAL A 1 15  ? -31.55568 14.42268 3.29163   1.000 5.96889  ?  20  VAL A C     1 
ATOM   92   O  O     . VAL A 1 15  ? -30.72203 15.29211 3.00978   1.000 6.39926  ?  20  VAL A O     1 
ATOM   93   C  CB    . VAL A 1 15  ? -31.44342 14.28561 5.81004   1.000 6.04058  ?  20  VAL A CB    1 
ATOM   94   C  CG1   . VAL A 1 15  ? -32.19255 14.56107 7.09787   1.000 7.86038  ?  20  VAL A CG1   1 
ATOM   95   C  CG2   . VAL A 1 15  ? -30.87753 12.86911 5.78634   1.000 7.01219  ?  20  VAL A CG2   1 
ATOM   96   N  N     . GLY A 1 16  ? -31.77984 13.37699 2.50584   1.000 5.80288  ?  21  GLY A N     1 
ATOM   97   C  CA    . GLY A 1 16  ? -31.10263 13.18028 1.24668   1.000 6.03840  ?  21  GLY A CA    1 
ATOM   98   C  C     . GLY A 1 16  ? -30.15591 11.99654 1.18449   1.000 4.75409  ?  21  GLY A C     1 
ATOM   99   O  O     . GLY A 1 16  ? -29.25040 12.00327 0.33823   1.000 6.30001  ?  21  GLY A O     1 
ATOM   100  N  N     . LYS A 1 17  ? -30.33856 10.98432 2.03769   1.000 6.04998  ?  22  LYS A N     1 
ATOM   101  C  CA    . LYS A 1 17  ? -29.43509 9.83535  2.05373   1.000 6.34244  ?  22  LYS A CA    1 
ATOM   102  C  C     . LYS A 1 17  ? -29.45275 9.10261  0.71920   1.000 5.71573  ?  22  LYS A C     1 
ATOM   103  O  O     . LYS A 1 17  ? -28.39882 8.85514  0.11556   1.000 6.50380  ?  22  LYS A O     1 
ATOM   104  C  CB    . LYS A 1 17  ? -29.82898 8.88686  3.18631   1.000 6.59538  ?  22  LYS A CB    1 
ATOM   105  C  CG    . LYS A 1 17  ? -29.82763 9.54048  4.56348   1.000 6.78678  ?  22  LYS A CG    1 
ATOM   106  C  CD    . LYS A 1 17  ? -30.19965 8.55622  5.67155   1.000 7.07609  ?  22  LYS A CD    1 
ATOM   107  C  CE    . LYS A 1 17  ? -31.63679 8.06428  5.57230   1.000 7.43716  ?  22  LYS A CE    1 
ATOM   108  N  NZ    . LYS A 1 17  ? -32.64181 9.16805  5.67337   1.000 7.06632  ?  22  LYS A NZ    1 
ATOM   109  N  N     . SER A 1 18  ? -30.64852 8.75441  0.23469   1.000 6.27353  ?  23  SER A N     1 
ATOM   110  C  CA    . SER A 1 18  ? -30.74660 8.04151  -1.03315  1.000 6.36460  ?  23  SER A CA    1 
ATOM   111  C  C     . SER A 1 18  ? -30.23260 8.89721  -2.17680  1.000 6.31114  ?  23  SER A C     1 
ATOM   112  O  O     . SER A 1 18  ? -29.55270 8.39749  -3.08107  1.000 6.91301  ?  23  SER A O     1 
ATOM   113  C  CB    . SER A 1 18  ? -32.19440 7.64318  -1.29929  1.000 7.57585  ?  23  SER A CB    1 
ATOM   114  O  OG    . SER A 1 18  ? -32.66975 6.75839  -0.30732  1.000 6.75046  ?  23  SER A OG    1 
ATOM   115  N  N     . SER A 1 19  ? -30.54589 10.19396 -2.14954  1.000 6.43340  ?  24  SER A N     1 
ATOM   116  C  CA    . SER A 1 19  ? -30.07108 11.08698 -3.19625  1.000 6.09419  ?  24  SER A CA    1 
ATOM   117  C  C     . SER A 1 19  ? -28.54969 11.12451 -3.22599  1.000 6.10631  ?  24  SER A C     1 
ATOM   118  O  O     . SER A 1 19  ? -27.94271 11.08443 -4.30191  1.000 7.16232  ?  24  SER A O     1 
ATOM   119  C  CB    . SER A 1 19  ? -30.64366 12.48951 -2.98814  1.000 7.26024  ?  24  SER A CB    1 
ATOM   120  O  OG    . SER A 1 19  ? -32.05428 12.50531 -3.11498  1.000 8.20966  ?  24  SER A OG    1 
ATOM   121  N  N     A MET A 1 20  ? -27.91455 11.21421 -2.05001  0.500 6.00887  ?  25  MET A N     1 
ATOM   122  N  N     B MET A 1 20  ? -27.91766 11.16984 -2.05400  0.500 6.55194  ?  25  MET A N     1 
ATOM   123  C  CA    A MET A 1 20  ? -26.45402 11.20550 -1.98142  0.500 6.34570  ?  25  MET A CA    1 
ATOM   124  C  CA    B MET A 1 20  ? -26.46173 11.21699 -1.99735  0.500 7.48173  ?  25  MET A CA    1 
ATOM   125  C  C     A MET A 1 20  ? -25.88820 9.93945  -2.60713  0.500 5.84171  ?  25  MET A C     1 
ATOM   126  C  C     B MET A 1 20  ? -25.84122 9.93877  -2.54931  0.500 6.80253  ?  25  MET A C     1 
ATOM   127  O  O     A MET A 1 20  ? -25.00459 9.99744  -3.46995  0.500 6.15740  ?  25  MET A O     1 
ATOM   128  O  O     B MET A 1 20  ? -24.86837 9.99321  -3.31062  0.500 8.30775  ?  25  MET A O     1 
ATOM   129  C  CB    A MET A 1 20  ? -25.98601 11.31425 -0.52579  0.500 7.65080  ?  25  MET A CB    1 
ATOM   130  C  CB    B MET A 1 20  ? -26.02428 11.45370 -0.55602  0.500 9.82209  ?  25  MET A CB    1 
ATOM   131  C  CG    A MET A 1 20  ? -26.14871 12.68490 0.11107   0.500 8.16198  ?  25  MET A CG    1 
ATOM   132  C  CG    B MET A 1 20  ? -24.54239 11.62606 -0.36810  0.500 13.08163 ?  25  MET A CG    1 
ATOM   133  S  SD    A MET A 1 20  ? -25.60988 12.76813 1.82969   0.500 10.81543 ?  25  MET A SD    1 
ATOM   134  S  SD    B MET A 1 20  ? -24.19066 11.93225 1.36700   0.500 14.79045 ?  25  MET A SD    1 
ATOM   135  C  CE    A MET A 1 20  ? -23.83298 12.67768 1.63283   0.500 13.95170 ?  25  MET A CE    1 
ATOM   136  C  CE    B MET A 1 20  ? -25.21351 13.37071 1.67606   0.500 15.47404 ?  25  MET A CE    1 
ATOM   137  N  N     . ILE A 1 21  ? -26.39302 8.78109  -2.18036  1.000 5.90671  ?  26  ILE A N     1 
ATOM   138  C  CA    . ILE A 1 21  ? -25.86235 7.50843  -2.65972  1.000 6.96922  ?  26  ILE A CA    1 
ATOM   139  C  C     . ILE A 1 21  ? -26.09287 7.35092  -4.15858  1.000 6.90184  ?  26  ILE A C     1 
ATOM   140  O  O     . ILE A 1 21  ? -25.19403 6.93126  -4.89749  1.000 8.07384  ?  26  ILE A O     1 
ATOM   141  C  CB    . ILE A 1 21  ? -26.47766 6.35444  -1.84770  1.000 8.53115  ?  26  ILE A CB    1 
ATOM   142  C  CG1   . ILE A 1 21  ? -26.04034 6.45061  -0.38438  1.000 8.12826  ?  26  ILE A CG1   1 
ATOM   143  C  CG2   . ILE A 1 21  ? -26.11421 5.00585  -2.45820  1.000 10.81856 ?  26  ILE A CG2   1 
ATOM   144  C  CD1   . ILE A 1 21  ? -26.78330 5.51030  0.52660   1.000 9.41759  ?  26  ILE A CD1   1 
ATOM   145  N  N     . GLN A 1 22  ? -27.29240 7.69488  -4.63497  1.000 7.44726  ?  27  GLN A N     1 
ATOM   146  C  CA    . GLN A 1 22  ? -27.58969 7.53208  -6.05494  1.000 8.19973  ?  27  GLN A CA    1 
ATOM   147  C  C     . GLN A 1 22  ? -26.82336 8.52524  -6.92164  1.000 7.28094  ?  27  GLN A C     1 
ATOM   148  O  O     . GLN A 1 22  ? -26.42312 8.18585  -8.04086  1.000 8.34948  ?  27  GLN A O     1 
ATOM   149  C  CB    . GLN A 1 22  ? -29.09680 7.60662  -6.29406  1.000 10.99604 ?  27  GLN A CB    1 
ATOM   150  C  CG    . GLN A 1 22  ? -29.83549 6.41486  -5.70409  1.000 14.60838 ?  27  GLN A CG    1 
ATOM   151  C  CD    . GLN A 1 22  ? -31.27366 6.30886  -6.16403  1.000 20.24581 ?  27  GLN A CD    1 
ATOM   152  O  OE1   . GLN A 1 22  ? -31.62623 6.75193  -7.25996  1.000 25.22806 ?  27  GLN A OE1   1 
ATOM   153  N  NE2   . GLN A 1 22  ? -32.11623 5.71020  -5.32604  1.000 18.86019 ?  27  GLN A NE2   1 
ATOM   154  N  N     . ARG A 1 23  ? -26.60001 9.74465  -6.43055  1.000 6.09374  ?  28  ARG A N     1 
ATOM   155  C  CA    . ARG A 1 23  ? -25.75664 10.67766 -7.16641  1.000 6.97649  ?  28  ARG A CA    1 
ATOM   156  C  C     . ARG A 1 23  ? -24.34542 10.12444 -7.29618  1.000 7.44291  ?  28  ARG A C     1 
ATOM   157  O  O     . ARG A 1 23  ? -23.75538 10.12575 -8.38463  1.000 8.30492  ?  28  ARG A O     1 
ATOM   158  C  CB    . ARG A 1 23  ? -25.73882 12.03033 -6.45485  1.000 7.74362  ?  28  ARG A CB    1 
ATOM   159  C  CG    . ARG A 1 23  ? -24.64560 12.96200 -6.94243  1.000 7.65432  ?  28  ARG A CG    1 
ATOM   160  C  CD    . ARG A 1 23  ? -24.89409 13.41225 -8.36806  1.000 9.38474  ?  28  ARG A CD    1 
ATOM   161  N  NE    . ARG A 1 23  ? -25.74582 14.59642 -8.41685  1.000 8.77937  ?  28  ARG A NE    1 
ATOM   162  C  CZ    . ARG A 1 23  ? -26.17838 15.15977 -9.53934  1.000 9.08499  ?  28  ARG A CZ    1 
ATOM   163  N  NH1   . ARG A 1 23  ? -25.85803 14.63345 -10.71309 1.000 12.40067 ?  28  ARG A NH1   1 
ATOM   164  N  NH2   . ARG A 1 23  ? -26.93320 16.24886 -9.48621  1.000 9.54574  ?  28  ARG A NH2   1 
ATOM   165  N  N     . TYR A 1 24  ? -23.80258 9.60938  -6.19169  1.000 7.74477  ?  29  TYR A N     1 
ATOM   166  C  CA    . TYR A 1 24  ? -22.43571 9.10316  -6.19473  1.000 7.11869  ?  29  TYR A CA    1 
ATOM   167  C  C     . TYR A 1 24  ? -22.28992 7.89097  -7.10436  1.000 8.41205  ?  29  TYR A C     1 
ATOM   168  O  O     . TYR A 1 24  ? -21.32773 7.79945  -7.87570  1.000 10.45107 ?  29  TYR A O     1 
ATOM   169  C  CB    . TYR A 1 24  ? -22.03103 8.74298  -4.76739  1.000 8.87241  ?  29  TYR A CB    1 
ATOM   170  C  CG    . TYR A 1 24  ? -20.59252 8.32411  -4.62099  1.000 8.22094  ?  29  TYR A CG    1 
ATOM   171  C  CD1   . TYR A 1 24  ? -19.56207 9.21136  -4.89545  1.000 10.16370 ?  29  TYR A CD1   1 
ATOM   172  C  CD2   . TYR A 1 24  ? -20.26509 7.05095  -4.18653  1.000 10.54608 ?  29  TYR A CD2   1 
ATOM   173  C  CE1   . TYR A 1 24  ? -18.24450 8.84075  -4.75200  1.000 10.72818 ?  29  TYR A CE1   1 
ATOM   174  C  CE2   . TYR A 1 24  ? -18.95299 6.66810  -4.03963  1.000 10.84837 ?  29  TYR A CE2   1 
ATOM   175  C  CZ    . TYR A 1 24  ? -17.94514 7.56616  -4.32381  1.000 10.58732 ?  29  TYR A CZ    1 
ATOM   176  O  OH    . TYR A 1 24  ? -16.63326 7.19160  -4.17353  1.000 12.93565 ?  29  TYR A OH    1 
ATOM   177  N  N     . CYS A 1 25  ? -23.23179 6.95121  -7.03085  1.000 7.96441  ?  30  CYS A N     1 
ATOM   178  C  CA    . CYS A 1 25  ? -23.08727 5.67999  -7.72995  1.000 8.51052  ?  30  CYS A CA    1 
ATOM   179  C  C     . CYS A 1 25  ? -23.65525 5.69635  -9.13991  1.000 9.51014  ?  30  CYS A C     1 
ATOM   180  O  O     . CYS A 1 25  ? -23.15024 4.97173  -10.00399 1.000 12.96030 ?  30  CYS A O     1 
ATOM   181  C  CB    . CYS A 1 25  ? -23.74994 4.55861  -6.92740  1.000 9.29976  ?  30  CYS A CB    1 
ATOM   182  S  SG    . CYS A 1 25  ? -22.98757 4.26384  -5.32609  1.000 10.16592 ?  30  CYS A SG    1 
ATOM   183  N  N     . LYS A 1 26  ? -24.69571 6.49051  -9.39557  1.000 9.94020  ?  31  LYS A N     1 
ATOM   184  C  CA    . LYS A 1 26  ? -25.37085 6.47792  -10.68325 1.000 11.67581 ?  31  LYS A CA    1 
ATOM   185  C  C     . LYS A 1 26  ? -25.34563 7.81270  -11.41222 1.000 11.09217 ?  31  LYS A C     1 
ATOM   186  O  O     . LYS A 1 26  ? -25.71653 7.85484  -12.59157 1.000 12.99066 ?  31  LYS A O     1 
ATOM   187  C  CB    . LYS A 1 26  ? -26.82403 5.99993  -10.52917 1.000 13.43859 ?  31  LYS A CB    1 
ATOM   188  C  CG    . LYS A 1 26  ? -26.95124 4.58916  -9.97477  1.000 18.22019 ?  31  LYS A CG    1 
ATOM   189  N  N     . GLY A 1 27  ? -24.93542 8.89556  -10.75287 1.000 9.58749  ?  32  GLY A N     1 
ATOM   190  C  CA    . GLY A 1 27  ? -24.76176 10.16909 -11.42002 1.000 10.74372 ?  32  GLY A CA    1 
ATOM   191  C  C     . GLY A 1 27  ? -26.02133 10.96282 -11.66826 1.000 11.71899 ?  32  GLY A C     1 
ATOM   192  O  O     . GLY A 1 27  ? -26.01293 11.85430 -12.51931 1.000 17.71799 ?  32  GLY A O     1 
ATOM   193  N  N     . ILE A 1 28  ? -27.10839 10.68004 -10.95187 1.000 9.72084  ?  33  ILE A N     1 
ATOM   194  C  CA    . ILE A 1 28  ? -28.38616 11.33124 -11.20415 1.000 10.85327 ?  33  ILE A CA    1 
ATOM   195  C  C     . ILE A 1 28  ? -28.92430 11.95013 -9.92257  1.000 10.03107 ?  33  ILE A C     1 
ATOM   196  O  O     . ILE A 1 28  ? -28.49533 11.62565 -8.81255  1.000 10.95173 ?  33  ILE A O     1 
ATOM   197  C  CB    . ILE A 1 28  ? -29.43472 10.36859 -11.79836 1.000 12.21579 ?  33  ILE A CB    1 
ATOM   198  C  CG1   . ILE A 1 28  ? -29.80005 9.30089  -10.76837 1.000 12.85995 ?  33  ILE A CG1   1 
ATOM   199  C  CG2   . ILE A 1 28  ? -28.91834 9.73676  -13.07885 1.000 14.94328 ?  33  ILE A CG2   1 
ATOM   200  C  CD1   . ILE A 1 28  ? -30.96843 8.43762  -11.17746 1.000 16.15556 ?  33  ILE A CD1   1 
ATOM   201  N  N     . PHE A 1 29  ? -29.89214 12.84772 -10.10098 1.000 9.98149  ?  34  PHE A N     1 
ATOM   202  C  CA    . PHE A 1 29  ? -30.63389 13.44975 -9.00374  1.000 7.95520  ?  34  PHE A CA    1 
ATOM   203  C  C     . PHE A 1 29  ? -32.02843 13.79147 -9.50353  1.000 8.31518  ?  34  PHE A C     1 
ATOM   204  O  O     . PHE A 1 29  ? -32.18098 14.30452 -10.61357 1.000 10.20136 ?  34  PHE A O     1 
ATOM   205  C  CB    . PHE A 1 29  ? -29.94565 14.72465 -8.49646  1.000 9.87212  ?  34  PHE A CB    1 
ATOM   206  C  CG    . PHE A 1 29  ? -30.77571 15.51290 -7.51822  1.000 9.78022  ?  34  PHE A CG    1 
ATOM   207  C  CD1   . PHE A 1 29  ? -30.84811 15.13126 -6.18967  1.000 10.52632 ?  34  PHE A CD1   1 
ATOM   208  C  CD2   . PHE A 1 29  ? -31.48161 16.63584 -7.92611  1.000 10.42267 ?  34  PHE A CD2   1 
ATOM   209  C  CE1   . PHE A 1 29  ? -31.61064 15.84926 -5.28724  1.000 10.74568 ?  34  PHE A CE1   1 
ATOM   210  C  CE2   . PHE A 1 29  ? -32.24578 17.35803 -7.02591  1.000 11.14396 ?  34  PHE A CE2   1 
ATOM   211  C  CZ    . PHE A 1 29  ? -32.30988 16.96215 -5.70572  1.000 10.77007 ?  34  PHE A CZ    1 
ATOM   212  N  N     . THR A 1 30  ? -33.04343 13.49915 -8.68890  1.000 7.97453  ?  35  THR A N     1 
ATOM   213  C  CA    . THR A 1 30  ? -34.40703 13.91701 -8.98845  1.000 9.07062  ?  35  THR A CA    1 
ATOM   214  C  C     . THR A 1 30  ? -35.01522 14.62862 -7.78728  1.000 9.74861  ?  35  THR A C     1 
ATOM   215  O  O     . THR A 1 30  ? -34.61760 14.40605 -6.63894  1.000 9.36981  ?  35  THR A O     1 
ATOM   216  C  CB    . THR A 1 30  ? -35.31911 12.75683 -9.44310  1.000 11.19399 ?  35  THR A CB    1 
ATOM   217  O  OG1   . THR A 1 30  ? -35.61829 11.90886 -8.32996  1.000 12.41273 ?  35  THR A OG1   1 
ATOM   218  C  CG2   . THR A 1 30  ? -34.65974 11.93451 -10.55163 1.000 12.01110 ?  35  THR A CG2   1 
ATOM   219  N  N     . LYS A 1 31  ? -35.99790 15.48356 -8.07287  1.000 10.75718 ?  36  LYS A N     1 
ATOM   220  C  CA    . LYS A 1 31  ? -36.61219 16.33351 -7.06026  1.000 10.87448 ?  36  LYS A CA    1 
ATOM   221  C  C     . LYS A 1 31  ? -37.72860 15.64368 -6.28723  1.000 10.93204 ?  36  LYS A C     1 
ATOM   222  O  O     . LYS A 1 31  ? -38.05695 16.08277 -5.17934  1.000 11.33961 ?  36  LYS A O     1 
ATOM   223  C  CB    . LYS A 1 31  ? -37.17647 17.59549 -7.71685  1.000 15.32978 ?  36  LYS A CB    1 
ATOM   224  C  CG    . LYS A 1 31  ? -36.12343 18.51286 -8.30959  1.000 18.85514 ?  36  LYS A CG    1 
ATOM   225  C  CD    . LYS A 1 31  ? -36.75897 19.71666 -8.99056  1.000 22.99598 ?  36  LYS A CD    1 
ATOM   226  C  CE    . LYS A 1 31  ? -37.58002 20.54123 -8.01167  1.000 26.71330 ?  36  LYS A CE    1 
ATOM   227  N  NZ    . LYS A 1 31  ? -38.17529 21.74223 -8.66042  1.000 28.25366 ?  36  LYS A NZ    1 
ATOM   228  N  N     . ASP A 1 32  ? -38.33398 14.60069 -6.84225  1.000 11.63728 ?  37  ASP A N     1 
ATOM   229  C  CA    . ASP A 1 32  ? -39.45035 13.94620 -6.17765  1.000 12.86196 ?  37  ASP A CA    1 
ATOM   230  C  C     . ASP A 1 32  ? -38.94079 13.06682 -5.04529  1.000 12.46338 ?  37  ASP A C     1 
ATOM   231  O  O     . ASP A 1 32  ? -37.90192 12.41444 -5.16566  1.000 17.35849 ?  37  ASP A O     1 
ATOM   232  C  CB    . ASP A 1 32  ? -40.23263 13.09268 -7.17300  1.000 13.92774 ?  37  ASP A CB    1 
ATOM   233  C  CG    . ASP A 1 32  ? -39.38818 11.99714 -7.78588  1.000 13.55060 ?  37  ASP A CG    1 
ATOM   234  O  OD1   . ASP A 1 32  ? -38.38245 12.32066 -8.45664  1.000 14.02140 ?  37  ASP A OD1   1 
ATOM   235  O  OD2   . ASP A 1 32  ? -39.72134 10.81126 -7.58069  1.000 16.21134 ?  37  ASP A OD2   1 
ATOM   236  N  N     . TYR A 1 33  ? -39.68232 13.04485 -3.94380  1.000 10.34956 ?  38  TYR A N     1 
ATOM   237  C  CA    . TYR A 1 33  ? -39.29620 12.29243 -2.75644  1.000 9.39805  ?  38  TYR A CA    1 
ATOM   238  C  C     . TYR A 1 33  ? -39.99390 10.93906 -2.77788  1.000 11.04986 ?  38  TYR A C     1 
ATOM   239  O  O     . TYR A 1 33  ? -41.22592 10.86710 -2.71310  1.000 13.63190 ?  38  TYR A O     1 
ATOM   240  C  CB    . TYR A 1 33  ? -39.67205 13.07074 -1.49496  1.000 10.31608 ?  38  TYR A CB    1 
ATOM   241  C  CG    . TYR A 1 33  ? -39.45608 12.33961 -0.17972  1.000 9.55534  ?  38  TYR A CG    1 
ATOM   242  C  CD1   . TYR A 1 33  ? -38.49515 11.33993 -0.04615  1.000 10.00997 ?  38  TYR A CD1   1 
ATOM   243  C  CD2   . TYR A 1 33  ? -40.21975 12.66107 0.93581   1.000 12.64728 ?  38  TYR A CD2   1 
ATOM   244  C  CE1   . TYR A 1 33  ? -38.31085 10.67929 1.16232   1.000 10.17226 ?  38  TYR A CE1   1 
ATOM   245  C  CE2   . TYR A 1 33  ? -40.04285 12.01138 2.14060   1.000 15.06440 ?  38  TYR A CE2   1 
ATOM   246  C  CZ    . TYR A 1 33  ? -39.08755 11.02403 2.25117   1.000 11.96744 ?  38  TYR A CZ    1 
ATOM   247  O  OH    . TYR A 1 33  ? -38.92364 10.38548 3.46038   1.000 13.62057 ?  38  TYR A OH    1 
ATOM   248  N  N     . LYS A 1 34  ? -39.20403 9.87266  -2.85752  1.000 11.34268 ?  39  LYS A N     1 
ATOM   249  C  CA    . LYS A 1 34  ? -39.69552 8.50867  -2.70179  1.000 11.95945 ?  39  LYS A CA    1 
ATOM   250  C  C     . LYS A 1 34  ? -38.98064 7.89917  -1.50291  1.000 11.20764 ?  39  LYS A C     1 
ATOM   251  O  O     . LYS A 1 34  ? -37.76531 7.67328  -1.54855  1.000 11.22544 ?  39  LYS A O     1 
ATOM   252  C  CB    . LYS A 1 34  ? -39.45003 7.69013  -3.96835  1.000 17.57093 ?  39  LYS A CB    1 
ATOM   253  C  CG    . LYS A 1 34  ? -40.22938 8.18147  -5.17625  1.000 21.53105 ?  39  LYS A CG    1 
ATOM   254  N  N     . LYS A 1 35  ? -39.72860 7.66348  -0.42482  1.000 12.14115 ?  40  LYS A N     1 
ATOM   255  C  CA    . LYS A 1 35  ? -39.16573 7.03467  0.76297   1.000 12.06767 ?  40  LYS A CA    1 
ATOM   256  C  C     . LYS A 1 35  ? -38.57929 5.67497  0.40543   1.000 9.90512  ?  40  LYS A C     1 
ATOM   257  O  O     . LYS A 1 35  ? -39.15785 4.91114  -0.37286  1.000 12.48504 ?  40  LYS A O     1 
ATOM   258  C  CB    . LYS A 1 35  ? -40.25481 6.86610  1.82421   1.000 14.52817 ?  40  LYS A CB    1 
ATOM   259  C  CG    . LYS A 1 35  ? -39.78608 6.23723  3.12534   1.000 19.48991 ?  40  LYS A CG    1 
ATOM   260  C  CD    . LYS A 1 35  ? -40.96389 6.01017  4.06033   1.000 24.60398 ?  40  LYS A CD    1 
ATOM   261  C  CE    . LYS A 1 35  ? -40.57483 5.18317  5.27717   1.000 27.56837 ?  40  LYS A CE    1 
ATOM   262  N  NZ    . LYS A 1 35  ? -39.69956 5.92120  6.22492   1.000 30.81730 ?  40  LYS A NZ    1 
ATOM   263  N  N     . THR A 1 36  ? -37.41788 5.37575  0.97503   1.000 8.58358  ?  41  THR A N     1 
ATOM   264  C  CA    . THR A 1 36  ? -36.72227 4.14318  0.63405   1.000 8.22785  ?  41  THR A CA    1 
ATOM   265  C  C     . THR A 1 36  ? -37.46355 2.92756  1.17869   1.000 9.16539  ?  41  THR A C     1 
ATOM   266  O  O     . THR A 1 36  ? -37.93128 2.91873  2.32240   1.000 9.66876  ?  41  THR A O     1 
ATOM   267  C  CB    . THR A 1 36  ? -35.29580 4.19085  1.16948   1.000 7.82851  ?  41  THR A CB    1 
ATOM   268  O  OG1   . THR A 1 36  ? -34.61277 5.28166  0.54353   1.000 8.31459  ?  41  THR A OG1   1 
ATOM   269  C  CG2   . THR A 1 36  ? -34.56296 2.89445  0.86521   1.000 8.48615  ?  41  THR A CG2   1 
ATOM   270  N  N     . ILE A 1 37  ? -37.56982 1.89687  0.34195   1.000 10.76744 ?  42  ILE A N     1 
ATOM   271  C  CA    . ILE A 1 37  ? -38.24304 0.65191  0.68779   1.000 11.88122 ?  42  ILE A CA    1 
ATOM   272  C  C     . ILE A 1 37  ? -37.18542 -0.38971 1.02073   1.000 11.01084 ?  42  ILE A C     1 
ATOM   273  O  O     . ILE A 1 37  ? -36.28289 -0.64902 0.21365   1.000 14.35274 ?  42  ILE A O     1 
ATOM   274  C  CB    . ILE A 1 37  ? -39.13869 0.17198  -0.46613  1.000 15.69337 ?  42  ILE A CB    1 
ATOM   275  C  CG1   . ILE A 1 37  ? -40.20862 1.21928  -0.77687  1.000 18.31503 ?  42  ILE A CG1   1 
ATOM   276  C  CG2   . ILE A 1 37  ? -39.76871 -1.17568 -0.12928  1.000 17.58325 ?  42  ILE A CG2   1 
ATOM   277  C  CD1   . ILE A 1 37  ? -41.09721 1.54838  0.40088   1.000 22.90079 ?  42  ILE A CD1   1 
ATOM   278  N  N     . GLY A 1 38  ? -37.29469 -0.98790 2.20539   1.000 10.40403 ?  43  GLY A N     1 
ATOM   279  C  CA    . GLY A 1 38  ? -36.33719 -2.00664 2.60110   1.000 10.44114 ?  43  GLY A CA    1 
ATOM   280  C  C     . GLY A 1 38  ? -34.92778 -1.45467 2.63341   1.000 9.70543  ?  43  GLY A C     1 
ATOM   281  O  O     . GLY A 1 38  ? -34.68555 -0.32296 3.06354   1.000 10.14552 ?  43  GLY A O     1 
ATOM   282  N  N     . VAL A 1 39  ? -33.97586 -2.26674 2.18293   1.000 9.65430  ?  44  VAL A N     1 
ATOM   283  C  CA    . VAL A 1 39  ? -32.58305 -1.85903 2.06442   1.000 9.17853  ?  44  VAL A CA    1 
ATOM   284  C  C     . VAL A 1 39  ? -32.19074 -1.93693 0.59694   1.000 9.24976  ?  44  VAL A C     1 
ATOM   285  O  O     . VAL A 1 39  ? -32.43975 -2.94997 -0.06709  1.000 11.71378 ?  44  VAL A O     1 
ATOM   286  C  CB    . VAL A 1 39  ? -31.65304 -2.72301 2.93682   1.000 10.22151 ?  44  VAL A CB    1 
ATOM   287  C  CG1   . VAL A 1 39  ? -30.20863 -2.26010 2.79402   1.000 12.28259 ?  44  VAL A CG1   1 
ATOM   288  C  CG2   . VAL A 1 39  ? -32.09524 -2.67914 4.39240   1.000 11.12405 ?  44  VAL A CG2   1 
ATOM   289  N  N     . ASP A 1 40  ? -31.59456 -0.86472 0.09149   1.000 9.02982  ?  45  ASP A N     1 
ATOM   290  C  CA    . ASP A 1 40  ? -31.11062 -0.79896 -1.27695  1.000 10.10352 ?  45  ASP A CA    1 
ATOM   291  C  C     . ASP A 1 40  ? -29.59004 -0.83655 -1.24029  1.000 9.59524  ?  45  ASP A C     1 
ATOM   292  O  O     . ASP A 1 40  ? -28.96446 -0.21864 -0.37504  1.000 11.85474 ?  45  ASP A O     1 
ATOM   293  C  CB    . ASP A 1 40  ? -31.59790 0.49412  -1.93930  1.000 11.28366 ?  45  ASP A CB    1 
ATOM   294  C  CG    . ASP A 1 40  ? -31.56621 0.44229  -3.45952  1.000 15.23624 ?  45  ASP A CG    1 
ATOM   295  O  OD1   . ASP A 1 40  ? -31.27648 -0.62621 -4.04187  1.000 16.63329 ?  45  ASP A OD1   1 
ATOM   296  O  OD2   . ASP A 1 40  ? -31.84762 1.49297  -4.07753  1.000 15.96530 ?  45  ASP A OD2   1 
ATOM   297  N  N     . PHE A 1 41  ? -28.99771 -1.58042 -2.16458  1.000 11.49807 ?  46  PHE A N     1 
ATOM   298  C  CA    . PHE A 1 41  ? -27.55385 -1.76434 -2.21607  1.000 12.34551 ?  46  PHE A CA    1 
ATOM   299  C  C     . PHE A 1 41  ? -27.03711 -1.12908 -3.49634  1.000 13.66500 ?  46  PHE A C     1 
ATOM   300  O  O     . PHE A 1 41  ? -27.45027 -1.51431 -4.59441  1.000 16.74479 ?  46  PHE A O     1 
ATOM   301  C  CB    . PHE A 1 41  ? -27.19766 -3.25253 -2.18728  1.000 13.86448 ?  46  PHE A CB    1 
ATOM   302  C  CG    . PHE A 1 41  ? -27.85847 -4.01504 -1.06972  1.000 13.65491 ?  46  PHE A CG    1 
ATOM   303  C  CD1   . PHE A 1 41  ? -27.32232 -4.00828 0.20868   1.000 15.53163 ?  46  PHE A CD1   1 
ATOM   304  C  CD2   . PHE A 1 41  ? -29.01842 -4.73994 -1.29901  1.000 14.12890 ?  46  PHE A CD2   1 
ATOM   305  C  CE1   . PHE A 1 41  ? -27.93019 -4.70946 1.23580   1.000 15.45531 ?  46  PHE A CE1   1 
ATOM   306  C  CE2   . PHE A 1 41  ? -29.63194 -5.44359 -0.27498  1.000 13.65039 ?  46  PHE A CE2   1 
ATOM   307  C  CZ    . PHE A 1 41  ? -29.08588 -5.42776 0.99327   1.000 13.84018 ?  46  PHE A CZ    1 
ATOM   308  N  N     . LEU A 1 42  ? -26.14627 -0.15580 -3.35635  1.000 12.61633 ?  47  LEU A N     1 
ATOM   309  C  CA    . LEU A 1 42  ? -25.49752 0.46512  -4.49864  1.000 12.07708 ?  47  LEU A CA    1 
ATOM   310  C  C     . LEU A 1 42  ? -23.99278 0.39239  -4.30461  1.000 12.54216 ?  47  LEU A C     1 
ATOM   311  O  O     . LEU A 1 42  ? -23.49529 0.28143  -3.18162  1.000 15.90995 ?  47  LEU A O     1 
ATOM   312  C  CB    . LEU A 1 42  ? -25.93809 1.92069  -4.70450  1.000 14.45737 ?  47  LEU A CB    1 
ATOM   313  C  CG    . LEU A 1 42  ? -27.37644 2.12638  -5.18347  1.000 16.32140 ?  47  LEU A CG    1 
ATOM   314  C  CD1   . LEU A 1 42  ? -28.34330 2.17628  -4.01094  1.000 17.92651 ?  47  LEU A CD1   1 
ATOM   315  C  CD2   . LEU A 1 42  ? -27.48536 3.38058  -6.03565  1.000 17.58276 ?  47  LEU A CD2   1 
ATOM   316  N  N     . GLU A 1 43  ? -23.26273 0.45043  -5.41231  1.000 13.08711 ?  48  GLU A N     1 
ATOM   317  C  CA    . GLU A 1 43  ? -21.81949 0.31696  -5.33528  1.000 15.12224 ?  48  GLU A CA    1 
ATOM   318  C  C     . GLU A 1 43  ? -21.13961 1.25666  -6.31823  1.000 14.16703 ?  48  GLU A C     1 
ATOM   319  O  O     . GLU A 1 43  ? -21.72883 1.69913  -7.30830  1.000 14.59315 ?  48  GLU A O     1 
ATOM   320  C  CB    . GLU A 1 43  ? -21.36021 -1.13421 -5.53762  1.000 21.68534 ?  48  GLU A CB    1 
ATOM   321  C  CG    . GLU A 1 43  ? -21.81723 -1.76335 -6.83374  1.000 26.60530 ?  48  GLU A CG    1 
ATOM   322  C  CD    . GLU A 1 43  ? -21.49233 -3.24438 -6.90136  1.000 29.80880 ?  48  GLU A CD    1 
ATOM   323  O  OE1   . GLU A 1 43  ? -21.44710 -3.89626 -5.83569  1.000 30.16700 ?  48  GLU A OE1   1 
ATOM   324  O  OE2   . GLU A 1 43  ? -21.27848 -3.75496 -8.01871  1.000 30.84713 ?  48  GLU A OE2   1 
ATOM   325  N  N     . ARG A 1 44  ? -19.88527 1.57399  -6.00961  1.000 13.78058 ?  49  ARG A N     1 
ATOM   326  C  CA    . ARG A 1 44  ? -19.03536 2.31637  -6.92676  1.000 15.28569 ?  49  ARG A CA    1 
ATOM   327  C  C     . ARG A 1 44  ? -17.60705 1.82700  -6.76562  1.000 16.81717 ?  49  ARG A C     1 
ATOM   328  O  O     . ARG A 1 44  ? -17.12895 1.65817  -5.64028  1.000 16.68572 ?  49  ARG A O     1 
ATOM   329  C  CB    . ARG A 1 44  ? -19.09976 3.82511  -6.67142  1.000 18.75501 ?  49  ARG A CB    1 
ATOM   330  C  CG    . ARG A 1 44  ? -18.23135 4.60650  -7.64341  1.000 21.74764 ?  49  ARG A CG    1 
ATOM   331  C  CD    . ARG A 1 44  ? -18.50146 6.09369  -7.61937  1.000 23.90796 ?  49  ARG A CD    1 
ATOM   332  N  NE    . ARG A 1 44  ? -17.68624 6.78756  -8.61178  1.000 27.52488 ?  49  ARG A NE    1 
ATOM   333  C  CZ    . ARG A 1 44  ? -17.75769 8.08998  -8.86240  1.000 30.61272 ?  49  ARG A CZ    1 
ATOM   334  N  NH1   . ARG A 1 44  ? -18.61424 8.85229  -8.19397  1.000 30.23726 ?  49  ARG A NH1   1 
ATOM   335  N  NH2   . ARG A 1 44  ? -16.97242 8.62945  -9.78490  1.000 32.66297 ?  49  ARG A NH2   1 
ATOM   336  N  N     . GLN A 1 45  ? -16.93786 1.59699  -7.88893  1.000 19.93135 ?  50  GLN A N     1 
ATOM   337  C  CA    . GLN A 1 45  ? -15.52894 1.23685  -7.90254  1.000 21.40211 ?  50  GLN A CA    1 
ATOM   338  C  C     . GLN A 1 45  ? -14.71191 2.50071  -8.12498  1.000 23.37680 ?  50  GLN A C     1 
ATOM   339  O  O     . GLN A 1 45  ? -14.94561 3.23241  -9.09276  1.000 25.02014 ?  50  GLN A O     1 
ATOM   340  C  CB    . GLN A 1 45  ? -15.24056 0.22900  -9.01650  1.000 23.19252 ?  50  GLN A CB    1 
ATOM   341  N  N     . ILE A 1 46  ? -13.76984 2.76497  -7.21935  1.000 23.11844 ?  51  ILE A N     1 
ATOM   342  C  CA    . ILE A 1 46  ? -12.89384 3.92408  -7.30969  1.000 24.10488 ?  51  ILE A CA    1 
ATOM   343  C  C     . ILE A 1 46  ? -11.45794 3.47512  -7.07522  1.000 25.64531 ?  51  ILE A C     1 
ATOM   344  O  O     . ILE A 1 46  ? -11.18895 2.32828  -6.71911  1.000 24.43664 ?  51  ILE A O     1 
ATOM   345  C  CB    . ILE A 1 46  ? -13.27402 5.04801  -6.32127  1.000 27.26468 ?  51  ILE A CB    1 
ATOM   346  C  CG1   . ILE A 1 46  ? -13.02437 4.60000  -4.87982  1.000 28.87932 ?  51  ILE A CG1   1 
ATOM   347  C  CG2   . ILE A 1 46  ? -14.72136 5.48291  -6.51678  1.000 28.02273 ?  51  ILE A CG2   1 
ATOM   348  C  CD1   . ILE A 1 46  ? -13.13820 5.72118  -3.86735  1.000 28.96787 ?  51  ILE A CD1   1 
ATOM   349  N  N     . GLN A 1 47  ? -10.53400 4.40784  -7.27871  1.000 27.72393 ?  52  GLN A N     1 
ATOM   350  C  CA    . GLN A 1 47  ? -9.11897  4.19348  -7.01781  1.000 31.19111 ?  52  GLN A CA    1 
ATOM   351  C  C     . GLN A 1 47  ? -8.71226  5.02470  -5.81002  1.000 34.10758 ?  52  GLN A C     1 
ATOM   352  O  O     . GLN A 1 47  ? -8.97883  6.23059  -5.76311  1.000 36.10055 ?  52  GLN A O     1 
ATOM   353  C  CB    . GLN A 1 47  ? -8.27768  4.60715  -8.22792  1.000 34.51323 ?  52  GLN A CB    1 
ATOM   354  C  CG    . GLN A 1 47  ? -8.59101  3.84131  -9.50404  1.000 38.33478 ?  52  GLN A CG    1 
ATOM   355  C  CD    . GLN A 1 47  ? -8.10157  2.40765  -9.46054  1.000 41.81648 ?  52  GLN A CD    1 
ATOM   356  O  OE1   . GLN A 1 47  ? -6.90542  2.15198  -9.32028  1.000 43.91636 ?  52  GLN A OE1   1 
ATOM   357  N  NE2   . GLN A 1 47  ? -9.02660  1.46246  -9.57913  1.000 43.11018 ?  52  GLN A NE2   1 
ATOM   358  N  N     . VAL A 1 48  ? -8.08567  4.37716  -4.83213  1.000 34.69988 ?  53  VAL A N     1 
ATOM   359  C  CA    . VAL A 1 48  ? -7.49103  5.05139  -3.68370  1.000 37.50100 ?  53  VAL A CA    1 
ATOM   360  C  C     . VAL A 1 48  ? -6.01751  4.67711  -3.65626  1.000 40.49951 ?  53  VAL A C     1 
ATOM   361  O  O     . VAL A 1 48  ? -5.67576  3.50208  -3.46805  1.000 41.22276 ?  53  VAL A O     1 
ATOM   362  C  CB    . VAL A 1 48  ? -8.18400  4.67096  -2.36660  1.000 38.62342 ?  53  VAL A CB    1 
ATOM   363  C  CG1   . VAL A 1 48  ? -7.54061  5.41011  -1.20367  1.000 39.20923 ?  53  VAL A CG1   1 
ATOM   364  C  CG2   . VAL A 1 48  ? -9.67103  4.98078  -2.44063  1.000 37.80973 ?  53  VAL A CG2   1 
ATOM   365  N  N     . ASN A 1 49  ? -5.15026  5.67437  -3.84471  1.000 42.00029 ?  54  ASN A N     1 
ATOM   366  C  CA    . ASN A 1 49  ? -3.72368  5.44548  -4.04711  1.000 36.80064 ?  54  ASN A CA    1 
ATOM   367  C  C     . ASN A 1 49  ? -3.51159  4.48023  -5.20734  1.000 39.12089 ?  54  ASN A C     1 
ATOM   368  O  O     . ASN A 1 49  ? -3.95866  4.74252  -6.32868  1.000 48.62874 ?  54  ASN A O     1 
ATOM   369  C  CB    . ASN A 1 49  ? -3.05624  4.93084  -2.76809  1.000 34.19382 ?  54  ASN A CB    1 
ATOM   370  N  N     . ASP A 1 50  ? -2.84018  3.35978  -4.95003  1.000 38.95945 ?  55  ASP A N     1 
ATOM   371  C  CA    . ASP A 1 50  ? -2.66037  2.33925  -5.97453  1.000 41.10707 ?  55  ASP A CA    1 
ATOM   372  C  C     . ASP A 1 50  ? -3.43094  1.08077  -5.59962  1.000 43.99121 ?  55  ASP A C     1 
ATOM   373  O  O     . ASP A 1 50  ? -2.83320  0.02413  -5.37062  1.000 53.46370 ?  55  ASP A O     1 
ATOM   374  C  CB    . ASP A 1 50  ? -1.17559  2.02186  -6.16634  1.000 35.23770 ?  55  ASP A CB    1 
ATOM   375  N  N     . GLU A 1 51  ? -4.75729  1.18295  -5.53288  1.000 41.01868 ?  56  GLU A N     1 
ATOM   376  C  CA    . GLU A 1 51  ? -5.57794  0.05464  -5.11515  1.000 36.99504 ?  56  GLU A CA    1 
ATOM   377  C  C     . GLU A 1 51  ? -6.99572  0.25417  -5.62525  1.000 36.47540 ?  56  GLU A C     1 
ATOM   378  O  O     . GLU A 1 51  ? -7.56137  1.34274  -5.48251  1.000 36.55273 ?  56  GLU A O     1 
ATOM   379  C  CB    . GLU A 1 51  ? -5.58812  -0.06821 -3.58763  1.000 32.57573 ?  56  GLU A CB    1 
ATOM   380  N  N     . ASP A 1 52  ? -7.55754  -0.79376 -6.22232  1.000 35.34751 ?  57  ASP A N     1 
ATOM   381  C  CA    . ASP A 1 52  ? -8.96583  -0.78476 -6.58698  1.000 32.30310 ?  57  ASP A CA    1 
ATOM   382  C  C     . ASP A 1 52  ? -9.80906  -0.94260 -5.32975  1.000 28.87288 ?  57  ASP A C     1 
ATOM   383  O  O     . ASP A 1 52  ? -9.55412  -1.82497 -4.50472  1.000 30.54405 ?  57  ASP A O     1 
ATOM   384  C  CB    . ASP A 1 52  ? -9.26172  -1.93242 -7.55029  1.000 34.69427 ?  57  ASP A CB    1 
ATOM   385  C  CG    . ASP A 1 52  ? -8.52731  -1.79321 -8.86799  1.000 47.13944 ?  57  ASP A CG    1 
ATOM   386  O  OD1   . ASP A 1 52  ? -7.93964  -0.71875 -9.11252  1.000 49.93074 ?  57  ASP A OD1   1 
ATOM   387  O  OD2   . ASP A 1 52  ? -8.53612  -2.76074 -9.65839  1.000 48.45250 ?  57  ASP A OD2   1 
ATOM   388  N  N     . VAL A 1 53  ? -10.81009 -0.08130 -5.17817  1.000 25.39646 ?  58  VAL A N     1 
ATOM   389  C  CA    . VAL A 1 53  ? -11.69133 -0.09332 -4.01846  1.000 22.77475 ?  58  VAL A CA    1 
ATOM   390  C  C     . VAL A 1 53  ? -13.12718 -0.11071 -4.51726  1.000 21.20690 ?  58  VAL A C     1 
ATOM   391  O  O     . VAL A 1 53  ? -13.48292 0.65529  -5.41891  1.000 25.27833 ?  58  VAL A O     1 
ATOM   392  C  CB    . VAL A 1 53  ? -11.44837 1.12945  -3.11259  1.000 25.47478 ?  58  VAL A CB    1 
ATOM   393  C  CG1   . VAL A 1 53  ? -12.43706 1.14559  -1.96030  1.000 26.52279 ?  58  VAL A CG1   1 
ATOM   394  C  CG2   . VAL A 1 53  ? -10.01827 1.12979  -2.59351  1.000 26.99511 ?  58  VAL A CG2   1 
ATOM   395  N  N     . ARG A 1 54  ? -13.94568 -0.98773 -3.94456  1.000 18.45433 ?  59  ARG A N     1 
ATOM   396  C  CA    . ARG A 1 54  ? -15.36996 -1.04508 -4.25213  1.000 17.67071 ?  59  ARG A CA    1 
ATOM   397  C  C     . ARG A 1 54  ? -16.14117 -0.63067 -3.00678  1.000 16.28312 ?  59  ARG A C     1 
ATOM   398  O  O     . ARG A 1 54  ? -16.13211 -1.34230 -1.99676  1.000 16.60378 ?  59  ARG A O     1 
ATOM   399  C  CB    . ARG A 1 54  ? -15.78492 -2.43873 -4.71699  1.000 22.07951 ?  59  ARG A CB    1 
ATOM   400  C  CG    . ARG A 1 54  ? -17.23175 -2.51048 -5.19067  1.000 26.26152 ?  59  ARG A CG    1 
ATOM   401  C  CD    . ARG A 1 54  ? -17.59967 -3.90786 -5.66390  1.000 29.88554 ?  59  ARG A CD    1 
ATOM   402  N  NE    . ARG A 1 54  ? -16.81141 -4.32092 -6.82115  1.000 33.82896 ?  59  ARG A NE    1 
ATOM   403  C  CZ    . ARG A 1 54  ? -17.19071 -4.15312 -8.08427  1.000 37.33059 ?  59  ARG A CZ    1 
ATOM   404  N  NH1   . ARG A 1 54  ? -18.35303 -3.57874 -8.36111  1.000 38.50442 ?  59  ARG A NH1   1 
ATOM   405  N  NH2   . ARG A 1 54  ? -16.40728 -4.56153 -9.07265  1.000 38.56252 ?  59  ARG A NH2   1 
ATOM   406  N  N     A LEU A 1 55  ? -16.81511 0.51374  -3.08214  0.500 14.12122 ?  60  LEU A N     1 
ATOM   407  N  N     B LEU A 1 55  ? -16.78336 0.53019  -3.07143  0.500 14.26236 ?  60  LEU A N     1 
ATOM   408  C  CA    A LEU A 1 55  ? -17.61581 1.01705  -1.97329  0.500 12.77746 ?  60  LEU A CA    1 
ATOM   409  C  CA    B LEU A 1 55  ? -17.63621 0.97737  -1.98195  0.500 13.10279 ?  60  LEU A CA    1 
ATOM   410  C  C     A LEU A 1 55  ? -19.01863 0.42937  -2.06137  0.500 14.19395 ?  60  LEU A C     1 
ATOM   411  C  C     B LEU A 1 55  ? -18.99539 0.30837  -2.11544  0.500 13.20982 ?  60  LEU A C     1 
ATOM   412  O  O     A LEU A 1 55  ? -19.74154 0.68072  -3.03089  0.500 16.05118 ?  60  LEU A O     1 
ATOM   413  O  O     B LEU A 1 55  ? -19.59876 0.32225  -3.19179  0.500 13.72403 ?  60  LEU A O     1 
ATOM   414  C  CB    A LEU A 1 55  ? -17.68617 2.54245  -2.01375  0.500 12.56526 ?  60  LEU A CB    1 
ATOM   415  C  CB    B LEU A 1 55  ? -17.79643 2.49759  -2.01427  0.500 13.96290 ?  60  LEU A CB    1 
ATOM   416  C  CG    A LEU A 1 55  ? -16.35972 3.29249  -1.90645  0.500 13.54238 ?  60  LEU A CG    1 
ATOM   417  C  CG    B LEU A 1 55  ? -16.63275 3.34187  -1.48619  0.500 15.21765 ?  60  LEU A CG    1 
ATOM   418  C  CD1   A LEU A 1 55  ? -16.60780 4.77543  -1.67558  0.500 12.08983 ?  60  LEU A CD1   1 
ATOM   419  C  CD1   B LEU A 1 55  ? -15.47164 3.36207  -2.46649  0.500 17.96025 ?  60  LEU A CD1   1 
ATOM   420  C  CD2   A LEU A 1 55  ? -15.50154 2.70715  -0.80229  0.500 12.73622 ?  60  LEU A CD2   1 
ATOM   421  C  CD2   B LEU A 1 55  ? -17.09135 4.75701  -1.17224  0.500 14.82013 ?  60  LEU A CD2   1 
ATOM   422  N  N     A MET A 1 56  ? -19.39993 -0.34585 -1.04957  0.500 14.21741 ?  61  MET A N     1 
ATOM   423  N  N     B MET A 1 56  ? -19.46275 -0.29506 -1.02982  0.500 12.52542 ?  61  MET A N     1 
ATOM   424  C  CA    A MET A 1 56  ? -20.72155 -0.96374 -0.96971  0.500 14.02209 ?  61  MET A CA    1 
ATOM   425  C  CA    B MET A 1 56  ? -20.75449 -0.97295 -0.98596  0.500 12.14196 ?  61  MET A CA    1 
ATOM   426  C  C     A MET A 1 56  ? -21.57390 -0.07805 -0.06838  0.500 11.78880 ?  61  MET A C     1 
ATOM   427  C  C     B MET A 1 56  ? -21.65370 -0.15563 -0.06884  0.500 10.75386 ?  61  MET A C     1 
ATOM   428  O  O     A MET A 1 56  ? -21.42202 -0.09443 1.15622   0.500 11.16384 ?  61  MET A O     1 
ATOM   429  O  O     B MET A 1 56  ? -21.60348 -0.29511 1.15706   0.500 11.11904 ?  61  MET A O     1 
ATOM   430  C  CB    A MET A 1 56  ? -20.60522 -2.37180 -0.39614  0.500 17.60494 ?  61  MET A CB    1 
ATOM   431  C  CB    B MET A 1 56  ? -20.59304 -2.40332 -0.48971  0.500 14.90802 ?  61  MET A CB    1 
ATOM   432  C  CG    A MET A 1 56  ? -19.41820 -3.16323 -0.92448  0.500 22.22031 ?  61  MET A CG    1 
ATOM   433  C  CG    B MET A 1 56  ? -19.70241 -3.24532 -1.37719  0.500 18.68365 ?  61  MET A CG    1 
ATOM   434  S  SD    A MET A 1 56  ? -19.55037 -3.53860 -2.68046  0.500 25.42416 ?  61  MET A SD    1 
ATOM   435  S  SD    B MET A 1 56  ? -19.51091 -4.91381 -0.74264  0.500 21.51835 ?  61  MET A SD    1 
ATOM   436  C  CE    A MET A 1 56  ? -20.99540 -4.59579 -2.68548  0.500 25.61060 ?  61  MET A CE    1 
ATOM   437  C  CE    B MET A 1 56  ? -18.73777 -4.58947 0.83962   0.500 20.44540 ?  61  MET A CE    1 
ATOM   438  N  N     . LEU A 1 57  ? -22.47016 0.70001  -0.67199  1.000 10.39000 ?  62  LEU A N     1 
ATOM   439  C  CA    . LEU A 1 57  ? -23.28456 1.65656  0.06272   1.000 10.03442 ?  62  LEU A CA    1 
ATOM   440  C  C     . LEU A 1 57  ? -24.65794 1.05793  0.34137   1.000 11.09991 ?  62  LEU A C     1 
ATOM   441  O  O     . LEU A 1 57  ? -25.37536 0.67055  -0.58736  1.000 16.11247 ?  62  LEU A O     1 
ATOM   442  C  CB    . LEU A 1 57  ? -23.39843 2.96344  -0.72128  1.000 11.82173 ?  62  LEU A CB    1 
ATOM   443  C  CG    . LEU A 1 57  ? -22.05578 3.59778  -1.10326  1.000 15.66202 ?  62  LEU A CG    1 
ATOM   444  C  CD1   . LEU A 1 57  ? -22.25330 4.95909  -1.75507  1.000 16.81009 ?  62  LEU A CD1   1 
ATOM   445  C  CD2   . LEU A 1 57  ? -21.12588 3.70056  0.09497   1.000 17.41117 ?  62  LEU A CD2   1 
ATOM   446  N  N     . TRP A 1 58  ? -25.01551 0.98400  1.61955   1.000 9.08502  ?  63  TRP A N     1 
ATOM   447  C  CA    . TRP A 1 58  ? -26.29285 0.44391  2.06212   1.000 8.71615  ?  63  TRP A CA    1 
ATOM   448  C  C     . TRP A 1 58  ? -27.23581 1.59358  2.38679   1.000 8.70591  ?  63  TRP A C     1 
ATOM   449  O  O     . TRP A 1 58  ? -26.87948 2.49650  3.14918   1.000 9.39580  ?  63  TRP A O     1 
ATOM   450  C  CB    . TRP A 1 58  ? -26.10046 -0.41335 3.31118   1.000 9.77355  ?  63  TRP A CB    1 
ATOM   451  C  CG    . TRP A 1 58  ? -25.43986 -1.73245 3.06698   1.000 10.88742 ?  63  TRP A CG    1 
ATOM   452  C  CD1   . TRP A 1 58  ? -24.35331 -1.98280 2.27405   1.000 12.14455 ?  63  TRP A CD1   1 
ATOM   453  C  CD2   . TRP A 1 58  ? -25.83375 -2.99337 3.61927   1.000 11.17736 ?  63  TRP A CD2   1 
ATOM   454  N  NE1   . TRP A 1 58  ? -24.04742 -3.32266 2.30604   1.000 12.34101 ?  63  TRP A NE1   1 
ATOM   455  C  CE2   . TRP A 1 58  ? -24.94146 -3.96437 3.12304   1.000 11.43891 ?  63  TRP A CE2   1 
ATOM   456  C  CE3   . TRP A 1 58  ? -26.85338 -3.39482 4.49027   1.000 11.22190 ?  63  TRP A CE3   1 
ATOM   457  C  CZ2   . TRP A 1 58  ? -25.03813 -5.31216 3.46810   1.000 12.99042 ?  63  TRP A CZ2   1 
ATOM   458  C  CZ3   . TRP A 1 58  ? -26.95046 -4.73393 4.82810   1.000 12.24649 ?  63  TRP A CZ3   1 
ATOM   459  C  CH2   . TRP A 1 58  ? -26.04675 -5.67522 4.31941   1.000 12.65672 ?  63  TRP A CH2   1 
ATOM   460  N  N     . ASP A 1 59  ? -28.44310 1.54302  1.83220   1.000 8.49298  ?  64  ASP A N     1 
ATOM   461  C  CA    . ASP A 1 59  ? -29.40345 2.63380  1.92244   1.000 7.12135  ?  64  ASP A CA    1 
ATOM   462  C  C     . ASP A 1 59  ? -30.70226 2.11552  2.52613   1.000 7.23363  ?  64  ASP A C     1 
ATOM   463  O  O     . ASP A 1 59  ? -31.23131 1.09218  2.08284   1.000 8.81801  ?  64  ASP A O     1 
ATOM   464  C  CB    . ASP A 1 59  ? -29.66686 3.18137  0.51614   1.000 8.03840  ?  64  ASP A CB    1 
ATOM   465  C  CG    . ASP A 1 59  ? -30.48120 4.46393  0.51876   1.000 8.04538  ?  64  ASP A CG    1 
ATOM   466  O  OD1   . ASP A 1 59  ? -30.35535 5.26923  1.46427   1.000 8.77025  ?  64  ASP A OD1   1 
ATOM   467  O  OD2   . ASP A 1 59  ? -31.25351 4.66535  -0.43916  1.000 10.01889 ?  64  ASP A OD2   1 
ATOM   468  N  N     . THR A 1 60  ? -31.22201 2.82381  3.52797   1.000 7.62920  ?  65  THR A N     1 
ATOM   469  C  CA    . THR A 1 60  ? -32.50380 2.46639  4.12341   1.000 7.60015  ?  65  THR A CA    1 
ATOM   470  C  C     . THR A 1 60  ? -33.16394 3.73685  4.64707   1.000 7.27579  ?  65  THR A C     1 
ATOM   471  O  O     . THR A 1 60  ? -32.50492 4.75992  4.84438   1.000 8.30587  ?  65  THR A O     1 
ATOM   472  C  CB    . THR A 1 60  ? -32.33695 1.39044  5.21087   1.000 9.21957  ?  65  THR A CB    1 
ATOM   473  O  OG1   . THR A 1 60  ? -33.58025 0.70688  5.41467   1.000 10.31690 ?  65  THR A OG1   1 
ATOM   474  C  CG2   . THR A 1 60  ? -31.88014 2.00389  6.52887   1.000 10.39297 ?  65  THR A CG2   1 
ATOM   475  N  N     . ALA A 1 61  ? -34.47991 3.67387  4.84197   1.000 6.70628  ?  66  ALA A N     1 
ATOM   476  C  CA    . ALA A 1 61  ? -35.21907 4.84913  5.28094   1.000 7.60272  ?  66  ALA A CA    1 
ATOM   477  C  C     . ALA A 1 61  ? -34.86073 5.21914  6.71492   1.000 8.21616  ?  66  ALA A C     1 
ATOM   478  O  O     . ALA A 1 61  ? -34.59256 4.35961  7.55944   1.000 10.91490 ?  66  ALA A O     1 
ATOM   479  C  CB    . ALA A 1 61  ? -36.72436 4.61572  5.17619   1.000 9.56244  ?  66  ALA A CB    1 
ATOM   480  N  N     . GLY A 1 62  ? -34.87640 6.52669  6.98864   1.000 8.44995  ?  67  GLY A N     1 
ATOM   481  C  CA    . GLY A 1 62  ? -34.49547 7.02078  8.30055   1.000 10.58853 ?  67  GLY A CA    1 
ATOM   482  C  C     . GLY A 1 62  ? -35.59713 7.01722  9.33875   1.000 18.15370 ?  67  GLY A C     1 
ATOM   483  O  O     . GLY A 1 62  ? -35.29887 7.00787  10.53688  1.000 22.52336 ?  67  GLY A O     1 
ATOM   484  N  N     . GLN A 1 63  ? -36.85746 7.02960  8.91979   1.000 21.57611 ?  68  GLN A N     1 
ATOM   485  C  CA    . GLN A 1 63  ? -37.96176 7.08263  9.87748   1.000 31.19967 ?  68  GLN A CA    1 
ATOM   486  C  C     . GLN A 1 63  ? -38.12008 5.76008  10.62265  1.000 33.73999 ?  68  GLN A C     1 
ATOM   487  O  O     . GLN A 1 63  ? -37.89827 4.68827  10.05828  1.000 37.18526 ?  68  GLN A O     1 
ATOM   488  C  CB    . GLN A 1 63  ? -39.27273 7.45808  9.18124   1.000 38.38107 ?  68  GLN A CB    1 
ATOM   489  N  N     . ILE A 1 69  ? -34.61173 0.50951  12.49514  1.000 26.66811 ?  74  ILE A N     1 
ATOM   490  C  CA    . ILE A 1 69  ? -33.66894 -0.08440 11.55365  1.000 24.92006 ?  74  ILE A CA    1 
ATOM   491  C  C     . ILE A 1 69  ? -33.07445 -1.37295 12.11871  1.000 25.36852 ?  74  ILE A C     1 
ATOM   492  O  O     . ILE A 1 69  ? -32.63424 -1.41754 13.26795  1.000 26.21134 ?  74  ILE A O     1 
ATOM   493  C  CB    . ILE A 1 69  ? -32.58262 0.92309  11.12638  1.000 22.23965 ?  74  ILE A CB    1 
ATOM   494  C  CG1   . ILE A 1 69  ? -33.22062 2.13093  10.43617  1.000 24.42572 ?  74  ILE A CG1   1 
ATOM   495  C  CG2   . ILE A 1 69  ? -31.57182 0.26172  10.20633  1.000 21.48821 ?  74  ILE A CG2   1 
ATOM   496  C  CD1   . ILE A 1 69  ? -32.23156 3.20999  10.05499  1.000 24.59504 ?  74  ILE A CD1   1 
ATOM   497  N  N     . THR A 1 70  ? -33.06643 -2.41746 11.29630  1.000 25.63794 ?  75  THR A N     1 
ATOM   498  C  CA    . THR A 1 70  ? -32.61498 -3.72800 11.73618  1.000 26.76465 ?  75  THR A CA    1 
ATOM   499  C  C     . THR A 1 70  ? -31.11533 -3.72946 12.02068  1.000 21.92390 ?  75  THR A C     1 
ATOM   500  O  O     . THR A 1 70  ? -30.34811 -2.94345 11.45910  1.000 21.35996 ?  75  THR A O     1 
ATOM   501  C  CB    . THR A 1 70  ? -32.93712 -4.76976 10.66398  1.000 31.05504 ?  75  THR A CB    1 
ATOM   502  O  OG1   . THR A 1 70  ? -32.32156 -6.01848 11.00134  1.000 35.62026 ?  75  THR A OG1   1 
ATOM   503  C  CG2   . THR A 1 70  ? -32.43347 -4.30879 9.30336   1.000 31.89970 ?  75  THR A CG2   1 
ATOM   504  N  N     . LYS A 1 71  ? -30.69986 -4.63864 12.90708  1.000 22.28362 ?  76  LYS A N     1 
ATOM   505  C  CA    . LYS A 1 71  ? -29.27789 -4.79406 13.19268  1.000 21.03360 ?  76  LYS A CA    1 
ATOM   506  C  C     . LYS A 1 71  ? -28.50406 -5.25545 11.96385  1.000 19.58713 ?  76  LYS A C     1 
ATOM   507  O  O     . LYS A 1 71  ? -27.30992 -4.96095 11.83722  1.000 18.49905 ?  76  LYS A O     1 
ATOM   508  C  CB    . LYS A 1 71  ? -29.07307 -5.76200 14.35873  1.000 25.41171 ?  76  LYS A CB    1 
ATOM   509  C  CG    . LYS A 1 71  ? -29.65345 -5.26378 15.67263  1.000 28.27921 ?  76  LYS A CG    1 
ATOM   510  C  CD    . LYS A 1 71  ? -29.07768 -6.01252 16.86098  1.000 32.62417 ?  76  LYS A CD    1 
ATOM   511  C  CE    . LYS A 1 71  ? -29.52543 -5.37672 18.16731  1.000 35.84031 ?  76  LYS A CE    1 
ATOM   512  N  NZ    . LYS A 1 71  ? -28.85435 -5.98869 19.34566  1.000 38.44433 ?  76  LYS A NZ    1 
ATOM   513  N  N     . ALA A 1 72  ? -29.16402 -5.97090 11.04844  1.000 18.50625 ?  77  ALA A N     1 
ATOM   514  C  CA    . ALA A 1 72  ? -28.48976 -6.43130 9.83921   1.000 17.14639 ?  77  ALA A CA    1 
ATOM   515  C  C     . ALA A 1 72  ? -28.03379 -5.26984 8.96478   1.000 14.85138 ?  77  ALA A C     1 
ATOM   516  O  O     . ALA A 1 72  ? -27.04020 -5.39462 8.23865   1.000 16.02631 ?  77  ALA A O     1 
ATOM   517  C  CB    . ALA A 1 72  ? -29.40396 -7.36505 9.04848   1.000 19.34773 ?  77  ALA A CB    1 
ATOM   518  N  N     . TYR A 1 73  ? -28.74293 -4.13856 9.01004   1.000 13.42470 ?  78  TYR A N     1 
ATOM   519  C  CA    . TYR A 1 73  ? -28.30688 -2.97616 8.24348   1.000 12.58725 ?  78  TYR A CA    1 
ATOM   520  C  C     . TYR A 1 73  ? -26.93725 -2.49362 8.70672   1.000 11.86198 ?  78  TYR A C     1 
ATOM   521  O  O     . TYR A 1 73  ? -26.06008 -2.20500 7.88288   1.000 13.25473 ?  78  TYR A O     1 
ATOM   522  C  CB    . TYR A 1 73  ? -29.33835 -1.85033 8.33981   1.000 11.87820 ?  78  TYR A CB    1 
ATOM   523  C  CG    . TYR A 1 73  ? -28.87949 -0.58416 7.65205   1.000 10.21879 ?  78  TYR A CG    1 
ATOM   524  C  CD1   . TYR A 1 73  ? -28.98254 -0.44628 6.27238   1.000 9.96633  ?  78  TYR A CD1   1 
ATOM   525  C  CD2   . TYR A 1 73  ? -28.32798 0.46514  8.37839   1.000 9.99783  ?  78  TYR A CD2   1 
ATOM   526  C  CE1   . TYR A 1 73  ? -28.55129 0.70061  5.63302   1.000 9.34506  ?  78  TYR A CE1   1 
ATOM   527  C  CE2   . TYR A 1 73  ? -27.89135 1.61579  7.74709   1.000 10.02031 ?  78  TYR A CE2   1 
ATOM   528  C  CZ    . TYR A 1 73  ? -28.00573 1.72844  6.37667   1.000 9.36622  ?  78  TYR A CZ    1 
ATOM   529  O  OH    . TYR A 1 73  ? -27.56546 2.87159  5.74562   1.000 10.38556 ?  78  TYR A OH    1 
ATOM   530  N  N     . TYR A 1 74  ? -26.73217 -2.40638 10.02324  1.000 12.49657 ?  79  TYR A N     1 
ATOM   531  C  CA    . TYR A 1 74  ? -25.47569 -1.89726 10.55924  1.000 13.39874 ?  79  TYR A CA    1 
ATOM   532  C  C     . TYR A 1 74  ? -24.37847 -2.94944 10.59066  1.000 14.05144 ?  79  TYR A C     1 
ATOM   533  O  O     . TYR A 1 74  ? -23.19778 -2.58800 10.60368  1.000 15.43298 ?  79  TYR A O     1 
ATOM   534  C  CB    . TYR A 1 74  ? -25.67352 -1.38989 11.98893  1.000 14.68611 ?  79  TYR A CB    1 
ATOM   535  C  CG    . TYR A 1 74  ? -26.64918 -0.24823 12.12617  1.000 14.89830 ?  79  TYR A CG    1 
ATOM   536  C  CD1   . TYR A 1 74  ? -26.26251 1.05686  11.85557  1.000 16.47323 ?  79  TYR A CD1   1 
ATOM   537  C  CD2   . TYR A 1 74  ? -27.95279 -0.47303 12.54811  1.000 17.78161 ?  79  TYR A CD2   1 
ATOM   538  C  CE1   . TYR A 1 74  ? -27.15048 2.10537  11.98876  1.000 18.97810 ?  79  TYR A CE1   1 
ATOM   539  C  CE2   . TYR A 1 74  ? -28.84749 0.56884  12.68531  1.000 20.82920 ?  79  TYR A CE2   1 
ATOM   540  C  CZ    . TYR A 1 74  ? -28.44133 1.85587  12.40321  1.000 20.67593 ?  79  TYR A CZ    1 
ATOM   541  O  OH    . TYR A 1 74  ? -29.32841 2.89739  12.53905  1.000 24.48753 ?  79  TYR A OH    1 
ATOM   542  N  N     . ARG A 1 75  ? -24.74241 -4.22982 10.60669  1.000 15.70405 ?  80  ARG A N     1 
ATOM   543  C  CA    . ARG A 1 75  ? -23.77652 -5.29571 10.83835  1.000 16.51342 ?  80  ARG A CA    1 
ATOM   544  C  C     . ARG A 1 75  ? -22.64940 -5.24711 9.81407   1.000 16.21248 ?  80  ARG A C     1 
ATOM   545  O  O     . ARG A 1 75  ? -22.88989 -5.20483 8.60497   1.000 17.00714 ?  80  ARG A O     1 
ATOM   546  C  CB    . ARG A 1 75  ? -24.49152 -6.64564 10.77478  1.000 18.88887 ?  80  ARG A CB    1 
ATOM   547  C  CG    . ARG A 1 75  ? -23.59594 -7.84307 11.03716  1.000 22.52024 ?  80  ARG A CG    1 
ATOM   548  C  CD    . ARG A 1 75  ? -24.40637 -9.12166 11.23688  1.000 25.39436 ?  80  ARG A CD    1 
ATOM   549  N  NE    . ARG A 1 75  ? -25.33540 -9.00994 12.35926  1.000 27.21507 ?  80  ARG A NE    1 
ATOM   550  C  CZ    . ARG A 1 75  ? -26.65526 -9.14157 12.26220  1.000 28.55843 ?  80  ARG A CZ    1 
ATOM   551  N  NH1   . ARG A 1 75  ? -27.41486 -9.01618 13.34269  1.000 27.83454 ?  80  ARG A NH1   1 
ATOM   552  N  NH2   . ARG A 1 75  ? -27.21677 -9.41310 11.09206  1.000 29.90976 ?  80  ARG A NH2   1 
ATOM   553  N  N     . GLY A 1 76  ? -21.41224 -5.24186 10.30690  1.000 15.87080 ?  81  GLY A N     1 
ATOM   554  C  CA    . GLY A 1 76  ? -20.25860 -5.22299 9.43255   1.000 17.04684 ?  81  GLY A CA    1 
ATOM   555  C  C     . GLY A 1 76  ? -19.97767 -3.90230 8.75556   1.000 15.48869 ?  81  GLY A C     1 
ATOM   556  O  O     . GLY A 1 76  ? -19.12012 -3.85266 7.86862   1.000 16.26990 ?  81  GLY A O     1 
ATOM   557  N  N     . ALA A 1 77  ? -20.67339 -2.83115 9.13428   1.000 13.92053 ?  82  ALA A N     1 
ATOM   558  C  CA    . ALA A 1 77  ? -20.38547 -1.52239 8.56341   1.000 12.40652 ?  82  ALA A CA    1 
ATOM   559  C  C     . ALA A 1 77  ? -18.95358 -1.12424 8.88957   1.000 13.21151 ?  82  ALA A C     1 
ATOM   560  O  O     . ALA A 1 77  ? -18.49878 -1.26815 10.02805  1.000 15.33619 ?  82  ALA A O     1 
ATOM   561  C  CB    . ALA A 1 77  ? -21.35670 -0.47872 9.11489   1.000 12.70120 ?  82  ALA A CB    1 
ATOM   562  N  N     . GLN A 1 78  ? -18.24086 -0.62898 7.87986   1.000 12.52912 ?  83  GLN A N     1 
ATOM   563  C  CA    . GLN A 1 78  ? -16.84665 -0.24729 8.02377   1.000 12.02646 ?  83  GLN A CA    1 
ATOM   564  C  C     . GLN A 1 78  ? -16.62366 1.25671  7.96582   1.000 11.00762 ?  83  GLN A C     1 
ATOM   565  O  O     . GLN A 1 78  ? -15.53437 1.71929  8.32254   1.000 13.33747 ?  83  GLN A O     1 
ATOM   566  C  CB    . GLN A 1 78  ? -15.99704 -0.96132 6.96292   1.000 14.52228 ?  83  GLN A CB    1 
ATOM   567  C  CG    . GLN A 1 78  ? -15.94884 -2.46215 7.18334   1.000 15.19648 ?  83  GLN A CG    1 
ATOM   568  C  CD    . GLN A 1 78  ? -15.50129 -3.22984 5.96142   1.000 15.20168 ?  83  GLN A CD    1 
ATOM   569  O  OE1   . GLN A 1 78  ? -16.10984 -3.13508 4.89653   1.000 16.23361 ?  83  GLN A OE1   1 
ATOM   570  N  NE2   . GLN A 1 78  ? -14.43845 -4.00811 6.11094   1.000 18.51394 ?  83  GLN A NE2   1 
ATOM   571  N  N     . ALA A 1 79  ? -17.61966 2.02507  7.53227   1.000 10.72950 ?  84  ALA A N     1 
ATOM   572  C  CA    . ALA A 1 79  ? -17.56746 3.47947  7.58234   1.000 10.40742 ?  84  ALA A CA    1 
ATOM   573  C  C     . ALA A 1 79  ? -18.99856 3.99212  7.59976   1.000 8.91416  ?  84  ALA A C     1 
ATOM   574  O  O     . ALA A 1 79  ? -19.93060 3.27988  7.21733   1.000 10.07923 ?  84  ALA A O     1 
ATOM   575  C  CB    . ALA A 1 79  ? -16.78457 4.06497  6.40303   1.000 11.13433 ?  84  ALA A CB    1 
ATOM   576  N  N     . CYS A 1 80  ? -19.16637 5.23526  8.05230   1.000 8.74534  ?  85  CYS A N     1 
ATOM   577  C  CA    . CYS A 1 80  ? -20.50081 5.77953  8.27862   1.000 8.60615  ?  85  CYS A CA    1 
ATOM   578  C  C     . CYS A 1 80  ? -20.57374 7.25081  7.89564   1.000 7.23883  ?  85  CYS A C     1 
ATOM   579  O  O     . CYS A 1 80  ? -19.69071 8.03317  8.25630   1.000 8.98708  ?  85  CYS A O     1 
ATOM   580  C  CB    . CYS A 1 80  ? -20.88786 5.61574  9.75304   1.000 11.38731 ?  85  CYS A CB    1 
ATOM   581  S  SG    . CYS A 1 80  ? -22.42309 6.43719  10.22201  1.000 13.74534 ?  85  CYS A SG    1 
ATOM   582  N  N     . VAL A 1 81  ? -21.63296 7.62481  7.17986   1.000 7.96763  ?  86  VAL A N     1 
ATOM   583  C  CA    . VAL A 1 81  ? -21.97267 9.02489  6.93457   1.000 7.34095  ?  86  VAL A CA    1 
ATOM   584  C  C     . VAL A 1 81  ? -23.15437 9.37501  7.83013   1.000 7.18148  ?  86  VAL A C     1 
ATOM   585  O  O     . VAL A 1 81  ? -24.19488 8.71115  7.77231   1.000 8.04779  ?  86  VAL A O     1 
ATOM   586  C  CB    . VAL A 1 81  ? -22.34352 9.26976  5.46176   1.000 9.26481  ?  86  VAL A CB    1 
ATOM   587  C  CG1   . VAL A 1 81  ? -22.57131 10.75119 5.22056   1.000 10.18478 ?  86  VAL A CG1   1 
ATOM   588  C  CG2   . VAL A 1 81  ? -21.27955 8.74219  4.51862   1.000 10.12578 ?  86  VAL A CG2   1 
ATOM   589  N  N     . LEU A 1 82  ? -23.00353 10.41177 8.65488   1.000 7.11261  ?  87  LEU A N     1 
ATOM   590  C  CA    . LEU A 1 82  ? -24.10405 10.98068 9.42947   1.000 7.74111  ?  87  LEU A CA    1 
ATOM   591  C  C     . LEU A 1 82  ? -24.59804 12.21440 8.68660   1.000 5.73751  ?  87  LEU A C     1 
ATOM   592  O  O     . LEU A 1 82  ? -23.82673 13.15795 8.47909   1.000 8.61584  ?  87  LEU A O     1 
ATOM   593  C  CB    . LEU A 1 82  ? -23.62525 11.40314 10.81700  1.000 9.64257  ?  87  LEU A CB    1 
ATOM   594  C  CG    . LEU A 1 82  ? -23.00603 10.35852 11.74080  1.000 11.35602 ?  87  LEU A CG    1 
ATOM   595  C  CD1   . LEU A 1 82  ? -22.46531 11.03294 12.98970  1.000 13.07721 ?  87  LEU A CD1   1 
ATOM   596  C  CD2   . LEU A 1 82  ? -24.02588 9.30375  12.10954  1.000 13.41078 ?  87  LEU A CD2   1 
ATOM   597  N  N     . VAL A 1 83  ? -25.87317 12.21801 8.29685   1.000 5.65655  ?  88  VAL A N     1 
ATOM   598  C  CA    . VAL A 1 83  ? -26.42637 13.26251 7.43936   1.000 7.07392  ?  88  VAL A CA    1 
ATOM   599  C  C     . VAL A 1 83  ? -27.53034 14.00126 8.18127   1.000 5.90200  ?  88  VAL A C     1 
ATOM   600  O  O     . VAL A 1 83  ? -28.41885 13.37570 8.76942   1.000 7.12023  ?  88  VAL A O     1 
ATOM   601  C  CB    . VAL A 1 83  ? -26.97963 12.68753 6.12185   1.000 7.93185  ?  88  VAL A CB    1 
ATOM   602  C  CG1   . VAL A 1 83  ? -27.40796 13.81532 5.19002   1.000 8.16691  ?  88  VAL A CG1   1 
ATOM   603  C  CG2   . VAL A 1 83  ? -25.96411 11.78772 5.44745   1.000 8.41647  ?  88  VAL A CG2   1 
ATOM   604  N  N     . PHE A 1 84  ? -27.48562 15.32989 8.13515   1.000 6.35763  ?  89  PHE A N     1 
ATOM   605  C  CA    . PHE A 1 84  ? -28.64336 16.14926 8.45773   1.000 6.42068  ?  89  PHE A CA    1 
ATOM   606  C  C     . PHE A 1 84  ? -28.89860 17.11472 7.30880   1.000 5.04277  ?  89  PHE A C     1 
ATOM   607  O  O     . PHE A 1 84  ? -28.06118 17.28969 6.42017   1.000 7.10426  ?  89  PHE A O     1 
ATOM   608  C  CB    . PHE A 1 84  ? -28.49887 16.88326 9.80065   1.000 6.87693  ?  89  PHE A CB    1 
ATOM   609  C  CG    . PHE A 1 84  ? -27.44132 17.95204 9.81361   1.000 7.41735  ?  89  PHE A CG    1 
ATOM   610  C  CD1   . PHE A 1 84  ? -26.12349 17.63104 10.09552  1.000 8.17671  ?  89  PHE A CD1   1 
ATOM   611  C  CD2   . PHE A 1 84  ? -27.77057 19.28079 9.58453   1.000 6.99749  ?  89  PHE A CD2   1 
ATOM   612  C  CE1   . PHE A 1 84  ? -25.14673 18.61060 10.12775  1.000 8.58680  ?  89  PHE A CE1   1 
ATOM   613  C  CE2   . PHE A 1 84  ? -26.79764 20.26558 9.61781   1.000 8.12214  ?  89  PHE A CE2   1 
ATOM   614  C  CZ    . PHE A 1 84  ? -25.48787 19.92767 9.89595   1.000 8.41905  ?  89  PHE A CZ    1 
ATOM   615  N  N     . SER A 1 85  ? -30.07048 17.74301 7.32568   1.000 6.26000  ?  90  SER A N     1 
ATOM   616  C  CA    . SER A 1 85  ? -30.49455 18.63291 6.25537   1.000 6.34690  ?  90  SER A CA    1 
ATOM   617  C  C     . SER A 1 85  ? -30.44936 20.09077 6.69003   1.000 6.88786  ?  90  SER A C     1 
ATOM   618  O  O     . SER A 1 85  ? -30.90154 20.44153 7.78638   1.000 8.08923  ?  90  SER A O     1 
ATOM   619  C  CB    . SER A 1 85  ? -31.91172 18.30153 5.79802   1.000 8.30687  ?  90  SER A CB    1 
ATOM   620  O  OG    . SER A 1 85  ? -32.42186 19.35747 5.00222   1.000 9.25477  ?  90  SER A OG    1 
ATOM   621  N  N     . THR A 1 86  ? -29.93518 20.93588 5.78899   1.000 7.32780  ?  91  THR A N     1 
ATOM   622  C  CA    . THR A 1 86  ? -29.92492 22.38433 5.98321   1.000 7.67982  ?  91  THR A CA    1 
ATOM   623  C  C     . THR A 1 86  ? -31.29287 22.93131 6.38642   1.000 9.07899  ?  91  THR A C     1 
ATOM   624  O  O     . THR A 1 86  ? -31.37249 23.91519 7.13088   1.000 9.97110  ?  91  THR A O     1 
ATOM   625  C  CB    . THR A 1 86  ? -29.45951 23.04632 4.67799   1.000 9.87573  ?  91  THR A CB    1 
ATOM   626  O  OG1   . THR A 1 86  ? -28.08987 22.71152 4.42520   1.000 8.99117  ?  91  THR A OG1   1 
ATOM   627  C  CG2   . THR A 1 86  ? -29.59649 24.56159 4.72520   1.000 11.38094 ?  91  THR A CG2   1 
ATOM   628  N  N     . THR A 1 87  ? -32.37833 22.31035 5.92223   1.000 8.80694  ?  92  THR A N     1 
ATOM   629  C  CA    . THR A 1 87  ? -33.71752 22.85813 6.10132   1.000 9.65134  ?  92  THR A CA    1 
ATOM   630  C  C     . THR A 1 87  ? -34.53440 22.12511 7.16282   1.000 11.86186 ?  92  THR A C     1 
ATOM   631  O  O     . THR A 1 87  ? -35.75618 22.29933 7.21944   1.000 15.22380 ?  92  THR A O     1 
ATOM   632  C  CB    . THR A 1 87  ? -34.46884 22.85713 4.77054   1.000 11.27469 ?  92  THR A CB    1 
ATOM   633  O  OG1   . THR A 1 87  ? -34.56736 21.51240 4.28669   1.000 13.59847 ?  92  THR A OG1   1 
ATOM   634  C  CG2   . THR A 1 87  ? -33.74263 23.71879 3.74331   1.000 13.93454 ?  92  THR A CG2   1 
ATOM   635  N  N     . ASP A 1 88  ? -33.89610 21.32014 8.01079   1.000 9.87400  ?  93  ASP A N     1 
ATOM   636  C  CA    . ASP A 1 88  ? -34.62360 20.46938 8.95696   1.000 9.47883  ?  93  ASP A CA    1 
ATOM   637  C  C     . ASP A 1 88  ? -33.87583 20.49569 10.28817  1.000 8.91890  ?  93  ASP A C     1 
ATOM   638  O  O     . ASP A 1 88  ? -32.91255 19.75154 10.48184  1.000 8.86098  ?  93  ASP A O     1 
ATOM   639  C  CB    . ASP A 1 88  ? -34.75904 19.05522 8.39639   1.000 9.68516  ?  93  ASP A CB    1 
ATOM   640  C  CG    . ASP A 1 88  ? -35.53160 18.11655 9.31011   1.000 12.43620 ?  93  ASP A CG    1 
ATOM   641  O  OD1   . ASP A 1 88  ? -35.78074 18.44995 10.48594  1.000 13.30030 ?  93  ASP A OD1   1 
ATOM   642  O  OD2   . ASP A 1 88  ? -35.89152 17.01905 8.84057   1.000 14.47272 ?  93  ASP A OD2   1 
ATOM   643  N  N     . ARG A 1 89  ? -34.34146 21.33596 11.21600  1.000 9.22644  ?  94  ARG A N     1 
ATOM   644  C  CA    . ARG A 1 89  ? -33.66639 21.45796 12.50506  1.000 9.77051  ?  94  ARG A CA    1 
ATOM   645  C  C     . ARG A 1 89  ? -33.69650 20.14609 13.27781  1.000 9.15361  ?  94  ARG A C     1 
ATOM   646  O  O     . ARG A 1 89  ? -32.71604 19.78273 13.93987  1.000 8.45273  ?  94  ARG A O     1 
ATOM   647  C  CB    . ARG A 1 89  ? -34.31164 22.56505 13.33336  1.000 9.53213  ?  94  ARG A CB    1 
ATOM   648  C  CG    . ARG A 1 89  ? -33.62898 22.79200 14.66667  1.000 11.74813 ?  94  ARG A CG    1 
ATOM   649  C  CD    . ARG A 1 89  ? -32.28461 23.46021 14.46572  1.000 13.23886 ?  94  ARG A CD    1 
ATOM   650  N  NE    . ARG A 1 89  ? -31.46081 23.44233 15.67008  1.000 12.16830 ?  94  ARG A NE    1 
ATOM   651  C  CZ    . ARG A 1 89  ? -30.39675 24.21681 15.85095  1.000 12.38322 ?  94  ARG A CZ    1 
ATOM   652  N  NH1   . ARG A 1 89  ? -30.04048 25.08524 14.91362  1.000 13.32075 ?  94  ARG A NH1   1 
ATOM   653  N  NH2   . ARG A 1 89  ? -29.69509 24.13137 16.97176  1.000 14.04075 ?  94  ARG A NH2   1 
ATOM   654  N  N     . GLU A 1 90  ? -34.82081 19.42817 13.22269  1.000 9.64743  ?  95  GLU A N     1 
ATOM   655  C  CA    . GLU A 1 90  ? -34.91268 18.15913 13.93442  1.000 9.38649  ?  95  GLU A CA    1 
ATOM   656  C  C     . GLU A 1 90  ? -33.85817 17.17475 13.44523  1.000 9.32927  ?  95  GLU A C     1 
ATOM   657  O  O     . GLU A 1 90  ? -33.29672 16.41143 14.23849  1.000 8.47475  ?  95  GLU A O     1 
ATOM   658  C  CB    . GLU A 1 90  ? -36.31686 17.57479 13.79011  1.000 12.52969 ?  95  GLU A CB    1 
ATOM   659  C  CG    . GLU A 1 90  ? -37.40392 18.40780 14.45582  1.000 16.75917 ?  95  GLU A CG    1 
ATOM   660  N  N     . SER A 1 91  ? -33.55429 17.19392 12.14586  1.000 7.62559  ?  96  SER A N     1 
ATOM   661  C  CA    . SER A 1 91  ? -32.53941 16.28578 11.62589  1.000 7.12547  ?  96  SER A CA    1 
ATOM   662  C  C     . SER A 1 91  ? -31.16188 16.61680 12.18432  1.000 7.18542  ?  96  SER A C     1 
ATOM   663  O  O     . SER A 1 91  ? -30.35731 15.71079 12.42938  1.000 7.64574  ?  96  SER A O     1 
ATOM   664  C  CB    . SER A 1 91  ? -32.54295 16.30383 10.09484  1.000 7.29739  ?  96  SER A CB    1 
ATOM   665  O  OG    . SER A 1 91  ? -31.92545 17.46288 9.55671   1.000 7.15194  ?  96  SER A OG    1 
ATOM   666  N  N     . PHE A 1 92  ? -30.88561 17.90374 12.40785  1.000 6.57328  ?  97  PHE A N     1 
ATOM   667  C  CA    . PHE A 1 92  ? -29.63954 18.31219 13.04703  1.000 7.39316  ?  97  PHE A CA    1 
ATOM   668  C  C     . PHE A 1 92  ? -29.60541 17.87012 14.50395  1.000 7.75432  ?  97  PHE A C     1 
ATOM   669  O  O     . PHE A 1 92  ? -28.60301 17.32001 14.97597  1.000 8.02073  ?  97  PHE A O     1 
ATOM   670  C  CB    . PHE A 1 92  ? -29.50557 19.83175 12.93832  1.000 7.55739  ?  97  PHE A CB    1 
ATOM   671  C  CG    . PHE A 1 92  ? -28.29192 20.40113 13.62114  1.000 8.00797  ?  97  PHE A CG    1 
ATOM   672  C  CD1   . PHE A 1 92  ? -27.02725 20.19501 13.09827  1.000 8.84890  ?  97  PHE A CD1   1 
ATOM   673  C  CD2   . PHE A 1 92  ? -28.42419 21.18188 14.75901  1.000 9.74526  ?  97  PHE A CD2   1 
ATOM   674  C  CE1   . PHE A 1 92  ? -25.91050 20.73442 13.71400  1.000 9.16289  ?  97  PHE A CE1   1 
ATOM   675  C  CE2   . PHE A 1 92  ? -27.31312 21.72864 15.38115  1.000 9.91837  ?  97  PHE A CE2   1 
ATOM   676  C  CZ    . PHE A 1 92  ? -26.05486 21.50494 14.85696  1.000 9.94249  ?  97  PHE A CZ    1 
ATOM   677  N  N     . GLU A 1 93  ? -30.69722 18.10400 15.23551  1.000 7.72589  ?  98  GLU A N     1 
ATOM   678  C  CA    . GLU A 1 93  ? -30.73245 17.72620 16.64320  1.000 8.48125  ?  98  GLU A CA    1 
ATOM   679  C  C     . GLU A 1 93  ? -30.57965 16.22251 16.82846  1.000 7.98457  ?  98  GLU A C     1 
ATOM   680  O  O     . GLU A 1 93  ? -30.08656 15.77390 17.86975  1.000 10.53154 ?  98  GLU A O     1 
ATOM   681  C  CB    . GLU A 1 93  ? -32.02790 18.22110 17.28422  1.000 10.92199 ?  98  GLU A CB    1 
ATOM   682  C  CG    . GLU A 1 93  ? -32.19015 19.73824 17.28500  1.000 11.42063 ?  98  GLU A CG    1 
ATOM   683  C  CD    . GLU A 1 93  ? -31.25357 20.44380 18.25318  1.000 13.41034 ?  98  GLU A CD    1 
ATOM   684  O  OE1   . GLU A 1 93  ? -30.69940 19.78019 19.15454  1.000 16.08429 ?  98  GLU A OE1   1 
ATOM   685  O  OE2   . GLU A 1 93  ? -31.07007 21.67037 18.11073  1.000 15.24602 ?  98  GLU A OE2   1 
ATOM   686  N  N     . ALA A 1 94  ? -30.97852 15.43045 15.83157  1.000 7.46768  ?  99  ALA A N     1 
ATOM   687  C  CA    . ALA A 1 94  ? -30.92712 13.97624 15.93181  1.000 8.08385  ?  99  ALA A CA    1 
ATOM   688  C  C     . ALA A 1 94  ? -29.54550 13.39014 15.65812  1.000 7.67553  ?  99  ALA A C     1 
ATOM   689  O  O     . ALA A 1 94  ? -29.37488 12.17582 15.80960  1.000 9.18577  ?  99  ALA A O     1 
ATOM   690  C  CB    . ALA A 1 94  ? -31.95010 13.34753 14.97968  1.000 9.48609  ?  99  ALA A CB    1 
ATOM   691  N  N     . VAL A 1 95  ? -28.56374 14.20373 15.25923  1.000 7.21109  ?  100 VAL A N     1 
ATOM   692  C  CA    . VAL A 1 95  ? -27.27381 13.65902 14.82617  1.000 7.52748  ?  100 VAL A CA    1 
ATOM   693  C  C     . VAL A 1 95  ? -26.63047 12.81926 15.92653  1.000 8.21582  ?  100 VAL A C     1 
ATOM   694  O  O     . VAL A 1 95  ? -26.14518 11.70942 15.67723  1.000 9.27218  ?  100 VAL A O     1 
ATOM   695  C  CB    . VAL A 1 95  ? -26.34163 14.77855 14.32838  1.000 7.80879  ?  100 VAL A CB    1 
ATOM   696  C  CG1   . VAL A 1 95  ? -24.91075 14.26362 14.17857  1.000 9.10047  ?  100 VAL A CG1   1 
ATOM   697  C  CG2   . VAL A 1 95  ? -26.85409 15.34515 13.00955  1.000 9.28113  ?  100 VAL A CG2   1 
ATOM   698  N  N     . SER A 1 96  ? -26.60684 13.33561 17.15856  1.000 8.29514  ?  101 SER A N     1 
ATOM   699  C  CA    . SER A 1 96  ? -25.97972 12.58703 18.24521  1.000 9.22465  ?  101 SER A CA    1 
ATOM   700  C  C     . SER A 1 96  ? -26.66437 11.24271 18.45405  1.000 9.39025  ?  101 SER A C     1 
ATOM   701  O  O     . SER A 1 96  ? -25.99647 10.22752 18.68613  1.000 10.45193 ?  101 SER A O     1 
ATOM   702  C  CB    . SER A 1 96  ? -25.99007 13.40747 19.53461  1.000 12.93494 ?  101 SER A CB    1 
ATOM   703  O  OG    . SER A 1 96  ? -25.46475 12.65235 20.60909  1.000 14.64081 ?  101 SER A OG    1 
ATOM   704  N  N     A SER A 1 97  ? -27.99823 11.21637 18.37078  0.500 9.16078  ?  102 SER A N     1 
ATOM   705  N  N     B SER A 1 97  ? -27.99650 11.21476 18.36526  0.500 8.50848  ?  102 SER A N     1 
ATOM   706  C  CA    A SER A 1 97  ? -28.72983 9.96218  18.52330  0.500 11.19223 ?  102 SER A CA    1 
ATOM   707  C  CA    B SER A 1 97  ? -28.72557 9.96088  18.52577  0.500 9.99569  ?  102 SER A CA    1 
ATOM   708  C  C     A SER A 1 97  ? -28.33078 8.95748  17.45016  0.500 10.28087 ?  102 SER A C     1 
ATOM   709  C  C     B SER A 1 97  ? -28.34040 8.95488  17.44802  0.500 9.34663  ?  102 SER A C     1 
ATOM   710  O  O     A SER A 1 97  ? -28.15441 7.76765  17.73746  0.500 11.42541 ?  102 SER A O     1 
ATOM   711  O  O     B SER A 1 97  ? -28.18384 7.76095  17.73004  0.500 9.89143  ?  102 SER A O     1 
ATOM   712  C  CB    A SER A 1 97  ? -30.23507 10.22603 18.47593  0.500 14.37478 ?  102 SER A CB    1 
ATOM   713  C  CB    B SER A 1 97  ? -30.22900 10.22907 18.50096  0.500 11.59119 ?  102 SER A CB    1 
ATOM   714  O  OG    A SER A 1 97  ? -30.63074 11.13123 19.49089  0.500 18.85731 ?  102 SER A OG    1 
ATOM   715  O  OG    B SER A 1 97  ? -30.95815 9.01858  18.56991  0.500 13.35579 ?  102 SER A OG    1 
ATOM   716  N  N     . TRP A 1 98  ? -28.18099 9.41704  16.20530  1.000 8.61028  ?  103 TRP A N     1 
ATOM   717  C  CA    . TRP A 1 98  ? -27.72956 8.52114  15.14452  1.000 7.91219  ?  103 TRP A CA    1 
ATOM   718  C  C     . TRP A 1 98  ? -26.30656 8.04403  15.39754  1.000 9.25762  ?  103 TRP A C     1 
ATOM   719  O  O     . TRP A 1 98  ? -25.99714 6.86443  15.19122  1.000 10.74635 ?  103 TRP A O     1 
ATOM   720  C  CB    . TRP A 1 98  ? -27.82343 9.21223  13.78448  1.000 8.95397  ?  103 TRP A CB    1 
ATOM   721  C  CG    . TRP A 1 98  ? -29.21883 9.32497  13.26127  1.000 8.65511  ?  103 TRP A CG    1 
ATOM   722  C  CD1   . TRP A 1 98  ? -29.93956 10.47083 13.07557  1.000 9.14481  ?  103 TRP A CD1   1 
ATOM   723  C  CD2   . TRP A 1 98  ? -30.06635 8.24721  12.85099  1.000 8.84997  ?  103 TRP A CD2   1 
ATOM   724  N  NE1   . TRP A 1 98  ? -31.18227 10.17033 12.57430  1.000 9.52048  ?  103 TRP A NE1   1 
ATOM   725  C  CE2   . TRP A 1 98  ? -31.28556 8.81194  12.42834  1.000 9.53394  ?  103 TRP A CE2   1 
ATOM   726  C  CE3   . TRP A 1 98  ? -29.91209 6.85831  12.80010  1.000 10.58845 ?  103 TRP A CE3   1 
ATOM   727  C  CZ2   . TRP A 1 98  ? -32.34469 8.03727  11.96200  1.000 10.88110 ?  103 TRP A CZ2   1 
ATOM   728  C  CZ3   . TRP A 1 98  ? -30.96561 6.09029  12.33976  1.000 12.64221 ?  103 TRP A CZ3   1 
ATOM   729  C  CH2   . TRP A 1 98  ? -32.16584 6.68155  11.92517  1.000 12.92338 ?  103 TRP A CH2   1 
ATOM   730  N  N     . ARG A 1 99  ? -25.42738 8.95106  15.83107  1.000 10.12362 ?  104 ARG A N     1 
ATOM   731  C  CA    A ARG A 1 99  ? -24.05376 8.56991  16.14292  0.500 11.04456 ?  104 ARG A CA    1 
ATOM   732  C  CA    B ARG A 1 99  ? -24.05353 8.56730  16.14000  0.500 11.29677 ?  104 ARG A CA    1 
ATOM   733  C  C     . ARG A 1 99  ? -24.01982 7.45868  17.18343  1.000 12.54728 ?  104 ARG A C     1 
ATOM   734  O  O     . ARG A 1 99  ? -23.30908 6.45929  17.02197  1.000 13.16129 ?  104 ARG A O     1 
ATOM   735  C  CB    A ARG A 1 99  ? -23.28176 9.79745  16.63214  0.500 11.83278 ?  104 ARG A CB    1 
ATOM   736  C  CB    B ARG A 1 99  ? -23.26621 9.78746  16.62463  0.500 12.62431 ?  104 ARG A CB    1 
ATOM   737  C  CG    A ARG A 1 99  ? -21.98762 9.49837  17.38107  0.500 16.42684 ?  104 ARG A CG    1 
ATOM   738  C  CG    B ARG A 1 99  ? -21.84715 9.48163  17.10182  0.500 17.67870 ?  104 ARG A CG    1 
ATOM   739  C  CD    A ARG A 1 99  ? -20.95253 8.85421  16.47967  0.500 17.96229 ?  104 ARG A CD    1 
ATOM   740  C  CD    B ARG A 1 99  ? -20.84139 9.54145  15.96342  0.500 20.94897 ?  104 ARG A CD    1 
ATOM   741  N  NE    A ARG A 1 99  ? -19.60318 9.33829  16.76178  0.500 16.99205 ?  104 ARG A NE    1 
ATOM   742  N  NE    B ARG A 1 99  ? -19.52600 9.03692  16.35652  0.500 21.98695 ?  104 ARG A NE    1 
ATOM   743  C  CZ    A ARG A 1 99  ? -18.51678 8.93622  16.11040  0.500 17.87720 ?  104 ARG A CZ    1 
ATOM   744  C  CZ    B ARG A 1 99  ? -18.56405 9.78099  16.89444  0.500 22.62609 ?  104 ARG A CZ    1 
ATOM   745  N  NH1   A ARG A 1 99  ? -18.61963 8.03563  15.14329  0.500 19.52919 ?  104 ARG A NH1   1 
ATOM   746  N  NH1   B ARG A 1 99  ? -18.76319 11.07330 17.11449  0.500 22.03287 ?  104 ARG A NH1   1 
ATOM   747  N  NH2   A ARG A 1 99  ? -17.32758 9.43255  16.42370  0.500 17.96861 ?  104 ARG A NH2   1 
ATOM   748  N  NH2   B ARG A 1 99  ? -17.40021 9.23131  17.21630  0.500 24.11651 ?  104 ARG A NH2   1 
ATOM   749  N  N     . GLU A 1 100 ? -24.79288 7.61439  18.25946  1.000 11.77105 ?  105 GLU A N     1 
ATOM   750  C  CA    . GLU A 1 100 ? -24.77773 6.61300  19.31906  1.000 13.14754 ?  105 GLU A CA    1 
ATOM   751  C  C     . GLU A 1 100 ? -25.39786 5.29618  18.86745  1.000 13.07616 ?  105 GLU A C     1 
ATOM   752  O  O     . GLU A 1 100 ? -24.98364 4.22976  19.33707  1.000 15.78498 ?  105 GLU A O     1 
ATOM   753  C  CB    . GLU A 1 100 ? -25.45125 7.15911  20.57803  1.000 14.87209 ?  105 GLU A CB    1 
ATOM   754  C  CG    . GLU A 1 100 ? -24.76307 8.40024  21.14516  1.000 18.33912 ?  105 GLU A CG    1 
ATOM   755  C  CD    . GLU A 1 100 ? -23.27812 8.18733  21.40834  1.000 23.15895 ?  105 GLU A CD    1 
ATOM   756  O  OE1   . GLU A 1 100 ? -22.90809 7.11847  21.94126  1.000 26.00777 ?  105 GLU A OE1   1 
ATOM   757  O  OE2   . GLU A 1 100 ? -22.47802 9.09085  21.07881  1.000 23.68071 ?  105 GLU A OE2   1 
ATOM   758  N  N     . LYS A 1 101 ? -26.37565 5.34362  17.95725  1.000 13.40770 ?  106 LYS A N     1 
ATOM   759  C  CA    . LYS A 1 101 ? -26.93288 4.10698  17.41806  1.000 12.91881 ?  106 LYS A CA    1 
ATOM   760  C  C     . LYS A 1 101 ? -25.87763 3.32452  16.65039  1.000 13.55591 ?  106 LYS A C     1 
ATOM   761  O  O     . LYS A 1 101 ? -25.76852 2.10133  16.79805  1.000 15.45124 ?  106 LYS A O     1 
ATOM   762  C  CB    . LYS A 1 101 ? -28.12899 4.41116  16.51545  1.000 14.45762 ?  106 LYS A CB    1 
ATOM   763  C  CG    . LYS A 1 101 ? -29.39380 4.82700  17.25418  1.000 18.32927 ?  106 LYS A CG    1 
ATOM   764  C  CD    . LYS A 1 101 ? -30.46769 5.28608  16.27663  1.000 21.86863 ?  106 LYS A CD    1 
ATOM   765  C  CE    . LYS A 1 101 ? -31.72672 5.74248  16.99676  1.000 25.81919 ?  106 LYS A CE    1 
ATOM   766  N  NZ    . LYS A 1 101 ? -32.77690 6.17859  16.03113  1.000 27.39643 ?  106 LYS A NZ    1 
ATOM   767  N  N     . VAL A 1 102 ? -25.08158 4.01454  15.83359  1.000 11.48971 ?  107 VAL A N     1 
ATOM   768  C  CA    . VAL A 1 102 ? -24.04986 3.33029  15.06186  1.000 10.84212 ?  107 VAL A CA    1 
ATOM   769  C  C     . VAL A 1 102 ? -22.97891 2.76718  15.98378  1.000 12.77009 ?  107 VAL A C     1 
ATOM   770  O  O     . VAL A 1 102 ? -22.55953 1.61225  15.83765  1.000 14.99684 ?  107 VAL A O     1 
ATOM   771  C  CB    . VAL A 1 102 ? -23.45789 4.27057  13.99748  1.000 11.91611 ?  107 VAL A CB    1 
ATOM   772  C  CG1   . VAL A 1 102 ? -22.29138 3.59990  13.28771  1.000 14.76367 ?  107 VAL A CG1   1 
ATOM   773  C  CG2   . VAL A 1 102 ? -24.53253 4.69817  13.00567  1.000 13.03887 ?  107 VAL A CG2   1 
ATOM   774  N  N     . VAL A 1 103 ? -22.52807 3.56946  16.95151  1.000 13.48299 ?  108 VAL A N     1 
ATOM   775  C  CA    . VAL A 1 103 ? -21.48980 3.12180  17.87464  1.000 15.26363 ?  108 VAL A CA    1 
ATOM   776  C  C     . VAL A 1 103 ? -21.95065 1.89428  18.64991  1.000 16.36309 ?  108 VAL A C     1 
ATOM   777  O  O     . VAL A 1 103 ? -21.18160 0.94765  18.85541  1.000 17.71682 ?  108 VAL A O     1 
ATOM   778  C  CB    . VAL A 1 103 ? -21.06175 4.27480  18.80215  1.000 16.70509 ?  108 VAL A CB    1 
ATOM   779  C  CG1   . VAL A 1 103 ? -20.13566 3.76289  19.89509  1.000 18.83793 ?  108 VAL A CG1   1 
ATOM   780  C  CG2   . VAL A 1 103 ? -20.38603 5.37515  17.99572  1.000 17.56868 ?  108 VAL A CG2   1 
ATOM   781  N  N     . ALA A 1 104 ? -23.21653 1.87904  19.07490  1.000 16.58223 ?  109 ALA A N     1 
ATOM   782  C  CA    . ALA A 1 104 ? -23.72411 0.73589  19.82672  1.000 18.03874 ?  109 ALA A CA    1 
ATOM   783  C  C     . ALA A 1 104 ? -23.71438 -0.53926 18.99525  1.000 18.64626 ?  109 ALA A C     1 
ATOM   784  O  O     . ALA A 1 104 ? -23.61427 -1.63892 19.55155  1.000 21.04274 ?  109 ALA A O     1 
ATOM   785  C  CB    . ALA A 1 104 ? -25.13340 1.02545  20.34279  1.000 18.14423 ?  109 ALA A CB    1 
ATOM   786  N  N     . GLU A 1 105 ? -23.80631 -0.41777 17.67082  1.000 17.46061 ?  110 GLU A N     1 
ATOM   787  C  CA    . GLU A 1 105 ? -23.84899 -1.58865 16.80225  1.000 18.78577 ?  110 GLU A CA    1 
ATOM   788  C  C     . GLU A 1 105 ? -22.45949 -2.08004 16.40287  1.000 19.74447 ?  110 GLU A C     1 
ATOM   789  O  O     . GLU A 1 105 ? -22.18843 -3.28275 16.46227  1.000 21.19569 ?  110 GLU A O     1 
ATOM   790  C  CB    . GLU A 1 105 ? -24.68873 -1.29801 15.55198  1.000 20.61791 ?  110 GLU A CB    1 
ATOM   791  C  CG    . GLU A 1 105 ? -26.15979 -1.03257 15.83131  1.000 22.98808 ?  110 GLU A CG    1 
ATOM   792  C  CD    . GLU A 1 105 ? -26.83928 -2.18228 16.54885  1.000 25.87642 ?  110 GLU A CD    1 
ATOM   793  O  OE1   . GLU A 1 105 ? -26.51405 -3.35303 16.25362  1.000 25.62564 ?  110 GLU A OE1   1 
ATOM   794  O  OE2   . GLU A 1 105 ? -27.69875 -1.91168 17.41364  1.000 27.85896 ?  110 GLU A OE2   1 
ATOM   795  N  N     . VAL A 1 106 ? -21.57169 -1.17491 15.99075  1.000 18.56798 ?  111 VAL A N     1 
ATOM   796  C  CA    . VAL A 1 106 ? -20.30198 -1.55578 15.38284  1.000 19.11645 ?  111 VAL A CA    1 
ATOM   797  C  C     . VAL A 1 106 ? -19.09052 -0.96696 16.08541  1.000 19.36410 ?  111 VAL A C     1 
ATOM   798  O  O     . VAL A 1 106 ? -17.95960 -1.23654 15.66677  1.000 22.74990 ?  111 VAL A O     1 
ATOM   799  C  CB    . VAL A 1 106 ? -20.26077 -1.24051 13.87401  1.000 18.94026 ?  111 VAL A CB    1 
ATOM   800  C  CG1   . VAL A 1 106 ? -21.31501 -2.04489 13.13576  1.000 20.87837 ?  111 VAL A CG1   1 
ATOM   801  C  CG2   . VAL A 1 106 ? -20.46230 0.24554  13.64240  1.000 18.61816 ?  111 VAL A CG2   1 
ATOM   802  N  N     . GLY A 1 107 ? -19.28099 -0.17669 17.13562  1.000 17.77039 ?  112 GLY A N     1 
ATOM   803  C  CA    . GLY A 1 107 ? -18.14890 0.43443  17.80207  1.000 19.25498 ?  112 GLY A CA    1 
ATOM   804  C  C     . GLY A 1 107 ? -17.55932 1.59299  17.02428  1.000 20.57511 ?  112 GLY A C     1 
ATOM   805  O  O     . GLY A 1 107 ? -18.28934 2.34591  16.37174  1.000 22.56829 ?  112 GLY A O     1 
ATOM   806  N  N     . ASP A 1 108 ? -16.23654 1.73926  17.07652  1.000 22.50174 ?  113 ASP A N     1 
ATOM   807  C  CA    . ASP A 1 108 ? -15.54569 2.87231  16.46796  1.000 22.56505 ?  113 ASP A CA    1 
ATOM   808  C  C     . ASP A 1 108 ? -15.21510 2.53898  15.01639  1.000 21.16300 ?  113 ASP A C     1 
ATOM   809  O  O     . ASP A 1 108 ? -14.40054 1.64989  14.74444  1.000 22.58362 ?  113 ASP A O     1 
ATOM   810  C  CB    . ASP A 1 108 ? -14.27897 3.20421  17.25397  1.000 24.11544 ?  113 ASP A CB    1 
ATOM   811  N  N     . ILE A 1 109 ? -15.85026 3.24730  14.08831  1.000 17.35827 ?  114 ILE A N     1 
ATOM   812  C  CA    . ILE A 1 109 ? -15.53734 3.12729  12.66468  1.000 15.07262 ?  114 ILE A CA    1 
ATOM   813  C  C     . ILE A 1 109 ? -15.39054 4.52866  12.08817  1.000 13.53562 ?  114 ILE A C     1 
ATOM   814  O  O     . ILE A 1 109 ? -15.94911 5.49897  12.62708  1.000 13.62691 ?  114 ILE A O     1 
ATOM   815  C  CB    . ILE A 1 109 ? -16.61800 2.32168  11.90372  1.000 14.65290 ?  114 ILE A CB    1 
ATOM   816  C  CG1   . ILE A 1 109 ? -17.98292 3.00834  12.00905  1.000 14.85887 ?  114 ILE A CG1   1 
ATOM   817  C  CG2   . ILE A 1 109 ? -16.67705 0.88574  12.40425  1.000 15.25717 ?  114 ILE A CG2   1 
ATOM   818  C  CD1   . ILE A 1 109 ? -19.01730 2.46451  11.03479  1.000 14.84482 ?  114 ILE A CD1   1 
ATOM   819  N  N     . PRO A 1 110 ? -14.63477 4.66909  10.99763  1.000 13.21293 ?  115 PRO A N     1 
ATOM   820  C  CA    . PRO A 1 110 ? -14.50902 5.97796  10.34130  1.000 12.86373 ?  115 PRO A CA    1 
ATOM   821  C  C     . PRO A 1 110 ? -15.86819 6.58592  10.02525  1.000 10.69329 ?  115 PRO A C     1 
ATOM   822  O  O     . PRO A 1 110 ? -16.73237 5.94692  9.41973   1.000 11.28172 ?  115 PRO A O     1 
ATOM   823  C  CB    . PRO A 1 110 ? -13.72900 5.65111  9.06417   1.000 15.65966 ?  115 PRO A CB    1 
ATOM   824  C  CG    . PRO A 1 110 ? -12.91608 4.46006  9.42758   1.000 16.18522 ?  115 PRO A CG    1 
ATOM   825  C  CD    . PRO A 1 110 ? -13.76371 3.65434  10.37516  1.000 14.18052 ?  115 PRO A CD    1 
ATOM   826  N  N     . THR A 1 111 ? -16.05692 7.83188  10.45324  1.000 9.90455  ?  116 THR A N     1 
ATOM   827  C  CA    . THR A 1 111 ? -17.34360 8.50189  10.34687  1.000 10.10158 ?  116 THR A CA    1 
ATOM   828  C  C     . THR A 1 111 ? -17.11876 9.93227  9.87923   1.000 9.70574  ?  116 THR A C     1 
ATOM   829  O  O     . THR A 1 111 ? -16.07460 10.53066 10.14634  1.000 10.71551 ?  116 THR A O     1 
ATOM   830  C  CB    . THR A 1 111 ? -18.08598 8.45387  11.69890  1.000 11.72959 ?  116 THR A CB    1 
ATOM   831  O  OG1   . THR A 1 111 ? -18.25671 7.08723  12.09633  1.000 13.37361 ?  116 THR A OG1   1 
ATOM   832  C  CG2   . THR A 1 111 ? -19.45730 9.11926  11.62148  1.000 12.43081 ?  116 THR A CG2   1 
ATOM   833  N  N     . VAL A 1 112 ? -18.10036 10.46661 9.15548   1.000 8.40834  ?  117 VAL A N     1 
ATOM   834  C  CA    . VAL A 1 112 ? -18.05799 11.83723 8.66858   1.000 8.32343  ?  117 VAL A CA    1 
ATOM   835  C  C     . VAL A 1 112 ? -19.43465 12.45391 8.87583   1.000 8.03614  ?  117 VAL A C     1 
ATOM   836  O  O     . VAL A 1 112 ? -20.45967 11.77120 8.78388   1.000 8.86377  ?  117 VAL A O     1 
ATOM   837  C  CB    . VAL A 1 112 ? -17.60898 11.89845 7.18520   1.000 10.23768 ?  117 VAL A CB    1 
ATOM   838  C  CG1   . VAL A 1 112 ? -18.63481 11.22949 6.27177   1.000 11.53783 ?  117 VAL A CG1   1 
ATOM   839  C  CG2   . VAL A 1 112 ? -17.32259 13.32909 6.74970   1.000 11.52219 ?  117 VAL A CG2   1 
ATOM   840  N  N     . LEU A 1 113 ? -19.45169 13.74907 9.18387   1.000 7.37857  ?  118 LEU A N     1 
ATOM   841  C  CA    . LEU A 1 113 ? -20.68703 14.50194 9.35870   1.000 7.04537  ?  118 LEU A CA    1 
ATOM   842  C  C     . LEU A 1 113 ? -20.96738 15.30213 8.09448   1.000 6.67918  ?  118 LEU A C     1 
ATOM   843  O  O     . LEU A 1 113 ? -20.07479 15.97319 7.57087   1.000 8.06485  ?  118 LEU A O     1 
ATOM   844  C  CB    . LEU A 1 113 ? -20.55944 15.45605 10.54695  1.000 8.70345  ?  118 LEU A CB    1 
ATOM   845  C  CG    . LEU A 1 113 ? -21.79616 16.29429 10.86707  1.000 9.31979  ?  118 LEU A CG    1 
ATOM   846  C  CD1   . LEU A 1 113 ? -22.96118 15.39644 11.26109  1.000 10.43026 ?  118 LEU A CD1   1 
ATOM   847  C  CD2   . LEU A 1 113 ? -21.48915 17.29771 11.96637  1.000 11.43178 ?  118 LEU A CD2   1 
ATOM   848  N  N     . VAL A 1 114 ? -22.20535 15.24356 7.61052   1.000 5.97073  ?  119 VAL A N     1 
ATOM   849  C  CA    . VAL A 1 114 ? -22.58412 15.91257 6.37119   1.000 6.28154  ?  119 VAL A CA    1 
ATOM   850  C  C     . VAL A 1 114 ? -23.82775 16.75446 6.60669   1.000 5.91050  ?  119 VAL A C     1 
ATOM   851  O  O     . VAL A 1 114 ? -24.83830 16.24839 7.10530   1.000 6.80541  ?  119 VAL A O     1 
ATOM   852  C  CB    . VAL A 1 114 ? -22.83403 14.90457 5.23527   1.000 6.37113  ?  119 VAL A CB    1 
ATOM   853  C  CG1   . VAL A 1 114 ? -23.38076 15.62208 4.01412   1.000 8.09872  ?  119 VAL A CG1   1 
ATOM   854  C  CG2   . VAL A 1 114 ? -21.55789 14.16886 4.89864   1.000 7.45912  ?  119 VAL A CG2   1 
ATOM   855  N  N     . GLN A 1 115 ? -23.75123 18.03541 6.24593   1.000 5.55081  ?  120 GLN A N     1 
ATOM   856  C  CA    . GLN A 1 115 ? -24.92334 18.89392 6.12868   1.000 6.54424  ?  120 GLN A CA    1 
ATOM   857  C  C     . GLN A 1 115 ? -25.31035 18.93355 4.65723   1.000 6.01499  ?  120 GLN A C     1 
ATOM   858  O  O     . GLN A 1 115 ? -24.61173 19.54645 3.84308   1.000 6.30159  ?  120 GLN A O     1 
ATOM   859  C  CB    . GLN A 1 115 ? -24.62605 20.30453 6.62584   1.000 7.25488  ?  120 GLN A CB    1 
ATOM   860  C  CG    . GLN A 1 115 ? -25.79301 21.25771 6.41844   1.000 8.08300  ?  120 GLN A CG    1 
ATOM   861  C  CD    . GLN A 1 115 ? -25.57868 22.60566 7.06961   1.000 9.19568  ?  120 GLN A CD    1 
ATOM   862  O  OE1   . GLN A 1 115 ? -24.72497 22.75932 7.94307   1.000 10.78939 ?  120 GLN A OE1   1 
ATOM   863  N  NE2   . GLN A 1 115 ? -26.35989 23.59271 6.64875   1.000 10.58856 ?  120 GLN A NE2   1 
ATOM   864  N  N     . ASN A 1 116 ? -26.41722 18.28254 4.31712   1.000 6.55740  ?  121 ASN A N     1 
ATOM   865  C  CA    . ASN A 1 116 ? -26.86445 18.22395 2.93500   1.000 6.21674  ?  121 ASN A CA    1 
ATOM   866  C  C     . ASN A 1 116 ? -27.85729 19.35250 2.63440   1.000 7.12186  ?  121 ASN A C     1 
ATOM   867  O  O     . ASN A 1 116 ? -28.32528 20.06598 3.52587   1.000 7.35452  ?  121 ASN A O     1 
ATOM   868  C  CB    . ASN A 1 116 ? -27.47117 16.84885 2.63558   1.000 7.12875  ?  121 ASN A CB    1 
ATOM   869  C  CG    . ASN A 1 116 ? -27.75001 16.63828 1.15516   1.000 6.95525  ?  121 ASN A CG    1 
ATOM   870  O  OD1   . ASN A 1 116 ? -26.94393 17.01656 0.29992   1.000 7.76834  ?  121 ASN A OD1   1 
ATOM   871  N  ND2   . ASN A 1 116 ? -28.89478 16.03519 0.84178   1.000 6.95655  ?  121 ASN A ND2   1 
ATOM   872  N  N     . LYS A 1 117 ? -28.17032 19.51269 1.34682   1.000 6.46473  ?  122 LYS A N     1 
ATOM   873  C  CA    . LYS A 1 117 ? -29.08851 20.54387 0.86116   1.000 7.30563  ?  122 LYS A CA    1 
ATOM   874  C  C     . LYS A 1 117 ? -28.54760 21.95323 1.07806   1.000 8.05916  ?  122 LYS A C     1 
ATOM   875  O  O     . LYS A 1 117 ? -29.31553 22.89246 1.29169   1.000 8.67156  ?  122 LYS A O     1 
ATOM   876  C  CB    . LYS A 1 117 ? -30.50965 20.40803 1.42516   1.000 8.04485  ?  122 LYS A CB    1 
ATOM   877  C  CG    . LYS A 1 117 ? -31.06218 18.98946 1.42920   1.000 7.19483  ?  122 LYS A CG    1 
ATOM   878  C  CD    . LYS A 1 117 ? -32.57735 18.98529 1.59457   1.000 7.24537  ?  122 LYS A CD    1 
ATOM   879  C  CE    . LYS A 1 117 ? -33.12248 17.56779 1.70936   1.000 7.05707  ?  122 LYS A CE    1 
ATOM   880  N  NZ    . LYS A 1 117 ? -34.60160 17.55866 1.89023   1.000 8.23179  ?  122 LYS A NZ    1 
ATOM   881  N  N     . ILE A 1 118 ? -27.22635 22.11813 0.99704   1.000 8.53770  ?  123 ILE A N     1 
ATOM   882  C  CA    . ILE A 1 118 ? -26.62725 23.42488 1.23192   1.000 9.53410  ?  123 ILE A CA    1 
ATOM   883  C  C     . ILE A 1 118 ? -27.04505 24.44072 0.17258   1.000 10.14214 ?  123 ILE A C     1 
ATOM   884  O  O     . ILE A 1 118 ? -26.88769 25.64872 0.37851   1.000 12.72301 ?  123 ILE A O     1 
ATOM   885  C  CB    . ILE A 1 118 ? -25.09291 23.29905 1.36534   1.000 11.25373 ?  123 ILE A CB    1 
ATOM   886  C  CG1   . ILE A 1 118 ? -24.52225 24.47153 2.16428   1.000 13.21292 ?  123 ILE A CG1   1 
ATOM   887  C  CG2   . ILE A 1 118 ? -24.43348 23.20375 -0.00040  1.000 11.80110 ?  123 ILE A CG2   1 
ATOM   888  C  CD1   . ILE A 1 118 ? -24.85837 24.42004 3.64149   1.000 14.01700 ?  123 ILE A CD1   1 
ATOM   889  N  N     . ASP A 1 119 ? -27.58531 23.98103 -0.95956  1.000 9.92619  ?  124 ASP A N     1 
ATOM   890  C  CA    . ASP A 1 119 ? -28.11771 24.89219 -1.96662  1.000 11.22958 ?  124 ASP A CA    1 
ATOM   891  C  C     . ASP A 1 119 ? -29.37273 25.61337 -1.49080  1.000 12.39992 ?  124 ASP A C     1 
ATOM   892  O  O     . ASP A 1 119 ? -29.75645 26.62382 -2.09052  1.000 14.05813 ?  124 ASP A O     1 
ATOM   893  C  CB    . ASP A 1 119 ? -28.42514 24.13243 -3.25900  1.000 9.83640  ?  124 ASP A CB    1 
ATOM   894  C  CG    . ASP A 1 119 ? -29.37811 22.96733 -3.03588  1.000 10.26047 ?  124 ASP A CG    1 
ATOM   895  O  OD1   . ASP A 1 119 ? -28.94623 21.93474 -2.47695  1.000 9.99086  ?  124 ASP A OD1   1 
ATOM   896  O  OD2   . ASP A 1 119 ? -30.57038 23.08993 -3.40074  1.000 12.01140 ?  124 ASP A OD2   1 
ATOM   897  N  N     . LEU A 1 120 ? -30.02235 25.11558 -0.43980  1.000 11.93575 ?  125 LEU A N     1 
ATOM   898  C  CA    . LEU A 1 120 ? -31.21806 25.73573 0.12989   1.000 12.72063 ?  125 LEU A CA    1 
ATOM   899  C  C     . LEU A 1 120 ? -30.88879 26.66592 1.28831   1.000 16.71099 ?  125 LEU A C     1 
ATOM   900  O  O     . LEU A 1 120 ? -31.65721 26.77390 2.24818   1.000 15.55935 ?  125 LEU A O     1 
ATOM   901  C  CB    . LEU A 1 120 ? -32.20727 24.65645 0.55637   1.000 13.84643 ?  125 LEU A CB    1 
ATOM   902  C  CG    . LEU A 1 120 ? -32.66828 23.67581 -0.52309  1.000 12.24392 ?  125 LEU A CG    1 
ATOM   903  C  CD1   . LEU A 1 120 ? -33.66932 22.69262 0.06251   1.000 12.35863 ?  125 LEU A CD1   1 
ATOM   904  C  CD2   . LEU A 1 120 ? -33.26405 24.41365 -1.71283  1.000 12.99579 ?  125 LEU A CD2   1 
ATOM   905  N  N     . LEU A 1 121 ? -29.74993 27.35821 1.21415   1.000 22.57624 ?  126 LEU A N     1 
ATOM   906  C  CA    . LEU A 1 121 ? -29.28730 28.17965 2.32741   1.000 26.34008 ?  126 LEU A CA    1 
ATOM   907  C  C     . LEU A 1 121 ? -30.28948 29.25683 2.72750   1.000 26.94860 ?  126 LEU A C     1 
ATOM   908  O  O     . LEU A 1 121 ? -30.25865 29.71502 3.87409   1.000 28.15957 ?  126 LEU A O     1 
ATOM   909  C  CB    . LEU A 1 121 ? -27.93321 28.80743 1.98724   1.000 30.21429 ?  126 LEU A CB    1 
ATOM   910  N  N     . ASP A 1 122 ? -31.18174 29.66446 1.82024   1.000 25.58881 ?  127 ASP A N     1 
ATOM   911  C  CA    . ASP A 1 122 ? -32.16799 30.68511 2.16503   1.000 29.61456 ?  127 ASP A CA    1 
ATOM   912  C  C     . ASP A 1 122 ? -33.20119 30.16789 3.16136   1.000 31.12647 ?  127 ASP A C     1 
ATOM   913  O  O     . ASP A 1 122 ? -33.79653 30.96014 3.90108   1.000 34.49057 ?  127 ASP A O     1 
ATOM   914  C  CB    . ASP A 1 122 ? -32.85152 31.20932 0.90197   1.000 31.20804 ?  127 ASP A CB    1 
ATOM   915  N  N     . ASP A 1 123 ? -33.43264 28.85473 3.19160   1.000 28.45575 ?  128 ASP A N     1 
ATOM   916  C  CA    . ASP A 1 123 ? -34.33550 28.22289 4.14523   1.000 25.75936 ?  128 ASP A CA    1 
ATOM   917  C  C     . ASP A 1 123 ? -33.58759 27.51460 5.26959   1.000 21.07056 ?  128 ASP A C     1 
ATOM   918  O  O     . ASP A 1 123 ? -34.12418 26.57700 5.87001   1.000 21.72809 ?  128 ASP A O     1 
ATOM   919  C  CB    . ASP A 1 123 ? -35.26197 27.23543 3.43126   1.000 26.63268 ?  128 ASP A CB    1 
ATOM   920  C  CG    . ASP A 1 123 ? -36.35868 27.92407 2.64493   1.000 45.62376 ?  128 ASP A CG    1 
ATOM   921  O  OD1   . ASP A 1 123 ? -36.04084 28.61537 1.65470   1.000 49.74555 ?  128 ASP A OD1   1 
ATOM   922  O  OD2   . ASP A 1 123 ? -37.54111 27.77025 3.01768   1.000 49.66211 ?  128 ASP A OD2   1 
ATOM   923  N  N     . SER A 1 124 ? -32.36391 27.94218 5.56346   1.000 18.37330 ?  129 SER A N     1 
ATOM   924  C  CA    . SER A 1 124 ? -31.52895 27.23175 6.52080   1.000 16.99465 ?  129 SER A CA    1 
ATOM   925  C  C     . SER A 1 124 ? -32.07037 27.36451 7.93953   1.000 16.14835 ?  129 SER A C     1 
ATOM   926  O  O     . SER A 1 124 ? -32.53953 28.43025 8.35120   1.000 19.45054 ?  129 SER A O     1 
ATOM   927  C  CB    . SER A 1 124 ? -30.10017 27.76720 6.46695   1.000 18.07476 ?  129 SER A CB    1 
ATOM   928  O  OG    . SER A 1 124 ? -29.28941 27.12823 7.43571   1.000 20.58100 ?  129 SER A OG    1 
ATOM   929  N  N     . CYS A 1 125 ? -31.99562 26.26358 8.68657   1.000 13.98318 ?  130 CYS A N     1 
ATOM   930  C  CA    . CYS A 1 125 ? -32.36616 26.21431 10.09412  1.000 14.28004 ?  130 CYS A CA    1 
ATOM   931  C  C     . CYS A 1 125 ? -31.16439 26.01471 11.00511  1.000 14.17592 ?  130 CYS A C     1 
ATOM   932  O  O     . CYS A 1 125 ? -31.33734 25.89991 12.22287  1.000 16.20751 ?  130 CYS A O     1 
ATOM   933  C  CB    . CYS A 1 125 ? -33.36752 25.07751 10.33780  1.000 20.53249 ?  130 CYS A CB    1 
ATOM   934  S  SG    . CYS A 1 125 ? -34.88086 25.17242 9.36835   1.000 28.05092 ?  130 CYS A SG    1 
ATOM   935  N  N     . ILE A 1 126 ? -29.95738 25.95459 10.45010  1.000 12.66545 ?  131 ILE A N     1 
ATOM   936  C  CA    . ILE A 1 126 ? -28.74139 25.69236 11.21043  1.000 12.77065 ?  131 ILE A CA    1 
ATOM   937  C  C     . ILE A 1 126 ? -27.70875 26.73771 10.80887  1.000 13.31556 ?  131 ILE A C     1 
ATOM   938  O  O     . ILE A 1 126 ? -27.39037 26.87620 9.62238   1.000 14.84776 ?  131 ILE A O     1 
ATOM   939  C  CB    . ILE A 1 126 ? -28.19972 24.27099 10.96339  1.000 12.65335 ?  131 ILE A CB    1 
ATOM   940  C  CG1   . ILE A 1 126 ? -29.24847 23.20876 11.31570  1.000 14.17920 ?  131 ILE A CG1   1 
ATOM   941  C  CG2   . ILE A 1 126 ? -26.93635 24.03504 11.77020  1.000 14.47272 ?  131 ILE A CG2   1 
ATOM   942  C  CD1   . ILE A 1 126 ? -29.94250 22.60084 10.11419  1.000 14.33566 ?  131 ILE A CD1   1 
ATOM   943  N  N     . LYS A 1 127 ? -27.19921 27.48064 11.78604  1.000 12.02682 ?  132 LYS A N     1 
ATOM   944  C  CA    . LYS A 1 127 ? -26.15136 28.44851 11.50160  1.000 12.66596 ?  132 LYS A CA    1 
ATOM   945  C  C     . LYS A 1 127 ? -24.83029 27.72653 11.27105  1.000 12.11721 ?  132 LYS A C     1 
ATOM   946  O  O     . LYS A 1 127 ? -24.59134 26.64364 11.80958  1.000 12.64972 ?  132 LYS A O     1 
ATOM   947  C  CB    . LYS A 1 127 ? -26.01500 29.43888 12.65898  1.000 14.44558 ?  132 LYS A CB    1 
ATOM   948  C  CG    . LYS A 1 127 ? -27.18941 30.40269 12.76840  1.000 20.13190 ?  132 LYS A CG    1 
ATOM   949  C  CD    . LYS A 1 127 ? -26.98990 31.44112 13.86079  1.000 26.51501 ?  132 LYS A CD    1 
ATOM   950  C  CE    . LYS A 1 127 ? -27.35225 30.89192 15.22731  1.000 30.97786 ?  132 LYS A CE    1 
ATOM   951  N  NZ    . LYS A 1 127 ? -27.38398 31.96818 16.25759  1.000 33.82354 ?  132 LYS A NZ    1 
ATOM   952  N  N     . ASN A 1 128 ? -23.97334 28.32931 10.43999  1.000 12.53087 ?  133 ASN A N     1 
ATOM   953  C  CA    . ASN A 1 128 ? -22.67985 27.71809 10.14589  1.000 13.60891 ?  133 ASN A CA    1 
ATOM   954  C  C     . ASN A 1 128 ? -21.92042 27.39719 11.42352  1.000 13.85734 ?  133 ASN A C     1 
ATOM   955  O  O     . ASN A 1 128 ? -21.31561 26.32603 11.54633  1.000 14.75917 ?  133 ASN A O     1 
ATOM   956  C  CB    . ASN A 1 128 ? -21.84336 28.64136 9.25745   1.000 17.23746 ?  133 ASN A CB    1 
ATOM   957  C  CG    . ASN A 1 128 ? -22.23194 28.55813 7.79414   1.000 23.99445 ?  133 ASN A CG    1 
ATOM   958  O  OD1   . ASN A 1 128 ? -23.36543 28.21578 7.45664   1.000 27.36801 ?  133 ASN A OD1   1 
ATOM   959  N  ND2   . ASN A 1 128 ? -21.28600 28.87141 6.91414   1.000 27.36593 ?  133 ASN A ND2   1 
ATOM   960  N  N     . GLU A 1 129 ? -21.95184 28.31431 12.39215  1.000 13.00318 ?  134 GLU A N     1 
ATOM   961  C  CA    . GLU A 1 129 ? -21.22351 28.10528 13.63848  1.000 14.37923 ?  134 GLU A CA    1 
ATOM   962  C  C     . GLU A 1 129 ? -21.79951 26.95195 14.45343  1.000 12.64181 ?  134 GLU A C     1 
ATOM   963  O  O     . GLU A 1 129 ? -21.05770 26.28311 15.18131  1.000 13.75352 ?  134 GLU A O     1 
ATOM   964  C  CB    . GLU A 1 129 ? -21.19711 29.39501 14.45990  1.000 18.51658 ?  134 GLU A CB    1 
ATOM   965  C  CG    . GLU A 1 129 ? -22.54404 30.09828 14.58240  1.000 24.91964 ?  134 GLU A CG    1 
ATOM   966  C  CD    . GLU A 1 129 ? -22.74722 31.19171 13.53927  1.000 28.48432 ?  134 GLU A CD    1 
ATOM   967  O  OE1   . GLU A 1 129 ? -22.42159 30.96910 12.35347  1.000 26.23383 ?  134 GLU A OE1   1 
ATOM   968  O  OE2   . GLU A 1 129 ? -23.23214 32.28233 13.91043  1.000 33.06717 ?  134 GLU A OE2   1 
ATOM   969  N  N     . GLU A 1 130 ? -23.10709 26.70089 14.34935  1.000 11.68032 ?  135 GLU A N     1 
ATOM   970  C  CA    . GLU A 1 130 ? -23.70014 25.57763 15.06969  1.000 9.46303  ?  135 GLU A CA    1 
ATOM   971  C  C     . GLU A 1 130 ? -23.25979 24.25010 14.46658  1.000 9.42461  ?  135 GLU A C     1 
ATOM   972  O  O     . GLU A 1 130 ? -22.90029 23.31460 15.19287  1.000 9.77775  ?  135 GLU A O     1 
ATOM   973  C  CB    . GLU A 1 130 ? -25.22563 25.68746 15.05753  1.000 10.00004 ?  135 GLU A CB    1 
ATOM   974  C  CG    . GLU A 1 130 ? -25.77149 26.87270 15.82377  1.000 12.07993 ?  135 GLU A CG    1 
ATOM   975  C  CD    . GLU A 1 130 ? -27.27941 26.98332 15.70980  1.000 15.46416 ?  135 GLU A CD    1 
ATOM   976  O  OE1   . GLU A 1 130 ? -27.79734 26.94833 14.57625  1.000 15.43805 ?  135 GLU A OE1   1 
ATOM   977  O  OE2   . GLU A 1 130 ? -27.95131 27.10020 16.75315  1.000 20.88448 ?  135 GLU A OE2   1 
ATOM   978  N  N     . ALA A 1 131 ? -23.29108 24.14684 13.13435  1.000 9.48279  ?  136 ALA A N     1 
ATOM   979  C  CA    . ALA A 1 131 ? -22.84181 22.92241 12.48214  1.000 9.63722  ?  136 ALA A CA    1 
ATOM   980  C  C     . ALA A 1 131 ? -21.37743 22.64437 12.78992  1.000 9.59078  ?  136 ALA A C     1 
ATOM   981  O  O     . ALA A 1 131 ? -21.00112 21.50478 13.08615  1.000 10.32292 ?  136 ALA A O     1 
ATOM   982  C  CB    . ALA A 1 131 ? -23.06656 23.01857 10.97361  1.000 11.46504 ?  136 ALA A CB    1 
ATOM   983  N  N     . GLU A 1 132 ? -20.53610 23.67794 12.74193  1.000 10.59489 ?  137 GLU A N     1 
ATOM   984  C  CA    . GLU A 1 132 ? -19.12348 23.48178 13.04188  1.000 11.78766 ?  137 GLU A CA    1 
ATOM   985  C  C     . GLU A 1 132 ? -18.89834 23.14333 14.51086  1.000 11.82798 ?  137 GLU A C     1 
ATOM   986  O  O     . GLU A 1 132 ? -17.99898 22.35748 14.83232  1.000 12.51827 ?  137 GLU A O     1 
ATOM   987  C  CB    . GLU A 1 132 ? -18.32099 24.70281 12.59097  1.000 15.61212 ?  137 GLU A CB    1 
ATOM   988  C  CG    . GLU A 1 132 ? -18.32951 24.85622 11.07219  1.000 18.12526 ?  137 GLU A CG    1 
ATOM   989  C  CD    . GLU A 1 132 ? -17.78924 26.18454 10.59030  1.000 22.98422 ?  137 GLU A CD    1 
ATOM   990  O  OE1   . GLU A 1 132 ? -17.01803 26.82481 11.33258  1.000 25.90204 ?  137 GLU A OE1   1 
ATOM   991  O  OE2   . GLU A 1 132 ? -18.14373 26.58882 9.46148   1.000 22.26582 ?  137 GLU A OE2   1 
ATOM   992  N  N     . ALA A 1 133 ? -19.71082 23.70314 15.40974  1.000 10.64912 ?  138 ALA A N     1 
ATOM   993  C  CA    . ALA A 1 133 ? -19.60567 23.34271 16.81978  1.000 10.85494 ?  138 ALA A CA    1 
ATOM   994  C  C     . ALA A 1 133 ? -19.96266 21.87772 17.04098  1.000 10.84135 ?  138 ALA A C     1 
ATOM   995  O  O     . ALA A 1 133 ? -19.32901 21.19183 17.85154  1.000 11.05030 ?  138 ALA A O     1 
ATOM   996  C  CB    . ALA A 1 133 ? -20.49735 24.25064 17.66574  1.000 12.06163 ?  138 ALA A CB    1 
ATOM   997  N  N     . LEU A 1 134 ? -20.97231 21.37730 16.32538  1.000 9.11031  ?  139 LEU A N     1 
ATOM   998  C  CA    . LEU A 1 134 ? -21.31989 19.96646 16.44814  1.000 8.78763  ?  139 LEU A CA    1 
ATOM   999  C  C     . LEU A 1 134 ? -20.19803 19.07644 15.93208  1.000 10.06784 ?  139 LEU A C     1 
ATOM   1000 O  O     . LEU A 1 134 ? -19.84215 18.08425 16.57709  1.000 10.24937 ?  139 LEU A O     1 
ATOM   1001 C  CB    . LEU A 1 134 ? -22.61895 19.66960 15.70120  1.000 9.01075  ?  139 LEU A CB    1 
ATOM   1002 C  CG    . LEU A 1 134 ? -23.08510 18.21443 15.80567  1.000 9.95702  ?  139 LEU A CG    1 
ATOM   1003 C  CD1   . LEU A 1 134 ? -23.41865 17.85985 17.25100  1.000 12.31949 ?  139 LEU A CD1   1 
ATOM   1004 C  CD2   . LEU A 1 134 ? -24.26905 17.95641 14.89038  1.000 11.36689 ?  139 LEU A CD2   1 
ATOM   1005 N  N     . ALA A 1 135 ? -19.63117 19.41852 14.77280  1.000 9.39885  ?  140 ALA A N     1 
ATOM   1006 C  CA    . ALA A 1 135 ? -18.50130 18.66222 14.24041  1.000 11.07990 ?  140 ALA A CA    1 
ATOM   1007 C  C     . ALA A 1 135 ? -17.36332 18.58819 15.25254  1.000 10.82383 ?  140 ALA A C     1 
ATOM   1008 O  O     . ALA A 1 135 ? -16.79126 17.51757 15.48521  1.000 12.35679 ?  140 ALA A O     1 
ATOM   1009 C  CB    . ALA A 1 135 ? -18.02594 19.29132 12.93135  1.000 13.19282 ?  140 ALA A CB    1 
ATOM   1010 N  N     . LYS A 1 136 ? -17.03713 19.71641 15.88482  1.000 10.18925 ?  141 LYS A N     1 
ATOM   1011 C  CA    . LYS A 1 136 ? -15.96338 19.72084 16.87261  1.000 11.49693 ?  141 LYS A CA    1 
ATOM   1012 C  C     . LYS A 1 136 ? -16.31148 18.85025 18.07291  1.000 10.71286 ?  141 LYS A C     1 
ATOM   1013 O  O     . LYS A 1 136 ? -15.47260 18.07951 18.55508  1.000 12.12603 ?  141 LYS A O     1 
ATOM   1014 C  CB    . LYS A 1 136 ? -15.66973 21.15120 17.32148  1.000 14.14834 ?  141 LYS A CB    1 
ATOM   1015 C  CG    . LYS A 1 136 ? -14.58068 21.24569 18.37566  1.000 18.20871 ?  141 LYS A CG    1 
ATOM   1016 C  CD    . LYS A 1 136 ? -14.36825 22.67380 18.84090  1.000 24.23515 ?  141 LYS A CD    1 
ATOM   1017 C  CE    . LYS A 1 136 ? -13.29299 22.74315 19.91444  1.000 27.95909 ?  141 LYS A CE    1 
ATOM   1018 N  NZ    . LYS A 1 136 ? -13.63215 21.90664 21.10213  1.000 29.95905 ?  141 LYS A NZ    1 
ATOM   1019 N  N     . ARG A 1 137 ? -17.54449 18.96320 18.57263  1.000 10.59181 ?  142 ARG A N     1 
ATOM   1020 C  CA    . ARG A 1 137 ? -17.93398 18.22285 19.76906  1.000 10.14414 ?  142 ARG A CA    1 
ATOM   1021 C  C     . ARG A 1 137 ? -17.95263 16.71951 19.51635  1.000 11.09425 ?  142 ARG A C     1 
ATOM   1022 O  O     . ARG A 1 137 ? -17.62270 15.93008 20.40991  1.000 12.99476 ?  142 ARG A O     1 
ATOM   1023 C  CB    . ARG A 1 137 ? -19.29504 18.71386 20.25962  1.000 10.70950 ?  142 ARG A CB    1 
ATOM   1024 C  CG    . ARG A 1 137 ? -19.84936 17.96098 21.45663  1.000 10.60477 ?  142 ARG A CG    1 
ATOM   1025 C  CD    . ARG A 1 137 ? -18.91090 17.99833 22.66311  1.000 11.93264 ?  142 ARG A CD    1 
ATOM   1026 N  NE    . ARG A 1 137 ? -19.51195 17.30812 23.80166  1.000 12.18451 ?  142 ARG A NE    1 
ATOM   1027 C  CZ    . ARG A 1 137 ? -19.55094 15.98522 23.93233  1.000 11.53941 ?  142 ARG A CZ    1 
ATOM   1028 N  NH1   . ARG A 1 137 ? -19.01237 15.21036 23.00007  1.000 12.46969 ?  142 ARG A NH1   1 
ATOM   1029 N  NH2   . ARG A 1 137 ? -20.12902 15.43515 24.99308  1.000 12.72540 ?  142 ARG A NH2   1 
ATOM   1030 N  N     . LEU A 1 138 ? -18.33717 16.30418 18.31037  1.000 10.06804 ?  143 LEU A N     1 
ATOM   1031 C  CA    . LEU A 1 138 ? -18.31753 14.89361 17.94722  1.000 11.05561 ?  143 LEU A CA    1 
ATOM   1032 C  C     . LEU A 1 138 ? -16.95668 14.42943 17.45123  1.000 11.74144 ?  143 LEU A C     1 
ATOM   1033 O  O     . LEU A 1 138 ? -16.78045 13.22757 17.22341  1.000 12.06960 ?  143 LEU A O     1 
ATOM   1034 C  CB    . LEU A 1 138 ? -19.36597 14.61755 16.86810  1.000 11.38999 ?  143 LEU A CB    1 
ATOM   1035 C  CG    . LEU A 1 138 ? -20.81575 14.88631 17.26497  1.000 13.58991 ?  143 LEU A CG    1 
ATOM   1036 C  CD1   . LEU A 1 138 ? -21.73265 14.62724 16.08733  1.000 15.39560 ?  143 LEU A CD1   1 
ATOM   1037 C  CD2   . LEU A 1 138 ? -21.20581 14.02320 18.45017  1.000 15.56775 ?  143 LEU A CD2   1 
ATOM   1038 N  N     . LYS A 1 139 ? -16.00375 15.34802 17.27993  1.000 11.65580 ?  144 LYS A N     1 
ATOM   1039 C  CA    . LYS A 1 139 ? -14.68044 15.03622 16.73651  1.000 12.95621 ?  144 LYS A CA    1 
ATOM   1040 C  C     . LYS A 1 139 ? -14.78012 14.35375 15.37192  1.000 11.04432 ?  144 LYS A C     1 
ATOM   1041 O  O     . LYS A 1 139 ? -14.22198 13.27796 15.14424  1.000 13.77260 ?  144 LYS A O     1 
ATOM   1042 C  CB    . LYS A 1 139 ? -13.83544 14.22581 17.72327  1.000 15.23612 ?  144 LYS A CB    1 
ATOM   1043 C  CG    . LYS A 1 139 ? -13.60894 14.93426 19.04989  1.000 17.84377 ?  144 LYS A CG    1 
ATOM   1044 C  CD    . LYS A 1 139 ? -12.82597 14.06936 20.02692  1.000 23.19685 ?  144 LYS A CD    1 
ATOM   1045 C  CE    . LYS A 1 139 ? -12.57956 14.80888 21.33197  1.000 28.76055 ?  144 LYS A CE    1 
ATOM   1046 N  NZ    . LYS A 1 139 ? -11.82803 13.97920 22.31516  1.000 31.98588 ?  144 LYS A NZ    1 
ATOM   1047 N  N     . LEU A 1 140 ? -15.50272 14.99568 14.45503  1.000 10.45257 ?  145 LEU A N     1 
ATOM   1048 C  CA    . LEU A 1 140 ? -15.74903 14.44584 13.12966  1.000 11.27537 ?  145 LEU A CA    1 
ATOM   1049 C  C     . LEU A 1 140 ? -15.40708 15.46792 12.05870  1.000 10.66811 ?  145 LEU A C     1 
ATOM   1050 O  O     . LEU A 1 140 ? -15.68678 16.66004 12.21215  1.000 12.53620 ?  145 LEU A O     1 
ATOM   1051 C  CB    . LEU A 1 140 ? -17.21922 14.05833 12.95219  1.000 11.41473 ?  145 LEU A CB    1 
ATOM   1052 C  CG    . LEU A 1 140 ? -17.75421 12.90252 13.79198  1.000 12.81063 ?  145 LEU A CG    1 
ATOM   1053 C  CD1   . LEU A 1 140 ? -19.24267 12.72187 13.54095  1.000 13.76639 ?  145 LEU A CD1   1 
ATOM   1054 C  CD2   . LEU A 1 140 ? -16.99869 11.62449 13.47348  1.000 15.07375 ?  145 LEU A CD2   1 
ATOM   1055 N  N     . ARG A 1 141 ? -14.81158 14.98515 10.97087  1.000 10.51852 ?  146 ARG A N     1 
ATOM   1056 C  CA    . ARG A 1 141 ? -14.69987 15.77830 9.75554   1.000 10.64002 ?  146 ARG A CA    1 
ATOM   1057 C  C     . ARG A 1 141 ? -16.09748 16.13032 9.26032   1.000 9.84398  ?  146 ARG A C     1 
ATOM   1058 O  O     . ARG A 1 141 ? -17.03116 15.32923 9.37074   1.000 9.09984  ?  146 ARG A O     1 
ATOM   1059 C  CB    . ARG A 1 141 ? -13.96527 14.96127 8.69058   1.000 13.85551 ?  146 ARG A CB    1 
ATOM   1060 C  CG    . ARG A 1 141 ? -13.81224 15.64198 7.33923   1.000 21.23127 ?  146 ARG A CG    1 
ATOM   1061 C  CD    . ARG A 1 141 ? -12.68251 16.65731 7.33503   1.000 27.77046 ?  146 ARG A CD    1 
ATOM   1062 N  NE    . ARG A 1 141 ? -11.36856 16.03272 7.46888   1.000 31.68557 ?  146 ARG A NE    1 
ATOM   1063 C  CZ    . ARG A 1 141 ? -10.60814 15.65249 6.44557   1.000 32.57992 ?  146 ARG A CZ    1 
ATOM   1064 N  NH1   . ARG A 1 141 ? -11.02818 15.82470 5.19918   1.000 32.78823 ?  146 ARG A NH1   1 
ATOM   1065 N  NH2   . ARG A 1 141 ? -9.42391  15.09781 6.66897   1.000 31.22472 ?  146 ARG A NH2   1 
ATOM   1066 N  N     . PHE A 1 142 ? -16.23949 17.33278 8.70482   1.000 9.47064  ?  147 PHE A N     1 
ATOM   1067 C  CA    . PHE A 1 142 ? -17.54160 17.88546 8.35619   1.000 8.92928  ?  147 PHE A CA    1 
ATOM   1068 C  C     . PHE A 1 142 ? -17.51957 18.38949 6.92091   1.000 8.02167  ?  147 PHE A C     1 
ATOM   1069 O  O     . PHE A 1 142 ? -16.61387 19.13793 6.53714   1.000 11.06844 ?  147 PHE A O     1 
ATOM   1070 C  CB    . PHE A 1 142 ? -17.88870 19.02693 9.32068   1.000 10.19649 ?  147 PHE A CB    1 
ATOM   1071 C  CG    . PHE A 1 142 ? -19.14397 19.77108 8.97084   1.000 9.08806  ?  147 PHE A CG    1 
ATOM   1072 C  CD1   . PHE A 1 142 ? -20.33838 19.09826 8.77154   1.000 9.42440  ?  147 PHE A CD1   1 
ATOM   1073 C  CD2   . PHE A 1 142 ? -19.13727 21.15395 8.87508   1.000 10.26859 ?  147 PHE A CD2   1 
ATOM   1074 C  CE1   . PHE A 1 142 ? -21.49511 19.79152 8.45969   1.000 9.75193  ?  147 PHE A CE1   1 
ATOM   1075 C  CE2   . PHE A 1 142 ? -20.29075 21.84661 8.56457   1.000 10.99701 ?  147 PHE A CE2   1 
ATOM   1076 C  CZ    . PHE A 1 142 ? -21.47111 21.16658 8.35743   1.000 9.57066  ?  147 PHE A CZ    1 
ATOM   1077 N  N     . TYR A 1 143 ? -18.51693 17.98123 6.13231   1.000 8.22002  ?  148 TYR A N     1 
ATOM   1078 C  CA    . TYR A 1 143 ? -18.69956 18.47388 4.77151   1.000 7.69364  ?  148 TYR A CA    1 
ATOM   1079 C  C     . TYR A 1 143 ? -20.10134 19.03605 4.60113   1.000 7.39132  ?  148 TYR A C     1 
ATOM   1080 O  O     . TYR A 1 143 ? -21.07245 18.47158 5.10826   1.000 8.64210  ?  148 TYR A O     1 
ATOM   1081 C  CB    . TYR A 1 143 ? -18.53910 17.36543 3.72416   1.000 9.20129  ?  148 TYR A CB    1 
ATOM   1082 C  CG    . TYR A 1 143 ? -17.12880 16.86971 3.54690   1.000 11.54871 ?  148 TYR A CG    1 
ATOM   1083 C  CD1   . TYR A 1 143 ? -16.64029 15.83017 4.32202   1.000 14.79540 ?  148 TYR A CD1   1 
ATOM   1084 C  CD2   . TYR A 1 143 ? -16.28879 17.43085 2.59633   1.000 14.20474 ?  148 TYR A CD2   1 
ATOM   1085 C  CE1   . TYR A 1 143 ? -15.35382 15.36735 4.16550   1.000 15.07960 ?  148 TYR A CE1   1 
ATOM   1086 C  CE2   . TYR A 1 143 ? -14.99424 16.97162 2.42982   1.000 16.41551 ?  148 TYR A CE2   1 
ATOM   1087 C  CZ    . TYR A 1 143 ? -14.53539 15.93930 3.21926   1.000 16.06929 ?  148 TYR A CZ    1 
ATOM   1088 O  OH    . TYR A 1 143 ? -13.25030 15.47275 3.07094   1.000 18.47057 ?  148 TYR A OH    1 
ATOM   1089 N  N     . ARG A 1 144 ? -20.20192 20.13967 3.87026   1.000 8.08129  ?  149 ARG A N     1 
ATOM   1090 C  CA    . ARG A 1 144 ? -21.47664 20.66281 3.40273   1.000 7.66937  ?  149 ARG A CA    1 
ATOM   1091 C  C     . ARG A 1 144 ? -21.65970 20.18201 1.97076   1.000 7.21179  ?  149 ARG A C     1 
ATOM   1092 O  O     . ARG A 1 144 ? -20.78841 20.40707 1.12483   1.000 11.33831 ?  149 ARG A O     1 
ATOM   1093 C  CB    . ARG A 1 144 ? -21.46799 22.19034 3.45590   1.000 9.39364  ?  149 ARG A CB    1 
ATOM   1094 C  CG    . ARG A 1 144 ? -21.30480 22.74111 4.86325   1.000 10.80282 ?  149 ARG A CG    1 
ATOM   1095 C  CD    . ARG A 1 144 ? -21.14900 24.25451 4.87186   1.000 12.53075 ?  149 ARG A CD    1 
ATOM   1096 N  NE    . ARG A 1 144 ? -21.23315 24.77461 6.23282   1.000 11.59895 ?  149 ARG A NE    1 
ATOM   1097 C  CZ    . ARG A 1 144 ? -20.18685 25.11404 6.98034   1.000 12.81948 ?  149 ARG A CZ    1 
ATOM   1098 N  NH1   . ARG A 1 144 ? -18.95636 25.01027 6.49715   1.000 14.02300 ?  149 ARG A NH1   1 
ATOM   1099 N  NH2   . ARG A 1 144 ? -20.37459 25.56283 8.21551   1.000 13.38220 ?  149 ARG A NH2   1 
ATOM   1100 N  N     . THR A 1 145 ? -22.77427 19.50774 1.69918   1.000 7.04995  ?  150 THR A N     1 
ATOM   1101 C  CA    . THR A 1 145 ? -23.01575 18.95733 0.37451   1.000 6.52122  ?  150 THR A CA    1 
ATOM   1102 C  C     . THR A 1 145 ? -24.29254 19.52104 -0.22989  1.000 6.79244  ?  150 THR A C     1 
ATOM   1103 O  O     . THR A 1 145 ? -25.21871 19.92806 0.48149   1.000 7.35103  ?  150 THR A O     1 
ATOM   1104 C  CB    . THR A 1 145 ? -23.13499 17.42266 0.39438   1.000 8.31143  ?  150 THR A CB    1 
ATOM   1105 O  OG1   . THR A 1 145 ? -24.22697 17.03187 1.23470   1.000 8.63388  ?  150 THR A OG1   1 
ATOM   1106 C  CG2   . THR A 1 145 ? -21.86215 16.78750 0.90093   1.000 9.43612  ?  150 THR A CG2   1 
ATOM   1107 N  N     . SER A 1 146 ? -24.33352 19.52216 -1.56057  1.000 7.40130  ?  151 SER A N     1 
ATOM   1108 C  CA    . SER A 1 146 ? -25.57844 19.64174 -2.31131  1.000 6.94203  ?  151 SER A CA    1 
ATOM   1109 C  C     . SER A 1 146 ? -25.60297 18.50404 -3.31762  1.000 7.04819  ?  151 SER A C     1 
ATOM   1110 O  O     . SER A 1 146 ? -24.79697 18.48192 -4.25177  1.000 8.45250  ?  151 SER A O     1 
ATOM   1111 C  CB    . SER A 1 146 ? -25.68833 20.98002 -3.03537  1.000 8.29773  ?  151 SER A CB    1 
ATOM   1112 O  OG    . SER A 1 146 ? -26.82958 20.96872 -3.88470  1.000 9.51107  ?  151 SER A OG    1 
ATOM   1113 N  N     . VAL A 1 147 ? -26.51317 17.55044 -3.12495  1.000 7.50436  ?  152 VAL A N     1 
ATOM   1114 C  CA    . VAL A 1 147 ? -26.68447 16.51369 -4.13495  1.000 6.75920  ?  152 VAL A CA    1 
ATOM   1115 C  C     . VAL A 1 147 ? -27.21359 17.11954 -5.42530  1.000 8.33207  ?  152 VAL A C     1 
ATOM   1116 O  O     . VAL A 1 147 ? -26.82364 16.71295 -6.52687  1.000 9.19241  ?  152 VAL A O     1 
ATOM   1117 C  CB    . VAL A 1 147 ? -27.60226 15.40157 -3.60890  1.000 8.71713  ?  152 VAL A CB    1 
ATOM   1118 C  CG1   . VAL A 1 147 ? -27.70559 14.29534 -4.63721  1.000 10.36177 ?  152 VAL A CG1   1 
ATOM   1119 C  CG2   . VAL A 1 147 ? -27.06908 14.87929 -2.30548  1.000 9.56264  ?  152 VAL A CG2   1 
ATOM   1120 N  N     . LYS A 1 148 ? -28.10769 18.10342 -5.30471  1.000 8.50032  ?  153 LYS A N     1 
ATOM   1121 C  CA    . LYS A 1 148 ? -28.67998 18.75420 -6.47768  1.000 9.13238  ?  153 LYS A CA    1 
ATOM   1122 C  C     . LYS A 1 148 ? -27.59074 19.35494 -7.35856  1.000 9.92963  ?  153 LYS A C     1 
ATOM   1123 O  O     . LYS A 1 148 ? -27.61267 19.19378 -8.58416  1.000 11.99987 ?  153 LYS A O     1 
ATOM   1124 C  CB    . LYS A 1 148 ? -29.66642 19.83331 -6.02808  1.000 11.04532 ?  153 LYS A CB    1 
ATOM   1125 C  CG    . LYS A 1 148 ? -30.26593 20.63930 -7.16640  1.000 13.63497 ?  153 LYS A CG    1 
ATOM   1126 C  CD    . LYS A 1 148 ? -31.24011 21.67440 -6.63985  1.000 17.68782 ?  153 LYS A CD    1 
ATOM   1127 C  CE    . LYS A 1 148 ? -31.87043 22.45881 -7.78062  1.000 21.70911 ?  153 LYS A CE    1 
ATOM   1128 N  NZ    . LYS A 1 148 ? -32.86269 23.44890 -7.28346  1.000 27.55750 ?  153 LYS A NZ    1 
ATOM   1129 N  N     . GLU A 1 149 ? -26.62305 20.03975 -6.75247  1.000 9.72424  ?  154 GLU A N     1 
ATOM   1130 C  CA    . GLU A 1 149 ? -25.55127 20.69401 -7.49057  1.000 11.47267 ?  154 GLU A CA    1 
ATOM   1131 C  C     . GLU A 1 149 ? -24.32008 19.81665 -7.65501  1.000 10.98323 ?  154 GLU A C     1 
ATOM   1132 O  O     . GLU A 1 149 ? -23.34521 20.25879 -8.27374  1.000 12.13768 ?  154 GLU A O     1 
ATOM   1133 C  CB    . GLU A 1 149 ? -25.15049 21.99439 -6.78921  1.000 12.89284 ?  154 GLU A CB    1 
ATOM   1134 C  CG    . GLU A 1 149 ? -26.26827 23.00964 -6.70501  1.000 15.86215 ?  154 GLU A CG    1 
ATOM   1135 C  CD    . GLU A 1 149 ? -26.57335 23.63344 -8.04676  1.000 23.36230 ?  154 GLU A CD    1 
ATOM   1136 O  OE1   . GLU A 1 149 ? -25.66491 24.27064 -8.62232  1.000 25.35389 ?  154 GLU A OE1   1 
ATOM   1137 O  OE2   . GLU A 1 149 ? -27.71307 23.47510 -8.53106  1.000 27.19860 ?  154 GLU A OE2   1 
ATOM   1138 N  N     . ASP A 1 150 ? -24.34341 18.59604 -7.11442  1.000 10.87599 ?  155 ASP A N     1 
ATOM   1139 C  CA    . ASP A 1 150 ? -23.19003 17.69225 -7.12490  1.000 10.50960 ?  155 ASP A CA    1 
ATOM   1140 C  C     . ASP A 1 150 ? -21.95729 18.35163 -6.50296  1.000 10.54356 ?  155 ASP A C     1 
ATOM   1141 O  O     . ASP A 1 150 ? -20.86668 18.36124 -7.08039  1.000 12.87482 ?  155 ASP A O     1 
ATOM   1142 C  CB    . ASP A 1 150 ? -22.89872 17.14308 -8.52679  1.000 13.43460 ?  155 ASP A CB    1 
ATOM   1143 C  CG    . ASP A 1 150 ? -22.05583 15.87532 -8.50049  1.000 15.73684 ?  155 ASP A CG    1 
ATOM   1144 O  OD1   . ASP A 1 150 ? -21.86413 15.29414 -7.41061  1.000 14.91574 ?  155 ASP A OD1   1 
ATOM   1145 O  OD2   . ASP A 1 150 ? -21.58390 15.45925 -9.57864  1.000 20.35849 ?  155 ASP A OD2   1 
ATOM   1146 N  N     . LEU A 1 151 ? -22.14254 18.91493 -5.31079  1.000 9.23259  ?  156 LEU A N     1 
ATOM   1147 C  CA    . LEU A 1 151 ? -21.07617 19.57722 -4.57008  1.000 10.01330 ?  156 LEU A CA    1 
ATOM   1148 C  C     . LEU A 1 151 ? -20.71431 18.73715 -3.35523  1.000 8.28535  ?  156 LEU A C     1 
ATOM   1149 O  O     . LEU A 1 151 ? -21.55721 18.51394 -2.47744  1.000 8.69208  ?  156 LEU A O     1 
ATOM   1150 C  CB    . LEU A 1 151 ? -21.50487 20.97453 -4.12400  1.000 13.44122 ?  156 LEU A CB    1 
ATOM   1151 C  CG    . LEU A 1 151 ? -21.59670 22.03819 -5.21405  1.000 15.12417 ?  156 LEU A CG    1 
ATOM   1152 C  CD1   . LEU A 1 151 ? -22.24389 23.29276 -4.66023  1.000 15.21644 ?  156 LEU A CD1   1 
ATOM   1153 C  CD2   . LEU A 1 151 ? -20.21596 22.34129 -5.77365  1.000 18.22052 ?  156 LEU A CD2   1 
ATOM   1154 N  N     . ASN A 1 152 ? -19.46934 18.26635 -3.31778  1.000 8.27107  ?  157 ASN A N     1 
ATOM   1155 C  CA    . ASN A 1 152 ? -18.81191 17.60659 -2.19101  1.000 8.08437  ?  157 ASN A CA    1 
ATOM   1156 C  C     . ASN A 1 152 ? -19.27168 16.17774 -1.94167  1.000 8.58200  ?  157 ASN A C     1 
ATOM   1157 O  O     . ASN A 1 152 ? -18.80590 15.55981 -0.97873  1.000 10.51008 ?  157 ASN A O     1 
ATOM   1158 C  CB    . ASN A 1 152 ? -18.83193 18.42398 -0.89097  1.000 8.95167  ?  157 ASN A CB    1 
ATOM   1159 C  CG    . ASN A 1 152 ? -18.00641 19.68328 -1.00313  1.000 9.30370  ?  157 ASN A CG    1 
ATOM   1160 O  OD1   . ASN A 1 152 ? -16.98039 19.69865 -1.68552  1.000 10.36289 ?  157 ASN A OD1   1 
ATOM   1161 N  ND2   . ASN A 1 152 ? -18.45301 20.75098 -0.35522  1.000 10.76523 ?  157 ASN A ND2   1 
ATOM   1162 N  N     . VAL A 1 153 ? -20.14883 15.62384 -2.77534  1.000 8.30994  ?  158 VAL A N     1 
ATOM   1163 C  CA    . VAL A 1 153 ? -20.58414 14.24633 -2.57307  1.000 7.82826  ?  158 VAL A CA    1 
ATOM   1164 C  C     . VAL A 1 153 ? -19.41867 13.28331 -2.77789  1.000 8.61439  ?  158 VAL A C     1 
ATOM   1165 O  O     . VAL A 1 153 ? -19.17670 12.39221 -1.95560  1.000 8.57611  ?  158 VAL A O     1 
ATOM   1166 C  CB    . VAL A 1 153 ? -21.78154 13.92391 -3.48373  1.000 9.39546  ?  158 VAL A CB    1 
ATOM   1167 C  CG1   . VAL A 1 153 ? -22.19302 12.47121 -3.32183  1.000 10.89605 ?  158 VAL A CG1   1 
ATOM   1168 C  CG2   . VAL A 1 153 ? -22.94826 14.86096 -3.16914  1.000 11.40442 ?  158 VAL A CG2   1 
ATOM   1169 N  N     . ASN A 1 154 ? -18.66162 13.46448 -3.86377  1.000 9.19852  ?  159 ASN A N     1 
ATOM   1170 C  CA    . ASN A 1 154 ? -17.52287 12.58655 -4.11885  1.000 9.56007  ?  159 ASN A CA    1 
ATOM   1171 C  C     . ASN A 1 154 ? -16.52368 12.64628 -2.97510  1.000 9.73335  ?  159 ASN A C     1 
ATOM   1172 O  O     . ASN A 1 154 ? -15.97088 11.61799 -2.56563  1.000 9.76113  ?  159 ASN A O     1 
ATOM   1173 C  CB    . ASN A 1 154 ? -16.83592 12.98240 -5.42431  1.000 11.70892 ?  159 ASN A CB    1 
ATOM   1174 C  CG    . ASN A 1 154 ? -17.73221 12.81777 -6.62581  1.000 12.92185 ?  159 ASN A CG    1 
ATOM   1175 O  OD1   . ASN A 1 154 ? -18.54707 11.89847 -6.68710  1.000 13.45365 ?  159 ASN A OD1   1 
ATOM   1176 N  ND2   . ASN A 1 154 ? -17.59285 13.71751 -7.59099  1.000 15.67270 ?  159 ASN A ND2   1 
ATOM   1177 N  N     . GLU A 1 155 ? -16.29998 13.84503 -2.43391  1.000 9.14133  ?  160 GLU A N     1 
ATOM   1178 C  CA    . GLU A 1 155 ? -15.29130 14.03200 -1.39907  1.000 9.21642  ?  160 GLU A CA    1 
ATOM   1179 C  C     . GLU A 1 155 ? -15.67821 13.33638 -0.10106  1.000 8.57329  ?  160 GLU A C     1 
ATOM   1180 O  O     . GLU A 1 155 ? -14.80218 12.83937 0.61641   1.000 9.98922  ?  160 GLU A O     1 
ATOM   1181 C  CB    . GLU A 1 155 ? -15.06189 15.52644 -1.17202  1.000 10.59634 ?  160 GLU A CB    1 
ATOM   1182 C  CG    . GLU A 1 155 ? -14.24837 16.20750 -2.27057  1.000 13.29817 ?  160 GLU A CG    1 
ATOM   1183 C  CD    . GLU A 1 155 ? -14.99857 16.40926 -3.58354  1.000 14.63025 ?  160 GLU A CD    1 
ATOM   1184 O  OE1   . GLU A 1 155 ? -16.23999 16.28300 -3.61722  1.000 13.76753 ?  160 GLU A OE1   1 
ATOM   1185 O  OE2   . GLU A 1 155 ? -14.33075 16.71272 -4.59558  1.000 19.98046 ?  160 GLU A OE2   1 
ATOM   1186 N  N     . VAL A 1 156 ? -16.97666 13.28569 0.21059   1.000 8.54314  ?  161 VAL A N     1 
ATOM   1187 C  CA    . VAL A 1 156 ? -17.43763 12.59816 1.41576   1.000 9.46042  ?  161 VAL A CA    1 
ATOM   1188 C  C     . VAL A 1 156 ? -17.02071 11.13443 1.38529   1.000 8.82451  ?  161 VAL A C     1 
ATOM   1189 O  O     . VAL A 1 156 ? -16.41876 10.61627 2.33401   1.000 9.12169  ?  161 VAL A O     1 
ATOM   1190 C  CB    . VAL A 1 156 ? -18.96261 12.74620 1.56491   1.000 9.67454  ?  161 VAL A CB    1 
ATOM   1191 C  CG1   . VAL A 1 156 ? -19.50286 11.72827 2.56615   1.000 10.69975 ?  161 VAL A CG1   1 
ATOM   1192 C  CG2   . VAL A 1 156 ? -19.31827 14.16337 1.98348   1.000 9.46095  ?  161 VAL A CG2   1 
ATOM   1193 N  N     . PHE A 1 157 ? -17.33524 10.44502 0.29049   1.000 8.58985  ?  162 PHE A N     1 
ATOM   1194 C  CA    . PHE A 1 157 ? -17.05033 9.01817  0.22120   1.000 9.13804  ?  162 PHE A CA    1 
ATOM   1195 C  C     . PHE A 1 157 ? -15.56494 8.74497  0.04290   1.000 10.15021 ?  162 PHE A C     1 
ATOM   1196 O  O     . PHE A 1 157 ? -15.05587 7.75078  0.57227   1.000 11.17185 ?  162 PHE A O     1 
ATOM   1197 C  CB    . PHE A 1 157 ? -17.90862 8.37135  -0.86084  1.000 10.09769 ?  162 PHE A CB    1 
ATOM   1198 C  CG    . PHE A 1 157 ? -19.36945 8.41170  -0.54138  1.000 9.03060  ?  162 PHE A CG    1 
ATOM   1199 C  CD1   . PHE A 1 157 ? -19.88619 7.60507  0.46046   1.000 11.32066 ?  162 PHE A CD1   1 
ATOM   1200 C  CD2   . PHE A 1 157 ? -20.22267 9.27864  -1.20519  1.000 9.67745  ?  162 PHE A CD2   1 
ATOM   1201 C  CE1   . PHE A 1 157 ? -21.22556 7.64275  0.77726   1.000 11.15072 ?  162 PHE A CE1   1 
ATOM   1202 C  CE2   . PHE A 1 157 ? -21.56864 9.32094  -0.89095  1.000 10.47788 ?  162 PHE A CE2   1 
ATOM   1203 C  CZ    . PHE A 1 157 ? -22.06877 8.50302  0.10497   1.000 10.35719 ?  162 PHE A CZ    1 
ATOM   1204 N  N     . LYS A 1 158 ? -14.85328 9.61586  -0.67812  1.000 10.65093 ?  163 LYS A N     1 
ATOM   1205 C  CA    A LYS A 1 158 ? -13.40575 9.47171  -0.79218  0.500 11.45457 ?  163 LYS A CA    1 
ATOM   1206 C  CA    B LYS A 1 158 ? -13.40808 9.45944  -0.78994  0.500 11.55682 ?  163 LYS A CA    1 
ATOM   1207 C  C     . LYS A 1 158 ? -12.73942 9.57944  0.57288   1.000 10.63462 ?  163 LYS A C     1 
ATOM   1208 O  O     . LYS A 1 158 ? -11.83219 8.80431  0.89400   1.000 11.50952 ?  163 LYS A O     1 
ATOM   1209 C  CB    A LYS A 1 158 ? -12.85186 10.53292 -1.74299  0.500 12.55469 ?  163 LYS A CB    1 
ATOM   1210 C  CB    B LYS A 1 158 ? -12.83313 10.47854 -1.77401  0.500 12.86151 ?  163 LYS A CB    1 
ATOM   1211 C  CG    A LYS A 1 158 ? -11.34888 10.45842 -1.96242  0.500 16.96576 ?  163 LYS A CG    1 
ATOM   1212 C  CG    B LYS A 1 158 ? -11.32904 10.35258 -1.97980  0.500 17.67004 ?  163 LYS A CG    1 
ATOM   1213 C  CD    A LYS A 1 158 ? -10.97032 9.20339  -2.72703  0.500 21.60258 ?  163 LYS A CD    1 
ATOM   1214 C  CD    B LYS A 1 158 ? -10.84169 11.25601 -3.10049  0.500 22.96839 ?  163 LYS A CD    1 
ATOM   1215 C  CE    A LYS A 1 158 ? -9.50203  9.21620  -3.11645  0.500 27.49137 ?  163 LYS A CE    1 
ATOM   1216 C  CE    B LYS A 1 158 ? -9.35426  11.06630 -3.35219  0.500 27.57381 ?  163 LYS A CE    1 
ATOM   1217 N  NZ    A LYS A 1 158 ? -9.14398  8.03452  -3.94407  0.500 30.55178 ?  163 LYS A NZ    1 
ATOM   1218 N  NZ    B LYS A 1 158 ? -8.86421  11.90541 -4.47991  0.500 30.33957 ?  163 LYS A NZ    1 
ATOM   1219 N  N     . TYR A 1 159 ? -13.18343 10.53583 1.39362   1.000 11.20174 ?  164 TYR A N     1 
ATOM   1220 C  CA    . TYR A 1 159 ? -12.62390 10.68328 2.73378   1.000 10.98705 ?  164 TYR A CA    1 
ATOM   1221 C  C     . TYR A 1 159 ? -12.78434 9.39892  3.53607   1.000 10.57003 ?  164 TYR A C     1 
ATOM   1222 O  O     . TYR A 1 159 ? -11.83340 8.92147  4.16320   1.000 11.19008 ?  164 TYR A O     1 
ATOM   1223 C  CB    . TYR A 1 159 ? -13.29597 11.84808 3.46255   1.000 10.28338 ?  164 TYR A CB    1 
ATOM   1224 C  CG    . TYR A 1 159 ? -12.98463 11.87791 4.94451   1.000 10.76448 ?  164 TYR A CG    1 
ATOM   1225 C  CD1   . TYR A 1 159 ? -11.75162 12.32227 5.40171   1.000 12.90761 ?  164 TYR A CD1   1 
ATOM   1226 C  CD2   . TYR A 1 159 ? -13.91677 11.44731 5.88430   1.000 12.36078 ?  164 TYR A CD2   1 
ATOM   1227 C  CE1   . TYR A 1 159 ? -11.45275 12.34612 6.75352   1.000 13.56528 ?  164 TYR A CE1   1 
ATOM   1228 C  CE2   . TYR A 1 159 ? -13.62921 11.46953 7.24090   1.000 11.24795 ?  164 TYR A CE2   1 
ATOM   1229 C  CZ    . TYR A 1 159 ? -12.39443 11.92154 7.66781   1.000 12.31747 ?  164 TYR A CZ    1 
ATOM   1230 O  OH    . TYR A 1 159 ? -12.09058 11.94564 9.01191   1.000 14.63352 ?  164 TYR A OH    1 
ATOM   1231 N  N     . LEU A 1 160 ? -13.98821 8.82356  3.52765   1.000 10.20141 ?  165 LEU A N     1 
ATOM   1232 C  CA    . LEU A 1 160 ? -14.22789 7.61360  4.30563   1.000 10.34350 ?  165 LEU A CA    1 
ATOM   1233 C  C     . LEU A 1 160 ? -13.39984 6.44766  3.78770   1.000 10.11095 ?  165 LEU A C     1 
ATOM   1234 O  O     . LEU A 1 160 ? -12.86598 5.66019  4.57622   1.000 12.17987 ?  165 LEU A O     1 
ATOM   1235 C  CB    . LEU A 1 160 ? -15.71123 7.26225  4.28988   1.000 11.45841 ?  165 LEU A CB    1 
ATOM   1236 C  CG    . LEU A 1 160 ? -16.61230 8.14198  5.15004   1.000 11.03826 ?  165 LEU A CG    1 
ATOM   1237 C  CD1   . LEU A 1 160 ? -18.03245 7.62295  5.07194   1.000 12.20570 ?  165 LEU A CD1   1 
ATOM   1238 C  CD2   . LEU A 1 160 ? -16.13363 8.19141  6.59496   1.000 12.59563 ?  165 LEU A CD2   1 
ATOM   1239 N  N     . ALA A 1 161 ? -13.28680 6.31468  2.46366   1.000 10.17656 ?  166 ALA A N     1 
ATOM   1240 C  CA    . ALA A 1 161 ? -12.48543 5.23202  1.90457   1.000 12.64600 ?  166 ALA A CA    1 
ATOM   1241 C  C     . ALA A 1 161 ? -11.02297 5.37315  2.30399   1.000 13.90126 ?  166 ALA A C     1 
ATOM   1242 O  O     . ALA A 1 161 ? -10.37831 4.39149  2.69444   1.000 15.13267 ?  166 ALA A O     1 
ATOM   1243 C  CB    . ALA A 1 161 ? -12.63132 5.20382  0.38364   1.000 13.25838 ?  166 ALA A CB    1 
ATOM   1244 N  N     . GLU A 1 162 ? -10.48693 6.59298  2.22322   1.000 13.67951 ?  167 GLU A N     1 
ATOM   1245 C  CA    . GLU A 1 162 ? -9.10179  6.82552  2.61667   1.000 15.61226 ?  167 GLU A CA    1 
ATOM   1246 C  C     . GLU A 1 162 ? -8.89617  6.55346  4.10032   1.000 15.13240 ?  167 GLU A C     1 
ATOM   1247 O  O     . GLU A 1 162 ? -7.88688  5.95776  4.49617   1.000 17.14571 ?  167 GLU A O     1 
ATOM   1248 C  CB    . GLU A 1 162 ? -8.70379  8.26107  2.28038   1.000 19.08267 ?  167 GLU A CB    1 
ATOM   1249 C  CG    . GLU A 1 162 ? -8.62303  8.55311  0.79334   1.000 21.92472 ?  167 GLU A CG    1 
ATOM   1250 C  CD    . GLU A 1 162 ? -8.36429  10.01832 0.50091   1.000 28.25910 ?  167 GLU A CD    1 
ATOM   1251 O  OE1   . GLU A 1 162 ? -8.69900  10.86813 1.35566   1.000 29.81052 ?  167 GLU A OE1   1 
ATOM   1252 O  OE2   . GLU A 1 162 ? -7.82393  10.32009 -0.58357  1.000 31.00580 ?  167 GLU A OE2   1 
ATOM   1253 N  N     . LYS A 1 163 ? -9.84372  6.98198  4.93734   1.000 15.20828 ?  168 LYS A N     1 
ATOM   1254 C  CA    A LYS A 1 163 ? -9.70598  6.77097  6.37372   0.500 16.45224 ?  168 LYS A CA    1 
ATOM   1255 C  CA    B LYS A 1 163 ? -9.71024  6.76905  6.37551   0.500 16.76408 ?  168 LYS A CA    1 
ATOM   1256 C  C     . LYS A 1 163 ? -9.72158  5.28628  6.71666   1.000 17.10952 ?  168 LYS A C     1 
ATOM   1257 O  O     . LYS A 1 163 ? -8.94510  4.82969  7.56576   1.000 18.84884 ?  168 LYS A O     1 
ATOM   1258 C  CB    A LYS A 1 163 ? -10.81131 7.51953  7.11739   0.500 17.97267 ?  168 LYS A CB    1 
ATOM   1259 C  CB    B LYS A 1 163 ? -10.82614 7.49720  7.12285   0.500 18.76388 ?  168 LYS A CB    1 
ATOM   1260 C  CG    A LYS A 1 163 ? -10.57930 7.65248  8.61047   0.500 18.23633 ?  168 LYS A CG    1 
ATOM   1261 C  CG    B LYS A 1 163 ? -10.67344 9.00420  7.14931   0.500 19.39150 ?  168 LYS A CG    1 
ATOM   1262 C  CD    A LYS A 1 163 ? -11.57877 8.61218  9.23379   0.500 20.66752 ?  168 LYS A CD    1 
ATOM   1263 C  CD    B LYS A 1 163 ? -9.49133  9.43000  8.00497   0.500 20.99990 ?  168 LYS A CD    1 
ATOM   1264 C  CE    A LYS A 1 163 ? -11.31218 8.79924  10.71652  0.500 22.91463 ?  168 LYS A CE    1 
ATOM   1265 C  CE    B LYS A 1 163 ? -9.68968  9.02482  9.45664   0.500 23.34662 ?  168 LYS A CE    1 
ATOM   1266 N  NZ    A LYS A 1 163 ? -9.94244  9.32510  10.96339  0.500 24.31258 ?  168 LYS A NZ    1 
ATOM   1267 N  NZ    B LYS A 1 163 ? -8.56400  9.47507  10.32195  0.500 25.44237 ?  168 LYS A NZ    1 
ATOM   1268 N  N     . TYR A 1 164 ? -10.59652 4.51570  6.06535   1.000 15.65709 ?  169 TYR A N     1 
ATOM   1269 C  CA    . TYR A 1 164 ? -10.63798 3.08103  6.32431   1.000 18.17288 ?  169 TYR A CA    1 
ATOM   1270 C  C     . TYR A 1 164 ? -9.33135  2.40905  5.92078   1.000 19.22016 ?  169 TYR A C     1 
ATOM   1271 O  O     . TYR A 1 164 ? -8.79881  1.57251  6.66010   1.000 20.27992 ?  169 TYR A O     1 
ATOM   1272 C  CB    . TYR A 1 164 ? -11.81528 2.43710  5.59144   1.000 18.26871 ?  169 TYR A CB    1 
ATOM   1273 C  CG    . TYR A 1 164 ? -11.77819 0.93044  5.67903   1.000 18.67414 ?  169 TYR A CG    1 
ATOM   1274 C  CD1   . TYR A 1 164 ? -12.24585 0.27222  6.80748   1.000 19.59671 ?  169 TYR A CD1   1 
ATOM   1275 C  CD2   . TYR A 1 164 ? -11.24756 0.16705  4.64713   1.000 22.34515 ?  169 TYR A CD2   1 
ATOM   1276 C  CE1   . TYR A 1 164 ? -12.19711 -1.10522 6.90205   1.000 21.15698 ?  169 TYR A CE1   1 
ATOM   1277 C  CE2   . TYR A 1 164 ? -11.19380 -1.20983 4.73253   1.000 23.00640 ?  169 TYR A CE2   1 
ATOM   1278 C  CZ    . TYR A 1 164 ? -11.67116 -1.84100 5.86100   1.000 23.68696 ?  169 TYR A CZ    1 
ATOM   1279 O  OH    . TYR A 1 164 ? -11.61904 -3.21347 5.94867   1.000 26.71958 ?  169 TYR A OH    1 
ATOM   1280 N  N     . LEU A 1 165 ? -8.80240  2.75757  4.74700   1.000 19.55808 ?  170 LEU A N     1 
ATOM   1281 C  CA    . LEU A 1 165 ? -7.58668  2.11980  4.25718   1.000 22.69893 ?  170 LEU A CA    1 
ATOM   1282 C  C     . LEU A 1 165 ? -6.35002  2.53144  5.04593   1.000 25.89071 ?  170 LEU A C     1 
ATOM   1283 O  O     . LEU A 1 165 ? -5.34237  1.81671  5.01012   1.000 28.92479 ?  170 LEU A O     1 
ATOM   1284 C  CB    . LEU A 1 165 ? -7.40611  2.41589  2.76792   1.000 23.06025 ?  170 LEU A CB    1 
ATOM   1285 C  CG    . LEU A 1 165 ? -8.49469  1.82228  1.87154   1.000 26.60279 ?  170 LEU A CG    1 
ATOM   1286 C  CD1   . LEU A 1 165 ? -8.30957  2.26976  0.43415   1.000 29.11627 ?  170 LEU A CD1   1 
ATOM   1287 C  CD2   . LEU A 1 165 ? -8.49853  0.30163  1.96576   1.000 27.02730 ?  170 LEU A CD2   1 
ATOM   1288 N  N     . GLN A 1 166 ? -6.40272  3.65430  5.75513   1.000 27.23067 ?  171 GLN A N     1 
ATOM   1289 C  CA    . GLN A 1 166 ? -5.27839  4.09805  6.57017   1.000 30.17244 ?  171 GLN A CA    1 
ATOM   1290 C  C     . GLN A 1 166 ? -5.32980  3.44849  7.94732   1.000 33.50006 ?  171 GLN A C     1 
ATOM   1291 O  O     . GLN A 1 166 ? -4.34321  3.45399  8.68199   1.000 37.22610 ?  171 GLN A O     1 
ATOM   1292 C  CB    . GLN A 1 166 ? -5.28209  5.62138  6.70897   1.000 30.15433 ?  171 GLN A CB    1 
HETATM 1293 P  PG    . GNP B 2 .   ? -35.79137 8.39951  3.52863   1.000 6.75869  ?  201 GNP A PG    1 
HETATM 1294 O  O1G   . GNP B 2 .   ? -35.45977 7.25461  2.66184   1.000 8.03475  ?  201 GNP A O1G   1 
HETATM 1295 O  O2G   . GNP B 2 .   ? -35.05860 8.33010  4.81912   1.000 8.34604  -1 201 GNP A O2G   1 
HETATM 1296 O  O3G   . GNP B 2 .   ? -37.26021 8.55313  3.71350   1.000 9.58782  -1 201 GNP A O3G   1 
HETATM 1297 N  N3B   . GNP B 2 .   ? -35.24823 9.81175  2.86203   1.000 7.86716  ?  201 GNP A N3B   1 
HETATM 1298 P  PB    . GNP B 2 .   ? -33.74851 10.18393 2.30137   1.000 6.07962  ?  201 GNP A PB    1 
HETATM 1299 O  O1B   . GNP B 2 .   ? -32.85968 10.60195 3.40668   1.000 6.07367  ?  201 GNP A O1B   1 
HETATM 1300 O  O2B   . GNP B 2 .   ? -33.21448 9.05854  1.47571   1.000 6.10938  -1 201 GNP A O2B   1 
HETATM 1301 O  O3A   . GNP B 2 .   ? -33.98648 11.43161 1.29572   1.000 7.24042  ?  201 GNP A O3A   1 
HETATM 1302 P  PA    . GNP B 2 .   ? -34.13543 11.47971 -0.29477  1.000 6.64709  ?  201 GNP A PA    1 
HETATM 1303 O  O1A   . GNP B 2 .   ? -32.81811 11.23337 -0.91879  1.000 7.05124  ?  201 GNP A O1A   1 
HETATM 1304 O  O2A   . GNP B 2 .   ? -35.30163 10.63775 -0.66249  1.000 7.96447  -1 201 GNP A O2A   1 
HETATM 1305 O  "O5'" . GNP B 2 .   ? -34.44439 13.02589 -0.54613  1.000 6.42741  ?  201 GNP A "O5'" 1 
HETATM 1306 C  "C5'" . GNP B 2 .   ? -35.59356 13.64907 0.06058   1.000 7.02455  ?  201 GNP A "C5'" 1 
HETATM 1307 C  "C4'" . GNP B 2 .   ? -35.92018 14.89703 -0.72285  1.000 6.84397  ?  201 GNP A "C4'" 1 
HETATM 1308 O  "O4'" . GNP B 2 .   ? -34.83204 15.84349 -0.61853  1.000 6.94042  ?  201 GNP A "O4'" 1 
HETATM 1309 C  "C3'" . GNP B 2 .   ? -36.17759 14.70094 -2.21851  1.000 8.48760  ?  201 GNP A "C3'" 1 
HETATM 1310 O  "O3'" . GNP B 2 .   ? -37.25214 15.53568 -2.63671  1.000 9.57242  ?  201 GNP A "O3'" 1 
HETATM 1311 C  "C2'" . GNP B 2 .   ? -34.85500 15.13422 -2.85591  1.000 6.98823  ?  201 GNP A "C2'" 1 
HETATM 1312 O  "O2'" . GNP B 2 .   ? -35.03752 15.65362 -4.16948  1.000 8.78142  ?  201 GNP A "O2'" 1 
HETATM 1313 C  "C1'" . GNP B 2 .   ? -34.42978 16.25299 -1.91170  1.000 7.01625  ?  201 GNP A "C1'" 1 
HETATM 1314 N  N9    . GNP B 2 .   ? -32.98019 16.48459 -1.88855  1.000 6.98564  ?  201 GNP A N9    1 
HETATM 1315 C  C8    . GNP B 2 .   ? -31.99323 15.58601 -1.58004  1.000 7.37875  ?  201 GNP A C8    1 
HETATM 1316 N  N7    . GNP B 2 .   ? -30.79190 16.11592 -1.59207  1.000 7.65934  ?  201 GNP A N7    1 
HETATM 1317 C  C5    . GNP B 2 .   ? -31.00440 17.44266 -1.92989  1.000 6.93914  ?  201 GNP A C5    1 
HETATM 1318 C  C6    . GNP B 2 .   ? -30.09183 18.53018 -2.07902  1.000 8.31522  ?  201 GNP A C6    1 
HETATM 1319 O  O6    . GNP B 2 .   ? -28.86907 18.49632 -1.94334  1.000 9.29529  ?  201 GNP A O6    1 
HETATM 1320 N  N1    . GNP B 2 .   ? -30.73614 19.70881 -2.40677  1.000 8.41556  ?  201 GNP A N1    1 
HETATM 1321 C  C2    . GNP B 2 .   ? -32.08882 19.84708 -2.57701  1.000 10.32758 ?  201 GNP A C2    1 
HETATM 1322 N  N2    . GNP B 2 .   ? -32.53839 21.06299 -2.89640  1.000 12.09674 ?  201 GNP A N2    1 
HETATM 1323 N  N3    . GNP B 2 .   ? -32.95102 18.84185 -2.44018  1.000 8.19677  ?  201 GNP A N3    1 
HETATM 1324 C  C4    . GNP B 2 .   ? -32.34762 17.68290 -2.11515  1.000 7.13994  ?  201 GNP A C4    1 
HETATM 1325 MG MG    . MG  C 3 .   ? -34.05130 7.14006  1.16907   1.000 7.00476  ?  202 MG  A MG    1 
HETATM 1326 O  O     . HOH D 4 .   ? -31.30685 -7.80961 11.85464  1.000 27.92968 ?  301 HOH A O     1 
HETATM 1327 O  O     . HOH D 4 .   ? -32.83280 -7.90898 9.68933   1.000 25.12001 ?  302 HOH A O     1 
HETATM 1328 O  O     . HOH D 4 .   ? -20.12539 6.55013  14.03964  1.000 32.30098 ?  303 HOH A O     1 
HETATM 1329 O  O     . HOH D 4 .   ? -30.09959 27.44547 17.82416  1.000 25.35791 ?  304 HOH A O     1 
HETATM 1330 O  O     . HOH D 4 .   ? -38.15391 7.83667  6.26467   1.000 15.85573 ?  305 HOH A O     1 
HETATM 1331 O  O     . HOH D 4 .   ? -21.79971 -2.31397 -10.00127 1.000 30.96391 ?  306 HOH A O     1 
HETATM 1332 O  O     . HOH D 4 .   ? -16.95230 -2.89255 14.03188  1.000 32.45234 ?  307 HOH A O     1 
HETATM 1333 O  O     . HOH D 4 .   ? -7.88131  5.84826  9.63992   1.000 40.52684 ?  308 HOH A O     1 
HETATM 1334 O  O     . HOH D 4 .   ? -12.84958 -4.84569 3.61638   1.000 30.91483 ?  309 HOH A O     1 
HETATM 1335 O  O     . HOH D 4 .   ? -41.43187 4.75920  -1.53267  1.000 29.35488 ?  310 HOH A O     1 
HETATM 1336 O  O     . HOH D 4 .   ? -25.92215 26.45655 7.53254   1.000 20.79181 ?  311 HOH A O     1 
HETATM 1337 O  O     . HOH D 4 .   ? -14.53185 -0.97806 14.91441  1.000 56.48498 ?  312 HOH A O     1 
HETATM 1338 O  O     . HOH D 4 .   ? -35.45741 16.16936 6.38187   1.000 12.77071 ?  313 HOH A O     1 
HETATM 1339 O  O     . HOH D 4 .   ? -36.63002 15.26212 10.66999  1.000 13.85575 ?  314 HOH A O     1 
HETATM 1340 O  O     . HOH D 4 .   ? -35.31078 8.02302  -0.27627  1.000 7.90205  ?  315 HOH A O     1 
HETATM 1341 O  O     . HOH D 4 .   ? -36.06697 8.41431  12.64688  1.000 38.29022 ?  316 HOH A O     1 
HETATM 1342 O  O     . HOH D 4 .   ? -18.05340 4.75689  15.29785  1.000 24.38261 ?  317 HOH A O     1 
HETATM 1343 O  O     . HOH D 4 .   ? -29.33778 17.59749 19.81215  1.000 26.64123 ?  318 HOH A O     1 
HETATM 1344 O  O     . HOH D 4 .   ? -23.35303 25.03878 8.02333   1.000 13.54258 ?  319 HOH A O     1 
HETATM 1345 O  O     . HOH D 4 .   ? -40.18996 2.42050  3.64130   1.000 34.68942 ?  320 HOH A O     1 
HETATM 1346 O  O     . HOH D 4 .   ? -29.62318 11.56576 -6.39909  1.000 11.87257 ?  321 HOH A O     1 
HETATM 1347 O  O     . HOH D 4 .   ? -29.48055 13.56277 19.24975  1.000 14.59789 ?  322 HOH A O     1 
HETATM 1348 O  O     . HOH D 4 .   ? -30.67080 -3.23346 -3.98631  1.000 14.97417 ?  323 HOH A O     1 
HETATM 1349 O  O     . HOH D 4 .   ? -36.29976 10.41501 -3.13737  1.000 12.10857 ?  324 HOH A O     1 
HETATM 1350 O  O     . HOH D 4 .   ? -33.11285 27.11600 13.82014  1.000 52.59437 ?  325 HOH A O     1 
HETATM 1351 O  O     . HOH D 4 .   ? -18.43672 -5.85099 6.21665   1.000 32.70494 ?  326 HOH A O     1 
HETATM 1352 O  O     . HOH D 4 .   ? -20.16559 -0.02058 21.14238  1.000 36.10993 ?  327 HOH A O     1 
HETATM 1353 O  O     . HOH D 4 .   ? -14.09772 12.19647 10.86720  1.000 11.33670 ?  328 HOH A O     1 
HETATM 1354 O  O     . HOH D 4 .   ? -17.68747 17.70927 -5.38224  1.000 23.45875 ?  329 HOH A O     1 
HETATM 1355 O  O     . HOH D 4 .   ? -22.94700 11.69978 20.54717  1.000 16.58481 ?  330 HOH A O     1 
HETATM 1356 O  O     . HOH D 4 .   ? -32.62187 6.31581  2.47341   1.000 7.44801  ?  331 HOH A O     1 
HETATM 1357 O  O     . HOH D 4 .   ? -29.54382 5.18654  4.03113   1.000 9.69245  ?  332 HOH A O     1 
HETATM 1358 O  O     . HOH D 4 .   ? -21.38439 -6.14232 -9.26420  1.000 25.40862 ?  333 HOH A O     1 
HETATM 1359 O  O     . HOH D 4 .   ? -28.65631 27.96202 -4.16071  1.000 32.31803 ?  334 HOH A O     1 
HETATM 1360 O  O     . HOH D 4 .   ? -17.13984 28.01015 13.75939  1.000 32.60940 ?  335 HOH A O     1 
HETATM 1361 O  O     . HOH D 4 .   ? -32.03734 4.00716  -2.94212  1.000 12.58019 ?  336 HOH A O     1 
HETATM 1362 O  O     . HOH D 4 .   ? -15.07153 9.39975  -4.23123  1.000 15.71401 ?  337 HOH A O     1 
HETATM 1363 O  O     . HOH D 4 .   ? -36.08506 21.11046 2.07613   1.000 21.08625 ?  338 HOH A O     1 
HETATM 1364 O  O     . HOH D 4 .   ? -17.93211 28.45053 7.49576   1.000 36.13910 ?  339 HOH A O     1 
HETATM 1365 O  O     . HOH D 4 .   ? -19.30983 13.99619 -9.88768  1.000 22.49953 ?  340 HOH A O     1 
HETATM 1366 O  O     . HOH D 4 .   ? -35.40118 -0.17676 -2.31756  1.000 33.59234 ?  341 HOH A O     1 
HETATM 1367 O  O     . HOH D 4 .   ? -29.80705 -0.66364 -6.33670  1.000 29.21774 ?  342 HOH A O     1 
HETATM 1368 O  O     . HOH D 4 .   ? -25.54896 -4.61024 14.02770  1.000 28.44397 ?  343 HOH A O     1 
HETATM 1369 O  O     . HOH D 4 .   ? -31.72011 24.94460 -5.04844  1.000 19.10836 ?  344 HOH A O     1 
HETATM 1370 O  O     . HOH D 4 .   ? -17.28443 -3.25797 11.47059  1.000 25.49889 ?  345 HOH A O     1 
HETATM 1371 O  O     . HOH D 4 .   ? -12.42975 14.21445 0.72174   1.000 16.29363 ?  346 HOH A O     1 
HETATM 1372 O  O     . HOH D 4 .   ? -31.46448 2.43246  14.20074  1.000 39.65959 ?  347 HOH A O     1 
HETATM 1373 O  O     . HOH D 4 .   ? -21.28625 2.94586  -9.71657  1.000 28.98013 ?  348 HOH A O     1 
HETATM 1374 O  O     . HOH D 4 .   ? -15.49546 22.73762 13.75889  1.000 24.96579 ?  349 HOH A O     1 
HETATM 1375 O  O     . HOH D 4 .   ? -34.63078 4.72746  -2.15034  1.000 11.97506 ?  350 HOH A O     1 
HETATM 1376 O  O     . HOH D 4 .   ? -36.35999 1.52568  4.22871   1.000 10.20039 ?  351 HOH A O     1 
HETATM 1377 O  O     . HOH D 4 .   ? -34.91934 18.26448 4.61829   1.000 9.80567  ?  352 HOH A O     1 
HETATM 1378 O  O     . HOH D 4 .   ? -27.98766 20.02548 18.70021  1.000 17.22486 ?  353 HOH A O     1 
HETATM 1379 O  O     . HOH D 4 .   ? -42.28473 10.09416 -6.84567  1.000 36.81994 ?  354 HOH A O     1 
HETATM 1380 O  O     . HOH D 4 .   ? -23.98969 25.95374 -7.20995  1.000 24.06794 ?  355 HOH A O     1 
HETATM 1381 O  O     . HOH D 4 .   ? -16.57433 21.83212 5.92361   1.000 40.90105 ?  356 HOH A O     1 
HETATM 1382 O  O     . HOH D 4 .   ? -37.75959 13.64095 8.79114   1.000 17.31185 ?  357 HOH A O     1 
HETATM 1383 O  O     . HOH D 4 .   ? -39.09464 16.84041 -1.03978  1.000 27.94640 ?  358 HOH A O     1 
HETATM 1384 O  O     . HOH D 4 .   ? -34.16919 10.11985 14.43952  1.000 23.24729 ?  359 HOH A O     1 
HETATM 1385 O  O     . HOH D 4 .   ? -39.46163 11.84037 5.75406   1.000 22.81618 ?  360 HOH A O     1 
HETATM 1386 O  O     . HOH D 4 .   ? -25.21551 27.08613 -1.29698  1.000 24.86629 ?  361 HOH A O     1 
HETATM 1387 O  O     . HOH D 4 .   ? -14.22040 19.01499 12.13343  1.000 30.73940 ?  362 HOH A O     1 
HETATM 1388 O  O     . HOH D 4 .   ? -15.70501 7.60635  14.41873  1.000 21.34404 ?  363 HOH A O     1 
HETATM 1389 O  O     . HOH D 4 .   ? -18.48345 27.06855 15.87105  1.000 22.12234 ?  364 HOH A O     1 
HETATM 1390 O  O     . HOH D 4 .   ? -16.93890 -5.34471 3.42535   1.000 26.16385 ?  365 HOH A O     1 
HETATM 1391 O  O     . HOH D 4 .   ? -12.42933 -6.61759 0.52344   1.000 38.15246 ?  366 HOH A O     1 
HETATM 1392 O  O     . HOH D 4 .   ? -32.331   4.644    -8.940    1.000 38.99254 ?  367 HOH A O     1 
HETATM 1393 O  O     . HOH D 4 .   ? -21.21682 12.55748 -7.14120  1.000 13.67436 ?  368 HOH A O     1 
HETATM 1394 O  O     . HOH D 4 .   ? -24.29379 32.46095 10.92582  1.000 50.82765 ?  369 HOH A O     1 
HETATM 1395 O  O     . HOH D 4 .   ? -21.52832 11.25859 -9.62341  1.000 12.10419 ?  370 HOH A O     1 
HETATM 1396 O  O     . HOH D 4 .   ? -30.45460 13.48135 10.67675  1.000 7.98658  ?  371 HOH A O     1 
HETATM 1397 O  O     . HOH D 4 .   ? -29.21543 6.92029  20.18556  1.000 21.04637 ?  372 HOH A O     1 
HETATM 1398 O  O     . HOH D 4 .   ? -26.89452 18.41913 16.89321  1.000 14.47812 ?  373 HOH A O     1 
HETATM 1399 O  O     . HOH D 4 .   ? -23.58848 4.34249  21.76148  1.000 21.13657 ?  374 HOH A O     1 
HETATM 1400 O  O     . HOH D 4 .   ? -34.58911 15.48030 16.54081  1.000 16.22514 ?  375 HOH A O     1 
HETATM 1401 O  O     . HOH D 4 .   ? -30.91077 28.98255 -1.09667  1.000 32.93264 ?  376 HOH A O     1 
HETATM 1402 O  O     . HOH D 4 .   ? -13.10838 11.48417 13.29108  1.000 22.96939 ?  377 HOH A O     1 
HETATM 1403 O  O     . HOH D 4 .   ? -28.14237 0.85074  17.71067  1.000 27.62922 ?  378 HOH A O     1 
HETATM 1404 O  O     . HOH D 4 .   ? -42.46180 8.34697  -0.43928  1.000 30.73206 ?  379 HOH A O     1 
HETATM 1405 O  O     . HOH D 4 .   ? -35.30731 1.63248  7.52378   1.000 23.17729 ?  380 HOH A O     1 
HETATM 1406 O  O     . HOH D 4 .   ? -29.64957 18.51689 -10.41382 1.000 18.70917 ?  381 HOH A O     1 
HETATM 1407 O  O     . HOH D 4 .   ? -32.61278 -6.22816 14.23929  1.000 39.15084 ?  382 HOH A O     1 
HETATM 1408 O  O     . HOH D 4 .   ? -19.72283 15.65394 -5.59401  1.000 13.80198 ?  383 HOH A O     1 
HETATM 1409 O  O     . HOH D 4 .   ? -30.11594 28.57290 14.37233  1.000 24.68197 ?  384 HOH A O     1 
HETATM 1410 O  O     . HOH D 4 .   ? -34.97886 12.32820 -4.73630  1.000 14.95715 ?  385 HOH A O     1 
HETATM 1411 O  O     . HOH D 4 .   ? -18.10577 22.56610 20.02400  1.000 21.63430 ?  386 HOH A O     1 
HETATM 1412 O  O     . HOH D 4 .   ? -39.39042 -0.77019 4.12461   1.000 26.49389 ?  387 HOH A O     1 
HETATM 1413 O  O     . HOH D 4 .   ? -19.73091 9.13770  20.29605  1.000 26.61826 ?  388 HOH A O     1 
HETATM 1414 O  O     . HOH D 4 .   ? -14.86875 10.85829 16.72785  1.000 23.99447 ?  389 HOH A O     1 
HETATM 1415 O  O     . HOH D 4 .   ? -13.79512 0.19174  10.00337  1.000 19.52079 ?  390 HOH A O     1 
HETATM 1416 O  O     . HOH D 4 .   ? -32.99449 15.44755 -13.10778 1.000 15.22128 ?  391 HOH A O     1 
HETATM 1417 O  O     . HOH D 4 .   ? -33.53791 22.84952 18.96975  1.000 34.01768 ?  392 HOH A O     1 
HETATM 1418 O  O     . HOH D 4 .   ? -31.90386 8.90846  15.74036  1.000 20.61054 ?  393 HOH A O     1 
HETATM 1419 O  O     . HOH D 4 .   ? -12.74085 18.21719 17.64167  1.000 32.36821 ?  394 HOH A O     1 
HETATM 1420 O  O     . HOH D 4 .   ? -9.11136  14.59133 3.41957   1.000 42.68681 ?  395 HOH A O     1 
HETATM 1421 O  O     . HOH D 4 .   ? -21.74875 -5.00606 1.78566   1.000 22.46771 ?  396 HOH A O     1 
HETATM 1422 O  O     . HOH D 4 .   ? -30.37223 4.95714  6.88918   1.000 10.81735 ?  397 HOH A O     1 
HETATM 1423 O  O     . HOH D 4 .   ? -38.61312 18.19813 11.05549  1.000 39.12775 ?  398 HOH A O     1 
HETATM 1424 O  O     . HOH D 4 .   ? -24.16725 -1.86591 22.38966  1.000 37.17259 ?  399 HOH A O     1 
HETATM 1425 O  O     . HOH D 4 .   ? -35.52658 19.23957 -0.28579  1.000 17.07766 ?  400 HOH A O     1 
HETATM 1426 O  O     . HOH D 4 .   ? -36.82966 22.79253 10.88253  1.000 24.12984 ?  401 HOH A O     1 
HETATM 1427 O  O     . HOH D 4 .   ? -15.49484 20.62152 4.30743   1.000 35.57834 ?  402 HOH A O     1 
HETATM 1428 O  O     . HOH D 4 .   ? -24.84213 5.46026  -13.98436 1.000 24.49344 ?  403 HOH A O     1 
HETATM 1429 O  O     . HOH D 4 .   ? -15.24337 15.61480 -7.12716  1.000 35.21726 ?  404 HOH A O     1 
HETATM 1430 O  O     . HOH D 4 .   ? -14.76142 -0.47856 18.24184  1.000 37.30006 ?  405 HOH A O     1 
HETATM 1431 O  O     . HOH D 4 .   ? -36.79400 10.64005 10.69186  1.000 19.00383 ?  406 HOH A O     1 
HETATM 1432 O  O     . HOH D 4 .   ? -18.45781 1.90797  -10.35509 1.000 30.57518 ?  407 HOH A O     1 
HETATM 1433 O  O     . HOH D 4 .   ? -10.00346 13.46229 1.61116   1.000 28.61353 ?  408 HOH A O     1 
HETATM 1434 O  O     . HOH D 4 .   ? -11.22522 6.98535  -8.45204  1.000 40.00535 ?  409 HOH A O     1 
HETATM 1435 O  O     . HOH D 4 .   ? -42.02773 14.77624 -3.93649  1.000 27.60516 ?  410 HOH A O     1 
HETATM 1436 O  O     . HOH D 4 .   ? -14.77072 17.99369 21.39321  1.000 33.95484 ?  411 HOH A O     1 
HETATM 1437 O  O     . HOH D 4 .   ? -15.126   28.399   9.742     1.000 51.69210 ?  412 HOH A O     1 
HETATM 1438 O  O     . HOH D 4 .   ? -7.93709  -1.23060 6.61827   1.000 35.16156 ?  413 HOH A O     1 
HETATM 1439 O  O     . HOH D 4 .   ? -20.71994 -5.71603 13.12272  1.000 31.16143 ?  414 HOH A O     1 
HETATM 1440 O  O     . HOH D 4 .   ? -35.84760 13.51025 15.13374  1.000 17.49717 ?  415 HOH A O     1 
HETATM 1441 O  O     . HOH D 4 .   ? -21.615   29.680   4.095     1.000 36.95512 ?  416 HOH A O     1 
HETATM 1442 O  O     . HOH D 4 .   ? -34.52973 2.15690  -5.12157  1.000 42.22050 ?  417 HOH A O     1 
HETATM 1443 O  O     . HOH D 4 .   ? -35.77340 6.87178  -3.58703  1.000 17.74326 ?  418 HOH A O     1 
HETATM 1444 O  O     . HOH D 4 .   ? -30.99199 6.54001  8.93240   1.000 12.53427 ?  419 HOH A O     1 
HETATM 1445 O  O     . HOH D 4 .   ? -31.54467 2.15709  -6.95116  1.000 39.24519 ?  420 HOH A O     1 
HETATM 1446 O  O     . HOH D 4 .   ? -36.72913 25.30776 6.52391   1.000 41.95971 ?  421 HOH A O     1 
HETATM 1447 O  O     . HOH D 4 .   ? -19.37210 11.43139 20.01280  1.000 43.54186 ?  422 HOH A O     1 
HETATM 1448 O  O     . HOH D 4 .   ? -20.90205 -6.83067 -6.01126  1.000 41.55941 ?  423 HOH A O     1 
HETATM 1449 O  O     . HOH D 4 .   ? -36.46984 2.39150  -2.39679  1.000 16.47894 ?  424 HOH A O     1 
HETATM 1450 O  O     . HOH D 4 .   ? -23.04816 -5.57522 14.69564  1.000 36.90556 ?  425 HOH A O     1 
HETATM 1451 O  O     . HOH D 4 .   ? -23.72684 -2.34834 -1.71030  1.000 24.43040 ?  426 HOH A O     1 
HETATM 1452 O  O     . HOH D 4 .   ? -17.69958 21.60070 2.99101   1.000 15.67535 ?  427 HOH A O     1 
HETATM 1453 O  O     . HOH D 4 .   ? -12.66789 0.65361  12.46869  1.000 41.42790 ?  428 HOH A O     1 
HETATM 1454 O  O     . HOH D 4 .   ? -36.97700 19.99260 5.36268   1.000 18.64866 ?  429 HOH A O     1 
HETATM 1455 O  O     . HOH D 4 .   ? -14.06484 19.39994 9.25928   1.000 17.30343 ?  430 HOH A O     1 
HETATM 1456 O  O     . HOH D 4 .   ? -14.11693 8.83859  12.59395  1.000 19.80936 ?  431 HOH A O     1 
HETATM 1457 O  O     . HOH D 4 .   ? -25.03928 0.72570  -7.89184  1.000 23.12669 ?  432 HOH A O     1 
HETATM 1458 O  O     . HOH D 4 .   ? -23.19608 -4.79667 -0.25092  1.000 32.74627 ?  433 HOH A O     1 
HETATM 1459 O  O     . HOH D 4 .   ? -29.27239 29.55577 9.33464   1.000 29.82270 ?  434 HOH A O     1 
HETATM 1460 O  O     . HOH D 4 .   ? -16.311   20.603   21.903    1.000 25.30468 ?  435 HOH A O     1 
HETATM 1461 O  O     . HOH D 4 .   ? -18.59889 29.47513 11.19864  1.000 40.97330 ?  436 HOH A O     1 
HETATM 1462 O  O     . HOH D 4 .   ? -31.01709 13.42569 21.52420  1.000 28.93476 ?  437 HOH A O     1 
HETATM 1463 O  O     . HOH D 4 .   ? -17.05844 12.90140 20.73532  1.000 30.44656 ?  438 HOH A O     1 
HETATM 1464 O  O     . HOH D 4 .   ? -34.61575 4.25159  -6.46331  1.000 25.07804 ?  439 HOH A O     1 
HETATM 1465 O  O     . HOH D 4 .   ? -23.24428 -6.89230 5.90306   1.000 24.86901 ?  440 HOH A O     1 
HETATM 1466 O  O     . HOH D 4 .   ? -37.71724 17.10497 1.74086   1.000 23.57778 ?  441 HOH A O     1 
HETATM 1467 O  O     . HOH D 4 .   ? -23.06235 13.13838 -11.16218 1.000 19.07222 ?  442 HOH A O     1 
HETATM 1468 O  O     . HOH D 4 .   ? -21.14151 8.83763  -10.87351 1.000 50.25595 ?  443 HOH A O     1 
HETATM 1469 O  O     . HOH D 4 .   ? -15.73716 11.18557 19.45536  1.000 39.95870 ?  444 HOH A O     1 
HETATM 1470 O  O     . HOH D 4 .   ? -26.439   29.641   18.285    1.000 44.63100 ?  445 HOH A O     1 
HETATM 1471 O  O     . HOH D 4 .   ? -23.00299 27.47226 4.29096   1.000 44.70229 ?  446 HOH A O     1 
HETATM 1472 O  O     . HOH D 4 .   ? -17.92578 7.45138  19.97141  1.000 42.25577 ?  447 HOH A O     1 
HETATM 1473 O  O     . HOH D 4 .   ? -41.90694 9.17326  4.37776   1.000 48.09628 ?  448 HOH A O     1 
HETATM 1474 O  O     . HOH D 4 .   ? -16.69514 5.96490  17.71453  1.000 32.24795 ?  449 HOH A O     1 
HETATM 1475 O  O     . HOH D 4 .   ? -32.27298 27.50425 -4.20658  1.000 40.20720 ?  450 HOH A O     1 
HETATM 1476 O  O     . HOH D 4 .   ? -12.56715 4.57817  13.71286  1.000 36.96366 ?  451 HOH A O     1 
HETATM 1477 O  O     . HOH D 4 .   ? -29.738   -11.404  14.352    1.000 34.94511 ?  452 HOH A O     1 
HETATM 1478 O  O     . HOH D 4 .   ? -32.59399 26.65391 16.70481  1.000 44.48388 ?  453 HOH A O     1 
HETATM 1479 O  O     . HOH D 4 .   ? -25.475   31.625   19.235    1.000 48.89244 ?  454 HOH A O     1 
HETATM 1480 O  O     . HOH D 4 .   ? -30.74574 29.37538 11.69227  1.000 29.50279 ?  455 HOH A O     1 
HETATM 1481 O  O     . HOH D 4 .   ? -15.467   16.333   23.243    1.000 38.29946 ?  456 HOH A O     1 
HETATM 1482 O  O     . HOH D 4 .   ? -13.99604 20.54824 14.18141  1.000 21.08643 ?  457 HOH A O     1 
HETATM 1483 O  O     . HOH D 4 .   ? -33.16976 14.01700 18.42227  1.000 24.97034 ?  458 HOH A O     1 
HETATM 1484 O  O     . HOH D 4 .   ? -27.572   -12.612  13.319    1.000 39.30576 ?  459 HOH A O     1 
HETATM 1485 O  O     . HOH D 4 .   ? -12.85610 13.40886 -4.47905  1.000 38.82726 ?  460 HOH A O     1 
HETATM 1486 O  O     . HOH D 4 .   ? -28.08550 4.46116  21.19388  1.000 32.39029 ?  461 HOH A O     1 
HETATM 1487 O  O     . HOH D 4 .   ? -32.407   15.268   20.617    1.000 29.36190 ?  462 HOH A O     1 
HETATM 1488 O  O     . HOH D 4 .   ? -14.77838 19.99442 -6.13151  1.000 43.62264 ?  463 HOH A O     1 
HETATM 1489 O  O     . HOH D 4 .   ? -38.28476 3.58413  -3.66092  1.000 43.64156 ?  464 HOH A O     1 
HETATM 1490 O  O     . HOH D 4 .   ? -22.26317 4.49186  -13.51980 1.000 47.56619 ?  465 HOH A O     1 
HETATM 1491 O  O     . HOH D 4 .   ? -20.32452 -8.30091 12.13179  1.000 43.55461 ?  466 HOH A O     1 
HETATM 1492 O  O     . HOH D 4 .   ? -16.324   17.812   25.744    1.000 26.41925 ?  467 HOH A O     1 
HETATM 1493 O  O     . HOH D 4 .   ? -14.41532 6.88894  16.59720  1.000 42.79286 ?  468 HOH A O     1 
HETATM 1494 O  O     . HOH D 4 .   ? -16.66278 25.43855 17.06206  1.000 29.87479 ?  469 HOH A O     1 
HETATM 1495 O  O     . HOH D 4 .   ? -26.10796 3.86057  23.03288  1.000 37.37373 ?  470 HOH A O     1 
HETATM 1496 O  O     . HOH D 4 .   ? -18.64601 -4.95484 14.73810  1.000 45.90680 ?  471 HOH A O     1 
HETATM 1497 O  O     . HOH D 4 .   ? -38.27940 16.77505 5.75555   1.000 37.30102 ?  472 HOH A O     1 
HETATM 1498 O  O     . HOH D 4 .   ? -27.47011 26.61335 -6.03507  1.000 49.94669 ?  473 HOH A O     1 
HETATM 1499 O  O     . HOH D 4 .   ? -37.16210 10.48944 13.23071  1.000 47.30724 ?  474 HOH A O     1 
HETATM 1500 O  O     . HOH D 4 .   ? -22.15899 2.31506  22.86998  1.000 38.29265 ?  475 HOH A O     1 
HETATM 1501 O  O     . HOH D 4 .   ? -13.122   27.040   12.040    1.000 30.78867 ?  476 HOH A O     1 
HETATM 1502 O  O     . HOH D 4 .   ? -19.74028 11.20147 -11.26489 1.000 29.63547 ?  477 HOH A O     1 
HETATM 1503 O  O     . HOH D 4 .   ? -15.97130 23.19098 8.68954   1.000 50.99165 ?  478 HOH A O     1 
HETATM 1504 O  O     . HOH D 4 .   ? -23.168   27.423   0.488     1.000 33.11220 ?  479 HOH A O     1 
HETATM 1505 O  O     . HOH D 4 .   ? -11.18590 14.40414 -2.12264  1.000 39.15016 ?  480 HOH A O     1 
HETATM 1506 O  O     . HOH D 4 .   ? -13.16683 -2.05490 13.27245  1.000 52.61628 ?  481 HOH A O     1 
HETATM 1507 O  O     . HOH D 4 .   ? -37.10448 23.82479 1.53902   1.000 36.03735 ?  482 HOH A O     1 
HETATM 1508 O  O     . HOH D 4 .   ? -38.16242 19.62009 3.07030   1.000 35.61272 ?  483 HOH A O     1 
HETATM 1509 O  O     . HOH D 4 .   ? -37.79715 0.46008  6.29192   1.000 22.43395 ?  484 HOH A O     1 
HETATM 1510 O  O     . HOH D 4 .   ? -38.81443 15.78375 12.17879  1.000 31.89021 ?  485 HOH A O     1 
HETATM 1511 O  O     . HOH D 4 .   ? -14.29543 24.76042 15.65340  0.50  25.40137 ?  486 HOH A O     1 
HETATM 1512 O  O     . HOH D 4 .   ? -14.14368 -2.36178 10.44234  1.000 29.56065 ?  487 HOH A O     1 
HETATM 1513 O  O     . HOH D 4 .   ? -28.78728 2.01369  20.38837  1.000 33.97101 ?  488 HOH A O     1 
HETATM 1514 O  O     . HOH D 4 .   ? -40.43183 14.27046 5.53521   1.000 35.86767 ?  489 HOH A O     1 
HETATM 1515 O  O     . HOH D 4 .   ? -35.68707 10.97795 16.46104  1.000 36.53809 ?  490 HOH A O     1 
HETATM 1516 O  O     . HOH D 4 .   ? -28.44339 0.06976  21.93668  1.000 46.40709 ?  491 HOH A O     1 
HETATM 1517 O  O     . HOH D 4 .   ? -11.81580 20.46557 15.65340  0.50  27.25558 ?  492 HOH A O     1 
HETATM 1518 O  O     . HOH D 4 .   ? -31.50950 3.21550  20.37432  1.000 43.32486 ?  493 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLU A 2   ? 0.51344 0.43646 0.53727 0.19421  0.09005  -0.09088 7   GLU A N   
2    C CA  . GLU A 2   ? 0.46738 0.44001 0.53519 0.16307  0.08909  -0.08869 7   GLU A CA  
3    C C   . GLU A 2   ? 0.40944 0.39913 0.51704 0.14832  0.08781  -0.07707 7   GLU A C   
4    O O   . GLU A 2   ? 0.46202 0.41698 0.52884 0.17483  0.07607  -0.07587 7   GLU A O   
5    C CB  . GLU A 2   ? 0.49201 0.49900 0.55788 0.15711  0.08912  -0.08825 7   GLU A CB  
6    C CG  . GLU A 2   ? 0.49926 0.55011 0.57237 0.13826  0.09230  -0.09827 7   GLU A CG  
7    C CD  . GLU A 2   ? 0.52108 0.58196 0.58520 0.13773  0.09675  -0.10736 7   GLU A CD  
8    O OE1 . GLU A 2   ? 0.53394 0.59646 0.59059 0.13506  0.09445  -0.09931 7   GLU A OE1 
9    O OE2 . GLU A 2   ? 0.53230 0.58451 0.59439 0.13767  0.08889  -0.13018 7   GLU A OE2 
10   N N   . VAL A 3   ? 0.28748 0.34729 0.47514 0.13198  0.10472  -0.06428 8   VAL A N   
11   C CA  . VAL A 3   ? 0.22996 0.34633 0.44285 0.09708  0.08797  -0.03411 8   VAL A CA  
12   C C   . VAL A 3   ? 0.21445 0.29874 0.41261 0.09939  0.09932  -0.01672 8   VAL A C   
13   O O   . VAL A 3   ? 0.21804 0.29274 0.40693 0.04702  0.08965  0.03115  8   VAL A O   
14   C CB  . VAL A 3   ? 0.20632 0.39625 0.45068 0.08165  0.06059  -0.03107 8   VAL A CB  
15   C CG1 . VAL A 3   ? 0.22629 0.41590 0.45511 0.10843  0.05099  -0.03122 8   VAL A CG1 
16   C CG2 . VAL A 3   ? 0.21420 0.42286 0.46209 0.08499  0.06729  -0.02947 8   VAL A CG2 
17   N N   . ALA A 4   ? 0.19860 0.23718 0.36288 0.08699  0.08530  -0.03212 9   ALA A N   
18   C CA  . ALA A 4   ? 0.19399 0.19071 0.34785 0.05512  0.07313  -0.01238 9   ALA A CA  
19   C C   . ALA A 4   ? 0.19877 0.16054 0.31196 0.07405  0.04652  0.01023  9   ALA A C   
20   O O   . ALA A 4   ? 0.25059 0.19558 0.32533 0.12013  0.04433  0.03347  9   ALA A O   
21   C CB  . ALA A 4   ? 0.22336 0.22899 0.36138 0.04023  0.06126  -0.01945 9   ALA A CB  
22   N N   . ILE A 5   ? 0.17288 0.10709 0.28188 0.03302  0.01665  -0.01046 10  ILE A N   
23   C CA  . ILE A 5   ? 0.14000 0.12337 0.25281 0.03149  0.00264  -0.00480 10  ILE A CA  
24   C C   . ILE A 5   ? 0.13513 0.13179 0.23229 0.02838  0.01268  0.00349  10  ILE A C   
25   O O   . ILE A 5   ? 0.16517 0.13332 0.21712 0.02087  0.01790  0.03048  10  ILE A O   
26   C CB  . ILE A 5   ? 0.13784 0.12833 0.25969 0.02400  0.01480  -0.01860 10  ILE A CB  
27   C CG1 . ILE A 5   ? 0.13988 0.17018 0.29979 0.01606  0.01600  -0.03165 10  ILE A CG1 
28   C CG2 . ILE A 5   ? 0.18915 0.12136 0.23492 0.04089  0.00151  -0.02791 10  ILE A CG2 
29   C CD1 . ILE A 5   ? 0.14839 0.20663 0.32136 -0.00563 -0.00831 -0.01503 10  ILE A CD1 
30   N N   . LYS A 6   ? 0.12055 0.10480 0.22826 0.03428  0.01824  0.00182  11  LYS A N   
31   C CA  . LYS A 6   ? 0.14206 0.07038 0.21101 0.03515  0.02617  -0.00192 11  LYS A CA  
32   C C   . LYS A 6   ? 0.11157 0.10107 0.20401 0.02435  0.01011  0.01767  11  LYS A C   
33   O O   . LYS A 6   ? 0.15469 0.12773 0.20291 0.02826  -0.01664 -0.00064 11  LYS A O   
34   C CB  . LYS A 6   ? 0.14114 0.12695 0.22458 0.02087  0.01421  0.00270  11  LYS A CB  
35   C CG  . LYS A 6   ? 0.13971 0.10791 0.22321 0.00534  0.00225  -0.02694 11  LYS A CG  
36   C CD  . LYS A 6   ? 0.13841 0.12030 0.22365 -0.00677 -0.01514 -0.00682 11  LYS A CD  
37   C CE  . LYS A 6   ? 0.14738 0.16192 0.19393 -0.01063 -0.02886 0.02667  11  LYS A CE  
38   N NZ  . LYS A 6   ? 0.17531 0.12262 0.19911 -0.06368 -0.05088 0.03338  11  LYS A NZ  
39   N N   . MET A 7   ? 0.11910 0.07958 0.18540 0.02435  0.01025  -0.00986 12  MET A N   
40   C CA  . MET A 7   ? 0.09554 0.06950 0.18216 -0.00644 0.02744  -0.00597 12  MET A CA  
41   C C   . MET A 7   ? 0.09752 0.09422 0.17141 0.01519  0.01399  0.00098  12  MET A C   
42   O O   . MET A 7   ? 0.10822 0.15117 0.14563 0.01452  -0.00772 -0.01180 12  MET A O   
43   C CB  . MET A 7   ? 0.12064 0.09103 0.20305 -0.01421 0.02495  0.00433  12  MET A CB  
44   C CG  . MET A 7   ? 0.10446 0.11537 0.22521 -0.01459 0.03766  0.02172  12  MET A CG  
45   S SD  . MET A 7   ? 0.14063 0.13785 0.23102 -0.00892 0.03595  0.00526  12  MET A SD  
46   C CE  . MET A 7   ? 0.12389 0.20039 0.22212 -0.01227 0.02688  -0.02063 12  MET A CE  
47   N N   . VAL A 8   ? 0.10651 0.08186 0.16223 0.01557  0.01045  -0.00213 13  VAL A N   
48   C CA  . VAL A 8   ? 0.09994 0.06944 0.16822 -0.00364 0.03364  0.00478  13  VAL A CA  
49   C C   . VAL A 8   ? 0.08627 0.07702 0.15329 -0.01440 -0.00109 0.00286  13  VAL A C   
50   O O   . VAL A 8   ? 0.08896 0.08356 0.17187 0.00859  -0.00230 -0.00477 13  VAL A O   
51   C CB  . VAL A 8   ? 0.12555 0.08678 0.17931 -0.00745 0.00837  0.01442  13  VAL A CB  
52   C CG1 . VAL A 8   ? 0.16918 0.07420 0.21438 -0.00787 -0.01215 0.02720  13  VAL A CG1 
53   C CG2 . VAL A 8   ? 0.11739 0.11717 0.17343 -0.00722 -0.00689 0.03139  13  VAL A CG2 
54   N N   . VAL A 9   ? 0.07796 0.06813 0.13924 0.00260  -0.00852 -0.01248 14  VAL A N   
55   C CA  . VAL A 9   ? 0.09133 0.06474 0.12549 0.00658  -0.00140 0.00991  14  VAL A CA  
56   C C   . VAL A 9   ? 0.08574 0.08380 0.10117 0.01944  -0.00175 -0.00526 14  VAL A C   
57   O O   . VAL A 9   ? 0.08259 0.10859 0.13203 -0.01153 -0.00179 -0.02243 14  VAL A O   
58   C CB  . VAL A 9   ? 0.09824 0.08169 0.12757 0.02779  0.02036  0.00512  14  VAL A CB  
59   C CG1 . VAL A 9   ? 0.09254 0.10218 0.13902 0.00278  0.01093  0.01349  14  VAL A CG1 
60   C CG2 . VAL A 9   ? 0.10618 0.10844 0.14539 0.00905  0.03108  -0.00342 14  VAL A CG2 
61   N N   . VAL A 10  ? 0.09087 0.06976 0.09189 -0.00191 0.00327  0.00108  15  VAL A N   
62   C CA  . VAL A 10  ? 0.09632 0.06056 0.09668 -0.01502 0.02140  0.00950  15  VAL A CA  
63   C C   . VAL A 10  ? 0.04929 0.06707 0.11664 -0.01378 0.00871  -0.00530 15  VAL A C   
64   O O   . VAL A 10  ? 0.08334 0.06737 0.15871 -0.01920 0.02360  -0.00288 15  VAL A O   
65   C CB  . VAL A 10  ? 0.16911 0.10428 0.12165 0.01643  -0.02634 0.00622  15  VAL A CB  
66   C CG1 . VAL A 10  ? 0.22944 0.07468 0.13948 0.02038  -0.01914 0.02864  15  VAL A CG1 
67   C CG2 . VAL A 10  ? 0.15113 0.15464 0.11713 -0.00178 -0.01720 0.01480  15  VAL A CG2 
68   N N   . GLY A 11  ? 0.05062 0.07366 0.09508 -0.01621 0.01553  -0.01519 16  GLY A N   
69   C CA  . GLY A 11  ? 0.06867 0.08067 0.10057 0.00862  0.02131  -0.01701 16  GLY A CA  
70   C C   . GLY A 11  ? 0.05162 0.09552 0.07867 0.00548  0.00473  0.00295  16  GLY A C   
71   O O   . GLY A 11  ? 0.07403 0.10377 0.09982 -0.02415 -0.00483 -0.01933 16  GLY A O   
72   N N   . ASN A 12  ? 0.06726 0.10984 0.07896 -0.00245 0.00492  -0.00369 17  ASN A N   
73   C CA  . ASN A 12  ? 0.07327 0.10214 0.08652 -0.00515 0.00035  -0.01147 17  ASN A CA  
74   C C   . ASN A 12  ? 0.05150 0.09103 0.10369 -0.03297 -0.00836 -0.00070 17  ASN A C   
75   O O   . ASN A 12  ? 0.06048 0.10401 0.09367 -0.01324 0.02019  -0.01493 17  ASN A O   
76   C CB  . ASN A 12  ? 0.10502 0.09255 0.09585 -0.00764 0.01053  -0.02139 17  ASN A CB  
77   C CG  . ASN A 12  ? 0.08545 0.15431 0.09813 0.00741  0.01973  -0.01597 17  ASN A CG  
78   O OD1 . ASN A 12  ? 0.11736 0.13233 0.10800 0.00709  -0.00096 -0.00770 17  ASN A OD1 
79   N ND2 . ASN A 12  ? 0.09520 0.17018 0.11356 -0.01307 0.01915  -0.04309 17  ASN A ND2 
80   N N   . GLY A 13  ? 0.07755 0.10106 0.10710 -0.02128 -0.01596 -0.00343 18  GLY A N   
81   C CA  . GLY A 13  ? 0.06800 0.10880 0.10006 -0.02724 0.00950  -0.00347 18  GLY A CA  
82   C C   . GLY A 13  ? 0.06787 0.09725 0.11244 -0.03426 0.01295  -0.02738 18  GLY A C   
83   O O   . GLY A 13  ? 0.10302 0.10128 0.11335 -0.02421 -0.00362 -0.02207 18  GLY A O   
84   N N   . ALA A 14  ? 0.06923 0.11766 0.09454 -0.01585 0.01565  0.01838  19  ALA A N   
85   C CA  . ALA A 14  ? 0.06903 0.08203 0.11861 -0.00373 -0.01686 0.00605  19  ALA A CA  
86   C C   . ALA A 14  ? 0.07600 0.07575 0.09775 0.02170  -0.01465 -0.01571 19  ALA A C   
87   O O   . ALA A 14  ? 0.11765 0.08728 0.09929 0.00111  -0.00915 -0.00454 19  ALA A O   
88   C CB  . ALA A 14  ? 0.09233 0.15124 0.14430 0.03501  -0.00892 0.03197  19  ALA A CB  
89   N N   . VAL A 15  ? 0.04708 0.10743 0.08325 -0.01479 0.01536  -0.01243 20  VAL A N   
90   C CA  . VAL A 15  ? 0.05816 0.10759 0.08999 -0.03044 0.00602  -0.00867 20  VAL A CA  
91   C C   . VAL A 15  ? 0.06840 0.08074 0.07765 -0.01992 0.01890  0.01647  20  VAL A C   
92   O O   . VAL A 15  ? 0.08733 0.08802 0.06780 -0.01371 0.01081  -0.00509 20  VAL A O   
93   C CB  . VAL A 15  ? 0.06954 0.06915 0.09082 -0.00749 -0.00382 -0.00599 20  VAL A CB  
94   C CG1 . VAL A 15  ? 0.09467 0.10128 0.10271 0.00220  0.03131  -0.00631 20  VAL A CG1 
95   C CG2 . VAL A 15  ? 0.08449 0.06107 0.12087 -0.01809 0.00059  -0.01738 20  VAL A CG2 
96   N N   . GLY A 16  ? 0.07045 0.06746 0.08258 -0.00614 0.00632  -0.02119 21  GLY A N   
97   C CA  . GLY A 16  ? 0.05626 0.09820 0.07497 0.01281  0.01547  -0.01601 21  GLY A CA  
98   C C   . GLY A 16  ? 0.04588 0.06933 0.06542 -0.02279 0.02172  0.00433  21  GLY A C   
99   O O   . GLY A 16  ? 0.07197 0.08727 0.08013 -0.01180 0.01833  0.01484  21  GLY A O   
100  N N   . LYS A 17  ? 0.08737 0.05342 0.08908 -0.02999 0.00591  0.00518  22  LYS A N   
101  C CA  . LYS A 17  ? 0.08937 0.06996 0.08165 -0.00576 0.01457  -0.00029 22  LYS A CA  
102  C C   . LYS A 17  ? 0.08215 0.06697 0.06806 -0.00979 0.01943  -0.02293 22  LYS A C   
103  O O   . LYS A 17  ? 0.09452 0.06705 0.08555 -0.00248 0.00359  0.00433  22  LYS A O   
104  C CB  . LYS A 17  ? 0.12166 0.04932 0.07961 -0.01718 0.03521  0.01032  22  LYS A CB  
105  C CG  . LYS A 17  ? 0.12359 0.07553 0.05874 0.00017  0.00000  -0.01522 22  LYS A CG  
106  C CD  . LYS A 17  ? 0.09211 0.09908 0.07767 -0.01691 0.02293  0.02129  22  LYS A CD  
107  C CE  . LYS A 17  ? 0.10589 0.07556 0.10113 -0.01016 -0.00180 0.00026  22  LYS A CE  
108  N NZ  . LYS A 17  ? 0.09313 0.07600 0.09936 0.00871  0.01237  -0.01733 22  LYS A NZ  
109  N N   . SER A 18  ? 0.10293 0.04774 0.08770 -0.01537 -0.02035 -0.00089 23  SER A N   
110  C CA  . SER A 18  ? 0.10990 0.05201 0.07991 -0.02220 0.00122  -0.01034 23  SER A CA  
111  C C   . SER A 18  ? 0.09789 0.07138 0.07053 -0.01698 0.01163  0.00709  23  SER A C   
112  O O   . SER A 18  ? 0.09179 0.09275 0.07812 -0.00148 0.01643  0.00473  23  SER A O   
113  C CB  . SER A 18  ? 0.08996 0.10464 0.09325 -0.04358 -0.00313 -0.00209 23  SER A CB  
114  O OG  . SER A 18  ? 0.10499 0.07126 0.08024 -0.04509 0.02325  -0.00271 23  SER A OG  
115  N N   . SER A 19  ? 0.11650 0.04718 0.08077 -0.02830 -0.01082 0.01317  24  SER A N   
116  C CA  . SER A 19  ? 0.09777 0.04197 0.09181 -0.00465 0.01209  0.02093  24  SER A CA  
117  C C   . SER A 19  ? 0.07559 0.07437 0.08206 -0.02013 -0.00185 0.01290  24  SER A C   
118  O O   . SER A 19  ? 0.09267 0.10616 0.07330 -0.00063 0.02357  0.00451  24  SER A O   
119  C CB  . SER A 19  ? 0.09386 0.06445 0.11754 -0.01361 0.00557  0.01202  24  SER A CB  
120  O OG  . SER A 19  ? 0.09659 0.10075 0.11459 0.01263  0.00980  -0.00011 24  SER A OG  
121  N N   A MET A 20  ? 0.07414 0.07787 0.07630 -0.01641 -0.02028 -0.00094 25  MET A N   
122  N N   B MET A 20  ? 0.07687 0.08731 0.08476 -0.01270 -0.00461 0.01263  25  MET A N   
123  C CA  A MET A 20  ? 0.11054 0.05247 0.07809 -0.02330 -0.01725 -0.01160 25  MET A CA  
124  C CA  B MET A 20  ? 0.11462 0.07139 0.09826 -0.02861 0.00646  0.02421  25  MET A CA  
125  C C   A MET A 20  ? 0.08748 0.06440 0.07007 -0.01797 -0.00455 -0.00071 25  MET A C   
126  C C   B MET A 20  ? 0.09448 0.07555 0.08844 -0.02133 0.02076  0.02335  25  MET A C   
127  O O   A MET A 20  ? 0.08747 0.08316 0.06332 -0.01281 -0.01641 -0.01241 25  MET A O   
128  O O   B MET A 20  ? 0.11386 0.10317 0.09862 0.00632  0.04272  0.02805  25  MET A O   
129  C CB  A MET A 20  ? 0.13967 0.07835 0.07268 -0.01576 -0.02554 -0.02964 25  MET A CB  
130  C CB  B MET A 20  ? 0.14944 0.11997 0.10379 -0.01317 0.00483  0.04062  25  MET A CB  
131  C CG  A MET A 20  ? 0.15724 0.08829 0.06459 -0.04489 -0.02234 -0.01020 25  MET A CG  
132  C CG  B MET A 20  ? 0.17024 0.19867 0.12813 -0.01323 -0.00366 0.03278  25  MET A CG  
133  S SD  A MET A 20  ? 0.22375 0.10992 0.07727 -0.05512 -0.01088 0.00991  25  MET A SD  
134  S SD  B MET A 20  ? 0.17053 0.24173 0.14970 -0.01936 -0.03029 -0.01108 25  MET A SD  
135  C CE  A MET A 20  ? 0.24401 0.15190 0.13419 0.04296  -0.01165 -0.00155 25  MET A CE  
136  C CE  B MET A 20  ? 0.18133 0.25206 0.15456 -0.00355 -0.02158 -0.01244 25  MET A CE  
137  N N   . ILE A 21  ? 0.08084 0.05314 0.09045 -0.00399 -0.00856 0.01622  26  ILE A N   
138  C CA  . ILE A 21  ? 0.11023 0.06654 0.08803 0.00447  0.00753  -0.00553 26  ILE A CA  
139  C C   . ILE A 21  ? 0.11237 0.06822 0.08165 0.00422  0.01768  0.00660  26  ILE A C   
140  O O   . ILE A 21  ? 0.11994 0.08635 0.10048 0.01672  0.02479  -0.00282 26  ILE A O   
141  C CB  . ILE A 21  ? 0.14722 0.07019 0.10674 -0.00321 -0.00316 -0.00138 26  ILE A CB  
142  C CG1 . ILE A 21  ? 0.08931 0.12088 0.09865 -0.02652 0.00433  0.03050  26  ILE A CG1 
143  C CG2 . ILE A 21  ? 0.21245 0.05787 0.14073 0.01589  0.01707  -0.01103 26  ILE A CG2 
144  C CD1 . ILE A 21  ? 0.12259 0.10628 0.12896 -0.02720 -0.00902 0.03347  26  ILE A CD1 
145  N N   . GLN A 22  ? 0.12320 0.07075 0.08901 -0.01719 -0.00287 -0.00360 27  GLN A N   
146  C CA  . GLN A 22  ? 0.11275 0.09215 0.10665 -0.01401 -0.00077 0.00233  27  GLN A CA  
147  C C   . GLN A 22  ? 0.12997 0.04933 0.09734 -0.00042 -0.00068 -0.01744 27  GLN A C   
148  O O   . GLN A 22  ? 0.10043 0.11743 0.09938 0.00216  0.01750  -0.02968 27  GLN A O   
149  C CB  . GLN A 22  ? 0.13524 0.14460 0.13796 -0.04052 0.00553  0.02189  27  GLN A CB  
150  C CG  . GLN A 22  ? 0.20305 0.18526 0.16674 -0.07423 0.00202  0.01369  27  GLN A CG  
151  C CD  . GLN A 22  ? 0.27436 0.28934 0.20555 -0.06834 -0.01610 0.02605  27  GLN A CD  
152  O OE1 . GLN A 22  ? 0.30133 0.39294 0.26429 -0.08541 -0.02553 0.00100  27  GLN A OE1 
153  N NE2 . GLN A 22  ? 0.28473 0.24388 0.18799 -0.06683 -0.01553 0.06199  27  GLN A NE2 
154  N N   . ARG A 23  ? 0.07695 0.06533 0.08926 -0.00381 0.00345  0.00700  28  ARG A N   
155  C CA  . ARG A 23  ? 0.08190 0.08222 0.10095 -0.02294 0.00063  0.00835  28  ARG A CA  
156  C C   . ARG A 23  ? 0.08696 0.09712 0.09872 -0.01631 -0.00992 0.01105  28  ARG A C   
157  O O   . ARG A 23  ? 0.12164 0.11471 0.07919 0.00938  -0.00123 0.00585  28  ARG A O   
158  C CB  . ARG A 23  ? 0.11987 0.06607 0.10827 -0.04476 0.02009  0.00534  28  ARG A CB  
159  C CG  . ARG A 23  ? 0.09879 0.09049 0.10156 -0.03358 0.01519  0.04046  28  ARG A CG  
160  C CD  . ARG A 23  ? 0.15034 0.10146 0.10477 0.03121  0.00624  0.03346  28  ARG A CD  
161  N NE  . ARG A 23  ? 0.12782 0.09886 0.10689 -0.01410 -0.00081 0.02923  28  ARG A NE  
162  C CZ  . ARG A 23  ? 0.15827 0.09431 0.09262 -0.00755 -0.00243 0.01383  28  ARG A CZ  
163  N NH1 . ARG A 23  ? 0.23751 0.13703 0.09663 0.01298  0.01715  0.00238  28  ARG A NH1 
164  N NH2 . ARG A 23  ? 0.12476 0.11223 0.12571 -0.01377 -0.01049 0.00294  28  ARG A NH2 
165  N N   . TYR A 24  ? 0.09606 0.09195 0.10626 0.00130  -0.02585 -0.00749 29  TYR A N   
166  C CA  . TYR A 24  ? 0.08748 0.08407 0.09893 0.01251  -0.01902 -0.00175 29  TYR A CA  
167  C C   . TYR A 24  ? 0.11443 0.09628 0.10891 -0.01078 0.00057  0.00629  29  TYR A C   
168  O O   . TYR A 24  ? 0.12534 0.14475 0.12700 0.00342  0.03279  -0.00205 29  TYR A O   
169  C CB  . TYR A 24  ? 0.09448 0.14557 0.09705 0.02279  -0.00671 -0.00124 29  TYR A CB  
170  C CG  . TYR A 24  ? 0.09811 0.09912 0.11513 0.00051  0.00265  0.00008  29  TYR A CG  
171  C CD1 . TYR A 24  ? 0.12614 0.12112 0.13892 -0.01426 0.00905  -0.00504 29  TYR A CD1 
172  C CD2 . TYR A 24  ? 0.13520 0.12283 0.14267 0.00701  -0.01906 -0.02613 29  TYR A CD2 
173  C CE1 . TYR A 24  ? 0.12232 0.12204 0.16326 0.00521  -0.01475 -0.03274 29  TYR A CE1 
174  C CE2 . TYR A 24  ? 0.10535 0.14627 0.16057 -0.01814 -0.02248 -0.00929 29  TYR A CE2 
175  C CZ  . TYR A 24  ? 0.11640 0.10668 0.17919 0.01337  -0.02593 -0.00728 29  TYR A CZ  
176  O OH  . TYR A 24  ? 0.09789 0.18605 0.20756 0.03567  -0.01954 -0.02734 29  TYR A OH  
177  N N   . CYS A 25  ? 0.09929 0.09113 0.11219 0.00022  -0.01663 -0.01112 30  CYS A N   
178  C CA  . CYS A 25  ? 0.12699 0.08094 0.11543 -0.00690 -0.00682 -0.02091 30  CYS A CA  
179  C C   . CYS A 25  ? 0.11423 0.13270 0.11441 0.00713  -0.01814 -0.03142 30  CYS A C   
180  O O   . CYS A 25  ? 0.14809 0.19319 0.15114 0.05816  0.01271  -0.04219 30  CYS A O   
181  C CB  . CYS A 25  ? 0.13040 0.09129 0.13166 0.00399  -0.00417 -0.00217 30  CYS A CB  
182  S SG  . CYS A 25  ? 0.13954 0.10652 0.14020 0.00572  0.01009  0.00369  30  CYS A SG  
183  N N   . LYS A 26  ? 0.12815 0.12806 0.12147 0.02847  -0.02694 -0.01355 31  LYS A N   
184  C CA  . LYS A 26  ? 0.15016 0.16576 0.12771 0.00063  -0.02233 0.00146  31  LYS A CA  
185  C C   . LYS A 26  ? 0.16047 0.16244 0.09854 0.00336  0.00796  -0.01546 31  LYS A C   
186  O O   . LYS A 26  ? 0.20213 0.18020 0.11126 0.00130  -0.00318 -0.02674 31  LYS A O   
187  C CB  . LYS A 26  ? 0.17343 0.18499 0.15218 -0.04206 -0.04736 0.02432  31  LYS A CB  
188  C CG  . LYS A 26  ? 0.23381 0.27078 0.18769 -0.04281 -0.06551 0.06201  31  LYS A CG  
189  N N   . GLY A 27  ? 0.14292 0.10520 0.11617 -0.01407 0.02447  -0.01515 32  GLY A N   
190  C CA  . GLY A 27  ? 0.12936 0.14879 0.13006 -0.01639 0.01600  0.00782  32  GLY A CA  
191  C C   . GLY A 27  ? 0.15781 0.16772 0.11973 0.01485  0.01994  0.03040  32  GLY A C   
192  O O   . GLY A 27  ? 0.22282 0.24479 0.20560 0.03142  0.06071  0.11778  32  GLY A O   
193  N N   . ILE A 28  ? 0.14616 0.12313 0.10005 -0.00028 -0.01688 -0.00125 33  ILE A N   
194  C CA  . ILE A 28  ? 0.13606 0.16116 0.11516 0.02169  -0.01124 -0.01679 33  ILE A CA  
195  C C   . ILE A 28  ? 0.13196 0.13248 0.11670 -0.00445 -0.00738 0.02411  33  ILE A C   
196  O O   . ILE A 28  ? 0.14811 0.15904 0.10897 0.01941  -0.00618 0.01220  33  ILE A O   
197  C CB  . ILE A 28  ? 0.17856 0.14473 0.14086 0.04142  -0.02449 -0.00207 33  ILE A CB  
198  C CG1 . ILE A 28  ? 0.16472 0.13979 0.18412 -0.01307 -0.03951 -0.02139 33  ILE A CG1 
199  C CG2 . ILE A 28  ? 0.25638 0.18483 0.12657 0.07932  -0.04573 -0.02661 33  ILE A CG2 
200  C CD1 . ILE A 28  ? 0.17555 0.20014 0.23815 -0.04280 -0.05473 -0.05002 33  ILE A CD1 
201  N N   . PHE A 29  ? 0.13625 0.11093 0.13207 0.01728  -0.00502 -0.00716 34  PHE A N   
202  C CA  . PHE A 29  ? 0.09033 0.08907 0.12287 0.01584  0.01396  0.00358  34  PHE A CA  
203  C C   . PHE A 29  ? 0.10186 0.10118 0.11290 0.00349  0.01138  0.01532  34  PHE A C   
204  O O   . PHE A 29  ? 0.14499 0.14296 0.09965 0.01814  0.00308  0.02902  34  PHE A O   
205  C CB  . PHE A 29  ? 0.14909 0.11037 0.11564 0.00138  0.00572  -0.01058 34  PHE A CB  
206  C CG  . PHE A 29  ? 0.14353 0.10775 0.12032 0.00395  -0.01622 -0.04131 34  PHE A CG  
207  C CD1 . PHE A 29  ? 0.14695 0.14041 0.11259 -0.00219 -0.02646 -0.04235 34  PHE A CD1 
208  C CD2 . PHE A 29  ? 0.16649 0.10438 0.12515 -0.00373 0.02020  -0.01912 34  PHE A CD2 
209  C CE1 . PHE A 29  ? 0.15123 0.11298 0.14408 0.00065  -0.00708 -0.04004 34  PHE A CE1 
210  C CE2 . PHE A 29  ? 0.18581 0.10497 0.13265 0.01278  0.00212  -0.01515 34  PHE A CE2 
211  C CZ  . PHE A 29  ? 0.16746 0.10392 0.13784 0.00549  -0.00368 -0.04184 34  PHE A CZ  
212  N N   . THR A 30  ? 0.09043 0.09110 0.12146 -0.02078 -0.01127 0.02465  35  THR A N   
213  C CA  . THR A 30  ? 0.09915 0.12823 0.11726 -0.01252 -0.02881 -0.00299 35  THR A CA  
214  C C   . THR A 30  ? 0.14830 0.11341 0.10870 -0.02683 -0.02783 0.01626  35  THR A C   
215  O O   . THR A 30  ? 0.12549 0.13743 0.09309 -0.00212 -0.01255 0.00904  35  THR A O   
216  C CB  . THR A 30  ? 0.16400 0.13020 0.13112 0.00207  -0.03038 -0.00535 35  THR A CB  
217  O OG1 . THR A 30  ? 0.18354 0.14051 0.14758 -0.02251 -0.03446 0.02716  35  THR A OG1 
218  C CG2 . THR A 30  ? 0.18113 0.10832 0.16692 0.01298  -0.00307 -0.01427 35  THR A CG2 
219  N N   . LYS A 31  ? 0.15745 0.12734 0.12394 0.02951  -0.02318 0.00934  36  LYS A N   
220  C CA  . LYS A 31  ? 0.17219 0.12025 0.12074 0.03929  -0.00535 0.02140  36  LYS A CA  
221  C C   . LYS A 31  ? 0.15470 0.15100 0.10966 0.01960  -0.04467 0.01434  36  LYS A C   
222  O O   . LYS A 31  ? 0.12884 0.19424 0.10777 0.03056  -0.03683 -0.00031 36  LYS A O   
223  C CB  . LYS A 31  ? 0.25303 0.16939 0.16004 0.04974  -0.00027 0.04711  36  LYS A CB  
224  C CG  . LYS A 31  ? 0.31946 0.20777 0.18918 0.05399  0.00352  0.07739  36  LYS A CG  
225  C CD  . LYS A 31  ? 0.40054 0.23736 0.23584 0.10609  -0.00097 0.05403  36  LYS A CD  
226  C CE  . LYS A 31  ? 0.45964 0.26431 0.29104 0.13010  0.00189  0.06363  36  LYS A CE  
227  N NZ  . LYS A 31  ? 0.49790 0.25241 0.32320 0.13615  -0.00730 0.02968  36  LYS A NZ  
228  N N   . ASP A 32  ? 0.14514 0.16296 0.13406 0.03876  -0.01520 0.03494  37  ASP A N   
229  C CA  . ASP A 32  ? 0.15170 0.19517 0.14183 0.01678  0.00398  0.04587  37  ASP A CA  
230  C C   . ASP A 32  ? 0.15562 0.19253 0.12540 0.03367  -0.00872 0.07912  37  ASP A C   
231  O O   . ASP A 32  ? 0.21544 0.27961 0.16449 0.12189  0.01403  0.07377  37  ASP A O   
232  C CB  . ASP A 32  ? 0.17210 0.18693 0.17017 0.01033  -0.01154 0.01376  37  ASP A CB  
233  C CG  . ASP A 32  ? 0.16323 0.17254 0.17909 -0.03010 0.01255  0.03656  37  ASP A CG  
234  O OD1 . ASP A 32  ? 0.19068 0.16570 0.17637 -0.00831 0.00673  0.03262  37  ASP A OD1 
235  O OD2 . ASP A 32  ? 0.22242 0.19382 0.19972 -0.00330 0.01037  0.01564  37  ASP A OD2 
236  N N   . TYR A 33  ? 0.13874 0.14052 0.11397 -0.02415 -0.02886 0.05687  38  TYR A N   
237  C CA  . TYR A 33  ? 0.11573 0.10430 0.13705 -0.00677 -0.01830 0.02257  38  TYR A CA  
238  C C   . TYR A 33  ? 0.11971 0.12632 0.17381 -0.02853 -0.03571 0.01086  38  TYR A C   
239  O O   . TYR A 33  ? 0.13275 0.16590 0.21930 -0.01702 -0.00166 0.02638  38  TYR A O   
240  C CB  . TYR A 33  ? 0.12720 0.13336 0.13140 0.00170  0.00887  -0.00480 38  TYR A CB  
241  C CG  . TYR A 33  ? 0.08732 0.13755 0.13818 0.00813  -0.00944 0.01038  38  TYR A CG  
242  C CD1 . TYR A 33  ? 0.09304 0.14535 0.14194 0.00192  -0.02620 -0.02086 38  TYR A CD1 
243  C CD2 . TYR A 33  ? 0.13009 0.20711 0.14334 0.03793  -0.00309 0.03257  38  TYR A CD2 
244  C CE1 . TYR A 33  ? 0.10585 0.14043 0.14023 -0.01793 -0.01378 -0.01683 38  TYR A CE1 
245  C CE2 . TYR A 33  ? 0.18449 0.23693 0.15096 0.09636  0.00459  0.03444  38  TYR A CE2 
246  C CZ  . TYR A 33  ? 0.14166 0.17171 0.14134 0.05600  0.01340  0.02797  38  TYR A CZ  
247  O OH  . TYR A 33  ? 0.15518 0.22219 0.14015 0.04734  0.02745  0.02870  38  TYR A OH  
248  N N   . LYS A 34  ? 0.14554 0.11891 0.16652 -0.00458 -0.06329 0.00375  39  LYS A N   
249  C CA  . LYS A 34  ? 0.14414 0.12456 0.18571 -0.02702 -0.05904 0.01792  39  LYS A CA  
250  C C   . LYS A 34  ? 0.13948 0.09868 0.18768 -0.03816 -0.05224 0.00943  39  LYS A C   
251  O O   . LYS A 34  ? 0.12069 0.13862 0.16721 -0.02273 -0.02562 0.00736  39  LYS A O   
252  C CB  . LYS A 34  ? 0.21252 0.24235 0.21275 0.02967  -0.08654 0.00745  39  LYS A CB  
253  C CG  . LYS A 34  ? 0.27616 0.30167 0.24025 0.08093  -0.07695 0.03876  39  LYS A CG  
254  N N   . LYS A 35  ? 0.16898 0.11695 0.17538 -0.02561 -0.03129 0.00802  40  LYS A N   
255  C CA  . LYS A 35  ? 0.14575 0.11787 0.19490 -0.02015 -0.00308 0.01408  40  LYS A CA  
256  C C   . LYS A 35  ? 0.12458 0.07490 0.17688 0.00244  -0.01536 0.00355  40  LYS A C   
257  O O   . LYS A 35  ? 0.16266 0.10751 0.20421 -0.03587 -0.01923 -0.00353 40  LYS A O   
258  C CB  . LYS A 35  ? 0.15382 0.18845 0.20973 -0.01250 0.00674  0.02269  40  LYS A CB  
259  C CG  . LYS A 35  ? 0.22049 0.25122 0.26882 -0.01817 0.02202  0.01249  40  LYS A CG  
260  C CD  . LYS A 35  ? 0.28278 0.35037 0.30169 0.01155  0.04279  0.05061  40  LYS A CD  
261  C CE  . LYS A 35  ? 0.31151 0.40401 0.33195 0.03443  0.04456  0.05968  40  LYS A CE  
262  N NZ  . LYS A 35  ? 0.33942 0.45839 0.37311 0.04257  0.07229  0.06014  40  LYS A NZ  
263  N N   . THR A 36  ? 0.10427 0.06955 0.15232 0.00228  0.00630  0.02184  41  THR A N   
264  C CA  . THR A 36  ? 0.09356 0.07680 0.14226 -0.03606 0.00039  0.00783  41  THR A CA  
265  C C   . THR A 36  ? 0.13083 0.08475 0.13266 -0.02261 -0.00146 -0.00051 41  THR A C   
266  O O   . THR A 36  ? 0.13096 0.10794 0.12846 -0.03657 -0.00852 0.01790  41  THR A O   
267  C CB  . THR A 36  ? 0.10355 0.04896 0.14493 -0.02830 -0.00470 0.00521  41  THR A CB  
268  O OG1 . THR A 36  ? 0.10774 0.08184 0.12634 -0.05425 0.00914  0.00626  41  THR A OG1 
269  C CG2 . THR A 36  ? 0.10452 0.07948 0.13844 -0.02469 0.00076  0.01155  41  THR A CG2 
270  N N   . ILE A 37  ? 0.14184 0.08402 0.18326 -0.05019 -0.02229 0.01857  42  ILE A N   
271  C CA  . ILE A 37  ? 0.15921 0.08571 0.20651 -0.05151 -0.03507 0.00122  42  ILE A CA  
272  C C   . ILE A 37  ? 0.15200 0.07289 0.19347 -0.05032 0.00053  -0.00253 42  ILE A C   
273  O O   . ILE A 37  ? 0.18076 0.14226 0.22232 -0.03629 0.00977  -0.01726 42  ILE A O   
274  C CB  . ILE A 37  ? 0.22267 0.11399 0.25962 -0.05526 -0.07409 -0.00540 42  ILE A CB  
275  C CG1 . ILE A 37  ? 0.23414 0.18329 0.27846 -0.04176 -0.08813 -0.00455 42  ILE A CG1 
276  C CG2 . ILE A 37  ? 0.23969 0.14822 0.28017 -0.08709 -0.06889 -0.00568 42  ILE A CG2 
277  C CD1 . ILE A 37  ? 0.28324 0.26958 0.31731 0.03557  -0.07337 -0.00010 42  ILE A CD1 
278  N N   . GLY A 38  ? 0.14271 0.08001 0.17259 -0.05424 -0.01357 -0.00669 43  GLY A N   
279  C CA  . GLY A 38  ? 0.10766 0.10997 0.17909 -0.02986 0.00449  0.00203  43  GLY A CA  
280  C C   . GLY A 38  ? 0.12713 0.08209 0.15954 0.00155  0.02603  0.00395  43  GLY A C   
281  O O   . GLY A 38  ? 0.13839 0.07686 0.17023 -0.01621 0.02035  -0.01287 43  GLY A O   
282  N N   . VAL A 39  ? 0.10851 0.11348 0.14483 -0.04874 0.01663  0.00424  44  VAL A N   
283  C CA  . VAL A 39  ? 0.10242 0.10752 0.13880 -0.00858 0.02328  0.01612  44  VAL A CA  
284  C C   . VAL A 39  ? 0.15021 0.07577 0.12546 -0.00945 0.02869  0.01057  44  VAL A C   
285  O O   . VAL A 39  ? 0.20827 0.09465 0.14214 -0.03852 0.04108  -0.02736 44  VAL A O   
286  C CB  . VAL A 39  ? 0.12875 0.10077 0.15885 -0.02122 0.00431  0.00967  44  VAL A CB  
287  C CG1 . VAL A 39  ? 0.16004 0.12900 0.17764 -0.01328 0.01006  0.02153  44  VAL A CG1 
288  C CG2 . VAL A 39  ? 0.16499 0.10787 0.14980 0.00348  -0.00975 -0.01892 44  VAL A CG2 
289  N N   . ASP A 40  ? 0.13481 0.09888 0.10940 -0.02913 0.01079  0.00576  45  ASP A N   
290  C CA  . ASP A 40  ? 0.16523 0.10212 0.11653 -0.02946 0.02739  -0.00838 45  ASP A CA  
291  C C   . ASP A 40  ? 0.16587 0.06370 0.13501 -0.03428 0.01744  -0.00513 45  ASP A C   
292  O O   . ASP A 40  ? 0.16077 0.14102 0.14863 -0.02217 -0.00380 -0.04640 45  ASP A O   
293  C CB  . ASP A 40  ? 0.19899 0.10202 0.12772 -0.02981 0.01293  0.02790  45  ASP A CB  
294  C CG  . ASP A 40  ? 0.26552 0.13543 0.17796 -0.01632 -0.00063 -0.00379 45  ASP A CG  
295  O OD1 . ASP A 40  ? 0.29634 0.15906 0.17658 -0.00134 -0.00319 -0.01575 45  ASP A OD1 
296  O OD2 . ASP A 40  ? 0.26848 0.15869 0.17944 0.00322  -0.01875 -0.00986 45  ASP A OD2 
297  N N   . PHE A 41  ? 0.13961 0.12679 0.17048 -0.02148 0.02347  -0.05941 46  PHE A N   
298  C CA  . PHE A 41  ? 0.13978 0.13366 0.19563 -0.04117 0.03770  -0.06275 46  PHE A CA  
299  C C   . PHE A 41  ? 0.15508 0.15648 0.20765 -0.06795 0.05222  -0.03127 46  PHE A C   
300  O O   . PHE A 41  ? 0.22774 0.22054 0.18794 -0.09543 0.04564  -0.05927 46  PHE A O   
301  C CB  . PHE A 41  ? 0.18261 0.14598 0.19820 0.01608  0.03214  -0.06801 46  PHE A CB  
302  C CG  . PHE A 41  ? 0.18212 0.15796 0.17875 -0.01589 0.01638  -0.05121 46  PHE A CG  
303  C CD1 . PHE A 41  ? 0.19305 0.19856 0.19852 -0.00711 -0.00807 -0.01761 46  PHE A CD1 
304  C CD2 . PHE A 41  ? 0.21193 0.15632 0.16859 -0.05004 0.02071  -0.05883 46  PHE A CD2 
305  C CE1 . PHE A 41  ? 0.18739 0.22249 0.17735 -0.00686 -0.06031 -0.04884 46  PHE A CE1 
306  C CE2 . PHE A 41  ? 0.19572 0.16462 0.15831 -0.06485 -0.01072 -0.04426 46  PHE A CE2 
307  C CZ  . PHE A 41  ? 0.18787 0.17813 0.15986 -0.02193 -0.03172 -0.03682 46  PHE A CZ  
308  N N   . LEU A 42  ? 0.13462 0.13805 0.20670 -0.02562 0.03189  -0.03688 47  LEU A N   
309  C CA  . LEU A 42  ? 0.15220 0.10429 0.20238 -0.04909 0.03180  -0.04081 47  LEU A CA  
310  C C   . LEU A 42  ? 0.14610 0.13849 0.19195 -0.01838 0.02347  -0.02842 47  LEU A C   
311  O O   . LEU A 42  ? 0.16662 0.25276 0.18512 -0.01677 0.00643  -0.02508 47  LEU A O   
312  C CB  . LEU A 42  ? 0.16913 0.13064 0.24955 -0.05539 0.00823  -0.02054 47  LEU A CB  
313  C CG  . LEU A 42  ? 0.19237 0.15536 0.27241 -0.04421 -0.00696 -0.02529 47  LEU A CG  
314  C CD1 . LEU A 42  ? 0.22090 0.18896 0.27126 -0.01909 0.01210  -0.00765 47  LEU A CD1 
315  C CD2 . LEU A 42  ? 0.21526 0.17994 0.27286 -0.00163 -0.01446 -0.02308 47  LEU A CD2 
316  N N   . GLU A 43  ? 0.14651 0.14452 0.20621 -0.02269 0.00029  -0.03120 48  GLU A N   
317  C CA  . GLU A 43  ? 0.15310 0.19563 0.22584 -0.00476 0.04625  -0.00109 48  GLU A CA  
318  C C   . GLU A 43  ? 0.15362 0.18169 0.20297 0.03025  0.04856  -0.00860 48  GLU A C   
319  O O   . GLU A 43  ? 0.17760 0.16960 0.20727 0.03113  0.01850  -0.02787 48  GLU A O   
320  C CB  . GLU A 43  ? 0.25836 0.28175 0.28383 0.04025  0.03931  -0.03627 48  GLU A CB  
321  C CG  . GLU A 43  ? 0.33392 0.33313 0.34383 0.06590  0.03490  -0.06297 48  GLU A CG  
322  C CD  . GLU A 43  ? 0.38300 0.36030 0.38930 0.06647  0.03687  -0.07877 48  GLU A CD  
323  O OE1 . GLU A 43  ? 0.38699 0.35738 0.40184 0.05548  0.02297  -0.10093 48  GLU A OE1 
324  O OE2 . GLU A 43  ? 0.38940 0.36896 0.41369 0.07406  0.07827  -0.07374 48  GLU A OE2 
325  N N   . ARG A 44  ? 0.14828 0.18038 0.19495 0.01922  0.04728  -0.01357 49  ARG A N   
326  C CA  . ARG A 44  ? 0.15051 0.21447 0.21581 0.02162  0.06105  -0.00990 49  ARG A CA  
327  C C   . ARG A 44  ? 0.18442 0.23707 0.21748 0.04502  0.06301  0.00338  49  ARG A C   
328  O O   . ARG A 44  ? 0.16653 0.26023 0.20722 0.03065  0.04460  -0.00388 49  ARG A O   
329  C CB  . ARG A 44  ? 0.16622 0.26916 0.27722 0.01584  0.05663  -0.00277 49  ARG A CB  
330  C CG  . ARG A 44  ? 0.18929 0.31517 0.32185 -0.01533 0.08271  0.02948  49  ARG A CG  
331  C CD  . ARG A 44  ? 0.20155 0.37284 0.33400 0.00041  0.09271  0.05746  49  ARG A CD  
332  N NE  . ARG A 44  ? 0.24252 0.43392 0.36938 -0.02917 0.09226  0.09189  49  ARG A NE  
333  C CZ  . ARG A 44  ? 0.28980 0.49545 0.37790 -0.06598 0.10796  0.07669  49  ARG A CZ  
334  N NH1 . ARG A 44  ? 0.28157 0.50255 0.36476 -0.13909 0.10979  0.06314  49  ARG A NH1 
335  N NH2 . ARG A 44  ? 0.33238 0.51531 0.39336 -0.05156 0.13577  0.09640  49  ARG A NH2 
336  N N   . GLN A 45  ? 0.22591 0.28754 0.24385 0.08694  0.08831  0.01860  50  GLN A N   
337  C CA  . GLN A 45  ? 0.21364 0.31291 0.28664 0.04978  0.12672  0.02000  50  GLN A CA  
338  C C   . GLN A 45  ? 0.23085 0.34361 0.31375 0.04261  0.11602  0.04739  50  GLN A C   
339  O O   . GLN A 45  ? 0.25740 0.35698 0.33628 0.03707  0.08051  0.06110  50  GLN A O   
340  C CB  . GLN A 45  ? 0.25272 0.33271 0.29578 0.09883  0.11628  -0.00026 50  GLN A CB  
341  N N   . ILE A 46  ? 0.19459 0.35790 0.32590 0.05364  0.08904  0.02008  51  ILE A N   
342  C CA  . ILE A 46  ? 0.19638 0.36538 0.35411 0.06373  0.08126  0.02919  51  ILE A CA  
343  C C   . ILE A 46  ? 0.20383 0.39419 0.37639 0.06391  0.09344  0.03597  51  ILE A C   
344  O O   . ILE A 46  ? 0.18753 0.37347 0.36748 0.06419  0.08859  0.05163  51  ILE A O   
345  C CB  . ILE A 46  ? 0.26375 0.39361 0.37858 0.11079  0.08606  0.01216  51  ILE A CB  
346  C CG1 . ILE A 46  ? 0.30772 0.40168 0.38788 0.13420  0.09473  -0.00859 51  ILE A CG1 
347  C CG2 . ILE A 46  ? 0.26920 0.40281 0.39273 0.11474  0.07733  -0.00427 51  ILE A CG2 
348  C CD1 . ILE A 46  ? 0.31337 0.39979 0.38749 0.17186  0.10102  -0.00978 51  ILE A CD1 
349  N N   . GLN A 47  ? 0.21196 0.43582 0.40560 0.04038  0.12021  0.03388  52  GLN A N   
350  C CA  . GLN A 47  ? 0.24924 0.48394 0.45194 -0.01028 0.14235  0.03143  52  GLN A CA  
351  C C   . GLN A 47  ? 0.29957 0.51630 0.48006 -0.00389 0.14834  0.03248  52  GLN A C   
352  O O   . GLN A 47  ? 0.34628 0.53649 0.48888 0.04557  0.13701  0.03868  52  GLN A O   
353  C CB  . GLN A 47  ? 0.29334 0.53273 0.48527 0.00176  0.13188  0.01269  52  GLN A CB  
354  C CG  . GLN A 47  ? 0.34786 0.59064 0.51805 0.04660  0.11529  -0.01318 52  GLN A CG  
355  C CD  . GLN A 47  ? 0.39948 0.63949 0.54987 0.06686  0.08792  -0.03392 52  GLN A CD  
356  O OE1 . GLN A 47  ? 0.43022 0.67161 0.56679 0.10121  0.08327  -0.04278 52  GLN A OE1 
357  N NE2 . GLN A 47  ? 0.42719 0.65211 0.55868 0.07455  0.07766  -0.03611 52  GLN A NE2 
358  N N   . VAL A 48  ? 0.29300 0.52605 0.49939 -0.04002 0.14272  0.02189  53  VAL A N   
359  C CA  . VAL A 48  ? 0.35192 0.55416 0.51879 -0.04316 0.13095  0.00701  53  VAL A CA  
360  C C   . VAL A 48  ? 0.43712 0.57172 0.52995 -0.03915 0.09243  0.00524  53  VAL A C   
361  O O   . VAL A 48  ? 0.42416 0.60529 0.53682 -0.04856 0.07968  0.01029  53  VAL A O   
362  C CB  . VAL A 48  ? 0.36172 0.57012 0.53568 -0.02103 0.12162  -0.01204 53  VAL A CB  
363  C CG1 . VAL A 48  ? 0.37170 0.57220 0.54587 -0.02540 0.10979  -0.02093 53  VAL A CG1 
364  C CG2 . VAL A 48  ? 0.34422 0.55690 0.53548 -0.01701 0.14184  -0.00446 53  VAL A CG2 
375  N N   . GLU A 51  ? 0.43319 0.59053 0.53480 -0.02326 0.10251  -0.00841 56  GLU A N   
376  C CA  . GLU A 51  ? 0.36394 0.54728 0.49443 -0.00653 0.10659  -0.00808 56  GLU A CA  
377  C C   . GLU A 51  ? 0.30606 0.55399 0.52585 0.02985  0.12174  -0.00412 56  GLU A C   
378  O O   . GLU A 51  ? 0.29550 0.54592 0.54741 0.03791  0.12113  0.00458  56  GLU A O   
380  N N   . ASP A 52  ? 0.31264 0.51608 0.51433 0.02160  0.11337  0.00041  57  ASP A N   
381  C CA  . ASP A 52  ? 0.32038 0.44111 0.46588 0.01576  0.11212  -0.00546 57  ASP A CA  
382  C C   . ASP A 52  ? 0.25280 0.41067 0.43356 0.05497  0.10884  -0.01220 57  ASP A C   
383  O O   . ASP A 52  ? 0.27641 0.43714 0.44698 0.09723  0.10342  -0.01707 57  ASP A O   
388  N N   . VAL A 53  ? 0.19267 0.37757 0.39471 0.04355  0.10763  -0.00504 58  VAL A N   
389  C CA  . VAL A 53  ? 0.15438 0.34245 0.36850 -0.00723 0.07655  -0.00875 58  VAL A CA  
390  C C   . VAL A 53  ? 0.14907 0.30723 0.34947 0.00413  0.07231  0.02058  58  VAL A C   
391  O O   . VAL A 53  ? 0.20807 0.38078 0.37161 0.04815  0.03868  0.05010  58  VAL A O   
392  C CB  . VAL A 53  ? 0.20245 0.39334 0.37214 0.01947  0.08344  -0.02214 58  VAL A CB  
393  C CG1 . VAL A 53  ? 0.23737 0.39699 0.37338 0.01111  0.08006  -0.02371 58  VAL A CG1 
394  C CG2 . VAL A 53  ? 0.23754 0.40529 0.38286 0.02913  0.06051  -0.03556 58  VAL A CG2 
395  N N   . ARG A 54  ? 0.15762 0.24053 0.30302 0.03693  0.07257  -0.01673 59  ARG A N   
396  C CA  . ARG A 54  ? 0.17448 0.22007 0.27686 0.04459  0.08843  -0.04580 59  ARG A CA  
397  C C   . ARG A 54  ? 0.16988 0.20419 0.24461 0.05568  0.06025  -0.02734 59  ARG A C   
398  O O   . ARG A 54  ? 0.16153 0.19450 0.27484 0.06334  0.05859  -0.02397 59  ARG A O   
399  C CB  . ARG A 54  ? 0.22954 0.29826 0.31112 0.04783  0.08966  -0.05856 59  ARG A CB  
400  C CG  . ARG A 54  ? 0.29485 0.35497 0.34800 0.05714  0.09612  -0.08827 59  ARG A CG  
401  C CD  . ARG A 54  ? 0.34581 0.41751 0.37219 0.07359  0.10958  -0.09286 59  ARG A CD  
402  N NE  . ARG A 54  ? 0.38401 0.50573 0.39561 0.10607  0.11425  -0.08158 59  ARG A NE  
403  C CZ  . ARG A 54  ? 0.42462 0.57270 0.42107 0.15023  0.10520  -0.04872 59  ARG A CZ  
404  N NH1 . ARG A 54  ? 0.42914 0.59879 0.43506 0.13778  0.09733  -0.03974 59  ARG A NH1 
405  N NH2 . ARG A 54  ? 0.45505 0.58418 0.42597 0.17178  0.10221  -0.05070 59  ARG A NH2 
406  N N   A LEU A 55  ? 0.14790 0.17656 0.21208 0.04637  0.03269  -0.02914 60  LEU A N   
407  N N   B LEU A 55  ? 0.13619 0.19260 0.21312 0.04177  0.03962  -0.04037 60  LEU A N   
408  C CA  A LEU A 55  ? 0.14719 0.13336 0.20494 0.03887  0.03454  -0.00564 60  LEU A CA  
409  C CA  B LEU A 55  ? 0.11833 0.17149 0.20804 0.02867  0.04206  -0.03017 60  LEU A CA  
410  C C   A LEU A 55  ? 0.17109 0.16357 0.20464 0.05504  -0.00850 -0.00954 60  LEU A C   
411  C C   B LEU A 55  ? 0.11611 0.18476 0.20103 0.03758  0.00800  -0.04860 60  LEU A C   
412  O O   A LEU A 55  ? 0.20309 0.19649 0.21029 0.07674  -0.03688 0.02615  60  LEU A O   
413  O O   B LEU A 55  ? 0.09921 0.23235 0.18989 0.00752  0.02551  -0.02945 60  LEU A O   
414  C CB  A LEU A 55  ? 0.15838 0.11160 0.20744 0.02366  0.03373  0.00899  60  LEU A CB  
415  C CB  B LEU A 55  ? 0.13644 0.17284 0.22125 0.00320  0.02515  -0.02628 60  LEU A CB  
416  C CG  A LEU A 55  ? 0.14836 0.14266 0.22353 0.01720  0.03925  0.00514  60  LEU A CG  
417  C CG  B LEU A 55  ? 0.13826 0.19894 0.24100 -0.02195 0.02921  -0.00396 60  LEU A CG  
418  C CD1 A LEU A 55  ? 0.11598 0.11982 0.22356 0.01686  0.07736  0.03934  60  LEU A CD1 
419  C CD1 B LEU A 55  ? 0.17545 0.23856 0.26840 0.00193  0.03341  -0.02265 60  LEU A CD1 
420  C CD2 A LEU A 55  ? 0.14707 0.10412 0.23273 -0.00585 0.01856  -0.00034 60  LEU A CD2 
421  C CD2 B LEU A 55  ? 0.09749 0.21287 0.25274 -0.03065 0.02877  0.01875  60  LEU A CD2 
422  N N   A MET A 56  ? 0.17115 0.16695 0.20209 0.03830  0.03845  0.00817  61  MET A N   
423  N N   B MET A 56  ? 0.12263 0.14893 0.20436 0.03806  0.03070  -0.03620 61  MET A N   
424  C CA  A MET A 56  ? 0.18342 0.13834 0.21101 0.03502  0.04049  0.01644  61  MET A CA  
425  C CA  B MET A 56  ? 0.15246 0.08861 0.22027 0.03970  0.02285  -0.02290 61  MET A CA  
426  C C   A MET A 56  ? 0.12880 0.13573 0.18339 0.01428  0.02321  0.00559  61  MET A C   
427  C C   B MET A 56  ? 0.11941 0.09739 0.19180 0.01250  0.00959  -0.01917 61  MET A C   
428  O O   A MET A 56  ? 0.12579 0.14575 0.15264 -0.00336 0.01314  0.00335  61  MET A O   
429  O O   B MET A 56  ? 0.13412 0.11257 0.17578 0.01252  -0.00800 -0.02035 61  MET A O   
430  C CB  A MET A 56  ? 0.25012 0.17831 0.24048 0.04382  0.06410  0.01518  61  MET A CB  
431  C CB  B MET A 56  ? 0.20923 0.10246 0.25474 0.04603  0.02733  -0.04997 61  MET A CB  
432  C CG  A MET A 56  ? 0.32979 0.24029 0.27419 0.05229  0.06776  0.00877  61  MET A CG  
433  C CG  B MET A 56  ? 0.28010 0.13528 0.29452 0.04850  0.01742  -0.08389 61  MET A CG  
434  S SD  A MET A 56  ? 0.38302 0.28761 0.29537 0.07476  0.08230  0.03206  61  MET A SD  
435  S SD  B MET A 56  ? 0.29099 0.16987 0.35673 0.03069  0.00576  -0.06177 61  MET A SD  
436  C CE  A MET A 56  ? 0.39364 0.28285 0.29659 0.05947  0.07488  0.01183  61  MET A CE  
437  C CE  B MET A 56  ? 0.26032 0.16197 0.35454 0.03474  -0.00706 -0.10534 61  MET A CE  
438  N N   . LEU A 57  ? 0.10168 0.11400 0.17910 -0.00507 0.01857  -0.00925 62  LEU A N   
439  C CA  . LEU A 57  ? 0.11331 0.11803 0.14993 0.00134  0.05656  0.01261  62  LEU A CA  
440  C C   . LEU A 57  ? 0.13773 0.14450 0.13951 -0.02222 0.01713  -0.00786 62  LEU A C   
441  O O   . LEU A 57  ? 0.16244 0.31178 0.13798 -0.05749 0.02463  -0.02447 62  LEU A O   
442  C CB  . LEU A 57  ? 0.12772 0.16222 0.15923 -0.00019 0.03056  0.03926  62  LEU A CB  
443  C CG  . LEU A 57  ? 0.19685 0.21502 0.18322 -0.04091 -0.00774 0.04656  62  LEU A CG  
444  C CD1 . LEU A 57  ? 0.21516 0.23937 0.18418 -0.02692 -0.00544 0.05813  62  LEU A CD1 
445  C CD2 . LEU A 57  ? 0.23650 0.21893 0.20612 -0.04348 0.01330  0.05258  62  LEU A CD2 
446  N N   . TRP A 58  ? 0.09716 0.12004 0.12800 -0.01020 0.03450  0.01104  63  TRP A N   
447  C CA  . TRP A 58  ? 0.09880 0.10034 0.13203 -0.00703 0.02820  0.00254  63  TRP A CA  
448  C C   . TRP A 58  ? 0.10988 0.07662 0.14428 0.00017  0.03778  0.01519  63  TRP A C   
449  O O   . TRP A 58  ? 0.11625 0.09033 0.15041 -0.01352 0.00030  -0.01578 63  TRP A O   
450  C CB  . TRP A 58  ? 0.12696 0.10557 0.13883 0.02159  0.01968  0.01605  63  TRP A CB  
451  C CG  . TRP A 58  ? 0.10724 0.13939 0.16705 -0.00692 0.04770  0.01507  63  TRP A CG  
452  C CD1 . TRP A 58  ? 0.16466 0.10361 0.19316 0.01331  0.03820  0.01846  63  TRP A CD1 
453  C CD2 . TRP A 58  ? 0.14202 0.11410 0.16857 -0.02931 0.01508  0.00659  63  TRP A CD2 
454  N NE1 . TRP A 58  ? 0.16625 0.10526 0.19739 0.00787  0.01031  0.01030  63  TRP A NE1 
455  C CE2 . TRP A 58  ? 0.14951 0.09313 0.19199 -0.02713 -0.00814 -0.00078 63  TRP A CE2 
456  C CE3 . TRP A 58  ? 0.14174 0.12092 0.16373 -0.04028 0.01231  -0.00350 63  TRP A CE3 
457  C CZ2 . TRP A 58  ? 0.19390 0.12779 0.17189 -0.02639 -0.00326 0.02071  63  TRP A CZ2 
458  C CZ3 . TRP A 58  ? 0.17184 0.11737 0.17610 -0.02761 -0.00302 -0.00426 63  TRP A CZ3 
459  C CH2 . TRP A 58  ? 0.18106 0.12050 0.17934 -0.00495 0.00210  0.01695  63  TRP A CH2 
460  N N   . ASP A 59  ? 0.10798 0.07471 0.14001 0.00128  0.01282  0.00125  64  ASP A N   
461  C CA  . ASP A 59  ? 0.07472 0.07262 0.12324 -0.01050 0.02821  0.00363  64  ASP A CA  
462  C C   . ASP A 59  ? 0.09679 0.05952 0.11854 -0.00404 0.02932  0.00273  64  ASP A C   
463  O O   . ASP A 59  ? 0.12116 0.07017 0.14372 -0.03524 0.01667  -0.01428 64  ASP A O   
464  C CB  . ASP A 59  ? 0.13372 0.04903 0.12267 0.00600  0.01614  0.02874  64  ASP A CB  
465  C CG  . ASP A 59  ? 0.11477 0.06811 0.12281 -0.00824 0.01762  0.01300  64  ASP A CG  
466  O OD1 . ASP A 59  ? 0.13145 0.07662 0.12516 -0.00014 0.00879  -0.02262 64  ASP A OD1 
467  O OD2 . ASP A 59  ? 0.13860 0.10401 0.13806 0.03072  -0.00578 -0.01082 64  ASP A OD2 
468  N N   . THR A 60  ? 0.10544 0.07869 0.10574 -0.01266 0.03105  0.00795  65  THR A N   
469  C CA  . THR A 60  ? 0.11720 0.07895 0.09262 0.00285  0.03181  0.01413  65  THR A CA  
470  C C   . THR A 60  ? 0.08028 0.09065 0.10551 -0.01438 0.02165  0.01807  65  THR A C   
471  O O   . THR A 60  ? 0.11463 0.08757 0.11339 -0.03891 0.01327  0.02140  65  THR A O   
472  C CB  . THR A 60  ? 0.12012 0.10968 0.12050 -0.05487 -0.00379 0.00377  65  THR A CB  
473  O OG1 . THR A 60  ? 0.13187 0.10340 0.15672 -0.04050 0.01263  0.01581  65  THR A OG1 
474  C CG2 . THR A 60  ? 0.15258 0.12642 0.11589 -0.06332 -0.00105 0.01259  65  THR A CG2 
475  N N   . ALA A 61  ? 0.09430 0.06738 0.09313 -0.01965 0.01186  -0.00633 66  ALA A N   
476  C CA  . ALA A 61  ? 0.08398 0.09564 0.10925 -0.01663 0.00910  -0.03275 66  ALA A CA  
477  C C   . ALA A 61  ? 0.11488 0.10495 0.09235 -0.03467 -0.00344 -0.02209 66  ALA A C   
478  O O   . ALA A 61  ? 0.19074 0.12012 0.10386 0.01583  0.00635  0.00447  66  ALA A O   
479  C CB  . ALA A 61  ? 0.09337 0.12461 0.14535 -0.00416 0.01158  -0.01404 66  ALA A CB  
480  N N   . GLY A 62  ? 0.12481 0.08390 0.11235 -0.04920 0.00801  -0.02201 67  GLY A N   
481  C CA  . GLY A 62  ? 0.15097 0.12530 0.12605 -0.06228 0.03185  -0.03471 67  GLY A CA  
482  C C   . GLY A 62  ? 0.20034 0.31303 0.17638 -0.07053 0.05690  -0.02283 67  GLY A C   
483  O O   . GLY A 62  ? 0.24030 0.44716 0.16832 -0.05873 0.04486  -0.00095 67  GLY A O   
484  N N   . GLN A 63  ? 0.20620 0.38227 0.23132 -0.07199 0.10546  -0.03048 68  GLN A N   
485  C CA  . GLN A 63  ? 0.34807 0.47039 0.36699 -0.03577 0.10270  0.02500  68  GLN A CA  
486  C C   . GLN A 63  ? 0.36163 0.52759 0.39275 -0.00755 0.09689  0.05134  68  GLN A C   
487  O O   . GLN A 63  ? 0.41917 0.58560 0.40810 0.03533  0.08829  0.05960  68  GLN A O   
489  N N   . ILE A 69  ? 0.37403 0.28519 0.35404 0.06164  0.09507  0.04647  74  ILE A N   
490  C CA  . ILE A 69  ? 0.36490 0.23554 0.34641 0.00577  0.07905  0.03101  74  ILE A CA  
491  C C   . ILE A 69  ? 0.37771 0.23721 0.34896 -0.02033 0.07840  0.03479  74  ILE A C   
492  O O   . ILE A 69  ? 0.39158 0.27396 0.33037 -0.00198 0.08377  0.04421  74  ILE A O   
493  C CB  . ILE A 69  ? 0.33770 0.17718 0.33013 -0.04725 0.06924  0.00907  74  ILE A CB  
494  C CG1 . ILE A 69  ? 0.36701 0.23225 0.32880 -0.06117 0.04967  0.00712  74  ILE A CG1 
495  C CG2 . ILE A 69  ? 0.30790 0.18496 0.32359 -0.02086 0.07930  0.01252  74  ILE A CG2 
496  C CD1 . ILE A 69  ? 0.37308 0.22265 0.33877 -0.09420 0.03385  -0.01839 74  ILE A CD1 
497  N N   . THR A 70  ? 0.36553 0.24106 0.36754 -0.09639 0.06445  0.02726  75  THR A N   
498  C CA  . THR A 70  ? 0.37841 0.27110 0.36742 -0.07117 0.04094  -0.01219 75  THR A CA  
499  C C   . THR A 70  ? 0.36639 0.15540 0.31122 -0.09066 0.03706  -0.00741 75  THR A C   
500  O O   . THR A 70  ? 0.36118 0.15898 0.29142 -0.08609 0.01518  -0.04327 75  THR A O   
501  C CB  . THR A 70  ? 0.41849 0.35565 0.40581 -0.03227 0.03410  -0.04505 75  THR A CB  
502  O OG1 . THR A 70  ? 0.45374 0.46283 0.43683 0.01659  0.05019  -0.06530 75  THR A OG1 
503  C CG2 . THR A 70  ? 0.41126 0.38548 0.41530 -0.04724 0.04516  -0.05230 75  THR A CG2 
504  N N   . LYS A 71  ? 0.36252 0.20255 0.28160 -0.07381 0.03052  0.03693  76  LYS A N   
505  C CA  . LYS A 71  ? 0.36619 0.17651 0.25648 -0.08255 0.03078  0.05364  76  LYS A CA  
506  C C   . LYS A 71  ? 0.35025 0.16722 0.22675 -0.04813 0.00305  0.03843  76  LYS A C   
507  O O   . LYS A 71  ? 0.33275 0.16525 0.20487 -0.05966 0.00628  0.01182  76  LYS A O   
508  C CB  . LYS A 71  ? 0.41593 0.26436 0.28524 -0.05912 0.03995  0.03713  76  LYS A CB  
509  C CG  . LYS A 71  ? 0.46338 0.29734 0.31376 -0.06832 0.04037  0.05042  76  LYS A CG  
510  C CD  . LYS A 71  ? 0.51185 0.38142 0.34630 -0.03511 0.02046  0.02595  76  LYS A CD  
511  C CE  . LYS A 71  ? 0.54601 0.44613 0.36962 0.01840  0.00495  0.01940  76  LYS A CE  
512  N NZ  . LYS A 71  ? 0.57530 0.49270 0.39271 0.03985  -0.00713 0.01552  76  LYS A NZ  
513  N N   . ALA A 72  ? 0.33021 0.15046 0.22248 -0.06375 -0.03245 0.07280  77  ALA A N   
514  C CA  . ALA A 72  ? 0.30906 0.12081 0.22162 -0.06159 -0.01298 0.04455  77  ALA A CA  
515  C C   . ALA A 72  ? 0.25367 0.10501 0.20561 -0.05568 -0.00728 0.02705  77  ALA A C   
516  O O   . ALA A 72  ? 0.26301 0.13229 0.21363 -0.03819 -0.00579 0.01782  77  ALA A O   
517  C CB  . ALA A 72  ? 0.31249 0.19174 0.23090 -0.08210 -0.03836 0.00820  77  ALA A CB  
518  N N   . TYR A 73  ? 0.20928 0.10468 0.19612 -0.07142 0.01325  0.02792  78  TYR A N   
519  C CA  . TYR A 73  ? 0.20834 0.09582 0.17410 -0.03912 -0.00628 0.03054  78  TYR A CA  
520  C C   . TYR A 73  ? 0.20050 0.08519 0.16501 -0.04388 -0.01458 0.03446  78  TYR A C   
521  O O   . TYR A 73  ? 0.22156 0.12066 0.16140 -0.01926 -0.00634 0.01907  78  TYR A O   
522  C CB  . TYR A 73  ? 0.17285 0.11240 0.16607 -0.03732 0.03312  0.01066  78  TYR A CB  
523  C CG  . TYR A 73  ? 0.15823 0.07363 0.15641 -0.03160 0.02061  -0.00986 78  TYR A CG  
524  C CD1 . TYR A 73  ? 0.13790 0.09561 0.14517 -0.00945 0.00411  0.00499  78  TYR A CD1 
525  C CD2 . TYR A 73  ? 0.13055 0.09170 0.15763 -0.02260 0.02495  -0.00828 78  TYR A CD2 
526  C CE1 . TYR A 73  ? 0.10413 0.08607 0.16487 -0.01975 -0.00042 -0.01174 78  TYR A CE1 
527  C CE2 . TYR A 73  ? 0.13149 0.08959 0.15964 -0.01789 0.02400  -0.01572 78  TYR A CE2 
528  C CZ  . TYR A 73  ? 0.13733 0.06276 0.15578 -0.01994 -0.00251 -0.02227 78  TYR A CZ  
529  O OH  . TYR A 73  ? 0.13277 0.08745 0.17439 -0.02506 -0.00098 -0.00303 78  TYR A OH  
530  N N   . TYR A 74  ? 0.21175 0.10540 0.15766 -0.03098 -0.02949 0.02583  79  TYR A N   
531  C CA  . TYR A 74  ? 0.21039 0.12340 0.17530 -0.03619 -0.04122 0.01883  79  TYR A CA  
532  C C   . TYR A 74  ? 0.21671 0.11105 0.20613 -0.04068 -0.05678 0.01584  79  TYR A C   
533  O O   . TYR A 74  ? 0.23509 0.12533 0.22596 -0.03277 -0.03665 0.00864  79  TYR A O   
534  C CB  . TYR A 74  ? 0.21556 0.16566 0.17679 -0.01995 -0.01966 0.02680  79  TYR A CB  
535  C CG  . TYR A 74  ? 0.24543 0.11986 0.20078 -0.02383 -0.03112 0.01604  79  TYR A CG  
536  C CD1 . TYR A 74  ? 0.27003 0.12528 0.23061 -0.03303 -0.05268 0.02096  79  TYR A CD1 
537  C CD2 . TYR A 74  ? 0.28770 0.16761 0.22031 0.00613  -0.04688 -0.00296 79  TYR A CD2 
538  C CE1 . TYR A 74  ? 0.29060 0.17651 0.25397 0.01269  -0.05557 -0.00667 79  TYR A CE1 
539  C CE2 . TYR A 74  ? 0.31218 0.23050 0.24874 0.04509  -0.05813 -0.00939 79  TYR A CE2 
540  C CZ  . TYR A 74  ? 0.31495 0.20759 0.26306 0.04436  -0.05967 -0.01344 79  TYR A CZ  
541  O OH  . TYR A 74  ? 0.36319 0.26435 0.30287 0.09809  -0.04920 -0.03386 79  TYR A OH  
542  N N   . ARG A 75  ? 0.25355 0.11552 0.22761 -0.01694 -0.04869 0.02334  80  ARG A N   
543  C CA  . ARG A 75  ? 0.25148 0.12101 0.25494 -0.00086 -0.05050 0.03984  80  ARG A CA  
544  C C   . ARG A 75  ? 0.24693 0.11319 0.25588 -0.00587 -0.07463 0.04507  80  ARG A C   
545  O O   . ARG A 75  ? 0.27907 0.11990 0.24722 0.02588  -0.08291 0.04926  80  ARG A O   
546  C CB  . ARG A 75  ? 0.29681 0.12672 0.29416 -0.04948 -0.04702 0.05163  80  ARG A CB  
547  C CG  . ARG A 75  ? 0.38618 0.14721 0.32227 0.01492  -0.05062 0.09065  80  ARG A CG  
548  C CD  . ARG A 75  ? 0.44568 0.18326 0.33593 0.00846  -0.01528 0.10662  80  ARG A CD  
549  N NE  . ARG A 75  ? 0.46386 0.22080 0.34939 -0.02720 0.01363  0.11790  80  ARG A NE  
550  C CZ  . ARG A 75  ? 0.49385 0.24727 0.34397 -0.03255 0.01404  0.10240  80  ARG A CZ  
551  N NH1 . ARG A 75  ? 0.49232 0.22922 0.33604 -0.07760 0.02917  0.10112  80  ARG A NH1 
552  N NH2 . ARG A 75  ? 0.51183 0.27432 0.35029 -0.02956 -0.01027 0.05979  80  ARG A NH2 
553  N N   . GLY A 76  ? 0.23381 0.11269 0.25651 0.02763  -0.05686 0.05525  81  GLY A N   
554  C CA  . GLY A 76  ? 0.26927 0.12127 0.25716 0.02232  -0.05837 0.04355  81  GLY A CA  
555  C C   . GLY A 76  ? 0.24387 0.10317 0.24146 0.01504  -0.02846 0.03448  81  GLY A C   
556  O O   . GLY A 76  ? 0.23658 0.13522 0.24638 0.01133  -0.04589 0.02001  81  GLY A O   
557  N N   . ALA A 77  ? 0.21741 0.08999 0.22152 -0.00945 -0.02983 0.04728  82  ALA A N   
558  C CA  . ALA A 77  ? 0.19079 0.07423 0.20637 0.01453  -0.01458 0.02417  82  ALA A CA  
559  C C   . ALA A 77  ? 0.17550 0.11917 0.20730 0.00456  -0.02271 -0.00081 82  ALA A C   
560  O O   . ALA A 77  ? 0.18913 0.16174 0.23184 -0.03024 -0.04130 0.02739  82  ALA A O   
561  C CB  . ALA A 77  ? 0.18109 0.10779 0.19371 0.02832  0.00883  0.02714  82  ALA A CB  
562  N N   . GLN A 78  ? 0.15430 0.11573 0.20602 0.01484  -0.02751 0.00594  83  GLN A N   
563  C CA  . GLN A 78  ? 0.16676 0.07953 0.21067 0.02328  -0.00488 0.00760  83  GLN A CA  
564  C C   . GLN A 78  ? 0.13634 0.06782 0.21408 0.00650  -0.01499 0.00702  83  GLN A C   
565  O O   . GLN A 78  ? 0.13182 0.13178 0.24316 0.00984  -0.02082 -0.01473 83  GLN A O   
566  C CB  . GLN A 78  ? 0.20261 0.10572 0.24345 0.04596  -0.01230 -0.02077 83  GLN A CB  
567  C CG  . GLN A 78  ? 0.22754 0.10412 0.24573 0.04897  -0.03244 0.00184  83  GLN A CG  
568  C CD  . GLN A 78  ? 0.20779 0.10072 0.26909 0.02950  -0.03224 -0.00248 83  GLN A CD  
569  O OE1 . GLN A 78  ? 0.20482 0.14467 0.26732 0.06808  -0.03427 0.00969  83  GLN A OE1 
570  N NE2 . GLN A 78  ? 0.22052 0.18762 0.29530 0.06979  -0.02435 -0.04409 83  GLN A NE2 
571  N N   . ALA A 79  ? 0.11990 0.08934 0.19843 0.05193  -0.00667 0.00774  84  ALA A N   
572  C CA  . ALA A 79  ? 0.11755 0.08098 0.19690 0.04321  -0.00722 0.00137  84  ALA A CA  
573  C C   . ALA A 79  ? 0.10043 0.07454 0.16372 0.03530  -0.01467 0.00850  84  ALA A C   
574  O O   . ALA A 79  ? 0.12085 0.09250 0.16961 -0.00396 -0.02871 -0.02720 84  ALA A O   
575  C CB  . ALA A 79  ? 0.12715 0.11135 0.18456 0.02495  0.02865  0.00158  84  ALA A CB  
576  N N   . CYS A 80  ? 0.10295 0.05801 0.17132 0.02875  -0.01093 0.00544  85  CYS A N   
577  C CA  . CYS A 80  ? 0.10096 0.06365 0.16239 0.02970  0.00312  0.02413  85  CYS A CA  
578  C C   . CYS A 80  ? 0.07296 0.06698 0.13510 0.01491  0.00469  -0.01328 85  CYS A C   
579  O O   . CYS A 80  ? 0.09827 0.08909 0.15411 -0.02513 -0.03696 0.00244  85  CYS A O   
580  C CB  . CYS A 80  ? 0.14107 0.12917 0.16243 0.03728  0.04676  0.06989  85  CYS A CB  
581  S SG  . CYS A 80  ? 0.17372 0.17021 0.17833 0.03716  0.04106  0.03028  85  CYS A SG  
582  N N   . VAL A 81  ? 0.08784 0.08750 0.12739 0.01446  0.01047  0.01160  86  VAL A N   
583  C CA  . VAL A 81  ? 0.09318 0.05897 0.12677 0.00633  -0.00209 0.00825  86  VAL A CA  
584  C C   . VAL A 81  ? 0.06778 0.08753 0.11755 0.00929  0.02738  0.00413  86  VAL A C   
585  O O   . VAL A 81  ? 0.06413 0.09280 0.14885 -0.01685 0.00504  -0.00894 86  VAL A O   
586  C CB  . VAL A 81  ? 0.11415 0.09388 0.14400 0.01094  0.01271  0.00997  86  VAL A CB  
587  C CG1 . VAL A 81  ? 0.12847 0.08482 0.17369 0.00292  0.00468  0.01694  86  VAL A CG1 
588  C CG2 . VAL A 81  ? 0.10947 0.15435 0.12091 -0.00663 0.02450  0.01296  86  VAL A CG2 
589  N N   . LEU A 82  ? 0.09257 0.05858 0.11909 0.01019  0.01451  0.00665  87  LEU A N   
590  C CA  . LEU A 82  ? 0.09902 0.08512 0.10998 0.00649  0.00936  -0.00899 87  LEU A CA  
591  C C   . LEU A 82  ? 0.06890 0.04517 0.10393 0.02373  -0.00840 0.01444  87  LEU A C   
592  O O   . LEU A 82  ? 0.10114 0.07125 0.15497 -0.03554 0.00049  0.03036  87  LEU A O   
593  C CB  . LEU A 82  ? 0.13490 0.09988 0.13159 -0.00778 -0.01625 0.00633  87  LEU A CB  
594  C CG  . LEU A 82  ? 0.15245 0.14962 0.12941 -0.01819 -0.02814 0.02145  87  LEU A CG  
595  C CD1 . LEU A 82  ? 0.17172 0.21576 0.10939 -0.01651 -0.02051 -0.00346 87  LEU A CD1 
596  C CD2 . LEU A 82  ? 0.16962 0.16518 0.17475 -0.04230 -0.03270 0.03893  87  LEU A CD2 
597  N N   . VAL A 83  ? 0.06560 0.06115 0.08817 0.00507  0.00102  0.00327  88  VAL A N   
598  C CA  . VAL A 83  ? 0.08171 0.08893 0.09813 -0.01214 -0.00654 -0.01295 88  VAL A CA  
599  C C   . VAL A 83  ? 0.07783 0.05393 0.09249 -0.00882 -0.01684 -0.00558 88  VAL A C   
600  O O   . VAL A 83  ? 0.07853 0.08859 0.10342 -0.01379 0.01438  0.01393  88  VAL A O   
601  C CB  . VAL A 83  ? 0.13157 0.08286 0.08694 -0.02069 -0.01123 -0.01631 88  VAL A CB  
602  C CG1 . VAL A 83  ? 0.12300 0.07928 0.10803 0.00152  -0.00109 0.01273  88  VAL A CG1 
603  C CG2 . VAL A 83  ? 0.12348 0.10457 0.09174 -0.00553 0.00628  -0.02253 88  VAL A CG2 
604  N N   . PHE A 84  ? 0.07827 0.06796 0.09534 -0.00599 -0.00688 -0.00640 89  PHE A N   
605  C CA  . PHE A 84  ? 0.07841 0.08932 0.07622 0.03403  -0.00052 -0.00264 89  PHE A CA  
606  C C   . PHE A 84  ? 0.07058 0.03951 0.08151 0.00419  0.00346  -0.00369 89  PHE A C   
607  O O   . PHE A 84  ? 0.08904 0.09068 0.09021 -0.01090 0.01627  0.01244  89  PHE A O   
608  C CB  . PHE A 84  ? 0.10416 0.07303 0.08410 -0.02214 -0.00591 -0.02691 89  PHE A CB  
609  C CG  . PHE A 84  ? 0.12123 0.07795 0.08265 -0.01996 0.02415  -0.01201 89  PHE A CG  
610  C CD1 . PHE A 84  ? 0.09996 0.11837 0.09235 -0.04401 0.03033  -0.02543 89  PHE A CD1 
611  C CD2 . PHE A 84  ? 0.12400 0.06304 0.07883 -0.04632 0.01402  -0.00669 89  PHE A CD2 
612  C CE1 . PHE A 84  ? 0.12437 0.10570 0.09620 0.00310  0.02330  -0.00259 89  PHE A CE1 
613  C CE2 . PHE A 84  ? 0.11681 0.10616 0.08563 0.01117  0.01598  -0.01421 89  PHE A CE2 
614  C CZ  . PHE A 84  ? 0.13077 0.10882 0.08030 0.00542  0.02017  -0.00804 89  PHE A CZ  
615  N N   . SER A 85  ? 0.08928 0.05194 0.09664 0.02633  -0.02396 -0.00115 90  SER A N   
616  C CA  . SER A 85  ? 0.10701 0.04515 0.08900 -0.00404 -0.01028 -0.02164 90  SER A CA  
617  C C   . SER A 85  ? 0.09118 0.08429 0.08624 0.00587  -0.01087 -0.01831 90  SER A C   
618  O O   . SER A 85  ? 0.12222 0.09205 0.09308 0.01816  -0.00480 -0.02031 90  SER A O   
619  C CB  . SER A 85  ? 0.09973 0.11417 0.10173 -0.00677 -0.04945 0.00265  90  SER A CB  
620  O OG  . SER A 85  ? 0.13296 0.10661 0.11207 0.00768  -0.02607 -0.01124 90  SER A OG  
621  N N   . THR A 86  ? 0.12454 0.04899 0.10489 -0.01620 -0.00319 0.00357  91  THR A N   
622  C CA  . THR A 86  ? 0.11589 0.05926 0.11665 -0.00997 0.01863  0.00225  91  THR A CA  
623  C C   . THR A 86  ? 0.12433 0.08820 0.13243 0.01776  0.01542  -0.02371 91  THR A C   
624  O O   . THR A 86  ? 0.13957 0.09456 0.14472 0.01852  0.02917  -0.03636 91  THR A O   
625  C CB  . THR A 86  ? 0.15772 0.06938 0.14813 -0.01295 -0.00214 0.01004  91  THR A CB  
626  O OG1 . THR A 86  ? 0.10203 0.09589 0.14370 -0.01031 -0.00251 -0.00409 91  THR A OG1 
627  C CG2 . THR A 86  ? 0.18984 0.05464 0.18794 -0.01675 0.00392  0.01682  91  THR A CG2 
628  N N   . THR A 87  ? 0.10568 0.10139 0.12755 0.02540  0.00611  0.00745  92  THR A N   
629  C CA  . THR A 87  ? 0.11667 0.11883 0.13121 0.02064  -0.00072 0.02168  92  THR A CA  
630  C C   . THR A 87  ? 0.14534 0.15553 0.14983 0.01460  0.00175  0.02280  92  THR A C   
631  O O   . THR A 87  ? 0.15368 0.22515 0.19961 0.02706  0.01488  0.03389  92  THR A O   
632  C CB  . THR A 87  ? 0.15029 0.13076 0.14734 -0.00655 0.00013  0.02705  92  THR A CB  
633  O OG1 . THR A 87  ? 0.15844 0.17508 0.18316 0.02297  -0.03293 -0.00464 92  THR A OG1 
634  C CG2 . THR A 87  ? 0.19392 0.19174 0.14379 0.03457  -0.01075 0.03273  92  THR A CG2 
635  N N   . ASP A 88  ? 0.15273 0.11772 0.10472 0.02436  -0.00554 -0.00072 93  ASP A N   
636  C CA  . ASP A 88  ? 0.14741 0.12336 0.08939 -0.00252 0.01647  -0.03264 93  ASP A CA  
637  C C   . ASP A 88  ? 0.11798 0.12643 0.09447 -0.00715 0.00257  -0.06353 93  ASP A C   
638  O O   . ASP A 88  ? 0.10118 0.10744 0.12806 0.01714  0.00431  -0.01336 93  ASP A O   
639  C CB  . ASP A 88  ? 0.13750 0.11007 0.12042 0.00339  0.01776  -0.02013 93  ASP A CB  
640  C CG  . ASP A 88  ? 0.15126 0.18875 0.13251 -0.02672 -0.00062 -0.04969 93  ASP A CG  
641  O OD1 . ASP A 88  ? 0.20424 0.20051 0.10060 0.00491  -0.00050 -0.03173 93  ASP A OD1 
642  O OD2 . ASP A 88  ? 0.22797 0.15869 0.16324 -0.03379 -0.00683 -0.03548 93  ASP A OD2 
643  N N   . ARG A 89  ? 0.11978 0.12512 0.10567 0.01406  0.00806  -0.05118 94  ARG A N   
644  C CA  . ARG A 89  ? 0.14498 0.13304 0.09321 0.02925  0.00632  -0.05416 94  ARG A CA  
645  C C   . ARG A 89  ? 0.12087 0.12576 0.10117 0.00722  0.00766  -0.02085 94  ARG A C   
646  O O   . ARG A 89  ? 0.10186 0.12535 0.09396 0.02635  0.00011  -0.01246 94  ARG A O   
647  C CB  . ARG A 89  ? 0.13001 0.13270 0.09947 0.00770  0.01692  -0.05530 94  ARG A CB  
648  C CG  . ARG A 89  ? 0.15020 0.17046 0.12571 -0.00252 -0.02084 -0.03521 94  ARG A CG  
649  C CD  . ARG A 89  ? 0.16059 0.20192 0.14050 -0.02754 -0.02144 -0.01222 94  ARG A CD  
650  N NE  . ARG A 89  ? 0.14294 0.17596 0.14343 -0.04289 -0.00493 -0.03248 94  ARG A NE  
651  C CZ  . ARG A 89  ? 0.14231 0.19670 0.13150 -0.01005 -0.00580 -0.04949 94  ARG A CZ  
652  N NH1 . ARG A 89  ? 0.16722 0.19404 0.14486 -0.01588 0.01226  -0.03194 94  ARG A NH1 
653  N NH2 . ARG A 89  ? 0.15889 0.24815 0.12644 0.02299  -0.03936 -0.05455 94  ARG A NH2 
654  N N   . GLU A 90  ? 0.13043 0.13644 0.09969 0.02427  0.03298  -0.02235 95  GLU A N   
655  C CA  . GLU A 90  ? 0.10465 0.14380 0.10819 -0.01290 0.03011  -0.05074 95  GLU A CA  
656  C C   . GLU A 90  ? 0.10665 0.15223 0.09559 0.01099  0.03233  -0.04332 95  GLU A C   
657  O O   . GLU A 90  ? 0.09770 0.12696 0.09734 -0.00137 0.01857  -0.01641 95  GLU A O   
658  C CB  . GLU A 90  ? 0.09673 0.20915 0.17019 -0.01516 0.04666  -0.03013 95  GLU A CB  
659  C CG  . GLU A 90  ? 0.15855 0.29279 0.18543 0.05569  0.05337  -0.03261 95  GLU A CG  
660  N N   . SER A 91  ? 0.10334 0.11251 0.07389 -0.02029 0.03834  -0.03314 96  SER A N   
661  C CA  . SER A 91  ? 0.09153 0.11320 0.06601 -0.01371 0.02047  -0.02286 96  SER A CA  
662  C C   . SER A 91  ? 0.07562 0.10919 0.08821 -0.02496 0.00805  -0.01756 96  SER A C   
663  O O   . SER A 91  ? 0.09141 0.10978 0.08932 -0.01974 0.00726  -0.00514 96  SER A O   
664  C CB  . SER A 91  ? 0.11528 0.09667 0.06532 -0.01215 0.01725  0.01643  96  SER A CB  
665  O OG  . SER A 91  ? 0.08458 0.11737 0.06979 0.00357  0.01946  -0.01032 96  SER A OG  
666  N N   . PHE A 92  ? 0.08511 0.08214 0.08250 -0.02411 0.00525  -0.03177 97  PHE A N   
667  C CA  . PHE A 92  ? 0.11069 0.08609 0.08412 -0.03800 0.00801  -0.01947 97  PHE A CA  
668  C C   . PHE A 92  ? 0.10970 0.09200 0.09294 0.00008  0.01244  -0.02342 97  PHE A C   
669  O O   . PHE A 92  ? 0.11859 0.09193 0.09423 -0.01162 0.02033  -0.01300 97  PHE A O   
670  C CB  . PHE A 92  ? 0.09264 0.09335 0.10116 -0.03719 -0.00552 -0.01638 97  PHE A CB  
671  C CG  . PHE A 92  ? 0.10491 0.09745 0.10191 -0.02339 -0.02159 -0.02048 97  PHE A CG  
672  C CD1 . PHE A 92  ? 0.08025 0.13617 0.11979 -0.01357 -0.02229 0.00275  97  PHE A CD1 
673  C CD2 . PHE A 92  ? 0.13055 0.11937 0.12035 -0.02100 -0.02953 -0.04405 97  PHE A CD2 
674  C CE1 . PHE A 92  ? 0.11104 0.13686 0.10025 0.01341  -0.00993 -0.00089 97  PHE A CE1 
675  C CE2 . PHE A 92  ? 0.13564 0.11270 0.12851 -0.00331 -0.00537 -0.04511 97  PHE A CE2 
676  C CZ  . PHE A 92  ? 0.13533 0.11529 0.12715 0.01866  -0.00361 -0.00737 97  PHE A CZ  
677  N N   . GLU A 93  ? 0.11784 0.10038 0.07534 -0.02274 0.02206  -0.02242 98  GLU A N   
678  C CA  . GLU A 93  ? 0.13751 0.09969 0.08504 -0.01379 0.03076  -0.01194 98  GLU A CA  
679  C C   . GLU A 93  ? 0.11709 0.09167 0.09462 -0.02115 0.01734  -0.02070 98  GLU A C   
680  O O   . GLU A 93  ? 0.17634 0.12832 0.09549 0.00472  -0.02002 0.00017  98  GLU A O   
681  C CB  . GLU A 93  ? 0.12978 0.16462 0.12058 0.00457  0.03657  -0.04116 98  GLU A CB  
682  C CG  . GLU A 93  ? 0.15795 0.13657 0.13941 0.01509  0.00160  -0.07249 98  GLU A CG  
683  C CD  . GLU A 93  ? 0.20909 0.15313 0.14731 -0.00783 -0.01000 -0.02975 98  GLU A CD  
684  O OE1 . GLU A 93  ? 0.28270 0.17248 0.15596 -0.00673 -0.05234 -0.02227 98  GLU A OE1 
685  O OE2 . GLU A 93  ? 0.25670 0.17899 0.14359 -0.01962 0.00140  -0.03283 98  GLU A OE2 
686  N N   . ALA A 94  ? 0.09993 0.08746 0.09635 -0.00877 0.00297  -0.01987 99  ALA A N   
687  C CA  . ALA A 94  ? 0.08771 0.11547 0.10397 -0.02372 0.02145  -0.02116 99  ALA A CA  
688  C C   . ALA A 94  ? 0.09126 0.10873 0.09164 -0.02461 0.02347  -0.02654 99  ALA A C   
689  O O   . ALA A 94  ? 0.12303 0.10107 0.12492 -0.01945 0.00784  -0.01328 99  ALA A O   
690  C CB  . ALA A 94  ? 0.12704 0.11734 0.11605 -0.05317 0.01188  -0.00557 99  ALA A CB  
691  N N   . VAL A 95  ? 0.07593 0.11326 0.08480 -0.00715 0.00406  -0.00396 100 VAL A N   
692  C CA  . VAL A 95  ? 0.07975 0.11448 0.09179 -0.00459 0.01610  0.00164  100 VAL A CA  
693  C C   . VAL A 95  ? 0.12886 0.10477 0.07853 -0.01482 0.00875  -0.00990 100 VAL A C   
694  O O   . VAL A 95  ? 0.13705 0.10566 0.10959 -0.00183 -0.00715 -0.00081 100 VAL A O   
695  C CB  . VAL A 95  ? 0.06311 0.11905 0.11453 -0.01396 0.01054  -0.00218 100 VAL A CB  
696  C CG1 . VAL A 95  ? 0.09886 0.11301 0.13391 -0.01972 0.01180  0.00865  100 VAL A CG1 
697  C CG2 . VAL A 95  ? 0.11624 0.13695 0.09946 0.03269  0.00315  -0.01070 100 VAL A CG2 
698  N N   . SER A 96  ? 0.11529 0.12286 0.07703 -0.01866 -0.01252 -0.00113 101 SER A N   
699  C CA  . SER A 96  ? 0.16090 0.09404 0.09556 -0.03552 -0.03280 -0.01281 101 SER A CA  
700  C C   . SER A 96  ? 0.14667 0.10968 0.10043 -0.00718 -0.01017 -0.01373 101 SER A C   
701  O O   . SER A 96  ? 0.16674 0.10681 0.12357 -0.00768 -0.00810 -0.00053 101 SER A O   
702  C CB  . SER A 96  ? 0.22795 0.13634 0.12718 -0.02109 -0.08090 -0.02346 101 SER A CB  
703  O OG  . SER A 96  ? 0.26176 0.17015 0.12437 -0.00623 -0.03611 -0.04218 101 SER A OG  
704  N N   A SER A 97  ? 0.12316 0.11392 0.11099 -0.03475 0.02397  -0.01944 102 SER A N   
705  N N   B SER A 97  ? 0.11648 0.09964 0.10716 -0.05267 0.02128  -0.02464 102 SER A N   
706  C CA  A SER A 97  ? 0.14674 0.14050 0.13801 0.00851  0.02811  0.00348  102 SER A CA  
707  C CA  B SER A 97  ? 0.13499 0.11232 0.13248 -0.02468 0.02350  -0.00688 102 SER A CA  
708  C C   A SER A 97  ? 0.15407 0.12185 0.11471 -0.00478 0.03571  0.00983  102 SER A C   
709  C C   B SER A 97  ? 0.14708 0.09566 0.11239 -0.03123 0.02935  -0.00549 102 SER A C   
710  O O   A SER A 97  ? 0.18955 0.13076 0.11381 0.00933  0.02370  0.03374  102 SER A O   
711  O O   B SER A 97  ? 0.17950 0.08619 0.11014 -0.03793 0.00130  -0.01214 102 SER A O   
712  C CB  A SER A 97  ? 0.15876 0.20737 0.18005 0.02827  0.04957  0.00350  102 SER A CB  
713  C CB  B SER A 97  ? 0.13133 0.14052 0.16856 -0.04458 0.04440  -0.01555 102 SER A CB  
714  O OG  A SER A 97  ? 0.22870 0.27317 0.21462 0.05408  0.04547  0.01315  102 SER A OG  
715  O OG  B SER A 97  ? 0.17187 0.13533 0.20025 -0.08060 0.04925  -0.01132 102 SER A OG  
716  N N   . TRP A 98  ? 0.12551 0.10574 0.09590 -0.01849 0.00793  -0.00109 103 TRP A N   
717  C CA  . TRP A 98  ? 0.13528 0.07251 0.09284 -0.00606 -0.00219 -0.00670 103 TRP A CA  
718  C C   . TRP A 98  ? 0.15237 0.08559 0.11379 0.01482  -0.00324 -0.01236 103 TRP A C   
719  O O   . TRP A 98  ? 0.17582 0.09178 0.14071 0.01711  -0.01848 -0.02162 103 TRP A O   
720  C CB  . TRP A 98  ? 0.14106 0.11009 0.08906 -0.00499 -0.03327 0.02677  103 TRP A CB  
721  C CG  . TRP A 98  ? 0.12288 0.11548 0.09049 -0.00780 -0.01597 0.01011  103 TRP A CG  
722  C CD1 . TRP A 98  ? 0.11655 0.14870 0.08221 -0.00981 0.02217  -0.00056 103 TRP A CD1 
723  C CD2 . TRP A 98  ? 0.12229 0.12229 0.09168 -0.01710 0.01087  -0.01783 103 TRP A CD2 
724  N NE1 . TRP A 98  ? 0.12686 0.12539 0.10948 -0.02226 0.01689  -0.00819 103 TRP A NE1 
725  C CE2 . TRP A 98  ? 0.11916 0.14187 0.10122 -0.01210 0.00477  -0.00667 103 TRP A CE2 
726  C CE3 . TRP A 98  ? 0.15740 0.12278 0.12214 -0.03617 -0.00792 0.01227  103 TRP A CE3 
727  C CZ2 . TRP A 98  ? 0.13113 0.13966 0.14264 -0.02366 -0.01251 -0.02752 103 TRP A CZ2 
728  C CZ3 . TRP A 98  ? 0.17766 0.14941 0.15328 -0.04970 -0.01885 0.00424  103 TRP A CZ3 
729  C CH2 . TRP A 98  ? 0.16914 0.15768 0.16421 -0.04528 -0.02229 -0.00421 103 TRP A CH2 
730  N N   . ARG A 99  ? 0.12653 0.13739 0.12073 0.00177  -0.01154 0.00023  104 ARG A N   
731  C CA  A ARG A 99  ? 0.12853 0.14884 0.14228 0.00604  -0.02790 0.01097  104 ARG A CA  
732  C CA  B ARG A 99  ? 0.13089 0.14880 0.14954 0.01077  -0.03387 0.01275  104 ARG A CA  
733  C C   . ARG A 99  ? 0.15962 0.16540 0.15172 0.02620  -0.02491 0.00373  104 ARG A C   
734  O O   . ARG A 99  ? 0.19424 0.13675 0.16908 0.04610  -0.02058 -0.00517 104 ARG A O   
735  C CB  A ARG A 99  ? 0.10624 0.16957 0.17378 -0.01565 -0.03773 -0.00025 104 ARG A CB  
736  C CB  B ARG A 99  ? 0.11513 0.16944 0.19510 0.00065  -0.05473 0.00453  104 ARG A CB  
737  C CG  A ARG A 99  ? 0.16804 0.24026 0.21584 0.03723  -0.02475 -0.02144 104 ARG A CG  
738  C CG  B ARG A 99  ? 0.17649 0.24227 0.25295 0.05408  -0.04825 -0.01252 104 ARG A CG  
739  C CD  A ARG A 99  ? 0.18530 0.27411 0.22308 0.05272  0.00012  -0.00212 104 ARG A CD  
740  C CD  B ARG A 99  ? 0.21422 0.28960 0.29214 0.08322  -0.04472 0.00978  104 ARG A CD  
741  N NE  A ARG A 99  ? 0.18524 0.24343 0.21694 0.04177  -0.00740 -0.02369 104 ARG A NE  
742  N NE  B ARG A 99  ? 0.21408 0.30197 0.31935 0.08033  -0.03383 0.00707  104 ARG A NE  
743  C CZ  A ARG A 99  ? 0.17469 0.29158 0.21298 0.08256  0.00412  0.00841  104 ARG A CZ  
744  C CZ  B ARG A 99  ? 0.20618 0.33073 0.32277 0.08980  -0.04349 0.00788  104 ARG A CZ  
745  N NH1 A ARG A 99  ? 0.20031 0.33299 0.20871 0.10573  0.04018  0.02493  104 ARG A NH1 
746  N NH1 B ARG A 99  ? 0.21529 0.29457 0.32729 0.06646  -0.02485 0.02094  104 ARG A NH1 
747  N NH2 A ARG A 99  ? 0.17662 0.28057 0.22554 0.09313  0.00916  -0.01039 104 ARG A NH2 
748  N NH2 B ARG A 99  ? 0.21676 0.36230 0.33726 0.06974  -0.02470 -0.00422 104 ARG A NH2 
749  N N   . GLU A 100 ? 0.17526 0.13765 0.13434 0.02198  -0.02238 0.01985  105 GLU A N   
750  C CA  . GLU A 100 ? 0.21517 0.15146 0.13292 0.03925  -0.00269 0.03789  105 GLU A CA  
751  C C   . GLU A 100 ? 0.22018 0.15389 0.12276 0.01138  -0.02435 0.03302  105 GLU A C   
752  O O   . GLU A 100 ? 0.25804 0.18444 0.15727 0.05786  -0.03243 0.02082  105 GLU A O   
753  C CB  . GLU A 100 ? 0.27863 0.13825 0.14819 0.00450  -0.01552 0.01281  105 GLU A CB  
754  C CG  . GLU A 100 ? 0.32873 0.18924 0.17883 0.01039  -0.06911 0.01292  105 GLU A CG  
755  C CD  . GLU A 100 ? 0.39630 0.24624 0.23739 0.02928  -0.09547 0.02953  105 GLU A CD  
756  O OE1 . GLU A 100 ? 0.42213 0.29670 0.26935 0.02212  -0.13399 0.01263  105 GLU A OE1 
757  O OE2 . GLU A 100 ? 0.39979 0.24389 0.25608 0.02146  -0.09389 0.00502  105 GLU A OE2 
758  N N   . LYS A 101 ? 0.24247 0.14737 0.11958 0.01321  0.01064  0.00389  106 LYS A N   
759  C CA  . LYS A 101 ? 0.22252 0.12513 0.14320 -0.00451 -0.00733 0.02077  106 LYS A CA  
760  C C   . LYS A 101 ? 0.22755 0.14333 0.14418 0.01448  0.01181  0.04540  106 LYS A C   
761  O O   . LYS A 101 ? 0.28248 0.13917 0.16543 0.02466  0.02142  0.04602  106 LYS A O   
762  C CB  . LYS A 101 ? 0.22109 0.16500 0.16323 0.00215  -0.00736 0.02071  106 LYS A CB  
763  C CG  . LYS A 101 ? 0.24758 0.22736 0.22148 0.02416  0.00681  -0.00048 106 LYS A CG  
764  C CD  . LYS A 101 ? 0.25048 0.32024 0.26018 0.03057  0.01638  -0.00586 106 LYS A CD  
765  C CE  . LYS A 101 ? 0.27137 0.42283 0.28681 0.07889  -0.01188 -0.01295 106 LYS A CE  
766  N NZ  . LYS A 101 ? 0.27320 0.46651 0.30123 0.08124  -0.04641 -0.04051 106 LYS A NZ  
767  N N   . VAL A 102 ? 0.18654 0.13261 0.11741 -0.00053 -0.00855 0.01532  107 VAL A N   
768  C CA  . VAL A 102 ? 0.16389 0.10978 0.13829 0.01173  0.00804  0.02412  107 VAL A CA  
769  C C   . VAL A 102 ? 0.20408 0.13264 0.14848 0.02650  -0.00702 0.02206  107 VAL A C   
770  O O   . VAL A 102 ? 0.26419 0.13434 0.17128 0.06361  0.00477  0.02685  107 VAL A O   
771  C CB  . VAL A 102 ? 0.20273 0.11429 0.13574 0.02580  0.00543  0.01179  107 VAL A CB  
772  C CG1 . VAL A 102 ? 0.23661 0.14997 0.17437 0.04901  0.04371  -0.00242 107 VAL A CG1 
773  C CG2 . VAL A 102 ? 0.22122 0.15209 0.12211 0.02853  -0.02791 0.00078  107 VAL A CG2 
774  N N   . VAL A 103 ? 0.21582 0.14169 0.15479 0.01773  -0.02525 0.02329  108 VAL A N   
775  C CA  . VAL A 103 ? 0.24285 0.15339 0.18370 0.03232  -0.05528 0.03479  108 VAL A CA  
776  C C   . VAL A 103 ? 0.27091 0.16417 0.18664 0.01917  -0.04862 0.04340  108 VAL A C   
777  O O   . VAL A 103 ? 0.26983 0.20079 0.20254 0.04801  -0.06838 0.03124  108 VAL A O   
778  C CB  . VAL A 103 ? 0.25585 0.18274 0.19613 0.05115  -0.07548 0.02618  108 VAL A CB  
779  C CG1 . VAL A 103 ? 0.28437 0.22578 0.20561 0.05498  -0.09994 0.01611  108 VAL A CG1 
780  C CG2 . VAL A 103 ? 0.24857 0.21580 0.20316 0.07373  -0.04539 0.04608  108 VAL A CG2 
781  N N   . ALA A 104 ? 0.30199 0.15420 0.17386 0.02423  -0.03276 0.04569  109 ALA A N   
782  C CA  . ALA A 104 ? 0.34014 0.16703 0.17823 0.02086  -0.01132 0.07100  109 ALA A CA  
783  C C   . ALA A 104 ? 0.34877 0.17306 0.18665 0.00659  -0.01243 0.07000  109 ALA A C   
784  O O   . ALA A 104 ? 0.39228 0.20006 0.20719 0.02741  -0.02569 0.07159  109 ALA A O   
785  C CB  . ALA A 104 ? 0.32457 0.18789 0.17694 -0.01398 0.02627  0.07211  109 ALA A CB  
786  N N   . GLU A 105 ? 0.32062 0.15390 0.18891 -0.02518 -0.00481 0.04523  110 GLU A N   
787  C CA  . GLU A 105 ? 0.34891 0.15179 0.21308 -0.03765 -0.03638 0.03539  110 GLU A CA  
788  C C   . GLU A 105 ? 0.37256 0.13912 0.23852 0.01232  -0.06542 0.03093  110 GLU A C   
789  O O   . GLU A 105 ? 0.42133 0.11561 0.26840 0.02090  -0.03607 0.03001  110 GLU A O   
790  C CB  . GLU A 105 ? 0.35411 0.18640 0.24288 -0.06733 -0.03070 0.03888  110 GLU A CB  
791  C CG  . GLU A 105 ? 0.40208 0.19939 0.27197 -0.07053 -0.01657 0.06349  110 GLU A CG  
792  C CD  . GLU A 105 ? 0.44407 0.22843 0.31068 -0.04601 -0.00271 0.03738  110 GLU A CD  
793  O OE1 . GLU A 105 ? 0.44935 0.19713 0.32717 -0.08190 0.00317  0.00658  110 GLU A OE1 
794  O OE2 . GLU A 105 ? 0.46198 0.27183 0.32471 -0.03560 0.01414  0.04604  110 GLU A OE2 
795  N N   . VAL A 106 ? 0.33358 0.13535 0.23658 -0.03055 -0.05790 0.02701  111 VAL A N   
796  C CA  . VAL A 106 ? 0.33431 0.15363 0.23840 0.02937  -0.04667 0.01748  111 VAL A CA  
797  C C   . VAL A 106 ? 0.31156 0.17802 0.24617 0.06310  -0.04191 0.04990  111 VAL A C   
798  O O   . VAL A 106 ? 0.31764 0.26852 0.27823 0.08147  -0.02505 0.03119  111 VAL A O   
799  C CB  . VAL A 106 ? 0.33815 0.15537 0.22612 0.02798  -0.05452 0.00091  111 VAL A CB  
800  C CG1 . VAL A 106 ? 0.37461 0.17562 0.24305 0.02078  -0.05049 -0.02762 111 VAL A CG1 
801  C CG2 . VAL A 106 ? 0.31370 0.17954 0.21416 0.02336  -0.02066 0.03794  111 VAL A CG2 
802  N N   . GLY A 107 ? 0.30081 0.15565 0.21873 0.04016  -0.08262 0.05379  112 GLY A N   
803  C CA  . GLY A 107 ? 0.27347 0.22232 0.23581 0.01045  -0.09887 0.03713  112 GLY A CA  
804  C C   . GLY A 107 ? 0.29790 0.23281 0.25105 0.02165  -0.10074 0.04658  112 GLY A C   
805  O O   . GLY A 107 ? 0.33305 0.25057 0.27388 0.05166  -0.09910 0.06241  112 GLY A O   
806  N N   . ASP A 108 ? 0.30665 0.28598 0.26233 0.02525  -0.10002 0.04251  113 ASP A N   
807  C CA  . ASP A 108 ? 0.28978 0.31321 0.25439 0.02128  -0.10396 0.03948  113 ASP A CA  
808  C C   . ASP A 108 ? 0.27607 0.26919 0.25883 0.03196  -0.07149 0.04715  113 ASP A C   
809  O O   . ASP A 108 ? 0.27272 0.31578 0.26957 0.05509  -0.09837 0.03228  113 ASP A O   
810  C CB  . ASP A 108 ? 0.29445 0.35023 0.27159 0.00972  -0.09325 0.04221  113 ASP A CB  
811  N N   . ILE A 109 ? 0.25824 0.17511 0.22618 0.01421  -0.05504 0.03869  114 ILE A N   
812  C CA  . ILE A 109 ? 0.19738 0.15482 0.22049 0.01886  -0.04224 0.01703  114 ILE A CA  
813  C C   . ILE A 109 ? 0.16174 0.14137 0.21118 0.04542  -0.04751 -0.01800 114 ILE A C   
814  O O   . ILE A 109 ? 0.16445 0.15160 0.20171 0.03414  -0.04098 0.01273  114 ILE A O   
815  C CB  . ILE A 109 ? 0.18021 0.14037 0.23617 0.01371  -0.03015 0.02053  114 ILE A CB  
816  C CG1 . ILE A 109 ? 0.16493 0.18205 0.21759 0.01503  -0.03532 0.02364  114 ILE A CG1 
817  C CG2 . ILE A 109 ? 0.19738 0.13368 0.24865 0.01087  -0.03068 0.03672  114 ILE A CG2 
818  C CD1 . ILE A 109 ? 0.19046 0.16593 0.20764 0.00552  -0.04142 0.03719  114 ILE A CD1 
819  N N   . PRO A 110 ? 0.13582 0.13555 0.23066 0.04382  -0.03495 0.02037  115 PRO A N   
820  C CA  . PRO A 110 ? 0.13822 0.13099 0.21955 0.04294  -0.03528 0.00486  115 PRO A CA  
821  C C   . PRO A 110 ? 0.10666 0.11354 0.18609 0.03324  -0.03293 0.00409  115 PRO A C   
822  O O   . PRO A 110 ? 0.11090 0.13869 0.17907 0.03279  -0.03309 -0.00662 115 PRO A O   
823  C CB  . PRO A 110 ? 0.16223 0.17576 0.25701 0.04319  0.01683  0.01601  115 PRO A CB  
824  C CG  . PRO A 110 ? 0.18953 0.16360 0.26183 0.06847  0.00091  0.01886  115 PRO A CG  
825  C CD  . PRO A 110 ? 0.17130 0.12056 0.24693 0.06115  -0.01089 0.02603  115 PRO A CD  
826  N N   . THR A 111 ? 0.09393 0.10496 0.17744 0.02018  -0.02377 0.02321  116 THR A N   
827  C CA  . THR A 111 ? 0.10545 0.10612 0.17225 0.01325  0.00453  0.02366  116 THR A CA  
828  C C   . THR A 111 ? 0.08043 0.12482 0.16352 0.00753  0.01208  0.01890  116 THR A C   
829  O O   . THR A 111 ? 0.09003 0.12434 0.19277 -0.00445 -0.03344 0.01719  116 THR A O   
830  C CB  . THR A 111 ? 0.14257 0.12402 0.17908 0.01876  -0.00067 0.02823  116 THR A CB  
831  O OG1 . THR A 111 ? 0.17418 0.14141 0.19255 -0.00377 -0.00683 0.01434  116 THR A OG1 
832  C CG2 . THR A 111 ? 0.15314 0.14853 0.17064 0.05132  0.01019  0.01370  116 THR A CG2 
833  N N   . VAL A 112 ? 0.07713 0.08272 0.15962 0.03241  -0.00748 -0.00050 117 VAL A N   
834  C CA  . VAL A 112 ? 0.07462 0.08933 0.15230 0.01523  0.00273  0.01896  117 VAL A CA  
835  C C   . VAL A 112 ? 0.07880 0.09154 0.13500 -0.00063 -0.00946 -0.00399 117 VAL A C   
836  O O   . VAL A 112 ? 0.07442 0.09235 0.17002 -0.01056 0.00349  -0.00949 117 VAL A O   
837  C CB  . VAL A 112 ? 0.12056 0.11494 0.15348 -0.00946 0.02102  0.00667  117 VAL A CB  
838  C CG1 . VAL A 112 ? 0.12962 0.15150 0.15727 -0.00979 -0.03113 -0.00557 117 VAL A CG1 
839  C CG2 . VAL A 112 ? 0.16029 0.12187 0.15563 -0.00434 0.02302  0.03091  117 VAL A CG2 
840  N N   . LEU A 113 ? 0.08468 0.08834 0.10733 0.01949  -0.01175 0.01849  118 LEU A N   
841  C CA  . LEU A 113 ? 0.09114 0.06221 0.11434 0.02468  -0.02452 -0.01073 118 LEU A CA  
842  C C   . LEU A 113 ? 0.07251 0.07554 0.10573 0.01198  -0.02708 -0.01989 118 LEU A C   
843  O O   . LEU A 113 ? 0.08671 0.09349 0.12623 -0.01561 0.00411  0.01193  118 LEU A O   
844  C CB  . LEU A 113 ? 0.10266 0.11233 0.11570 0.01462  -0.00784 -0.03584 118 LEU A CB  
845  C CG  . LEU A 113 ? 0.10077 0.13553 0.11781 -0.00113 0.03004  -0.04185 118 LEU A CG  
846  C CD1 . LEU A 113 ? 0.13120 0.13287 0.13223 0.01086  0.03864  0.00562  118 LEU A CD1 
847  C CD2 . LEU A 113 ? 0.16140 0.14066 0.13230 0.02410  0.00054  -0.04833 118 LEU A CD2 
848  N N   . VAL A 114 ? 0.06606 0.07029 0.09050 -0.00776 -0.00327 0.00680  119 VAL A N   
849  C CA  . VAL A 114 ? 0.10229 0.04200 0.09438 0.01254  -0.00741 -0.00975 119 VAL A CA  
850  C C   . VAL A 114 ? 0.08365 0.05149 0.08944 -0.03587 -0.00630 0.00932  119 VAL A C   
851  O O   . VAL A 114 ? 0.07970 0.07165 0.10723 -0.02056 0.01096  0.00850  119 VAL A O   
852  C CB  . VAL A 114 ? 0.10700 0.05900 0.07607 -0.01688 0.00330  -0.00323 119 VAL A CB  
853  C CG1 . VAL A 114 ? 0.15577 0.08062 0.07132 0.01382  -0.01703 0.00371  119 VAL A CG1 
854  C CG2 . VAL A 114 ? 0.06161 0.08867 0.13313 -0.00766 0.00858  -0.01238 119 VAL A CG2 
855  N N   . GLN A 115 ? 0.06455 0.05832 0.08803 -0.00406 0.00534  -0.00467 120 GLN A N   
856  C CA  . GLN A 115 ? 0.09136 0.07071 0.08659 -0.00097 0.00680  -0.00886 120 GLN A CA  
857  C C   . GLN A 115 ? 0.06615 0.09107 0.07133 -0.03407 0.01731  0.00151  120 GLN A C   
858  O O   . GLN A 115 ? 0.08481 0.07676 0.07786 -0.00851 0.01883  0.00699  120 GLN A O   
859  C CB  . GLN A 115 ? 0.09229 0.06857 0.11479 -0.00913 0.01029  -0.02189 120 GLN A CB  
860  C CG  . GLN A 115 ? 0.09952 0.07614 0.13146 0.02015  0.02488  -0.02682 120 GLN A CG  
861  C CD  . GLN A 115 ? 0.13168 0.07554 0.14217 -0.02489 0.00599  -0.01564 120 GLN A CD  
862  O OE1 . GLN A 115 ? 0.15553 0.09870 0.15571 0.01023  -0.01359 -0.04400 120 GLN A OE1 
863  N NE2 . GLN A 115 ? 0.16776 0.06973 0.16482 0.01435  0.01721  -0.00522 120 GLN A NE2 
864  N N   . ASN A 116 ? 0.08467 0.06509 0.09938 -0.01089 0.00387  -0.01474 121 ASN A N   
865  C CA  . ASN A 116 ? 0.08544 0.07456 0.07620 -0.02256 -0.00801 0.00932  121 ASN A CA  
866  C C   . ASN A 116 ? 0.08948 0.08689 0.09422 0.00515  -0.00289 0.01028  121 ASN A C   
867  O O   . ASN A 116 ? 0.10267 0.07923 0.09753 -0.00006 0.01068  0.00346  121 ASN A O   
868  C CB  . ASN A 116 ? 0.10183 0.07721 0.09181 -0.01688 -0.01458 0.00065  121 ASN A CB  
869  C CG  . ASN A 116 ? 0.09799 0.08492 0.08135 -0.01506 0.00817  -0.01270 121 ASN A CG  
870  O OD1 . ASN A 116 ? 0.10914 0.08828 0.09774 -0.02711 0.02320  -0.02248 121 ASN A OD1 
871  N ND2 . ASN A 116 ? 0.09228 0.07432 0.09772 -0.01144 -0.00683 -0.02653 121 ASN A ND2 
872  N N   . LYS A 117 ? 0.09464 0.07084 0.08015 0.00072  -0.01749 0.02593  122 LYS A N   
873  C CA  . LYS A 117 ? 0.09910 0.06561 0.11287 -0.02362 -0.01278 0.02323  122 LYS A CA  
874  C C   . LYS A 117 ? 0.10596 0.07935 0.12090 -0.02445 -0.00025 0.00982  122 LYS A C   
875  O O   . LYS A 117 ? 0.11919 0.07663 0.13366 0.00636  0.00497  0.00719  122 LYS A O   
876  C CB  . LYS A 117 ? 0.09884 0.09208 0.11474 -0.03900 -0.00685 0.00775  122 LYS A CB  
877  C CG  . LYS A 117 ? 0.09927 0.07715 0.09695 -0.03739 -0.02274 0.00503  122 LYS A CG  
878  C CD  . LYS A 117 ? 0.08810 0.07461 0.11259 -0.02744 -0.02270 -0.00807 122 LYS A CD  
879  C CE  . LYS A 117 ? 0.07543 0.07714 0.11557 -0.02037 0.00485  0.00269  122 LYS A CE  
880  N NZ  . LYS A 117 ? 0.08446 0.11086 0.11745 -0.01661 0.00558  0.00680  122 LYS A NZ  
881  N N   . ILE A 118 ? 0.12854 0.07460 0.12125 -0.04200 -0.00277 0.01250  123 ILE A N   
882  C CA  . ILE A 118 ? 0.12871 0.08784 0.14570 -0.06037 -0.00514 0.01223  123 ILE A CA  
883  C C   . ILE A 118 ? 0.14978 0.07506 0.16052 -0.02875 -0.02969 0.00570  123 ILE A C   
884  O O   . ILE A 118 ? 0.20976 0.07710 0.19656 -0.02180 -0.03408 0.00216  123 ILE A O   
885  C CB  . ILE A 118 ? 0.14562 0.12645 0.15552 -0.08063 0.00030  -0.00856 123 ILE A CB  
886  C CG1 . ILE A 118 ? 0.18660 0.15935 0.15608 -0.04506 -0.01310 0.00509  123 ILE A CG1 
887  C CG2 . ILE A 118 ? 0.20128 0.13003 0.11707 -0.03732 0.01855  0.01219  123 ILE A CG2 
888  C CD1 . ILE A 118 ? 0.20089 0.16621 0.16549 -0.02407 -0.02321 -0.01206 123 ILE A CD1 
889  N N   . ASP A 119 ? 0.14827 0.08580 0.14307 -0.02893 -0.01698 0.02852  124 ASP A N   
890  C CA  . ASP A 119 ? 0.17725 0.08415 0.16528 -0.00379 0.00164  0.01398  124 ASP A CA  
891  C C   . ASP A 119 ? 0.19570 0.09855 0.17690 0.01555  0.01010  0.02222  124 ASP A C   
892  O O   . ASP A 119 ? 0.23151 0.11253 0.19010 0.04077  0.03193  0.03495  124 ASP A O   
893  C CB  . ASP A 119 ? 0.15948 0.08249 0.13177 -0.03884 0.01275  0.04243  124 ASP A CB  
894  C CG  . ASP A 119 ? 0.15530 0.09241 0.14213 0.00464  0.00835  0.05312  124 ASP A CG  
895  O OD1 . ASP A 119 ? 0.14940 0.08164 0.14857 -0.01141 -0.01061 0.03851  124 ASP A OD1 
896  O OD2 . ASP A 119 ? 0.18316 0.09410 0.17912 -0.00514 0.00659  0.02755  124 ASP A OD2 
897  N N   . LEU A 120 ? 0.18274 0.10921 0.16155 0.00875  0.01296  -0.00324 125 LEU A N   
898  C CA  . LEU A 120 ? 0.20579 0.08975 0.18779 -0.01066 0.01359  0.00379  125 LEU A CA  
899  C C   . LEU A 120 ? 0.28518 0.12546 0.22430 0.01049  0.03272  0.00499  125 LEU A C   
900  O O   . LEU A 120 ? 0.22983 0.14159 0.21977 0.01979  0.00103  0.00794  125 LEU A O   
901  C CB  . LEU A 120 ? 0.19518 0.14675 0.18417 0.02621  -0.00578 0.00547  125 LEU A CB  
902  C CG  . LEU A 120 ? 0.15033 0.14485 0.17003 0.00544  -0.00781 0.01238  125 LEU A CG  
903  C CD1 . LEU A 120 ? 0.16166 0.13601 0.17190 0.00971  -0.01070 0.01531  125 LEU A CD1 
904  C CD2 . LEU A 120 ? 0.17820 0.14464 0.17094 0.04727  -0.05178 0.03537  125 LEU A CD2 
905  N N   . LEU A 121 ? 0.40026 0.19132 0.26622 -0.03528 0.03739  -0.06481 126 LEU A N   
906  C CA  . LEU A 121 ? 0.48377 0.21642 0.30061 -0.07151 0.03108  -0.08068 126 LEU A CA  
907  C C   . LEU A 121 ? 0.52953 0.18204 0.31235 -0.02175 0.04011  -0.04519 126 LEU A C   
908  O O   . LEU A 121 ? 0.57071 0.20794 0.29128 -0.02039 0.04675  -0.04263 126 LEU A O   
909  C CB  . LEU A 121 ? 0.50737 0.32068 0.31996 -0.07944 0.02617  -0.09436 126 LEU A CB  
910  N N   . ASP A 122 ? 0.52528 0.13416 0.31281 0.00192  0.03434  -0.01602 127 ASP A N   
911  C CA  . ASP A 122 ? 0.51115 0.27243 0.34163 0.12324  0.04168  -0.01250 127 ASP A CA  
912  C C   . ASP A 122 ? 0.54337 0.31203 0.32726 0.20929  0.04376  -0.02958 127 ASP A C   
913  O O   . ASP A 122 ? 0.61288 0.34437 0.35324 0.24953  0.02660  -0.01610 127 ASP A O   
915  N N   . ASP A 123 ? 0.48747 0.28986 0.30386 0.20154  0.01344  0.00812  128 ASP A N   
916  C CA  . ASP A 123 ? 0.37560 0.30048 0.30265 0.17681  0.00588  -0.01911 128 ASP A CA  
917  C C   . ASP A 123 ? 0.29274 0.23847 0.26937 0.09862  -0.02315 -0.00460 128 ASP A C   
918  O O   . ASP A 123 ? 0.25577 0.30015 0.26964 0.07173  -0.02691 -0.01978 128 ASP A O   
923  N N   . SER A 124 ? 0.29125 0.16557 0.24128 0.05536  -0.00025 0.00564  129 SER A N   
924  C CA  . SER A 124 ? 0.25919 0.15299 0.23354 0.03284  0.00994  0.01222  129 SER A CA  
925  C C   . SER A 124 ? 0.21757 0.17676 0.21923 0.03246  0.03097  -0.02999 129 SER A C   
926  O O   . SER A 124 ? 0.27822 0.21511 0.24570 0.08639  0.05938  -0.03014 129 SER A O   
927  C CB  . SER A 124 ? 0.28492 0.15314 0.24870 -0.00534 -0.00586 0.01521  129 SER A CB  
928  O OG  . SER A 124 ? 0.30562 0.22748 0.24888 0.02547  -0.03036 -0.01264 129 SER A OG  
929  N N   . CYS A 125 ? 0.17052 0.17531 0.18546 0.00988  0.00777  -0.02265 130 CYS A N   
930  C CA  . CYS A 125 ? 0.16154 0.19323 0.18781 0.00483  -0.00513 -0.03825 130 CYS A CA  
931  C C   . CYS A 125 ? 0.18493 0.18313 0.17056 0.03080  -0.01025 -0.02771 130 CYS A C   
932  O O   . CYS A 125 ? 0.22314 0.21696 0.17571 0.01959  -0.02308 -0.02851 130 CYS A O   
933  C CB  . CYS A 125 ? 0.16188 0.38362 0.23464 -0.04521 -0.01069 0.01590  130 CYS A CB  
934  S SG  . CYS A 125 ? 0.25141 0.48372 0.33068 -0.03488 -0.02139 -0.03940 130 CYS A SG  
935  N N   . ILE A 126 ? 0.15223 0.15565 0.17335 -0.03466 -0.00954 -0.03358 131 ILE A N   
936  C CA  . ILE A 126 ? 0.14484 0.15237 0.18801 -0.03636 -0.02348 -0.03384 131 ILE A CA  
937  C C   . ILE A 126 ? 0.17078 0.17008 0.16506 -0.03684 -0.00116 -0.01206 131 ILE A C   
938  O O   . ILE A 126 ? 0.19605 0.21811 0.14999 -0.02429 -0.01529 0.00207  131 ILE A O   
939  C CB  . ILE A 126 ? 0.16320 0.11557 0.20199 -0.05014 -0.03368 -0.03681 131 ILE A CB  
940  C CG1 . ILE A 126 ? 0.19956 0.15694 0.18225 -0.01088 -0.04121 -0.02919 131 ILE A CG1 
941  C CG2 . ILE A 126 ? 0.15323 0.17465 0.22201 -0.02057 -0.03692 -0.05726 131 ILE A CG2 
942  C CD1 . ILE A 126 ? 0.20072 0.16006 0.18391 0.01779  -0.01485 -0.01879 131 ILE A CD1 
943  N N   . LYS A 127 ? 0.16340 0.14517 0.14839 -0.02406 -0.00400 -0.00575 132 LYS A N   
944  C CA  . LYS A 127 ? 0.19785 0.11669 0.16671 -0.02943 -0.00851 0.00449  132 LYS A CA  
945  C C   . LYS A 127 ? 0.17039 0.13102 0.15899 -0.03387 -0.01818 -0.01765 132 LYS A C   
946  O O   . LYS A 127 ? 0.18423 0.12670 0.16970 -0.01876 -0.03070 0.00523  132 LYS A O   
947  C CB  . LYS A 127 ? 0.23201 0.11874 0.19811 -0.05006 -0.00549 -0.01151 132 LYS A CB  
948  C CG  . LYS A 127 ? 0.31579 0.19620 0.25293 -0.00514 -0.00655 -0.04776 132 LYS A CG  
949  C CD  . LYS A 127 ? 0.41230 0.30907 0.28608 -0.00805 -0.01064 -0.04450 132 LYS A CD  
950  C CE  . LYS A 127 ? 0.48209 0.37783 0.31709 0.01885  -0.03052 -0.07068 132 LYS A CE  
951  N NZ  . LYS A 127 ? 0.53004 0.42148 0.33361 0.02765  -0.03465 -0.08445 132 LYS A NZ  
952  N N   . ASN A 128 ? 0.15439 0.14878 0.17295 -0.03119 -0.02561 -0.00126 133 ASN A N   
953  C CA  . ASN A 128 ? 0.16094 0.16508 0.19105 -0.08516 0.00129  0.00519  133 ASN A CA  
954  C C   . ASN A 128 ? 0.17855 0.15136 0.19660 -0.03941 -0.01451 0.01426  133 ASN A C   
955  O O   . ASN A 128 ? 0.17987 0.16211 0.21880 -0.04908 0.01284  0.02279  133 ASN A O   
956  C CB  . ASN A 128 ? 0.23764 0.18712 0.23019 -0.08678 0.02996  0.02567  133 ASN A CB  
957  C CG  . ASN A 128 ? 0.32068 0.31537 0.27563 -0.02166 0.06438  0.06248  133 ASN A CG  
958  O OD1 . ASN A 128 ? 0.37179 0.37508 0.29299 0.01878  0.06765  0.04403  133 ASN A OD1 
959  N ND2 . ASN A 128 ? 0.36957 0.36524 0.30496 0.04808  0.05677  0.05399  133 ASN A ND2 
960  N N   . GLU A 129 ? 0.19102 0.11511 0.18793 -0.07128 -0.02064 -0.02133 134 GLU A N   
961  C CA  . GLU A 129 ? 0.19959 0.14895 0.19780 -0.05296 -0.04181 -0.03206 134 GLU A CA  
962  C C   . GLU A 129 ? 0.16366 0.13156 0.18512 -0.07640 0.00097  0.01490  134 GLU A C   
963  O O   . GLU A 129 ? 0.18212 0.12721 0.21324 -0.02960 -0.02115 -0.01595 134 GLU A O   
964  C CB  . GLU A 129 ? 0.29319 0.14738 0.26297 -0.05086 -0.02186 -0.02225 134 GLU A CB  
965  C CG  . GLU A 129 ? 0.39986 0.20975 0.33722 0.00364  0.00071  -0.03361 134 GLU A CG  
966  C CD  . GLU A 129 ? 0.47959 0.20819 0.39449 0.03132  0.02712  -0.05391 134 GLU A CD  
967  O OE1 . GLU A 129 ? 0.46179 0.14050 0.39447 -0.05932 0.06349  -0.03305 134 GLU A OE1 
968  O OE2 . GLU A 129 ? 0.53069 0.29117 0.43454 0.06647  0.02378  -0.09300 134 GLU A OE2 
969  N N   . GLU A 130 ? 0.17220 0.10037 0.17122 -0.06328 -0.01752 -0.01103 135 GLU A N   
970  C CA  . GLU A 130 ? 0.11313 0.11530 0.13112 -0.05018 0.00465  -0.02394 135 GLU A CA  
971  C C   . GLU A 130 ? 0.14048 0.10405 0.11355 -0.01664 -0.00178 -0.02625 135 GLU A C   
972  O O   . GLU A 130 ? 0.12529 0.11667 0.12954 -0.01587 -0.00023 -0.00952 135 GLU A O   
973  C CB  . GLU A 130 ? 0.10407 0.14930 0.12658 -0.00130 -0.00501 -0.04390 135 GLU A CB  
974  C CG  . GLU A 130 ? 0.19507 0.13299 0.13093 0.04266  -0.00529 -0.04465 135 GLU A CG  
975  C CD  . GLU A 130 ? 0.20843 0.23389 0.14525 0.05886  -0.00376 -0.02043 135 GLU A CD  
976  O OE1 . GLU A 130 ? 0.22168 0.21632 0.14858 0.00349  0.01000  -0.02969 135 GLU A OE1 
977  O OE2 . GLU A 130 ? 0.22024 0.42006 0.15322 0.09031  -0.00577 0.00818  135 GLU A OE2 
978  N N   . ALA A 131 ? 0.12483 0.12301 0.11246 -0.03429 -0.00739 -0.03572 136 ALA A N   
979  C CA  . ALA A 131 ? 0.12397 0.11893 0.12327 -0.04177 -0.00212 -0.04544 136 ALA A CA  
980  C C   . ALA A 131 ? 0.10733 0.13764 0.11944 -0.05313 0.02455  -0.02798 136 ALA A C   
981  O O   . ALA A 131 ? 0.14257 0.11782 0.13183 -0.03867 0.02917  -0.01015 136 ALA A O   
982  C CB  . ALA A 131 ? 0.14785 0.16761 0.12016 -0.05366 -0.01229 -0.01666 136 ALA A CB  
983  N N   . GLU A 132 ? 0.10004 0.16224 0.14028 -0.04422 0.00161  0.00366  137 GLU A N   
984  C CA  . GLU A 132 ? 0.12113 0.17296 0.15379 -0.05934 -0.02030 0.02378  137 GLU A CA  
985  C C   . GLU A 132 ? 0.10042 0.19749 0.15150 -0.05548 -0.02026 -0.00556 137 GLU A C   
986  O O   . GLU A 132 ? 0.12234 0.18507 0.16823 -0.01935 -0.01650 0.00442  137 GLU A O   
987  C CB  . GLU A 132 ? 0.17311 0.22861 0.19147 -0.03184 -0.01214 0.05884  137 GLU A CB  
988  C CG  . GLU A 132 ? 0.22034 0.25785 0.21049 -0.07805 -0.00729 0.07358  137 GLU A CG  
989  C CD  . GLU A 132 ? 0.28148 0.34661 0.24521 -0.10742 -0.04902 0.04846  137 GLU A CD  
990  O OE1 . GLU A 132 ? 0.32301 0.36683 0.29432 -0.12537 -0.08822 0.03223  137 GLU A OE1 
991  O OE2 . GLU A 132 ? 0.28600 0.32416 0.23584 -0.12619 -0.04572 0.03148  137 GLU A OE2 
992  N N   . ALA A 133 ? 0.11315 0.15123 0.14024 -0.05225 0.01253  -0.00495 138 ALA A N   
993  C CA  . ALA A 133 ? 0.12853 0.13289 0.15102 -0.02622 -0.00274 -0.02730 138 ALA A CA  
994  C C   . ALA A 133 ? 0.13137 0.13518 0.14536 -0.02958 0.00019  -0.03372 138 ALA A C   
995  O O   . ALA A 133 ? 0.12669 0.15478 0.13840 -0.02159 0.00176  -0.03211 138 ALA A O   
996  C CB  . ALA A 133 ? 0.17180 0.11678 0.16971 0.00153  0.01158  -0.03072 138 ALA A CB  
997  N N   . LEU A 134 ? 0.10987 0.10129 0.13499 -0.03574 0.00780  -0.02509 139 LEU A N   
998  C CA  . LEU A 134 ? 0.10228 0.10113 0.13048 -0.02795 -0.00518 -0.02283 139 LEU A CA  
999  C C   . LEU A 134 ? 0.12598 0.12757 0.12898 -0.00626 -0.00043 -0.03387 139 LEU A C   
1000 O O   . LEU A 134 ? 0.11527 0.13185 0.14231 -0.01209 -0.00741 -0.02131 139 LEU A O   
1001 C CB  . LEU A 134 ? 0.11085 0.09033 0.14119 -0.04554 -0.03206 -0.02073 139 LEU A CB  
1002 C CG  . LEU A 134 ? 0.11312 0.10904 0.15616 -0.04782 -0.01889 -0.01358 139 LEU A CG  
1003 C CD1 . LEU A 134 ? 0.14433 0.14938 0.17438 -0.01824 -0.00209 0.01941  139 LEU A CD1 
1004 C CD2 . LEU A 134 ? 0.11962 0.13684 0.17543 -0.04959 -0.03030 -0.02738 139 LEU A CD2 
1005 N N   . ALA A 135 ? 0.10976 0.12053 0.12682 -0.01551 -0.00181 -0.03109 140 ALA A N   
1006 C CA  . ALA A 135 ? 0.11495 0.18183 0.12421 0.00245  0.00145  -0.01885 140 ALA A CA  
1007 C C   . ALA A 135 ? 0.10699 0.18454 0.11973 -0.00404 -0.01006 -0.03220 140 ALA A C   
1008 O O   . ALA A 135 ? 0.14726 0.19159 0.13066 0.03039  -0.03250 -0.03816 140 ALA A O   
1009 C CB  . ALA A 135 ? 0.16363 0.21501 0.12262 0.05433  0.00352  -0.00243 140 ALA A CB  
1010 N N   . LYS A 136 ? 0.09631 0.16374 0.12709 -0.02226 -0.00861 -0.02594 141 LYS A N   
1011 C CA  . LYS A 136 ? 0.11044 0.18066 0.14573 -0.04665 -0.02128 -0.02509 141 LYS A CA  
1012 C C   . LYS A 136 ? 0.11999 0.15272 0.13433 -0.01904 -0.01659 -0.01521 141 LYS A C   
1013 O O   . LYS A 136 ? 0.13112 0.18495 0.14466 0.00567  -0.02801 -0.01605 141 LYS A O   
1014 C CB  . LYS A 136 ? 0.14074 0.20533 0.19150 -0.06214 -0.01640 -0.03163 141 LYS A CB  
1015 C CG  . LYS A 136 ? 0.21203 0.25148 0.22834 -0.05772 -0.04937 -0.05199 141 LYS A CG  
1016 C CD  . LYS A 136 ? 0.30990 0.34672 0.26421 -0.02731 -0.04431 -0.01695 141 LYS A CD  
1017 C CE  . LYS A 136 ? 0.37070 0.40570 0.28592 -0.01955 -0.04753 0.01280  141 LYS A CE  
1018 N NZ  . LYS A 136 ? 0.39204 0.43171 0.31456 -0.03273 -0.05272 0.01070  141 LYS A NZ  
1019 N N   . ARG A 137 ? 0.12352 0.13871 0.14021 -0.04288 -0.00477 -0.01118 142 ARG A N   
1020 C CA  . ARG A 137 ? 0.12214 0.13235 0.13094 -0.02682 0.00145  -0.04302 142 ARG A CA  
1021 C C   . ARG A 137 ? 0.12140 0.14672 0.15341 -0.03288 -0.02401 -0.03251 142 ARG A C   
1022 O O   . ARG A 137 ? 0.16426 0.16556 0.16393 0.01349  -0.02068 -0.01440 142 ARG A O   
1023 C CB  . ARG A 137 ? 0.10784 0.15481 0.14426 -0.02165 0.01007  -0.01317 142 ARG A CB  
1024 C CG  . ARG A 137 ? 0.11181 0.15055 0.14058 -0.03026 -0.01312 -0.00869 142 ARG A CG  
1025 C CD  . ARG A 137 ? 0.15537 0.16607 0.13194 -0.02498 -0.00414 0.00813  142 ARG A CD  
1026 N NE  . ARG A 137 ? 0.16118 0.16085 0.14093 -0.02835 0.00256  -0.00027 142 ARG A NE  
1027 C CZ  . ARG A 137 ? 0.15706 0.14329 0.13809 -0.02035 0.01665  0.00033  142 ARG A CZ  
1028 N NH1 . ARG A 137 ? 0.16667 0.16070 0.14642 0.01434  -0.01587 -0.02987 142 ARG A NH1 
1029 N NH2 . ARG A 137 ? 0.16881 0.16419 0.15051 -0.03444 0.01598  -0.00247 142 ARG A NH2 
1030 N N   . LEU A 138 ? 0.11276 0.12407 0.14571 -0.03563 -0.00275 -0.04643 143 LEU A N   
1031 C CA  . LEU A 138 ? 0.12480 0.13380 0.16147 0.00110  -0.03504 -0.04053 143 LEU A CA  
1032 C C   . LEU A 138 ? 0.14260 0.16467 0.13886 0.02722  -0.03332 -0.02045 143 LEU A C   
1033 O O   . LEU A 138 ? 0.15620 0.16641 0.13598 0.01678  -0.03460 -0.01627 143 LEU A O   
1034 C CB  . LEU A 138 ? 0.12324 0.12564 0.18389 0.01447  -0.04062 -0.07326 143 LEU A CB  
1035 C CG  . LEU A 138 ? 0.11791 0.16631 0.23214 0.00106  -0.01944 -0.06387 143 LEU A CG  
1036 C CD1 . LEU A 138 ? 0.13027 0.18404 0.27065 0.00667  -0.07033 -0.07901 143 LEU A CD1 
1037 C CD2 . LEU A 138 ? 0.16713 0.15443 0.26994 -0.00800 0.02298  -0.04185 143 LEU A CD2 
1038 N N   . LYS A 139 ? 0.11550 0.19080 0.13656 -0.03557 -0.01104 -0.02080 144 LYS A N   
1039 C CA  . LYS A 139 ? 0.13500 0.21839 0.13889 0.03142  -0.01587 -0.04394 144 LYS A CA  
1040 C C   . LYS A 139 ? 0.14183 0.14230 0.13551 0.01707  0.00614  -0.03023 144 LYS A C   
1041 O O   . LYS A 139 ? 0.16607 0.18862 0.16861 0.04403  -0.02271 -0.03815 144 LYS A O   
1042 C CB  . LYS A 139 ? 0.15384 0.25667 0.16840 0.00661  -0.02280 -0.02467 144 LYS A CB  
1043 C CG  . LYS A 139 ? 0.19755 0.29649 0.18394 0.01872  -0.02943 -0.03128 144 LYS A CG  
1044 C CD  . LYS A 139 ? 0.26055 0.39687 0.22396 0.06178  -0.05328 -0.03787 144 LYS A CD  
1045 C CE  . LYS A 139 ? 0.32601 0.48836 0.27840 0.09071  -0.05664 -0.02554 144 LYS A CE  
1046 N NZ  . LYS A 139 ? 0.36164 0.53705 0.31663 0.08777  -0.06235 -0.01993 144 LYS A NZ  
1047 N N   . LEU A 140 ? 0.10865 0.15889 0.12961 -0.01705 -0.02049 -0.02263 145 LEU A N   
1048 C CA  . LEU A 140 ? 0.13784 0.15128 0.13929 -0.00101 -0.02097 -0.03532 145 LEU A CA  
1049 C C   . LEU A 140 ? 0.10619 0.13418 0.16497 -0.01154 -0.01849 -0.01501 145 LEU A C   
1050 O O   . LEU A 140 ? 0.16136 0.13703 0.17793 0.00793  -0.00041 -0.03223 145 LEU A O   
1051 C CB  . LEU A 140 ? 0.12310 0.16555 0.14506 -0.01494 -0.01553 -0.05385 145 LEU A CB  
1052 C CG  . LEU A 140 ? 0.15773 0.16327 0.16575 -0.05934 -0.00923 -0.00586 145 LEU A CG  
1053 C CD1 . LEU A 140 ? 0.16212 0.20389 0.15706 -0.06097 -0.03258 -0.00762 145 LEU A CD1 
1054 C CD2 . LEU A 140 ? 0.24222 0.13137 0.19915 -0.01198 -0.02535 -0.01300 145 LEU A CD2 
1055 N N   . ARG A 141 ? 0.08675 0.16332 0.14959 -0.00073 -0.02285 -0.02540 146 ARG A N   
1056 C CA  . ARG A 141 ? 0.09488 0.13730 0.17209 -0.01247 -0.01784 -0.00194 146 ARG A CA  
1057 C C   . ARG A 141 ? 0.09519 0.12591 0.15293 -0.03183 -0.03339 -0.00504 146 ARG A C   
1058 O O   . ARG A 141 ? 0.08436 0.10939 0.15200 -0.01576 -0.02760 -0.02406 146 ARG A O   
1059 C CB  . ARG A 141 ? 0.10487 0.22371 0.19787 0.00626  0.01061  0.00869  146 ARG A CB  
1060 C CG  . ARG A 141 ? 0.19508 0.33486 0.27674 0.06703  0.01169  0.03983  146 ARG A CG  
1061 C CD  . ARG A 141 ? 0.29122 0.41121 0.35272 0.10148  -0.01009 0.06648  146 ARG A CD  
1062 N NE  . ARG A 141 ? 0.34266 0.44870 0.41254 0.08584  0.01072  0.07732  146 ARG A NE  
1063 C CZ  . ARG A 141 ? 0.34828 0.44618 0.44342 0.04609  -0.01067 0.06900  146 ARG A CZ  
1064 N NH1 . ARG A 141 ? 0.35332 0.44561 0.44688 -0.00419 -0.02593 0.07424  146 ARG A NH1 
1065 N NH2 . ARG A 141 ? 0.31354 0.40994 0.46292 -0.02511 -0.00798 0.07385  146 ARG A NH2 
1066 N N   . PHE A 142 ? 0.08169 0.13651 0.14164 -0.01420 -0.02392 0.02775  147 PHE A N   
1067 C CA  . PHE A 142 ? 0.08496 0.10055 0.15376 -0.00217 -0.00733 0.01244  147 PHE A CA  
1068 C C   . PHE A 142 ? 0.06954 0.08478 0.15047 -0.03506 -0.00405 0.02290  147 PHE A C   
1069 O O   . PHE A 142 ? 0.09413 0.17051 0.15591 -0.05403 0.00393  0.02599  147 PHE A O   
1070 C CB  . PHE A 142 ? 0.11153 0.11694 0.15895 -0.03983 -0.00876 -0.02597 147 PHE A CB  
1071 C CG  . PHE A 142 ? 0.09977 0.09915 0.14639 -0.02114 0.01529  0.01594  147 PHE A CG  
1072 C CD1 . PHE A 142 ? 0.09834 0.11479 0.14495 -0.01310 0.01608  0.00139  147 PHE A CD1 
1073 C CD2 . PHE A 142 ? 0.10750 0.13182 0.15084 -0.02483 0.00262  0.00701  147 PHE A CD2 
1074 C CE1 . PHE A 142 ? 0.10718 0.11219 0.15116 0.01967  0.00597  -0.00235 147 PHE A CE1 
1075 C CE2 . PHE A 142 ? 0.10654 0.14933 0.16196 -0.01087 -0.00392 -0.00890 147 PHE A CE2 
1076 C CZ  . PHE A 142 ? 0.08733 0.13682 0.13949 -0.02577 -0.00592 -0.01521 147 PHE A CZ  
1077 N N   . TYR A 143 ? 0.07789 0.11107 0.12335 -0.01395 -0.02298 -0.00942 148 TYR A N   
1078 C CA  . TYR A 143 ? 0.09283 0.09842 0.10107 -0.01148 -0.01246 0.00504  148 TYR A CA  
1079 C C   . TYR A 143 ? 0.09556 0.07991 0.10536 -0.02479 0.00537  0.01305  148 TYR A C   
1080 O O   . TYR A 143 ? 0.09282 0.10998 0.12556 -0.02327 0.02606  0.03739  148 TYR A O   
1081 C CB  . TYR A 143 ? 0.08805 0.12334 0.13821 -0.03550 0.01481  -0.02482 148 TYR A CB  
1082 C CG  . TYR A 143 ? 0.09334 0.16253 0.18293 -0.05608 0.01860  -0.02193 148 TYR A CG  
1083 C CD1 . TYR A 143 ? 0.17176 0.16220 0.22819 0.02532  0.01823  -0.02994 148 TYR A CD1 
1084 C CD2 . TYR A 143 ? 0.10212 0.21757 0.22002 -0.01384 0.03231  0.00562  148 TYR A CD2 
1085 C CE1 . TYR A 143 ? 0.14997 0.18760 0.23539 0.00507  0.01039  -0.06117 148 TYR A CE1 
1086 C CE2 . TYR A 143 ? 0.11666 0.26270 0.24435 0.01125  0.02695  -0.03698 148 TYR A CE2 
1087 C CZ  . TYR A 143 ? 0.15988 0.19717 0.25351 0.03458  0.03541  -0.05336 148 TYR A CZ  
1088 O OH  . TYR A 143 ? 0.17716 0.24709 0.27755 0.04922  0.03695  -0.05895 148 TYR A OH  
1089 N N   . ARG A 144 ? 0.10213 0.09728 0.10764 -0.01364 -0.00300 0.00385  149 ARG A N   
1090 C CA  . ARG A 144 ? 0.12308 0.06773 0.10059 -0.01420 -0.01358 -0.01730 149 ARG A CA  
1091 C C   . ARG A 144 ? 0.08630 0.08659 0.10113 -0.05158 -0.00341 0.00620  149 ARG A C   
1092 O O   . ARG A 144 ? 0.13387 0.18177 0.11516 -0.06873 0.02982  0.01342  149 ARG A O   
1093 C CB  . ARG A 144 ? 0.15346 0.09561 0.10784 -0.04643 -0.00113 -0.03560 149 ARG A CB  
1094 C CG  . ARG A 144 ? 0.20302 0.08833 0.11911 -0.04885 0.03023  -0.03651 149 ARG A CG  
1095 C CD  . ARG A 144 ? 0.22903 0.09209 0.15499 -0.05655 0.01068  -0.03265 149 ARG A CD  
1096 N NE  . ARG A 144 ? 0.21205 0.09219 0.13647 -0.04284 0.00980  -0.03444 149 ARG A NE  
1097 C CZ  . ARG A 144 ? 0.22545 0.12999 0.13164 -0.07133 0.03160  -0.00339 149 ARG A CZ  
1098 N NH1 . ARG A 144 ? 0.20111 0.17978 0.15191 -0.06652 -0.00884 0.02551  149 ARG A NH1 
1099 N NH2 . ARG A 144 ? 0.26840 0.11618 0.12388 -0.03683 0.01931  -0.01189 149 ARG A NH2 
1100 N N   . THR A 145 ? 0.07476 0.09986 0.09326 -0.01974 0.00499  0.00644  150 THR A N   
1101 C CA  . THR A 145 ? 0.09472 0.07903 0.07402 -0.01855 0.00076  0.01883  150 THR A CA  
1102 C C   . THR A 145 ? 0.10239 0.08397 0.07172 -0.03282 0.01004  0.00312  150 THR A C   
1103 O O   . THR A 145 ? 0.10590 0.08803 0.08538 -0.00941 0.01124  0.00362  150 THR A O   
1104 C CB  . THR A 145 ? 0.10157 0.09740 0.11682 -0.02074 0.04006  0.03271  150 THR A CB  
1105 O OG1 . THR A 145 ? 0.11935 0.08591 0.12279 -0.03022 0.02154  0.00921  150 THR A OG1 
1106 C CG2 . THR A 145 ? 0.09442 0.12403 0.14008 0.01747  -0.00686 0.02992  150 THR A CG2 
1107 N N   . SER A 146 ? 0.12120 0.07348 0.08654 -0.02743 -0.00128 0.01406  151 SER A N   
1108 C CA  . SER A 146 ? 0.11941 0.06256 0.08180 -0.01510 -0.04437 0.02053  151 SER A CA  
1109 C C   . SER A 146 ? 0.09656 0.06916 0.10207 -0.02202 0.00946  0.01439  151 SER A C   
1110 O O   . SER A 146 ? 0.09929 0.10529 0.11659 -0.04195 0.02671  0.00621  151 SER A O   
1111 C CB  . SER A 146 ? 0.13583 0.08235 0.09710 -0.00139 -0.04050 0.03382  151 SER A CB  
1112 O OG  . SER A 146 ? 0.15552 0.09755 0.10830 0.00030  -0.00426 0.02706  151 SER A OG  
1113 N N   . VAL A 147 ? 0.11081 0.04568 0.12863 -0.01465 0.00941  0.01579  152 VAL A N   
1114 C CA  . VAL A 147 ? 0.09919 0.04629 0.11134 -0.02593 0.02440  0.00492  152 VAL A CA  
1115 C C   . VAL A 147 ? 0.11658 0.09117 0.10883 -0.00919 -0.00165 -0.00987 152 VAL A C   
1116 O O   . VAL A 147 ? 0.12864 0.10306 0.11756 -0.01328 0.01633  -0.01375 152 VAL A O   
1117 C CB  . VAL A 147 ? 0.14945 0.06046 0.12130 -0.03926 0.01408  0.01403  152 VAL A CB  
1118 C CG1 . VAL A 147 ? 0.19716 0.05338 0.14316 -0.00974 0.00913  -0.00297 152 VAL A CG1 
1119 C CG2 . VAL A 147 ? 0.18122 0.07089 0.11123 -0.03456 0.03434  0.01548  152 VAL A CG2 
1120 N N   . LYS A 148 ? 0.11020 0.08310 0.12968 -0.02902 -0.00127 0.00259  153 LYS A N   
1121 C CA  . LYS A 148 ? 0.12635 0.08844 0.13220 0.00351  -0.01382 0.00015  153 LYS A CA  
1122 C C   . LYS A 148 ? 0.14124 0.11380 0.12224 -0.03024 0.01002  0.01044  153 LYS A C   
1123 O O   . LYS A 148 ? 0.19169 0.15390 0.11035 -0.00894 -0.00445 0.01141  153 LYS A O   
1124 C CB  . LYS A 148 ? 0.17608 0.12478 0.11881 0.03120  -0.02946 -0.01999 153 LYS A CB  
1125 C CG  . LYS A 148 ? 0.20197 0.17291 0.14319 0.05985  -0.06696 -0.00483 153 LYS A CG  
1126 C CD  . LYS A 148 ? 0.26766 0.22297 0.18142 0.11734  -0.06351 -0.01363 153 LYS A CD  
1127 C CE  . LYS A 148 ? 0.32360 0.29122 0.21003 0.17434  -0.05452 -0.01203 153 LYS A CE  
1128 N NZ  . LYS A 148 ? 0.39928 0.37439 0.27339 0.17153  -0.02956 -0.01236 153 LYS A NZ  
1129 N N   . GLU A 149 ? 0.13811 0.10592 0.12545 -0.04215 -0.00662 0.03419  154 GLU A N   
1130 C CA  . GLU A 149 ? 0.16055 0.14311 0.13225 -0.06459 -0.00843 0.02646  154 GLU A CA  
1131 C C   . GLU A 149 ? 0.15695 0.14805 0.11231 -0.06687 0.02990  0.01340  154 GLU A C   
1132 O O   . GLU A 149 ? 0.18133 0.13917 0.14068 -0.03327 0.02773  0.03814  154 GLU A O   
1133 C CB  . GLU A 149 ? 0.18550 0.14832 0.15605 -0.05829 -0.01197 0.02010  154 GLU A CB  
1134 C CG  . GLU A 149 ? 0.22222 0.18776 0.19270 -0.02492 -0.02737 0.06288  154 GLU A CG  
1135 C CD  . GLU A 149 ? 0.30113 0.31171 0.27482 -0.02026 -0.07328 0.09806  154 GLU A CD  
1136 O OE1 . GLU A 149 ? 0.31891 0.33861 0.30581 -0.04805 -0.08332 0.09180  154 GLU A OE1 
1137 O OE2 . GLU A 149 ? 0.36213 0.35859 0.31270 -0.03095 -0.11294 0.08130  154 GLU A OE2 
1138 N N   . ASP A 150 ? 0.17395 0.12569 0.11360 -0.03510 0.02451  0.00998  155 ASP A N   
1139 C CA  . ASP A 150 ? 0.13000 0.13846 0.13085 -0.01756 0.02523  -0.00493 155 ASP A CA  
1140 C C   . ASP A 150 ? 0.14092 0.12099 0.13869 -0.03295 0.02984  0.00069  155 ASP A C   
1141 O O   . ASP A 150 ? 0.15692 0.18125 0.15102 -0.04998 0.02813  -0.00742 155 ASP A O   
1142 C CB  . ASP A 150 ? 0.19783 0.17995 0.13268 -0.00757 0.04699  0.01152  155 ASP A CB  
1143 C CG  . ASP A 150 ? 0.25829 0.17896 0.16068 -0.03992 0.07692  0.01818  155 ASP A CG  
1144 O OD1 . ASP A 150 ? 0.19412 0.17748 0.19512 -0.04896 0.05113  -0.01327 155 ASP A OD1 
1145 O OD2 . ASP A 150 ? 0.36362 0.22412 0.18579 0.05426  0.10319  0.02436  155 ASP A OD2 
1146 N N   . LEU A 151 ? 0.11360 0.12781 0.10939 -0.02811 0.00489  0.02185  156 LEU A N   
1147 C CA  . LEU A 151 ? 0.14337 0.11329 0.12380 -0.01828 0.01940  0.03010  156 LEU A CA  
1148 C C   . LEU A 151 ? 0.10970 0.09639 0.10871 -0.02691 0.03463  0.02690  156 LEU A C   
1149 O O   . LEU A 151 ? 0.11877 0.10449 0.10700 -0.03022 0.02606  0.00807  156 LEU A O   
1150 C CB  . LEU A 151 ? 0.21571 0.13389 0.16111 0.02008  0.02128  0.04991  156 LEU A CB  
1151 C CG  . LEU A 151 ? 0.20405 0.17055 0.20004 -0.02954 -0.01268 0.04657  156 LEU A CG  
1152 C CD1 . LEU A 151 ? 0.23372 0.10541 0.23902 -0.00459 -0.05359 0.03138  156 LEU A CD1 
1153 C CD2 . LEU A 151 ? 0.23214 0.23118 0.22897 -0.05270 0.00204  0.08398  156 LEU A CD2 
1154 N N   . ASN A 152 ? 0.10269 0.08387 0.12770 -0.01465 0.00307  -0.00232 157 ASN A N   
1155 C CA  . ASN A 152 ? 0.09575 0.09598 0.11544 -0.03070 0.01563  0.00332  157 ASN A CA  
1156 C C   . ASN A 152 ? 0.09067 0.10960 0.12580 -0.05262 0.02769  0.00244  157 ASN A C   
1157 O O   . ASN A 152 ? 0.14670 0.10486 0.14778 -0.03199 0.01920  0.00507  157 ASN A O   
1158 C CB  . ASN A 152 ? 0.10719 0.10907 0.12386 -0.03131 0.01972  0.01719  157 ASN A CB  
1159 C CG  . ASN A 152 ? 0.11189 0.11041 0.13120 -0.06292 0.01893  0.00873  157 ASN A CG  
1160 O OD1 . ASN A 152 ? 0.10446 0.13330 0.15599 -0.06160 0.03466  -0.00325 157 ASN A OD1 
1161 N ND2 . ASN A 152 ? 0.16354 0.09099 0.15450 -0.04500 0.03352  -0.00515 157 ASN A ND2 
1162 N N   . VAL A 153 ? 0.08432 0.09577 0.13565 -0.04753 0.00944  -0.00578 158 VAL A N   
1163 C CA  . VAL A 153 ? 0.09613 0.06620 0.13511 -0.03825 0.02243  0.00623  158 VAL A CA  
1164 C C   . VAL A 153 ? 0.11392 0.09158 0.12181 -0.01437 0.02560  -0.00506 158 VAL A C   
1165 O O   . VAL A 153 ? 0.12794 0.08025 0.11767 -0.01827 0.02262  0.00224  158 VAL A O   
1166 C CB  . VAL A 153 ? 0.09004 0.09571 0.17124 -0.02829 0.01123  -0.02372 158 VAL A CB  
1167 C CG1 . VAL A 153 ? 0.13736 0.07750 0.19915 -0.04755 -0.01365 -0.00341 158 VAL A CG1 
1168 C CG2 . VAL A 153 ? 0.10497 0.13251 0.19584 -0.01627 0.00718  -0.04252 158 VAL A CG2 
1169 N N   . ASN A 154 ? 0.12254 0.10060 0.12637 -0.02207 0.03139  -0.02190 159 ASN A N   
1170 C CA  . ASN A 154 ? 0.10300 0.13166 0.12858 0.00082  0.03665  0.00633  159 ASN A CA  
1171 C C   . ASN A 154 ? 0.11927 0.12763 0.12292 0.01892  0.02711  0.03011  159 ASN A C   
1172 O O   . ASN A 154 ? 0.13236 0.10450 0.13402 -0.00832 0.01543  0.01085  159 ASN A O   
1173 C CB  . ASN A 154 ? 0.12781 0.16984 0.14723 -0.01913 0.03438  0.04136  159 ASN A CB  
1174 C CG  . ASN A 154 ? 0.16123 0.17726 0.15248 0.00073  0.04038  0.03033  159 ASN A CG  
1175 O OD1 . ASN A 154 ? 0.17130 0.16291 0.17697 -0.01289 0.02932  0.01158  159 ASN A OD1 
1176 N ND2 . ASN A 154 ? 0.23226 0.21779 0.14544 0.00014  0.03764  0.02613  159 ASN A ND2 
1177 N N   . GLU A 155 ? 0.11313 0.11783 0.11637 -0.02316 0.02678  -0.00617 160 GLU A N   
1178 C CA  . GLU A 155 ? 0.11653 0.10006 0.13359 -0.03358 -0.01094 -0.01176 160 GLU A CA  
1179 C C   . GLU A 155 ? 0.10314 0.09347 0.12914 -0.01375 0.01094  0.00528  160 GLU A C   
1180 O O   . GLU A 155 ? 0.11155 0.11335 0.15464 0.00120  -0.00556 0.01910  160 GLU A O   
1181 C CB  . GLU A 155 ? 0.15725 0.09446 0.15090 -0.02032 -0.01382 -0.01053 160 GLU A CB  
1182 C CG  . GLU A 155 ? 0.18180 0.14342 0.18005 -0.04051 0.01479  0.03657  160 GLU A CG  
1183 C CD  . GLU A 155 ? 0.17506 0.17722 0.20360 -0.05917 0.07481  0.04110  160 GLU A CD  
1184 O OE1 . GLU A 155 ? 0.19752 0.13721 0.18837 -0.03565 0.07242  0.03195  160 GLU A OE1 
1185 O OE2 . GLU A 155 ? 0.23542 0.29230 0.23144 -0.02857 0.06750  0.03200  160 GLU A OE2 
1186 N N   . VAL A 156 ? 0.11335 0.08598 0.12527 -0.01564 0.01333  0.01482  161 VAL A N   
1187 C CA  . VAL A 156 ? 0.12322 0.11899 0.11725 -0.01507 0.01829  0.00616  161 VAL A CA  
1188 C C   . VAL A 156 ? 0.11203 0.09448 0.12878 -0.01170 0.00590  -0.00682 161 VAL A C   
1189 O O   . VAL A 156 ? 0.11518 0.10687 0.12453 -0.00544 -0.00339 -0.01430 161 VAL A O   
1190 C CB  . VAL A 156 ? 0.14939 0.09852 0.11968 -0.00600 0.02532  0.00775  161 VAL A CB  
1191 C CG1 . VAL A 156 ? 0.17528 0.08900 0.14226 -0.00994 0.00493  0.00807  161 VAL A CG1 
1192 C CG2 . VAL A 156 ? 0.16477 0.06275 0.13195 0.01875  0.02492  -0.00202 161 VAL A CG2 
1193 N N   . PHE A 157 ? 0.11687 0.07428 0.13522 -0.00324 0.01509  -0.01082 162 PHE A N   
1194 C CA  . PHE A 157 ? 0.10078 0.11068 0.13575 -0.00530 -0.00513 -0.03057 162 PHE A CA  
1195 C C   . PHE A 157 ? 0.09430 0.11689 0.17447 -0.00902 0.02279  -0.03390 162 PHE A C   
1196 O O   . PHE A 157 ? 0.11869 0.11624 0.18956 0.01565  0.01189  -0.00371 162 PHE A O   
1197 C CB  . PHE A 157 ? 0.11223 0.13873 0.13271 -0.00150 -0.00102 -0.03815 162 PHE A CB  
1198 C CG  . PHE A 157 ? 0.11295 0.09826 0.13191 -0.00412 -0.00066 -0.00362 162 PHE A CG  
1199 C CD1 . PHE A 157 ? 0.17650 0.10186 0.15177 -0.02860 0.01620  -0.00070 162 PHE A CD1 
1200 C CD2 . PHE A 157 ? 0.10965 0.12319 0.13486 0.01608  -0.01038 -0.01963 162 PHE A CD2 
1201 C CE1 . PHE A 157 ? 0.15007 0.12133 0.15228 -0.01475 0.02190  -0.00730 162 PHE A CE1 
1202 C CE2 . PHE A 157 ? 0.11994 0.12463 0.15354 -0.02069 0.01147  0.00586  162 PHE A CE2 
1203 C CZ  . PHE A 157 ? 0.10697 0.12544 0.16112 -0.02519 -0.00766 -0.01412 162 PHE A CZ  
1204 N N   . LYS A 158 ? 0.08855 0.12139 0.19475 -0.02891 0.03700  -0.01011 163 LYS A N   
1205 C CA  A LYS A 158 ? 0.10804 0.13060 0.19659 -0.01595 0.03726  -0.00398 163 LYS A CA  
1206 C CA  B LYS A 158 ? 0.10921 0.13285 0.19704 -0.01927 0.03419  0.00221  163 LYS A CA  
1207 C C   . LYS A 158 ? 0.10567 0.11307 0.18532 -0.01289 0.02296  -0.00789 163 LYS A C   
1208 O O   . LYS A 158 ? 0.11262 0.12905 0.19564 0.00580  0.02093  0.00879  163 LYS A O   
1209 C CB  A LYS A 158 ? 0.10150 0.16829 0.20723 -0.00994 0.07177  0.02294  163 LYS A CB  
1210 C CB  B LYS A 158 ? 0.10588 0.17307 0.20973 -0.02066 0.06263  0.04243  163 LYS A CB  
1211 C CG  A LYS A 158 ? 0.17386 0.22620 0.24456 0.01809  0.09330  0.00032  163 LYS A CG  
1212 C CG  B LYS A 158 ? 0.19048 0.23416 0.24674 -0.00098 0.07354  0.04049  163 LYS A CG  
1213 C CD  A LYS A 158 ? 0.22411 0.31572 0.28097 0.07538  0.10446  -0.01990 163 LYS A CD  
1214 C CD  B LYS A 158 ? 0.26428 0.32580 0.28261 0.05662  0.07341  0.03312  163 LYS A CD  
1215 C CE  A LYS A 158 ? 0.31803 0.41013 0.31638 0.13180  0.08508  -0.02634 163 LYS A CE  
1216 C CE  B LYS A 158 ? 0.32883 0.41152 0.30733 0.10971  0.06757  0.00692  163 LYS A CE  
1217 N NZ  A LYS A 158 ? 0.37757 0.44877 0.33449 0.16953  0.07823  -0.03360 163 LYS A NZ  
1218 N NZ  B LYS A 158 ? 0.36449 0.46804 0.32023 0.13500  0.07546  -0.00685 163 LYS A NZ  
1219 N N   . TYR A 159 ? 0.12509 0.13388 0.16665 -0.01053 0.02183  0.01475  164 TYR A N   
1220 C CA  . TYR A 159 ? 0.10808 0.13565 0.17372 0.00013  0.00712  0.01317  164 TYR A CA  
1221 C C   . TYR A 159 ? 0.12270 0.10423 0.17469 0.00829  0.00793  0.01606  164 TYR A C   
1222 O O   . TYR A 159 ? 0.10084 0.13394 0.19040 0.00540  0.00069  0.01874  164 TYR A O   
1223 C CB  . TYR A 159 ? 0.10639 0.11010 0.17423 -0.01410 0.00895  -0.01489 164 TYR A CB  
1224 C CG  . TYR A 159 ? 0.11236 0.12933 0.16731 -0.02511 0.01404  -0.02780 164 TYR A CG  
1225 C CD1 . TYR A 159 ? 0.14435 0.16086 0.18522 -0.01735 -0.01411 -0.00511 164 TYR A CD1 
1226 C CD2 . TYR A 159 ? 0.15685 0.14732 0.16549 0.01362  0.00614  -0.01963 164 TYR A CD2 
1227 C CE1 . TYR A 159 ? 0.13962 0.19116 0.18464 -0.00298 0.01915  -0.00043 164 TYR A CE1 
1228 C CE2 . TYR A 159 ? 0.10619 0.14799 0.17319 -0.02158 -0.00871 -0.03036 164 TYR A CE2 
1229 C CZ  . TYR A 159 ? 0.11212 0.18679 0.16910 -0.01502 0.00014  -0.00409 164 TYR A CZ  
1230 O OH  . TYR A 159 ? 0.13788 0.23722 0.18090 -0.00652 -0.00122 -0.00684 164 TYR A OH  
1231 N N   . LEU A 160 ? 0.10912 0.10635 0.17213 -0.00927 0.01654  0.01233  165 LEU A N   
1232 C CA  . LEU A 160 ? 0.10222 0.11143 0.17935 -0.02412 0.01919  -0.00770 165 LEU A CA  
1233 C C   . LEU A 160 ? 0.11513 0.09569 0.17336 0.00640  0.00300  -0.01749 165 LEU A C   
1234 O O   . LEU A 160 ? 0.11936 0.15404 0.18938 0.02395  -0.02449 0.01459  165 LEU A O   
1235 C CB  . LEU A 160 ? 0.09570 0.15184 0.18783 -0.01908 -0.00150 -0.01009 165 LEU A CB  
1236 C CG  . LEU A 160 ? 0.10857 0.13434 0.17650 0.00695  0.00830  -0.03474 165 LEU A CG  
1237 C CD1 . LEU A 160 ? 0.11745 0.14790 0.19842 -0.00726 0.00953  -0.03473 165 LEU A CD1 
1238 C CD2 . LEU A 160 ? 0.12877 0.16174 0.18807 0.03388  -0.00003 0.00179  165 LEU A CD2 
1239 N N   . ALA A 161 ? 0.08252 0.13891 0.16523 0.01038  0.02233  -0.02115 166 ALA A N   
1240 C CA  . ALA A 161 ? 0.12481 0.15605 0.19964 0.01576  0.00506  -0.01059 166 ALA A CA  
1241 C C   . ALA A 161 ? 0.12167 0.18462 0.22190 0.04084  -0.00643 0.02122  166 ALA A C   
1242 O O   . ALA A 161 ? 0.14748 0.18876 0.23873 0.06979  -0.00306 0.02378  166 ALA A O   
1243 C CB  . ALA A 161 ? 0.15389 0.16753 0.18234 0.04200  0.02026  0.01617  166 ALA A CB  
1244 N N   . GLU A 162 ? 0.10832 0.17442 0.23702 0.01555  0.00310  0.02648  167 GLU A N   
1245 C CA  . GLU A 162 ? 0.10732 0.22219 0.26369 0.00240  -0.00910 0.01374  167 GLU A CA  
1246 C C   . GLU A 162 ? 0.12965 0.18128 0.26403 0.03006  -0.02134 0.01273  167 GLU A C   
1247 O O   . GLU A 162 ? 0.14519 0.22282 0.28345 0.06196  -0.01562 0.01280  167 GLU A O   
1248 C CB  . GLU A 162 ? 0.14781 0.27403 0.30321 -0.02643 -0.00404 0.02944  167 GLU A CB  
1249 C CG  . GLU A 162 ? 0.18318 0.31931 0.33055 -0.04618 0.01503  0.05060  167 GLU A CG  
1250 C CD  . GLU A 162 ? 0.28829 0.40363 0.38179 -0.04674 0.03017  0.04557  167 GLU A CD  
1251 O OE1 . GLU A 162 ? 0.34096 0.37824 0.41347 -0.06230 0.02003  0.05367  167 GLU A OE1 
1252 O OE2 . GLU A 162 ? 0.32958 0.45280 0.39571 -0.03255 0.04287  0.06490  167 GLU A OE2 
1253 N N   . LYS A 163 ? 0.12647 0.20372 0.24765 0.01191  -0.02762 0.01239  168 LYS A N   
1254 C CA  A LYS A 163 ? 0.13916 0.22981 0.25613 -0.00673 -0.02655 0.03028  168 LYS A CA  
1255 C CA  B LYS A 163 ? 0.14904 0.22843 0.25949 -0.00467 -0.03037 0.02362  168 LYS A CA  
1256 C C   . LYS A 163 ? 0.15840 0.22888 0.26281 0.01842  -0.04872 0.02526  168 LYS A C   
1257 O O   . LYS A 163 ? 0.17531 0.26202 0.27884 0.02854  -0.05659 0.02778  168 LYS A O   
1258 C CB  A LYS A 163 ? 0.15424 0.26651 0.26213 -0.00074 -0.01703 0.02128  168 LYS A CB  
1259 C CB  B LYS A 163 ? 0.18195 0.25906 0.27193 0.00507  -0.02813 0.00120  168 LYS A CB  
1260 C CG  A LYS A 163 ? 0.13791 0.28931 0.26568 -0.00789 -0.02898 -0.00023 168 LYS A CG  
1261 C CG  B LYS A 163 ? 0.18745 0.26847 0.28087 -0.00486 -0.04883 -0.03815 168 LYS A CG  
1262 C CD  A LYS A 163 ? 0.16436 0.33647 0.28444 0.01615  -0.02166 -0.00709 168 LYS A CD  
1263 C CD  B LYS A 163 ? 0.19894 0.29364 0.30532 -0.00772 -0.05844 -0.03022 168 LYS A CD  
1264 C CE  A LYS A 163 ? 0.19868 0.37879 0.29318 0.04291  -0.01901 -0.01516 168 LYS A CE  
1265 C CE  B LYS A 163 ? 0.23072 0.33458 0.32177 0.01567  -0.06805 -0.02756 168 LYS A CE  
1266 N NZ  A LYS A 163 ? 0.20918 0.41477 0.29982 0.03482  0.00854  -0.01508 168 LYS A NZ  
1267 N NZ  B LYS A 163 ? 0.24576 0.39062 0.33031 0.04616  -0.06470 -0.02448 168 LYS A NZ  
1268 N N   . TYR A 164 ? 0.13157 0.19287 0.27046 -0.00243 -0.04857 0.05388  169 TYR A N   
1269 C CA  . TYR A 164 ? 0.16892 0.20737 0.31419 0.01351  -0.05681 0.03546  169 TYR A CA  
1270 C C   . TYR A 164 ? 0.16385 0.23276 0.33367 0.03684  -0.06621 0.04333  169 TYR A C   
1271 O O   . TYR A 164 ? 0.17763 0.25873 0.33418 0.04290  -0.07056 0.05714  169 TYR A O   
1272 C CB  . TYR A 164 ? 0.18996 0.16258 0.34158 -0.00672 -0.06208 0.04454  169 TYR A CB  
1273 C CG  . TYR A 164 ? 0.18530 0.14888 0.37535 0.01833  -0.07013 0.07102  169 TYR A CG  
1274 C CD1 . TYR A 164 ? 0.19434 0.16994 0.38030 -0.01688 -0.05501 0.09578  169 TYR A CD1 
1275 C CD2 . TYR A 164 ? 0.23481 0.21056 0.40365 0.03420  -0.06561 0.06424  169 TYR A CD2 
1276 C CE1 . TYR A 164 ? 0.24007 0.16097 0.40283 0.01778  -0.06321 0.06125  169 TYR A CE1 
1277 C CE2 . TYR A 164 ? 0.24656 0.20919 0.41838 0.05656  -0.06781 0.05548  169 TYR A CE2 
1278 C CZ  . TYR A 164 ? 0.25564 0.21353 0.43083 0.04081  -0.05418 0.06433  169 TYR A CZ  
1279 O OH  . TYR A 164 ? 0.30863 0.24602 0.46057 0.08432  -0.03080 0.06378  169 TYR A OH  
1280 N N   . LEU A 165 ? 0.16313 0.22204 0.35795 0.08396  -0.03805 0.03991  170 LEU A N   
1281 C CA  . LEU A 165 ? 0.17215 0.29359 0.39672 0.07328  -0.01894 0.05194  170 LEU A CA  
1282 C C   . LEU A 165 ? 0.17769 0.36596 0.44008 0.10279  -0.05118 0.05550  170 LEU A C   
1283 O O   . LEU A 165 ? 0.21625 0.41801 0.46475 0.13275  -0.03325 0.05736  170 LEU A O   
1284 C CB  . LEU A 165 ? 0.18601 0.28852 0.40165 0.08197  -0.00564 0.03187  170 LEU A CB  
1285 C CG  . LEU A 165 ? 0.27659 0.31712 0.41707 0.14177  0.01648  0.03427  170 LEU A CG  
1286 C CD1 . LEU A 165 ? 0.33038 0.34998 0.42593 0.12334  0.01906  0.03120  170 LEU A CD1 
1287 C CD2 . LEU A 165 ? 0.27584 0.32292 0.42815 0.16335  0.01968  0.02331  170 LEU A CD2 
1288 N N   . GLN A 166 ? 0.17892 0.39629 0.45943 0.06600  -0.09385 0.03482  171 GLN A N   
1289 C CA  . GLN A 166 ? 0.20524 0.45289 0.48829 0.06309  -0.10677 0.03604  171 GLN A CA  
1290 C C   . GLN A 166 ? 0.26884 0.49796 0.50604 0.12359  -0.11137 0.05172  171 GLN A C   
1291 O O   . GLN A 166 ? 0.35101 0.53470 0.52872 0.13645  -0.07660 0.06590  171 GLN A O   
1292 C CB  . GLN A 166 ? 0.20711 0.44082 0.49780 0.00799  -0.10847 0.02612  171 GLN A CB  
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