data_9CSW
# 
_entry.id   9CSW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   9CSW         pdb_00009csw 10.2210/pdb9csw/pdb 
WWPDB D_1000286229 ?            ?                   
# 
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 2024-12-11 
2 'Structure model' 1 1 2024-12-18 
3 'Structure model' 1 2 2025-01-01 
# 
_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        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_id_ISSN'         
2 2 'Structure model' '_citation.pdbx_database_id_DOI'    
3 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
4 2 'Structure model' '_citation.title'                   
5 2 'Structure model' '_citation_author.identifier_ORCID' 
6 3 'Structure model' '_citation.journal_volume'          
7 3 'Structure model' '_citation.page_first'              
8 3 'Structure model' '_citation.page_last'               
9 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CSW 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              aborovik@uci.edu 
_pdbx_contact_author.name_first         Andrew 
_pdbx_contact_author.name_last          Borovik 
_pdbx_contact_author.name_mi            S 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5049-9952 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Uyeda, K.S.'   1 0000-0002-3159-795X 
'Follmer, A.H.' 2 0000-0002-6244-6804 
'Borovik, A.S.' 3 0000-0001-5049-9952 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Chem Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-6520 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                98 
_citation.page_last                 103 
_citation.title                     'Selective oxidation of active site aromatic residues in engineered Cu proteins.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1039/d4sc06667g 
_citation.pdbx_database_id_PubMed   39600509 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Uyeda, K.S.'   1 ? 
primary 'Follmer, A.H.' 2 ? 
primary 'Borovik, A.S.' 3 ? 
# 
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 Streptavidin 16587.025 1   ? 'E101Q, S112A, K121Y' ? ? 
2 non-polymer syn 
'N-(2-{bis[(pyridin-2-yl)methyl]amino}ethyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide' 468.615   1 
? ?                     ? ? 
3 non-polymer syn 'COPPER (II) ION' 63.546    2   ? ?                     ? ? 
4 non-polymer syn 'ACETIC ACID' 60.052    1   ? ?                     ? ? 
5 water       nat water 18.015    103 ? ?                     ? ? 
# 
_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       
;MASMTGGQQMGRDEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRYDSAPATDGSGTALGWTVAWK
NNYRNAHSATTWSGQYVGGAQARINTQWLLTAGTTEANAWYSTLVGHDTFTKVKPSAASIDAAKKAGVNNGNPLDAVQQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MASMTGGQQMGRDEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRYDSAPATDGSGTALGWTVAWK
NNYRNAHSATTWSGQYVGGAQARINTQWLLTAGTTEANAWYSTLVGHDTFTKVKPSAASIDAAKKAGVNNGNPLDAVQQ
;
_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 'N-(2-{bis[(pyridin-2-yl)methyl]amino}ethyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide' QG7 
3 'COPPER (II) ION'                                                                                                      CU  
4 'ACETIC ACID'                                                                                                          ACY 
5 water                                                                                                                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   SER n 
1 4   MET n 
1 5   THR n 
1 6   GLY n 
1 7   GLY n 
1 8   GLN n 
1 9   GLN n 
1 10  MET n 
1 11  GLY n 
1 12  ARG n 
1 13  ASP n 
1 14  GLU n 
1 15  ALA n 
1 16  GLY n 
1 17  ILE n 
1 18  THR n 
1 19  GLY n 
1 20  THR n 
1 21  TRP n 
1 22  TYR n 
1 23  ASN n 
1 24  GLN n 
1 25  LEU n 
1 26  GLY n 
1 27  SER n 
1 28  THR n 
1 29  PHE n 
1 30  ILE n 
1 31  VAL n 
1 32  THR n 
1 33  ALA n 
1 34  GLY n 
1 35  ALA n 
1 36  ASP n 
1 37  GLY n 
1 38  ALA n 
1 39  LEU n 
1 40  THR n 
1 41  GLY n 
1 42  THR n 
1 43  TYR n 
1 44  GLU n 
1 45  SER n 
1 46  ALA n 
1 47  VAL n 
1 48  GLY n 
1 49  ASN n 
1 50  ALA n 
1 51  GLU n 
1 52  SER n 
1 53  ARG n 
1 54  TYR n 
1 55  VAL n 
1 56  LEU n 
1 57  THR n 
1 58  GLY n 
1 59  ARG n 
1 60  TYR n 
1 61  ASP n 
1 62  SER n 
1 63  ALA n 
1 64  PRO n 
1 65  ALA n 
1 66  THR n 
1 67  ASP n 
1 68  GLY n 
1 69  SER n 
1 70  GLY n 
1 71  THR n 
1 72  ALA n 
1 73  LEU n 
1 74  GLY n 
1 75  TRP n 
1 76  THR n 
1 77  VAL n 
1 78  ALA n 
1 79  TRP n 
1 80  LYS n 
1 81  ASN n 
1 82  ASN n 
1 83  TYR n 
1 84  ARG n 
1 85  ASN n 
1 86  ALA n 
1 87  HIS n 
1 88  SER n 
1 89  ALA n 
1 90  THR n 
1 91  THR n 
1 92  TRP n 
1 93  SER n 
1 94  GLY n 
1 95  GLN n 
1 96  TYR n 
1 97  VAL n 
1 98  GLY n 
1 99  GLY n 
1 100 ALA n 
1 101 GLN n 
1 102 ALA n 
1 103 ARG n 
1 104 ILE n 
1 105 ASN n 
1 106 THR n 
1 107 GLN n 
1 108 TRP n 
1 109 LEU n 
1 110 LEU n 
1 111 THR n 
1 112 ALA n 
1 113 GLY n 
1 114 THR n 
1 115 THR n 
1 116 GLU n 
1 117 ALA n 
1 118 ASN n 
1 119 ALA n 
1 120 TRP n 
1 121 TYR n 
1 122 SER n 
1 123 THR n 
1 124 LEU n 
1 125 VAL n 
1 126 GLY n 
1 127 HIS n 
1 128 ASP n 
1 129 THR n 
1 130 PHE n 
1 131 THR n 
1 132 LYS n 
1 133 VAL n 
1 134 LYS n 
1 135 PRO n 
1 136 SER n 
1 137 ALA n 
1 138 ALA n 
1 139 SER n 
1 140 ILE n 
1 141 ASP n 
1 142 ALA n 
1 143 ALA n 
1 144 LYS n 
1 145 LYS n 
1 146 ALA n 
1 147 GLY n 
1 148 VAL n 
1 149 ASN n 
1 150 ASN n 
1 151 GLY n 
1 152 ASN n 
1 153 PRO n 
1 154 LEU n 
1 155 ASP n 
1 156 ALA n 
1 157 VAL n 
1 158 GLN n 
1 159 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   159 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Streptomyces avidinii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1895 
_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 BL21' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_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 
ACY non-polymer         . 'ACETIC ACID' ? 'C2 H4 O2'        60.052  
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 
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'            63.546  
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
QG7 non-polymer         . 
'N-(2-{bis[(pyridin-2-yl)methyl]amino}ethyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide' ? 
'C24 H32 N6 O2 S' 468.615 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   MET 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   GLY 7   7   ?   ?   ?   A . n 
A 1 8   GLN 8   8   ?   ?   ?   A . n 
A 1 9   GLN 9   9   ?   ?   ?   A . n 
A 1 10  MET 10  10  ?   ?   ?   A . n 
A 1 11  GLY 11  11  ?   ?   ?   A . n 
A 1 12  ARG 12  12  12  ARG ARG A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  TRP 21  21  21  TRP TRP A . n 
A 1 22  TYR 22  22  22  TYR TYR A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  THR 28  28  28  THR THR A . n 
A 1 29  PHE 29  29  29  PHE PHE A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  TYR 43  43  43  TYR TYR A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  TYR 60  60  60  TYR TYR A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  TRP 75  75  75  TRP TRP A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  ASN 81  81  81  ASN ASN A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  HIS 87  87  87  HIS HIS A . n 
A 1 88  SER 88  88  88  SER SER A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  TRP 92  92  92  TRP TRP A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  GLN 95  95  95  GLN GLN A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 GLN 101 101 101 GLN GLN A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 TRP 108 108 108 TRP TRP A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 THR 114 114 114 THR THR A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 TRP 120 120 120 TRP TRP A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 SER 122 122 122 SER SER A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 HIS 127 127 127 HIS HIS A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 PRO 135 135 ?   ?   ?   A . n 
A 1 136 SER 136 136 ?   ?   ?   A . n 
A 1 137 ALA 137 137 ?   ?   ?   A . n 
A 1 138 ALA 138 138 ?   ?   ?   A . n 
A 1 139 SER 139 139 ?   ?   ?   A . n 
A 1 140 ILE 140 140 ?   ?   ?   A . n 
A 1 141 ASP 141 141 ?   ?   ?   A . n 
A 1 142 ALA 142 142 ?   ?   ?   A . n 
A 1 143 ALA 143 143 ?   ?   ?   A . n 
A 1 144 LYS 144 144 ?   ?   ?   A . n 
A 1 145 LYS 145 145 ?   ?   ?   A . n 
A 1 146 ALA 146 146 ?   ?   ?   A . n 
A 1 147 GLY 147 147 ?   ?   ?   A . n 
A 1 148 VAL 148 148 ?   ?   ?   A . n 
A 1 149 ASN 149 149 ?   ?   ?   A . n 
A 1 150 ASN 150 150 ?   ?   ?   A . n 
A 1 151 GLY 151 151 ?   ?   ?   A . n 
A 1 152 ASN 152 152 ?   ?   ?   A . n 
A 1 153 PRO 153 153 ?   ?   ?   A . n 
A 1 154 LEU 154 154 ?   ?   ?   A . n 
A 1 155 ASP 155 155 ?   ?   ?   A . n 
A 1 156 ALA 156 156 ?   ?   ?   A . n 
A 1 157 VAL 157 157 ?   ?   ?   A . n 
A 1 158 GLN 158 158 ?   ?   ?   A . n 
A 1 159 GLN 159 159 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ACY ? ? ACY ? ? 'SUBJECT OF INVESTIGATION' ? 
2 QG7 ? ? QG7 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 QG7 1   201 201 QG7 UYE A . 
C 3 CU  1   202 2   CU  CU  A . 
D 4 ACY 1   203 3   ACY ACT A . 
E 3 CU  1   204 1   CU  CU  A . 
F 5 HOH 1   301 103 HOH HOH A . 
F 5 HOH 2   302 44  HOH HOH A . 
F 5 HOH 3   303 35  HOH HOH A . 
F 5 HOH 4   304 70  HOH HOH A . 
F 5 HOH 5   305 4   HOH HOH A . 
F 5 HOH 6   306 21  HOH HOH A . 
F 5 HOH 7   307 40  HOH HOH A . 
F 5 HOH 8   308 77  HOH HOH A . 
F 5 HOH 9   309 72  HOH HOH A . 
F 5 HOH 10  310 101 HOH HOH A . 
F 5 HOH 11  311 99  HOH HOH A . 
F 5 HOH 12  312 19  HOH HOH A . 
F 5 HOH 13  313 15  HOH HOH A . 
F 5 HOH 14  314 25  HOH HOH A . 
F 5 HOH 15  315 13  HOH HOH A . 
F 5 HOH 16  316 67  HOH HOH A . 
F 5 HOH 17  317 2   HOH HOH A . 
F 5 HOH 18  318 6   HOH HOH A . 
F 5 HOH 19  319 62  HOH HOH A . 
F 5 HOH 20  320 107 HOH HOH A . 
F 5 HOH 21  321 60  HOH HOH A . 
F 5 HOH 22  322 26  HOH HOH A . 
F 5 HOH 23  323 28  HOH HOH A . 
F 5 HOH 24  324 33  HOH HOH A . 
F 5 HOH 25  325 39  HOH HOH A . 
F 5 HOH 26  326 23  HOH HOH A . 
F 5 HOH 27  327 66  HOH HOH A . 
F 5 HOH 28  328 58  HOH HOH A . 
F 5 HOH 29  329 7   HOH HOH A . 
F 5 HOH 30  330 75  HOH HOH A . 
F 5 HOH 31  331 100 HOH HOH A . 
F 5 HOH 32  332 48  HOH HOH A . 
F 5 HOH 33  333 11  HOH HOH A . 
F 5 HOH 34  334 3   HOH HOH A . 
F 5 HOH 35  335 8   HOH HOH A . 
F 5 HOH 36  336 76  HOH HOH A . 
F 5 HOH 37  337 46  HOH HOH A . 
F 5 HOH 38  338 9   HOH HOH A . 
F 5 HOH 39  339 57  HOH HOH A . 
F 5 HOH 40  340 61  HOH HOH A . 
F 5 HOH 41  341 82  HOH HOH A . 
F 5 HOH 42  342 18  HOH HOH A . 
F 5 HOH 43  343 49  HOH HOH A . 
F 5 HOH 44  344 17  HOH HOH A . 
F 5 HOH 45  345 32  HOH HOH A . 
F 5 HOH 46  346 78  HOH HOH A . 
F 5 HOH 47  347 54  HOH HOH A . 
F 5 HOH 48  348 97  HOH HOH A . 
F 5 HOH 49  349 30  HOH HOH A . 
F 5 HOH 50  350 43  HOH HOH A . 
F 5 HOH 51  351 5   HOH HOH A . 
F 5 HOH 52  352 22  HOH HOH A . 
F 5 HOH 53  353 50  HOH HOH A . 
F 5 HOH 54  354 56  HOH HOH A . 
F 5 HOH 55  355 85  HOH HOH A . 
F 5 HOH 56  356 83  HOH HOH A . 
F 5 HOH 57  357 20  HOH HOH A . 
F 5 HOH 58  358 88  HOH HOH A . 
F 5 HOH 59  359 16  HOH HOH A . 
F 5 HOH 60  360 31  HOH HOH A . 
F 5 HOH 61  361 27  HOH HOH A . 
F 5 HOH 62  362 29  HOH HOH A . 
F 5 HOH 63  363 59  HOH HOH A . 
F 5 HOH 64  364 24  HOH HOH A . 
F 5 HOH 65  365 14  HOH HOH A . 
F 5 HOH 66  366 92  HOH HOH A . 
F 5 HOH 67  367 91  HOH HOH A . 
F 5 HOH 68  368 38  HOH HOH A . 
F 5 HOH 69  369 69  HOH HOH A . 
F 5 HOH 70  370 41  HOH HOH A . 
F 5 HOH 71  371 10  HOH HOH A . 
F 5 HOH 72  372 51  HOH HOH A . 
F 5 HOH 73  373 53  HOH HOH A . 
F 5 HOH 74  374 73  HOH HOH A . 
F 5 HOH 75  375 45  HOH HOH A . 
F 5 HOH 76  376 68  HOH HOH A . 
F 5 HOH 77  377 104 HOH HOH A . 
F 5 HOH 78  378 79  HOH HOH A . 
F 5 HOH 79  379 55  HOH HOH A . 
F 5 HOH 80  380 80  HOH HOH A . 
F 5 HOH 81  381 1   HOH HOH A . 
F 5 HOH 82  382 52  HOH HOH A . 
F 5 HOH 83  383 42  HOH HOH A . 
F 5 HOH 84  384 34  HOH HOH A . 
F 5 HOH 85  385 71  HOH HOH A . 
F 5 HOH 86  386 90  HOH HOH A . 
F 5 HOH 87  387 102 HOH HOH A . 
F 5 HOH 88  388 65  HOH HOH A . 
F 5 HOH 89  389 47  HOH HOH A . 
F 5 HOH 90  390 74  HOH HOH A . 
F 5 HOH 91  391 86  HOH HOH A . 
F 5 HOH 92  392 98  HOH HOH A . 
F 5 HOH 93  393 105 HOH HOH A . 
F 5 HOH 94  394 84  HOH HOH A . 
F 5 HOH 95  395 81  HOH HOH A . 
F 5 HOH 96  396 94  HOH HOH A . 
F 5 HOH 97  397 106 HOH HOH A . 
F 5 HOH 98  398 108 HOH HOH A . 
F 5 HOH 99  399 64  HOH HOH A . 
F 5 HOH 100 400 95  HOH HOH A . 
F 5 HOH 101 401 63  HOH HOH A . 
F 5 HOH 102 402 93  HOH HOH A . 
F 5 HOH 103 403 96  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? 7.4.0           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487-000 2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .               3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .               4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CSW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.770 
_cell.length_a_esd                 ? 
_cell.length_b                     57.770 
_cell.length_b_esd                 ? 
_cell.length_c                     184.250 
_cell.length_c_esd                 ? 
_cell.volume                       614910.957 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9CSW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                98 
_symmetry.space_group_name_Hall            'I 4bw 2bw' 
_symmetry.space_group_name_H-M             'I 41 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CSW 
_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             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.91 
_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              6 
_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    'ammonium sulfate, sodium acetate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-06 
_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   ? 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          17.17 
_reflns.entry_id                                       9CSW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.30 
_reflns.d_resolution_low                               42.08 
_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                                     38754 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.33 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                47.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          62.91 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.6537 
_reflns.pdbx_Rpim_I_all                                0.09512 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.957 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.6465 
_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                                    1.3 
_reflns_shell.d_res_low                                     1.349 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.26 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3812 
_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                               48.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               3.847 
_reflns_shell.pdbx_Rpim_I_all                               0.5524 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.607 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.08 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  3.806 
_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                               22.91 
_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                                 9CSW 
_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                            1.30 
_refine.ls_d_res_low                             42.08 
_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                     38754 
_refine.ls_number_reflns_R_free                  3707 
_refine.ls_number_reflns_R_work                  68494 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.91 
_refine.ls_percent_reflns_R_free                 5.13 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1672 
_refine.ls_R_factor_R_free                       0.1886 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1660 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       '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             1.1000 
_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                 19.9139 
_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                            0.1680 
_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                       1.30 
_refine_hist.d_res_low                        42.08 
_refine_hist.number_atoms_solvent             103 
_refine_hist.number_atoms_total               1068 
_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        926 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_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' ? 0.0080  ? 1025 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0535  ? 1409 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0921  ? 157  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0073  ? 177  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 21.6488 ? 158  ? 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' 1.30 1.32  . . 111 2373 88.15  . . . . 0.3655 . . . . . . . . . . . 0.4907 
'X-RAY DIFFRACTION' 1.32 1.34  . . 156 2660 99.68  . . . . 0.3037 . . . . . . . . . . . 0.3140 
'X-RAY DIFFRACTION' 1.34 1.36  . . 137 2639 99.89  . . . . 0.2781 . . . . . . . . . . . 0.2764 
'X-RAY DIFFRACTION' 1.36 1.38  . . 138 2673 100.00 . . . . 0.2722 . . . . . . . . . . . 0.2911 
'X-RAY DIFFRACTION' 1.38 1.40  . . 132 2677 99.93  . . . . 0.2463 . . . . . . . . . . . 0.3053 
'X-RAY DIFFRACTION' 1.40 1.42  . . 147 2644 99.93  . . . . 0.2615 . . . . . . . . . . . 0.2889 
'X-RAY DIFFRACTION' 1.42 1.45  . . 130 2675 99.36  . . . . 0.2455 . . . . . . . . . . . 0.2957 
'X-RAY DIFFRACTION' 1.45 1.47  . . 164 2606 99.14  . . . . 0.2170 . . . . . . . . . . . 0.2862 
'X-RAY DIFFRACTION' 1.47 1.50  . . 130 2657 99.29  . . . . 0.2108 . . . . . . . . . . . 0.2646 
'X-RAY DIFFRACTION' 1.50 1.53  . . 166 2645 99.86  . . . . 0.1875 . . . . . . . . . . . 0.1928 
'X-RAY DIFFRACTION' 1.53 1.56  . . 147 2668 100.00 . . . . 0.1401 . . . . . . . . . . . 0.1607 
'X-RAY DIFFRACTION' 1.56 1.60  . . 131 2703 99.96  . . . . 0.1360 . . . . . . . . . . . 0.1672 
'X-RAY DIFFRACTION' 1.60 1.64  . . 147 2620 100.00 . . . . 0.1344 . . . . . . . . . . . 0.1792 
'X-RAY DIFFRACTION' 1.64 1.68  . . 132 2687 99.96  . . . . 0.1369 . . . . . . . . . . . 0.1654 
'X-RAY DIFFRACTION' 1.68 1.73  . . 140 2640 100.00 . . . . 0.1404 . . . . . . . . . . . 0.1963 
'X-RAY DIFFRACTION' 1.73 1.79  . . 144 2663 99.89  . . . . 0.1420 . . . . . . . . . . . 0.1756 
'X-RAY DIFFRACTION' 1.79 1.85  . . 160 2652 99.93  . . . . 0.1328 . . . . . . . . . . . 0.1753 
'X-RAY DIFFRACTION' 1.85 1.93  . . 137 2544 95.75  . . . . 0.2044 . . . . . . . . . . . 0.1911 
'X-RAY DIFFRACTION' 1.93 2.02  . . 118 2609 97.18  . . . . 0.1547 . . . . . . . . . . . 0.2175 
'X-RAY DIFFRACTION' 2.02 2.12  . . 160 2603 98.75  . . . . 0.1428 . . . . . . . . . . . 0.1840 
'X-RAY DIFFRACTION' 2.12 2.26  . . 162 2594 97.73  . . . . 0.1790 . . . . . . . . . . . 0.1989 
'X-RAY DIFFRACTION' 2.26 2.43  . . 147 2604 98.25  . . . . 0.1590 . . . . . . . . . . . 0.1685 
'X-RAY DIFFRACTION' 2.43 2.67  . . 145 2663 99.96  . . . . 0.1595 . . . . . . . . . . . 0.1654 
'X-RAY DIFFRACTION' 2.67 3.06  . . 136 2675 99.89  . . . . 0.1647 . . . . . . . . . . . 0.1442 
'X-RAY DIFFRACTION' 3.06 3.86  . . 117 2684 99.54  . . . . 0.1551 . . . . . . . . . . . 0.1882 
'X-RAY DIFFRACTION' 3.86 42.08 . . 173 2636 99.89  . . . . 0.1525 . . . . . . . . . . . 0.1770 
# 
_struct.entry_id                     9CSW 
_struct.title                        'Streptavidin-E101Q-S112A-K121Y bound to Cu(II)-biotin-ethyl-dipicolylamine cofactor' 
_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        9CSW 
_struct_keywords.text            'biotin-streptavidin complex, artificial metalloprotein, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 3 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SAV_STRAV 
_struct_ref.pdbx_db_accession          P22629 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWS
GQYVGGAEARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAASIDAAKKAGVNNGNPLDAVQQ
;
_struct_ref.pdbx_align_begin           38 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9CSW 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 14 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 159 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P22629 
_struct_ref_seq.db_align_beg                  38 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  183 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       14 
_struct_ref_seq.pdbx_auth_seq_align_end       159 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CSW MET A 1   ? UNP P22629 ?   ?   'expression tag'      1   1  
1 9CSW ALA A 2   ? UNP P22629 ?   ?   'expression tag'      2   2  
1 9CSW SER A 3   ? UNP P22629 ?   ?   'expression tag'      3   3  
1 9CSW MET A 4   ? UNP P22629 ?   ?   'expression tag'      4   4  
1 9CSW THR A 5   ? UNP P22629 ?   ?   'expression tag'      5   5  
1 9CSW GLY A 6   ? UNP P22629 ?   ?   'expression tag'      6   6  
1 9CSW GLY A 7   ? UNP P22629 ?   ?   'expression tag'      7   7  
1 9CSW GLN A 8   ? UNP P22629 ?   ?   'expression tag'      8   8  
1 9CSW GLN A 9   ? UNP P22629 ?   ?   'expression tag'      9   9  
1 9CSW MET A 10  ? UNP P22629 ?   ?   'expression tag'      10  10 
1 9CSW GLY A 11  ? UNP P22629 ?   ?   'expression tag'      11  11 
1 9CSW ARG A 12  ? UNP P22629 ?   ?   'expression tag'      12  12 
1 9CSW ASP A 13  ? UNP P22629 ?   ?   'expression tag'      13  13 
1 9CSW GLN A 101 ? UNP P22629 GLU 125 'engineered mutation' 101 14 
1 9CSW ALA A 112 ? UNP P22629 SER 136 'engineered mutation' 112 15 
1 9CSW TYR A 121 ? UNP P22629 LYS 145 'engineered mutation' 121 16 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 10370 ? 
1 MORE         -135  ? 
1 'SSA (A^2)'  18990 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z        1.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
1.0000000000  0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 8_665  -y+1,-x+1,-z 0.0000000000  -1.0000000000 0.0000000000 57.7700000000 -1.0000000000 
0.0000000000  0.0000000000 57.7700000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
3 'crystal symmetry operation' 10_665 -x+1,-y+1,z  -1.0000000000 0.0000000000  0.0000000000 57.7700000000 0.0000000000  
-1.0000000000 0.0000000000 57.7700000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
4 'crystal symmetry operation' 15_555 y,x,-z       0.0000000000  1.0000000000  0.0000000000 0.0000000000  1.0000000000  
0.0000000000  0.0000000000 0.0000000000  0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 13  ? THR A 18  ? ASP A 13  THR A 18  1 ? 6 
HELX_P HELX_P2 AA2 THR A 115 ? TYR A 121 ? THR A 115 TYR A 121 5 ? 7 
# 
_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 HIS 87 NE2 ? ? ? 1_555 C CU  . CU ? ? A HIS 87  A CU  202 1_555 ? ? ? ? ? ? ? 2.466 ? ? 
metalc2 metalc ? ? B QG7 .  N3  ? ? ? 1_555 E CU  . CU ? ? A QG7 201 A CU  204 1_555 ? ? ? ? ? ? ? 2.145 ? ? 
metalc3 metalc ? ? B QG7 .  N4  ? ? ? 1_555 E CU  . CU ? ? A QG7 201 A CU  204 1_555 ? ? ? ? ? ? ? 1.963 ? ? 
metalc4 metalc ? ? B QG7 .  N5  ? ? ? 1_555 E CU  . CU ? ? A QG7 201 A CU  204 1_555 ? ? ? ? ? ? ? 1.932 ? ? 
metalc5 metalc ? ? D ACY .  OXT ? ? ? 1_555 E CU  . CU ? ? A ACY 203 A CU  204 1_555 ? ? ? ? ? ? ? 2.093 ? ? 
metalc6 metalc ? ? E CU  .  CU  ? ? ? 1_555 F HOH . O  ? ? A CU  204 A HOH 381 1_555 ? ? ? ? ? ? ? 2.614 ? ? 
# 
_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  N3  ? B QG7 . ? A QG7 201 ? 1_555 CU ? E CU . ? A CU 204 ? 1_555 N4  ? B QG7 . ? A QG7 201 ? 1_555 86.8  ? 
2  N3  ? B QG7 . ? A QG7 201 ? 1_555 CU ? E CU . ? A CU 204 ? 1_555 N5  ? B QG7 . ? A QG7 201 ? 1_555 77.6  ? 
3  N4  ? B QG7 . ? A QG7 201 ? 1_555 CU ? E CU . ? A CU 204 ? 1_555 N5  ? B QG7 . ? A QG7 201 ? 1_555 163.4 ? 
4  N3  ? B QG7 . ? A QG7 201 ? 1_555 CU ? E CU . ? A CU 204 ? 1_555 OXT ? D ACY . ? A ACY 203 ? 1_555 175.5 ? 
5  N4  ? B QG7 . ? A QG7 201 ? 1_555 CU ? E CU . ? A CU 204 ? 1_555 OXT ? D ACY . ? A ACY 203 ? 1_555 91.8  ? 
6  N5  ? B QG7 . ? A QG7 201 ? 1_555 CU ? E CU . ? A CU 204 ? 1_555 OXT ? D ACY . ? A ACY 203 ? 1_555 104.2 ? 
7  N3  ? B QG7 . ? A QG7 201 ? 1_555 CU ? E CU . ? A CU 204 ? 1_555 O   ? F HOH . ? A HOH 381 ? 1_555 97.2  ? 
8  N4  ? B QG7 . ? A QG7 201 ? 1_555 CU ? E CU . ? A CU 204 ? 1_555 O   ? F HOH . ? A HOH 381 ? 1_555 87.6  ? 
9  N5  ? B QG7 . ? A QG7 201 ? 1_555 CU ? E CU . ? A CU 204 ? 1_555 O   ? F HOH . ? A HOH 381 ? 1_555 88.7  ? 
10 OXT ? D ACY . ? A ACY 203 ? 1_555 CU ? E CU . ? A CU 204 ? 1_555 O   ? F HOH . ? A HOH 381 ? 1_555 87.0  ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   9 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY A 19  ? ASN A 23  ? GLY A 19  ASN A 23  
AA1 2 THR A 28  ? ALA A 33  ? THR A 28  ALA A 33  
AA1 3 ALA A 38  ? GLU A 44  ? ALA A 38  GLU A 44  
AA1 4 TYR A 54  ? TYR A 60  ? TYR A 54  TYR A 60  
AA1 5 THR A 71  ? LYS A 80  ? THR A 71  LYS A 80  
AA1 6 ASN A 85  ? VAL A 97  ? ASN A 85  VAL A 97  
AA1 7 ARG A 103 ? ALA A 112 ? ARG A 103 ALA A 112 
AA1 8 THR A 123 ? THR A 131 ? THR A 123 THR A 131 
AA1 9 GLY A 19  ? ASN A 23  ? GLY A 19  ASN A 23  
# 
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 TRP A 21  ? N TRP A 21  O PHE A 29  ? O PHE A 29  
AA1 2 3 N ILE A 30  ? N ILE A 30  O THR A 42  ? O THR A 42  
AA1 3 4 N TYR A 43  ? N TYR A 43  O TYR A 54  ? O TYR A 54  
AA1 4 5 N THR A 57  ? N THR A 57  O THR A 76  ? O THR A 76  
AA1 5 6 N TRP A 79  ? N TRP A 79  O SER A 88  ? O SER A 88  
AA1 6 7 N VAL A 97  ? N VAL A 97  O ARG A 103 ? O ARG A 103 
AA1 7 8 N ILE A 104 ? N ILE A 104 O PHE A 130 ? O PHE A 130 
AA1 8 9 O THR A 131 ? O THR A 131 N TYR A 22  ? N TYR A 22  
# 
_pdbx_entry_details.entry_id                   9CSW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    309 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    310 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.92 
# 
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 SER A 52  ? ? 62.94   -156.65 
2 1 TRP A 79  ? ? -83.65  49.10   
3 1 GLN A 101 ? ? -115.50 62.55   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     314 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z                
2  -y+1/2,x,z+3/4       
3  y+1/2,-x,z+3/4       
4  x+1/2,-y,-z+3/4      
5  -x+1/2,y,-z+3/4      
6  -x,-y,z              
7  y,x,-z               
8  -y,-x,-z             
9  x+1/2,y+1/2,z+1/2    
10 -y+1,x+1/2,z+5/4     
11 y+1,-x+1/2,z+5/4     
12 x+1,-y+1/2,-z+5/4    
13 -x+1,y+1/2,-z+5/4    
14 -x+1/2,-y+1/2,z+1/2  
15 y+1/2,x+1/2,-z+1/2   
16 -y+1/2,-x+1/2,-z+1/2 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       403 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.15 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 MET 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A SER 3   ? A SER 3   
4  1 Y 1 A MET 4   ? A MET 4   
5  1 Y 1 A THR 5   ? A THR 5   
6  1 Y 1 A GLY 6   ? A GLY 6   
7  1 Y 1 A GLY 7   ? A GLY 7   
8  1 Y 1 A GLN 8   ? A GLN 8   
9  1 Y 1 A GLN 9   ? A GLN 9   
10 1 Y 1 A MET 10  ? A MET 10  
11 1 Y 1 A GLY 11  ? A GLY 11  
12 1 Y 1 A PRO 135 ? A PRO 135 
13 1 Y 1 A SER 136 ? A SER 136 
14 1 Y 1 A ALA 137 ? A ALA 137 
15 1 Y 1 A ALA 138 ? A ALA 138 
16 1 Y 1 A SER 139 ? A SER 139 
17 1 Y 1 A ILE 140 ? A ILE 140 
18 1 Y 1 A ASP 141 ? A ASP 141 
19 1 Y 1 A ALA 142 ? A ALA 142 
20 1 Y 1 A ALA 143 ? A ALA 143 
21 1 Y 1 A LYS 144 ? A LYS 144 
22 1 Y 1 A LYS 145 ? A LYS 145 
23 1 Y 1 A ALA 146 ? A ALA 146 
24 1 Y 1 A GLY 147 ? A GLY 147 
25 1 Y 1 A VAL 148 ? A VAL 148 
26 1 Y 1 A ASN 149 ? A ASN 149 
27 1 Y 1 A ASN 150 ? A ASN 150 
28 1 Y 1 A GLY 151 ? A GLY 151 
29 1 Y 1 A ASN 152 ? A ASN 152 
30 1 Y 1 A PRO 153 ? A PRO 153 
31 1 Y 1 A LEU 154 ? A LEU 154 
32 1 Y 1 A ASP 155 ? A ASP 155 
33 1 Y 1 A ALA 156 ? A ALA 156 
34 1 Y 1 A VAL 157 ? A VAL 157 
35 1 Y 1 A GLN 158 ? A GLN 158 
36 1 Y 1 A GLN 159 ? A GLN 159 
# 
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 
ACY C    C  N N 1   
ACY O    O  N N 2   
ACY OXT  O  N N 3   
ACY CH3  C  N N 4   
ACY HXT  H  N N 5   
ACY H1   H  N N 6   
ACY H2   H  N N 7   
ACY H3   H  N N 8   
ALA N    N  N N 9   
ALA CA   C  N S 10  
ALA C    C  N N 11  
ALA O    O  N N 12  
ALA CB   C  N N 13  
ALA OXT  O  N N 14  
ALA H    H  N N 15  
ALA H2   H  N N 16  
ALA HA   H  N N 17  
ALA HB1  H  N N 18  
ALA HB2  H  N N 19  
ALA HB3  H  N N 20  
ALA HXT  H  N N 21  
ARG N    N  N N 22  
ARG CA   C  N S 23  
ARG C    C  N N 24  
ARG O    O  N N 25  
ARG CB   C  N N 26  
ARG CG   C  N N 27  
ARG CD   C  N N 28  
ARG NE   N  N N 29  
ARG CZ   C  N N 30  
ARG NH1  N  N N 31  
ARG NH2  N  N N 32  
ARG OXT  O  N N 33  
ARG H    H  N N 34  
ARG H2   H  N N 35  
ARG HA   H  N N 36  
ARG HB2  H  N N 37  
ARG HB3  H  N N 38  
ARG HG2  H  N N 39  
ARG HG3  H  N N 40  
ARG HD2  H  N N 41  
ARG HD3  H  N N 42  
ARG HE   H  N N 43  
ARG HH11 H  N N 44  
ARG HH12 H  N N 45  
ARG HH21 H  N N 46  
ARG HH22 H  N N 47  
ARG HXT  H  N N 48  
ASN N    N  N N 49  
ASN CA   C  N S 50  
ASN C    C  N N 51  
ASN O    O  N N 52  
ASN CB   C  N N 53  
ASN CG   C  N N 54  
ASN OD1  O  N N 55  
ASN ND2  N  N N 56  
ASN OXT  O  N N 57  
ASN H    H  N N 58  
ASN H2   H  N N 59  
ASN HA   H  N N 60  
ASN HB2  H  N N 61  
ASN HB3  H  N N 62  
ASN HD21 H  N N 63  
ASN HD22 H  N N 64  
ASN HXT  H  N N 65  
ASP N    N  N N 66  
ASP CA   C  N S 67  
ASP C    C  N N 68  
ASP O    O  N N 69  
ASP CB   C  N N 70  
ASP CG   C  N N 71  
ASP OD1  O  N N 72  
ASP OD2  O  N N 73  
ASP OXT  O  N N 74  
ASP H    H  N N 75  
ASP H2   H  N N 76  
ASP HA   H  N N 77  
ASP HB2  H  N N 78  
ASP HB3  H  N N 79  
ASP HD2  H  N N 80  
ASP HXT  H  N N 81  
CU  CU   CU N N 82  
GLN N    N  N N 83  
GLN CA   C  N S 84  
GLN C    C  N N 85  
GLN O    O  N N 86  
GLN CB   C  N N 87  
GLN CG   C  N N 88  
GLN CD   C  N N 89  
GLN OE1  O  N N 90  
GLN NE2  N  N N 91  
GLN OXT  O  N N 92  
GLN H    H  N N 93  
GLN H2   H  N N 94  
GLN HA   H  N N 95  
GLN HB2  H  N N 96  
GLN HB3  H  N N 97  
GLN HG2  H  N N 98  
GLN HG3  H  N N 99  
GLN HE21 H  N N 100 
GLN HE22 H  N N 101 
GLN HXT  H  N N 102 
GLU N    N  N N 103 
GLU CA   C  N S 104 
GLU C    C  N N 105 
GLU O    O  N N 106 
GLU CB   C  N N 107 
GLU CG   C  N N 108 
GLU CD   C  N N 109 
GLU OE1  O  N N 110 
GLU OE2  O  N N 111 
GLU OXT  O  N N 112 
GLU H    H  N N 113 
GLU H2   H  N N 114 
GLU HA   H  N N 115 
GLU HB2  H  N N 116 
GLU HB3  H  N N 117 
GLU HG2  H  N N 118 
GLU HG3  H  N N 119 
GLU HE2  H  N N 120 
GLU HXT  H  N N 121 
GLY N    N  N N 122 
GLY CA   C  N N 123 
GLY C    C  N N 124 
GLY O    O  N N 125 
GLY OXT  O  N N 126 
GLY H    H  N N 127 
GLY H2   H  N N 128 
GLY HA2  H  N N 129 
GLY HA3  H  N N 130 
GLY HXT  H  N N 131 
HIS N    N  N N 132 
HIS CA   C  N S 133 
HIS C    C  N N 134 
HIS O    O  N N 135 
HIS CB   C  N N 136 
HIS CG   C  Y N 137 
HIS ND1  N  Y N 138 
HIS CD2  C  Y N 139 
HIS CE1  C  Y N 140 
HIS NE2  N  Y N 141 
HIS OXT  O  N N 142 
HIS H    H  N N 143 
HIS H2   H  N N 144 
HIS HA   H  N N 145 
HIS HB2  H  N N 146 
HIS HB3  H  N N 147 
HIS HD1  H  N N 148 
HIS HD2  H  N N 149 
HIS HE1  H  N N 150 
HIS HE2  H  N N 151 
HIS HXT  H  N N 152 
HOH O    O  N N 153 
HOH H1   H  N N 154 
HOH H2   H  N N 155 
ILE N    N  N N 156 
ILE CA   C  N S 157 
ILE C    C  N N 158 
ILE O    O  N N 159 
ILE CB   C  N S 160 
ILE CG1  C  N N 161 
ILE CG2  C  N N 162 
ILE CD1  C  N N 163 
ILE OXT  O  N N 164 
ILE H    H  N N 165 
ILE H2   H  N N 166 
ILE HA   H  N N 167 
ILE HB   H  N N 168 
ILE HG12 H  N N 169 
ILE HG13 H  N N 170 
ILE HG21 H  N N 171 
ILE HG22 H  N N 172 
ILE HG23 H  N N 173 
ILE HD11 H  N N 174 
ILE HD12 H  N N 175 
ILE HD13 H  N N 176 
ILE HXT  H  N N 177 
LEU N    N  N N 178 
LEU CA   C  N S 179 
LEU C    C  N N 180 
LEU O    O  N N 181 
LEU CB   C  N N 182 
LEU CG   C  N N 183 
LEU CD1  C  N N 184 
LEU CD2  C  N N 185 
LEU OXT  O  N N 186 
LEU H    H  N N 187 
LEU H2   H  N N 188 
LEU HA   H  N N 189 
LEU HB2  H  N N 190 
LEU HB3  H  N N 191 
LEU HG   H  N N 192 
LEU HD11 H  N N 193 
LEU HD12 H  N N 194 
LEU HD13 H  N N 195 
LEU HD21 H  N N 196 
LEU HD22 H  N N 197 
LEU HD23 H  N N 198 
LEU HXT  H  N N 199 
LYS N    N  N N 200 
LYS CA   C  N S 201 
LYS C    C  N N 202 
LYS O    O  N N 203 
LYS CB   C  N N 204 
LYS CG   C  N N 205 
LYS CD   C  N N 206 
LYS CE   C  N N 207 
LYS NZ   N  N N 208 
LYS OXT  O  N N 209 
LYS H    H  N N 210 
LYS H2   H  N N 211 
LYS HA   H  N N 212 
LYS HB2  H  N N 213 
LYS HB3  H  N N 214 
LYS HG2  H  N N 215 
LYS HG3  H  N N 216 
LYS HD2  H  N N 217 
LYS HD3  H  N N 218 
LYS HE2  H  N N 219 
LYS HE3  H  N N 220 
LYS HZ1  H  N N 221 
LYS HZ2  H  N N 222 
LYS HZ3  H  N N 223 
LYS HXT  H  N N 224 
MET N    N  N N 225 
MET CA   C  N S 226 
MET C    C  N N 227 
MET O    O  N N 228 
MET CB   C  N N 229 
MET CG   C  N N 230 
MET SD   S  N N 231 
MET CE   C  N N 232 
MET OXT  O  N N 233 
MET H    H  N N 234 
MET H2   H  N N 235 
MET HA   H  N N 236 
MET HB2  H  N N 237 
MET HB3  H  N N 238 
MET HG2  H  N N 239 
MET HG3  H  N N 240 
MET HE1  H  N N 241 
MET HE2  H  N N 242 
MET HE3  H  N N 243 
MET HXT  H  N N 244 
PHE N    N  N N 245 
PHE CA   C  N S 246 
PHE C    C  N N 247 
PHE O    O  N N 248 
PHE CB   C  N N 249 
PHE CG   C  Y N 250 
PHE CD1  C  Y N 251 
PHE CD2  C  Y N 252 
PHE CE1  C  Y N 253 
PHE CE2  C  Y N 254 
PHE CZ   C  Y N 255 
PHE OXT  O  N N 256 
PHE H    H  N N 257 
PHE H2   H  N N 258 
PHE HA   H  N N 259 
PHE HB2  H  N N 260 
PHE HB3  H  N N 261 
PHE HD1  H  N N 262 
PHE HD2  H  N N 263 
PHE HE1  H  N N 264 
PHE HE2  H  N N 265 
PHE HZ   H  N N 266 
PHE HXT  H  N N 267 
PRO N    N  N N 268 
PRO CA   C  N S 269 
PRO C    C  N N 270 
PRO O    O  N N 271 
PRO CB   C  N N 272 
PRO CG   C  N N 273 
PRO CD   C  N N 274 
PRO OXT  O  N N 275 
PRO H    H  N N 276 
PRO HA   H  N N 277 
PRO HB2  H  N N 278 
PRO HB3  H  N N 279 
PRO HG2  H  N N 280 
PRO HG3  H  N N 281 
PRO HD2  H  N N 282 
PRO HD3  H  N N 283 
PRO HXT  H  N N 284 
QG7 C10  C  N S 285 
QG7 C15  C  Y N 286 
QG7 C17  C  N N 287 
QG7 C11  C  N N 288 
QG7 C12  C  Y N 289 
QG7 C14  C  Y N 290 
QG7 O2   O  N N 291 
QG7 C9   C  N N 292 
QG7 N1   N  N N 293 
QG7 N2   N  N N 294 
QG7 C8   C  N R 295 
QG7 C7   C  N N 296 
QG7 S1   S  N N 297 
QG7 C6   C  N S 298 
QG7 C5   C  N N 299 
QG7 C4   C  N N 300 
QG7 C3   C  N N 301 
QG7 C2   C  N N 302 
QG7 C1   C  N N 303 
QG7 C24  C  N N 304 
QG7 O1   O  N N 305 
QG7 N6   N  N N 306 
QG7 C23  C  N N 307 
QG7 N3   N  N N 308 
QG7 N4   N  Y N 309 
QG7 C16  C  Y N 310 
QG7 C13  C  Y N 311 
QG7 N5   N  Y N 312 
QG7 C18  C  Y N 313 
QG7 C22  C  Y N 314 
QG7 C21  C  Y N 315 
QG7 C20  C  Y N 316 
QG7 C19  C  Y N 317 
QG7 H1   H  N N 318 
QG7 H2   H  N N 319 
QG7 H3   H  N N 320 
QG7 H4   H  N N 321 
QG7 H5   H  N N 322 
QG7 H6   H  N N 323 
QG7 H7   H  N N 324 
QG7 H8   H  N N 325 
QG7 H9   H  N N 326 
QG7 H10  H  N N 327 
QG7 H11  H  N N 328 
QG7 H12  H  N N 329 
QG7 H13  H  N N 330 
QG7 H14  H  N N 331 
QG7 H15  H  N N 332 
QG7 H16  H  N N 333 
QG7 H17  H  N N 334 
QG7 H18  H  N N 335 
QG7 H19  H  N N 336 
QG7 H20  H  N N 337 
QG7 H21  H  N N 338 
QG7 H22  H  N N 339 
QG7 H23  H  N N 340 
QG7 H24  H  N N 341 
QG7 H25  H  N N 342 
QG7 H26  H  N N 343 
QG7 H28  H  N N 344 
QG7 H29  H  N N 345 
QG7 H30  H  N N 346 
QG7 H31  H  N N 347 
QG7 H32  H  N N 348 
QG7 H33  H  N N 349 
SER N    N  N N 350 
SER CA   C  N S 351 
SER C    C  N N 352 
SER O    O  N N 353 
SER CB   C  N N 354 
SER OG   O  N N 355 
SER OXT  O  N N 356 
SER H    H  N N 357 
SER H2   H  N N 358 
SER HA   H  N N 359 
SER HB2  H  N N 360 
SER HB3  H  N N 361 
SER HG   H  N N 362 
SER HXT  H  N N 363 
THR N    N  N N 364 
THR CA   C  N S 365 
THR C    C  N N 366 
THR O    O  N N 367 
THR CB   C  N R 368 
THR OG1  O  N N 369 
THR CG2  C  N N 370 
THR OXT  O  N N 371 
THR H    H  N N 372 
THR H2   H  N N 373 
THR HA   H  N N 374 
THR HB   H  N N 375 
THR HG1  H  N N 376 
THR HG21 H  N N 377 
THR HG22 H  N N 378 
THR HG23 H  N N 379 
THR HXT  H  N N 380 
TRP N    N  N N 381 
TRP CA   C  N S 382 
TRP C    C  N N 383 
TRP O    O  N N 384 
TRP CB   C  N N 385 
TRP CG   C  Y N 386 
TRP CD1  C  Y N 387 
TRP CD2  C  Y N 388 
TRP NE1  N  Y N 389 
TRP CE2  C  Y N 390 
TRP CE3  C  Y N 391 
TRP CZ2  C  Y N 392 
TRP CZ3  C  Y N 393 
TRP CH2  C  Y N 394 
TRP OXT  O  N N 395 
TRP H    H  N N 396 
TRP H2   H  N N 397 
TRP HA   H  N N 398 
TRP HB2  H  N N 399 
TRP HB3  H  N N 400 
TRP HD1  H  N N 401 
TRP HE1  H  N N 402 
TRP HE3  H  N N 403 
TRP HZ2  H  N N 404 
TRP HZ3  H  N N 405 
TRP HH2  H  N N 406 
TRP HXT  H  N N 407 
TYR N    N  N N 408 
TYR CA   C  N S 409 
TYR C    C  N N 410 
TYR O    O  N N 411 
TYR CB   C  N N 412 
TYR CG   C  Y N 413 
TYR CD1  C  Y N 414 
TYR CD2  C  Y N 415 
TYR CE1  C  Y N 416 
TYR CE2  C  Y N 417 
TYR CZ   C  Y N 418 
TYR OH   O  N N 419 
TYR OXT  O  N N 420 
TYR H    H  N N 421 
TYR H2   H  N N 422 
TYR HA   H  N N 423 
TYR HB2  H  N N 424 
TYR HB3  H  N N 425 
TYR HD1  H  N N 426 
TYR HD2  H  N N 427 
TYR HE1  H  N N 428 
TYR HE2  H  N N 429 
TYR HH   H  N N 430 
TYR HXT  H  N N 431 
VAL N    N  N N 432 
VAL CA   C  N S 433 
VAL C    C  N N 434 
VAL O    O  N N 435 
VAL CB   C  N N 436 
VAL CG1  C  N N 437 
VAL CG2  C  N N 438 
VAL OXT  O  N N 439 
VAL H    H  N N 440 
VAL H2   H  N N 441 
VAL HA   H  N N 442 
VAL HB   H  N N 443 
VAL HG11 H  N N 444 
VAL HG12 H  N N 445 
VAL HG13 H  N N 446 
VAL HG21 H  N N 447 
VAL HG22 H  N N 448 
VAL HG23 H  N N 449 
VAL HXT  H  N N 450 
# 
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 
ACY C   O    doub N N 1   
ACY C   OXT  sing N N 2   
ACY C   CH3  sing N N 3   
ACY OXT HXT  sing N N 4   
ACY CH3 H1   sing N N 5   
ACY CH3 H2   sing N N 6   
ACY CH3 H3   sing N N 7   
ALA N   CA   sing N N 8   
ALA N   H    sing N N 9   
ALA N   H2   sing N N 10  
ALA CA  C    sing N N 11  
ALA CA  CB   sing N N 12  
ALA CA  HA   sing N N 13  
ALA C   O    doub N N 14  
ALA C   OXT  sing N N 15  
ALA CB  HB1  sing N N 16  
ALA CB  HB2  sing N N 17  
ALA CB  HB3  sing N N 18  
ALA OXT HXT  sing N N 19  
ARG N   CA   sing N N 20  
ARG N   H    sing N N 21  
ARG N   H2   sing N N 22  
ARG CA  C    sing N N 23  
ARG CA  CB   sing N N 24  
ARG CA  HA   sing N N 25  
ARG C   O    doub N N 26  
ARG C   OXT  sing N N 27  
ARG CB  CG   sing N N 28  
ARG CB  HB2  sing N N 29  
ARG CB  HB3  sing N N 30  
ARG CG  CD   sing N N 31  
ARG CG  HG2  sing N N 32  
ARG CG  HG3  sing N N 33  
ARG CD  NE   sing N N 34  
ARG CD  HD2  sing N N 35  
ARG CD  HD3  sing N N 36  
ARG NE  CZ   sing N N 37  
ARG NE  HE   sing N N 38  
ARG CZ  NH1  sing N N 39  
ARG CZ  NH2  doub N N 40  
ARG NH1 HH11 sing N N 41  
ARG NH1 HH12 sing N N 42  
ARG NH2 HH21 sing N N 43  
ARG NH2 HH22 sing N N 44  
ARG OXT HXT  sing N N 45  
ASN N   CA   sing N N 46  
ASN N   H    sing N N 47  
ASN N   H2   sing N N 48  
ASN CA  C    sing N N 49  
ASN CA  CB   sing N N 50  
ASN CA  HA   sing N N 51  
ASN C   O    doub N N 52  
ASN C   OXT  sing N N 53  
ASN CB  CG   sing N N 54  
ASN CB  HB2  sing N N 55  
ASN CB  HB3  sing N N 56  
ASN CG  OD1  doub N N 57  
ASN CG  ND2  sing N N 58  
ASN ND2 HD21 sing N N 59  
ASN ND2 HD22 sing N N 60  
ASN OXT HXT  sing N N 61  
ASP N   CA   sing N N 62  
ASP N   H    sing N N 63  
ASP N   H2   sing N N 64  
ASP CA  C    sing N N 65  
ASP CA  CB   sing N N 66  
ASP CA  HA   sing N N 67  
ASP C   O    doub N N 68  
ASP C   OXT  sing N N 69  
ASP CB  CG   sing N N 70  
ASP CB  HB2  sing N N 71  
ASP CB  HB3  sing N N 72  
ASP CG  OD1  doub N N 73  
ASP CG  OD2  sing N N 74  
ASP OD2 HD2  sing N N 75  
ASP OXT HXT  sing N N 76  
GLN N   CA   sing N N 77  
GLN N   H    sing N N 78  
GLN N   H2   sing N N 79  
GLN CA  C    sing N N 80  
GLN CA  CB   sing N N 81  
GLN CA  HA   sing N N 82  
GLN C   O    doub N N 83  
GLN C   OXT  sing N N 84  
GLN CB  CG   sing N N 85  
GLN CB  HB2  sing N N 86  
GLN CB  HB3  sing N N 87  
GLN CG  CD   sing N N 88  
GLN CG  HG2  sing N N 89  
GLN CG  HG3  sing N N 90  
GLN CD  OE1  doub N N 91  
GLN CD  NE2  sing N N 92  
GLN NE2 HE21 sing N N 93  
GLN NE2 HE22 sing N N 94  
GLN OXT HXT  sing N N 95  
GLU N   CA   sing N N 96  
GLU N   H    sing N N 97  
GLU N   H2   sing N N 98  
GLU CA  C    sing N N 99  
GLU CA  CB   sing N N 100 
GLU CA  HA   sing N N 101 
GLU C   O    doub N N 102 
GLU C   OXT  sing N N 103 
GLU CB  CG   sing N N 104 
GLU CB  HB2  sing N N 105 
GLU CB  HB3  sing N N 106 
GLU CG  CD   sing N N 107 
GLU CG  HG2  sing N N 108 
GLU CG  HG3  sing N N 109 
GLU CD  OE1  doub N N 110 
GLU CD  OE2  sing N N 111 
GLU OE2 HE2  sing N N 112 
GLU OXT HXT  sing N N 113 
GLY N   CA   sing N N 114 
GLY N   H    sing N N 115 
GLY N   H2   sing N N 116 
GLY CA  C    sing N N 117 
GLY CA  HA2  sing N N 118 
GLY CA  HA3  sing N N 119 
GLY C   O    doub N N 120 
GLY C   OXT  sing N N 121 
GLY OXT HXT  sing N N 122 
HIS N   CA   sing N N 123 
HIS N   H    sing N N 124 
HIS N   H2   sing N N 125 
HIS CA  C    sing N N 126 
HIS CA  CB   sing N N 127 
HIS CA  HA   sing N N 128 
HIS C   O    doub N N 129 
HIS C   OXT  sing N N 130 
HIS CB  CG   sing N N 131 
HIS CB  HB2  sing N N 132 
HIS CB  HB3  sing N N 133 
HIS CG  ND1  sing Y N 134 
HIS CG  CD2  doub Y N 135 
HIS ND1 CE1  doub Y N 136 
HIS ND1 HD1  sing N N 137 
HIS CD2 NE2  sing Y N 138 
HIS CD2 HD2  sing N N 139 
HIS CE1 NE2  sing Y N 140 
HIS CE1 HE1  sing N N 141 
HIS NE2 HE2  sing N N 142 
HIS OXT HXT  sing N N 143 
HOH O   H1   sing N N 144 
HOH O   H2   sing N N 145 
ILE N   CA   sing N N 146 
ILE N   H    sing N N 147 
ILE N   H2   sing N N 148 
ILE CA  C    sing N N 149 
ILE CA  CB   sing N N 150 
ILE CA  HA   sing N N 151 
ILE C   O    doub N N 152 
ILE C   OXT  sing N N 153 
ILE CB  CG1  sing N N 154 
ILE CB  CG2  sing N N 155 
ILE CB  HB   sing N N 156 
ILE CG1 CD1  sing N N 157 
ILE CG1 HG12 sing N N 158 
ILE CG1 HG13 sing N N 159 
ILE CG2 HG21 sing N N 160 
ILE CG2 HG22 sing N N 161 
ILE CG2 HG23 sing N N 162 
ILE CD1 HD11 sing N N 163 
ILE CD1 HD12 sing N N 164 
ILE CD1 HD13 sing N N 165 
ILE OXT HXT  sing N N 166 
LEU N   CA   sing N N 167 
LEU N   H    sing N N 168 
LEU N   H2   sing N N 169 
LEU CA  C    sing N N 170 
LEU CA  CB   sing N N 171 
LEU CA  HA   sing N N 172 
LEU C   O    doub N N 173 
LEU C   OXT  sing N N 174 
LEU CB  CG   sing N N 175 
LEU CB  HB2  sing N N 176 
LEU CB  HB3  sing N N 177 
LEU CG  CD1  sing N N 178 
LEU CG  CD2  sing N N 179 
LEU CG  HG   sing N N 180 
LEU CD1 HD11 sing N N 181 
LEU CD1 HD12 sing N N 182 
LEU CD1 HD13 sing N N 183 
LEU CD2 HD21 sing N N 184 
LEU CD2 HD22 sing N N 185 
LEU CD2 HD23 sing N N 186 
LEU OXT HXT  sing N N 187 
LYS N   CA   sing N N 188 
LYS N   H    sing N N 189 
LYS N   H2   sing N N 190 
LYS CA  C    sing N N 191 
LYS CA  CB   sing N N 192 
LYS CA  HA   sing N N 193 
LYS C   O    doub N N 194 
LYS C   OXT  sing N N 195 
LYS CB  CG   sing N N 196 
LYS CB  HB2  sing N N 197 
LYS CB  HB3  sing N N 198 
LYS CG  CD   sing N N 199 
LYS CG  HG2  sing N N 200 
LYS CG  HG3  sing N N 201 
LYS CD  CE   sing N N 202 
LYS CD  HD2  sing N N 203 
LYS CD  HD3  sing N N 204 
LYS CE  NZ   sing N N 205 
LYS CE  HE2  sing N N 206 
LYS CE  HE3  sing N N 207 
LYS NZ  HZ1  sing N N 208 
LYS NZ  HZ2  sing N N 209 
LYS NZ  HZ3  sing N N 210 
LYS OXT HXT  sing N N 211 
MET N   CA   sing N N 212 
MET N   H    sing N N 213 
MET N   H2   sing N N 214 
MET CA  C    sing N N 215 
MET CA  CB   sing N N 216 
MET CA  HA   sing N N 217 
MET C   O    doub N N 218 
MET C   OXT  sing N N 219 
MET CB  CG   sing N N 220 
MET CB  HB2  sing N N 221 
MET CB  HB3  sing N N 222 
MET CG  SD   sing N N 223 
MET CG  HG2  sing N N 224 
MET CG  HG3  sing N N 225 
MET SD  CE   sing N N 226 
MET CE  HE1  sing N N 227 
MET CE  HE2  sing N N 228 
MET CE  HE3  sing N N 229 
MET OXT HXT  sing N N 230 
PHE N   CA   sing N N 231 
PHE N   H    sing N N 232 
PHE N   H2   sing N N 233 
PHE CA  C    sing N N 234 
PHE CA  CB   sing N N 235 
PHE CA  HA   sing N N 236 
PHE C   O    doub N N 237 
PHE C   OXT  sing N N 238 
PHE CB  CG   sing N N 239 
PHE CB  HB2  sing N N 240 
PHE CB  HB3  sing N N 241 
PHE CG  CD1  doub Y N 242 
PHE CG  CD2  sing Y N 243 
PHE CD1 CE1  sing Y N 244 
PHE CD1 HD1  sing N N 245 
PHE CD2 CE2  doub Y N 246 
PHE CD2 HD2  sing N N 247 
PHE CE1 CZ   doub Y N 248 
PHE CE1 HE1  sing N N 249 
PHE CE2 CZ   sing Y N 250 
PHE CE2 HE2  sing N N 251 
PHE CZ  HZ   sing N N 252 
PHE OXT HXT  sing N N 253 
PRO N   CA   sing N N 254 
PRO N   CD   sing N N 255 
PRO N   H    sing N N 256 
PRO CA  C    sing N N 257 
PRO CA  CB   sing N N 258 
PRO CA  HA   sing N N 259 
PRO C   O    doub N N 260 
PRO C   OXT  sing N N 261 
PRO CB  CG   sing N N 262 
PRO CB  HB2  sing N N 263 
PRO CB  HB3  sing N N 264 
PRO CG  CD   sing N N 265 
PRO CG  HG2  sing N N 266 
PRO CG  HG3  sing N N 267 
PRO CD  HD2  sing N N 268 
PRO CD  HD3  sing N N 269 
PRO OXT HXT  sing N N 270 
QG7 C22 C21  doub Y N 271 
QG7 C22 N5   sing Y N 272 
QG7 C21 C20  sing Y N 273 
QG7 N5  C18  doub Y N 274 
QG7 C20 C19  doub Y N 275 
QG7 C18 C19  sing Y N 276 
QG7 C18 C17  sing N N 277 
QG7 C11 N3   sing N N 278 
QG7 C11 C12  sing N N 279 
QG7 N3  C17  sing N N 280 
QG7 N3  C23  sing N N 281 
QG7 O1  C1   doub N N 282 
QG7 C24 C23  sing N N 283 
QG7 C24 N6   sing N N 284 
QG7 C1  N6   sing N N 285 
QG7 C1  C2   sing N N 286 
QG7 N4  C12  doub Y N 287 
QG7 N4  C16  sing Y N 288 
QG7 C12 C13  sing Y N 289 
QG7 C2  C3   sing N N 290 
QG7 C16 C15  doub Y N 291 
QG7 C13 C14  doub Y N 292 
QG7 C3  C4   sing N N 293 
QG7 C15 C14  sing Y N 294 
QG7 C4  C5   sing N N 295 
QG7 C5  C6   sing N N 296 
QG7 C6  C10  sing N N 297 
QG7 C6  S1   sing N N 298 
QG7 N2  C10  sing N N 299 
QG7 N2  C9   sing N N 300 
QG7 C10 C8   sing N N 301 
QG7 S1  C7   sing N N 302 
QG7 C9  O2   doub N N 303 
QG7 C9  N1   sing N N 304 
QG7 C8  C7   sing N N 305 
QG7 C8  N1   sing N N 306 
QG7 C10 H1   sing N N 307 
QG7 C15 H2   sing N N 308 
QG7 C17 H3   sing N N 309 
QG7 C17 H4   sing N N 310 
QG7 C11 H5   sing N N 311 
QG7 C11 H6   sing N N 312 
QG7 C14 H7   sing N N 313 
QG7 N1  H8   sing N N 314 
QG7 N2  H9   sing N N 315 
QG7 C8  H10  sing N N 316 
QG7 C7  H11  sing N N 317 
QG7 C7  H12  sing N N 318 
QG7 C6  H13  sing N N 319 
QG7 C5  H14  sing N N 320 
QG7 C5  H15  sing N N 321 
QG7 C4  H16  sing N N 322 
QG7 C4  H17  sing N N 323 
QG7 C3  H18  sing N N 324 
QG7 C3  H19  sing N N 325 
QG7 C2  H20  sing N N 326 
QG7 C2  H21  sing N N 327 
QG7 C24 H22  sing N N 328 
QG7 C24 H23  sing N N 329 
QG7 N6  H24  sing N N 330 
QG7 C23 H25  sing N N 331 
QG7 C23 H26  sing N N 332 
QG7 C16 H28  sing N N 333 
QG7 C13 H29  sing N N 334 
QG7 C22 H30  sing N N 335 
QG7 C21 H31  sing N N 336 
QG7 C20 H32  sing N N 337 
QG7 C19 H33  sing N N 338 
SER N   CA   sing N N 339 
SER N   H    sing N N 340 
SER N   H2   sing N N 341 
SER CA  C    sing N N 342 
SER CA  CB   sing N N 343 
SER CA  HA   sing N N 344 
SER C   O    doub N N 345 
SER C   OXT  sing N N 346 
SER CB  OG   sing N N 347 
SER CB  HB2  sing N N 348 
SER CB  HB3  sing N N 349 
SER OG  HG   sing N N 350 
SER OXT HXT  sing N N 351 
THR N   CA   sing N N 352 
THR N   H    sing N N 353 
THR N   H2   sing N N 354 
THR CA  C    sing N N 355 
THR CA  CB   sing N N 356 
THR CA  HA   sing N N 357 
THR C   O    doub N N 358 
THR C   OXT  sing N N 359 
THR CB  OG1  sing N N 360 
THR CB  CG2  sing N N 361 
THR CB  HB   sing N N 362 
THR OG1 HG1  sing N N 363 
THR CG2 HG21 sing N N 364 
THR CG2 HG22 sing N N 365 
THR CG2 HG23 sing N N 366 
THR OXT HXT  sing N N 367 
TRP N   CA   sing N N 368 
TRP N   H    sing N N 369 
TRP N   H2   sing N N 370 
TRP CA  C    sing N N 371 
TRP CA  CB   sing N N 372 
TRP CA  HA   sing N N 373 
TRP C   O    doub N N 374 
TRP C   OXT  sing N N 375 
TRP CB  CG   sing N N 376 
TRP CB  HB2  sing N N 377 
TRP CB  HB3  sing N N 378 
TRP CG  CD1  doub Y N 379 
TRP CG  CD2  sing Y N 380 
TRP CD1 NE1  sing Y N 381 
TRP CD1 HD1  sing N N 382 
TRP CD2 CE2  doub Y N 383 
TRP CD2 CE3  sing Y N 384 
TRP NE1 CE2  sing Y N 385 
TRP NE1 HE1  sing N N 386 
TRP CE2 CZ2  sing Y N 387 
TRP CE3 CZ3  doub Y N 388 
TRP CE3 HE3  sing N N 389 
TRP CZ2 CH2  doub Y N 390 
TRP CZ2 HZ2  sing N N 391 
TRP CZ3 CH2  sing Y N 392 
TRP CZ3 HZ3  sing N N 393 
TRP CH2 HH2  sing N N 394 
TRP OXT HXT  sing N N 395 
TYR N   CA   sing N N 396 
TYR N   H    sing N N 397 
TYR N   H2   sing N N 398 
TYR CA  C    sing N N 399 
TYR CA  CB   sing N N 400 
TYR CA  HA   sing N N 401 
TYR C   O    doub N N 402 
TYR C   OXT  sing N N 403 
TYR CB  CG   sing N N 404 
TYR CB  HB2  sing N N 405 
TYR CB  HB3  sing N N 406 
TYR CG  CD1  doub Y N 407 
TYR CG  CD2  sing Y N 408 
TYR CD1 CE1  sing Y N 409 
TYR CD1 HD1  sing N N 410 
TYR CD2 CE2  doub Y N 411 
TYR CD2 HD2  sing N N 412 
TYR CE1 CZ   doub Y N 413 
TYR CE1 HE1  sing N N 414 
TYR CE2 CZ   sing Y N 415 
TYR CE2 HE2  sing N N 416 
TYR CZ  OH   sing N N 417 
TYR OH  HH   sing N N 418 
TYR OXT HXT  sing N N 419 
VAL N   CA   sing N N 420 
VAL N   H    sing N N 421 
VAL N   H2   sing N N 422 
VAL CA  C    sing N N 423 
VAL CA  CB   sing N N 424 
VAL CA  HA   sing N N 425 
VAL C   O    doub N N 426 
VAL C   OXT  sing N N 427 
VAL CB  CG1  sing N N 428 
VAL CB  CG2  sing N N 429 
VAL CB  HB   sing N N 430 
VAL CG1 HG11 sing N N 431 
VAL CG1 HG12 sing N N 432 
VAL CG1 HG13 sing N N 433 
VAL CG2 HG21 sing N N 434 
VAL CG2 HG22 sing N N 435 
VAL CG2 HG23 sing N N 436 
VAL OXT HXT  sing N N 437 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM120349 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2QCB 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 41 2 2' 
_space_group.name_Hall        'I 4bw 2bw' 
_space_group.IT_number        98 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CSW 
_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]   0.017310 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017310 
_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]   0.005427 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CU ? ? 23.42449 5.47274 ? ? 2.18335  24.96234 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345  0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ARG A 1 12  ? 3.14721  21.89670 14.96620  1.000 58.89390 ? 12  ARG A N   1 
ATOM   2    C  CA  . ARG A 1 12  ? 3.90160  23.14549 14.95984  1.000 57.47404 ? 12  ARG A CA  1 
ATOM   3    C  C   . ARG A 1 12  ? 3.79109  23.84683 13.61038  1.000 55.11322 ? 12  ARG A C   1 
ATOM   4    O  O   . ARG A 1 12  ? 2.80385  24.52897 13.32767  1.000 55.90003 ? 12  ARG A O   1 
ATOM   5    C  CB  . ARG A 1 12  ? 5.37443  22.89913 15.30940  1.000 57.13993 ? 12  ARG A CB  1 
ATOM   6    C  CG  . ARG A 1 12  ? 5.81412  21.44704 15.18939  1.000 57.45946 ? 12  ARG A CG  1 
ATOM   7    C  CD  . ARG A 1 12  ? 5.77990  20.97124 13.74514  1.000 58.28311 ? 12  ARG A CD  1 
ATOM   8    N  NE  . ARG A 1 12  ? 5.46590  19.55003 13.64927  1.000 60.02689 ? 12  ARG A NE  1 
ATOM   9    C  CZ  . ARG A 1 12  ? 4.30369  19.07212 13.22784  1.000 61.29725 ? 12  ARG A CZ  1 
ATOM   10   N  NH1 . ARG A 1 12  ? 3.31305  19.87863 12.88062  1.000 61.85279 ? 12  ARG A NH1 1 
ATOM   11   N  NH2 . ARG A 1 12  ? 4.12630  17.75361 13.16546  1.000 61.43557 ? 12  ARG A NH2 1 
ATOM   12   N  N   . ASP A 1 13  ? 4.80557  23.67785 12.76631  1.000 51.27798 ? 13  ASP A N   1 
ATOM   13   C  CA  . ASP A 1 13  ? 4.84388  24.37403 11.49196  1.000 45.76292 ? 13  ASP A CA  1 
ATOM   14   C  C   . ASP A 1 13  ? 4.47514  23.48831 10.31838  1.000 44.28340 ? 13  ASP A C   1 
ATOM   15   O  O   . ASP A 1 13  ? 4.68234  23.89017 9.17516   1.000 43.56115 ? 13  ASP A O   1 
ATOM   16   C  CB  . ASP A 1 13  ? 6.21498  24.99577 11.27138  1.000 43.10173 ? 13  ASP A CB  1 
ATOM   17   C  CG  . ASP A 1 13  ? 6.78084  25.57328 12.53453  1.000 40.01879 ? 13  ASP A CG  1 
ATOM   18   O  OD1 . ASP A 1 13  ? 6.11839  26.42697 13.16998  1.000 40.40017 ? 13  ASP A OD1 1 
ATOM   19   O  OD2 . ASP A 1 13  ? 7.86909  25.13095 12.91647  1.000 36.59511 ? 13  ASP A OD2 1 
ATOM   20   N  N   . GLU A 1 14  ? 3.94538  22.28980 10.56303  1.000 43.87673 ? 14  GLU A N   1 
ATOM   21   C  CA  . GLU A 1 14  ? 3.42357  21.49756 9.45411   1.000 42.43056 ? 14  GLU A CA  1 
ATOM   22   C  C   . GLU A 1 14  ? 2.44834  22.32511 8.62112   1.000 38.77645 ? 14  GLU A C   1 
ATOM   23   O  O   . GLU A 1 14  ? 2.61247  22.46890 7.40410   1.000 35.36536 ? 14  GLU A O   1 
ATOM   24   C  CB  . GLU A 1 14  ? 2.75762  20.22825 9.98803   1.000 44.44626 ? 14  GLU A CB  1 
ATOM   25   C  CG  . GLU A 1 14  ? 2.60760  19.13774 8.95750   1.000 46.69979 ? 14  GLU A CG  1 
ATOM   26   C  CD  . GLU A 1 14  ? 1.84650  17.93096 9.47932   1.000 48.76988 ? 14  GLU A CD  1 
ATOM   27   O  OE1 . GLU A 1 14  ? 1.83192  17.71228 10.70974  1.000 49.04540 ? 14  GLU A OE1 1 
ATOM   28   O  OE2 . GLU A 1 14  ? 1.26507  17.20055 8.65125   1.000 50.10015 ? 14  GLU A OE2 1 
ATOM   29   N  N   . ALA A 1 15  ? 1.45254  22.92251 9.27849   1.000 38.11867 ? 15  ALA A N   1 
ATOM   30   C  CA  . ALA A 1 15  ? 0.48946  23.75831 8.57139   1.000 36.79945 ? 15  ALA A CA  1 
ATOM   31   C  C   . ALA A 1 15  ? 1.14646  25.00367 7.98683   1.000 36.57536 ? 15  ALA A C   1 
ATOM   32   O  O   . ALA A 1 15  ? 0.84947  25.39141 6.84793   1.000 38.80489 ? 15  ALA A O   1 
ATOM   33   C  CB  . ALA A 1 15  ? -0.65013 24.14203 9.51701   1.000 36.23150 ? 15  ALA A CB  1 
ATOM   34   N  N   . GLY A 1 16  ? 2.03522  25.65148 8.75174   1.000 32.40012 ? 16  GLY A N   1 
ATOM   35   C  CA  . GLY A 1 16  ? 2.67829  26.86267 8.26609   1.000 27.99868 ? 16  GLY A CA  1 
ATOM   36   C  C   . GLY A 1 16  ? 3.54808  26.64199 7.04204   1.000 24.92439 ? 16  GLY A C   1 
ATOM   37   O  O   . GLY A 1 16  ? 3.62479  27.51461 6.16762   1.000 24.66357 ? 16  GLY A O   1 
ATOM   38   N  N   . ILE A 1 17  ? 4.20611  25.47853 6.94967   1.000 22.43736 ? 17  ILE A N   1 
ATOM   39   C  CA  . ILE A 1 17  ? 5.11177  25.22669 5.82380   1.000 20.39903 ? 17  ILE A CA  1 
ATOM   40   C  C   . ILE A 1 17  ? 4.35797  24.71455 4.59621   1.000 20.99423 ? 17  ILE A C   1 
ATOM   41   O  O   . ILE A 1 17  ? 4.66673  25.09074 3.46110   1.000 21.04018 ? 17  ILE A O   1 
ATOM   42   C  CB  . ILE A 1 17  ? 6.23744  24.26446 6.23182   1.000 20.55716 ? 17  ILE A CB  1 
ATOM   43   C  CG1 . ILE A 1 17  ? 7.17993  24.93668 7.23199   1.000 21.70199 ? 17  ILE A CG1 1 
ATOM   44   C  CG2 . ILE A 1 17  ? 7.00151  23.75961 4.99739   1.000 20.61341 ? 17  ILE A CG2 1 
ATOM   45   C  CD1 . ILE A 1 17  ? 8.18139  23.95620 7.85275   1.000 23.20960 ? 17  ILE A CD1 1 
ATOM   46   N  N   . THR A 1 18  ? 3.39977  23.81459 4.78550   1.000 20.13760 ? 18  THR A N   1 
ATOM   47   C  CA  . THR A 1 18  ? 2.67596  23.24364 3.65362   1.000 19.34079 ? 18  THR A CA  1 
ATOM   48   C  C   . THR A 1 18  ? 1.98221  24.32062 2.82787   1.000 19.94951 ? 18  THR A C   1 
ATOM   49   O  O   . THR A 1 18  ? 1.27918  25.18280 3.36244   1.000 23.46277 ? 18  THR A O   1 
ATOM   50   C  CB  . THR A 1 18  ? 1.63468  22.26558 4.19634   1.000 20.35405 ? 18  THR A CB  1 
ATOM   51   O  OG1 . THR A 1 18  ? 2.33332  21.17670 4.80458   1.000 21.35709 ? 18  THR A OG1 1 
ATOM   52   C  CG2 . THR A 1 18  ? 0.74312  21.75123 3.08501   1.000 21.84804 ? 18  THR A CG2 1 
ATOM   53   N  N   . GLY A 1 19  ? 2.15232  24.25122 1.51116   1.000 19.49331 ? 19  GLY A N   1 
ATOM   54   C  CA  . GLY A 1 19  ? 1.48390  25.18981 0.64440   1.000 20.80345 ? 19  GLY A CA  1 
ATOM   55   C  C   . GLY A 1 19  ? 2.38845  25.61515 -0.49429  1.000 18.92537 ? 19  GLY A C   1 
ATOM   56   O  O   . GLY A 1 19  ? 3.41501  24.99543 -0.76830  1.000 20.38198 ? 19  GLY A O   1 
ATOM   57   N  N   . THR A 1 20  ? 1.97481  26.68584 -1.16726  1.000 21.11102 ? 20  THR A N   1 
ATOM   58   C  CA  . THR A 1 20  ? 2.65847  27.23771 -2.32475  1.000 20.60469 ? 20  THR A CA  1 
ATOM   59   C  C   . THR A 1 20  ? 3.44821  28.46092 -1.88969  1.000 21.46752 ? 20  THR A C   1 
ATOM   60   O  O   . THR A 1 20  ? 2.90373  29.36030 -1.22801  1.000 22.83981 ? 20  THR A O   1 
ATOM   61   C  CB  . THR A 1 20  ? 1.65055  27.62591 -3.40410  1.000 22.34095 ? 20  THR A CB  1 
ATOM   62   O  OG1 . THR A 1 20  ? 0.89838  26.46565 -3.78925  1.000 23.30263 ? 20  THR A OG1 1 
ATOM   63   C  CG2 . THR A 1 20  ? 2.35533  28.16196 -4.62835  1.000 24.21426 ? 20  THR A CG2 1 
ATOM   64   N  N   . TRP A 1 21  ? 4.72624  28.48494 -2.25958  1.000 19.62470 ? 21  TRP A N   1 
ATOM   65   C  CA  . TRP A 1 21  ? 5.64205  29.57489 -1.97487  1.000 18.28910 ? 21  TRP A CA  1 
ATOM   66   C  C   . TRP A 1 21  ? 6.24032  30.08883 -3.27537  1.000 18.22087 ? 21  TRP A C   1 
ATOM   67   O  O   . TRP A 1 21  ? 6.34213  29.36248 -4.26516  1.000 19.32126 ? 21  TRP A O   1 
ATOM   68   C  CB  . TRP A 1 21  ? 6.76297  29.08575 -1.06137  1.000 19.45776 ? 21  TRP A CB  1 
ATOM   69   C  CG  . TRP A 1 21  ? 6.31311  28.62530 0.28927   1.000 18.52986 ? 21  TRP A CG  1 
ATOM   70   C  CD1 . TRP A 1 21  ? 5.80194  27.39919 0.61645   1.000 19.94236 ? 21  TRP A CD1 1 
ATOM   71   C  CD2 . TRP A 1 21  ? 6.34393  29.38296 1.50033   1.000 17.49966 ? 21  TRP A CD2 1 
ATOM   72   N  NE1 . TRP A 1 21  ? 5.52455  27.34430 1.96671   1.000 19.05738 ? 21  TRP A NE1 1 
ATOM   73   C  CE2 . TRP A 1 21  ? 5.85997  28.54663 2.53388   1.000 18.27351 ? 21  TRP A CE2 1 
ATOM   74   C  CE3 . TRP A 1 21  ? 6.75924  30.68712 1.82292   1.000 19.28677 ? 21  TRP A CE3 1 
ATOM   75   C  CZ2 . TRP A 1 21  ? 5.76977  28.97697 3.86569   1.000 19.72638 ? 21  TRP A CZ2 1 
ATOM   76   C  CZ3 . TRP A 1 21  ? 6.66531  31.10719 3.14303   1.000 20.51419 ? 21  TRP A CZ3 1 
ATOM   77   C  CH2 . TRP A 1 21  ? 6.15548  30.26063 4.13934   1.000 20.94180 ? 21  TRP A CH2 1 
ATOM   78   N  N   . TYR A 1 22  ? 6.66968  31.35127 -3.25323  1.000 18.65817 ? 22  TYR A N   1 
ATOM   79   C  CA  . TYR A 1 22  ? 7.23617  32.01043 -4.41345  1.000 19.33647 ? 22  TYR A CA  1 
ATOM   80   C  C   . TYR A 1 22  ? 8.51118  32.72912 -4.00577  1.000 18.61162 ? 22  TYR A C   1 
ATOM   81   O  O   . TYR A 1 22  ? 8.56276  33.35382 -2.93889  1.000 20.25046 ? 22  TYR A O   1 
ATOM   82   C  CB  . TYR A 1 22  ? 6.24051  33.05788 -4.97028  1.000 19.50610 ? 22  TYR A CB  1 
ATOM   83   C  CG  . TYR A 1 22  ? 4.83146  32.53684 -5.17986  1.000 20.91571 ? 22  TYR A CG  1 
ATOM   84   C  CD1 . TYR A 1 22  ? 4.47509  31.93579 -6.37117  1.000 22.89063 ? 22  TYR A CD1 1 
ATOM   85   C  CD2 . TYR A 1 22  ? 3.85757  32.63959 -4.17392  1.000 20.50870 ? 22  TYR A CD2 1 
ATOM   86   C  CE1 . TYR A 1 22  ? 3.18999  31.45572 -6.57699  1.000 21.97035 ? 22  TYR A CE1 1 
ATOM   87   C  CE2 . TYR A 1 22  ? 2.59345  32.16978 -4.36995  1.000 21.23109 ? 22  TYR A CE2 1 
ATOM   88   C  CZ  . TYR A 1 22  ? 2.26216  31.57933 -5.56692  1.000 21.93490 ? 22  TYR A CZ  1 
ATOM   89   O  OH  . TYR A 1 22  ? 0.98393  31.12298 -5.76603  1.000 22.13625 ? 22  TYR A OH  1 
ATOM   90   N  N   . ASN A 1 23  ? 9.54829  32.64427 -4.83923  1.000 17.10106 ? 23  ASN A N   1 
ATOM   91   C  CA  . ASN A 1 23  ? 10.76052 33.37981 -4.51797  1.000 17.22553 ? 23  ASN A CA  1 
ATOM   92   C  C   . ASN A 1 23  ? 10.88025 34.66675 -5.33621  1.000 18.29127 ? 23  ASN A C   1 
ATOM   93   O  O   . ASN A 1 23  ? 9.99559  35.04897 -6.11049  1.000 19.46651 ? 23  ASN A O   1 
ATOM   94   C  CB  . ASN A 1 23  ? 12.00403 32.48710 -4.56048  1.000 16.16746 ? 23  ASN A CB  1 
ATOM   95   C  CG  . ASN A 1 23  ? 12.45318 32.13485 -5.98631  1.000 16.11994 ? 23  ASN A CG  1 
ATOM   96   O  OD1 . ASN A 1 23  ? 11.94969 32.66713 -6.98577  1.000 17.05164 ? 23  ASN A OD1 1 
ATOM   97   N  ND2 . ASN A 1 23  ? 13.40837 31.23456 -6.06779  1.000 15.58386 ? 23  ASN A ND2 1 
ATOM   98   N  N   . GLN A 1 24  ? 12.00279 35.35394 -5.12571  1.000 17.57413 ? 24  GLN A N   1 
ATOM   99   C  CA  . GLN A 1 24  ? 12.21360 36.65629 -5.73155  1.000 18.17222 ? 24  GLN A CA  1 
ATOM   100  C  C   . GLN A 1 24  ? 12.42804 36.57023 -7.23644  1.000 18.94106 ? 24  GLN A C   1 
ATOM   101  O  O   . GLN A 1 24  ? 12.33976 37.59731 -7.92306  1.000 22.01969 ? 24  GLN A O   1 
ATOM   102  C  CB  . GLN A 1 24  ? 13.37972 37.35759 -5.02047  1.000 18.12336 ? 24  GLN A CB  1 
ATOM   103  C  CG  . GLN A 1 24  ? 14.79168 36.82835 -5.37612  1.000 18.47812 ? 24  GLN A CG  1 
ATOM   104  C  CD  . GLN A 1 24  ? 15.11739 35.44047 -4.83793  1.000 18.98154 ? 24  GLN A CD  1 
ATOM   105  O  OE1 . GLN A 1 24  ? 14.42881 34.90169 -3.95956  1.000 19.33755 ? 24  GLN A OE1 1 
ATOM   106  N  NE2 . GLN A 1 24  ? 16.16963 34.84239 -5.39054  1.000 19.30286 ? 24  GLN A NE2 1 
ATOM   107  N  N   . LEU A 1 25  ? 12.69873 35.37935 -7.75974  1.000 18.88832 ? 25  LEU A N   1 
ATOM   108  C  CA  . LEU A 1 25  ? 12.84885 35.19526 -9.19864  1.000 19.54731 ? 25  LEU A CA  1 
ATOM   109  C  C   . LEU A 1 25  ? 11.53754 34.86371 -9.88392  1.000 21.47922 ? 25  LEU A C   1 
ATOM   110  O  O   . LEU A 1 25  ? 11.50783 34.78044 -11.12007 1.000 24.32220 ? 25  LEU A O   1 
ATOM   111  C  CB  . LEU A 1 25  ? 13.83507 34.05283 -9.47346  1.000 19.77124 ? 25  LEU A CB  1 
ATOM   112  C  CG  . LEU A 1 25  ? 15.27640 34.28635 -9.02066  1.000 21.41066 ? 25  LEU A CG  1 
ATOM   113  C  CD1 . LEU A 1 25  ? 16.04229 32.97191 -8.94226  1.000 22.28972 ? 25  LEU A CD1 1 
ATOM   114  C  CD2 . LEU A 1 25  ? 15.95005 35.24406 -10.00495 1.000 22.14532 ? 25  LEU A CD2 1 
ATOM   115  N  N   . GLY A 1 26  ? 10.47531 34.64699 -9.10922  1.000 21.25824 ? 26  GLY A N   1 
ATOM   116  C  CA  . GLY A 1 26  ? 9.21443  34.18803 -9.64066  1.000 21.06164 ? 26  GLY A CA  1 
ATOM   117  C  C   . GLY A 1 26  ? 9.07692  32.68423 -9.71655  1.000 19.93664 ? 26  GLY A C   1 
ATOM   118  O  O   . GLY A 1 26  ? 8.09670  32.20761 -10.31227 1.000 21.92840 ? 26  GLY A O   1 
ATOM   119  N  N   . SER A 1 27  ? 10.00655 31.92146 -9.10776  1.000 18.51375 ? 27  SER A N   1 
ATOM   120  C  CA  . SER A 1 27  ? 9.86607  30.47400 -9.08809  1.000 17.33232 ? 27  SER A CA  1 
ATOM   121  C  C   . SER A 1 27  ? 8.80963  30.05152 -8.06250  1.000 16.91077 ? 27  SER A C   1 
ATOM   122  O  O   . SER A 1 27  ? 8.53663  30.77263 -7.10716  1.000 18.33365 ? 27  SER A O   1 
ATOM   123  C  CB  . SER A 1 27  ? 11.20875 29.83900 -8.72090  1.000 16.78052 ? 27  SER A CB  1 
ATOM   124  O  OG  . SER A 1 27  ? 12.18486 30.20748 -9.69014  1.000 17.71514 ? 27  SER A OG  1 
ATOM   125  N  N   . THR A 1 28  ? 8.22021  28.86590 -8.27891  1.000 17.55841 ? 28  THR A N   1 
ATOM   126  C  CA  . THR A 1 28  ? 7.10136  28.33743 -7.49520  1.000 18.21443 ? 28  THR A CA  1 
ATOM   127  C  C   . THR A 1 28  ? 7.50904  27.04561 -6.79577  1.000 18.10950 ? 28  THR A C   1 
ATOM   128  O  O   . THR A 1 28  ? 7.89014  26.06460 -7.45099  1.000 18.27307 ? 28  THR A O   1 
ATOM   129  C  CB  . THR A 1 28  ? 5.86716  28.07562 -8.36745  1.000 19.75805 ? 28  THR A CB  1 
ATOM   130  O  OG1 . THR A 1 28  ? 5.52602  29.25289 -9.09849  1.000 22.67833 ? 28  THR A OG1 1 
ATOM   131  C  CG2 . THR A 1 28  ? 4.66894  27.66178 -7.51199  1.000 21.91448 ? 28  THR A CG2 1 
ATOM   132  N  N   . PHE A 1 29  ? 7.41821  27.05108 -5.47265  1.000 18.36400 ? 29  PHE A N   1 
ATOM   133  C  CA  . PHE A 1 29  ? 7.83643  25.95719 -4.59843  1.000 17.61730 ? 29  PHE A CA  1 
ATOM   134  C  C   . PHE A 1 29  ? 6.55164  25.43023 -3.95193  1.000 18.30156 ? 29  PHE A C   1 
ATOM   135  O  O   . PHE A 1 29  ? 5.93126  26.11466 -3.13126  1.000 18.87247 ? 29  PHE A O   1 
ATOM   136  C  CB  . PHE A 1 29  ? 8.83509  26.53943 -3.58233  1.000 17.33107 ? 29  PHE A CB  1 
ATOM   137  C  CG  . PHE A 1 29  ? 9.18747  25.66115 -2.41790  1.000 18.48432 ? 29  PHE A CG  1 
ATOM   138  C  CD1 . PHE A 1 29  ? 9.50973  24.32383 -2.58763  1.000 19.16406 ? 29  PHE A CD1 1 
ATOM   139  C  CD2 . PHE A 1 29  ? 9.28343  26.22453 -1.14406  1.000 19.08618 ? 29  PHE A CD2 1 
ATOM   140  C  CE1 . PHE A 1 29  ? 9.87480  23.53101 -1.49169  1.000 17.63405 ? 29  PHE A CE1 1 
ATOM   141  C  CE2 . PHE A 1 29  ? 9.66315  25.44378 -0.05577  1.000 18.88096 ? 29  PHE A CE2 1 
ATOM   142  C  CZ  . PHE A 1 29  ? 9.93666  24.08981 -0.22880  1.000 17.57053 ? 29  PHE A CZ  1 
ATOM   143  N  N   . ILE A 1 30  ? 6.12319  24.24171 -4.35721  1.000 17.35963 ? 30  ILE A N   1 
ATOM   144  C  CA  . ILE A 1 30  ? 4.89932  23.63241 -3.85009  1.000 18.00355 ? 30  ILE A CA  1 
ATOM   145  C  C   . ILE A 1 30  ? 5.30219  22.49056 -2.93086  1.000 18.74686 ? 30  ILE A C   1 
ATOM   146  O  O   . ILE A 1 30  ? 5.95231  21.53681 -3.37340  1.000 20.37102 ? 30  ILE A O   1 
ATOM   147  C  CB  . ILE A 1 30  ? 4.03232  23.13279 -5.00732  1.000 21.53716 ? 30  ILE A CB  1 
ATOM   148  C  CG1 . ILE A 1 30  ? 3.45563  24.32915 -5.76702  1.000 23.11825 ? 30  ILE A CG1 1 
ATOM   149  C  CG2 . ILE A 1 30  ? 2.92362  22.23838 -4.48631  1.000 22.12736 ? 30  ILE A CG2 1 
ATOM   150  C  CD1 . ILE A 1 30  ? 2.74677  23.97954 -7.03599  1.000 24.49050 ? 30  ILE A CD1 1 
ATOM   151  N  N   . VAL A 1 31  ? 4.97021  22.59150 -1.64193  1.000 18.67176 ? 31  VAL A N   1 
ATOM   152  C  CA  . VAL A 1 31  ? 5.52130  21.64423 -0.67269  1.000 18.44159 ? 31  VAL A CA  1 
ATOM   153  C  C   . VAL A 1 31  ? 4.45117  21.14631 0.30337   1.000 18.48614 ? 31  VAL A C   1 
ATOM   154  O  O   . VAL A 1 31  ? 3.54719  21.88533 0.70660   1.000 19.65649 ? 31  VAL A O   1 
ATOM   155  C  CB  . VAL A 1 31  ? 6.74623  22.25333 0.06236   1.000 18.97533 ? 31  VAL A CB  1 
ATOM   156  C  CG1 . VAL A 1 31  ? 6.29402  23.43160 0.96518   1.000 20.57091 ? 31  VAL A CG1 1 
ATOM   157  C  CG2 . VAL A 1 31  ? 7.53920  21.19280 0.81534   1.000 20.02831 ? 31  VAL A CG2 1 
ATOM   158  N  N   . THR A 1 32  ? 4.58325  19.88502 0.71557   1.000 19.54588 ? 32  THR A N   1 
ATOM   159  C  CA  . THR A 1 32  ? 3.82220  19.33432 1.82658   1.000 20.71116 ? 32  THR A CA  1 
ATOM   160  C  C   . THR A 1 32  ? 4.79521  18.91809 2.91776   1.000 19.25368 ? 32  THR A C   1 
ATOM   161  O  O   . THR A 1 32  ? 5.75791  18.19203 2.65527   1.000 19.53793 ? 32  THR A O   1 
ATOM   162  C  CB  . THR A 1 32  ? 2.98770  18.13191 1.39305   1.000 22.35735 ? 32  THR A CB  1 
ATOM   163  O  OG1 . THR A 1 32  ? 2.06065  18.53559 0.37349   1.000 24.10106 ? 32  THR A OG1 1 
ATOM   164  C  CG2 . THR A 1 32  ? 2.22160  17.53728 2.59567   1.000 23.05975 ? 32  THR A CG2 1 
ATOM   165  N  N   . ALA A 1 33  ? 4.55289  19.39463 4.13869   1.000 20.29276 ? 33  ALA A N   1 
ATOM   166  C  CA  . ALA A 1 33  ? 5.35709  19.03925 5.30287   1.000 20.32488 ? 33  ALA A CA  1 
ATOM   167  C  C   . ALA A 1 33  ? 4.63652  17.92708 6.04762   1.000 21.90646 ? 33  ALA A C   1 
ATOM   168  O  O   . ALA A 1 33  ? 3.50011  18.11746 6.50910   1.000 25.03198 ? 33  ALA A O   1 
ATOM   169  C  CB  . ALA A 1 33  ? 5.53623  20.24793 6.21605   1.000 21.00537 ? 33  ALA A CB  1 
ATOM   170  N  N   . GLY A 1 34  ? 5.27927  16.78111 6.14905   1.000 20.83826 ? 34  GLY A N   1 
ATOM   171  C  CA  . GLY A 1 34  ? 4.68928  15.65059 6.83528   1.000 22.89198 ? 34  GLY A CA  1 
ATOM   172  C  C   . GLY A 1 34  ? 4.93495  15.67754 8.33274   1.000 23.70976 ? 34  GLY A C   1 
ATOM   173  O  O   . GLY A 1 34  ? 5.87126  16.30677 8.83130   1.000 23.78603 ? 34  GLY A O   1 
ATOM   174  N  N   . ALA A 1 35  ? 4.07563  14.96077 9.05566   1.000 24.84592 ? 35  ALA A N   1 
ATOM   175  C  CA  . ALA A 1 35  ? 4.22698  14.87780 10.50045  1.000 27.73948 ? 35  ALA A CA  1 
ATOM   176  C  C   . ALA A 1 35  ? 5.57818  14.30221 10.90131  1.000 29.90589 ? 35  ALA A C   1 
ATOM   177  O  O   . ALA A 1 35  ? 6.05845  14.59365 12.00093  1.000 34.02243 ? 35  ALA A O   1 
ATOM   178  C  CB  . ALA A 1 35  ? 3.09032  14.04366 11.09968  1.000 28.85702 ? 35  ALA A CB  1 
ATOM   179  N  N   . ASP A 1 36  ? 6.20466  13.51512 10.02303  1.000 28.15832 ? 36  ASP A N   1 
ATOM   180  C  CA  . ASP A 1 36  ? 7.44669  12.80410 10.29585  1.000 28.94626 ? 36  ASP A CA  1 
ATOM   181  C  C   . ASP A 1 36  ? 8.70041  13.60782 9.95796   1.000 26.10111 ? 36  ASP A C   1 
ATOM   182  O  O   . ASP A 1 36  ? 9.80248  13.05437 10.02705  1.000 27.63038 ? 36  ASP A O   1 
ATOM   183  C  CB  . ASP A 1 36  ? 7.46502  11.48674 9.50565   1.000 31.04489 ? 36  ASP A CB  1 
ATOM   184  C  CG  . ASP A 1 36  ? 7.42021  11.69900 7.99032   1.000 32.93691 ? 36  ASP A CG  1 
ATOM   185  O  OD1 . ASP A 1 36  ? 7.05932  12.80992 7.53958   1.000 30.32601 ? 36  ASP A OD1 1 
ATOM   186  O  OD2 . ASP A 1 36  ? 7.72201  10.74065 7.23873   1.000 35.83631 ? 36  ASP A OD2 1 
ATOM   187  N  N   . GLY A 1 37  ? 8.56485  14.87894 9.58887   1.000 22.81520 ? 37  GLY A N   1 
ATOM   188  C  CA  . GLY A 1 37  ? 9.69033  15.68085 9.15983   1.000 20.63592 ? 37  GLY A CA  1 
ATOM   189  C  C   . GLY A 1 37  ? 9.94876  15.68826 7.66339   1.000 18.43514 ? 37  GLY A C   1 
ATOM   190  O  O   . GLY A 1 37  ? 10.92882 16.30962 7.22996   1.000 17.47407 ? 37  GLY A O   1 
ATOM   191  N  N   . ALA A 1 38  ? 9.12064  15.00966 6.86053   1.000 18.68627 ? 38  ALA A N   1 
ATOM   192  C  CA  . ALA A 1 38  ? 9.37098  14.96719 5.41760   1.000 19.42034 ? 38  ALA A CA  1 
ATOM   193  C  C   . ALA A 1 38  ? 8.87962  16.22820 4.73138   1.000 18.14227 ? 38  ALA A C   1 
ATOM   194  O  O   . ALA A 1 38  ? 7.86777  16.81842 5.12823   1.000 18.81578 ? 38  ALA A O   1 
ATOM   195  C  CB  . ALA A 1 38  ? 8.64856  13.78546 4.76653   1.000 22.53446 ? 38  ALA A CB  1 
ATOM   196  N  N   . LEU A 1 39  ? 9.59277  16.61706 3.66683   1.000 17.83004 ? 39  LEU A N   1 
ATOM   197  C  CA  . LEU A 1 39  ? 9.12357  17.60514 2.70247   1.000 17.03249 ? 39  LEU A CA  1 
ATOM   198  C  C   . LEU A 1 39  ? 9.00282  16.92370 1.34616   1.000 17.05395 ? 39  LEU A C   1 
ATOM   199  O  O   . LEU A 1 39  ? 9.92200  16.23260 0.92082   1.000 18.23599 ? 39  LEU A O   1 
ATOM   200  C  CB  . LEU A 1 39  ? 10.11361 18.77667 2.57754   1.000 17.06808 ? 39  LEU A CB  1 
ATOM   201  C  CG  . LEU A 1 39  ? 10.33537 19.62478 3.84940   1.000 17.00171 ? 39  LEU A CG  1 
ATOM   202  C  CD1 . LEU A 1 39  ? 11.35939 20.70161 3.49524   1.000 16.84178 ? 39  LEU A CD1 1 
ATOM   203  C  CD2 . LEU A 1 39  ? 9.03838  20.25350 4.35596   1.000 17.81442 ? 39  LEU A CD2 1 
ATOM   204  N  N   . THR A 1 40  ? 7.85052  17.06647 0.70107   1.000 16.72209 ? 40  THR A N   1 
ATOM   205  C  CA  . THR A 1 40  ? 7.61650  16.51478 -0.63079  1.000 18.23552 ? 40  THR A CA  1 
ATOM   206  C  C   . THR A 1 40  ? 6.90447  17.56133 -1.47897  1.000 19.24933 ? 40  THR A C   1 
ATOM   207  O  O   . THR A 1 40  ? 6.09562  18.33762 -0.96935  1.000 22.44593 ? 40  THR A O   1 
ATOM   208  C  CB  . THR A 1 40  ? 6.71242  15.27240 -0.52373  1.000 19.91749 ? 40  THR A CB  1 
ATOM   209  O  OG1 A THR A 1 40  ? 5.49080  15.62939 0.10371   0.560 20.49183 ? 40  THR A OG1 1 
ATOM   210  O  OG1 B THR A 1 40  ? 7.15687  14.44069 0.56311   0.440 20.58296 ? 40  THR A OG1 1 
ATOM   211  C  CG2 A THR A 1 40  ? 7.38431  14.18724 0.30566   0.560 21.34596 ? 40  THR A CG2 1 
ATOM   212  C  CG2 B THR A 1 40  ? 6.69738  14.48461 -1.81054  0.440 19.81131 ? 40  THR A CG2 1 
ATOM   213  N  N   . GLY A 1 41  ? 7.15129  17.54494 -2.78301  1.000 17.85179 ? 41  GLY A N   1 
ATOM   214  C  CA  . GLY A 1 41  ? 6.37106  18.42657 -3.64197  1.000 18.12370 ? 41  GLY A CA  1 
ATOM   215  C  C   . GLY A 1 41  ? 7.07466  18.64406 -4.97043  1.000 16.58879 ? 41  GLY A C   1 
ATOM   216  O  O   . GLY A 1 41  ? 7.74037  17.74190 -5.48952  1.000 18.52719 ? 41  GLY A O   1 
ATOM   217  N  N   . THR A 1 42  ? 6.88353  19.84938 -5.52576  1.000 16.71101 ? 42  THR A N   1 
ATOM   218  C  CA  . THR A 1 42  ? 7.39817  20.16802 -6.85402  1.000 17.71857 ? 42  THR A CA  1 
ATOM   219  C  C   . THR A 1 42  ? 7.99619  21.56233 -6.85509  1.000 18.00971 ? 42  THR A C   1 
ATOM   220  O  O   . THR A 1 42  ? 7.60907  22.41765 -6.06046  1.000 18.80221 ? 42  THR A O   1 
ATOM   221  C  CB  . THR A 1 42  ? 6.31063  20.07923 -7.94552  1.000 18.83468 ? 42  THR A CB  1 
ATOM   222  O  OG1 . THR A 1 42  ? 5.28276  21.04137 -7.68636  1.000 20.63869 ? 42  THR A OG1 1 
ATOM   223  C  CG2 . THR A 1 42  ? 5.71091  18.65619 -8.02404  1.000 19.40248 ? 42  THR A CG2 1 
ATOM   224  N  N   . TYR A 1 43  ? 8.93304  21.78093 -7.76580  1.000 16.84155 ? 43  TYR A N   1 
ATOM   225  C  CA  . TYR A 1 43  ? 9.56858  23.07676 -7.94901  1.000 16.50012 ? 43  TYR A CA  1 
ATOM   226  C  C   . TYR A 1 43  ? 9.51239  23.45758 -9.41924  1.000 16.64416 ? 43  TYR A C   1 
ATOM   227  O  O   . TYR A 1 43  ? 9.74929  22.62171 -10.29216 1.000 17.62269 ? 43  TYR A O   1 
ATOM   228  C  CB  . TYR A 1 43  ? 11.04181 23.00631 -7.49069  1.000 16.28605 ? 43  TYR A CB  1 
ATOM   229  C  CG  . TYR A 1 43  ? 11.62624 24.37375 -7.15404  1.000 15.65299 ? 43  TYR A CG  1 
ATOM   230  C  CD1 . TYR A 1 43  ? 12.18282 25.17958 -8.16103  1.000 15.41985 ? 43  TYR A CD1 1 
ATOM   231  C  CD2 . TYR A 1 43  ? 11.63700 24.86347 -5.84636  1.000 15.62719 ? 43  TYR A CD2 1 
ATOM   232  C  CE1 . TYR A 1 43  ? 12.69560 26.42688 -7.88511  1.000 16.44709 ? 43  TYR A CE1 1 
ATOM   233  C  CE2 . TYR A 1 43  ? 12.17053 26.10666 -5.54902  1.000 15.70563 ? 43  TYR A CE2 1 
ATOM   234  C  CZ  . TYR A 1 43  ? 12.69969 26.88373 -6.55654  1.000 14.93191 ? 43  TYR A CZ  1 
ATOM   235  O  OH  . TYR A 1 43  ? 13.22325 28.11657 -6.25191  1.000 16.18186 ? 43  TYR A OH  1 
ATOM   236  N  N   . GLU A 1 44  ? 9.19468  24.71810 -9.68509  1.000 16.98675 ? 44  GLU A N   1 
ATOM   237  C  CA  . GLU A 1 44  ? 9.16984  25.25398 -11.03693 1.000 17.61761 ? 44  GLU A CA  1 
ATOM   238  C  C   . GLU A 1 44  ? 10.05526 26.48382 -11.00534 1.000 17.82177 ? 44  GLU A C   1 
ATOM   239  O  O   . GLU A 1 44  ? 9.73508  27.44120 -10.29970 1.000 18.09715 ? 44  GLU A O   1 
ATOM   240  C  CB  . GLU A 1 44  ? 7.74908  25.64028 -11.43062 1.000 21.00551 ? 44  GLU A CB  1 
ATOM   241  C  CG  . GLU A 1 44  ? 7.70009  26.33194 -12.75665 1.000 25.38818 ? 44  GLU A CG  1 
ATOM   242  C  CD  . GLU A 1 44  ? 6.31970  26.34968 -13.39809 1.000 29.33715 ? 44  GLU A CD  1 
ATOM   243  O  OE1 . GLU A 1 44  ? 5.31829  25.96439 -12.72664 1.000 30.01470 ? 44  GLU A OE1 1 
ATOM   244  O  OE2 . GLU A 1 44  ? 6.25013  26.75714 -14.58377 1.000 31.68476 ? 44  GLU A OE2 1 
ATOM   245  N  N   . SER A 1 45  ? 11.17880 26.44620 -11.73065 1.000 18.32329 ? 45  SER A N   1 
ATOM   246  C  CA  . SER A 1 45  ? 12.10448 27.56620 -11.76528 1.000 17.48214 ? 45  SER A CA  1 
ATOM   247  C  C   . SER A 1 45  ? 11.71346 28.52214 -12.88269 1.000 19.33752 ? 45  SER A C   1 
ATOM   248  O  O   . SER A 1 45  ? 11.49057 28.10596 -14.03299 1.000 21.65987 ? 45  SER A O   1 
ATOM   249  C  CB  . SER A 1 45  ? 13.53054 27.10902 -12.00873 1.000 17.50403 ? 45  SER A CB  1 
ATOM   250  O  OG  . SER A 1 45  ? 14.36002 28.27192 -12.01956 1.000 17.15076 ? 45  SER A OG  1 
ATOM   251  N  N   . ALA A 1 46  ? 11.68010 29.80456 -12.54989 1.000 17.82574 ? 46  ALA A N   1 
ATOM   252  C  CA  . ALA A 1 46  ? 11.41430 30.81243 -13.56052 1.000 19.82677 ? 46  ALA A CA  1 
ATOM   253  C  C   . ALA A 1 46  ? 12.63819 31.11484 -14.40669 1.000 19.27955 ? 46  ALA A C   1 
ATOM   254  O  O   . ALA A 1 46  ? 12.51460 31.84630 -15.39770 1.000 22.46061 ? 46  ALA A O   1 
ATOM   255  C  CB  . ALA A 1 46  ? 10.89684 32.10246 -12.92947 1.000 22.04101 ? 46  ALA A CB  1 
ATOM   256  N  N   . VAL A 1 47  ? 13.81787 30.61646 -14.01390 1.000 18.76615 ? 47  VAL A N   1 
ATOM   257  C  CA  . VAL A 1 47  ? 15.08021 30.92866 -14.67764 1.000 17.48359 ? 47  VAL A CA  1 
ATOM   258  C  C   . VAL A 1 47  ? 15.87015 29.64910 -14.93576 1.000 17.62906 ? 47  VAL A C   1 
ATOM   259  O  O   . VAL A 1 47  ? 15.67567 28.61426 -14.28545 1.000 17.91045 ? 47  VAL A O   1 
ATOM   260  C  CB  . VAL A 1 47  ? 15.94469 31.93496 -13.85898 1.000 17.38169 ? 47  VAL A CB  1 
ATOM   261  C  CG1 . VAL A 1 47  ? 15.20431 33.25617 -13.65793 1.000 19.91998 ? 47  VAL A CG1 1 
ATOM   262  C  CG2 . VAL A 1 47  ? 16.41940 31.31200 -12.51992 1.000 18.60859 ? 47  VAL A CG2 1 
ATOM   263  N  N   . GLY A 1 48  ? 16.80860 29.75553 -15.88034 1.000 17.92824 ? 48  GLY A N   1 
ATOM   264  C  CA  . GLY A 1 48  ? 17.74912 28.70373 -16.14502 1.000 17.10439 ? 48  GLY A CA  1 
ATOM   265  C  C   . GLY A 1 48  ? 17.21891 27.64078 -17.09398 1.000 18.50905 ? 48  GLY A C   1 
ATOM   266  O  O   . GLY A 1 48  ? 16.20748 27.79965 -17.79706 1.000 18.94017 ? 48  GLY A O   1 
ATOM   267  N  N   . ASN A 1 49  ? 17.93768 26.52098 -17.10455 1.000 18.28203 ? 49  ASN A N   1 
ATOM   268  C  CA  . ASN A 1 49  ? 17.67249 25.42017 -18.03207 1.000 18.82245 ? 49  ASN A CA  1 
ATOM   269  C  C   . ASN A 1 49  ? 16.63681 24.49405 -17.40687 1.000 18.39256 ? 49  ASN A C   1 
ATOM   270  O  O   . ASN A 1 49  ? 16.94598 23.42970 -16.86710 1.000 20.45531 ? 49  ASN A O   1 
ATOM   271  C  CB  . ASN A 1 49  ? 18.96672 24.69282 -18.35390 1.000 21.20947 ? 49  ASN A CB  1 
ATOM   272  C  CG  . ASN A 1 49  ? 18.76769 23.64015 -19.42773 1.000 24.34173 ? 49  ASN A CG  1 
ATOM   273  O  OD1 . ASN A 1 49  ? 17.69941 23.57230 -20.05305 1.000 25.34276 ? 49  ASN A OD1 1 
ATOM   274  N  ND2 . ASN A 1 49  ? 19.77896 22.81791 -19.64908 1.000 25.88051 ? 49  ASN A ND2 1 
ATOM   275  N  N   . ALA A 1 50  ? 15.37883 24.93960 -17.45402 1.000 18.70007 ? 50  ALA A N   1 
ATOM   276  C  CA  . ALA A 1 50  ? 14.32042 24.34019 -16.65861 1.000 19.88629 ? 50  ALA A CA  1 
ATOM   277  C  C   . ALA A 1 50  ? 12.99059 24.70777 -17.28664 1.000 20.00122 ? 50  ALA A C   1 
ATOM   278  O  O   . ALA A 1 50  ? 12.80344 25.83930 -17.73989 1.000 21.41457 ? 50  ALA A O   1 
ATOM   279  C  CB  . ALA A 1 50  ? 14.36540 24.83505 -15.20240 1.000 21.42077 ? 50  ALA A CB  1 
ATOM   280  N  N   . GLU A 1 51  ? 12.06227 23.75535 -17.31284 1.000 19.72101 ? 51  GLU A N   1 
ATOM   281  C  CA  . GLU A 1 51  ? 10.70340 24.08068 -17.72048 1.000 22.51807 ? 51  GLU A CA  1 
ATOM   282  C  C   . GLU A 1 51  ? 9.75072  23.16443 -16.97098 1.000 20.11555 ? 51  GLU A C   1 
ATOM   283  O  O   . GLU A 1 51  ? 10.09100 22.01680 -16.66681 1.000 21.11588 ? 51  GLU A O   1 
ATOM   284  C  CB  . GLU A 1 51  ? 10.49107 23.97683 -19.22715 1.000 28.27468 ? 51  GLU A CB  1 
ATOM   285  C  CG  . GLU A 1 51  ? 10.36918 22.57120 -19.73745 1.000 29.44644 ? 51  GLU A CG  1 
ATOM   286  C  CD  . GLU A 1 51  ? 10.17153 22.53127 -21.25159 1.000 30.85214 ? 51  GLU A CD  1 
ATOM   287  O  OE1 . GLU A 1 51  ? 9.02025  22.55325 -21.74796 1.000 32.36890 ? 51  GLU A OE1 1 
ATOM   288  O  OE2 . GLU A 1 51  ? 11.17989 22.52003 -21.95950 1.000 31.37686 ? 51  GLU A OE2 1 
ATOM   289  N  N   . SER A 1 52  ? 8.60099  23.71573 -16.59187 1.000 19.98222 ? 52  SER A N   1 
ATOM   290  C  CA  . SER A 1 52  ? 7.57771  22.98787 -15.85595 1.000 19.88130 ? 52  SER A CA  1 
ATOM   291  C  C   . SER A 1 52  ? 8.08296  22.53704 -14.49418 1.000 19.78530 ? 52  SER A C   1 
ATOM   292  O  O   . SER A 1 52  ? 9.01631  23.13210 -13.94690 1.000 20.26446 ? 52  SER A O   1 
ATOM   293  C  CB  . SER A 1 52  ? 7.05036  21.78814 -16.65023 1.000 24.30480 ? 52  SER A CB  1 
ATOM   294  O  OG  . SER A 1 52  ? 5.78157  21.38222 -16.14639 1.000 28.62019 ? 52  SER A OG  1 
ATOM   295  N  N   . ARG A 1 53  ? 7.46529  21.49781 -13.94138 1.000 19.21509 ? 53  ARG A N   1 
ATOM   296  C  CA  . ARG A 1 53  ? 7.70977  21.10115 -12.55989 1.000 18.66595 ? 53  ARG A CA  1 
ATOM   297  C  C   . ARG A 1 53  ? 8.73515  19.98084 -12.45198 1.000 17.20633 ? 53  ARG A C   1 
ATOM   298  O  O   . ARG A 1 53  ? 8.83768  19.09998 -13.31346 1.000 19.43388 ? 53  ARG A O   1 
ATOM   299  C  CB  . ARG A 1 53  ? 6.40554  20.65311 -11.90114 1.000 20.94793 ? 53  ARG A CB  1 
ATOM   300  C  CG  . ARG A 1 53  ? 5.45645  21.82525 -11.58925 1.000 23.15960 ? 53  ARG A CG  1 
ATOM   301  C  CD  . ARG A 1 53  ? 4.01941  21.34499 -11.33510 1.000 29.63374 ? 53  ARG A CD  1 
ATOM   302  N  NE  A ARG A 1 53  ? 3.14238  22.31930 -10.69521 0.380 30.93311 ? 53  ARG A NE  1 
ATOM   303  N  NE  B ARG A 1 53  ? 3.53681  20.42579 -12.36112 0.620 33.47293 ? 53  ARG A NE  1 
ATOM   304  C  CZ  A ARG A 1 53  ? 1.87932  22.06589 -10.37309 0.380 31.91911 ? 53  ARG A CZ  1 
ATOM   305  C  CZ  B ARG A 1 53  ? 2.93335  20.78522 -13.48855 0.620 38.25601 ? 53  ARG A CZ  1 
ATOM   306  N  NH1 A ARG A 1 53  ? 1.10387  22.98627 -9.81833  0.380 31.40462 ? 53  ARG A NH1 1 
ATOM   307  N  NH1 B ARG A 1 53  ? 2.53461  19.88704 -14.37605 0.620 40.14922 ? 53  ARG A NH1 1 
ATOM   308  N  NH2 A ARG A 1 53  ? 1.38531  20.85211 -10.60461 0.380 32.11355 ? 53  ARG A NH2 1 
ATOM   309  N  NH2 B ARG A 1 53  ? 2.73205  22.07740 -13.73724 0.620 39.07707 ? 53  ARG A NH2 1 
ATOM   310  N  N   . TYR A 1 54  ? 9.47551  20.00339 -11.35143 1.000 17.57293 ? 54  TYR A N   1 
ATOM   311  C  CA  . TYR A 1 54  ? 10.44702 18.97915 -11.01600 1.000 16.96048 ? 54  TYR A CA  1 
ATOM   312  C  C   . TYR A 1 54  ? 10.13896 18.46672 -9.62137  1.000 17.25575 ? 54  TYR A C   1 
ATOM   313  O  O   . TYR A 1 54  ? 9.72130  19.22825 -8.75760  1.000 17.23316 ? 54  TYR A O   1 
ATOM   314  C  CB  . TYR A 1 54  ? 11.88576 19.57594 -10.99289 1.000 16.90347 ? 54  TYR A CB  1 
ATOM   315  C  CG  . TYR A 1 54  ? 12.31126 20.06609 -12.35214 1.000 16.72212 ? 54  TYR A CG  1 
ATOM   316  C  CD1 . TYR A 1 54  ? 11.86285 21.30002 -12.84853 1.000 17.26500 ? 54  TYR A CD1 1 
ATOM   317  C  CD2 . TYR A 1 54  ? 13.13078 19.29174 -13.16539 1.000 17.16735 ? 54  TYR A CD2 1 
ATOM   318  C  CE1 . TYR A 1 54  ? 12.23631 21.74392 -14.12558 1.000 17.73423 ? 54  TYR A CE1 1 
ATOM   319  C  CE2 . TYR A 1 54  ? 13.48999 19.72581 -14.44422 1.000 16.94989 ? 54  TYR A CE2 1 
ATOM   320  C  CZ  . TYR A 1 54  ? 13.03578 20.93686 -14.92192 1.000 17.97248 ? 54  TYR A CZ  1 
ATOM   321  O  OH  . TYR A 1 54  ? 13.40057 21.32920 -16.19174 1.000 17.84399 ? 54  TYR A OH  1 
ATOM   322  N  N   . VAL A 1 55  ? 10.38711 17.17837 -9.39973  1.000 17.33045 ? 55  VAL A N   1 
ATOM   323  C  CA  . VAL A 1 55  ? 10.19615 16.58846 -8.07754  1.000 17.69907 ? 55  VAL A CA  1 
ATOM   324  C  C   . VAL A 1 55  ? 11.17949 17.18452 -7.09011  1.000 16.97375 ? 55  VAL A C   1 
ATOM   325  O  O   . VAL A 1 55  ? 12.35681 17.40187 -7.40563  1.000 17.11865 ? 55  VAL A O   1 
ATOM   326  C  CB  . VAL A 1 55  ? 10.37901 15.06771 -8.17552  1.000 18.91926 ? 55  VAL A CB  1 
ATOM   327  C  CG1 . VAL A 1 55  ? 10.38644 14.42594 -6.78837  1.000 19.14728 ? 55  VAL A CG1 1 
ATOM   328  C  CG2 . VAL A 1 55  ? 9.29516  14.46223 -9.08450  1.000 19.33493 ? 55  VAL A CG2 1 
ATOM   329  N  N   . LEU A 1 56  ? 10.71350 17.42134 -5.86689  1.000 17.01969 ? 56  LEU A N   1 
ATOM   330  C  CA  . LEU A 1 56  ? 11.62366 17.77022 -4.78632  1.000 17.36686 ? 56  LEU A CA  1 
ATOM   331  C  C   . LEU A 1 56  ? 11.32172 16.89942 -3.58354  1.000 16.96944 ? 56  LEU A C   1 
ATOM   332  O  O   . LEU A 1 56  ? 10.18764 16.43289 -3.39308  1.000 17.49862 ? 56  LEU A O   1 
ATOM   333  C  CB  . LEU A 1 56  ? 11.54020 19.24719 -4.35962  1.000 17.33715 ? 56  LEU A CB  1 
ATOM   334  C  CG  . LEU A 1 56  ? 10.23998 19.68918 -3.66953  1.000 17.46114 ? 56  LEU A CG  1 
ATOM   335  C  CD1 . LEU A 1 56  ? 10.31740 19.56011 -2.11876  1.000 18.12723 ? 56  LEU A CD1 1 
ATOM   336  C  CD2 . LEU A 1 56  ? 9.90527  21.12920 -4.07458  1.000 18.31750 ? 56  LEU A CD2 1 
ATOM   337  N  N   . THR A 1 57  ? 12.35110 16.70932 -2.76431  1.000 15.97918 ? 57  THR A N   1 
ATOM   338  C  CA  A THR A 1 57  ? 12.19247 16.06330 -1.47338  0.620 15.47031 ? 57  THR A CA  1 
ATOM   339  C  CA  B THR A 1 57  ? 12.19769 16.05581 -1.47033  0.380 15.73660 ? 57  THR A CA  1 
ATOM   340  C  C   . THR A 1 57  ? 13.15100 16.71290 -0.49113  1.000 15.22913 ? 57  THR A C   1 
ATOM   341  O  O   . THR A 1 57  ? 14.21273 17.20527 -0.87523  1.000 15.53908 ? 57  THR A O   1 
ATOM   342  C  CB  A THR A 1 57  ? 12.38092 14.53289 -1.53946  0.620 17.35934 ? 57  THR A CB  1 
ATOM   343  C  CB  B THR A 1 57  ? 12.47157 14.53247 -1.47791  0.380 17.20627 ? 57  THR A CB  1 
ATOM   344  O  OG1 A THR A 1 57  ? 12.12955 13.96563 -0.25833  0.620 18.28288 ? 57  THR A OG1 1 
ATOM   345  O  OG1 B THR A 1 57  ? 13.82118 14.27751 -1.88799  0.380 17.33462 ? 57  THR A OG1 1 
ATOM   346  C  CG2 A THR A 1 57  ? 13.79295 14.15057 -1.98676  0.620 16.83813 ? 57  THR A CG2 1 
ATOM   347  C  CG2 B THR A 1 57  ? 11.52405 13.80333 -2.41269  0.380 17.52844 ? 57  THR A CG2 1 
ATOM   348  N  N   . GLY A 1 58  ? 12.76708 16.72311 0.77506   1.000 15.60017 ? 58  GLY A N   1 
ATOM   349  C  CA  . GLY A 1 58  ? 13.63525 17.30602 1.77022   1.000 15.64744 ? 58  GLY A CA  1 
ATOM   350  C  C   . GLY A 1 58  ? 13.17366 16.93630 3.16216   1.000 14.58199 ? 58  GLY A C   1 
ATOM   351  O  O   . GLY A 1 58  ? 12.42220 15.97662 3.35013   1.000 15.68364 ? 58  GLY A O   1 
ATOM   352  N  N   . ARG A 1 59  ? 13.67422 17.67041 4.15286   1.000 15.49295 ? 59  ARG A N   1 
ATOM   353  C  CA  . ARG A 1 59  ? 13.39814 17.39781 5.56791   1.000 14.57170 ? 59  ARG A CA  1 
ATOM   354  C  C   . ARG A 1 59  ? 13.29735 18.71468 6.33407   1.000 15.23360 ? 59  ARG A C   1 
ATOM   355  O  O   . ARG A 1 59  ? 13.93365 19.70978 5.97404   1.000 16.64361 ? 59  ARG A O   1 
ATOM   356  C  CB  . ARG A 1 59  ? 14.53617 16.60404 6.22950   1.000 15.62760 ? 59  ARG A CB  1 
ATOM   357  C  CG  . ARG A 1 59  ? 14.83586 15.27539 5.56316   1.000 16.87834 ? 59  ARG A CG  1 
ATOM   358  C  CD  . ARG A 1 59  ? 13.79411 14.19535 5.87835   1.000 17.36755 ? 59  ARG A CD  1 
ATOM   359  N  NE  . ARG A 1 59  ? 13.72291 13.92868 7.32608   1.000 16.59964 ? 59  ARG A NE  1 
ATOM   360  C  CZ  . ARG A 1 59  ? 12.69921 13.31654 7.91180   1.000 17.62699 ? 59  ARG A CZ  1 
ATOM   361  N  NH1 . ARG A 1 59  ? 11.67989 12.86952 7.19949   1.000 18.76111 ? 59  ARG A NH1 1 
ATOM   362  N  NH2 . ARG A 1 59  ? 12.68497 13.18379 9.24214   1.000 18.52400 ? 59  ARG A NH2 1 
ATOM   363  N  N   . TYR A 1 60  ? 12.54531 18.70773 7.43046   1.000 16.30164 ? 60  TYR A N   1 
ATOM   364  C  CA  . TYR A 1 60  ? 12.47007 19.89828 8.27386   1.000 15.70681 ? 60  TYR A CA  1 
ATOM   365  C  C   . TYR A 1 60  ? 12.42763 19.43101 9.72033   1.000 17.19413 ? 60  TYR A C   1 
ATOM   366  O  O   . TYR A 1 60  ? 12.07398 18.28733 9.99656   1.000 18.20574 ? 60  TYR A O   1 
ATOM   367  C  CB  . TYR A 1 60  ? 11.24784 20.79658 7.92099   1.000 16.83579 ? 60  TYR A CB  1 
ATOM   368  C  CG  . TYR A 1 60  ? 9.90888  20.26481 8.38995   1.000 17.63942 ? 60  TYR A CG  1 
ATOM   369  C  CD1 . TYR A 1 60  ? 9.31525  19.17287 7.75891   1.000 18.99819 ? 60  TYR A CD1 1 
ATOM   370  C  CD2 . TYR A 1 60  ? 9.25733  20.81900 9.49089   1.000 17.91366 ? 60  TYR A CD2 1 
ATOM   371  C  CE1 . TYR A 1 60  ? 8.10416  18.66289 8.20474   1.000 19.56770 ? 60  TYR A CE1 1 
ATOM   372  C  CE2 . TYR A 1 60  ? 8.02818  20.32314 9.92298   1.000 20.06797 ? 60  TYR A CE2 1 
ATOM   373  C  CZ  . TYR A 1 60  ? 7.46333  19.24836 9.27958   1.000 20.02699 ? 60  TYR A CZ  1 
ATOM   374  O  OH  . TYR A 1 60  ? 6.26529  18.74145 9.74375   1.000 21.75318 ? 60  TYR A OH  1 
ATOM   375  N  N   . ASP A 1 61  ? 12.82411 20.32307 10.63815  1.000 16.19377 ? 61  ASP A N   1 
ATOM   376  C  CA  . ASP A 1 61  ? 12.74118 20.07474 12.07797  1.000 16.20283 ? 61  ASP A CA  1 
ATOM   377  C  C   . ASP A 1 61  ? 11.28038 20.13154 12.49414  1.000 18.00657 ? 61  ASP A C   1 
ATOM   378  O  O   . ASP A 1 61  ? 10.68629 21.21527 12.53206  1.000 19.39440 ? 61  ASP A O   1 
ATOM   379  C  CB  . ASP A 1 61  ? 13.53785 21.16794 12.78949  1.000 17.40345 ? 61  ASP A CB  1 
ATOM   380  C  CG  . ASP A 1 61  ? 13.50203 21.02453 14.30634  1.000 18.26879 ? 61  ASP A CG  1 
ATOM   381  O  OD1 . ASP A 1 61  ? 12.88443 20.05195 14.82624  1.000 17.60405 ? 61  ASP A OD1 1 
ATOM   382  O  OD2 . ASP A 1 61  ? 14.12857 21.88071 14.96656  1.000 18.39092 ? 61  ASP A OD2 1 
ATOM   383  N  N   . SER A 1 62  ? 10.70502 18.97801 12.82297  1.000 18.25356 ? 62  SER A N   1 
ATOM   384  C  CA  . SER A 1 62  ? 9.29603  18.91273 13.17628  1.000 20.21479 ? 62  SER A CA  1 
ATOM   385  C  C   . SER A 1 62  ? 9.02400  19.21297 14.65151  1.000 23.15086 ? 62  SER A C   1 
ATOM   386  O  O   . SER A 1 62  ? 7.87147  19.11895 15.09099  1.000 24.76628 ? 62  SER A O   1 
ATOM   387  C  CB  . SER A 1 62  ? 8.72102  17.54559 12.78650  1.000 21.66655 ? 62  SER A CB  1 
ATOM   388  O  OG  . SER A 1 62  ? 9.49062  16.51553 13.36294  1.000 23.94397 ? 62  SER A OG  1 
ATOM   389  N  N   . ALA A 1 63  ? 10.03786 19.57438 15.42728  1.000 23.54320 ? 63  ALA A N   1 
ATOM   390  C  CA  . ALA A 1 63  ? 9.85334  19.95532 16.83016  1.000 23.29706 ? 63  ALA A CA  1 
ATOM   391  C  C   . ALA A 1 63  ? 10.82272 21.08699 17.11930  1.000 23.41589 ? 63  ALA A C   1 
ATOM   392  O  O   . ALA A 1 63  ? 11.78743 20.93129 17.87284  1.000 24.41146 ? 63  ALA A O   1 
ATOM   393  C  CB  . ALA A 1 63  ? 10.07387 18.76346 17.76363  1.000 24.75498 ? 63  ALA A CB  1 
ATOM   394  N  N   . PRO A 1 64  ? 10.60738 22.24312 16.50370  1.000 23.55627 ? 64  PRO A N   1 
ATOM   395  C  CA  . PRO A 1 64  ? 11.56549 23.34678 16.64035  1.000 25.18946 ? 64  PRO A CA  1 
ATOM   396  C  C   . PRO A 1 64  ? 11.55235 23.91723 18.05236  1.000 25.44607 ? 64  PRO A C   1 
ATOM   397  O  O   . PRO A 1 64  ? 10.70590 23.60642 18.90392  1.000 27.45280 ? 64  PRO A O   1 
ATOM   398  C  CB  . PRO A 1 64  ? 11.07076 24.37600 15.61723  1.000 25.67187 ? 64  PRO A CB  1 
ATOM   399  C  CG  . PRO A 1 64  ? 9.58444  24.09330 15.49196  1.000 25.11056 ? 64  PRO A CG  1 
ATOM   400  C  CD  . PRO A 1 64  ? 9.45261  22.59754 15.65016  1.000 24.14648 ? 64  PRO A CD  1 
ATOM   401  N  N   . ALA A 1 65  ? 12.53716 24.76987 18.30165  1.000 25.44795 ? 65  ALA A N   1 
ATOM   402  C  CA  . ALA A 1 65  ? 12.62285 25.43516 19.58960  1.000 28.85047 ? 65  ALA A CA  1 
ATOM   403  C  C   . ALA A 1 65  ? 11.44716 26.39377 19.74725  1.000 32.21643 ? 65  ALA A C   1 
ATOM   404  O  O   . ALA A 1 65  ? 10.83173 26.82480 18.76754  1.000 31.59582 ? 65  ALA A O   1 
ATOM   405  C  CB  . ALA A 1 65  ? 13.96574 26.15640 19.71537  1.000 28.67718 ? 65  ALA A CB  1 
ATOM   406  N  N   . THR A 1 66  ? 11.11193 26.70011 21.00254  1.000 36.06411 ? 66  THR A N   1 
ATOM   407  C  CA  . THR A 1 66  ? 9.98238  27.56615 21.32631  1.000 39.81818 ? 66  THR A CA  1 
ATOM   408  C  C   . THR A 1 66  ? 10.42528 28.94377 21.80787  1.000 41.07761 ? 66  THR A C   1 
ATOM   409  O  O   . THR A 1 66  ? 9.63447  29.67738 22.40978  1.000 43.29752 ? 66  THR A O   1 
ATOM   410  C  CB  . THR A 1 66  ? 9.05455  26.89331 22.34050  1.000 42.08359 ? 66  THR A CB  1 
ATOM   411  O  OG1 . THR A 1 66  ? 9.81349  26.47056 23.47997  1.000 42.90797 ? 66  THR A OG1 1 
ATOM   412  C  CG2 . THR A 1 66  ? 8.40043  25.68468 21.70520  1.000 42.88731 ? 66  THR A CG2 1 
ATOM   413  N  N   . ASP A 1 67  ? 11.67778 29.30668 21.54664  1.000 39.08293 ? 67  ASP A N   1 
ATOM   414  C  CA  . ASP A 1 67  ? 12.27337 30.55708 21.98885  1.000 37.91269 ? 67  ASP A CA  1 
ATOM   415  C  C   . ASP A 1 67  ? 12.19591 31.65268 20.92480  1.000 37.00650 ? 67  ASP A C   1 
ATOM   416  O  O   . ASP A 1 67  ? 12.91970 32.65155 21.02044  1.000 39.11270 ? 67  ASP A O   1 
ATOM   417  C  CB  . ASP A 1 67  ? 13.73165 30.31174 22.37675  1.000 36.79015 ? 67  ASP A CB  1 
ATOM   418  C  CG  . ASP A 1 67  ? 14.55344 29.79451 21.22155  1.000 37.94387 ? 67  ASP A CG  1 
ATOM   419  O  OD1 . ASP A 1 67  ? 13.98813 29.65874 20.11723  1.000 37.17559 ? 67  ASP A OD1 1 
ATOM   420  O  OD2 . ASP A 1 67  ? 15.75795 29.51650 21.41725  1.000 38.90076 ? 67  ASP A OD2 1 
ATOM   421  N  N   . GLY A 1 68  ? 11.34934 31.47977 19.91035  1.000 33.93889 ? 68  GLY A N   1 
ATOM   422  C  CA  . GLY A 1 68  ? 11.23926 32.43330 18.82505  1.000 32.67881 ? 68  GLY A CA  1 
ATOM   423  C  C   . GLY A 1 68  ? 12.14503 32.15888 17.64462  1.000 30.71846 ? 68  GLY A C   1 
ATOM   424  O  O   . GLY A 1 68  ? 12.13073 32.92710 16.67091  1.000 31.42430 ? 68  GLY A O   1 
ATOM   425  N  N   . SER A 1 69  ? 12.94363 31.10432 17.70269  1.000 26.00453 ? 69  SER A N   1 
ATOM   426  C  CA  . SER A 1 69  ? 13.80216 30.77225 16.57533  1.000 22.76415 ? 69  SER A CA  1 
ATOM   427  C  C   . SER A 1 69  ? 12.99536 30.22428 15.39957  1.000 21.24662 ? 69  SER A C   1 
ATOM   428  O  O   . SER A 1 69  ? 11.89942 29.66978 15.55890  1.000 22.78510 ? 69  SER A O   1 
ATOM   429  C  CB  . SER A 1 69  ? 14.81860 29.71463 16.99765  1.000 24.40735 ? 69  SER A CB  1 
ATOM   430  O  OG  . SER A 1 69  ? 15.68821 30.23267 17.99153  1.000 28.34239 ? 69  SER A OG  1 
ATOM   431  N  N   . GLY A 1 70  ? 13.58273 30.33403 14.20750  1.000 19.69631 ? 70  GLY A N   1 
ATOM   432  C  CA  . GLY A 1 70  ? 13.01379 29.72327 13.02480  1.000 18.32392 ? 70  GLY A CA  1 
ATOM   433  C  C   . GLY A 1 70  ? 13.10772 28.20388 13.05182  1.000 17.47535 ? 70  GLY A C   1 
ATOM   434  O  O   . GLY A 1 70  ? 13.67511 27.58867 13.95462  1.000 18.75909 ? 70  GLY A O   1 
ATOM   435  N  N   . THR A 1 71  ? 12.53266 27.59557 12.01927  1.000 17.19353 ? 71  THR A N   1 
ATOM   436  C  CA  . THR A 1 71  ? 12.48981 26.14330 11.84878  1.000 17.11802 ? 71  THR A CA  1 
ATOM   437  C  C   . THR A 1 71  ? 13.42602 25.74369 10.70446  1.000 16.83409 ? 71  THR A C   1 
ATOM   438  O  O   . THR A 1 71  ? 13.19607 26.12481 9.54957   1.000 18.06522 ? 71  THR A O   1 
ATOM   439  C  CB  . THR A 1 71  ? 11.05932 25.72439 11.52539  1.000 18.64659 ? 71  THR A CB  1 
ATOM   440  O  OG1 . THR A 1 71  ? 10.19722 26.09645 12.61341  1.000 21.19765 ? 71  THR A OG1 1 
ATOM   441  C  CG2 . THR A 1 71  ? 10.98104 24.20251 11.27360  1.000 19.00948 ? 71  THR A CG2 1 
ATOM   442  N  N   . ALA A 1 72  ? 14.47700 24.98497 11.02278  1.000 16.41897 ? 72  ALA A N   1 
ATOM   443  C  CA  . ALA A 1 72  ? 15.46066 24.58657 10.01164  1.000 15.83032 ? 72  ALA A CA  1 
ATOM   444  C  C   . ALA A 1 72  ? 14.87483 23.58397 9.00809   1.000 15.16713 ? 72  ALA A C   1 
ATOM   445  O  O   . ALA A 1 72  ? 14.07500 22.70984 9.37194   1.000 16.55580 ? 72  ALA A O   1 
ATOM   446  C  CB  . ALA A 1 72  ? 16.69505 23.95931 10.70381  1.000 16.26042 ? 72  ALA A CB  1 
ATOM   447  N  N   . LEU A 1 73  ? 15.27042 23.71034 7.73594   1.000 15.59673 ? 73  LEU A N   1 
ATOM   448  C  CA  A LEU A 1 73  ? 14.77684 22.79834 6.71477   0.560 15.21098 ? 73  LEU A CA  1 
ATOM   449  C  CA  B LEU A 1 73  ? 14.77668 22.80132 6.71019   0.440 15.98820 ? 73  LEU A CA  1 
ATOM   450  C  C   . LEU A 1 73  ? 15.72105 22.82633 5.51506   1.000 15.37198 ? 73  LEU A C   1 
ATOM   451  O  O   . LEU A 1 73  ? 16.59709 23.68385 5.40869   1.000 15.48377 ? 73  LEU A O   1 
ATOM   452  C  CB  A LEU A 1 73  ? 13.32844 23.14386 6.32690   0.560 15.14530 ? 73  LEU A CB  1 
ATOM   453  C  CB  B LEU A 1 73  ? 13.35617 23.17668 6.27625   0.440 17.24566 ? 73  LEU A CB  1 
ATOM   454  C  CG  A LEU A 1 73  ? 13.07654 24.22106 5.25717   0.560 16.14902 ? 73  LEU A CG  1 
ATOM   455  C  CG  B LEU A 1 73  ? 13.08011 24.64125 5.91702   0.440 17.94518 ? 73  LEU A CG  1 
ATOM   456  C  CD1 A LEU A 1 73  ? 11.58592 24.28127 4.86181   0.560 17.06553 ? 73  LEU A CD1 1 
ATOM   457  C  CD1 B LEU A 1 73  ? 13.63892 25.04418 4.54638   0.440 18.89223 ? 73  LEU A CD1 1 
ATOM   458  C  CD2 A LEU A 1 73  ? 13.56256 25.58174 5.70496   0.560 15.08281 ? 73  LEU A CD2 1 
ATOM   459  C  CD2 B LEU A 1 73  ? 11.57169 24.88964 5.99951   0.440 16.94960 ? 73  LEU A CD2 1 
ATOM   460  N  N   . GLY A 1 74  ? 15.54082 21.85547 4.61907   1.000 14.01015 ? 74  GLY A N   1 
ATOM   461  C  CA  . GLY A 1 74  ? 16.24775 21.88162 3.35213   1.000 13.23825 ? 74  GLY A CA  1 
ATOM   462  C  C   . GLY A 1 74  ? 15.56156 20.94752 2.38301   1.000 13.07137 ? 74  GLY A C   1 
ATOM   463  O  O   . GLY A 1 74  ? 14.78887 20.07261 2.77246   1.000 14.82985 ? 74  GLY A O   1 
ATOM   464  N  N   . TRP A 1 75  ? 15.85018 21.13857 1.10251   1.000 13.37466 ? 75  TRP A N   1 
ATOM   465  C  CA  . TRP A 1 75  ? 15.29591 20.25645 0.07754   1.000 14.73759 ? 75  TRP A CA  1 
ATOM   466  C  C   . TRP A 1 75  ? 16.18989 20.25973 -1.15025  1.000 14.63363 ? 75  TRP A C   1 
ATOM   467  O  O   . TRP A 1 75  ? 17.04795 21.13166 -1.32499  1.000 13.72998 ? 75  TRP A O   1 
ATOM   468  C  CB  . TRP A 1 75  ? 13.84581 20.60354 -0.27282  1.000 14.65393 ? 75  TRP A CB  1 
ATOM   469  C  CG  . TRP A 1 75  ? 13.68017 21.92268 -1.02701  1.000 14.46943 ? 75  TRP A CG  1 
ATOM   470  C  CD1 . TRP A 1 75  ? 13.61902 22.09923 -2.41335  1.000 15.66539 ? 75  TRP A CD1 1 
ATOM   471  C  CD2 . TRP A 1 75  ? 13.50086 23.23393 -0.45679  1.000 14.56734 ? 75  TRP A CD2 1 
ATOM   472  N  NE1 . TRP A 1 75  ? 13.44117 23.45069 -2.70532  1.000 15.72134 ? 75  TRP A NE1 1 
ATOM   473  C  CE2 . TRP A 1 75  ? 13.35590 24.15104 -1.52750  1.000 15.38944 ? 75  TRP A CE2 1 
ATOM   474  C  CE3 . TRP A 1 75  ? 13.45003 23.71841 0.86507   1.000 14.31507 ? 75  TRP A CE3 1 
ATOM   475  C  CZ2 . TRP A 1 75  ? 13.18102 25.53572 -1.31572  1.000 15.97832 ? 75  TRP A CZ2 1 
ATOM   476  C  CZ3 . TRP A 1 75  ? 13.27012 25.08691 1.06976   1.000 16.57854 ? 75  TRP A CZ3 1 
ATOM   477  C  CH2 . TRP A 1 75  ? 13.13260 25.97653 -0.01662  1.000 16.33455 ? 75  TRP A CH2 1 
ATOM   478  N  N   . THR A 1 76  ? 15.97891 19.25837 -2.00360  1.000 13.10244 ? 76  THR A N   1 
ATOM   479  C  CA  . THR A 1 76  ? 16.77676 19.08433 -3.21511  1.000 13.51708 ? 76  THR A CA  1 
ATOM   480  C  C   . THR A 1 76  ? 15.86121 18.96153 -4.42431  1.000 13.61458 ? 76  THR A C   1 
ATOM   481  O  O   . THR A 1 76  ? 14.82517 18.29447 -4.35600  1.000 15.35485 ? 76  THR A O   1 
ATOM   482  C  CB  . THR A 1 76  ? 17.57248 17.76060 -3.14157  1.000 13.60555 ? 76  THR A CB  1 
ATOM   483  O  OG1 . THR A 1 76  ? 18.39574 17.74530 -1.98242  1.000 14.48932 ? 76  THR A OG1 1 
ATOM   484  C  CG2 . THR A 1 76  ? 18.44651 17.53948 -4.38851  1.000 15.56410 ? 76  THR A CG2 1 
ATOM   485  N  N   . VAL A 1 77  ? 16.30066 19.53334 -5.54515  1.000 14.15137 ? 77  VAL A N   1 
ATOM   486  C  CA  . VAL A 1 77  ? 15.73678 19.26453 -6.87675  1.000 14.16902 ? 77  VAL A CA  1 
ATOM   487  C  C   . VAL A 1 77  ? 16.86902 18.78704 -7.77499  1.000 15.69996 ? 77  VAL A C   1 
ATOM   488  O  O   . VAL A 1 77  ? 17.88453 19.46843 -7.88249  1.000 15.86179 ? 77  VAL A O   1 
ATOM   489  C  CB  . VAL A 1 77  ? 15.12418 20.54269 -7.48375  1.000 14.63963 ? 77  VAL A CB  1 
ATOM   490  C  CG1 . VAL A 1 77  ? 14.80206 20.36766 -8.98643  1.000 16.02869 ? 77  VAL A CG1 1 
ATOM   491  C  CG2 . VAL A 1 77  ? 13.86067 20.99028 -6.72543  1.000 16.12584 ? 77  VAL A CG2 1 
ATOM   492  N  N   . ALA A 1 78  ? 16.69865 17.63595 -8.43219  1.000 15.02431 ? 78  ALA A N   1 
ATOM   493  C  CA  . ALA A 1 78  ? 17.53197 17.25524 -9.56507  1.000 15.65342 ? 78  ALA A CA  1 
ATOM   494  C  C   . ALA A 1 78  ? 16.84150 17.71802 -10.83993 1.000 15.60605 ? 78  ALA A C   1 
ATOM   495  O  O   . ALA A 1 78  ? 15.65475 17.44947 -11.03277 1.000 16.06915 ? 78  ALA A O   1 
ATOM   496  C  CB  . ALA A 1 78  ? 17.72692 15.74405 -9.62432  1.000 16.49080 ? 78  ALA A CB  1 
ATOM   497  N  N   . TRP A 1 79  ? 17.57827 18.41677 -11.70451 1.000 15.90238 ? 79  TRP A N   1 
ATOM   498  C  CA  . TRP A 1 79  ? 16.94866 19.15348 -12.80439 1.000 15.00792 ? 79  TRP A CA  1 
ATOM   499  C  C   . TRP A 1 79  ? 16.66038 18.28637 -14.02080 1.000 16.78023 ? 79  TRP A C   1 
ATOM   500  O  O   . TRP A 1 79  ? 16.96826 18.67153 -15.15574 1.000 16.65075 ? 79  TRP A O   1 
ATOM   501  C  CB  . TRP A 1 79  ? 17.77236 20.40086 -13.13007 1.000 15.86959 ? 79  TRP A CB  1 
ATOM   502  C  CG  . TRP A 1 79  ? 17.77853 21.34929 -11.98849 1.000 15.28787 ? 79  TRP A CG  1 
ATOM   503  C  CD1 . TRP A 1 79  ? 18.81991 21.58571 -11.12579 1.000 15.26215 ? 79  TRP A CD1 1 
ATOM   504  C  CD2 . TRP A 1 79  ? 16.69600 22.19696 -11.56789 1.000 14.41102 ? 79  TRP A CD2 1 
ATOM   505  N  NE1 . TRP A 1 79  ? 18.44017 22.51889 -10.19399 1.000 15.06996 ? 79  TRP A NE1 1 
ATOM   506  C  CE2 . TRP A 1 79  ? 17.14316 22.90280 -10.43623 1.000 14.65370 ? 79  TRP A CE2 1 
ATOM   507  C  CE3 . TRP A 1 79  ? 15.36922 22.38383 -12.01128 1.000 15.59865 ? 79  TRP A CE3 1 
ATOM   508  C  CZ2 . TRP A 1 79  ? 16.32971 23.82578 -9.74971  1.000 14.74688 ? 79  TRP A CZ2 1 
ATOM   509  C  CZ3 . TRP A 1 79  ? 14.56069 23.32657 -11.33958 1.000 16.38755 ? 79  TRP A CZ3 1 
ATOM   510  C  CH2 . TRP A 1 79  ? 15.04054 24.01443 -10.22237 1.000 15.55557 ? 79  TRP A CH2 1 
ATOM   511  N  N   . LYS A 1 80  ? 16.03593 17.13818 -13.77157 1.000 16.99940 ? 80  LYS A N   1 
ATOM   512  C  CA  . LYS A 1 80  ? 15.56474 16.22045 -14.80021 1.000 16.99643 ? 80  LYS A CA  1 
ATOM   513  C  C   . LYS A 1 80  ? 14.06367 16.03465 -14.64629 1.000 17.48821 ? 80  LYS A C   1 
ATOM   514  O  O   . LYS A 1 80  ? 13.58238 15.74595 -13.55349 1.000 17.45981 ? 80  LYS A O   1 
ATOM   515  C  CB  . LYS A 1 80  ? 16.25402 14.85454 -14.69944 1.000 18.51866 ? 80  LYS A CB  1 
ATOM   516  C  CG  . LYS A 1 80  ? 15.66068 13.78413 -15.62271 1.000 20.54626 ? 80  LYS A CG  1 
ATOM   517  C  CD  . LYS A 1 80  ? 16.32461 12.41714 -15.40769 1.000 22.78561 ? 80  LYS A CD  1 
ATOM   518  C  CE  . LYS A 1 80  ? 15.64176 11.31289 -16.20993 1.000 25.05534 ? 80  LYS A CE  1 
ATOM   519  N  NZ  . LYS A 1 80  ? 14.35021 10.91910 -15.58031 1.000 26.92412 ? 80  LYS A NZ  1 
ATOM   520  N  N   . ASN A 1 81  ? 13.32598 16.21436 -15.73454 1.000 17.77241 ? 81  ASN A N   1 
ATOM   521  C  CA  . ASN A 1 81  ? 11.91011 15.87552 -15.76719 1.000 17.62919 ? 81  ASN A CA  1 
ATOM   522  C  C   . ASN A 1 81  ? 11.61180 15.34150 -17.16471 1.000 18.69466 ? 81  ASN A C   1 
ATOM   523  O  O   . ASN A 1 81  ? 12.52862 14.98710 -17.91437 1.000 20.92547 ? 81  ASN A O   1 
ATOM   524  C  CB  . ASN A 1 81  ? 11.01401 17.03115 -15.30084 1.000 18.62125 ? 81  ASN A CB  1 
ATOM   525  C  CG  . ASN A 1 81  ? 11.02030 18.20699 -16.25431 1.000 18.78364 ? 81  ASN A CG  1 
ATOM   526  O  OD1 . ASN A 1 81  ? 11.58674 18.13121 -17.34833 1.000 19.45837 ? 81  ASN A OD1 1 
ATOM   527  N  ND2 . ASN A 1 81  ? 10.37985 19.30269 -15.84530 1.000 18.77343 ? 81  ASN A ND2 1 
ATOM   528  N  N   . ASN A 1 82  ? 10.32758 15.25482 -17.52763 1.000 19.29223 ? 82  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 82  ? 10.02045 14.65246 -18.82171 1.000 22.75314 ? 82  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 82  ? 10.35685 15.55904 -19.99852 1.000 23.57950 ? 82  ASN A C   1 
ATOM   531  O  O   . ASN A 1 82  ? 10.32612 15.09564 -21.14691 1.000 25.64232 ? 82  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 82  ? 8.54765  14.23529 -18.90925 1.000 28.08790 ? 82  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 82  ? 8.24952  13.00022 -18.10232 1.000 34.96933 ? 82  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 82  ? 7.13671  12.83230 -17.60250 1.000 38.33573 ? 82  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 82  ? 9.26426  12.15816 -17.90431 1.000 37.57271 ? 82  ASN A ND2 1 
ATOM   536  N  N   . TYR A 1 83  ? 10.64297 16.83530 -19.75160 1.000 21.39416 ? 83  TYR A N   1 
ATOM   537  C  CA  . TYR A 1 83  ? 10.90505 17.81399 -20.79994 1.000 21.26892 ? 83  TYR A CA  1 
ATOM   538  C  C   . TYR A 1 83  ? 12.37942 18.06728 -21.02419 1.000 21.13748 ? 83  TYR A C   1 
ATOM   539  O  O   . TYR A 1 83  ? 12.80453 18.26918 -22.16425 1.000 21.92054 ? 83  TYR A O   1 
ATOM   540  C  CB  . TYR A 1 83  ? 10.24966 19.14354 -20.42031 1.000 21.60306 ? 83  TYR A CB  1 
ATOM   541  C  CG  . TYR A 1 83  ? 8.77227  19.02302 -20.24765 1.000 24.03900 ? 83  TYR A CG  1 
ATOM   542  C  CD1 . TYR A 1 83  ? 7.94995  18.99147 -21.34826 1.000 27.79614 ? 83  TYR A CD1 1 
ATOM   543  C  CD2 . TYR A 1 83  ? 8.20285  18.93714 -19.00345 1.000 25.13950 ? 83  TYR A CD2 1 
ATOM   544  C  CE1 . TYR A 1 83  ? 6.59988  18.87456 -21.21808 1.000 30.66329 ? 83  TYR A CE1 1 
ATOM   545  C  CE2 . TYR A 1 83  ? 6.84632  18.81670 -18.85480 1.000 29.07729 ? 83  TYR A CE2 1 
ATOM   546  C  CZ  . TYR A 1 83  ? 6.04538  18.78781 -19.97399 1.000 31.75703 ? 83  TYR A CZ  1 
ATOM   547  O  OH  . TYR A 1 83  ? 4.68868  18.68031 -19.85799 1.000 34.76360 ? 83  TYR A OH  1 
ATOM   548  N  N   . ARG A 1 84  ? 13.17215 18.09921 -19.96037 1.000 20.13492 ? 84  ARG A N   1 
ATOM   549  C  CA  . ARG A 1 84  ? 14.56004 18.51980 -20.07136 1.000 19.89650 ? 84  ARG A CA  1 
ATOM   550  C  C   . ARG A 1 84  ? 15.38399 17.82097 -19.00802 1.000 19.71300 ? 84  ARG A C   1 
ATOM   551  O  O   . ARG A 1 84  ? 14.85685 17.33942 -18.00661 1.000 20.01706 ? 84  ARG A O   1 
ATOM   552  C  CB  . ARG A 1 84  ? 14.70528 20.01463 -19.79614 1.000 22.92116 ? 84  ARG A CB  1 
ATOM   553  C  CG  . ARG A 1 84  ? 14.10380 20.90027 -20.83639 1.000 26.34505 ? 84  ARG A CG  1 
ATOM   554  C  CD  . ARG A 1 84  ? 14.43562 22.29291 -20.41382 1.000 28.79114 ? 84  ARG A CD  1 
ATOM   555  N  NE  . ARG A 1 84  ? 13.64413 23.23676 -21.18160 1.000 29.48467 ? 84  ARG A NE  1 
ATOM   556  C  CZ  . ARG A 1 84  ? 13.96418 24.50927 -21.30642 1.000 30.06358 ? 84  ARG A CZ  1 
ATOM   557  N  NH1 . ARG A 1 84  ? 15.10684 24.97801 -20.82949 1.000 28.98924 ? 84  ARG A NH1 1 
ATOM   558  N  NH2 . ARG A 1 84  ? 13.12300 25.32686 -21.92697 1.000 30.66995 ? 84  ARG A NH2 1 
ATOM   559  N  N   . ASN A 1 85  ? 16.69296 17.81486 -19.22495 1.000 18.39172 ? 85  ASN A N   1 
ATOM   560  C  CA  . ASN A 1 85  ? 17.63962 17.36127 -18.21031 1.000 18.91149 ? 85  ASN A CA  1 
ATOM   561  C  C   . ASN A 1 85  ? 18.87108 18.25891 -18.23051 1.000 19.57591 ? 85  ASN A C   1 
ATOM   562  O  O   . ASN A 1 85  ? 19.66727 18.20998 -19.18189 1.000 20.67135 ? 85  ASN A O   1 
ATOM   563  C  CB  . ASN A 1 85  ? 18.04114 15.91387 -18.44985 1.000 18.05758 ? 85  ASN A CB  1 
ATOM   564  C  CG  . ASN A 1 85  ? 18.82881 15.35170 -17.28749 1.000 18.31029 ? 85  ASN A CG  1 
ATOM   565  O  OD1 . ASN A 1 85  ? 19.25334 16.10011 -16.39336 1.000 18.74425 ? 85  ASN A OD1 1 
ATOM   566  N  ND2 . ASN A 1 85  ? 19.01151 14.03513 -17.26966 1.000 18.94652 ? 85  ASN A ND2 1 
ATOM   567  N  N   . ALA A 1 86  ? 19.02659 19.07551 -17.18807 1.000 17.74935 ? 86  ALA A N   1 
ATOM   568  C  CA  . ALA A 1 86  ? 20.12978 20.00984 -17.09424 1.000 17.72026 ? 86  ALA A CA  1 
ATOM   569  C  C   . ALA A 1 86  ? 21.32416 19.42204 -16.35822 1.000 17.98405 ? 86  ALA A C   1 
ATOM   570  O  O   . ALA A 1 86  ? 22.24851 20.16466 -16.02439 1.000 19.21313 ? 86  ALA A O   1 
ATOM   571  C  CB  . ALA A 1 86  ? 19.65757 21.29007 -16.41053 1.000 18.41509 ? 86  ALA A CB  1 
ATOM   572  N  N   . HIS A 1 87  ? 21.29997 18.12013 -16.06318 1.000 16.93726 ? 87  HIS A N   1 
ATOM   573  C  CA  . HIS A 1 87  ? 22.43678 17.42112 -15.45283 1.000 17.18731 ? 87  HIS A CA  1 
ATOM   574  C  C   . HIS A 1 87  ? 23.00714 18.21653 -14.27922 1.000 16.14529 ? 87  HIS A C   1 
ATOM   575  O  O   . HIS A 1 87  ? 24.20262 18.53502 -14.21224 1.000 16.82347 ? 87  HIS A O   1 
ATOM   576  C  CB  . HIS A 1 87  ? 23.52051 17.10137 -16.48391 1.000 18.85737 ? 87  HIS A CB  1 
ATOM   577  C  CG  . HIS A 1 87  ? 23.02731 16.27593 -17.63765 1.000 19.52582 ? 87  HIS A CG  1 
ATOM   578  N  ND1 . HIS A 1 87  ? 22.33094 15.09724 -17.45610 1.000 19.29456 ? 87  HIS A ND1 1 
ATOM   579  C  CD2 . HIS A 1 87  ? 23.07848 16.48184 -18.97622 1.000 20.80250 ? 87  HIS A CD2 1 
ATOM   580  C  CE1 . HIS A 1 87  ? 21.99333 14.60255 -18.63326 1.000 19.10339 ? 87  HIS A CE1 1 
ATOM   581  N  NE2 . HIS A 1 87  ? 22.43571 15.42214 -19.57879 1.000 20.16581 ? 87  HIS A NE2 1 
ATOM   582  N  N   . SER A 1 88  ? 22.13576 18.48640 -13.31559 1.000 16.38547 ? 88  SER A N   1 
ATOM   583  C  CA  . SER A 1 88  ? 22.51223 19.32239 -12.18018 1.000 15.52480 ? 88  SER A CA  1 
ATOM   584  C  C   . SER A 1 88  ? 21.48134 19.14640 -11.07949 1.000 15.94346 ? 88  SER A C   1 
ATOM   585  O  O   . SER A 1 88  ? 20.38240 18.62731 -11.30541 1.000 16.62603 ? 88  SER A O   1 
ATOM   586  C  CB  . SER A 1 88  ? 22.64985 20.79499 -12.59854 1.000 17.37649 ? 88  SER A CB  1 
ATOM   587  O  OG  . SER A 1 88  ? 21.48099 21.23714 -13.28133 1.000 17.43114 ? 88  SER A OG  1 
ATOM   588  N  N   . ALA A 1 89  ? 21.83973 19.60135 -9.88531  1.000 15.06099 ? 89  ALA A N   1 
ATOM   589  C  CA  . ALA A 1 89  ? 20.92581 19.49677 -8.75859  1.000 13.91129 ? 89  ALA A CA  1 
ATOM   590  C  C   . ALA A 1 89  ? 21.12920 20.72326 -7.89384  1.000 13.69996 ? 89  ALA A C   1 
ATOM   591  O  O   . ALA A 1 89  ? 22.26583 21.12385 -7.66283  1.000 14.77870 ? 89  ALA A O   1 
ATOM   592  C  CB  . ALA A 1 89  ? 21.19956 18.22255 -7.92519  1.000 15.01067 ? 89  ALA A CB  1 
ATOM   593  N  N   . THR A 1 90  ? 20.04612 21.28134 -7.37051  1.000 13.15383 ? 90  THR A N   1 
ATOM   594  C  CA  . THR A 1 90  ? 20.13407 22.34353 -6.37644  1.000 13.01819 ? 90  THR A CA  1 
ATOM   595  C  C   . THR A 1 90  ? 19.65625 21.84706 -5.02477  1.000 12.66231 ? 90  THR A C   1 
ATOM   596  O  O   . THR A 1 90  ? 18.61991 21.16566 -4.93618  1.000 13.16160 ? 90  THR A O   1 
ATOM   597  C  CB  . THR A 1 90  ? 19.28923 23.53181 -6.80603  1.000 13.35716 ? 90  THR A CB  1 
ATOM   598  O  OG1 . THR A 1 90  ? 19.76016 23.97502 -8.06609  1.000 13.94986 ? 90  THR A OG1 1 
ATOM   599  C  CG2 . THR A 1 90  ? 19.37443 24.68539 -5.80795  1.000 15.02038 ? 90  THR A CG2 1 
ATOM   600  N  N   . THR A 1 91  ? 20.39824 22.18842 -3.97030  1.000 12.73210 ? 91  THR A N   1 
ATOM   601  C  CA  . THR A 1 91  ? 19.88321 22.02367 -2.61288  1.000 12.21081 ? 91  THR A CA  1 
ATOM   602  C  C   . THR A 1 91  ? 19.66759 23.39284 -1.97550  1.000 12.15697 ? 91  THR A C   1 
ATOM   603  O  O   . THR A 1 91  ? 20.55007 24.25301 -2.04911  1.000 14.15895 ? 91  THR A O   1 
ATOM   604  C  CB  . THR A 1 91  ? 20.81805 21.20432 -1.71124  1.000 13.55243 ? 91  THR A CB  1 
ATOM   605  O  OG1 . THR A 1 91  ? 22.09623 21.82655 -1.59464  1.000 14.69209 ? 91  THR A OG1 1 
ATOM   606  C  CG2 . THR A 1 91  ? 21.02922 19.83173 -2.30169  1.000 14.91094 ? 91  THR A CG2 1 
ATOM   607  N  N   . TRP A 1 92  ? 18.50142 23.59614 -1.34941  1.000 12.73979 ? 92  TRP A N   1 
ATOM   608  C  CA  . TRP A 1 92  ? 18.23426 24.79887 -0.56542  1.000 12.31636 ? 92  TRP A CA  1 
ATOM   609  C  C   . TRP A 1 92  ? 18.30672 24.41954 0.90682   1.000 12.49641 ? 92  TRP A C   1 
ATOM   610  O  O   . TRP A 1 92  ? 17.67388 23.43836 1.32877   1.000 14.01860 ? 92  TRP A O   1 
ATOM   611  C  CB  . TRP A 1 92  ? 16.82726 25.36053 -0.84470  1.000 12.18127 ? 92  TRP A CB  1 
ATOM   612  C  CG  . TRP A 1 92  ? 16.60367 25.97953 -2.18428  1.000 12.96424 ? 92  TRP A CG  1 
ATOM   613  C  CD1 . TRP A 1 92  ? 16.52466 27.31667 -2.46729  1.000 13.44710 ? 92  TRP A CD1 1 
ATOM   614  C  CD2 . TRP A 1 92  ? 16.36380 25.29250 -3.43285  1.000 13.12743 ? 92  TRP A CD2 1 
ATOM   615  N  NE1 . TRP A 1 92  ? 16.27270 27.50507 -3.81832  1.000 14.18133 ? 92  TRP A NE1 1 
ATOM   616  C  CE2 . TRP A 1 92  ? 16.13860 26.27709 -4.42434  1.000 13.71806 ? 92  TRP A CE2 1 
ATOM   617  C  CE3 . TRP A 1 92  ? 16.26931 23.93995 -3.79887  1.000 13.65036 ? 92  TRP A CE3 1 
ATOM   618  C  CZ2 . TRP A 1 92  ? 15.86692 25.94805 -5.77317  1.000 15.62026 ? 92  TRP A CZ2 1 
ATOM   619  C  CZ3 . TRP A 1 92  ? 15.99916 23.61426 -5.12629  1.000 14.41465 ? 92  TRP A CZ3 1 
ATOM   620  C  CH2 . TRP A 1 92  ? 15.78140 24.62347 -6.09869  1.000 15.93556 ? 92  TRP A CH2 1 
ATOM   621  N  N   . SER A 1 93  ? 19.03709 25.21098 1.68058   1.000 13.31427 ? 93  SER A N   1 
ATOM   622  C  CA  . SER A 1 93  ? 19.19697 25.02012 3.11891   1.000 14.04697 ? 93  SER A CA  1 
ATOM   623  C  C   . SER A 1 93  ? 18.76265 26.31549 3.80534   1.000 13.92978 ? 93  SER A C   1 
ATOM   624  O  O   . SER A 1 93  ? 19.18815 27.40922 3.40121   1.000 14.85795 ? 93  SER A O   1 
ATOM   625  C  CB  . SER A 1 93  ? 20.67044 24.74396 3.39996   1.000 13.43853 ? 93  SER A CB  1 
ATOM   626  O  OG  . SER A 1 93  ? 20.82598 24.48154 4.78140   1.000 15.15298 ? 93  SER A OG  1 
ATOM   627  N  N   . GLY A 1 94  ? 17.84657 26.23504 4.76626   1.000 14.04437 ? 94  GLY A N   1 
ATOM   628  C  CA  . GLY A 1 94  ? 17.32290 27.48628 5.27049   1.000 14.91704 ? 94  GLY A CA  1 
ATOM   629  C  C   . GLY A 1 94  ? 16.49835 27.33587 6.51774   1.000 14.79688 ? 94  GLY A C   1 
ATOM   630  O  O   . GLY A 1 94  ? 16.58872 26.32115 7.22377   1.000 16.35541 ? 94  GLY A O   1 
ATOM   631  N  N   . GLN A 1 95  ? 15.68385 28.36614 6.78594   1.000 15.41194 ? 95  GLN A N   1 
ATOM   632  C  CA  . GLN A 1 95  ? 14.76468 28.28886 7.90495   1.000 15.77166 ? 95  GLN A CA  1 
ATOM   633  C  C   . GLN A 1 95  ? 13.44743 28.95521 7.54662   1.000 15.58911 ? 95  GLN A C   1 
ATOM   634  O  O   . GLN A 1 95  ? 13.41136 29.97065 6.83313   1.000 15.99234 ? 95  GLN A O   1 
ATOM   635  C  CB  . GLN A 1 95  ? 15.37165 28.84929 9.19028   1.000 18.10296 ? 95  GLN A CB  1 
ATOM   636  C  CG  . GLN A 1 95  ? 15.78542 30.31295 9.15080   1.000 18.80373 ? 95  GLN A CG  1 
ATOM   637  C  CD  . GLN A 1 95  ? 16.39629 30.73659 10.47793  1.000 18.25736 ? 95  GLN A CD  1 
ATOM   638  O  OE1 . GLN A 1 95  ? 15.86153 30.41177 11.53258  1.000 18.06068 ? 95  GLN A OE1 1 
ATOM   639  N  NE2 . GLN A 1 95  ? 17.53304 31.43767 10.43016  1.000 19.01288 ? 95  GLN A NE2 1 
ATOM   640  N  N   . TYR A 1 96  ? 12.37296 28.37764 8.08610   1.000 16.60950 ? 96  TYR A N   1 
ATOM   641  C  CA  . TYR A 1 96  ? 11.03530 28.94688 7.99780   1.000 16.96163 ? 96  TYR A CA  1 
ATOM   642  C  C   . TYR A 1 96  ? 10.81872 29.86405 9.19022   1.000 18.77887 ? 96  TYR A C   1 
ATOM   643  O  O   . TYR A 1 96  ? 11.12492 29.48994 10.33380  1.000 18.95321 ? 96  TYR A O   1 
ATOM   644  C  CB  . TYR A 1 96  ? 10.02269 27.80032 8.01909   1.000 18.42027 ? 96  TYR A CB  1 
ATOM   645  C  CG  . TYR A 1 96  ? 8.63549  28.18511 8.39520   1.000 19.39259 ? 96  TYR A CG  1 
ATOM   646  C  CD1 . TYR A 1 96  ? 7.75056  28.69105 7.45085   1.000 19.55210 ? 96  TYR A CD1 1 
ATOM   647  C  CD2 . TYR A 1 96  ? 8.17982  28.02431 9.69971   1.000 21.75549 ? 96  TYR A CD2 1 
ATOM   648  C  CE1 . TYR A 1 96  ? 6.44970  29.03523 7.80533   1.000 21.63197 ? 96  TYR A CE1 1 
ATOM   649  C  CE2 . TYR A 1 96  ? 6.88368  28.36471 10.05099  1.000 23.49432 ? 96  TYR A CE2 1 
ATOM   650  C  CZ  . TYR A 1 96  ? 6.02572  28.86243 9.10681   1.000 22.51947 ? 96  TYR A CZ  1 
ATOM   651  O  OH  . TYR A 1 96  ? 4.74879  29.19520 9.48061   1.000 25.84516 ? 96  TYR A OH  1 
ATOM   652  N  N   . VAL A 1 97  ? 10.32027 31.06564 8.91188   1.000 19.55940 ? 97  VAL A N   1 
ATOM   653  C  CA  . VAL A 1 97  ? 10.03583 32.07645 9.92030   1.000 21.96322 ? 97  VAL A CA  1 
ATOM   654  C  C   . VAL A 1 97  ? 8.54938  32.36832 9.79207   1.000 24.11094 ? 97  VAL A C   1 
ATOM   655  O  O   . VAL A 1 97  ? 8.09593  32.89446 8.76743   1.000 25.65883 ? 97  VAL A O   1 
ATOM   656  C  CB  . VAL A 1 97  ? 10.88222 33.34327 9.69689   1.000 24.06930 ? 97  VAL A CB  1 
ATOM   657  C  CG1 . VAL A 1 97  ? 10.59957 34.39508 10.76736  1.000 26.48588 ? 97  VAL A CG1 1 
ATOM   658  C  CG2 . VAL A 1 97  ? 12.37371 32.99627 9.65553   1.000 24.88828 ? 97  VAL A CG2 1 
ATOM   659  N  N   . GLY A 1 98  ? 7.78511  31.99130 10.80410  1.000 26.02922 ? 98  GLY A N   1 
ATOM   660  C  CA  . GLY A 1 98  ? 6.34881  32.16887 10.76723  1.000 29.22583 ? 98  GLY A CA  1 
ATOM   661  C  C   . GLY A 1 98  ? 5.93863  33.60735 11.00939  1.000 33.92468 ? 98  GLY A C   1 
ATOM   662  O  O   . GLY A 1 98  ? 6.75828  34.48054 11.28234  1.000 34.23206 ? 98  GLY A O   1 
ATOM   663  N  N   . GLY A 1 99  ? 4.63754  33.85535 10.88458  1.000 38.70907 ? 99  GLY A N   1 
ATOM   664  C  CA  . GLY A 1 99  ? 4.05819  35.12914 11.24716  1.000 41.72212 ? 99  GLY A CA  1 
ATOM   665  C  C   . GLY A 1 99  ? 3.23507  35.69827 10.11751  1.000 44.90122 ? 99  GLY A C   1 
ATOM   666  O  O   . GLY A 1 99  ? 2.99802  35.04962 9.09118   1.000 47.12754 ? 99  GLY A O   1 
ATOM   667  N  N   . ALA A 1 100 ? 2.80757  36.94875 10.29334  1.000 44.93737 ? 100 ALA A N   1 
ATOM   668  C  CA  . ALA A 1 100 ? 1.91949  37.56218 9.31351   1.000 44.67017 ? 100 ALA A CA  1 
ATOM   669  C  C   . ALA A 1 100 ? 2.60310  37.71134 7.96626   1.000 45.68175 ? 100 ALA A C   1 
ATOM   670  O  O   . ALA A 1 100 ? 1.93866  37.68306 6.92195   1.000 47.49041 ? 100 ALA A O   1 
ATOM   671  C  CB  . ALA A 1 100 ? 1.41387  38.91201 9.83235   1.000 44.34363 ? 100 ALA A CB  1 
ATOM   672  N  N   . GLN A 1 101 ? 3.92598  37.85679 7.97055   1.000 43.01300 ? 101 GLN A N   1 
ATOM   673  C  CA  . GLN A 1 101 ? 4.71622  37.89509 6.75099   1.000 42.38150 ? 101 GLN A CA  1 
ATOM   674  C  C   . GLN A 1 101 ? 5.63659  36.68049 6.74039   1.000 35.43349 ? 101 GLN A C   1 
ATOM   675  O  O   . GLN A 1 101 ? 6.86690  36.81618 6.76855   1.000 35.65095 ? 101 GLN A O   1 
ATOM   676  C  CB  . GLN A 1 101 ? 5.54942  39.17596 6.70002   1.000 48.71283 ? 101 GLN A CB  1 
ATOM   677  C  CG  . GLN A 1 101 ? 4.73007  40.45805 6.58504   1.000 55.48579 ? 101 GLN A CG  1 
ATOM   678  C  CD  . GLN A 1 101 ? 3.96084  40.53506 5.27678   1.000 60.95470 ? 101 GLN A CD  1 
ATOM   679  O  OE1 . GLN A 1 101 ? 2.76012  40.26261 5.23252   1.000 63.37825 ? 101 GLN A OE1 1 
ATOM   680  N  NE2 . GLN A 1 101 ? 4.65398  40.89433 4.20127   1.000 62.38692 ? 101 GLN A NE2 1 
ATOM   681  N  N   . ALA A 1 102 ? 5.05908  35.48315 6.72018   1.000 31.22647 ? 102 ALA A N   1 
ATOM   682  C  CA  . ALA A 1 102 ? 5.88468  34.28311 6.79023   1.000 26.28106 ? 102 ALA A CA  1 
ATOM   683  C  C   . ALA A 1 102 ? 6.89208  34.23891 5.65081   1.000 23.91242 ? 102 ALA A C   1 
ATOM   684  O  O   . ALA A 1 102 ? 6.62842  34.68273 4.52808   1.000 24.94859 ? 102 ALA A O   1 
ATOM   685  C  CB  . ALA A 1 102 ? 5.01171  33.02964 6.72438   1.000 27.13594 ? 102 ALA A CB  1 
ATOM   686  N  N   . ARG A 1 103 ? 8.04498  33.64502 5.94334   1.000 20.13258 ? 103 ARG A N   1 
ATOM   687  C  CA  . ARG A 1 103 ? 9.13360  33.54280 4.97942   1.000 19.32144 ? 103 ARG A CA  1 
ATOM   688  C  C   . ARG A 1 103 ? 9.86713  32.23159 5.14660   1.000 18.89868 ? 103 ARG A C   1 
ATOM   689  O  O   . ARG A 1 103 ? 9.98058  31.70244 6.25501   1.000 19.55473 ? 103 ARG A O   1 
ATOM   690  C  CB  . ARG A 1 103 ? 10.18807 34.65165 5.20335   1.000 25.18763 ? 103 ARG A CB  1 
ATOM   691  C  CG  . ARG A 1 103 ? 9.65955  36.04886 4.97894   0.680 28.95623 ? 103 ARG A CG  1 
ATOM   692  C  CD  . ARG A 1 103 ? 9.93662  36.49369 3.56521   0.660 30.79229 ? 103 ARG A CD  1 
ATOM   693  N  NE  . ARG A 1 103 ? 9.78396  37.93203 3.38029   0.750 32.24956 ? 103 ARG A NE  1 
ATOM   694  C  CZ  . ARG A 1 103 ? 8.62253  38.57401 3.42493   0.420 33.88025 ? 103 ARG A CZ  1 
ATOM   695  N  NH1 . ARG A 1 103 ? 7.48750  37.93947 3.67828   0.830 34.66824 ? 103 ARG A NH1 1 
ATOM   696  N  NH2 . ARG A 1 103 ? 8.59759  39.88631 3.21208   0.570 34.39227 ? 103 ARG A NH2 1 
ATOM   697  N  N   . ILE A 1 104 ? 10.40603 31.73427 4.03710   1.000 17.61702 ? 104 ILE A N   1 
ATOM   698  C  CA  . ILE A 1 104 ? 11.46732 30.73209 4.08958   1.000 16.80318 ? 104 ILE A CA  1 
ATOM   699  C  C   . ILE A 1 104 ? 12.72197 31.37739 3.51189   1.000 16.12543 ? 104 ILE A C   1 
ATOM   700  O  O   . ILE A 1 104 ? 12.76609 31.69524 2.31628   1.000 16.85340 ? 104 ILE A O   1 
ATOM   701  C  CB  . ILE A 1 104 ? 11.09659 29.42461 3.36407   1.000 16.85429 ? 104 ILE A CB  1 
ATOM   702  C  CG1 . ILE A 1 104 ? 9.82423  28.80228 3.97520   1.000 18.64147 ? 104 ILE A CG1 1 
ATOM   703  C  CG2 . ILE A 1 104 ? 12.28752 28.44000 3.42209   1.000 17.54044 ? 104 ILE A CG2 1 
ATOM   704  C  CD1 . ILE A 1 104 ? 9.28434  27.62020 3.15568   1.000 19.41485 ? 104 ILE A CD1 1 
ATOM   705  N  N   . ASN A 1 105 ? 13.73833 31.59089 4.35524   1.000 14.99370 ? 105 ASN A N   1 
ATOM   706  C  CA  . ASN A 1 105 ? 14.98356 32.23929 3.94081   1.000 14.94951 ? 105 ASN A CA  1 
ATOM   707  C  C   . ASN A 1 105 ? 16.02891 31.15868 3.70175   1.000 14.93171 ? 105 ASN A C   1 
ATOM   708  O  O   . ASN A 1 105 ? 16.30580 30.36126 4.60950   1.000 15.89536 ? 105 ASN A O   1 
ATOM   709  C  CB  . ASN A 1 105 ? 15.45111 33.17369 5.05038   1.000 17.62617 ? 105 ASN A CB  1 
ATOM   710  C  CG  . ASN A 1 105 ? 14.49109 34.32239 5.25328   1.000 20.53963 ? 105 ASN A CG  1 
ATOM   711  O  OD1 . ASN A 1 105 ? 13.98402 34.86749 4.28513   1.000 22.08555 ? 105 ASN A OD1 1 
ATOM   712  N  ND2 . ASN A 1 105 ? 14.20167 34.65755 6.50445   1.000 22.91205 ? 105 ASN A ND2 1 
ATOM   713  N  N   . THR A 1 106 ? 16.58900 31.10297 2.48022   1.000 14.48389 ? 106 THR A N   1 
ATOM   714  C  CA  A THR A 1 106 ? 17.49027 30.02219 2.10507   0.990 14.05975 ? 106 THR A CA  1 
ATOM   715  C  CA  B THR A 1 106 ? 17.48193 30.01749 2.11510   0.010 14.56910 ? 106 THR A CA  1 
ATOM   716  C  C   . THR A 1 106 ? 18.78211 30.52081 1.49032   1.000 14.46159 ? 106 THR A C   1 
ATOM   717  O  O   . THR A 1 106 ? 18.87820 31.63747 0.95742   1.000 14.10698 ? 106 THR A O   1 
ATOM   718  C  CB  A THR A 1 106 ? 16.86575 29.07490 1.06985   0.990 14.33989 ? 106 THR A CB  1 
ATOM   719  C  CB  B THR A 1 106 ? 16.77342 29.03551 1.16550   0.010 14.45347 ? 106 THR A CB  1 
ATOM   720  O  OG1 A THR A 1 106 ? 16.78715 29.72347 -0.21435  0.990 14.44471 ? 106 THR A OG1 1 
ATOM   721  O  OG1 B THR A 1 106 ? 15.55542 28.58370 1.77081   0.010 14.39534 ? 106 THR A OG1 1 
ATOM   722  C  CG2 A THR A 1 106 ? 15.48481 28.61122 1.54188   0.990 15.74297 ? 106 THR A CG2 1 
ATOM   723  C  CG2 B THR A 1 106 ? 17.64994 27.83334 0.87749   0.010 14.38101 ? 106 THR A CG2 1 
ATOM   724  N  N   . GLN A 1 107 ? 19.77869 29.64636 1.55193   1.000 13.02911 ? 107 GLN A N   1 
ATOM   725  C  CA  . GLN A 1 107 ? 20.94630 29.70265 0.68854   1.000 13.25836 ? 107 GLN A CA  1 
ATOM   726  C  C   . GLN A 1 107 ? 20.95998 28.38637 -0.06474  1.000 12.69227 ? 107 GLN A C   1 
ATOM   727  O  O   . GLN A 1 107 ? 20.41502 27.38279 0.41721   1.000 14.62720 ? 107 GLN A O   1 
ATOM   728  C  CB  . GLN A 1 107 ? 22.22761 29.92545 1.51382   1.000 15.71355 ? 107 GLN A CB  1 
ATOM   729  C  CG  A GLN A 1 107 ? 22.13823 31.28825 2.20005   0.730 16.28150 ? 107 GLN A CG  1 
ATOM   730  C  CG  B GLN A 1 107 ? 22.25112 31.25232 2.21751   0.270 17.75550 ? 107 GLN A CG  1 
ATOM   731  C  CD  A GLN A 1 107 ? 23.40306 31.71146 2.89777   0.730 14.83750 ? 107 GLN A CD  1 
ATOM   732  C  CD  B GLN A 1 107 ? 23.40018 32.11534 1.77545   0.270 19.59712 ? 107 GLN A CD  1 
ATOM   733  O  OE1 A GLN A 1 107 ? 24.32761 32.20664 2.27635   0.730 17.48826 ? 107 GLN A OE1 1 
ATOM   734  O  OE1 B GLN A 1 107 ? 23.69507 32.22964 0.57865   0.270 22.15164 ? 107 GLN A OE1 1 
ATOM   735  N  NE2 A GLN A 1 107 ? 23.45568 31.50484 4.21603   0.730 13.76701 ? 107 GLN A NE2 1 
ATOM   736  N  NE2 B GLN A 1 107 ? 24.05969 32.73927 2.74011   0.270 19.06070 ? 107 GLN A NE2 1 
ATOM   737  N  N   . TRP A 1 108 ? 21.55065 28.39170 -1.25301  1.000 13.10164 ? 108 TRP A N   1 
ATOM   738  C  CA  . TRP A 1 108 ? 21.46979 27.20335 -2.10139  1.000 12.73155 ? 108 TRP A CA  1 
ATOM   739  C  C   . TRP A 1 108 ? 22.78987 26.90642 -2.78119  1.000 12.88620 ? 108 TRP A C   1 
ATOM   740  O  O   . TRP A 1 108 ? 23.62650 27.79117 -2.99915  1.000 13.54197 ? 108 TRP A O   1 
ATOM   741  C  CB  . TRP A 1 108 ? 20.30301 27.27434 -3.13806  1.000 13.02653 ? 108 TRP A CB  1 
ATOM   742  C  CG  . TRP A 1 108 ? 20.25954 28.49326 -4.02105  1.000 12.47457 ? 108 TRP A CG  1 
ATOM   743  C  CD1 . TRP A 1 108 ? 19.39445 29.54427 -3.90270  1.000 13.70308 ? 108 TRP A CD1 1 
ATOM   744  C  CD2 . TRP A 1 108 ? 21.05585 28.75932 -5.17585  1.000 12.88931 ? 108 TRP A CD2 1 
ATOM   745  N  NE1 . TRP A 1 108 ? 19.60625 30.44405 -4.90975  1.000 14.30063 ? 108 TRP A NE1 1 
ATOM   746  C  CE2 . TRP A 1 108 ? 20.62456 29.99245 -5.70573  1.000 14.14460 ? 108 TRP A CE2 1 
ATOM   747  C  CE3 . TRP A 1 108 ? 22.08367 28.06092 -5.83191  1.000 13.92408 ? 108 TRP A CE3 1 
ATOM   748  C  CZ2 . TRP A 1 108 ? 21.18328 30.55798 -6.85529  1.000 13.56475 ? 108 TRP A CZ2 1 
ATOM   749  C  CZ3 . TRP A 1 108 ? 22.66123 28.63151 -6.95545  1.000 13.08492 ? 108 TRP A CZ3 1 
ATOM   750  C  CH2 . TRP A 1 108 ? 22.21256 29.87798 -7.46292  1.000 13.84091 ? 108 TRP A CH2 1 
ATOM   751  N  N   . LEU A 1 109 ? 22.96863 25.63282 -3.12139  1.000 12.68874 ? 109 LEU A N   1 
ATOM   752  C  CA  . LEU A 1 109 ? 24.13440 25.14271 -3.86470  1.000 12.85812 ? 109 LEU A CA  1 
ATOM   753  C  C   . LEU A 1 109 ? 23.62862 24.37565 -5.07190  1.000 13.40361 ? 109 LEU A C   1 
ATOM   754  O  O   . LEU A 1 109 ? 22.86126 23.41894 -4.90913  1.000 14.73996 ? 109 LEU A O   1 
ATOM   755  C  CB  . LEU A 1 109 ? 24.98567 24.19157 -3.02972  1.000 13.67767 ? 109 LEU A CB  1 
ATOM   756  C  CG  . LEU A 1 109 ? 25.65478 24.74777 -1.79091  1.000 13.64454 ? 109 LEU A CG  1 
ATOM   757  C  CD1 . LEU A 1 109 ? 26.22559 23.61480 -0.94688  1.000 14.91941 ? 109 LEU A CD1 1 
ATOM   758  C  CD2 . LEU A 1 109 ? 26.73314 25.75253 -2.17016  1.000 13.77249 ? 109 LEU A CD2 1 
ATOM   759  N  N   . LEU A 1 110 ? 24.04573 24.79482 -6.27104  1.000 13.03108 ? 110 LEU A N   1 
ATOM   760  C  CA  A LEU A 1 110 ? 23.64289 24.13148 -7.51173  0.520 13.81704 ? 110 LEU A CA  1 
ATOM   761  C  CA  B LEU A 1 110 ? 23.64281 24.15382 -7.52426  0.480 13.53121 ? 110 LEU A CA  1 
ATOM   762  C  C   . LEU A 1 110 ? 24.88978 23.48373 -8.10280  1.000 13.74097 ? 110 LEU A C   1 
ATOM   763  O  O   . LEU A 1 110 ? 25.80813 24.17844 -8.55088  1.000 14.52098 ? 110 LEU A O   1 
ATOM   764  C  CB  A LEU A 1 110 ? 23.02141 25.12360 -8.48987  0.520 15.78246 ? 110 LEU A CB  1 
ATOM   765  C  CB  B LEU A 1 110 ? 23.09691 25.22835 -8.46786  0.480 14.92488 ? 110 LEU A CB  1 
ATOM   766  C  CG  A LEU A 1 110 ? 22.48072 24.54077 -9.80244  0.520 16.91951 ? 110 LEU A CG  1 
ATOM   767  C  CG  B LEU A 1 110 ? 22.84494 24.99430 -9.96540  0.480 15.27652 ? 110 LEU A CG  1 
ATOM   768  C  CD1 A LEU A 1 110 ? 21.59893 25.56743 -10.48927 0.520 16.99474 ? 110 LEU A CD1 1 
ATOM   769  C  CD1 B LEU A 1 110 ? 22.07074 23.70587 -10.19142 0.480 15.50338 ? 110 LEU A CD1 1 
ATOM   770  C  CD2 A LEU A 1 110 ? 23.61401 24.07421 -10.73607 0.520 17.02299 ? 110 LEU A CD2 1 
ATOM   771  C  CD2 B LEU A 1 110 ? 22.10605 26.19810 -10.57238 0.480 15.03362 ? 110 LEU A CD2 1 
ATOM   772  N  N   . THR A 1 111 ? 24.93890 22.14819 -8.07710  1.000 14.14743 ? 111 THR A N   1 
ATOM   773  C  CA  . THR A 1 111 ? 26.08542 21.40135 -8.60037  1.000 14.54519 ? 111 THR A CA  1 
ATOM   774  C  C   . THR A 1 111 ? 25.71529 20.76302 -9.93016  1.000 14.31335 ? 111 THR A C   1 
ATOM   775  O  O   . THR A 1 111 ? 24.65014 20.14136 -10.05171 1.000 15.21567 ? 111 THR A O   1 
ATOM   776  C  CB  . THR A 1 111 ? 26.56078 20.32045 -7.62055  1.000 15.25555 ? 111 THR A CB  1 
ATOM   777  O  OG1 . THR A 1 111 ? 26.77226 20.89888 -6.32805  1.000 15.21142 ? 111 THR A OG1 1 
ATOM   778  C  CG2 . THR A 1 111 ? 27.87353 19.70545 -8.10480  1.000 15.14448 ? 111 THR A CG2 1 
ATOM   779  N  N   . ALA A 1 112 ? 26.58305 20.94786 -10.92888 1.000 14.10770 ? 112 ALA A N   1 
ATOM   780  C  CA  . ALA A 1 112 ? 26.45158 20.29679 -12.22423 1.000 15.81776 ? 112 ALA A CA  1 
ATOM   781  C  C   . ALA A 1 112 ? 27.29999 19.02848 -12.24227 1.000 15.84408 ? 112 ALA A C   1 
ATOM   782  O  O   . ALA A 1 112 ? 28.33713 18.95137 -11.58101 1.000 17.67139 ? 112 ALA A O   1 
ATOM   783  C  CB  . ALA A 1 112 ? 26.93306 21.22432 -13.32878 1.000 17.20626 ? 112 ALA A CB  1 
ATOM   784  N  N   . GLY A 1 113 ? 26.84411 18.02134 -12.98535 1.000 16.61065 ? 113 GLY A N   1 
ATOM   785  C  CA  . GLY A 1 113 ? 27.72643 16.92794 -13.36192 1.000 18.09250 ? 113 GLY A CA  1 
ATOM   786  C  C   . GLY A 1 113 ? 28.77685 17.43482 -14.34479 1.000 19.06079 ? 113 GLY A C   1 
ATOM   787  O  O   . GLY A 1 113 ? 28.42845 18.00134 -15.39324 1.000 22.39614 ? 113 GLY A O   1 
ATOM   788  N  N   . THR A 1 114 ? 30.05726 17.24838 -14.02529 1.000 18.63167 ? 114 THR A N   1 
ATOM   789  C  CA  . THR A 1 114 ? 31.15783 17.77561 -14.82420 1.000 18.58879 ? 114 THR A CA  1 
ATOM   790  C  C   . THR A 1 114 ? 32.20561 16.69522 -15.02028 1.000 19.41931 ? 114 THR A C   1 
ATOM   791  O  O   . THR A 1 114 ? 32.21974 15.68385 -14.32325 1.000 20.63541 ? 114 THR A O   1 
ATOM   792  C  CB  . THR A 1 114 ? 31.85871 18.95580 -14.11562 1.000 19.42956 ? 114 THR A CB  1 
ATOM   793  O  OG1 . THR A 1 114 ? 32.60696 18.49618 -12.97141 1.000 18.87748 ? 114 THR A OG1 1 
ATOM   794  C  CG2 . THR A 1 114 ? 30.85385 20.01923 -13.66563 1.000 19.04196 ? 114 THR A CG2 1 
ATOM   795  N  N   . THR A 1 115 ? 33.12163 16.93956 -15.95544 1.000 21.59471 ? 115 THR A N   1 
ATOM   796  C  CA  . THR A 1 115 ? 34.32333 16.12551 -15.99104 1.000 22.08913 ? 115 THR A CA  1 
ATOM   797  C  C   . THR A 1 115 ? 35.20366 16.50201 -14.80473 1.000 22.08150 ? 115 THR A C   1 
ATOM   798  O  O   . THR A 1 115 ? 35.00564 17.53494 -14.16148 1.000 21.40206 ? 115 THR A O   1 
ATOM   799  C  CB  . THR A 1 115 ? 35.11575 16.41150 -17.26385 1.000 24.50479 ? 115 THR A CB  1 
ATOM   800  O  OG1 . THR A 1 115 ? 35.46777 17.79612 -17.26568 1.000 25.66163 ? 115 THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 115 ? 34.28225 16.09710 -18.49921 1.000 26.75180 ? 115 THR A CG2 1 
ATOM   802  N  N   . GLU A 1 116 ? 36.19886 15.66020 -14.50366 1.000 24.13400 ? 116 GLU A N   1 
ATOM   803  C  CA  . GLU A 1 116 ? 37.08744 15.99759 -13.39442 1.000 24.83639 ? 116 GLU A CA  1 
ATOM   804  C  C   . GLU A 1 116 ? 37.83432 17.29715 -13.67317 1.000 23.99025 ? 116 GLU A C   1 
ATOM   805  O  O   . GLU A 1 116 ? 38.02289 18.11545 -12.76751 1.000 24.59467 ? 116 GLU A O   1 
ATOM   806  C  CB  . GLU A 1 116 ? 38.04952 14.83757 -13.07846 1.000 28.52557 ? 116 GLU A CB  1 
ATOM   807  C  CG  . GLU A 1 116 ? 37.32631 13.54669 -12.71248 1.000 33.05321 ? 116 GLU A CG  1 
ATOM   808  C  CD  . GLU A 1 116 ? 38.20654 12.31968 -12.86628 0.370 37.54968 ? 116 GLU A CD  1 
ATOM   809  O  OE1 . GLU A 1 116 ? 39.28201 12.42441 -13.49535 0.220 39.00095 ? 116 GLU A OE1 1 
ATOM   810  O  OE2 . GLU A 1 116 ? 37.81967 11.24946 -12.35605 0.740 39.39311 ? 116 GLU A OE2 1 
ATOM   811  N  N   . ALA A 1 117 ? 38.22426 17.52552 -14.93200 1.000 24.26238 ? 117 ALA A N   1 
ATOM   812  C  CA  . ALA A 1 117 ? 38.95647 18.73625 -15.28053 1.000 25.20338 ? 117 ALA A CA  1 
ATOM   813  C  C   . ALA A 1 117 ? 38.14443 19.99050 -15.00014 1.000 24.61425 ? 117 ALA A C   1 
ATOM   814  O  O   . ALA A 1 117 ? 38.72189 21.04740 -14.71189 1.000 25.67433 ? 117 ALA A O   1 
ATOM   815  C  CB  . ALA A 1 117 ? 39.35051 18.69357 -16.75772 1.000 26.84174 ? 117 ALA A CB  1 
ATOM   816  N  N   . ASN A 1 118 ? 36.81689 19.91171 -15.09538 1.000 23.48454 ? 118 ASN A N   1 
ATOM   817  C  CA  . ASN A 1 118 ? 35.94960 21.07379 -14.90760 1.000 22.99231 ? 118 ASN A CA  1 
ATOM   818  C  C   . ASN A 1 118 ? 35.28419 21.09681 -13.53765 1.000 20.42573 ? 118 ASN A C   1 
ATOM   819  O  O   . ASN A 1 118 ? 34.44036 21.96058 -13.27248 1.000 18.87162 ? 118 ASN A O   1 
ATOM   820  C  CB  . ASN A 1 118 ? 34.87884 21.12581 -15.99991 1.000 25.68460 ? 118 ASN A CB  1 
ATOM   821  C  CG  . ASN A 1 118 ? 35.46290 21.33037 -17.38743 1.000 28.37842 ? 118 ASN A CG  1 
ATOM   822  O  OD1 . ASN A 1 118 ? 36.48902 21.99063 -17.56555 1.000 29.17239 ? 118 ASN A OD1 1 
ATOM   823  N  ND2 . ASN A 1 118 ? 34.80013 20.76094 -18.38303 1.000 31.36763 ? 118 ASN A ND2 1 
ATOM   824  N  N   . ALA A 1 119 ? 35.64811 20.17508 -12.65571 1.000 18.12638 ? 119 ALA A N   1 
ATOM   825  C  CA  . ALA A 1 119 ? 34.94863 20.09384 -11.37606 1.000 16.92596 ? 119 ALA A CA  1 
ATOM   826  C  C   . ALA A 1 119 ? 35.14294 21.33999 -10.51669 1.000 17.55206 ? 119 ALA A C   1 
ATOM   827  O  O   . ALA A 1 119 ? 34.28612 21.65122 -9.68083  1.000 17.68682 ? 119 ALA A O   1 
ATOM   828  C  CB  . ALA A 1 119 ? 35.38474 18.84070 -10.60658 1.000 19.79403 ? 119 ALA A CB  1 
ATOM   829  N  N   . TRP A 1 120 ? 36.23050 22.08462 -10.71209 1.000 18.04636 ? 120 TRP A N   1 
ATOM   830  C  CA  . TRP A 1 120 ? 36.47012 23.25064 -9.86776  1.000 17.21800 ? 120 TRP A CA  1 
ATOM   831  C  C   . TRP A 1 120 ? 35.39238 24.31899 -10.03766 1.000 16.73391 ? 120 TRP A C   1 
ATOM   832  O  O   . TRP A 1 120 ? 35.21458 25.15930 -9.14823  1.000 17.84330 ? 120 TRP A O   1 
ATOM   833  C  CB  . TRP A 1 120 ? 37.86106 23.84015 -10.16566 1.000 18.91514 ? 120 TRP A CB  1 
ATOM   834  C  CG  . TRP A 1 120 ? 38.01296 24.46489 -11.53652 1.000 18.94183 ? 120 TRP A CG  1 
ATOM   835  C  CD1 . TRP A 1 120 ? 38.43897 23.83539 -12.69267 1.000 19.47374 ? 120 TRP A CD1 1 
ATOM   836  C  CD2 . TRP A 1 120 ? 37.73089 25.82406 -11.90529 1.000 18.66853 ? 120 TRP A CD2 1 
ATOM   837  N  NE1 . TRP A 1 120 ? 38.43677 24.72806 -13.73386 1.000 19.94150 ? 120 TRP A NE1 1 
ATOM   838  C  CE2 . TRP A 1 120 ? 38.02156 25.95310 -13.28342 1.000 20.46674 ? 120 TRP A CE2 1 
ATOM   839  C  CE3 . TRP A 1 120 ? 37.28091 26.95501 -11.19898 1.000 18.57525 ? 120 TRP A CE3 1 
ATOM   840  C  CZ2 . TRP A 1 120 ? 37.85575 27.16052 -13.97856 1.000 21.57919 ? 120 TRP A CZ2 1 
ATOM   841  C  CZ3 . TRP A 1 120 ? 37.13277 28.14949 -11.89347 1.000 20.26442 ? 120 TRP A CZ3 1 
ATOM   842  C  CH2 . TRP A 1 120 ? 37.40880 28.23737 -13.26623 1.000 21.55003 ? 120 TRP A CH2 1 
ATOM   843  N  N   . TYR A 1 121 ? 34.67841 24.32631 -11.16618 1.000 16.37114 ? 121 TYR A N   1 
ATOM   844  C  CA  . TYR A 1 121 ? 33.58027 25.26570 -11.38326 1.000 15.87062 ? 121 TYR A CA  1 
ATOM   845  C  C   . TYR A 1 121 ? 32.22939 24.56010 -11.48118 1.000 15.51085 ? 121 TYR A C   1 
ATOM   846  O  O   . TYR A 1 121 ? 31.28469 25.08076 -12.08522 1.000 17.78144 ? 121 TYR A O   1 
ATOM   847  C  CB  . TYR A 1 121 ? 33.84258 26.24721 -12.52781 1.000 19.75817 ? 121 TYR A CB  1 
ATOM   848  C  CG  . TYR A 1 121 ? 33.88715 25.72847 -13.93630 1.000 20.80621 ? 121 TYR A CG  1 
ATOM   849  C  CD1 . TYR A 1 121 ? 35.00019 25.04458 -14.43152 1.000 22.71748 ? 121 TYR A CD1 1 
ATOM   850  C  CD2 . TYR A 1 121 ? 32.84569 25.99978 -14.81729 1.000 23.45714 ? 121 TYR A CD2 1 
ATOM   851  C  CE1 . TYR A 1 121 ? 35.05395 24.62124 -15.74973 1.000 25.44641 ? 121 TYR A CE1 1 
ATOM   852  C  CE2 . TYR A 1 121 ? 32.89843 25.59284 -16.14993 1.000 26.98450 ? 121 TYR A CE2 1 
ATOM   853  C  CZ  . TYR A 1 121 ? 33.99556 24.88634 -16.61179 1.000 28.65681 ? 121 TYR A CZ  1 
ATOM   854  O  OH  . TYR A 1 121 ? 34.04505 24.46909 -17.93961 1.000 33.11199 ? 121 TYR A OH  1 
ATOM   855  N  N   . SER A 1 122 ? 32.10107 23.41984 -10.80911 1.000 14.87567 ? 122 SER A N   1 
ATOM   856  C  CA  . SER A 1 122 ? 30.85286 22.67151 -10.82712 1.000 15.41192 ? 122 SER A CA  1 
ATOM   857  C  C   . SER A 1 122 ? 29.71865 23.32255 -10.03857 1.000 14.64289 ? 122 SER A C   1 
ATOM   858  O  O   . SER A 1 122 ? 28.56399 22.94820 -10.27269 1.000 15.08389 ? 122 SER A O   1 
ATOM   859  C  CB  . SER A 1 122 ? 31.08107 21.27738 -10.22456 1.000 15.69442 ? 122 SER A CB  1 
ATOM   860  O  OG  . SER A 1 122 ? 31.38347 21.40618 -8.83352  1.000 17.44037 ? 122 SER A OG  1 
ATOM   861  N  N   . THR A 1 123 ? 29.99601 24.22789 -9.08721  1.000 13.51122 ? 123 THR A N   1 
ATOM   862  C  CA  . THR A 1 123 ? 29.01477 24.58863 -8.06351  1.000 14.22308 ? 123 THR A CA  1 
ATOM   863  C  C   . THR A 1 123 ? 28.75003 26.08217 -7.99623  1.000 13.78416 ? 123 THR A C   1 
ATOM   864  O  O   . THR A 1 123 ? 29.66940 26.86586 -7.73097  1.000 14.72477 ? 123 THR A O   1 
ATOM   865  C  CB  . THR A 1 123 ? 29.45676 24.11338 -6.68157  1.000 13.72930 ? 123 THR A CB  1 
ATOM   866  O  OG1 . THR A 1 123 ? 29.85012 22.73564 -6.78141  1.000 14.87177 ? 123 THR A OG1 1 
ATOM   867  C  CG2 . THR A 1 123 ? 28.27084 24.20795 -5.71466  1.000 15.64251 ? 123 THR A CG2 1 
ATOM   868  N  N   . LEU A 1 124 ? 27.49751 26.46828 -8.21469  1.000 13.83750 ? 124 LEU A N   1 
ATOM   869  C  CA  . LEU A 1 124 ? 27.01621 27.82407 -8.00850  1.000 13.65493 ? 124 LEU A CA  1 
ATOM   870  C  C   . LEU A 1 124 ? 26.40225 27.94722 -6.61309  1.000 14.19913 ? 124 LEU A C   1 
ATOM   871  O  O   . LEU A 1 124 ? 25.83611 26.99089 -6.06275  1.000 13.90094 ? 124 LEU A O   1 
ATOM   872  C  CB  . LEU A 1 124 ? 25.94000 28.13505 -9.03750  1.000 15.33315 ? 124 LEU A CB  1 
ATOM   873  C  CG  . LEU A 1 124 ? 26.45402 28.22017 -10.47806 1.000 16.71326 ? 124 LEU A CG  1 
ATOM   874  C  CD1 . LEU A 1 124 ? 25.29928 28.07229 -11.46055 1.000 17.84540 ? 124 LEU A CD1 1 
ATOM   875  C  CD2 . LEU A 1 124 ? 27.17618 29.56863 -10.68072 1.000 18.26117 ? 124 LEU A CD2 1 
ATOM   876  N  N   . VAL A 1 125 ? 26.50243 29.14158 -6.03821  1.000 13.85463 ? 125 VAL A N   1 
ATOM   877  C  CA  . VAL A 1 125 ? 25.89426 29.43247 -4.73417  1.000 13.77704 ? 125 VAL A CA  1 
ATOM   878  C  C   . VAL A 1 125 ? 25.05062 30.70201 -4.83316  1.000 13.04632 ? 125 VAL A C   1 
ATOM   879  O  O   . VAL A 1 125 ? 25.41832 31.65059 -5.53372  1.000 14.43297 ? 125 VAL A O   1 
ATOM   880  C  CB  . VAL A 1 125 ? 26.98333 29.56974 -3.63711  1.000 13.93400 ? 125 VAL A CB  1 
ATOM   881  C  CG1 . VAL A 1 125 ? 27.94027 30.73538 -3.92418  1.000 14.49941 ? 125 VAL A CG1 1 
ATOM   882  C  CG2 . VAL A 1 125 ? 26.32164 29.72892 -2.24371  1.000 16.55570 ? 125 VAL A CG2 1 
ATOM   883  N  N   . GLY A 1 126 ? 23.92075 30.71098 -4.13439  1.000 12.96815 ? 126 GLY A N   1 
ATOM   884  C  CA  . GLY A 1 126 ? 23.09433 31.89062 -4.07931  1.000 13.42100 ? 126 GLY A CA  1 
ATOM   885  C  C   . GLY A 1 126 ? 22.14380 31.83299 -2.90872  1.000 12.64051 ? 126 GLY A C   1 
ATOM   886  O  O   . GLY A 1 126 ? 22.28893 31.01112 -1.99689  1.000 13.46671 ? 126 GLY A O   1 
ATOM   887  N  N   . HIS A 1 127 ? 21.15865 32.72496 -2.92795  1.000 13.22105 ? 127 HIS A N   1 
ATOM   888  C  CA  . HIS A 1 127 ? 20.23044 32.84187 -1.81271  1.000 13.74875 ? 127 HIS A CA  1 
ATOM   889  C  C   . HIS A 1 127 ? 18.87123 33.21943 -2.37476  1.000 14.61719 ? 127 HIS A C   1 
ATOM   890  O  O   . HIS A 1 127 ? 18.77480 34.15271 -3.17710  1.000 15.98488 ? 127 HIS A O   1 
ATOM   891  C  CB  . HIS A 1 127 ? 20.69816 33.91145 -0.80366  1.000 14.92204 ? 127 HIS A CB  1 
ATOM   892  C  CG  . HIS A 1 127 ? 21.21417 35.16307 -1.44393  1.000 15.85102 ? 127 HIS A CG  1 
ATOM   893  N  ND1 . HIS A 1 127 ? 20.46793 36.31038 -1.57368  1.000 18.70319 ? 127 HIS A ND1 1 
ATOM   894  C  CD2 . HIS A 1 127 ? 22.42172 35.44057 -1.98944  1.000 15.89951 ? 127 HIS A CD2 1 
ATOM   895  C  CE1 . HIS A 1 127 ? 21.18481 37.23596 -2.18952  1.000 19.61588 ? 127 HIS A CE1 1 
ATOM   896  N  NE2 . HIS A 1 127 ? 22.37495 36.73332 -2.45966  1.000 20.14415 ? 127 HIS A NE2 1 
ATOM   897  N  N   . ASP A 1 128 ? 17.82675 32.50760 -1.94205  1.000 14.49998 ? 128 ASP A N   1 
ATOM   898  C  CA  . ASP A 1 128 ? 16.44844 32.76302 -2.33193  1.000 14.20927 ? 128 ASP A CA  1 
ATOM   899  C  C   . ASP A 1 128 ? 15.59811 32.99154 -1.08444  1.000 14.85733 ? 128 ASP A C   1 
ATOM   900  O  O   . ASP A 1 128 ? 15.73307 32.29517 -0.07395  1.000 16.54087 ? 128 ASP A O   1 
ATOM   901  C  CB  . ASP A 1 128 ? 15.85862 31.52046 -3.01223  1.000 15.10064 ? 128 ASP A CB  1 
ATOM   902  C  CG  . ASP A 1 128 ? 16.39990 31.26612 -4.40153  1.000 14.25470 ? 128 ASP A CG  1 
ATOM   903  O  OD1 . ASP A 1 128 ? 17.13988 32.11027 -4.97002  1.000 15.70471 ? 128 ASP A OD1 1 
ATOM   904  O  OD2 . ASP A 1 128 ? 16.05504 30.19634 -4.94804  1.000 15.22703 ? 128 ASP A OD2 1 
ATOM   905  N  N   . THR A 1 129 ? 14.71116 33.96149 -1.14778  1.000 16.16689 ? 129 THR A N   1 
ATOM   906  C  CA  A THR A 1 129 ? 13.72440 34.18755 -0.10548  0.620 17.23822 ? 129 THR A CA  1 
ATOM   907  C  CA  B THR A 1 129 ? 13.72871 34.17796 -0.10121  0.380 17.36439 ? 129 THR A CA  1 
ATOM   908  C  C   . THR A 1 129 ? 12.35311 33.85952 -0.66688  1.000 17.61219 ? 129 THR A C   1 
ATOM   909  O  O   . THR A 1 129 ? 11.98385 34.35585 -1.73520  1.000 18.11719 ? 129 THR A O   1 
ATOM   910  C  CB  A THR A 1 129 ? 13.75523 35.63251 0.39564   0.620 20.26929 ? 129 THR A CB  1 
ATOM   911  C  CB  B THR A 1 129 ? 13.79323 35.61245 0.42566   0.380 19.36064 ? 129 THR A CB  1 
ATOM   912  O  OG1 A THR A 1 129 ? 15.04350 35.91415 0.94991   0.620 22.67005 ? 129 THR A OG1 1 
ATOM   913  O  OG1 B THR A 1 129 ? 12.87019 35.77147 1.51328   0.380 22.00562 ? 129 THR A OG1 1 
ATOM   914  C  CG2 A THR A 1 129 ? 12.69626 35.83800 1.47723   0.620 22.67457 ? 129 THR A CG2 1 
ATOM   915  C  CG2 B THR A 1 129 ? 13.45247 36.58289 -0.67556  0.380 19.37790 ? 129 THR A CG2 1 
ATOM   916  N  N   . PHE A 1 130 ? 11.62131 32.99247 0.02792   1.000 16.52704 ? 130 PHE A N   1 
ATOM   917  C  CA  . PHE A 1 130 ? 10.29173 32.55994 -0.38690  1.000 16.53424 ? 130 PHE A CA  1 
ATOM   918  C  C   . PHE A 1 130 ? 9.24114  33.20043 0.51481   1.000 18.15623 ? 130 PHE A C   1 
ATOM   919  O  O   . PHE A 1 130 ? 9.41563  33.29223 1.74234   1.000 18.69402 ? 130 PHE A O   1 
ATOM   920  C  CB  . PHE A 1 130 ? 10.16672 31.04071 -0.28509  1.000 16.86292 ? 130 PHE A CB  1 
ATOM   921  C  CG  . PHE A 1 130 ? 11.08737 30.29765 -1.21645  1.000 14.99655 ? 130 PHE A CG  1 
ATOM   922  C  CD1 . PHE A 1 130 ? 12.37800 30.03551 -0.85575  1.000 16.10373 ? 130 PHE A CD1 1 
ATOM   923  C  CD2 . PHE A 1 130 ? 10.64355 29.86513 -2.47084  1.000 16.54805 ? 130 PHE A CD2 1 
ATOM   924  C  CE1 . PHE A 1 130 ? 13.23564 29.36259 -1.71940  1.000 15.60531 ? 130 PHE A CE1 1 
ATOM   925  C  CE2 . PHE A 1 130 ? 11.48944 29.17245 -3.32666  1.000 16.31538 ? 130 PHE A CE2 1 
ATOM   926  C  CZ  . PHE A 1 130 ? 12.80481 28.90968 -2.93409  1.000 15.47632 ? 130 PHE A CZ  1 
ATOM   927  N  N   . THR A 1 131 ? 8.14272  33.61814 -0.10785  1.000 17.90311 ? 131 THR A N   1 
ATOM   928  C  CA  . THR A 1 131 ? 7.00356  34.21256 0.57251   1.000 19.48075 ? 131 THR A CA  1 
ATOM   929  C  C   . THR A 1 131 ? 5.73722  33.53184 0.08225   1.000 20.81741 ? 131 THR A C   1 
ATOM   930  O  O   . THR A 1 131 ? 5.73480  32.84499 -0.94402  1.000 20.29259 ? 131 THR A O   1 
ATOM   931  C  CB  . THR A 1 131 ? 6.93217  35.73267 0.35876   1.000 22.84816 ? 131 THR A CB  1 
ATOM   932  O  OG1 . THR A 1 131 ? 6.83100  36.01505 -1.04651  1.000 27.56007 ? 131 THR A OG1 1 
ATOM   933  C  CG2 . THR A 1 131 ? 8.15554  36.41157 0.95493   1.000 23.89661 ? 131 THR A CG2 1 
ATOM   934  N  N   . LYS A 1 132 ? 4.65245  33.72532 0.83482   1.000 23.62844 ? 132 LYS A N   1 
ATOM   935  C  CA  . LYS A 1 132 ? 3.36350  33.14654 0.47814   1.000 25.41874 ? 132 LYS A CA  1 
ATOM   936  C  C   . LYS A 1 132 ? 2.65663  33.94886 -0.60996  1.000 27.67187 ? 132 LYS A C   1 
ATOM   937  O  O   . LYS A 1 132 ? 1.64612  33.48529 -1.15061  1.000 27.44348 ? 132 LYS A O   1 
ATOM   938  C  CB  . LYS A 1 132 ? 2.47159  33.08295 1.72632   1.000 27.77700 ? 132 LYS A CB  1 
ATOM   939  C  CG  . LYS A 1 132 ? 2.88596  32.04967 2.73952   1.000 30.58506 ? 132 LYS A CG  1 
ATOM   940  C  CD  . LYS A 1 132 ? 2.87267  30.65679 2.18530   1.000 33.02968 ? 132 LYS A CD  1 
ATOM   941  C  CE  . LYS A 1 132 ? 1.51262  30.32491 1.59676   1.000 35.88773 ? 132 LYS A CE  1 
ATOM   942  N  NZ  . LYS A 1 132 ? 1.39865  28.86101 1.29619   1.000 35.89731 ? 132 LYS A NZ  1 
ATOM   943  N  N   . VAL A 1 133 ? 3.14780  35.14276 -0.93191  1.000 31.51037 ? 133 VAL A N   1 
ATOM   944  C  CA  . VAL A 1 133 ? 2.52478  36.01865 -1.91936  1.000 36.97001 ? 133 VAL A CA  1 
ATOM   945  C  C   . VAL A 1 133 ? 3.51330  36.27127 -3.04815  1.000 39.50714 ? 133 VAL A C   1 
ATOM   946  O  O   . VAL A 1 133 ? 4.73094  36.24333 -2.84542  1.000 40.75427 ? 133 VAL A O   1 
ATOM   947  C  CB  . VAL A 1 133 ? 2.06504  37.36195 -1.30938  1.000 41.63271 ? 133 VAL A CB  1 
ATOM   948  C  CG1 . VAL A 1 133 ? 1.01024  38.01503 -2.20098  1.000 43.81756 ? 133 VAL A CG1 1 
ATOM   949  C  CG2 . VAL A 1 133 ? 1.56138  37.16919 0.11634   1.000 43.30131 ? 133 VAL A CG2 1 
ATOM   950  N  N   . LYS A 1 134 ? 2.97430  36.52850 -4.23895  1.000 45.32215 ? 134 LYS A N   1 
ATOM   951  C  CA  . LYS A 1 134 ? 3.74801  36.94637 -5.41666  1.000 49.70983 ? 134 LYS A CA  1 
ATOM   952  C  C   . LYS A 1 134 ? 4.18561  35.74946 -6.24843  1.000 50.06433 ? 134 LYS A C   1 
ATOM   953  O  O   . LYS A 1 134 ? 3.51758  35.37761 -7.21461  1.000 50.08058 ? 134 LYS A O   1 
ATOM   954  C  CB  . LYS A 1 134 ? 4.95567  37.80675 -5.02049  1.000 52.08649 ? 134 LYS A CB  1 
ATOM   955  C  CG  . LYS A 1 134 ? 6.01927  37.95642 -6.09585  1.000 53.47697 ? 134 LYS A CG  1 
ATOM   956  C  CD  . LYS A 1 134 ? 5.41458  38.32919 -7.44026  1.000 55.54045 ? 134 LYS A CD  1 
ATOM   957  C  CE  . LYS A 1 134 ? 5.54355  39.81894 -7.71757  1.000 56.92028 ? 134 LYS A CE  1 
ATOM   958  N  NZ  . LYS A 1 134 ? 5.57839  40.10960 -9.18130  1.000 57.89594 ? 134 LYS A NZ  1 
HETATM 959  C  C10 . QG7 B 2 .   ? 17.54853 29.16580 -9.71646  1.000 15.43878 ? 201 QG7 A C10 1 
HETATM 960  C  C15 . QG7 B 2 .   ? 21.16219 29.21502 -18.23207 1.000 36.73840 ? 201 QG7 A C15 1 
HETATM 961  C  C17 . QG7 B 2 .   ? 25.17351 25.93031 -14.71701 1.000 30.08271 ? 201 QG7 A C17 1 
HETATM 962  C  C11 . QG7 B 2 .   ? 24.07188 27.84149 -15.45566 1.000 32.79483 ? 201 QG7 A C11 1 
HETATM 963  C  C12 . QG7 B 2 .   ? 23.02922 28.37808 -16.42340 1.000 34.01710 ? 201 QG7 A C12 1 
HETATM 964  C  C14 . QG7 B 2 .   ? 21.44630 29.99426 -17.08748 1.000 37.06869 ? 201 QG7 A C14 1 
HETATM 965  O  O2  . QG7 B 2 .   ? 14.34879 29.45987 -8.28755  1.000 15.15285 ? 201 QG7 A O2  1 
HETATM 966  C  C9  . QG7 B 2 .   ? 15.59691 29.40782 -8.53155  1.000 16.95195 ? 201 QG7 A C9  1 
HETATM 967  N  N1  . QG7 B 2 .   ? 16.55232 29.59374 -7.63494  1.000 15.88982 ? 201 QG7 A N1  1 
HETATM 968  N  N2  . QG7 B 2 .   ? 16.09446 29.14939 -9.73326  1.000 16.91826 ? 201 QG7 A N2  1 
HETATM 969  C  C8  . QG7 B 2 .   ? 17.89140 29.43788 -8.22683  1.000 14.32727 ? 201 QG7 A C8  1 
HETATM 970  C  C7  . QG7 B 2 .   ? 18.57216 28.19160 -7.66859  1.000 14.88863 ? 201 QG7 A C7  1 
HETATM 971  S  S1  . QG7 B 2 .   ? 18.02948 26.77481 -8.63453  1.000 15.38621 ? 201 QG7 A S1  1 
HETATM 972  C  C6  . QG7 B 2 .   ? 18.17430 27.81219 -10.10688 1.000 15.42614 ? 201 QG7 A C6  1 
HETATM 973  C  C5  . QG7 B 2 .   ? 17.59553 27.18064 -11.41475 1.000 16.21526 ? 201 QG7 A C5  1 
HETATM 974  C  C4  . QG7 B 2 .   ? 18.42898 26.04437 -12.01851 1.000 16.83711 ? 201 QG7 A C4  1 
HETATM 975  C  C3  . QG7 B 2 .   ? 17.77011 25.32218 -13.16910 1.000 17.62534 ? 201 QG7 A C3  1 
HETATM 976  C  C2  . QG7 B 2 .   ? 18.64711 24.25750 -13.78262 1.000 19.17747 ? 201 QG7 A C2  1 
HETATM 977  C  C1  . QG7 B 2 .   ? 19.85996 24.82594 -14.44457 1.000 20.79634 ? 201 QG7 A C1  1 
HETATM 978  C  C24 . QG7 B 2 .   ? 22.29676 24.56344 -14.94159 1.000 25.51969 ? 201 QG7 A C24 1 
HETATM 979  O  O1  . QG7 B 2 .   ? 19.85235 25.88526 -15.10016 1.000 19.73426 ? 201 QG7 A O1  1 
HETATM 980  N  N6  . QG7 B 2 .   ? 21.06386 24.10202 -14.27799 1.000 22.96004 ? 201 QG7 A N6  1 
HETATM 981  C  C23 . QG7 B 2 .   ? 22.80008 25.94749 -14.43469 1.000 28.30997 ? 201 QG7 A C23 1 
HETATM 982  N  N3  . QG7 B 2 .   ? 23.89577 26.38564 -15.30589 1.000 30.30411 ? 201 QG7 A N3  1 
HETATM 983  N  N4  . QG7 B 2 .   ? 22.71226 27.67448 -17.52460 1.000 32.98245 ? 201 QG7 A N4  1 
HETATM 984  C  C16 . QG7 B 2 .   ? 21.84110 28.00455 -18.45161 1.000 35.50678 ? 201 QG7 A C16 1 
HETATM 985  C  C13 . QG7 B 2 .   ? 22.39390 29.59781 -16.13959 1.000 35.10380 ? 201 QG7 A C13 1 
HETATM 986  N  N5  . QG7 B 2 .   ? 25.17626 24.78897 -16.84593 1.000 28.16131 ? 201 QG7 A N5  1 
HETATM 987  C  C18 . QG7 B 2 .   ? 25.82460 24.96440 -15.70616 1.000 28.95410 ? 201 QG7 A C18 1 
HETATM 988  C  C22 . QG7 B 2 .   ? 25.70633 23.97902 -17.75735 1.000 31.43914 ? 201 QG7 A C22 1 
HETATM 989  C  C21 . QG7 B 2 .   ? 26.90656 23.28633 -17.49529 1.000 30.64941 ? 201 QG7 A C21 1 
HETATM 990  C  C20 . QG7 B 2 .   ? 27.60975 23.42720 -16.28803 1.000 29.99915 ? 201 QG7 A C20 1 
HETATM 991  C  C19 . QG7 B 2 .   ? 27.02197 24.31258 -15.36432 1.000 28.96156 ? 201 QG7 A C19 1 
HETATM 992  H  H1  . QG7 B 2 .   ? 17.93032 29.89684 -10.42761 1.000 18.52714 ? 201 QG7 A H1  1 
HETATM 993  H  H2  . QG7 B 2 .   ? 20.41332 29.55407 -18.94785 1.000 44.08668 ? 201 QG7 A H2  1 
HETATM 994  H  H3  . QG7 B 2 .   ? 25.82883 26.78666 -14.55786 1.000 36.09985 ? 201 QG7 A H3  1 
HETATM 995  H  H4  . QG7 B 2 .   ? 24.97974 25.41432 -13.77664 1.000 36.09985 ? 201 QG7 A H4  1 
HETATM 996  H  H5  . QG7 B 2 .   ? 25.06735 28.04236 -15.85438 1.000 39.35440 ? 201 QG7 A H5  1 
HETATM 997  H  H6  . QG7 B 2 .   ? 23.93847 28.31986 -14.48424 1.000 39.35440 ? 201 QG7 A H6  1 
HETATM 998  H  H7  . QG7 B 2 .   ? 20.91066 30.93198 -16.93962 1.000 44.48303 ? 201 QG7 A H7  1 
HETATM 999  H  H8  . QG7 B 2 .   ? 16.38349 29.81529 -6.66411  1.000 19.06838 ? 201 QG7 A H8  1 
HETATM 1000 H  H9  . QG7 B 2 .   ? 15.53543 28.96503 -10.55398 1.000 20.30251 ? 201 QG7 A H9  1 
HETATM 1001 H  H10 . QG7 B 2 .   ? 18.54805 30.28815 -8.04257  1.000 17.19332 ? 201 QG7 A H10 1 
HETATM 1002 H  H11 . QG7 B 2 .   ? 19.65486 28.29677 -7.73784  1.000 17.86696 ? 201 QG7 A H11 1 
HETATM 1003 H  H12 . QG7 B 2 .   ? 18.29865 28.05566 -6.62225  1.000 17.86696 ? 201 QG7 A H12 1 
HETATM 1004 H  H13 . QG7 B 2 .   ? 19.21989 27.93486 -10.38933 1.000 18.51197 ? 201 QG7 A H13 1 
HETATM 1005 H  H14 . QG7 B 2 .   ? 16.61981 26.76404 -11.16473 1.000 19.45892 ? 201 QG7 A H14 1 
HETATM 1006 H  H15 . QG7 B 2 .   ? 17.54877 27.97442 -12.16029 1.000 19.45892 ? 201 QG7 A H15 1 
HETATM 1007 H  H16 . QG7 B 2 .   ? 18.59030 25.31021 -11.22915 1.000 20.20513 ? 201 QG7 A H16 1 
HETATM 1008 H  H17 . QG7 B 2 .   ? 19.34724 26.48882 -12.40238 1.000 20.20513 ? 201 QG7 A H17 1 
HETATM 1009 H  H18 . QG7 B 2 .   ? 17.54382 26.05724 -13.94149 1.000 21.15101 ? 201 QG7 A H18 1 
HETATM 1010 H  H19 . QG7 B 2 .   ? 16.86959 24.83860 -12.79050 1.000 21.15101 ? 201 QG7 A H19 1 
HETATM 1011 H  H20 . QG7 B 2 .   ? 18.96196 23.56509 -13.00190 1.000 23.01357 ? 201 QG7 A H20 1 
HETATM 1012 H  H21 . QG7 B 2 .   ? 18.06755 23.70397 -14.52142 1.000 23.01357 ? 201 QG7 A H21 1 
HETATM 1013 H  H22 . QG7 B 2 .   ? 22.10357 24.63798 -16.01174 1.000 30.62423 ? 201 QG7 A H22 1 
HETATM 1014 H  H23 . QG7 B 2 .   ? 23.07936 23.82595 -14.76345 1.000 30.62423 ? 201 QG7 A H23 1 
HETATM 1015 H  H24 . QG7 B 2 .   ? 21.07820 23.27031 -13.70514 1.000 27.55265 ? 201 QG7 A H24 1 
HETATM 1016 H  H25 . QG7 B 2 .   ? 21.98646 26.66959 -14.48489 1.000 33.97256 ? 201 QG7 A H25 1 
HETATM 1017 H  H26 . QG7 B 2 .   ? 23.16641 25.84828 -13.41396 1.000 33.97256 ? 201 QG7 A H26 1 
HETATM 1018 H  H28 . QG7 B 2 .   ? 21.65842 27.38325 -19.32838 1.000 42.60874 ? 201 QG7 A H28 1 
HETATM 1019 H  H29 . QG7 B 2 .   ? 22.62125 30.18793 -15.25180 1.000 42.12516 ? 201 QG7 A H29 1 
HETATM 1020 H  H30 . QG7 B 2 .   ? 25.20796 23.84921 -18.71688 1.000 37.72758 ? 201 QG7 A H30 1 
HETATM 1021 H  H31 . QG7 B 2 .   ? 27.30291 22.61666 -18.25855 1.000 36.77990 ? 201 QG7 A H31 1 
HETATM 1022 H  H32 . QG7 B 2 .   ? 28.53746 22.89327 -16.08219 1.000 35.99958 ? 201 QG7 A H32 1 
HETATM 1023 H  H33 . QG7 B 2 .   ? 27.49010 24.49006 -14.39610 1.000 34.75448 ? 201 QG7 A H33 1 
HETATM 1024 CU CU  . CU  C 3 .   ? 22.05951 15.40213 -22.01563 0.710 75.98209 ? 202 CU  A CU  1 
HETATM 1025 C  C   . ACY D 4 .   ? 22.93283 24.82957 -19.63467 1.000 25.51373 ? 203 ACY A C   1 
HETATM 1026 O  O   . ACY D 4 .   ? 22.38632 24.10866 -18.75028 1.000 30.18286 ? 203 ACY A O   1 
HETATM 1027 O  OXT . ACY D 4 .   ? 23.73635 25.78789 -19.49526 1.000 29.60395 ? 203 ACY A OXT 1 
HETATM 1028 C  CH3 . ACY D 4 .   ? 22.57091 24.51132 -21.12803 1.000 26.70496 ? 203 ACY A CH3 1 
HETATM 1029 CU CU  . CU  E 3 .   ? 23.89376 26.10909 -17.43348 1.000 37.52286 ? 204 CU  A CU  1 
HETATM 1030 O  O   . HOH F 5 .   ? 3.97205  19.32916 -16.25427 1.000 54.52748 ? 301 HOH A O   1 
HETATM 1031 O  O   . HOH F 5 .   ? 0.79860  30.83428 -0.97501  1.000 27.10765 ? 302 HOH A O   1 
HETATM 1032 O  O   . HOH F 5 .   ? -0.32374 33.91028 -2.77172  1.000 24.13665 ? 303 HOH A O   1 
HETATM 1033 O  O   . HOH F 5 .   ? 0.65438  35.57968 -4.96938  1.000 45.84951 ? 304 HOH A O   1 
HETATM 1034 O  O   . HOH F 5 .   ? 15.92761 20.83306 -16.70516 1.000 18.03266 ? 305 HOH A O   1 
HETATM 1035 O  O   . HOH F 5 .   ? 4.49003  35.42012 3.19132   1.000 26.18255 ? 306 HOH A O   1 
HETATM 1036 O  O   . HOH F 5 .   ? 3.10575  29.58828 -10.06812 1.000 35.03904 ? 307 HOH A O   1 
HETATM 1037 O  O   . HOH F 5 .   ? 7.94862  26.58907 -16.60626 1.000 39.73963 ? 308 HOH A O   1 
HETATM 1038 O  O   . HOH F 5 .   ? 9.73485  13.08414 0.48802   1.000 34.46653 ? 309 HOH A O   1 
HETATM 1039 O  O   . HOH F 5 .   ? 10.84610 13.41462 2.01504   1.000 30.66712 ? 310 HOH A O   1 
HETATM 1040 O  O   . HOH F 5 .   ? 1.99477  27.76311 4.06588   1.000 38.16493 ? 311 HOH A O   1 
HETATM 1041 O  O   . HOH F 5 .   ? 12.41471 16.44648 11.90417  1.000 21.17387 ? 312 HOH A O   1 
HETATM 1042 O  O   . HOH F 5 .   ? 11.201   18.708   -24.261   1.000 22.50447 ? 313 HOH A O   1 
HETATM 1043 O  O   . HOH F 5 .   ? 16.68985 16.68985 0.00000   0.50  15.14439 ? 314 HOH A O   1 
HETATM 1044 O  O   . HOH F 5 .   ? 25.071   32.870   -7.898    1.000 21.99409 ? 315 HOH A O   1 
HETATM 1045 O  O   . HOH F 5 .   ? 5.11620  12.15392 5.80870   1.000 39.84108 ? 316 HOH A O   1 
HETATM 1046 O  O   . HOH F 5 .   ? 14.232   16.113   -8.842    1.000 17.04752 ? 317 HOH A O   1 
HETATM 1047 O  O   . HOH F 5 .   ? 10.99389 24.95193 -14.16870 1.000 18.78478 ? 318 HOH A O   1 
HETATM 1048 O  O   . HOH F 5 .   ? 3.13580  18.94340 -2.06622  1.000 35.78200 ? 319 HOH A O   1 
HETATM 1049 O  O   . HOH F 5 .   ? 28.75876 20.23025 -16.88443 1.000 38.76206 ? 320 HOH A O   1 
HETATM 1050 O  O   . HOH F 5 .   ? 0.56368  30.10439 -8.23329  1.000 42.36786 ? 321 HOH A O   1 
HETATM 1051 O  O   . HOH F 5 .   ? 8.04557  22.45956 12.53571  1.000 27.56653 ? 322 HOH A O   1 
HETATM 1052 O  O   . HOH F 5 .   ? 4.57775  25.04080 -10.28805 1.000 25.09763 ? 323 HOH A O   1 
HETATM 1053 O  O   . HOH F 5 .   ? 7.08642  29.74831 -11.27381 1.000 24.30987 ? 324 HOH A O   1 
HETATM 1054 O  O   . HOH F 5 .   ? 21.61678 19.42525 -20.65675 1.000 37.42331 ? 325 HOH A O   1 
HETATM 1055 O  O   . HOH F 5 .   ? 5.78543  15.32784 2.80137   1.000 24.79075 ? 326 HOH A O   1 
HETATM 1056 O  O   . HOH F 5 .   ? 36.77732 18.45676 -19.59011 1.000 38.50652 ? 327 HOH A O   1 
HETATM 1057 O  O   . HOH F 5 .   ? 9.86848  28.38910 14.09758  1.000 30.98383 ? 328 HOH A O   1 
HETATM 1058 O  O   . HOH F 5 .   ? 32.182   18.950   -7.879    1.000 20.86048 ? 329 HOH A O   1 
HETATM 1059 O  O   . HOH F 5 .   ? 12.50891 28.39246 -16.58201 1.000 35.39776 ? 330 HOH A O   1 
HETATM 1060 O  O   . HOH F 5 .   ? 4.07621  27.94618 12.09988  1.000 44.27571 ? 331 HOH A O   1 
HETATM 1061 O  O   . HOH F 5 .   ? 2.61412  20.34088 -7.85758  1.000 30.60938 ? 332 HOH A O   1 
HETATM 1062 O  O   . HOH F 5 .   ? 14.22089 25.89393 16.06937  1.000 20.31540 ? 333 HOH A O   1 
HETATM 1063 O  O   . HOH F 5 .   ? 14.82323 24.27455 13.76012  1.000 18.80722 ? 334 HOH A O   1 
HETATM 1064 O  O   . HOH F 5 .   ? 29.300   20.853   -4.825    1.000 15.76289 ? 335 HOH A O   1 
HETATM 1065 O  O   . HOH F 5 .   ? 10.28207 36.44131 -2.39489  1.000 36.06626 ? 336 HOH A O   1 
HETATM 1066 O  O   . HOH F 5 .   ? 6.33623  15.44675 -6.21440  1.000 29.30834 ? 337 HOH A O   1 
HETATM 1067 O  O   . HOH F 5 .   ? 19.70980 16.57566 -13.67983 1.000 17.80095 ? 338 HOH A O   1 
HETATM 1068 O  O   . HOH F 5 .   ? 10.27852 29.43666 17.83605  1.000 33.42061 ? 339 HOH A O   1 
HETATM 1069 O  O   . HOH F 5 .   ? -0.640   38.534   6.203     1.000 34.78466 ? 340 HOH A O   1 
HETATM 1070 O  O   . HOH F 5 .   ? 11.17660 27.36793 -19.46621 1.000 42.88192 ? 341 HOH A O   1 
HETATM 1071 O  O   . HOH F 5 .   ? 6.06240  23.65362 -8.42183  1.000 22.27986 ? 342 HOH A O   1 
HETATM 1072 O  O   . HOH F 5 .   ? 32.00623 22.86929 -14.37941 1.000 25.74563 ? 343 HOH A O   1 
HETATM 1073 O  O   . HOH F 5 .   ? 6.92340  18.25222 -15.21019 1.000 26.72535 ? 344 HOH A O   1 
HETATM 1074 O  O   . HOH F 5 .   ? 2.12499  13.46460 7.66284   1.000 36.42580 ? 345 HOH A O   1 
HETATM 1075 O  O   . HOH F 5 .   ? 8.08792  22.55841 18.72568  1.000 50.62586 ? 346 HOH A O   1 
HETATM 1076 O  O   . HOH F 5 .   ? 28.60259 25.84511 -12.54183 1.000 32.10411 ? 347 HOH A O   1 
HETATM 1077 O  O   . HOH F 5 .   ? 18.940   33.300   -6.798    1.000 18.40031 ? 348 HOH A O   1 
HETATM 1078 O  O   . HOH F 5 .   ? 17.80878 34.14014 1.73129   1.000 24.23947 ? 349 HOH A O   1 
HETATM 1079 O  O   . HOH F 5 .   ? 26.50998 24.54361 -11.41808 1.000 25.04902 ? 350 HOH A O   1 
HETATM 1080 O  O   . HOH F 5 .   ? 11.34443 15.65924 -11.79984 1.000 19.39276 ? 351 HOH A O   1 
HETATM 1081 O  O   . HOH F 5 .   ? 38.78779 20.62738 -11.65516 1.000 25.74906 ? 352 HOH A O   1 
HETATM 1082 O  O   . HOH F 5 .   ? 7.96908  15.96960 -16.08189 1.000 32.43944 ? 353 HOH A O   1 
HETATM 1083 O  O   . HOH F 5 .   ? 14.77257 14.38243 -19.60372 1.000 35.69625 ? 354 HOH A O   1 
HETATM 1084 O  O   . HOH F 5 .   ? 8.91303  30.62859 13.07321  1.000 43.77288 ? 355 HOH A O   1 
HETATM 1085 O  O   . HOH F 5 .   ? 9.13533  13.77343 -3.71922  1.000 47.45111 ? 356 HOH A O   1 
HETATM 1086 O  O   . HOH F 5 .   ? 18.98136 31.13767 5.33925   1.000 19.74631 ? 357 HOH A O   1 
HETATM 1087 O  O   . HOH F 5 .   ? 1.40029  21.69418 -1.20802  1.000 33.15470 ? 358 HOH A O   1 
HETATM 1088 O  O   . HOH F 5 .   ? 14.326   14.542   11.201    1.000 21.86795 ? 359 HOH A O   1 
HETATM 1089 O  O   . HOH F 5 .   ? 38.83902 23.63255 -16.39590 1.000 30.15304 ? 360 HOH A O   1 
HETATM 1090 O  O   . HOH F 5 .   ? 26.75956 16.52557 -17.27448 1.000 23.78232 ? 361 HOH A O   1 
HETATM 1091 O  O   . HOH F 5 .   ? 32.37584 19.31565 -17.64052 1.000 25.42375 ? 362 HOH A O   1 
HETATM 1092 O  O   . HOH F 5 .   ? 10.46883 10.19902 8.06960   1.000 36.62042 ? 363 HOH A O   1 
HETATM 1093 O  O   . HOH F 5 .   ? 11.64151 12.01376 4.39627   1.000 29.17468 ? 364 HOH A O   1 
HETATM 1094 O  O   . HOH F 5 .   ? 21.22054 34.34400 -5.38371  1.000 18.83199 ? 365 HOH A O   1 
HETATM 1095 O  O   . HOH F 5 .   ? 18.220   35.991   -7.179    1.000 22.98456 ? 366 HOH A O   1 
HETATM 1096 O  O   . HOH F 5 .   ? 34.099   22.321   -6.807    1.000 23.86310 ? 367 HOH A O   1 
HETATM 1097 O  O   . HOH F 5 .   ? 12.31534 36.65878 7.60344   1.000 40.50186 ? 368 HOH A O   1 
HETATM 1098 O  O   . HOH F 5 .   ? 36.52664 13.13876 -16.04117 1.000 39.40207 ? 369 HOH A O   1 
HETATM 1099 O  O   . HOH F 5 .   ? 14.073   11.243   -12.617   1.000 29.13016 ? 370 HOH A O   1 
HETATM 1100 O  O   . HOH F 5 .   ? 17.82660 36.08293 -0.17154  1.000 25.83966 ? 371 HOH A O   1 
HETATM 1101 O  O   . HOH F 5 .   ? 9.52710  20.84119 -24.15773 1.000 36.15187 ? 372 HOH A O   1 
HETATM 1102 O  O   . HOH F 5 .   ? 24.350   37.291   -4.661    1.000 25.69897 ? 373 HOH A O   1 
HETATM 1103 O  O   . HOH F 5 .   ? 38.53018 15.38444 -17.07951 1.000 33.61010 ? 374 HOH A O   1 
HETATM 1104 O  O   . HOH F 5 .   ? 2.31495  35.16232 5.21762   1.000 36.46729 ? 375 HOH A O   1 
HETATM 1105 O  O   . HOH F 5 .   ? 41.36218 21.03068 -13.11145 1.000 36.73801 ? 376 HOH A O   1 
HETATM 1106 O  O   . HOH F 5 .   ? 14.395   8.440    -17.455   1.000 53.06255 ? 377 HOH A O   1 
HETATM 1107 O  O   . HOH F 5 .   ? 1.81808  26.01037 -10.10471 1.000 37.96591 ? 378 HOH A O   1 
HETATM 1108 O  O   . HOH F 5 .   ? 17.14872 27.15224 19.91945  1.000 34.84582 ? 379 HOH A O   1 
HETATM 1109 O  O   . HOH F 5 .   ? 16.98840 12.63768 -19.20633 1.000 34.02625 ? 380 HOH A O   1 
HETATM 1110 O  O   . HOH F 5 .   ? 25.88295 27.71735 -17.97399 1.000 48.04851 ? 381 HOH A O   1 
HETATM 1111 O  O   . HOH F 5 .   ? 19.48580 16.51711 -21.94991 1.000 36.64839 ? 382 HOH A O   1 
HETATM 1112 O  O   . HOH F 5 .   ? 19.69449 36.71958 -4.94641  1.000 33.79540 ? 383 HOH A O   1 
HETATM 1113 O  O   . HOH F 5 .   ? 12.831   11.598   12.100    1.000 26.11528 ? 384 HOH A O   1 
HETATM 1114 O  O   . HOH F 5 .   ? 11.01671 10.05812 10.56216  1.000 39.60110 ? 385 HOH A O   1 
HETATM 1115 O  O   . HOH F 5 .   ? 13.078   19.654   20.640    1.000 49.72091 ? 386 HOH A O   1 
HETATM 1116 O  O   . HOH F 5 .   ? 8.67468  15.85009 -12.70514 1.000 31.78161 ? 387 HOH A O   1 
HETATM 1117 O  O   . HOH F 5 .   ? 7.95900  27.34015 15.77101  1.000 43.54773 ? 388 HOH A O   1 
HETATM 1118 O  O   . HOH F 5 .   ? 22.154   39.554   -4.191    1.000 34.15559 ? 389 HOH A O   1 
HETATM 1119 O  O   . HOH F 5 .   ? 5.53653  15.76037 -17.91297 1.000 48.84495 ? 390 HOH A O   1 
HETATM 1120 O  O   . HOH F 5 .   ? 13.789   15.545   -23.915   1.000 46.02271 ? 391 HOH A O   1 
HETATM 1121 O  O   . HOH F 5 .   ? 6.97846  16.95451 -10.89952 1.000 31.13142 ? 392 HOH A O   1 
HETATM 1122 O  O   . HOH F 5 .   ? 17.77109 38.55787 1.16020   1.000 41.04151 ? 393 HOH A O   1 
HETATM 1123 O  O   . HOH F 5 .   ? 3.99044  15.82822 -4.56002  1.000 41.07934 ? 394 HOH A O   1 
HETATM 1124 O  O   . HOH F 5 .   ? 39.19732 19.93764 -9.03634  1.000 34.40794 ? 395 HOH A O   1 
HETATM 1125 O  O   . HOH F 5 .   ? 9.11370  11.60500 -1.82556  1.000 31.63386 ? 396 HOH A O   1 
HETATM 1126 O  O   . HOH F 5 .   ? 31.11585 21.71052 -16.57472 1.000 38.99346 ? 397 HOH A O   1 
HETATM 1127 O  O   . HOH F 5 .   ? 28.54511 19.57263 -19.36380 1.000 42.52632 ? 398 HOH A O   1 
HETATM 1128 O  O   . HOH F 5 .   ? 28.89710 27.50438 -14.71830 1.000 40.88529 ? 399 HOH A O   1 
HETATM 1129 O  O   . HOH F 5 .   ? 11.245   7.859    7.105     1.000 40.23639 ? 400 HOH A O   1 
HETATM 1130 O  O   . HOH F 5 .   ? 7.20177  13.12820 -5.23433  1.000 31.45281 ? 401 HOH A O   1 
HETATM 1131 O  O   . HOH F 5 .   ? 5.78901  15.33984 -8.96495  1.000 32.07727 ? 402 HOH A O   1 
HETATM 1132 O  O   . HOH F 5 .   ? 6.08212  12.79761 -9.69911  1.000 38.61042 ? 403 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   . ARG A 12  ? 0.70292 0.76537 0.76941 -0.03867 0.06504  0.04624  12  ARG A N   
2    C  CA  . ARG A 12  ? 0.67121 0.74721 0.76533 -0.02812 0.06661  0.04012  12  ARG A CA  
3    C  C   . ARG A 12  ? 0.63945 0.71312 0.74148 -0.02715 0.08562  0.03958  12  ARG A C   
4    O  O   . ARG A 12  ? 0.65056 0.72671 0.74668 -0.00162 0.09396  0.03530  12  ARG A O   
5    C  CB  . ARG A 12  ? 0.64284 0.74639 0.78183 -0.02032 0.05183  0.03618  12  ARG A CB  
6    C  CG  . ARG A 12  ? 0.64286 0.74410 0.79623 -0.02984 0.03031  0.03240  12  ARG A CG  
7    C  CD  . ARG A 12  ? 0.65617 0.75126 0.80707 -0.01791 0.00880  0.02620  12  ARG A CD  
8    N  NE  . ARG A 12  ? 0.68254 0.78237 0.81584 -0.00947 -0.00735 0.02193  12  ARG A NE  
9    C  CZ  . ARG A 12  ? 0.70445 0.80297 0.82159 -0.00836 -0.01808 0.01673  12  ARG A CZ  
10   N  NH1 . ARG A 12  ? 0.70661 0.81998 0.82354 -0.00447 -0.02132 0.02055  12  ARG A NH1 
11   N  NH2 . ARG A 12  ? 0.71806 0.79338 0.82283 -0.01119 -0.02078 0.00863  12  ARG A NH2 
12   N  N   . ASP A 13  ? 0.58524 0.65286 0.71023 -0.05246 0.08653  0.04049  13  ASP A N   
13   C  CA  . ASP A 13  ? 0.49562 0.56786 0.67530 -0.06496 0.08980  0.04709  13  ASP A CA  
14   C  C   . ASP A 13  ? 0.48171 0.55919 0.64167 -0.06426 0.08719  0.06055  13  ASP A C   
15   O  O   . ASP A 13  ? 0.45461 0.56058 0.63994 -0.05922 0.08590  0.07873  13  ASP A O   
16   C  CB  . ASP A 13  ? 0.45532 0.50739 0.67496 -0.03814 0.09050  0.03755  13  ASP A CB  
17   C  CG  . ASP A 13  ? 0.40149 0.44329 0.67575 -0.01411 0.08417  0.02903  13  ASP A CG  
18   O  OD1 . ASP A 13  ? 0.40467 0.45501 0.67534 0.02726  0.07814  0.01496  13  ASP A OD1 
19   O  OD2 . ASP A 13  ? 0.33644 0.37856 0.67545 0.00379  0.09368  0.03125  13  ASP A OD2 
20   N  N   . GLU A 14  ? 0.51871 0.54007 0.60833 -0.06526 0.08679  0.05245  14  GLU A N   
21   C  CA  . GLU A 14  ? 0.53515 0.50059 0.57643 -0.03795 0.08972  0.04678  14  GLU A CA  
22   C  C   . GLU A 14  ? 0.50847 0.42497 0.53989 0.02833  0.09465  0.02136  14  GLU A C   
23   O  O   . GLU A 14  ? 0.49218 0.32007 0.53147 0.05723  0.09816  0.02896  14  GLU A O   
24   C  CB  . GLU A 14  ? 0.57376 0.53365 0.58135 -0.04855 0.08667  0.05941  14  GLU A CB  
25   C  CG  . GLU A 14  ? 0.62189 0.56706 0.58543 -0.04424 0.07715  0.06577  14  GLU A CG  
26   C  CD  . GLU A 14  ? 0.67354 0.58973 0.58977 -0.03567 0.06152  0.06887  14  GLU A CD  
27   O  OE1 . GLU A 14  ? 0.68695 0.58707 0.58948 -0.03832 0.05421  0.07484  14  GLU A OE1 
28   O  OE2 . GLU A 14  ? 0.70205 0.60880 0.59273 -0.02677 0.05494  0.06764  14  GLU A OE2 
29   N  N   . ALA A 15  ? 0.46929 0.46951 0.50954 0.03188  0.10033  0.00221  15  ALA A N   
30   C  CA  . ALA A 15  ? 0.44208 0.47710 0.47903 0.03742  0.11348  -0.01768 15  ALA A CA  
31   C  C   . ALA A 15  ? 0.44215 0.50100 0.44655 0.01755  0.09701  -0.02039 15  ALA A C   
32   O  O   . ALA A 15  ? 0.44930 0.57424 0.45086 0.02446  0.09370  -0.02746 15  ALA A O   
33   C  CB  . ALA A 15  ? 0.41506 0.48193 0.47964 0.01639  0.13387  -0.02479 15  ALA A CB  
34   N  N   . GLY A 16  ? 0.42023 0.40320 0.40763 0.01102  0.08177  -0.02910 16  GLY A N   
35   C  CA  . GLY A 16  ? 0.31705 0.37512 0.37165 0.04784  0.07171  -0.01870 16  GLY A CA  
36   C  C   . GLY A 16  ? 0.24077 0.36755 0.33870 0.04229  0.03924  -0.00776 16  GLY A C   
37   O  O   . GLY A 16  ? 0.23814 0.35759 0.34137 0.05493  0.01665  0.00561  16  GLY A O   
38   N  N   . ILE A 17  ? 0.20563 0.33402 0.31287 0.02351  0.01979  -0.00608 17  ILE A N   
39   C  CA  . ILE A 17  ? 0.17866 0.30066 0.29575 0.02871  -0.00644 0.00646  17  ILE A CA  
40   C  C   . ILE A 17  ? 0.22065 0.28734 0.28970 0.00498  -0.00660 0.01412  17  ILE A C   
41   O  O   . ILE A 17  ? 0.24035 0.27864 0.28044 0.01812  -0.00070 0.03008  17  ILE A O   
42   C  CB  . ILE A 17  ? 0.18472 0.31133 0.28504 0.03354  -0.02361 0.01474  17  ILE A CB  
43   C  CG1 . ILE A 17  ? 0.22943 0.31349 0.28165 0.00254  -0.04446 0.01893  17  ILE A CG1 
44   C  CG2 . ILE A 17  ? 0.20096 0.29820 0.28405 0.04387  -0.01100 0.01318  17  ILE A CG2 
45   C  CD1 . ILE A 17  ? 0.22661 0.36524 0.29000 0.05191  -0.04254 0.02496  17  ILE A CD1 
46   N  N   . THR A 18  ? 0.17084 0.30442 0.28988 0.00125  0.00279  0.01799  18  THR A N   
47   C  CA  . THR A 18  ? 0.16207 0.28239 0.29040 -0.00233 0.00389  0.02183  18  THR A CA  
48   C  C   . THR A 18  ? 0.15677 0.31864 0.28257 0.04133  0.02272  0.02066  18  THR A C   
49   O  O   . THR A 18  ? 0.22357 0.37623 0.29168 0.06461  0.03045  0.00546  18  THR A O   
50   C  CB  . THR A 18  ? 0.17150 0.29847 0.30339 -0.00399 0.00401  0.02028  18  THR A CB  
51   O  OG1 . THR A 18  ? 0.18374 0.31947 0.30826 0.01213  0.00773  0.04554  18  THR A OG1 
52   C  CG2 . THR A 18  ? 0.18723 0.33143 0.31146 -0.03153 0.00832  0.00087  18  THR A CG2 
53   N  N   . GLY A 19  ? 0.13964 0.32932 0.27170 0.03593  -0.00252 0.01825  19  GLY A N   
54   C  CA  . GLY A 19  ? 0.16114 0.35067 0.27862 0.04398  -0.00210 0.02951  19  GLY A CA  
55   C  C   . GLY A 19  ? 0.10923 0.32423 0.28562 0.02625  -0.00692 0.02697  19  GLY A C   
56   O  O   . GLY A 19  ? 0.16542 0.32240 0.28660 0.01947  -0.01657 0.01291  19  GLY A O   
57   N  N   . THR A 20  ? 0.15856 0.34080 0.30276 0.02847  0.00213  0.03543  20  THR A N   
58   C  CA  . THR A 20  ? 0.14947 0.31703 0.31639 -0.00414 0.00468  0.03949  20  THR A CA  
59   C  C   . THR A 20  ? 0.16724 0.33208 0.31636 -0.01132 0.01497  0.00476  20  THR A C   
60   O  O   . THR A 20  ? 0.19365 0.34615 0.32801 0.00199  0.01948  -0.02492 20  THR A O   
61   C  CB  . THR A 20  ? 0.18172 0.33570 0.33143 -0.02904 -0.00263 0.06173  20  THR A CB  
62   O  OG1 . THR A 20  ? 0.19052 0.34843 0.34645 -0.03010 -0.03442 0.07539  20  THR A OG1 
63   C  CG2 . THR A 20  ? 0.20557 0.38180 0.33265 -0.03820 0.00765  0.06672  20  THR A CG2 
64   N  N   . TRP A 21  ? 0.14556 0.29475 0.30533 -0.00606 0.00096  0.01789  21  TRP A N   
65   C  CA  . TRP A 21  ? 0.15431 0.24362 0.29697 0.01119  -0.00007 0.02265  21  TRP A CA  
66   C  C   . TRP A 21  ? 0.16191 0.22651 0.30390 0.01527  -0.00710 0.02207  21  TRP A C   
67   O  O   . TRP A 21  ? 0.18703 0.23909 0.30800 0.00057  -0.00210 0.01127  21  TRP A O   
68   C  CB  . TRP A 21  ? 0.16276 0.28498 0.29157 0.01809  0.00482  0.01592  21  TRP A CB  
69   C  CG  . TRP A 21  ? 0.14118 0.27928 0.28359 -0.00160 0.00346  0.00162  21  TRP A CG  
70   C  CD1 . TRP A 21  ? 0.16303 0.31108 0.28361 0.00421  0.00460  0.00382  21  TRP A CD1 
71   C  CD2 . TRP A 21  ? 0.14238 0.24714 0.27539 0.00177  0.00087  -0.02093 21  TRP A CD2 
72   N  NE1 . TRP A 21  ? 0.16972 0.27678 0.27760 0.01436  0.01308  0.00045  21  TRP A NE1 
73   C  CE2 . TRP A 21  ? 0.16303 0.25753 0.27374 0.02072  0.01310  -0.02745 21  TRP A CE2 
74   C  CE3 . TRP A 21  ? 0.18270 0.27326 0.27685 0.02329  0.00004  -0.02833 21  TRP A CE3 
75   C  CZ2 . TRP A 21  ? 0.18294 0.29181 0.27476 0.00791  -0.00637 -0.03218 21  TRP A CZ2 
76   C  CZ3 . TRP A 21  ? 0.19912 0.30571 0.27461 0.01423  0.00284  -0.01956 21  TRP A CZ3 
77   C  CH2 . TRP A 21  ? 0.19220 0.32488 0.27862 -0.00278 -0.00679 -0.01887 21  TRP A CH2 
78   N  N   . TYR A 22  ? 0.17208 0.22998 0.30686 0.00369  -0.00441 0.04080  22  TYR A N   
79   C  CA  . TYR A 22  ? 0.20042 0.23163 0.30264 0.02441  -0.02679 0.03806  22  TYR A CA  
80   C  C   . TYR A 22  ? 0.18935 0.22960 0.28821 0.04093  -0.02213 0.01827  22  TYR A C   
81   O  O   . TYR A 22  ? 0.21505 0.27083 0.28355 0.04113  -0.01585 -0.00937 22  TYR A O   
82   C  CB  . TYR A 22  ? 0.20272 0.22846 0.30996 0.04312  -0.04721 0.04366  22  TYR A CB  
83   C  CG  . TYR A 22  ? 0.19974 0.27982 0.31514 0.03235  -0.03706 0.03798  22  TYR A CG  
84   C  CD1 . TYR A 22  ? 0.21878 0.33193 0.31904 0.04297  -0.06039 0.04989  22  TYR A CD1 
85   C  CD2 . TYR A 22  ? 0.15841 0.29958 0.32125 0.01295  -0.02748 0.02108  22  TYR A CD2 
86   C  CE1 . TYR A 22  ? 0.18863 0.32434 0.32180 0.01701  -0.03523 0.04104  22  TYR A CE1 
87   C  CE2 . TYR A 22  ? 0.16153 0.32211 0.32304 0.01031  -0.01362 0.01801  22  TYR A CE2 
88   C  CZ  . TYR A 22  ? 0.19108 0.31694 0.32541 -0.00674 -0.02591 0.02078  22  TYR A CZ  
89   O  OH  . TYR A 22  ? 0.17840 0.33475 0.32792 0.00095  -0.02793 0.00025  22  TYR A OH  
90   N  N   . ASN A 23  ? 0.17961 0.19065 0.27950 0.01035  -0.01765 0.01540  23  ASN A N   
91   C  CA  . ASN A 23  ? 0.18967 0.19299 0.27183 0.00430  -0.01973 0.00415  23  ASN A CA  
92   C  C   . ASN A 23  ? 0.20794 0.19879 0.28825 0.02489  -0.03110 0.01541  23  ASN A C   
93   O  O   . ASN A 23  ? 0.23170 0.21002 0.29792 0.01964  -0.03191 0.02971  23  ASN A O   
94   C  CB  . ASN A 23  ? 0.17949 0.18419 0.25061 0.02543  -0.02030 -0.00095 23  ASN A CB  
95   C  CG  . ASN A 23  ? 0.16776 0.19825 0.24648 0.04380  -0.02173 -0.00022 23  ASN A CG  
96   O  OD1 . ASN A 23  ? 0.17720 0.22729 0.24339 0.03349  -0.03029 0.00878  23  ASN A OD1 
97   N  ND2 . ASN A 23  ? 0.17759 0.16131 0.25322 0.02148  -0.02679 -0.00064 23  ASN A ND2 
98   N  N   . GLN A 24  ? 0.20450 0.17114 0.29210 0.01041  -0.02149 0.01118  24  GLN A N   
99   C  CA  . GLN A 24  ? 0.19901 0.19996 0.29149 0.01604  -0.04507 0.02685  24  GLN A CA  
100  C  C   . GLN A 24  ? 0.23032 0.19695 0.29240 -0.00416 -0.06420 0.03686  24  GLN A C   
101  O  O   . GLN A 24  ? 0.29046 0.24814 0.29805 0.00953  -0.07727 0.04526  24  GLN A O   
102  C  CB  . GLN A 24  ? 0.18053 0.21303 0.29505 0.02385  -0.04453 0.01983  24  GLN A CB  
103  C  CG  . GLN A 24  ? 0.19956 0.20825 0.29428 0.05129  -0.03334 0.03521  24  GLN A CG  
104  C  CD  . GLN A 24  ? 0.18680 0.24293 0.29148 0.06389  -0.01972 0.03748  24  GLN A CD  
105  O  OE1 . GLN A 24  ? 0.21015 0.24671 0.27788 0.03223  -0.01259 0.03690  24  GLN A OE1 
106  N  NE2 . GLN A 24  ? 0.21519 0.21807 0.30016 0.04284  -0.02532 0.02741  24  GLN A NE2 
107  N  N   . LEU A 25  ? 0.22637 0.20132 0.28997 0.01132  -0.04911 0.02575  25  LEU A N   
108  C  CA  . LEU A 25  ? 0.21792 0.22526 0.29953 0.01517  -0.06009 0.03874  25  LEU A CA  
109  C  C   . LEU A 25  ? 0.26906 0.24152 0.30553 0.03836  -0.07160 0.05490  25  LEU A C   
110  O  O   . LEU A 25  ? 0.33373 0.28231 0.30809 0.02180  -0.09105 0.04202  25  LEU A O   
111  C  CB  . LEU A 25  ? 0.19632 0.24514 0.30975 0.01343  -0.02729 0.03962  25  LEU A CB  
112  C  CG  . LEU A 25  ? 0.22761 0.26501 0.32088 -0.01082 -0.03366 0.05142  25  LEU A CG  
113  C  CD1 . LEU A 25  ? 0.25050 0.27244 0.32397 -0.00403 -0.01280 0.03469  25  LEU A CD1 
114  C  CD2 . LEU A 25  ? 0.24171 0.26508 0.33463 -0.05411 -0.03282 0.06309  25  LEU A CD2 
115  N  N   . GLY A 26  ? 0.23099 0.26796 0.30877 0.03223  -0.07572 0.05869  26  GLY A N   
116  C  CA  . GLY A 26  ? 0.23736 0.25044 0.31245 0.01755  -0.07053 0.05225  26  GLY A CA  
117  C  C   . GLY A 26  ? 0.21773 0.22789 0.31188 0.01143  -0.06519 0.03546  26  GLY A C   
118  O  O   . GLY A 26  ? 0.24545 0.25668 0.33105 0.00662  -0.07312 0.01538  26  GLY A O   
119  N  N   . SER A 27  ? 0.18125 0.23537 0.28682 0.01386  -0.01841 0.05619  27  SER A N   
120  C  CA  . SER A 27  ? 0.16402 0.22336 0.27116 0.02978  -0.00953 0.04279  27  SER A CA  
121  C  C   . SER A 27  ? 0.14993 0.22807 0.26453 0.00013  -0.02066 0.03603  27  SER A C   
122  O  O   . SER A 27  ? 0.19537 0.22733 0.27389 0.00511  -0.00503 0.01102  27  SER A O   
123  C  CB  . SER A 27  ? 0.16479 0.20139 0.27140 0.01136  -0.01326 0.03475  27  SER A CB  
124  O  OG  . SER A 27  ? 0.18360 0.22897 0.26053 0.00421  -0.02527 0.02798  27  SER A OG  
125  N  N   . THR A 28  ? 0.16646 0.23814 0.26255 -0.00727 -0.03902 0.04349  28  THR A N   
126  C  CA  . THR A 28  ? 0.17199 0.25678 0.26330 -0.00451 -0.03211 0.03581  28  THR A CA  
127  C  C   . THR A 28  ? 0.18627 0.24827 0.25354 0.00121  -0.00980 0.02313  28  THR A C   
128  O  O   . THR A 28  ? 0.23511 0.21631 0.24287 -0.00379 0.00752  -0.00271 28  THR A O   
129  C  CB  . THR A 28  ? 0.18471 0.28495 0.28105 -0.04690 -0.03636 0.05479  28  THR A CB  
130  O  OG1 . THR A 28  ? 0.25524 0.31317 0.29326 -0.01455 -0.04632 0.05851  28  THR A OG1 
131  C  CG2 . THR A 28  ? 0.21193 0.33582 0.28489 -0.03404 -0.04129 0.05496  28  THR A CG2 
132  N  N   . PHE A 29  ? 0.17550 0.26537 0.25688 0.00728  -0.00904 0.02672  29  PHE A N   
133  C  CA  . PHE A 29  ? 0.15782 0.25323 0.25833 0.00958  -0.02248 0.01826  29  PHE A CA  
134  C  C   . PHE A 29  ? 0.17549 0.25404 0.26584 -0.00771 -0.01350 0.00830  29  PHE A C   
135  O  O   . PHE A 29  ? 0.19701 0.25802 0.26204 0.00523  -0.01531 -0.01244 29  PHE A O   
136  C  CB  . PHE A 29  ? 0.15236 0.24972 0.25642 0.02762  -0.02587 0.00832  29  PHE A CB  
137  C  CG  . PHE A 29  ? 0.17982 0.26568 0.25682 0.03698  -0.01861 -0.02041 29  PHE A CG  
138  C  CD1 . PHE A 29  ? 0.19164 0.27652 0.25998 0.04870  -0.01434 -0.01566 29  PHE A CD1 
139  C  CD2 . PHE A 29  ? 0.19830 0.26714 0.25975 0.01682  -0.02761 -0.02649 29  PHE A CD2 
140  C  CE1 . PHE A 29  ? 0.15336 0.25291 0.26374 0.00948  -0.00440 -0.00133 29  PHE A CE1 
141  C  CE2 . PHE A 29  ? 0.20625 0.24369 0.26745 0.02215  -0.01674 -0.02146 29  PHE A CE2 
142  C  CZ  . PHE A 29  ? 0.16166 0.23702 0.26892 0.00061  -0.00044 -0.01846 29  PHE A CZ  
143  N  N   . ILE A 30  ? 0.17633 0.22000 0.26325 -0.03580 -0.02909 0.01659  30  ILE A N   
144  C  CA  . ILE A 30  ? 0.16831 0.24230 0.27345 -0.02048 -0.04656 0.00733  30  ILE A CA  
145  C  C   . ILE A 30  ? 0.20111 0.24069 0.27050 0.00462  -0.00992 0.01637  30  ILE A C   
146  O  O   . ILE A 30  ? 0.27128 0.22882 0.27390 0.02609  -0.00657 0.01762  30  ILE A O   
147  C  CB  . ILE A 30  ? 0.21446 0.31838 0.28547 -0.03299 -0.05062 0.01657  30  ILE A CB  
148  C  CG1 . ILE A 30  ? 0.24275 0.33767 0.29796 -0.01385 -0.06698 0.02503  30  ILE A CG1 
149  C  CG2 . ILE A 30  ? 0.18613 0.36017 0.29443 -0.07107 -0.01979 0.01007  30  ILE A CG2 
150  C  CD1 . ILE A 30  ? 0.23063 0.39245 0.30745 -0.00358 -0.08140 0.02787  30  ILE A CD1 
151  N  N   . VAL A 31  ? 0.16925 0.27213 0.26806 0.01161  -0.01784 0.01952  31  VAL A N   
152  C  CA  . VAL A 31  ? 0.15702 0.26459 0.27908 0.02337  -0.00544 0.01579  31  VAL A CA  
153  C  C   . VAL A 31  ? 0.15417 0.26183 0.28638 0.03976  -0.00923 0.01220  31  VAL A C   
154  O  O   . VAL A 31  ? 0.15523 0.29926 0.29237 0.02368  -0.00674 0.02046  31  VAL A O   
155  C  CB  . VAL A 31  ? 0.17513 0.26329 0.28255 0.06220  -0.01443 -0.00021 31  VAL A CB  
156  C  CG1 . VAL A 31  ? 0.21084 0.29198 0.27878 0.05249  -0.01262 -0.02682 31  VAL A CG1 
157  C  CG2 . VAL A 31  ? 0.17916 0.29626 0.28556 0.03103  -0.02994 0.02307  31  VAL A CG2 
158  N  N   . THR A 32  ? 0.18353 0.26309 0.29604 -0.01742 -0.00963 0.01335  32  THR A N   
159  C  CA  . THR A 32  ? 0.20650 0.27141 0.30902 -0.03705 -0.01912 0.02212  32  THR A CA  
160  C  C   . THR A 32  ? 0.17925 0.24502 0.30729 -0.01608 0.00178  0.02700  32  THR A C   
161  O  O   . THR A 32  ? 0.20950 0.22786 0.30499 0.00571  0.00485  0.02650  32  THR A O   
162  C  CB  . THR A 32  ? 0.22519 0.30063 0.32366 -0.05332 -0.02644 0.03829  32  THR A CB  
163  O  OG1 . THR A 32  ? 0.25245 0.32458 0.33870 -0.00816 -0.03547 0.04194  32  THR A OG1 
164  C  CG2 . THR A 32  ? 0.22275 0.32666 0.32676 -0.10382 -0.01628 0.04688  32  THR A CG2 
165  N  N   . ALA A 33  ? 0.18919 0.27466 0.30718 -0.01770 -0.01114 0.00843  33  ALA A N   
166  C  CA  . ALA A 33  ? 0.15942 0.29577 0.31706 -0.00964 0.01046  0.00139  33  ALA A CA  
167  C  C   . ALA A 33  ? 0.18479 0.31650 0.33106 -0.01069 0.02704  0.02282  33  ALA A C   
168  O  O   . ALA A 33  ? 0.23844 0.36898 0.34368 0.00888  0.04216  0.02470  33  ALA A O   
169  C  CB  . ALA A 33  ? 0.19470 0.28720 0.31622 0.01430  0.01062  -0.02121 33  ALA A CB  
170  N  N   . GLY A 34  ? 0.22892 0.23058 0.33226 -0.03489 0.02194  0.03686  34  GLY A N   
171  C  CA  . GLY A 34  ? 0.25370 0.27730 0.33879 -0.04029 0.03671  0.05506  34  GLY A CA  
172  C  C   . GLY A 34  ? 0.21520 0.33639 0.34927 -0.03584 0.03709  0.07154  34  GLY A C   
173  O  O   . GLY A 34  ? 0.19807 0.36145 0.34424 -0.05720 0.03631  0.06551  34  GLY A O   
174  N  N   . ALA A 35  ? 0.20898 0.37082 0.36423 -0.03788 0.05004  0.09115  35  ALA A N   
175  C  CA  . ALA A 35  ? 0.24163 0.43222 0.38013 -0.08648 0.06400  0.11746  35  ALA A CA  
176  C  C   . ALA A 35  ? 0.27005 0.47382 0.39242 -0.09817 0.05161  0.12692  35  ALA A C   
177  O  O   . ALA A 35  ? 0.34667 0.54893 0.39710 -0.08480 0.03391  0.13771  35  ALA A O   
178  C  CB  . ALA A 35  ? 0.26853 0.44256 0.38535 -0.08187 0.06929  0.10509  35  ALA A CB  
179  N  N   . ASP A 36  ? 0.23698 0.43148 0.40142 -0.05729 0.04998  0.11619  36  ASP A N   
180  C  CA  . ASP A 36  ? 0.26088 0.42765 0.41130 -0.06004 0.04233  0.09528  36  ASP A CA  
181  C  C   . ASP A 36  ? 0.21735 0.39378 0.38059 -0.03803 0.04714  0.11566  36  ASP A C   
182  O  O   . ASP A 36  ? 0.23361 0.42171 0.39450 -0.01881 0.03718  0.16170  36  ASP A O   
183  C  CB  . ASP A 36  ? 0.33481 0.40482 0.43994 -0.07592 0.03215  0.07287  36  ASP A CB  
184  C  CG  . ASP A 36  ? 0.38090 0.41048 0.46007 -0.06643 0.03299  0.04826  36  ASP A CG  
185  O  OD1 . ASP A 36  ? 0.33644 0.35013 0.46568 -0.06459 0.02601  0.06520  36  ASP A OD1 
186  O  OD2 . ASP A 36  ? 0.45676 0.43650 0.46835 -0.09953 0.02323  0.02530  36  ASP A OD2 
187  N  N   . GLY A 37  ? 0.21243 0.32457 0.32987 -0.03539 0.03171  0.08640  37  GLY A N   
188  C  CA  . GLY A 37  ? 0.19342 0.29443 0.29622 -0.02261 0.01254  0.05441  37  GLY A CA  
189  C  C   . GLY A 37  ? 0.19007 0.23529 0.27509 -0.00631 0.02145  0.03944  37  GLY A C   
190  O  O   . GLY A 37  ? 0.18968 0.20908 0.26517 -0.01617 0.03084  0.01947  37  GLY A O   
191  N  N   . ALA A 38  ? 0.19486 0.24451 0.27062 0.00001  0.00466  0.03669  38  ALA A N   
192  C  CA  . ALA A 38  ? 0.21614 0.25177 0.26998 -0.01743 -0.01165 0.02298  38  ALA A CA  
193  C  C   . ALA A 38  ? 0.15518 0.26869 0.26545 -0.00421 0.00677  0.03281  38  ALA A C   
194  O  O   . ALA A 38  ? 0.16734 0.27511 0.27246 0.00938  0.01444  0.04015  38  ALA A O   
195  C  CB  . ALA A 38  ? 0.31718 0.26167 0.27736 -0.08268 -0.02428 0.00914  38  ALA A CB  
196  N  N   . LEU A 39  ? 0.18321 0.23959 0.25466 -0.03547 -0.00532 0.02971  39  LEU A N   
197  C  CA  . LEU A 39  ? 0.16976 0.22943 0.24797 -0.01750 -0.01147 0.01861  39  LEU A CA  
198  C  C   . LEU A 39  ? 0.16877 0.23272 0.24648 -0.03556 -0.01132 0.00979  39  LEU A C   
199  O  O   . LEU A 39  ? 0.18922 0.25942 0.24425 -0.04734 0.00374  0.00400  39  LEU A O   
200  C  CB  . LEU A 39  ? 0.18044 0.21590 0.25217 -0.05294 0.00059  -0.00008 39  LEU A CB  
201  C  CG  . LEU A 39  ? 0.16174 0.22165 0.26261 0.00707  0.00165  -0.02206 39  LEU A CG  
202  C  CD1 . LEU A 39  ? 0.15232 0.22311 0.26448 -0.02420 0.00178  -0.00674 39  LEU A CD1 
203  C  CD2 . LEU A 39  ? 0.17273 0.23718 0.26697 0.02877  0.00628  -0.00087 39  LEU A CD2 
204  N  N   . THR A 40  ? 0.15676 0.22679 0.25181 -0.02838 -0.03801 0.01978  40  THR A N   
205  C  CA  . THR A 40  ? 0.18539 0.23995 0.26753 -0.04329 -0.02175 0.03420  40  THR A CA  
206  C  C   . THR A 40  ? 0.22635 0.24168 0.26336 0.00017  -0.01486 0.02272  40  THR A C   
207  O  O   . THR A 40  ? 0.32578 0.26045 0.26661 0.05293  -0.00816 0.00590  40  THR A O   
208  C  CB  . THR A 40  ? 0.21924 0.24781 0.28973 -0.02196 -0.03265 0.04802  40  THR A CB  
209  O  OG1 A THR A 40  ? 0.21062 0.26829 0.29968 0.00033  -0.00662 0.03990  40  THR A OG1 
210  O  OG1 B THR A 40  ? 0.23298 0.25597 0.29311 -0.07011 -0.03767 0.04875  40  THR A OG1 
211  C  CG2 A THR A 40  ? 0.25848 0.26223 0.29034 0.00479  -0.05450 0.06139  40  THR A CG2 
212  C  CG2 B THR A 40  ? 0.19470 0.26487 0.29317 -0.03191 -0.02607 0.03582  40  THR A CG2 
213  N  N   . GLY A 41  ? 0.18382 0.23049 0.26398 -0.00046 -0.02185 0.00937  41  GLY A N   
214  C  CA  . GLY A 41  ? 0.19261 0.22624 0.26977 -0.01030 -0.01252 0.02352  41  GLY A CA  
215  C  C   . GLY A 41  ? 0.13646 0.22519 0.26865 -0.02215 -0.01847 0.01798  41  GLY A C   
216  O  O   . GLY A 41  ? 0.15956 0.26849 0.27590 0.00088  -0.02887 0.01612  41  GLY A O   
217  N  N   . THR A 42  ? 0.16572 0.20507 0.26415 -0.01592 -0.02422 0.02816  42  THR A N   
218  C  CA  . THR A 42  ? 0.17900 0.23116 0.26306 -0.03628 -0.03558 0.02318  42  THR A CA  
219  C  C   . THR A 42  ? 0.17390 0.25503 0.25536 -0.02651 -0.03989 0.01367  42  THR A C   
220  O  O   . THR A 42  ? 0.21800 0.23305 0.26334 -0.02010 -0.04609 0.00193  42  THR A O   
221  C  CB  . THR A 42  ? 0.21301 0.23158 0.27104 -0.00659 -0.04667 0.01776  42  THR A CB  
222  O  OG1 . THR A 42  ? 0.23048 0.28611 0.26759 -0.00618 -0.05180 0.02642  42  THR A OG1 
223  C  CG2 . THR A 42  ? 0.22008 0.23590 0.28122 -0.02266 -0.04055 0.02047  42  THR A CG2 
224  N  N   . TYR A 43  ? 0.15912 0.23801 0.24278 -0.02148 -0.03059 0.00415  43  TYR A N   
225  C  CA  . TYR A 43  ? 0.15561 0.23457 0.23674 -0.01614 -0.02948 0.01628  43  TYR A CA  
226  C  C   . TYR A 43  ? 0.18225 0.21318 0.23696 0.00322  -0.02493 0.02449  43  TYR A C   
227  O  O   . TYR A 43  ? 0.21486 0.22784 0.22689 0.00628  -0.01623 0.00319  43  TYR A O   
228  C  CB  . TYR A 43  ? 0.16559 0.21672 0.23648 -0.01428 -0.05151 0.00507  43  TYR A CB  
229  C  CG  . TYR A 43  ? 0.18237 0.17941 0.23296 -0.01536 -0.03628 0.00382  43  TYR A CG  
230  C  CD1 . TYR A 43  ? 0.19427 0.15748 0.23413 0.02150  -0.02245 0.01001  43  TYR A CD1 
231  C  CD2 . TYR A 43  ? 0.16766 0.19090 0.23520 0.02547  -0.02241 -0.00443 43  TYR A CD2 
232  C  CE1 . TYR A 43  ? 0.17142 0.22140 0.23209 0.00164  -0.05302 0.00097  43  TYR A CE1 
233  C  CE2 . TYR A 43  ? 0.17018 0.19100 0.23556 -0.01419 -0.02350 0.02075  43  TYR A CE2 
234  C  CZ  . TYR A 43  ? 0.15553 0.18117 0.23065 -0.02058 -0.04058 0.00217  43  TYR A CZ  
235  O  OH  . TYR A 43  ? 0.17387 0.20516 0.23581 -0.00028 -0.03808 0.00615  43  TYR A OH  
236  N  N   . GLU A 44  ? 0.17437 0.22580 0.24524 -0.00690 -0.05163 0.04359  44  GLU A N   
237  C  CA  . GLU A 44  ? 0.18675 0.22260 0.26004 0.01293  -0.05235 0.05631  44  GLU A CA  
238  C  C   . GLU A 44  ? 0.18805 0.23904 0.25006 0.00900  -0.03771 0.04295  44  GLU A C   
239  O  O   . GLU A 44  ? 0.20199 0.24154 0.24408 0.01300  -0.04599 0.03074  44  GLU A O   
240  C  CB  . GLU A 44  ? 0.21741 0.29675 0.28395 0.00444  -0.08237 0.07034  44  GLU A CB  
241  C  CG  . GLU A 44  ? 0.26317 0.40069 0.30078 0.00547  -0.09492 0.09342  44  GLU A CG  
242  C  CD  . GLU A 44  ? 0.31107 0.48424 0.31938 -0.00401 -0.10198 0.11506  44  GLU A CD  
243  O  OE1 . GLU A 44  ? 0.26998 0.53981 0.33063 -0.01041 -0.09783 0.13249  44  GLU A OE1 
244  O  OE2 . GLU A 44  ? 0.38498 0.49307 0.32583 -0.01626 -0.10977 0.11127  44  GLU A OE2 
245  N  N   . SER A 45  ? 0.19435 0.25308 0.24878 -0.03711 -0.04280 0.02491  45  SER A N   
246  C  CA  . SER A 45  ? 0.17240 0.24764 0.24420 0.00966  -0.05728 0.02572  45  SER A CA  
247  C  C   . SER A 45  ? 0.20743 0.27176 0.25555 0.01147  -0.05482 0.03130  45  SER A C   
248  O  O   . SER A 45  ? 0.25126 0.30448 0.26723 0.00912  -0.06022 0.02745  45  SER A O   
249  C  CB  . SER A 45  ? 0.18276 0.24104 0.24127 -0.00835 -0.03943 0.01469  45  SER A CB  
250  O  OG  . SER A 45  ? 0.21375 0.20422 0.23368 0.00019  -0.05006 0.02094  45  SER A OG  
251  N  N   . ALA A 46  ? 0.19295 0.22589 0.25846 0.01376  -0.02507 0.04903  46  ALA A N   
252  C  CA  . ALA A 46  ? 0.24040 0.25083 0.26210 0.03796  -0.02764 0.04721  46  ALA A CA  
253  C  C   . ALA A 46  ? 0.22993 0.25339 0.24922 0.00224  -0.02333 0.05136  46  ALA A C   
254  O  O   . ALA A 46  ? 0.30572 0.29970 0.24797 0.02066  -0.01963 0.06975  46  ALA A O   
255  C  CB  . ALA A 46  ? 0.28631 0.27807 0.27307 0.05420  -0.01268 0.05327  46  ALA A CB  
256  N  N   . VAL A 47  ? 0.20912 0.25856 0.24535 -0.00715 -0.03235 0.02958  47  VAL A N   
257  C  CA  . VAL A 47  ? 0.23073 0.19143 0.24213 -0.00218 -0.04016 0.02115  47  VAL A CA  
258  C  C   . VAL A 47  ? 0.23820 0.20186 0.22976 -0.00650 -0.04078 0.02355  47  VAL A C   
259  O  O   . VAL A 47  ? 0.23796 0.21478 0.22778 -0.00249 -0.04457 0.01013  47  VAL A O   
260  C  CB  . VAL A 47  ? 0.21713 0.18651 0.25679 0.02397  -0.06072 0.02061  47  VAL A CB  
261  C  CG1 . VAL A 47  ? 0.27243 0.22188 0.26255 0.03181  -0.05049 0.04965  47  VAL A CG1 
262  C  CG2 . VAL A 47  ? 0.25342 0.19504 0.25858 0.00917  -0.06717 0.01264  47  VAL A CG2 
263  N  N   . GLY A 48  ? 0.20905 0.24381 0.22834 -0.01187 -0.05543 0.00909  48  GLY A N   
264  C  CA  . GLY A 48  ? 0.20971 0.21491 0.22528 0.01703  -0.03014 0.01286  48  GLY A CA  
265  C  C   . GLY A 48  ? 0.26305 0.21264 0.22757 0.00385  -0.03281 0.01178  48  GLY A C   
266  O  O   . GLY A 48  ? 0.24812 0.23855 0.23297 -0.03450 -0.04023 0.00378  48  GLY A O   
267  N  N   . ASN A 49  ? 0.27069 0.19285 0.23109 -0.00809 -0.02595 0.00696  49  ASN A N   
268  C  CA  . ASN A 49  ? 0.26760 0.21396 0.23361 0.00005  -0.02259 0.01453  49  ASN A CA  
269  C  C   . ASN A 49  ? 0.24345 0.21684 0.23855 -0.01189 -0.04685 0.01889  49  ASN A C   
270  O  O   . ASN A 49  ? 0.30293 0.23152 0.24276 -0.01756 -0.03437 0.01008  49  ASN A O   
271  C  CB  . ASN A 49  ? 0.31505 0.25369 0.23713 0.02490  -0.03110 0.01085  49  ASN A CB  
272  C  CG  . ASN A 49  ? 0.37490 0.30849 0.24148 0.02225  -0.02818 0.02018  49  ASN A CG  
273  O  OD1 . ASN A 49  ? 0.38600 0.32434 0.25258 0.01336  -0.02622 0.00016  49  ASN A OD1 
274  N  ND2 . ASN A 49  ? 0.39539 0.34636 0.24159 0.01320  -0.01634 0.03399  49  ASN A ND2 
275  N  N   . ALA A 50  ? 0.21294 0.25941 0.23817 -0.03305 -0.05610 0.01562  50  ALA A N   
276  C  CA  . ALA A 50  ? 0.24471 0.27220 0.23869 -0.05989 -0.05739 0.01449  50  ALA A CA  
277  C  C   . ALA A 50  ? 0.23524 0.27336 0.25135 -0.05287 -0.04505 0.01703  50  ALA A C   
278  O  O   . ALA A 50  ? 0.27559 0.27400 0.26406 -0.03960 -0.02312 0.01927  50  ALA A O   
279  C  CB  . ALA A 50  ? 0.30872 0.27352 0.23165 -0.05982 -0.06684 0.01185  50  ALA A CB  
280  N  N   . GLU A 51  ? 0.23955 0.26120 0.24856 -0.03184 -0.05267 -0.00376 51  GLU A N   
281  C  CA  . GLU A 51  ? 0.28023 0.32048 0.25488 -0.02796 -0.04737 0.01412  51  GLU A CA  
282  C  C   . GLU A 51  ? 0.22031 0.28108 0.26291 -0.03919 -0.04666 0.02690  51  GLU A C   
283  O  O   . GLU A 51  ? 0.25391 0.27797 0.27042 -0.00576 -0.04132 0.02537  51  GLU A O   
284  C  CB  . GLU A 51  ? 0.40258 0.40751 0.26421 -0.06858 -0.04262 0.01130  51  GLU A CB  
285  C  CG  . GLU A 51  ? 0.43780 0.41269 0.26834 -0.08117 -0.03975 -0.00014 51  GLU A CG  
286  C  CD  . GLU A 51  ? 0.44258 0.45646 0.27320 -0.06863 -0.03692 0.00609  51  GLU A CD  
287  O  OE1 . GLU A 51  ? 0.44929 0.50248 0.27810 -0.04790 -0.03818 0.01797  51  GLU A OE1 
288  O  OE2 . GLU A 51  ? 0.44003 0.47829 0.27386 -0.05695 -0.02281 -0.00386 51  GLU A OE2 
289  N  N   . SER A 52  ? 0.21170 0.28907 0.25846 0.00554  -0.05330 0.03155  52  SER A N   
290  C  CA  . SER A 52  ? 0.20819 0.28875 0.25846 -0.02295 -0.05126 0.03298  52  SER A CA  
291  C  C   . SER A 52  ? 0.23878 0.26757 0.24541 -0.02213 -0.04564 0.02497  52  SER A C   
292  O  O   . SER A 52  ? 0.26445 0.25996 0.24554 -0.03787 -0.04125 0.02611  52  SER A O   
293  C  CB  . SER A 52  ? 0.23040 0.41565 0.27743 -0.09944 -0.06371 0.04157  52  SER A CB  
294  O  OG  . SER A 52  ? 0.28164 0.51252 0.29328 -0.08461 -0.07418 0.04528  52  SER A OG  
295  N  N   . ARG A 53  ? 0.23977 0.25062 0.23969 0.00637  -0.05624 0.02617  53  ARG A N   
296  C  CA  . ARG A 53  ? 0.20831 0.25685 0.24406 0.00799  -0.04442 0.01329  53  ARG A CA  
297  C  C   . ARG A 53  ? 0.17788 0.24575 0.23012 0.01316  -0.05371 -0.00828 53  ARG A C   
298  O  O   . ARG A 53  ? 0.23087 0.27528 0.23225 -0.01970 -0.03381 -0.00769 53  ARG A O   
299  C  CB  . ARG A 53  ? 0.20127 0.32155 0.27311 -0.01360 -0.02156 -0.00468 53  ARG A CB  
300  C  CG  . ARG A 53  ? 0.19889 0.37915 0.30192 0.02194  0.00363  -0.01734 53  ARG A CG  
301  C  CD  . ARG A 53  ? 0.30778 0.48670 0.33146 0.00459  -0.00201 -0.03112 53  ARG A CD  
302  N  NE  A ARG A 53  ? 0.33395 0.50098 0.34039 -0.02575 -0.02907 -0.03646 53  ARG A NE  
303  N  NE  B ARG A 53  ? 0.39385 0.53295 0.34502 0.01186  -0.02632 -0.04371 53  ARG A NE  
304  C  CZ  A ARG A 53  ? 0.35171 0.51368 0.34739 -0.03761 -0.06209 -0.04147 53  ARG A CZ  
305  C  CZ  B ARG A 53  ? 0.53115 0.55950 0.36290 0.07412  -0.03460 -0.04785 53  ARG A CZ  
306  N  NH1 A ARG A 53  ? 0.34453 0.50113 0.34758 -0.04224 -0.07765 -0.04841 53  ARG A NH1 
307  N  NH1 B ARG A 53  ? 0.57763 0.57829 0.36956 0.07501  -0.04123 -0.04681 53  ARG A NH1 
308  N  NH2 A ARG A 53  ? 0.34176 0.52758 0.35082 -0.04052 -0.07501 -0.03867 53  ARG A NH2 
309  N  NH2 B ARG A 53  ? 0.56750 0.54813 0.36912 0.13163  -0.03433 -0.05592 53  ARG A NH2 
310  N  N   . TYR A 54  ? 0.18092 0.26186 0.22491 -0.00376 -0.06918 0.00307  54  TYR A N   
311  C  CA  . TYR A 54  ? 0.18121 0.23964 0.22357 -0.01440 -0.03390 0.01544  54  TYR A CA  
312  C  C   . TYR A 54  ? 0.20136 0.23946 0.21482 -0.04858 -0.02797 0.00033  54  TYR A C   
313  O  O   . TYR A 54  ? 0.20110 0.23969 0.21398 -0.01554 -0.01360 -0.01527 54  TYR A O   
314  C  CB  . TYR A 54  ? 0.17683 0.24439 0.22104 -0.00267 -0.03624 0.01933  54  TYR A CB  
315  C  CG  . TYR A 54  ? 0.19052 0.23550 0.20934 -0.01443 -0.03802 -0.00434 54  TYR A CG  
316  C  CD1 . TYR A 54  ? 0.20321 0.24269 0.21009 -0.03393 -0.02426 0.01175  54  TYR A CD1 
317  C  CD2 . TYR A 54  ? 0.20089 0.24774 0.20365 -0.03515 -0.02895 -0.02234 54  TYR A CD2 
318  C  CE1 . TYR A 54  ? 0.20279 0.26616 0.20487 -0.03095 -0.03921 0.00447  54  TYR A CE1 
319  C  CE2 . TYR A 54  ? 0.20531 0.23571 0.20300 -0.02823 -0.03680 -0.00769 54  TYR A CE2 
320  C  CZ  . TYR A 54  ? 0.23363 0.24856 0.20068 -0.03455 -0.03648 -0.00009 54  TYR A CZ  
321  O  OH  . TYR A 54  ? 0.24788 0.23766 0.19246 -0.00753 -0.04393 0.00736  54  TYR A OH  
322  N  N   . VAL A 55  ? 0.22265 0.22576 0.21007 -0.04548 -0.02722 0.03263  55  VAL A N   
323  C  CA  . VAL A 55  ? 0.23613 0.21738 0.21898 -0.04815 -0.04772 0.01346  55  VAL A CA  
324  C  C   . VAL A 55  ? 0.19358 0.22098 0.23036 -0.01103 -0.02702 -0.00549 55  VAL A C   
325  O  O   . VAL A 55  ? 0.17171 0.23277 0.24595 -0.00450 -0.02517 -0.01427 55  VAL A O   
326  C  CB  . VAL A 55  ? 0.26310 0.23216 0.22358 -0.04062 -0.05218 0.01790  55  VAL A CB  
327  C  CG1 . VAL A 55  ? 0.26723 0.23247 0.22781 -0.03117 -0.05031 0.02843  55  VAL A CG1 
328  C  CG2 . VAL A 55  ? 0.24472 0.26409 0.22583 -0.05886 -0.04314 -0.00772 55  VAL A CG2 
329  N  N   . LEU A 56  ? 0.18915 0.23071 0.22681 -0.03442 -0.03336 -0.00662 56  LEU A N   
330  C  CA  . LEU A 56  ? 0.20652 0.22017 0.23318 -0.04567 -0.04118 0.00581  56  LEU A CA  
331  C  C   . LEU A 56  ? 0.18246 0.22841 0.23389 -0.05569 -0.03198 0.01352  56  LEU A C   
332  O  O   . LEU A 56  ? 0.17478 0.24877 0.24133 -0.02079 -0.04000 0.03239  56  LEU A O   
333  C  CB  . LEU A 56  ? 0.18676 0.22872 0.24326 -0.03211 -0.01479 0.00517  56  LEU A CB  
334  C  CG  . LEU A 56  ? 0.18617 0.23200 0.24527 0.01044  -0.01506 0.00978  56  LEU A CG  
335  C  CD1 . LEU A 56  ? 0.18034 0.27154 0.23687 0.00967  -0.03386 0.01178  56  LEU A CD1 
336  C  CD2 . LEU A 56  ? 0.21142 0.23370 0.25086 0.02851  -0.01764 0.02611  56  LEU A CD2 
337  N  N   . THR A 57  ? 0.17486 0.20522 0.22705 -0.03646 -0.03158 0.00767  57  THR A N   
338  C  CA  A THR A 57  ? 0.17524 0.18286 0.22969 -0.04193 -0.02700 0.02179  57  THR A CA  
339  C  CA  B THR A 57  ? 0.15986 0.21168 0.22638 -0.03121 -0.02361 0.01191  57  THR A CA  
340  C  C   . THR A 57  ? 0.17176 0.19143 0.21545 -0.03264 -0.02088 0.01191  57  THR A C   
341  O  O   . THR A 57  ? 0.16997 0.21014 0.21031 -0.04867 -0.02697 0.01641  57  THR A O   
342  C  CB  A THR A 57  ? 0.21298 0.19852 0.24807 -0.03256 -0.03489 -0.00063 57  THR A CB  
343  C  CB  B THR A 57  ? 0.15642 0.26097 0.23637 -0.02637 -0.02302 -0.00808 57  THR A CB  
344  O  OG1 A THR A 57  ? 0.22909 0.20917 0.25641 -0.01445 -0.05066 -0.00661 57  THR A OG1 
345  O  OG1 B THR A 57  ? 0.13946 0.27776 0.24142 -0.01228 -0.01461 -0.00956 57  THR A OG1 
346  C  CG2 A THR A 57  ? 0.21211 0.17667 0.25099 -0.01891 -0.03154 -0.00278 57  THR A CG2 
347  C  CG2 B THR A 57  ? 0.14802 0.28140 0.23659 -0.03662 -0.03529 -0.01588 57  THR A CG2 
348  N  N   . GLY A 58  ? 0.18991 0.20153 0.20129 -0.01990 -0.01418 0.01386  58  GLY A N   
349  C  CA  . GLY A 58  ? 0.19934 0.19515 0.20004 -0.03099 -0.01116 0.01947  58  GLY A CA  
350  C  C   . GLY A 58  ? 0.19378 0.15939 0.20088 -0.01024 -0.00207 0.04555  58  GLY A C   
351  O  O   . GLY A 58  ? 0.19348 0.19848 0.20394 -0.01428 0.00808  0.03370  58  GLY A O   
352  N  N   . ARG A 59  ? 0.17232 0.21832 0.19801 -0.02620 -0.00485 0.04123  59  ARG A N   
353  C  CA  . ARG A 59  ? 0.19017 0.16392 0.19956 0.00060  -0.01605 0.03706  59  ARG A CA  
354  C  C   . ARG A 59  ? 0.17237 0.20044 0.20600 0.00121  -0.00014 0.01962  59  ARG A C   
355  O  O   . ARG A 59  ? 0.19603 0.21956 0.21680 -0.03542 0.01339  0.04301  59  ARG A O   
356  C  CB  . ARG A 59  ? 0.20773 0.17452 0.21152 0.01612  -0.02056 0.02513  59  ARG A CB  
357  C  CG  . ARG A 59  ? 0.23946 0.18298 0.21887 0.01033  0.00084  0.04223  59  ARG A CG  
358  C  CD  . ARG A 59  ? 0.24688 0.18735 0.22565 -0.02166 0.02526  0.04261  59  ARG A CD  
359  N  NE  . ARG A 59  ? 0.22253 0.17793 0.23026 -0.01687 0.02230  0.02986  59  ARG A NE  
360  C  CZ  . ARG A 59  ? 0.22078 0.21327 0.23570 -0.02156 0.01072  0.00649  59  ARG A CZ  
361  N  NH1 . ARG A 59  ? 0.23724 0.22328 0.25232 -0.01834 0.00139  0.00750  59  ARG A NH1 
362  N  NH2 . ARG A 59  ? 0.22041 0.24748 0.23594 -0.00752 0.02276  0.00302  59  ARG A NH2 
363  N  N   . TYR A 60  ? 0.18796 0.21814 0.21329 0.01447  0.01420  0.01165  60  TYR A N   
364  C  CA  . TYR A 60  ? 0.16457 0.20843 0.22379 0.02137  0.02308  0.02835  60  TYR A CA  
365  C  C   . TYR A 60  ? 0.19840 0.23416 0.22074 -0.00801 0.02489  0.02793  60  TYR A C   
366  O  O   . TYR A 60  ? 0.25485 0.20964 0.22724 -0.02936 0.01933  0.02820  60  TYR A O   
367  C  CB  . TYR A 60  ? 0.13789 0.25043 0.25136 0.00815  0.02409  0.03293  60  TYR A CB  
368  C  CG  . TYR A 60  ? 0.15950 0.24260 0.26812 -0.00003 0.02467  0.03302  60  TYR A CG  
369  C  CD1 . TYR A 60  ? 0.16893 0.26952 0.28340 0.00971  0.02373  0.01530  60  TYR A CD1 
370  C  CD2 . TYR A 60  ? 0.13360 0.27644 0.27060 0.01367  0.02243  0.04061  60  TYR A CD2 
371  C  CE1 . TYR A 60  ? 0.20012 0.25174 0.29162 -0.01469 0.03820  0.02155  60  TYR A CE1 
372  C  CE2 . TYR A 60  ? 0.16640 0.31645 0.27964 -0.01239 0.02710  0.03568  60  TYR A CE2 
373  C  CZ  . TYR A 60  ? 0.15923 0.31189 0.28982 -0.01841 0.04289  0.02815  60  TYR A CZ  
374  O  OH  . TYR A 60  ? 0.20546 0.31729 0.30378 -0.02575 0.05291  -0.00240 60  TYR A OH  
375  N  N   . ASP A 61  ? 0.17080 0.23360 0.21089 0.01591  0.03678  0.01023  61  ASP A N   
376  C  CA  . ASP A 61  ? 0.16237 0.23480 0.21847 -0.03258 0.04744  0.01505  61  ASP A CA  
377  C  C   . ASP A 61  ? 0.19411 0.24924 0.24082 -0.02295 0.04103  0.01539  61  ASP A C   
378  O  O   . ASP A 61  ? 0.22337 0.26086 0.25267 0.02366  0.03811  0.02425  61  ASP A O   
379  C  CB  . ASP A 61  ? 0.21116 0.24750 0.20259 -0.00707 0.02714  0.01351  61  ASP A CB  
380  C  CG  . ASP A 61  ? 0.22795 0.26462 0.20155 0.00643  0.03157  0.02099  61  ASP A CG  
381  O  OD1 . ASP A 61  ? 0.21828 0.24609 0.20451 0.00061  0.04003  0.03121  61  ASP A OD1 
382  O  OD2 . ASP A 61  ? 0.22529 0.27263 0.20085 -0.00380 0.01843  0.00547  61  ASP A OD2 
383  N  N   . SER A 62  ? 0.17754 0.26618 0.24983 -0.03699 0.02447  0.03233  62  SER A N   
384  C  CA  . SER A 62  ? 0.20276 0.30274 0.26257 -0.03781 0.02537  0.03411  62  SER A CA  
385  C  C   . SER A 62  ? 0.25467 0.36662 0.25834 -0.04270 0.03841  0.02303  62  SER A C   
386  O  O   . SER A 62  ? 0.22490 0.45555 0.26055 -0.03456 0.05399  0.02706  62  SER A O   
387  C  CB  . SER A 62  ? 0.23956 0.29107 0.29260 -0.03978 -0.00229 0.05087  62  SER A CB  
388  O  OG  . SER A 62  ? 0.26220 0.32593 0.32163 -0.05958 -0.01170 0.05430  62  SER A OG  
389  N  N   . ALA A 63  ? 0.32895 0.31087 0.25471 -0.03957 0.03746  0.01321  63  ALA A N   
390  C  CA  . ALA A 63  ? 0.31299 0.31451 0.25768 -0.01863 0.05444  0.01284  63  ALA A CA  
391  C  C   . ALA A 63  ? 0.29048 0.32760 0.27162 0.00627  0.06451  0.01074  63  ALA A C   
392  O  O   . ALA A 63  ? 0.29691 0.36515 0.26547 0.01122  0.05369  0.00560  63  ALA A O   
393  C  CB  . ALA A 63  ? 0.34102 0.34619 0.25337 -0.01967 0.05964  0.01256  63  ALA A CB  
394  N  N   . PRO A 64  ? 0.27982 0.31943 0.29578 -0.02827 0.07647  0.02911  64  PRO A N   
395  C  CA  . PRO A 64  ? 0.33623 0.31738 0.30348 0.00239  0.07531  0.01109  64  PRO A CA  
396  C  C   . PRO A 64  ? 0.34624 0.32497 0.29562 -0.00094 0.10871  -0.00598 64  PRO A C   
397  O  O   . PRO A 64  ? 0.39269 0.35535 0.29504 0.02110  0.11797  -0.01155 64  PRO A O   
398  C  CB  . PRO A 64  ? 0.30746 0.35454 0.31342 -0.00694 0.07587  0.03262  64  PRO A CB  
399  C  CG  . PRO A 64  ? 0.28624 0.35120 0.31665 -0.01766 0.07589  0.03725  64  PRO A CG  
400  C  CD  . PRO A 64  ? 0.26230 0.34548 0.30967 -0.02837 0.07959  0.03568  64  PRO A CD  
401  N  N   . ALA A 65  ? 0.32695 0.34271 0.29725 -0.01899 0.09965  -0.03148 65  ALA A N   
402  C  CA  . ALA A 65  ? 0.41313 0.37074 0.31233 -0.01692 0.10048  -0.04720 65  ALA A CA  
403  C  C   . ALA A 65  ? 0.47515 0.41885 0.33008 -0.01517 0.12708  -0.06371 65  ALA A C   
404  O  O   . ALA A 65  ? 0.46564 0.39895 0.33590 0.00731  0.13275  -0.04977 65  ALA A O   
405  C  CB  . ALA A 65  ? 0.42961 0.34872 0.31127 -0.00726 0.08951  -0.04321 65  ALA A CB  
406  N  N   . THR A 66  ? 0.54990 0.47588 0.34449 -0.02282 0.14211  -0.08548 66  THR A N   
407  C  CA  . THR A 66  ? 0.59146 0.55945 0.36200 -0.03761 0.16540  -0.07312 66  THR A CA  
408  C  C   . THR A 66  ? 0.62275 0.57198 0.36603 -0.01998 0.16965  -0.08400 66  THR A C   
409  O  O   . THR A 66  ? 0.64250 0.62450 0.37811 -0.00534 0.17445  -0.08224 66  THR A O   
410  C  CB  . THR A 66  ? 0.62064 0.60826 0.37008 -0.04516 0.18358  -0.06124 66  THR A CB  
411  O  OG1 . THR A 66  ? 0.63619 0.62414 0.36999 -0.02454 0.20339  -0.03752 66  THR A OG1 
412  C  CG2 . THR A 66  ? 0.62640 0.62567 0.37745 -0.06061 0.18049  -0.06322 66  THR A CG2 
413  N  N   . ASP A 67  ? 0.60959 0.51562 0.35976 -0.04653 0.16087  -0.08232 67  ASP A N   
414  C  CA  . ASP A 67  ? 0.61181 0.47554 0.35316 -0.03455 0.13759  -0.08161 67  ASP A CA  
415  C  C   . ASP A 67  ? 0.59943 0.45744 0.34921 -0.01898 0.13839  -0.07978 67  ASP A C   
416  O  O   . ASP A 67  ? 0.65253 0.47934 0.35423 -0.04226 0.13927  -0.09115 67  ASP A O   
417  C  CB  . ASP A 67  ? 0.59673 0.44834 0.35278 -0.01074 0.11431  -0.08420 67  ASP A CB  
418  C  CG  . ASP A 67  ? 0.59184 0.48931 0.36054 -0.03139 0.09160  -0.06536 67  ASP A CG  
419  O  OD1 . ASP A 67  ? 0.59968 0.45808 0.35475 -0.04189 0.09501  -0.04581 67  ASP A OD1 
420  O  OD2 . ASP A 67  ? 0.57755 0.52982 0.37068 -0.04616 0.06745  -0.07405 67  ASP A OD2 
421  N  N   . GLY A 68  ? 0.52333 0.42821 0.33798 0.04984  0.13717  -0.08017 68  GLY A N   
422  C  CA  . GLY A 68  ? 0.49018 0.42549 0.32598 0.07242  0.12814  -0.07364 68  GLY A CA  
423  C  C   . GLY A 68  ? 0.44834 0.40284 0.31598 0.05924  0.10426  -0.05526 68  GLY A C   
424  O  O   . GLY A 68  ? 0.46380 0.40425 0.32593 0.06364  0.10263  -0.03440 68  GLY A O   
425  N  N   . SER A 69  ? 0.36465 0.32486 0.29855 0.03152  0.07873  -0.05350 69  SER A N   
426  C  CA  . SER A 69  ? 0.28511 0.29372 0.28610 0.00547  0.05223  -0.04832 69  SER A CA  
427  C  C   . SER A 69  ? 0.24241 0.28911 0.27576 -0.00778 0.05997  -0.01968 69  SER A C   
428  O  O   . SER A 69  ? 0.26534 0.31578 0.28461 -0.00522 0.05176  -0.00071 69  SER A O   
429  C  CB  . SER A 69  ? 0.31203 0.32372 0.29162 0.01184  0.00270  -0.05285 69  SER A CB  
430  O  OG  . SER A 69  ? 0.39041 0.38606 0.30042 0.00892  -0.01024 -0.05234 69  SER A OG  
431  N  N   . GLY A 70  ? 0.25906 0.22914 0.26017 0.02724  0.06724  -0.02869 70  GLY A N   
432  C  CA  . GLY A 70  ? 0.26198 0.18434 0.24991 0.01097  0.05757  -0.03243 70  GLY A CA  
433  C  C   . GLY A 70  ? 0.21243 0.21377 0.23779 0.00586  0.05988  -0.03488 70  GLY A C   
434  O  O   . GLY A 70  ? 0.23739 0.25158 0.22378 0.00206  0.03939  -0.02604 70  GLY A O   
435  N  N   . THR A 71  ? 0.20317 0.21203 0.23807 0.00850  0.05619  -0.04277 71  THR A N   
436  C  CA  . THR A 71  ? 0.17203 0.22973 0.24864 0.01585  0.04954  -0.02687 71  THR A CA  
437  C  C   . THR A 71  ? 0.16228 0.23545 0.24188 -0.00185 0.04260  -0.01782 71  THR A C   
438  O  O   . THR A 71  ? 0.19109 0.25822 0.23709 0.01172  0.02850  0.00287  71  THR A O   
439  C  CB  . THR A 71  ? 0.18049 0.26101 0.26699 0.00749  0.04783  -0.02458 71  THR A CB  
440  O  OG1 . THR A 71  ? 0.23778 0.28549 0.28215 0.01875  0.07108  -0.00210 71  THR A OG1 
441  C  CG2 . THR A 71  ? 0.17710 0.27720 0.26797 -0.02018 0.03302  -0.01397 71  THR A CG2 
442  N  N   . ALA A 72  ? 0.15591 0.22711 0.24083 0.02310  0.04568  -0.01892 72  ALA A N   
443  C  CA  . ALA A 72  ? 0.14489 0.22564 0.23095 0.00208  0.03448  -0.00983 72  ALA A CA  
444  C  C   . ALA A 72  ? 0.17042 0.17800 0.22786 -0.01111 0.03306  0.00636  72  ALA A C   
445  O  O   . ALA A 72  ? 0.19891 0.19584 0.23429 -0.01023 0.01317  0.00836  72  ALA A O   
446  C  CB  . ALA A 72  ? 0.15763 0.22875 0.23144 0.04808  0.02486  -0.00582 72  ALA A CB  
447  N  N   . LEU A 73  ? 0.17435 0.19399 0.22427 0.00255  0.01734  -0.00493 73  LEU A N   
448  C  CA  A LEU A 73  ? 0.16357 0.18910 0.22528 -0.00878 0.00871  -0.00427 73  LEU A CA  
449  C  CA  B LEU A 73  ? 0.17587 0.21006 0.22156 0.00076  0.02193  -0.00945 73  LEU A CA  
450  C  C   . LEU A 73  ? 0.18097 0.18896 0.21414 -0.02937 0.01800  0.00417  73  LEU A C   
451  O  O   . LEU A 73  ? 0.19139 0.17436 0.22256 -0.00800 0.02033  -0.00063 73  LEU A O   
452  C  CB  A LEU A 73  ? 0.15418 0.17909 0.24218 -0.00984 -0.02246 0.00004  73  LEU A CB  
453  C  CB  B LEU A 73  ? 0.18137 0.24407 0.22982 0.03014  0.01874  -0.01710 73  LEU A CB  
454  C  CG  A LEU A 73  ? 0.16422 0.19641 0.25296 -0.01654 -0.02541 0.00025  73  LEU A CG  
455  C  CG  B LEU A 73  ? 0.17737 0.27034 0.23413 0.03896  0.02923  -0.02860 73  LEU A CG  
456  C  CD1 A LEU A 73  ? 0.17088 0.22305 0.25448 0.01801  -0.03715 -0.01533 73  LEU A CD1 
457  C  CD1 B LEU A 73  ? 0.15953 0.32041 0.23788 0.08901  0.04866  -0.02260 73  LEU A CD1 
458  C  CD2 A LEU A 73  ? 0.13494 0.18239 0.25574 -0.01754 -0.05040 -0.00317 73  LEU A CD2 
459  C  CD2 B LEU A 73  ? 0.15658 0.25116 0.23626 0.04691  0.01324  -0.03285 73  LEU A CD2 
460  N  N   . GLY A 74  ? 0.14000 0.19353 0.19879 -0.01267 0.02970  0.00530  74  GLY A N   
461  C  CA  . GLY A 74  ? 0.12928 0.17710 0.19661 -0.03588 0.01918  0.00809  74  GLY A CA  
462  C  C   . GLY A 74  ? 0.13164 0.16554 0.19947 -0.00563 0.00154  0.01370  74  GLY A C   
463  O  O   . GLY A 74  ? 0.16946 0.17907 0.21494 -0.00294 0.00447  0.02551  74  GLY A O   
464  N  N   . TRP A 75  ? 0.14424 0.17780 0.18614 0.02134  0.00048  0.01443  75  TRP A N   
465  C  CA  . TRP A 75  ? 0.16172 0.19602 0.20222 0.00222  -0.01284 -0.01913 75  TRP A CA  
466  C  C   . TRP A 75  ? 0.18211 0.17456 0.19934 -0.02061 -0.00772 -0.00105 75  TRP A C   
467  O  O   . TRP A 75  ? 0.16092 0.15813 0.20263 0.00095  -0.00186 -0.02137 75  TRP A O   
468  C  CB  . TRP A 75  ? 0.15517 0.17834 0.22327 -0.00328 -0.02177 0.00330  75  TRP A CB  
469  C  CG  . TRP A 75  ? 0.14258 0.17231 0.23488 0.00067  -0.00727 0.01480  75  TRP A CG  
470  C  CD1 . TRP A 75  ? 0.14504 0.20837 0.24180 0.01856  -0.01181 0.03281  75  TRP A CD1 
471  C  CD2 . TRP A 75  ? 0.11521 0.18842 0.24986 -0.00282 -0.01952 0.00224  75  TRP A CD2 
472  N  NE1 . TRP A 75  ? 0.14387 0.20331 0.25016 0.00515  -0.00667 0.01972  75  TRP A NE1 
473  C  CE2 . TRP A 75  ? 0.12816 0.19832 0.25825 -0.00602 -0.00637 -0.00080 75  TRP A CE2 
474  C  CE3 . TRP A 75  ? 0.11086 0.17276 0.26029 0.00704  -0.03150 -0.01661 75  TRP A CE3 
475  C  CZ2 . TRP A 75  ? 0.13780 0.20291 0.26639 -0.00405 0.00295  -0.00301 75  TRP A CZ2 
476  C  CZ3 . TRP A 75  ? 0.17620 0.18956 0.26414 0.01361  -0.02919 -0.00092 75  TRP A CZ3 
477  C  CH2 . TRP A 75  ? 0.17287 0.17897 0.26880 -0.00361 -0.01133 -0.00160 75  TRP A CH2 
478  N  N   . THR A 76  ? 0.16666 0.14765 0.18353 -0.00435 0.00431  -0.00317 76  THR A N   
479  C  CA  . THR A 76  ? 0.18856 0.14175 0.18327 0.00342  0.01335  -0.01011 76  THR A CA  
480  C  C   . THR A 76  ? 0.17666 0.14813 0.19251 -0.03768 -0.00818 0.00291  76  THR A C   
481  O  O   . THR A 76  ? 0.19723 0.17762 0.20857 -0.01173 -0.01988 0.01114  76  THR A O   
482  C  CB  . THR A 76  ? 0.16589 0.16377 0.18729 0.00414  -0.00011 -0.00325 76  THR A CB  
483  O  OG1 . THR A 76  ? 0.17016 0.18964 0.19073 -0.01207 -0.03595 0.00159  76  THR A OG1 
484  C  CG2 . THR A 76  ? 0.17368 0.22814 0.18954 0.02575  0.01704  0.00696  76  THR A CG2 
485  N  N   . VAL A 77  ? 0.18717 0.17363 0.17689 -0.00761 -0.02182 -0.00405 77  VAL A N   
486  C  CA  . VAL A 77  ? 0.18089 0.17391 0.18355 -0.00197 -0.02943 0.00018  77  VAL A CA  
487  C  C   . VAL A 77  ? 0.19451 0.20397 0.19805 -0.02925 -0.02134 -0.00564 77  VAL A C   
488  O  O   . VAL A 77  ? 0.20277 0.19023 0.20967 -0.02205 -0.01560 -0.03223 77  VAL A O   
489  C  CB  . VAL A 77  ? 0.15588 0.20672 0.19363 0.01335  -0.02724 0.01783  77  VAL A CB  
490  C  CG1 . VAL A 77  ? 0.19907 0.21420 0.19574 0.00804  -0.04213 0.01166  77  VAL A CG1 
491  C  CG2 . VAL A 77  ? 0.17255 0.22685 0.21331 0.01045  -0.00825 0.00496  77  VAL A CG2 
492  N  N   . ALA A 78  ? 0.18134 0.19168 0.19783 -0.01385 -0.02117 0.00080  78  ALA A N   
493  C  CA  . ALA A 78  ? 0.19487 0.19836 0.20153 0.00954  -0.04283 0.00465  78  ALA A CA  
494  C  C   . ALA A 78  ? 0.19396 0.19968 0.19933 -0.00968 -0.03356 0.00497  78  ALA A C   
495  O  O   . ALA A 78  ? 0.18682 0.21152 0.21222 -0.02367 -0.03622 0.01167  78  ALA A O   
496  C  CB  . ALA A 78  ? 0.23929 0.18142 0.20586 0.02243  -0.03764 0.00239  78  ALA A CB  
497  N  N   . TRP A 79  ? 0.21943 0.20065 0.18413 0.00723  -0.02625 -0.00224 79  TRP A N   
498  C  CA  . TRP A 79  ? 0.19307 0.19094 0.18623 0.00003  -0.02754 -0.00433 79  TRP A CA  
499  C  C   . TRP A 79  ? 0.23190 0.20334 0.20233 -0.00408 -0.02825 -0.01384 79  TRP A C   
500  O  O   . TRP A 79  ? 0.22151 0.20138 0.20976 -0.03144 -0.02799 -0.00843 79  TRP A O   
501  C  CB  . TRP A 79  ? 0.23133 0.18703 0.18461 -0.02889 -0.03479 -0.00563 79  TRP A CB  
502  C  CG  . TRP A 79  ? 0.19530 0.19490 0.19067 -0.02011 -0.03850 -0.00389 79  TRP A CG  
503  C  CD1 . TRP A 79  ? 0.19021 0.19370 0.19598 -0.01038 -0.02885 0.00532  79  TRP A CD1 
504  C  CD2 . TRP A 79  ? 0.17213 0.17620 0.19922 -0.00864 -0.04517 0.01099  79  TRP A CD2 
505  N  NE1 . TRP A 79  ? 0.19473 0.17411 0.20375 0.00255  -0.02025 0.00330  79  TRP A NE1 
506  C  CE2 . TRP A 79  ? 0.18560 0.16450 0.20667 0.00153  -0.02105 0.01048  79  TRP A CE2 
507  C  CE3 . TRP A 79  ? 0.20868 0.17677 0.20722 -0.02775 -0.03478 -0.00945 79  TRP A CE3 
508  C  CZ2 . TRP A 79  ? 0.17113 0.17793 0.21126 -0.00037 -0.02205 0.01516  79  TRP A CZ2 
509  C  CZ3 . TRP A 79  ? 0.21727 0.18750 0.21789 -0.03891 -0.03977 -0.00470 79  TRP A CZ3 
510  C  CH2 . TRP A 79  ? 0.16287 0.21384 0.21433 -0.02485 -0.05002 0.01738  79  TRP A CH2 
511  N  N   . LYS A 80  ? 0.23831 0.19918 0.20842 -0.04004 -0.03922 -0.02477 80  LYS A N   
512  C  CA  . LYS A 80  ? 0.21537 0.21192 0.21850 0.00023  -0.03262 -0.03523 80  LYS A CA  
513  C  C   . LYS A 80  ? 0.21726 0.23059 0.21662 -0.02288 -0.02995 -0.01027 80  LYS A C   
514  O  O   . LYS A 80  ? 0.23293 0.22107 0.20939 -0.01929 -0.01544 -0.01292 80  LYS A O   
515  C  CB  . LYS A 80  ? 0.25520 0.21947 0.22896 0.00767  -0.02564 -0.04177 80  LYS A CB  
516  C  CG  . LYS A 80  ? 0.30619 0.22824 0.24623 0.02793  -0.03603 -0.05147 80  LYS A CG  
517  C  CD  . LYS A 80  ? 0.36378 0.23428 0.26769 -0.01668 -0.02181 -0.06654 80  LYS A CD  
518  C  CE  . LYS A 80  ? 0.39414 0.26900 0.28885 -0.02731 -0.01739 -0.04910 80  LYS A CE  
519  N  NZ  . LYS A 80  ? 0.40167 0.32140 0.29992 -0.02959 -0.00909 -0.02682 80  LYS A NZ  
520  N  N   . ASN A 81  ? 0.23253 0.22528 0.21746 -0.02207 -0.04363 -0.01325 81  ASN A N   
521  C  CA  . ASN A 81  ? 0.22429 0.22516 0.22038 -0.00253 -0.04660 -0.00924 81  ASN A CA  
522  C  C   . ASN A 81  ? 0.23214 0.24253 0.23564 -0.03008 -0.06380 -0.01097 81  ASN A C   
523  O  O   . ASN A 81  ? 0.26975 0.27741 0.24791 -0.01729 -0.05857 -0.03432 81  ASN A O   
524  C  CB  . ASN A 81  ? 0.27175 0.22243 0.21334 -0.02600 -0.04543 -0.00152 81  ASN A CB  
525  C  CG  . ASN A 81  ? 0.24791 0.25227 0.21352 -0.03757 -0.04522 -0.00883 81  ASN A CG  
526  O  OD1 . ASN A 81  ? 0.27559 0.25060 0.21314 -0.01400 -0.04453 -0.02857 81  ASN A OD1 
527  N  ND2 . ASN A 81  ? 0.24581 0.25640 0.21109 -0.01779 -0.06840 -0.02007 81  ASN A ND2 
528  N  N   . ASN A 82  ? 0.24446 0.23998 0.24858 -0.06609 -0.10320 -0.00481 82  ASN A N   
529  C  CA  . ASN A 82  ? 0.29949 0.29358 0.27144 -0.11851 -0.11163 -0.00394 82  ASN A CA  
530  C  C   . ASN A 82  ? 0.33299 0.29661 0.26632 -0.08778 -0.10283 0.00035  82  ASN A C   
531  O  O   . ASN A 82  ? 0.37594 0.33256 0.26579 -0.05249 -0.10332 -0.00989 82  ASN A O   
532  C  CB  . ASN A 82  ? 0.39805 0.36186 0.30730 -0.13492 -0.09729 0.01950  82  ASN A CB  
533  C  CG  . ASN A 82  ? 0.51888 0.46271 0.34708 -0.12236 -0.06026 0.03428  82  ASN A CG  
534  O  OD1 . ASN A 82  ? 0.59784 0.49170 0.36704 -0.10766 -0.04522 0.03590  82  ASN A OD1 
535  N  ND2 . ASN A 82  ? 0.55698 0.51229 0.35832 -0.10077 -0.05399 0.03759  82  ASN A ND2 
536  N  N   . TYR A 83  ? 0.30310 0.25245 0.25733 -0.04844 -0.10113 0.02485  83  TYR A N   
537  C  CA  . TYR A 83  ? 0.28092 0.27231 0.25489 -0.02246 -0.09735 0.01847  83  TYR A CA  
538  C  C   . TYR A 83  ? 0.26184 0.29578 0.24551 -0.00734 -0.08084 0.01308  83  TYR A C   
539  O  O   . TYR A 83  ? 0.24902 0.33569 0.24816 -0.01278 -0.05944 0.03213  83  TYR A O   
540  C  CB  . TYR A 83  ? 0.26370 0.28555 0.27157 -0.01444 -0.10442 0.00742  83  TYR A CB  
541  C  CG  . TYR A 83  ? 0.24420 0.37066 0.29851 -0.00891 -0.09660 -0.00372 83  TYR A CG  
542  C  CD1 . TYR A 83  ? 0.25050 0.49738 0.30825 0.00010  -0.09977 -0.01402 83  TYR A CD1 
543  C  CD2 . TYR A 83  ? 0.22467 0.41787 0.31265 -0.01770 -0.09382 -0.00967 83  TYR A CD2 
544  C  CE1 . TYR A 83  ? 0.24849 0.59511 0.32147 0.02304  -0.09249 -0.02147 83  TYR A CE1 
545  C  CE2 . TYR A 83  ? 0.23008 0.55105 0.32368 0.00199  -0.08583 -0.01194 83  TYR A CE2 
546  C  CZ  . TYR A 83  ? 0.23760 0.63462 0.33440 0.03061  -0.07932 -0.02664 83  TYR A CZ  
547  O  OH  . TYR A 83  ? 0.25129 0.71549 0.35408 0.04473  -0.06681 -0.03741 83  TYR A OH  
548  N  N   . ARG A 84  ? 0.25933 0.27216 0.23355 -0.02884 -0.08083 0.00649  84  ARG A N   
549  C  CA  . ARG A 84  ? 0.23846 0.28167 0.23585 0.00018  -0.09702 -0.00986 84  ARG A CA  
550  C  C   . ARG A 84  ? 0.24661 0.27592 0.22648 -0.01556 -0.07461 -0.01228 84  ARG A C   
551  O  O   . ARG A 84  ? 0.25929 0.27350 0.22776 -0.01948 -0.06001 -0.00727 84  ARG A O   
552  C  CB  . ARG A 84  ? 0.32757 0.28999 0.25334 0.00158  -0.11276 0.00675  84  ARG A CB  
553  C  CG  . ARG A 84  ? 0.41202 0.32353 0.26544 -0.01729 -0.10457 -0.01660 84  ARG A CG  
554  C  CD  . ARG A 84  ? 0.44529 0.37909 0.26955 -0.02935 -0.07069 -0.00542 84  ARG A CD  
555  N  NE  . ARG A 84  ? 0.42983 0.43461 0.25584 -0.02331 -0.05993 0.01261  84  ARG A NE  
556  C  CZ  . ARG A 84  ? 0.40250 0.48972 0.25006 -0.05713 -0.03742 0.00597  84  ARG A CZ  
557  N  NH1 . ARG A 84  ? 0.36836 0.48932 0.24377 -0.06977 -0.04536 -0.02021 84  ARG A NH1 
558  N  NH2 . ARG A 84  ? 0.38481 0.52715 0.25336 -0.04475 -0.04407 0.01815  84  ARG A NH2 
559  N  N   . ASN A 85  ? 0.21971 0.26047 0.21862 0.00599  -0.06709 -0.01014 85  ASN A N   
560  C  CA  . ASN A 85  ? 0.23277 0.27159 0.21419 0.03131  -0.05256 -0.01083 85  ASN A CA  
561  C  C   . ASN A 85  ? 0.23627 0.29292 0.21460 0.00855  -0.03351 -0.00762 85  ASN A C   
562  O  O   . ASN A 85  ? 0.25231 0.30969 0.22341 -0.00309 -0.03501 -0.00372 85  ASN A O   
563  C  CB  . ASN A 85  ? 0.24196 0.23588 0.20826 0.03619  -0.03824 -0.00756 85  ASN A CB  
564  C  CG  . ASN A 85  ? 0.26576 0.21480 0.21515 0.01344  -0.03786 -0.01543 85  ASN A CG  
565  O  OD1 . ASN A 85  ? 0.26164 0.23128 0.21928 -0.01091 -0.02227 -0.01740 85  ASN A OD1 
566  N  ND2 . ASN A 85  ? 0.26547 0.23093 0.22348 0.00217  -0.02677 -0.04435 85  ASN A ND2 
567  N  N   . ALA A 86  ? 0.22469 0.24579 0.20392 -0.03284 -0.01353 -0.00187 86  ALA A N   
568  C  CA  . ALA A 86  ? 0.22552 0.23983 0.20794 0.02046  -0.02226 0.00529  86  ALA A CA  
569  C  C   . ALA A 86  ? 0.22902 0.23544 0.21886 0.00275  -0.02387 0.00402  86  ALA A C   
570  O  O   . ALA A 86  ? 0.24960 0.24697 0.23344 -0.02654 -0.03177 0.00868  86  ALA A O   
571  C  CB  . ALA A 86  ? 0.22785 0.25505 0.21679 0.01498  -0.00712 -0.00932 86  ALA A CB  
572  N  N   . HIS A 87  ? 0.24303 0.18467 0.21584 0.00755  -0.02479 -0.02598 87  HIS A N   
573  C  CA  . HIS A 87  ? 0.23143 0.22283 0.19877 0.03839  -0.01166 -0.04160 87  HIS A CA  
574  C  C   . HIS A 87  ? 0.21373 0.20820 0.19152 -0.01575 -0.01691 -0.02166 87  HIS A C   
575  O  O   . HIS A 87  ? 0.21675 0.23162 0.19084 0.00719  -0.01572 -0.01466 87  HIS A O   
576  C  CB  . HIS A 87  ? 0.23780 0.27911 0.19959 0.03473  0.00120  -0.04382 87  HIS A CB  
577  C  CG  . HIS A 87  ? 0.23328 0.31017 0.19845 -0.02470 -0.00594 -0.05831 87  HIS A CG  
578  N  ND1 . HIS A 87  ? 0.22950 0.30318 0.20043 -0.01707 -0.01857 -0.06419 87  HIS A ND1 
579  C  CD2 . HIS A 87  ? 0.27317 0.32423 0.19300 -0.02049 -0.00671 -0.06276 87  HIS A CD2 
580  C  CE1 . HIS A 87  ? 0.24188 0.29825 0.18571 -0.00798 -0.01524 -0.05752 87  HIS A CE1 
581  N  NE2 . HIS A 87  ? 0.27718 0.30590 0.18312 -0.01731 0.00441  -0.06391 87  HIS A NE2 
582  N  N   . SER A 88  ? 0.22100 0.21726 0.18432 -0.00225 -0.01642 -0.01614 88  SER A N   
583  C  CA  . SER A 88  ? 0.21115 0.18428 0.19444 -0.01676 -0.00476 -0.04639 88  SER A CA  
584  C  C   . SER A 88  ? 0.23347 0.17553 0.19679 -0.02847 -0.00556 -0.03257 88  SER A C   
585  O  O   . SER A 88  ? 0.22142 0.20613 0.20417 -0.03348 -0.00852 -0.01347 88  SER A O   
586  C  CB  . SER A 88  ? 0.20481 0.24331 0.21211 -0.00287 -0.02492 -0.02507 88  SER A CB  
587  O  OG  . SER A 88  ? 0.19789 0.23868 0.22574 -0.00093 -0.02139 -0.02233 88  SER A OG  
588  N  N   . ALA A 89  ? 0.20602 0.17936 0.18687 -0.00620 0.00256  -0.02181 89  ALA A N   
589  C  CA  . ALA A 89  ? 0.19058 0.15331 0.18467 -0.00647 -0.00690 -0.02452 89  ALA A CA  
590  C  C   . ALA A 89  ? 0.17365 0.16126 0.18563 -0.00096 -0.02327 -0.02359 89  ALA A C   
591  O  O   . ALA A 89  ? 0.17496 0.18842 0.19814 -0.02559 -0.01583 -0.02574 89  ALA A O   
592  C  CB  . ALA A 89  ? 0.20987 0.16209 0.19837 0.01748  -0.00333 -0.00765 89  ALA A CB  
593  N  N   . THR A 90  ? 0.15656 0.17169 0.17154 0.01541  -0.01218 -0.02184 90  THR A N   
594  C  CA  . THR A 90  ? 0.17076 0.15041 0.17347 0.00828  -0.00378 0.00454  90  THR A CA  
595  C  C   . THR A 90  ? 0.14442 0.16643 0.17026 -0.01474 -0.01758 0.00328  90  THR A C   
596  O  O   . THR A 90  ? 0.15949 0.16445 0.17614 -0.00666 -0.01352 0.00537  90  THR A O   
597  C  CB  . THR A 90  ? 0.17026 0.15578 0.18147 -0.01309 0.00498  0.00101  90  THR A CB  
598  O  OG1 . THR A 90  ? 0.17655 0.17740 0.17608 -0.02611 0.00421  -0.01072 90  THR A OG1 
599  C  CG2 . THR A 90  ? 0.20180 0.18391 0.18499 0.02307  0.00711  0.00975  90  THR A CG2 
600  N  N   . THR A 91  ? 0.15319 0.16510 0.16547 -0.00659 -0.01002 -0.01427 91  THR A N   
601  C  CA  . THR A 91  ? 0.14366 0.15171 0.16859 -0.00700 -0.01332 -0.00689 91  THR A CA  
602  C  C   . THR A 91  ? 0.13213 0.14916 0.18062 0.00151  -0.00936 -0.00698 91  THR A C   
603  O  O   . THR A 91  ? 0.18648 0.15042 0.20108 0.00340  0.00790  -0.00812 91  THR A O   
604  C  CB  . THR A 91  ? 0.15181 0.17200 0.19112 -0.01093 -0.02636 -0.00194 91  THR A CB  
605  O  OG1 . THR A 91  ? 0.16400 0.19067 0.20356 0.00419  -0.03151 -0.00934 91  THR A OG1 
606  C  CG2 . THR A 91  ? 0.21878 0.13809 0.20968 -0.01536 -0.00243 0.00425  91  THR A CG2 
607  N  N   . TRP A 92  ? 0.14880 0.15514 0.18012 0.03323  -0.00645 -0.00480 92  TRP A N   
608  C  CA  . TRP A 92  ? 0.14266 0.14280 0.18251 0.02434  -0.00153 0.01250  92  TRP A CA  
609  C  C   . TRP A 92  ? 0.12657 0.16470 0.18353 0.01575  -0.01499 0.01578  92  TRP A C   
610  O  O   . TRP A 92  ? 0.17351 0.17222 0.18690 -0.01071 -0.01137 0.01847  92  TRP A O   
611  C  CB  . TRP A 92  ? 0.11314 0.14929 0.20040 0.00605  -0.01569 0.00983  92  TRP A CB  
612  C  CG  . TRP A 92  ? 0.12886 0.15882 0.20491 -0.00128 -0.01133 0.01760  92  TRP A CG  
613  C  CD1 . TRP A 92  ? 0.12349 0.18133 0.20611 0.00665  -0.02359 0.02937  92  TRP A CD1 
614  C  CD2 . TRP A 92  ? 0.14004 0.15845 0.20029 -0.00758 0.00208  -0.01190 92  TRP A CD2 
615  N  NE1 . TRP A 92  ? 0.13253 0.20397 0.20233 0.00629  -0.02341 -0.00081 92  TRP A NE1 
616  C  CE2 . TRP A 92  ? 0.14217 0.18319 0.19586 0.00162  -0.00444 -0.01435 92  TRP A CE2 
617  C  CE3 . TRP A 92  ? 0.13511 0.18384 0.19970 -0.01469 0.00042  -0.03883 92  TRP A CE3 
618  C  CZ2 . TRP A 92  ? 0.17634 0.22349 0.19367 0.01662  -0.00508 -0.01500 92  TRP A CZ2 
619  C  CZ3 . TRP A 92  ? 0.14192 0.21173 0.19404 -0.03214 -0.00199 -0.02139 92  TRP A CZ3 
620  C  CH2 . TRP A 92  ? 0.17638 0.23587 0.19323 0.02220  -0.02242 -0.01194 92  TRP A CH2 
621  N  N   . SER A 93  ? 0.14417 0.17710 0.18461 0.01695  -0.03244 -0.00533 93  SER A N   
622  C  CA  . SER A 93  ? 0.17522 0.16063 0.19786 0.00251  -0.02845 -0.00516 93  SER A CA  
623  C  C   . SER A 93  ? 0.16311 0.16122 0.20494 0.00186  0.01278  -0.00801 93  SER A C   
624  O  O   . SER A 93  ? 0.16786 0.18071 0.21596 -0.00337 0.00551  0.01168  93  SER A O   
625  C  CB  . SER A 93  ? 0.13754 0.18259 0.19047 0.02788  -0.04610 0.00594  93  SER A CB  
626  O  OG  . SER A 93  ? 0.17569 0.21518 0.18487 0.01636  -0.02610 -0.00467 93  SER A OG  
627  N  N   . GLY A 94  ? 0.14603 0.18252 0.20508 0.01797  0.01342  -0.00526 94  GLY A N   
628  C  CA  . GLY A 94  ? 0.14949 0.20995 0.20735 0.03804  0.02894  -0.01077 94  GLY A CA  
629  C  C   . GLY A 94  ? 0.14628 0.20106 0.21487 0.04142  0.01569  -0.00866 94  GLY A C   
630  O  O   . GLY A 94  ? 0.19570 0.20554 0.22018 0.01028  0.01245  0.00435  94  GLY A O   
631  N  N   . GLN A 95  ? 0.13923 0.22419 0.22216 0.04608  0.03896  -0.00451 95  GLN A N   
632  C  CA  . GLN A 95  ? 0.15009 0.21863 0.23053 0.04059  0.03828  0.00074  95  GLN A CA  
633  C  C   . GLN A 95  ? 0.17923 0.17426 0.23882 0.03977  0.03631  0.02549  95  GLN A C   
634  O  O   . GLN A 95  ? 0.17750 0.18965 0.24048 0.03015  0.01540  0.02051  95  GLN A O   
635  C  CB  . GLN A 95  ? 0.20685 0.24506 0.23591 0.00636  0.04039  0.00089  95  GLN A CB  
636  C  CG  . GLN A 95  ? 0.22551 0.24887 0.24008 -0.01490 0.04629  -0.00111 95  GLN A CG  
637  C  CD  . GLN A 95  ? 0.20778 0.23351 0.25241 0.00057  0.04665  -0.02902 95  GLN A CD  
638  O  OE1 . GLN A 95  ? 0.19684 0.23700 0.25239 -0.00149 0.04734  -0.01727 95  GLN A OE1 
639  N  NE2 . GLN A 95  ? 0.21052 0.25100 0.26088 -0.03363 0.02542  -0.03644 95  GLN A NE2 
640  N  N   . TYR A 96  ? 0.18175 0.20214 0.24720 0.01457  0.04008  0.01828  96  TYR A N   
641  C  CA  . TYR A 96  ? 0.18593 0.19615 0.26238 0.02378  0.02963  -0.00005 96  TYR A CA  
642  C  C   . TYR A 96  ? 0.21588 0.22151 0.27612 0.05317  0.02343  -0.00509 96  TYR A C   
643  O  O   . TYR A 96  ? 0.19711 0.25927 0.26376 0.06057  0.02145  0.00093  96  TYR A O   
644  C  CB  . TYR A 96  ? 0.16293 0.26841 0.26854 0.00038  0.03139  0.00910  96  TYR A CB  
645  C  CG  . TYR A 96  ? 0.16808 0.28930 0.27944 0.00116  0.04325  0.00720  96  TYR A CG  
646  C  CD1 . TYR A 96  ? 0.16540 0.28410 0.29340 -0.00761 0.03456  -0.00772 96  TYR A CD1 
647  C  CD2 . TYR A 96  ? 0.19498 0.34572 0.28590 0.00400  0.05775  0.01429  96  TYR A CD2 
648  C  CE1 . TYR A 96  ? 0.18244 0.33937 0.30011 0.00025  0.07044  -0.01468 96  TYR A CE1 
649  C  CE2 . TYR A 96  ? 0.20440 0.39051 0.29777 0.00931  0.06415  0.00183  96  TYR A CE2 
650  C  CZ  . TYR A 96  ? 0.15860 0.38537 0.31167 -0.00027 0.07815  -0.01764 96  TYR A CZ  
651  O  OH  . TYR A 96  ? 0.18695 0.45681 0.33824 0.00917  0.05898  -0.03129 96  TYR A OH  
652  N  N   . VAL A 97  ? 0.21152 0.22625 0.30540 0.05057  0.01724  -0.04328 97  VAL A N   
653  C  CA  . VAL A 97  ? 0.24100 0.25393 0.33957 0.06941  0.02023  -0.03986 97  VAL A CA  
654  C  C   . VAL A 97  ? 0.23946 0.31164 0.36500 0.07757  0.04470  -0.02327 97  VAL A C   
655  O  O   . VAL A 97  ? 0.23672 0.37893 0.35927 0.09503  0.04179  -0.00288 97  VAL A O   
656  C  CB  . VAL A 97  ? 0.27603 0.29114 0.34736 0.04909  0.00536  -0.07173 97  VAL A CB  
657  C  CG1 . VAL A 97  ? 0.34462 0.31547 0.34626 0.04357  -0.02420 -0.09208 97  VAL A CG1 
658  C  CG2 . VAL A 97  ? 0.26084 0.33150 0.35330 0.01112  -0.00591 -0.06109 97  VAL A CG2 
659  N  N   . GLY A 98  ? 0.25670 0.33129 0.40100 0.07412  0.07051  -0.00825 98  GLY A N   
660  C  CA  . GLY A 98  ? 0.28127 0.38760 0.44158 0.06579  0.08546  -0.01223 98  GLY A CA  
661  C  C   . GLY A 98  ? 0.37640 0.43347 0.47912 0.12720  0.09115  -0.03116 98  GLY A C   
662  O  O   . GLY A 98  ? 0.41948 0.39671 0.48447 0.13111  0.08346  -0.02656 98  GLY A O   
663  N  N   . GLY A 99  ? 0.44918 0.51218 0.50941 0.16154  0.09682  -0.04741 99  GLY A N   
664  C  CA  . GLY A 99  ? 0.46331 0.58947 0.53248 0.22388  0.11040  -0.05808 99  GLY A CA  
665  C  C   . GLY A 99  ? 0.49265 0.66252 0.55087 0.24032  0.12744  -0.05735 99  GLY A C   
666  O  O   . GLY A 99  ? 0.50386 0.72930 0.55747 0.23808  0.13556  -0.05342 99  GLY A O   
667  N  N   . ALA A 100 ? 0.50426 0.64196 0.56120 0.26039  0.13451  -0.05205 100 ALA A N   
668  C  CA  . ALA A 100 ? 0.52470 0.60316 0.56940 0.27461  0.12150  -0.03855 100 ALA A CA  
669  C  C   . ALA A 100 ? 0.57123 0.59022 0.57425 0.24504  0.10626  -0.01762 100 ALA A C   
670  O  O   . ALA A 100 ? 0.61748 0.60527 0.58167 0.24224  0.10871  -0.01506 100 ALA A O   
671  C  CB  . ALA A 100 ? 0.52575 0.58763 0.57148 0.29522  0.11343  -0.04377 100 ALA A CB  
672  N  N   . GLN A 101 ? 0.51671 0.54797 0.56961 0.26062  0.09847  -0.00501 101 GLN A N   
673  C  CA  . GLN A 101 ? 0.51449 0.53267 0.56315 0.21653  0.08424  0.00520  101 GLN A CA  
674  C  C   . GLN A 101 ? 0.40312 0.42334 0.51985 0.19564  0.07538  -0.00670 101 GLN A C   
675  O  O   . GLN A 101 ? 0.42968 0.40175 0.52315 0.10586  0.06919  -0.00531 101 GLN A O   
676  C  CB  . GLN A 101 ? 0.61713 0.63723 0.59650 0.17105  0.08048  0.02449  101 GLN A CB  
677  C  CG  . GLN A 101 ? 0.71399 0.77026 0.62395 0.10723  0.07360  0.04154  101 GLN A CG  
678  C  CD  . GLN A 101 ? 0.79295 0.87901 0.64403 0.04911  0.06844  0.05370  101 GLN A CD  
679  O  OE1 . GLN A 101 ? 0.83105 0.92499 0.65204 0.03533  0.06651  0.05622  101 GLN A OE1 
680  N  NE2 . GLN A 101 ? 0.81301 0.90827 0.64914 0.02307  0.06932  0.05916  101 GLN A NE2 
681  N  N   . ALA A 102 ? 0.33163 0.38393 0.47091 0.18783  0.05440  -0.00877 102 ALA A N   
682  C  CA  . ALA A 102 ? 0.25415 0.32303 0.42139 0.14957  0.05177  -0.01676 102 ALA A CA  
683  C  C   . ALA A 102 ? 0.23521 0.29783 0.37552 0.11289  0.02354  -0.02043 102 ALA A C   
684  O  O   . ALA A 102 ? 0.26134 0.31859 0.36800 0.10560  0.01533  -0.03310 102 ALA A O   
685  C  CB  . ALA A 102 ? 0.29086 0.31848 0.42170 0.05246  0.05765  -0.02504 102 ALA A CB  
686  N  N   . ARG A 103 ? 0.17054 0.25390 0.34051 0.08208  0.01958  -0.03166 103 ARG A N   
687  C  CA  . ARG A 103 ? 0.20812 0.20423 0.32178 0.07303  0.02071  -0.02754 103 ARG A CA  
688  C  C   . ARG A 103 ? 0.19512 0.23800 0.28494 0.04456  0.01352  -0.02901 103 ARG A C   
689  O  O   . ARG A 103 ? 0.18419 0.28856 0.27024 0.03716  0.01488  -0.01182 103 ARG A O   
690  C  CB  . ARG A 103 ? 0.35872 0.24882 0.34947 0.04606  0.00098  -0.03128 103 ARG A CB  
691  C  CG  . ARG A 103 ? 0.45356 0.28142 0.36523 0.07016  -0.00713 -0.02491 103 ARG A CG  
692  C  CD  . ARG A 103 ? 0.50570 0.28824 0.37603 0.08789  -0.01885 -0.01611 103 ARG A CD  
693  N  NE  . ARG A 103 ? 0.55149 0.28766 0.38619 0.09815  -0.03818 -0.01516 103 ARG A NE  
694  C  CZ  . ARG A 103 ? 0.58232 0.31115 0.39383 0.08153  -0.06716 -0.01766 103 ARG A CZ  
695  N  NH1 . ARG A 103 ? 0.60216 0.31916 0.39591 0.10358  -0.08073 -0.02220 103 ARG A NH1 
696  N  NH2 . ARG A 103 ? 0.59872 0.31118 0.39686 0.02465  -0.07765 -0.01404 103 ARG A NH2 
697  N  N   . ILE A 104 ? 0.18106 0.21980 0.26851 0.03537  0.01827  -0.02981 104 ILE A N   
698  C  CA  . ILE A 104 ? 0.17248 0.19972 0.26625 0.02847  0.02841  -0.00299 104 ILE A CA  
699  C  C   . ILE A 104 ? 0.16413 0.19655 0.25201 0.01672  0.00886  0.00338  104 ILE A C   
700  O  O   . ILE A 104 ? 0.18804 0.20415 0.24816 0.02703  -0.00314 0.00510  104 ILE A O   
701  C  CB  . ILE A 104 ? 0.14127 0.22121 0.27790 0.00572  0.02391  0.00032  104 ILE A CB  
702  C  CG1 . ILE A 104 ? 0.19239 0.23019 0.28571 0.00740  0.00620  -0.02005 104 ILE A CG1 
703  C  CG2 . ILE A 104 ? 0.16849 0.21164 0.28633 0.01530  0.02598  0.01513  104 ILE A CG2 
704  C  CD1 . ILE A 104 ? 0.21554 0.22911 0.29302 -0.00294 -0.00012 -0.01833 104 ILE A CD1 
705  N  N   . ASN A 105 ? 0.15930 0.17135 0.23904 0.00926  0.01509  0.00243  105 ASN A N   
706  C  CA  . ASN A 105 ? 0.15534 0.18527 0.22741 0.05669  -0.00420 -0.02473 105 ASN A CA  
707  C  C   . ASN A 105 ? 0.14496 0.20822 0.21415 0.04052  -0.01305 -0.01551 105 ASN A C   
708  O  O   . ASN A 105 ? 0.17709 0.21486 0.21200 0.02553  -0.00454 0.02163  105 ASN A O   
709  C  CB  . ASN A 105 ? 0.22684 0.20546 0.23742 0.04959  -0.01220 -0.02603 105 ASN A CB  
710  C  CG  . ASN A 105 ? 0.26665 0.25899 0.25477 0.07459  -0.02559 -0.03486 105 ASN A CG  
711  O  OD1 . ASN A 105 ? 0.30419 0.26983 0.26514 0.08827  -0.01141 -0.02730 105 ASN A OD1 
712  N  ND2 . ASN A 105 ? 0.30674 0.30445 0.25936 0.06709  -0.02003 -0.03949 105 ASN A ND2 
713  N  N   . THR A 106 ? 0.15761 0.18263 0.21008 0.01145  0.01084  -0.02264 106 THR A N   
714  C  CA  A THR A 106 ? 0.14183 0.18230 0.21008 0.02646  -0.00163 -0.00132 106 THR A CA  
715  C  CA  B THR A 106 ? 0.16557 0.17939 0.20860 0.01334  0.00654  -0.01673 106 THR A CA  
716  C  C   . THR A 106 ? 0.17226 0.16811 0.20910 0.01459  0.00325  -0.00844 106 THR A C   
717  O  O   . THR A 106 ? 0.15840 0.15785 0.21975 0.01265  0.00660  0.00204  106 THR A O   
718  C  CB  A THR A 106 ? 0.14782 0.18385 0.21318 -0.01381 -0.00168 0.00836  106 THR A CB  
719  C  CB  B THR A 106 ? 0.16320 0.18084 0.20513 0.01366  0.00729  -0.01710 106 THR A CB  
720  O  OG1 A THR A 106 ? 0.16496 0.17611 0.20777 0.01042  -0.00751 0.01155  106 THR A OG1 
721  O  OG1 B THR A 106 ? 0.16190 0.18123 0.20383 0.01199  0.00762  -0.01838 106 THR A OG1 
722  C  CG2 A THR A 106 ? 0.12626 0.24603 0.22587 -0.00469 0.01447  0.00372  106 THR A CG2 
723  C  CG2 B THR A 106 ? 0.16229 0.18056 0.20355 0.01599  0.00768  -0.01701 106 THR A CG2 
724  N  N   . GLN A 107 ? 0.13911 0.15103 0.20490 0.01523  0.00169  -0.00662 107 GLN A N   
725  C  CA  . GLN A 107 ? 0.11965 0.17638 0.20773 -0.00959 -0.00293 -0.04020 107 GLN A CA  
726  C  C   . GLN A 107 ? 0.13681 0.14227 0.20317 0.01274  -0.00681 -0.01980 107 GLN A C   
727  O  O   . GLN A 107 ? 0.19963 0.15588 0.20026 0.00415  0.01174  -0.00440 107 GLN A O   
728  C  CB  . GLN A 107 ? 0.14927 0.23710 0.21068 -0.03358 0.00666  -0.06694 107 GLN A CB  
729  C  CG  A GLN A 107 ? 0.17388 0.24238 0.20236 -0.02358 0.01521  -0.06574 107 GLN A CG  
730  C  CG  B GLN A 107 ? 0.19121 0.26936 0.21406 -0.01032 -0.00167 -0.09620 107 GLN A CG  
731  C  CD  A GLN A 107 ? 0.15171 0.22529 0.18676 -0.01932 0.01870  -0.04408 107 GLN A CD  
732  C  CD  B GLN A 107 ? 0.21968 0.30927 0.21565 0.01148  -0.01473 -0.11851 107 GLN A CD  
733  O  OE1 A GLN A 107 ? 0.21363 0.25343 0.19742 -0.06414 -0.01203 -0.05893 107 GLN A OE1 
734  O  OE1 B GLN A 107 ? 0.21951 0.40437 0.21778 0.03292  -0.02916 -0.13112 107 GLN A OE1 
735  N  NE2 A GLN A 107 ? 0.17464 0.18218 0.16626 0.00974  0.02403  -0.01301 107 GLN A NE2 
736  N  NE2 B GLN A 107 ? 0.26353 0.24747 0.21322 -0.01421 -0.01333 -0.12981 107 GLN A NE2 
737  N  N   . TRP A 108 ? 0.15467 0.14718 0.19596 0.01242  0.00631  -0.01777 108 TRP A N   
738  C  CA  . TRP A 108 ? 0.13305 0.16872 0.18196 0.02963  -0.01429 -0.01205 108 TRP A CA  
739  C  C   . TRP A 108 ? 0.11544 0.18820 0.18598 -0.01232 -0.01198 -0.00753 108 TRP A C   
740  O  O   . TRP A 108 ? 0.15944 0.16669 0.18841 -0.01996 -0.00540 -0.01209 108 TRP A O   
741  C  CB  . TRP A 108 ? 0.14696 0.16453 0.18347 0.00708  -0.02129 0.01762  108 TRP A CB  
742  C  CG  . TRP A 108 ? 0.13166 0.15283 0.18949 0.01000  -0.00338 0.00555  108 TRP A CG  
743  C  CD1 . TRP A 108 ? 0.17363 0.15937 0.18765 0.00482  -0.01595 -0.00438 108 TRP A CD1 
744  C  CD2 . TRP A 108 ? 0.14415 0.15719 0.18840 0.01473  -0.01394 -0.00544 108 TRP A CD2 
745  N  NE1 . TRP A 108 ? 0.18821 0.17361 0.18154 0.00883  -0.02186 -0.00002 108 TRP A NE1 
746  C  CE2 . TRP A 108 ? 0.17933 0.17323 0.18487 0.00299  -0.01671 0.01005  108 TRP A CE2 
747  C  CE3 . TRP A 108 ? 0.15922 0.17810 0.19173 -0.03051 0.01368  -0.01528 108 TRP A CE3 
748  C  CZ2 . TRP A 108 ? 0.16774 0.16362 0.18404 -0.00418 -0.02339 -0.00233 108 TRP A CZ2 
749  C  CZ3 . TRP A 108 ? 0.15840 0.15104 0.18772 -0.00338 -0.00695 0.00109  108 TRP A CZ3 
750  C  CH2 . TRP A 108 ? 0.15353 0.18427 0.18809 0.02554  -0.01798 -0.00072 108 TRP A CH2 
751  N  N   . LEU A 109 ? 0.16261 0.13189 0.18761 0.02657  -0.01317 -0.00490 109 LEU A N   
752  C  CA  . LEU A 109 ? 0.13088 0.17468 0.18299 0.02694  -0.02678 -0.00297 109 LEU A CA  
753  C  C   . LEU A 109 ? 0.16396 0.15131 0.19401 0.00750  -0.00947 -0.00357 109 LEU A C   
754  O  O   . LEU A 109 ? 0.16591 0.19320 0.20094 -0.02768 -0.00148 0.00870  109 LEU A O   
755  C  CB  . LEU A 109 ? 0.17126 0.16379 0.18464 0.01030  -0.03625 -0.01545 109 LEU A CB  
756  C  CG  . LEU A 109 ? 0.15405 0.18667 0.17771 -0.00938 -0.03637 -0.00149 109 LEU A CG  
757  C  CD1 . LEU A 109 ? 0.19327 0.19475 0.17885 0.07041  -0.03469 0.00664  109 LEU A CD1 
758  C  CD2 . LEU A 109 ? 0.14476 0.18434 0.19420 -0.00692 -0.02699 -0.01069 109 LEU A CD2 
759  N  N   . LEU A 110 ? 0.16355 0.14019 0.19138 0.00733  -0.01610 -0.01559 110 LEU A N   
760  C  CA  A LEU A 110 ? 0.16544 0.16458 0.19496 0.02846  -0.00917 -0.00681 110 LEU A CA  
761  C  CA  B LEU A 110 ? 0.16154 0.16115 0.19144 0.04789  -0.00437 -0.01384 110 LEU A CA  
762  C  C   . LEU A 110 ? 0.15340 0.16716 0.20153 0.02224  0.00813  -0.00478 110 LEU A C   
763  O  O   . LEU A 110 ? 0.15387 0.17676 0.22110 -0.00510 0.01801  -0.01129 110 LEU A O   
764  C  CB  A LEU A 110 ? 0.20511 0.19505 0.19950 -0.00498 -0.00859 0.01644  110 LEU A CB  
765  C  CB  B LEU A 110 ? 0.19805 0.18050 0.18852 0.05073  0.00378  -0.00456 110 LEU A CB  
766  C  CG  A LEU A 110 ? 0.21645 0.22042 0.20599 -0.00285 0.00075  0.02799  110 LEU A CG  
767  C  CG  B LEU A 110 ? 0.20650 0.18566 0.18828 0.02166  0.02019  0.00598  110 LEU A CG  
768  C  CD1 A LEU A 110 ? 0.21026 0.22609 0.20937 -0.01025 -0.01138 0.04334  110 LEU A CD1 
769  C  CD1 B LEU A 110 ? 0.22127 0.18275 0.18504 -0.03422 0.02631  0.01088  110 LEU A CD1 
770  C  CD2 A LEU A 110 ? 0.21110 0.23203 0.20367 0.00240  0.01197  0.04113  110 LEU A CD2 
771  C  CD2 B LEU A 110 ? 0.18719 0.19245 0.19157 0.00424  0.00995  0.01385  110 LEU A CD2 
772  N  N   . THR A 111 ? 0.14384 0.19370 0.19999 0.03587  0.01094  -0.00248 111 THR A N   
773  C  CA  . THR A 111 ? 0.16490 0.18611 0.20164 0.01208  -0.01845 -0.00927 111 THR A CA  
774  C  C   . THR A 111 ? 0.16416 0.18020 0.19948 -0.00318 -0.00836 -0.02530 111 THR A C   
775  O  O   . THR A 111 ? 0.16721 0.20563 0.20529 -0.01765 0.00890  -0.02878 111 THR A O   
776  C  CB  . THR A 111 ? 0.17293 0.19499 0.21172 0.02066  -0.02457 -0.00743 111 THR A CB  
777  O  OG1 . THR A 111 ? 0.20467 0.15801 0.21528 0.00885  -0.02145 0.00009  111 THR A OG1 
778  C  CG2 . THR A 111 ? 0.15566 0.20955 0.21022 0.03172  -0.02142 -0.01086 111 THR A CG2 
779  N  N   . ALA A 112 ? 0.16624 0.18106 0.18873 0.01505  -0.01615 -0.03105 112 ALA A N   
780  C  CA  . ALA A 112 ? 0.20865 0.19950 0.19286 -0.00459 -0.00497 -0.04292 112 ALA A CA  
781  C  C   . ALA A 112 ? 0.19080 0.20420 0.20700 -0.01126 -0.00746 -0.05418 112 ALA A C   
782  O  O   . ALA A 112 ? 0.19172 0.26258 0.21713 0.00987  -0.02444 -0.05956 112 ALA A O   
783  C  CB  . ALA A 112 ? 0.25556 0.20912 0.18908 0.01923  0.00869  -0.02492 112 ALA A CB  
784  N  N   . GLY A 113 ? 0.19733 0.22185 0.21195 -0.00589 0.00294  -0.05345 113 GLY A N   
785  C  CA  . GLY A 113 ? 0.22169 0.24547 0.22027 0.02024  0.03215  -0.05070 113 GLY A CA  
786  C  C   . GLY A 113 ? 0.22440 0.27587 0.22395 0.06447  0.03425  -0.04427 113 GLY A C   
787  O  O   . GLY A 113 ? 0.29460 0.33828 0.21807 0.06168  0.02327  -0.02731 113 GLY A O   
788  N  N   . THR A 114 ? 0.22016 0.24998 0.23778 0.02862  0.04899  -0.04843 114 THR A N   
789  C  CA  . THR A 114 ? 0.22440 0.23448 0.24741 0.02394  0.06496  -0.05408 114 THR A CA  
790  C  C   . THR A 114 ? 0.24076 0.23128 0.26581 -0.01422 0.07310  -0.05682 114 THR A C   
791  O  O   . THR A 114 ? 0.27613 0.23348 0.27444 0.00816  0.04988  -0.04347 114 THR A O   
792  C  CB  . THR A 114 ? 0.25233 0.24139 0.24451 0.00045  0.03260  -0.04727 114 THR A CB  
793  O  OG1 . THR A 114 ? 0.24739 0.23134 0.23853 0.00485  0.03390  -0.05236 114 THR A OG1 
794  C  CG2 . THR A 114 ? 0.24756 0.23102 0.24493 0.03651  0.03584  -0.04719 114 THR A CG2 
795  N  N   . THR A 115 ? 0.27899 0.25742 0.28409 -0.00976 0.09892  -0.06530 115 THR A N   
796  C  CA  . THR A 115 ? 0.27353 0.25491 0.31085 -0.00208 0.08898  -0.05253 115 THR A CA  
797  C  C   . THR A 115 ? 0.26074 0.24307 0.33519 0.01598  0.05691  -0.04718 115 THR A C   
798  O  O   . THR A 115 ? 0.26250 0.21839 0.33230 0.01998  0.05186  -0.05927 115 THR A O   
799  C  CB  . THR A 115 ? 0.31660 0.29865 0.31583 -0.01605 0.09659  -0.07341 115 THR A CB  
800  O  OG1 . THR A 115 ? 0.36558 0.28611 0.32333 -0.01507 0.10365  -0.05632 115 THR A OG1 
801  C  CG2 . THR A 115 ? 0.34541 0.36048 0.31056 -0.02106 0.08996  -0.07866 115 THR A CG2 
802  N  N   . GLU A 116 ? 0.27422 0.28154 0.36122 0.05138  0.03787  -0.02035 116 GLU A N   
803  C  CA  . GLU A 116 ? 0.30496 0.25375 0.38495 0.05708  0.03016  -0.00858 116 GLU A CA  
804  C  C   . GLU A 116 ? 0.26406 0.26684 0.38062 0.01248  0.05180  -0.04276 116 GLU A C   
805  O  O   . GLU A 116 ? 0.23803 0.31141 0.38504 0.01391  0.04999  -0.05880 116 GLU A O   
806  C  CB  . GLU A 116 ? 0.39459 0.28138 0.40787 0.06033  0.03109  0.02268  116 GLU A CB  
807  C  CG  . GLU A 116 ? 0.49045 0.33953 0.42589 0.07886  0.03235  0.04353  116 GLU A CG  
808  C  CD  . GLU A 116 ? 0.54467 0.44173 0.44033 0.07696  0.04647  0.05396  116 GLU A CD  
809  O  OE1 . GLU A 116 ? 0.56033 0.47718 0.44435 0.06946  0.04489  0.05116  116 GLU A OE1 
810  O  OE2 . GLU A 116 ? 0.56388 0.48643 0.44645 0.08850  0.05862  0.06362  116 GLU A OE2 
811  N  N   . ALA A 117 ? 0.27064 0.27707 0.37415 0.01383  0.07948  -0.05432 117 ALA A N   
812  C  CA  . ALA A 117 ? 0.31302 0.28392 0.36067 -0.00956 0.09747  -0.06704 117 ALA A CA  
813  C  C   . ALA A 117 ? 0.29018 0.29520 0.34985 -0.01329 0.09546  -0.06751 117 ALA A C   
814  O  O   . ALA A 117 ? 0.28384 0.32428 0.36739 -0.04229 0.08843  -0.06303 117 ALA A O   
815  C  CB  . ALA A 117 ? 0.34125 0.31413 0.36449 -0.01740 0.11759  -0.05829 117 ALA A CB  
816  N  N   . ASN A 118 ? 0.29320 0.27700 0.32210 0.00312  0.10463  -0.05712 118 ASN A N   
817  C  CA  . ASN A 118 ? 0.30700 0.28100 0.28560 0.00232  0.12039  -0.03804 118 ASN A CA  
818  C  C   . ASN A 118 ? 0.26017 0.25490 0.26102 -0.00499 0.08644  -0.02070 118 ASN A C   
819  O  O   . ASN A 118 ? 0.25592 0.21151 0.24960 0.00832  0.06840  -0.03303 118 ASN A O   
820  C  CB  . ASN A 118 ? 0.37527 0.32312 0.27751 -0.02317 0.13990  -0.02187 118 ASN A CB  
821  C  CG  . ASN A 118 ? 0.47116 0.32748 0.27961 -0.04760 0.14732  -0.03210 118 ASN A CG  
822  O  OD1 . ASN A 118 ? 0.48669 0.33878 0.28295 -0.08441 0.15672  -0.04965 118 ASN A OD1 
823  N  ND2 . ASN A 118 ? 0.57360 0.33847 0.27976 -0.03242 0.12876  -0.02222 118 ASN A ND2 
824  N  N   . ALA A 119 ? 0.23740 0.20079 0.25053 -0.01521 0.06433  -0.00710 119 ALA A N   
825  C  CA  . ALA A 119 ? 0.23275 0.16863 0.24173 0.00685  0.04334  -0.01608 119 ALA A CA  
826  C  C   . ALA A 119 ? 0.22317 0.20120 0.24253 -0.00015 0.01991  -0.03407 119 ALA A C   
827  O  O   . ALA A 119 ? 0.20502 0.23089 0.23610 0.01477  0.01025  -0.03326 119 ALA A O   
828  C  CB  . ALA A 119 ? 0.29189 0.21929 0.24091 0.01523  0.02398  0.00157  119 ALA A CB  
829  N  N   . TRP A 120 ? 0.21658 0.21781 0.25129 -0.00148 0.00924  -0.02475 120 TRP A N   
830  C  CA  . TRP A 120 ? 0.18038 0.22473 0.24910 -0.00939 0.00037  -0.02821 120 TRP A CA  
831  C  C   . TRP A 120 ? 0.18850 0.20800 0.23931 -0.01067 0.01210  -0.03646 120 TRP A C   
832  O  O   . TRP A 120 ? 0.22818 0.22091 0.22887 -0.04246 0.01201  -0.04991 120 TRP A O   
833  C  CB  . TRP A 120 ? 0.19318 0.27293 0.25258 -0.01883 0.00728  -0.03251 120 TRP A CB  
834  C  CG  . TRP A 120 ? 0.21617 0.24329 0.26025 -0.02722 0.02829  -0.04838 120 TRP A CG  
835  C  CD1 . TRP A 120 ? 0.22504 0.24637 0.26850 -0.03079 0.05755  -0.03904 120 TRP A CD1 
836  C  CD2 . TRP A 120 ? 0.21887 0.21932 0.27113 -0.02546 0.05111  -0.04228 120 TRP A CD2 
837  N  NE1 . TRP A 120 ? 0.25834 0.22393 0.27541 -0.04637 0.05030  -0.03906 120 TRP A NE1 
838  C  CE2 . TRP A 120 ? 0.27286 0.22611 0.27867 -0.08269 0.03660  -0.03724 120 TRP A CE2 
839  C  CE3 . TRP A 120 ? 0.19573 0.22323 0.28682 -0.04417 0.02436  -0.03421 120 TRP A CE3 
840  C  CZ2 . TRP A 120 ? 0.27204 0.25995 0.28792 -0.06332 0.03658  -0.02663 120 TRP A CZ2 
841  C  CZ3 . TRP A 120 ? 0.21565 0.25658 0.29772 -0.03798 0.03942  -0.02922 120 TRP A CZ3 
842  C  CH2 . TRP A 120 ? 0.26342 0.26035 0.29504 -0.06279 0.03607  -0.02074 120 TRP A CH2 
843  N  N   . TYR A 121 ? 0.17784 0.20802 0.23616 -0.00646 0.00867  -0.03686 121 TYR A N   
844  C  CA  . TYR A 121 ? 0.17354 0.19444 0.23502 0.00659  0.01622  0.00218  121 TYR A CA  
845  C  C   . TYR A 121 ? 0.18137 0.18216 0.22581 0.00126  0.01597  -0.02100 121 TYR A C   
846  O  O   . TYR A 121 ? 0.22646 0.21626 0.23289 -0.00928 0.01711  -0.00983 121 TYR A O   
847  C  CB  . TYR A 121 ? 0.23974 0.25693 0.25405 -0.00498 0.02203  0.01572  121 TYR A CB  
848  C  CG  . TYR A 121 ? 0.26257 0.26427 0.26370 0.00335  0.03891  0.02661  121 TYR A CG  
849  C  CD1 . TYR A 121 ? 0.31093 0.28275 0.26948 -0.00732 0.05831  0.00659  121 TYR A CD1 
850  C  CD2 . TYR A 121 ? 0.32199 0.30709 0.26218 0.00822  0.02443  0.04038  121 TYR A CD2 
851  C  CE1 . TYR A 121 ? 0.36243 0.34009 0.26433 -0.01042 0.05632  0.01355  121 TYR A CE1 
852  C  CE2 . TYR A 121 ? 0.37731 0.38610 0.26187 0.03572  0.04222  0.03149  121 TYR A CE2 
853  C  CZ  . TYR A 121 ? 0.41000 0.42199 0.25683 0.02543  0.05514  0.01823  121 TYR A CZ  
854  O  OH  . TYR A 121 ? 0.50306 0.50316 0.25189 0.03818  0.03822  0.01421  121 TYR A OH  
855  N  N   . SER A 122 ? 0.18894 0.15370 0.22257 -0.00707 0.01247  -0.04273 122 SER A N   
856  C  CA  . SER A 122 ? 0.16994 0.19803 0.21762 -0.00369 0.00581  -0.01663 122 SER A CA  
857  C  C   . SER A 122 ? 0.16940 0.18948 0.19748 -0.01633 0.00937  -0.02859 122 SER A C   
858  O  O   . SER A 122 ? 0.17723 0.20247 0.19342 -0.02657 0.00504  -0.02275 122 SER A O   
859  C  CB  . SER A 122 ? 0.20195 0.16116 0.23321 -0.00223 -0.00926 -0.01054 122 SER A CB  
860  O  OG  . SER A 122 ? 0.22486 0.19485 0.24295 0.00367  -0.02349 -0.01113 122 SER A OG  
861  N  N   . THR A 123 ? 0.16975 0.15320 0.19041 -0.00538 0.00601  -0.00845 123 THR A N   
862  C  CA  . THR A 123 ? 0.18748 0.16316 0.18977 0.01474  0.01073  0.00502  123 THR A CA  
863  C  C   . THR A 123 ? 0.17179 0.16129 0.19065 0.02647  -0.00097 -0.00014 123 THR A C   
864  O  O   . THR A 123 ? 0.17540 0.18041 0.20367 -0.01761 -0.00464 0.01109  123 THR A O   
865  C  CB  . THR A 123 ? 0.18495 0.13824 0.19845 0.00211  0.00548  0.00013  123 THR A CB  
866  O  OG1 . THR A 123 ? 0.18260 0.16912 0.21334 0.01199  0.01544  0.01482  123 THR A OG1 
867  C  CG2 . THR A 123 ? 0.19219 0.20010 0.20205 0.01073  0.01641  -0.00884 123 THR A CG2 
868  N  N   . LEU A 124 ? 0.18188 0.14773 0.19615 0.00734  -0.00066 -0.01190 124 LEU A N   
869  C  CA  . LEU A 124 ? 0.16855 0.14942 0.20085 0.00759  0.00037  0.00361  124 LEU A CA  
870  C  C   . LEU A 124 ? 0.17174 0.16617 0.20159 -0.00106 0.00941  -0.00693 124 LEU A C   
871  O  O   . LEU A 124 ? 0.16973 0.15942 0.19903 -0.01407 0.00942  -0.01058 124 LEU A O   
872  C  CB  . LEU A 124 ? 0.19596 0.18757 0.19906 0.01489  0.01148  0.00097  124 LEU A CB  
873  C  CG  . LEU A 124 ? 0.25755 0.17530 0.20217 -0.01722 -0.01897 0.01655  124 LEU A CG  
874  C  CD1 . LEU A 124 ? 0.28207 0.20456 0.19142 -0.00841 -0.07404 -0.00683 124 LEU A CD1 
875  C  CD2 . LEU A 124 ? 0.30409 0.17451 0.21524 -0.00952 0.01383  0.01806  124 LEU A CD2 
876  N  N   . VAL A 125 ? 0.15840 0.16640 0.20161 0.01770  0.00213  -0.01220 125 VAL A N   
877  C  CA  . VAL A 125 ? 0.13536 0.18338 0.20472 0.03694  0.01194  -0.00190 125 VAL A CA  
878  C  C   . VAL A 125 ? 0.13457 0.16516 0.19597 -0.00745 0.02598  0.00988  125 VAL A C   
879  O  O   . VAL A 125 ? 0.18177 0.16362 0.20300 -0.00247 0.03323  0.00060  125 VAL A O   
880  C  CB  . VAL A 125 ? 0.14416 0.17343 0.21184 -0.00397 0.00646  0.01769  125 VAL A CB  
881  C  CG1 . VAL A 125 ? 0.13960 0.18361 0.22769 0.00018  0.01462  0.02380  125 VAL A CG1 
882  C  CG2 . VAL A 125 ? 0.20180 0.21376 0.21348 0.02026  0.02781  0.01164  125 VAL A CG2 
883  N  N   . GLY A 126 ? 0.14980 0.15624 0.18669 -0.01153 0.01636  -0.00528 126 GLY A N   
884  C  CA  . GLY A 126 ? 0.15612 0.16537 0.18844 0.00544  0.02262  0.00346  126 GLY A CA  
885  C  C   . GLY A 126 ? 0.13125 0.15651 0.19251 -0.00486 -0.00288 -0.00645 126 GLY A C   
886  O  O   . GLY A 126 ? 0.16883 0.14803 0.19481 0.00355  0.00186  0.01054  126 GLY A O   
887  N  N   . HIS A 127 ? 0.15574 0.14441 0.20219 0.00931  0.00756  -0.01300 127 HIS A N   
888  C  CA  . HIS A 127 ? 0.13251 0.17311 0.21677 -0.00118 -0.00239 -0.00814 127 HIS A CA  
889  C  C   . HIS A 127 ? 0.14643 0.18520 0.22376 0.02398  -0.01389 -0.00137 127 HIS A C   
890  O  O   . HIS A 127 ? 0.16099 0.21230 0.23406 0.01419  -0.01945 0.03210  127 HIS A O   
891  C  CB  . HIS A 127 ? 0.15582 0.18177 0.22938 0.01190  -0.01873 -0.00374 127 HIS A CB  
892  C  CG  . HIS A 127 ? 0.19840 0.15756 0.24630 0.01651  -0.03165 0.00041  127 HIS A CG  
893  N  ND1 . HIS A 127 ? 0.24796 0.20421 0.25846 0.01862  -0.02610 -0.00185 127 HIS A ND1 
894  C  CD2 . HIS A 127 ? 0.19153 0.15295 0.25963 -0.01858 -0.02465 0.00325  127 HIS A CD2 
895  C  CE1 . HIS A 127 ? 0.27639 0.20538 0.26354 -0.00021 -0.01104 0.01653  127 HIS A CE1 
896  N  NE2 . HIS A 127 ? 0.28539 0.21372 0.26627 -0.04798 -0.02711 0.02181  127 HIS A NE2 
897  N  N   . ASP A 128 ? 0.14865 0.17583 0.22645 0.00898  -0.01929 -0.01569 128 ASP A N   
898  C  CA  . ASP A 128 ? 0.14990 0.16247 0.22752 0.00448  -0.01166 -0.00308 128 ASP A CA  
899  C  C   . ASP A 128 ? 0.15286 0.16209 0.24956 0.02630  -0.01278 -0.00611 128 ASP A C   
900  O  O   . ASP A 128 ? 0.18550 0.19491 0.24807 0.02824  -0.02501 0.01027  128 ASP A O   
901  C  CB  . ASP A 128 ? 0.17486 0.17711 0.22178 -0.00110 0.00098  -0.00577 128 ASP A CB  
902  C  CG  . ASP A 128 ? 0.15966 0.16709 0.21486 0.00837  -0.02062 0.00834  128 ASP A CG  
903  O  OD1 . ASP A 128 ? 0.18462 0.19738 0.21470 0.02055  -0.01899 0.02592  128 ASP A OD1 
904  O  OD2 . ASP A 128 ? 0.18836 0.18560 0.20459 0.00896  -0.02176 0.00514  128 ASP A OD2 
905  N  N   . THR A 129 ? 0.14220 0.19772 0.27434 0.03013  0.00394  -0.01393 129 THR A N   
906  C  CA  A THR A 129 ? 0.14567 0.22060 0.28871 0.02279  0.00958  -0.02849 129 THR A CA  
907  C  CA  B THR A 129 ? 0.15908 0.21573 0.28496 0.02784  0.01161  -0.01432 129 THR A CA  
908  C  C   . THR A 129 ? 0.16135 0.22205 0.28578 0.01145  -0.00723 -0.00507 129 THR A C   
909  O  O   . THR A 129 ? 0.16814 0.23229 0.28794 0.01144  -0.01216 0.01076  129 THR A O   
910  C  CB  A THR A 129 ? 0.18746 0.27826 0.30442 -0.00911 0.01123  -0.07117 129 THR A CB  
911  C  CB  B THR A 129 ? 0.19854 0.24328 0.29379 0.02331  0.02530  -0.02866 129 THR A CB  
912  O  OG1 A THR A 129 ? 0.20908 0.33950 0.31278 -0.00031 -0.00375 -0.08290 129 THR A OG1 
913  O  OG1 B THR A 129 ? 0.24539 0.28885 0.30188 0.04287  0.03714  -0.03708 129 THR A OG1 
914  C  CG2 A THR A 129 ? 0.24389 0.30456 0.31308 0.00787  0.02835  -0.08022 129 THR A CG2 
915  C  CG2 B THR A 129 ? 0.20487 0.23633 0.29507 0.02606  0.02505  -0.02244 129 THR A CG2 
916  N  N   . PHE A 130 ? 0.14966 0.20015 0.27814 -0.01894 -0.01056 0.00098  130 PHE A N   
917  C  CA  . PHE A 130 ? 0.13650 0.20907 0.28265 -0.00412 -0.00097 -0.00568 130 PHE A CA  
918  C  C   . PHE A 130 ? 0.16656 0.22659 0.29670 0.03939  -0.00710 -0.00769 130 PHE A C   
919  O  O   . PHE A 130 ? 0.17169 0.24591 0.29269 0.03022  0.00007  0.00210  130 PHE A O   
920  C  CB  . PHE A 130 ? 0.17577 0.19487 0.27007 0.02486  -0.00416 -0.02094 130 PHE A CB  
921  C  CG  . PHE A 130 ? 0.13483 0.18399 0.25098 0.00642  -0.00339 -0.00411 130 PHE A CG  
922  C  CD1 . PHE A 130 ? 0.17244 0.19519 0.24424 0.00531  -0.01658 -0.00212 130 PHE A CD1 
923  C  CD2 . PHE A 130 ? 0.17627 0.20989 0.24259 -0.00026 -0.00685 0.00500  130 PHE A CD2 
924  C  CE1 . PHE A 130 ? 0.15175 0.20526 0.23592 -0.00120 -0.01198 -0.01143 130 PHE A CE1 
925  C  CE2 . PHE A 130 ? 0.16650 0.21539 0.23802 0.01715  -0.00859 0.01272  130 PHE A CE2 
926  C  CZ  . PHE A 130 ? 0.17369 0.18088 0.23346 -0.00098 -0.01625 0.01430  130 PHE A CZ  
927  N  N   . THR A 131 ? 0.12328 0.23158 0.32537 0.03427  -0.00914 -0.00942 131 THR A N   
928  C  CA  . THR A 131 ? 0.16306 0.22876 0.34836 0.02415  -0.01207 -0.01206 131 THR A CA  
929  C  C   . THR A 131 ? 0.14808 0.28678 0.35611 0.06146  -0.01120 -0.04010 131 THR A C   
930  O  O   . THR A 131 ? 0.16440 0.25803 0.34860 0.05400  -0.00244 -0.04433 131 THR A O   
931  C  CB  . THR A 131 ? 0.26536 0.23249 0.37028 0.00274  -0.01656 -0.00544 131 THR A CB  
932  O  OG1 . THR A 131 ? 0.37285 0.28557 0.38873 0.01512  -0.04220 0.00312  131 THR A OG1 
933  C  CG2 . THR A 131 ? 0.29777 0.23270 0.37749 0.02349  -0.01067 -0.00437 131 THR A CG2 
934  N  N   . LYS A 132 ? 0.15111 0.37346 0.37321 0.05153  -0.01371 -0.04622 132 LYS A N   
935  C  CA  . LYS A 132 ? 0.17702 0.39269 0.39609 0.04701  -0.01142 -0.03470 132 LYS A CA  
936  C  C   . LYS A 132 ? 0.22652 0.39698 0.42791 0.11080  -0.02647 -0.00764 132 LYS A C   
937  O  O   . LYS A 132 ? 0.22128 0.39616 0.42529 0.07614  -0.02390 -0.01955 132 LYS A O   
938  C  CB  . LYS A 132 ? 0.22690 0.43652 0.39199 -0.00239 -0.01463 -0.03420 132 LYS A CB  
939  C  CG  . LYS A 132 ? 0.31489 0.45450 0.39270 -0.01701 -0.00613 -0.03478 132 LYS A CG  
940  C  CD  . LYS A 132 ? 0.38859 0.47403 0.39235 -0.01972 0.00826  -0.03316 132 LYS A CD  
941  C  CE  . LYS A 132 ? 0.51183 0.45789 0.39385 -0.04158 0.05039  -0.03071 132 LYS A CE  
942  N  NZ  . LYS A 132 ? 0.59706 0.37436 0.39251 -0.00912 0.08667  -0.03482 132 LYS A NZ  
943  N  N   . VAL A 133 ? 0.33221 0.39785 0.46719 0.14114  -0.03926 0.03261  133 VAL A N   
944  C  CA  . VAL A 133 ? 0.45920 0.43613 0.50936 0.14557  -0.03270 0.06375  133 VAL A CA  
945  C  C   . VAL A 133 ? 0.51016 0.45113 0.53980 0.09806  -0.02602 0.08905  133 VAL A C   
946  O  O   . VAL A 133 ? 0.54112 0.46360 0.54376 0.08981  -0.04046 0.09872  133 VAL A O   
947  C  CB  . VAL A 133 ? 0.56515 0.49682 0.51988 0.16918  -0.03019 0.07351  133 VAL A CB  
948  C  CG1 . VAL A 133 ? 0.62015 0.51941 0.52531 0.16172  -0.03096 0.07666  133 VAL A CG1 
949  C  CG2 . VAL A 133 ? 0.59968 0.52152 0.52405 0.18395  -0.02544 0.06974  133 VAL A CG2 
950  N  N   . LYS A 134 ? 0.60296 0.55404 0.56503 0.01907  -0.01086 0.08677  134 LYS A N   
951  C  CA  . LYS A 134 ? 0.68263 0.61710 0.58903 -0.00596 -0.00607 0.08500  134 LYS A CA  
952  C  C   . LYS A 134 ? 0.71732 0.59276 0.59214 0.01818  -0.01968 0.09967  134 LYS A C   
953  O  O   . LYS A 134 ? 0.73705 0.57247 0.59331 0.04210  -0.03625 0.11126  134 LYS A O   
954  C  CB  . LYS A 134 ? 0.70812 0.66433 0.60660 -0.03131 0.01162  0.07707  134 LYS A CB  
955  C  CG  . LYS A 134 ? 0.70695 0.70464 0.62030 -0.04117 0.02489  0.06982  134 LYS A CG  
956  C  CD  . LYS A 134 ? 0.73073 0.74766 0.63190 -0.04454 0.02901  0.06501  134 LYS A CD  
957  C  CE  . LYS A 134 ? 0.74731 0.77571 0.63969 -0.05613 0.02695  0.05969  134 LYS A CE  
958  N  NZ  . LYS A 134 ? 0.75592 0.79971 0.64415 -0.05564 0.02009  0.05346  134 LYS A NZ  
959  C  C10 . QG7 B .   ? 0.17693 0.20435 0.20532 -0.00358 -0.01519 0.00236  201 QG7 A C10 
960  C  C15 . QG7 B .   ? 0.47976 0.47252 0.44361 -0.00190 -0.00052 -0.00053 201 QG7 A C15 
961  C  C17 . QG7 B .   ? 0.37978 0.38498 0.37825 0.01317  -0.00147 -0.01637 201 QG7 A C17 
962  C  C11 . QG7 B .   ? 0.42735 0.42097 0.39773 -0.00488 -0.00848 0.01427  201 QG7 A C11 
963  C  C12 . QG7 B .   ? 0.42752 0.43455 0.43042 0.00614  -0.00119 0.00311  201 QG7 A C12 
964  C  C14 . QG7 B .   ? 0.48694 0.48363 0.43786 -0.00077 0.00068  0.00073  201 QG7 A C14 
965  O  O2  . QG7 B .   ? 0.17664 0.18062 0.21848 0.02334  -0.01817 0.00184  201 QG7 A O2  
966  C  C9  . QG7 B .   ? 0.22420 0.21919 0.20071 0.01614  -0.02146 0.00907  201 QG7 A C9  
967  N  N1  . QG7 B .   ? 0.21310 0.19597 0.19467 -0.00261 -0.02553 0.01536  201 QG7 A N1  
968  N  N2  . QG7 B .   ? 0.21736 0.21739 0.20807 0.00325  -0.01857 0.00534  201 QG7 A N2  
969  C  C8  . QG7 B .   ? 0.18708 0.15665 0.20065 0.01340  -0.03008 0.02251  201 QG7 A C8  
970  C  C7  . QG7 B .   ? 0.18454 0.17651 0.20465 0.03115  -0.04775 0.01084  201 QG7 A C7  
971  S  S1  . QG7 B .   ? 0.18521 0.18643 0.21297 -0.00024 -0.03952 -0.00213 201 QG7 A S1  
972  C  C6  . QG7 B .   ? 0.18327 0.19559 0.20726 -0.00723 -0.02432 0.00677  201 QG7 A C6  
973  C  C5  . QG7 B .   ? 0.20816 0.19541 0.21254 -0.02426 -0.02917 0.00991  201 QG7 A C5  
974  C  C4  . QG7 B .   ? 0.19594 0.22099 0.22281 -0.01345 -0.04289 0.01426  201 QG7 A C4  
975  C  C3  . QG7 B .   ? 0.23291 0.20246 0.23431 -0.03643 -0.03807 0.00727  201 QG7 A C3  
976  C  C2  . QG7 B .   ? 0.24375 0.24303 0.24188 -0.03386 -0.02128 -0.00878 201 QG7 A C2  
977  C  C1  . QG7 B .   ? 0.26410 0.27529 0.25078 0.00547  -0.00626 -0.01444 201 QG7 A C1  
978  C  C24 . QG7 B .   ? 0.31384 0.32725 0.32855 -0.01827 -0.00258 0.00840  201 QG7 A C24 
979  O  O1  . QG7 B .   ? 0.22959 0.28390 0.23632 0.00935  -0.00656 -0.00384 201 QG7 A O1  
980  N  N6  . QG7 B .   ? 0.28859 0.29671 0.28708 0.01367  -0.00719 0.00415  201 QG7 A N6  
981  C  C23 . QG7 B .   ? 0.36298 0.35585 0.35682 -0.00528 -0.00148 -0.00457 201 QG7 A C23 
982  N  N3  . QG7 B .   ? 0.38673 0.38813 0.37656 0.00907  -0.00242 -0.00805 201 QG7 A N3  
983  N  N4  . QG7 B .   ? 0.40007 0.40309 0.45002 0.01372  -0.01002 0.00355  201 QG7 A N4  
984  C  C16 . QG7 B .   ? 0.44548 0.45015 0.45347 -0.00073 -0.00577 0.00056  201 QG7 A C16 
985  C  C13 . QG7 B .   ? 0.45192 0.44874 0.43312 -0.00664 -0.00360 0.00111  201 QG7 A C13 
986  N  N5  . QG7 B .   ? 0.35658 0.33180 0.38163 0.02910  0.01836  -0.00564 201 QG7 A N5  
987  C  C18 . QG7 B .   ? 0.36398 0.35334 0.38280 0.01638  0.01469  -0.00480 201 QG7 A C18 
988  C  C22 . QG7 B .   ? 0.40866 0.41001 0.37587 0.00023  -0.00061 -0.00769 201 QG7 A C22 
989  C  C21 . QG7 B .   ? 0.39370 0.39394 0.37689 0.00667  -0.00794 -0.00828 201 QG7 A C21 
990  C  C20 . QG7 B .   ? 0.37751 0.37862 0.38370 0.01017  0.00840  -0.00756 201 QG7 A C20 
991  C  C19 . QG7 B .   ? 0.35915 0.35523 0.38603 -0.00512 0.01002  -0.00556 201 QG7 A C19 
1024 CU CU  . CU  C .   ? 0.96145 0.96476 0.96077 -0.00469 -0.00130 -0.00312 202 CU  A CU  
1025 C  C   . ACY D .   ? 0.31602 0.30345 0.34994 -0.04780 0.00275  0.00977  203 ACY A C   
1026 O  O   . ACY D .   ? 0.38351 0.41410 0.34921 -0.01214 0.00132  0.01614  203 ACY A O   
1027 O  OXT . ACY D .   ? 0.39434 0.37641 0.35406 -0.02678 -0.03013 -0.01757 203 ACY A OXT 
1028 C  CH3 . ACY D .   ? 0.34447 0.33366 0.33654 -0.00920 -0.00343 -0.01253 203 ACY A CH3 
1029 CU CU  . CU  E .   ? 0.50727 0.54848 0.36995 0.03259  -0.06652 -0.02016 204 CU  A CU  
# 
