data_9DAR
# 
_entry.id   9DAR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9DAR         pdb_00009dar 10.2210/pdb9dar/pdb 
WWPDB D_1000287437 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'Structure model' 1 1 2025-03-26 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DAR 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-22 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 jjez@wustl.edu      Joseph  Jez       M 'principal investigator/group leader' 0000-0001-7911-9108 
4 wencewicz@wustl.edu Timothy Wencewicz A 'principal investigator/group leader' 0000-0002-5839-6672 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Berkovich, D.A.' 1 ? 
'Jez, J.M.'       2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Infect Dis.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2373-8227 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            11 
_citation.language                  ? 
_citation.page_first                689 
_citation.page_last                 702 
_citation.title                     
'Expanding the Landscape of Dual Action Antifolate Antibacterials through 2,4-Diamino-1,6-dihydro-1,3,5-triazines.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsinfecdis.4c00768 
_citation.pdbx_database_id_PubMed   39950956 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Georgiades, J.D.' 1  ? 
primary 'Berkovich, D.A.'  2  ? 
primary 'McKee, S.R.'      3  ? 
primary 'Smith, A.R.'      4  ? 
primary 'Sankaran, B.'     5  ? 
primary 'Flentie, K.N.'    6  ? 
primary 'Castaneda, C.H.'  7  ? 
primary 'Grohmann, D.G.'   8  ? 
primary 'Rohatgi, R.'      9  ? 
primary 'Lasky, C.'        10 ? 
primary 'Mason, T.A.'      11 ? 
primary 'Champine, J.E.'   12 ? 
primary 'Miller, P.A.'     13 ? 
primary 'Mollmann, U.'     14 ? 
primary 'Moraski, G.C.'    15 ? 
primary 'Franzblau, S.G.'  16 ? 
primary 'Miller, M.J.'     17 ? 
primary 'Stallings, C.L.'  18 ? 
primary 'Jez, J.M.'        19 ? 
primary 'Hathaway, B.A.'   20 ? 
primary 'Wencewicz, T.A.'  21 ? 
# 
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 'Dihydrofolate reductase'                                                18244.568 1  1.5.1.3 ? ? ? 
2 non-polymer syn '1-(4-chlorophenyl)-6,6-dimethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine' 251.715   1  ?       ? ? ? 
3 non-polymer syn 'CITRATE ANION'                                                          189.100   1  ?       ? ? ? 
4 water       nat water                                                                    18.015    48 ?       ? ? ? 
# 
_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       
;SHMISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSV
DEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILER
R
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SHMISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSV
DEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILER
R
;
_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 '1-(4-chlorophenyl)-6,6-dimethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine' 1CY 
3 'CITRATE ANION'                                                          FLC 
4 water                                                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   HIS n 
1 3   MET n 
1 4   ILE n 
1 5   SER n 
1 6   LEU n 
1 7   ILE n 
1 8   ALA n 
1 9   ALA n 
1 10  LEU n 
1 11  ALA n 
1 12  VAL n 
1 13  ASP n 
1 14  ARG n 
1 15  VAL n 
1 16  ILE n 
1 17  GLY n 
1 18  MET n 
1 19  GLU n 
1 20  ASN n 
1 21  ALA n 
1 22  MET n 
1 23  PRO n 
1 24  TRP n 
1 25  ASN n 
1 26  LEU n 
1 27  PRO n 
1 28  ALA n 
1 29  ASP n 
1 30  LEU n 
1 31  ALA n 
1 32  TRP n 
1 33  PHE n 
1 34  LYS n 
1 35  ARG n 
1 36  ASN n 
1 37  THR n 
1 38  LEU n 
1 39  ASN n 
1 40  LYS n 
1 41  PRO n 
1 42  VAL n 
1 43  ILE n 
1 44  MET n 
1 45  GLY n 
1 46  ARG n 
1 47  HIS n 
1 48  THR n 
1 49  TRP n 
1 50  GLU n 
1 51  SER n 
1 52  ILE n 
1 53  GLY n 
1 54  ARG n 
1 55  PRO n 
1 56  LEU n 
1 57  PRO n 
1 58  GLY n 
1 59  ARG n 
1 60  LYS n 
1 61  ASN n 
1 62  ILE n 
1 63  ILE n 
1 64  LEU n 
1 65  SER n 
1 66  SER n 
1 67  GLN n 
1 68  PRO n 
1 69  GLY n 
1 70  THR n 
1 71  ASP n 
1 72  ASP n 
1 73  ARG n 
1 74  VAL n 
1 75  THR n 
1 76  TRP n 
1 77  VAL n 
1 78  LYS n 
1 79  SER n 
1 80  VAL n 
1 81  ASP n 
1 82  GLU n 
1 83  ALA n 
1 84  ILE n 
1 85  ALA n 
1 86  ALA n 
1 87  CYS n 
1 88  GLY n 
1 89  ASP n 
1 90  VAL n 
1 91  PRO n 
1 92  GLU n 
1 93  ILE n 
1 94  MET n 
1 95  VAL n 
1 96  ILE n 
1 97  GLY n 
1 98  GLY n 
1 99  GLY n 
1 100 ARG n 
1 101 VAL n 
1 102 TYR n 
1 103 GLU n 
1 104 GLN n 
1 105 PHE n 
1 106 LEU n 
1 107 PRO n 
1 108 LYS n 
1 109 ALA n 
1 110 GLN n 
1 111 LYS n 
1 112 LEU n 
1 113 TYR n 
1 114 LEU n 
1 115 THR n 
1 116 HIS n 
1 117 ILE n 
1 118 ASP n 
1 119 ALA n 
1 120 GLU n 
1 121 VAL n 
1 122 GLU n 
1 123 GLY n 
1 124 ASP n 
1 125 THR n 
1 126 HIS n 
1 127 PHE n 
1 128 PRO n 
1 129 ASP n 
1 130 TYR n 
1 131 GLU n 
1 132 PRO n 
1 133 ASP n 
1 134 ASP n 
1 135 TRP n 
1 136 GLU n 
1 137 SER n 
1 138 VAL n 
1 139 PHE n 
1 140 SER n 
1 141 GLU n 
1 142 PHE n 
1 143 HIS n 
1 144 ASP n 
1 145 ALA n 
1 146 ASP n 
1 147 ALA n 
1 148 GLN n 
1 149 ASN n 
1 150 SER n 
1 151 HIS n 
1 152 SER n 
1 153 TYR n 
1 154 CYS n 
1 155 PHE n 
1 156 GLU n 
1 157 ILE n 
1 158 LEU n 
1 159 GLU n 
1 160 ARG n 
1 161 ARG 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                   161 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'folA, c0058' 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
1CY non-polymer         . '1-(4-chlorophenyl)-6,6-dimethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine' Cycloguanil 'C11 H14 Cl N5'  
251.715 
ALA 'L-peptide linking' y ALANINE                                                                  ?           'C3 H7 N O2'     
89.093  
ARG 'L-peptide linking' y ARGININE                                                                 ?           'C6 H15 N4 O2 1' 
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                               ?           'C4 H8 N2 O3'    
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                          ?           'C4 H7 N O4'     
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                 ?           'C3 H7 N O2 S'   
121.158 
FLC non-polymer         . 'CITRATE ANION'                                                          ?           'C6 H5 O7 -3'    
189.100 
GLN 'L-peptide linking' y GLUTAMINE                                                                ?           'C5 H10 N2 O3'   
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                          ?           'C5 H9 N O4'     
147.129 
GLY 'peptide linking'   y GLYCINE                                                                  ?           'C2 H5 N O2'     
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                ?           'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                                                    ?           'H2 O'           
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                               ?           'C6 H13 N O2'    
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                  ?           'C6 H13 N O2'    
131.173 
LYS 'L-peptide linking' y LYSINE                                                                   ?           'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking' y METHIONINE                                                               ?           'C5 H11 N O2 S'  
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                            ?           'C9 H11 N O2'    
165.189 
PRO 'L-peptide linking' y PROLINE                                                                  ?           'C5 H9 N O2'     
115.130 
SER 'L-peptide linking' y SERINE                                                                   ?           'C3 H7 N O3'     
105.093 
THR 'L-peptide linking' y THREONINE                                                                ?           'C4 H9 N O3'     
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                               ?           'C11 H12 N2 O2'  
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                 ?           'C9 H11 N O3'    
181.189 
VAL 'L-peptide linking' y VALINE                                                                   ?           'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   -1  -1  SER SER A . n 
A 1 2   HIS 2   0   0   HIS HIS A . n 
A 1 3   MET 3   1   1   MET MET A . n 
A 1 4   ILE 4   2   2   ILE ILE A . n 
A 1 5   SER 5   3   3   SER SER A . n 
A 1 6   LEU 6   4   4   LEU LEU A . n 
A 1 7   ILE 7   5   5   ILE ILE A . n 
A 1 8   ALA 8   6   6   ALA ALA A . n 
A 1 9   ALA 9   7   7   ALA ALA A . n 
A 1 10  LEU 10  8   8   LEU LEU A . n 
A 1 11  ALA 11  9   9   ALA ALA A . n 
A 1 12  VAL 12  10  10  VAL VAL A . n 
A 1 13  ASP 13  11  11  ASP ASP A . n 
A 1 14  ARG 14  12  12  ARG ARG A . n 
A 1 15  VAL 15  13  13  VAL VAL A . n 
A 1 16  ILE 16  14  14  ILE ILE A . n 
A 1 17  GLY 17  15  15  GLY GLY A . n 
A 1 18  MET 18  16  16  MET MET A . n 
A 1 19  GLU 19  17  17  GLU GLU A . n 
A 1 20  ASN 20  18  18  ASN ASN A . n 
A 1 21  ALA 21  19  19  ALA ALA A . n 
A 1 22  MET 22  20  20  MET MET A . n 
A 1 23  PRO 23  21  21  PRO PRO A . n 
A 1 24  TRP 24  22  22  TRP TRP A . n 
A 1 25  ASN 25  23  23  ASN ASN A . n 
A 1 26  LEU 26  24  24  LEU LEU A . n 
A 1 27  PRO 27  25  25  PRO PRO A . n 
A 1 28  ALA 28  26  26  ALA ALA A . n 
A 1 29  ASP 29  27  27  ASP ASP A . n 
A 1 30  LEU 30  28  28  LEU LEU A . n 
A 1 31  ALA 31  29  29  ALA ALA A . n 
A 1 32  TRP 32  30  30  TRP TRP A . n 
A 1 33  PHE 33  31  31  PHE PHE A . n 
A 1 34  LYS 34  32  32  LYS LYS A . n 
A 1 35  ARG 35  33  33  ARG ARG A . n 
A 1 36  ASN 36  34  34  ASN ASN A . n 
A 1 37  THR 37  35  35  THR THR A . n 
A 1 38  LEU 38  36  36  LEU LEU A . n 
A 1 39  ASN 39  37  37  ASN ASN A . n 
A 1 40  LYS 40  38  38  LYS LYS A . n 
A 1 41  PRO 41  39  39  PRO PRO A . n 
A 1 42  VAL 42  40  40  VAL VAL A . n 
A 1 43  ILE 43  41  41  ILE ILE A . n 
A 1 44  MET 44  42  42  MET MET A . n 
A 1 45  GLY 45  43  43  GLY GLY A . n 
A 1 46  ARG 46  44  44  ARG ARG A . n 
A 1 47  HIS 47  45  45  HIS HIS A . n 
A 1 48  THR 48  46  46  THR THR A . n 
A 1 49  TRP 49  47  47  TRP TRP A . n 
A 1 50  GLU 50  48  48  GLU GLU A . n 
A 1 51  SER 51  49  49  SER SER A . n 
A 1 52  ILE 52  50  50  ILE ILE A . n 
A 1 53  GLY 53  51  51  GLY GLY A . n 
A 1 54  ARG 54  52  52  ARG ARG A . n 
A 1 55  PRO 55  53  53  PRO PRO A . n 
A 1 56  LEU 56  54  54  LEU LEU A . n 
A 1 57  PRO 57  55  55  PRO PRO A . n 
A 1 58  GLY 58  56  56  GLY GLY A . n 
A 1 59  ARG 59  57  57  ARG ARG A . n 
A 1 60  LYS 60  58  58  LYS LYS A . n 
A 1 61  ASN 61  59  59  ASN ASN A . n 
A 1 62  ILE 62  60  60  ILE ILE A . n 
A 1 63  ILE 63  61  61  ILE ILE A . n 
A 1 64  LEU 64  62  62  LEU LEU A . n 
A 1 65  SER 65  63  63  SER SER A . n 
A 1 66  SER 66  64  64  SER SER A . n 
A 1 67  GLN 67  65  65  GLN GLN A . n 
A 1 68  PRO 68  66  66  PRO PRO A . n 
A 1 69  GLY 69  67  67  GLY GLY A . n 
A 1 70  THR 70  68  68  THR THR A . n 
A 1 71  ASP 71  69  69  ASP ASP A . n 
A 1 72  ASP 72  70  70  ASP ASP A . n 
A 1 73  ARG 73  71  71  ARG ARG A . n 
A 1 74  VAL 74  72  72  VAL VAL A . n 
A 1 75  THR 75  73  73  THR THR A . n 
A 1 76  TRP 76  74  74  TRP TRP A . n 
A 1 77  VAL 77  75  75  VAL VAL A . n 
A 1 78  LYS 78  76  76  LYS LYS A . n 
A 1 79  SER 79  77  77  SER SER A . n 
A 1 80  VAL 80  78  78  VAL VAL A . n 
A 1 81  ASP 81  79  79  ASP ASP A . n 
A 1 82  GLU 82  80  80  GLU GLU A . n 
A 1 83  ALA 83  81  81  ALA ALA A . n 
A 1 84  ILE 84  82  82  ILE ILE A . n 
A 1 85  ALA 85  83  83  ALA ALA A . n 
A 1 86  ALA 86  84  84  ALA ALA A . n 
A 1 87  CYS 87  85  85  CYS CYS A . n 
A 1 88  GLY 88  86  86  GLY GLY A . n 
A 1 89  ASP 89  87  87  ASP ASP A . n 
A 1 90  VAL 90  88  88  VAL VAL A . n 
A 1 91  PRO 91  89  89  PRO PRO A . n 
A 1 92  GLU 92  90  90  GLU GLU A . n 
A 1 93  ILE 93  91  91  ILE ILE A . n 
A 1 94  MET 94  92  92  MET MET A . n 
A 1 95  VAL 95  93  93  VAL VAL A . n 
A 1 96  ILE 96  94  94  ILE ILE A . n 
A 1 97  GLY 97  95  95  GLY GLY A . n 
A 1 98  GLY 98  96  96  GLY GLY A . n 
A 1 99  GLY 99  97  97  GLY GLY A . n 
A 1 100 ARG 100 98  98  ARG ARG A . n 
A 1 101 VAL 101 99  99  VAL VAL A . n 
A 1 102 TYR 102 100 100 TYR TYR A . n 
A 1 103 GLU 103 101 101 GLU GLU A . n 
A 1 104 GLN 104 102 102 GLN GLN A . n 
A 1 105 PHE 105 103 103 PHE PHE A . n 
A 1 106 LEU 106 104 104 LEU LEU A . n 
A 1 107 PRO 107 105 105 PRO PRO A . n 
A 1 108 LYS 108 106 106 LYS LYS A . n 
A 1 109 ALA 109 107 107 ALA ALA A . n 
A 1 110 GLN 110 108 108 GLN GLN A . n 
A 1 111 LYS 111 109 109 LYS LYS A . n 
A 1 112 LEU 112 110 110 LEU LEU A . n 
A 1 113 TYR 113 111 111 TYR TYR A . n 
A 1 114 LEU 114 112 112 LEU LEU A . n 
A 1 115 THR 115 113 113 THR THR A . n 
A 1 116 HIS 116 114 114 HIS HIS A . n 
A 1 117 ILE 117 115 115 ILE ILE A . n 
A 1 118 ASP 118 116 116 ASP ASP A . n 
A 1 119 ALA 119 117 117 ALA ALA A . n 
A 1 120 GLU 120 118 118 GLU GLU A . n 
A 1 121 VAL 121 119 119 VAL VAL A . n 
A 1 122 GLU 122 120 120 GLU GLU A . n 
A 1 123 GLY 123 121 121 GLY GLY A . n 
A 1 124 ASP 124 122 122 ASP ASP A . n 
A 1 125 THR 125 123 123 THR THR A . n 
A 1 126 HIS 126 124 124 HIS HIS A . n 
A 1 127 PHE 127 125 125 PHE PHE A . n 
A 1 128 PRO 128 126 126 PRO PRO A . n 
A 1 129 ASP 129 127 127 ASP ASP A . n 
A 1 130 TYR 130 128 128 TYR TYR A . n 
A 1 131 GLU 131 129 129 GLU GLU A . n 
A 1 132 PRO 132 130 130 PRO PRO A . n 
A 1 133 ASP 133 131 131 ASP ASP A . n 
A 1 134 ASP 134 132 132 ASP ASP A . n 
A 1 135 TRP 135 133 133 TRP TRP A . n 
A 1 136 GLU 136 134 134 GLU GLU A . n 
A 1 137 SER 137 135 135 SER SER A . n 
A 1 138 VAL 138 136 136 VAL VAL A . n 
A 1 139 PHE 139 137 137 PHE PHE A . n 
A 1 140 SER 140 138 138 SER SER A . n 
A 1 141 GLU 141 139 139 GLU GLU A . n 
A 1 142 PHE 142 140 140 PHE PHE A . n 
A 1 143 HIS 143 141 141 HIS HIS A . n 
A 1 144 ASP 144 142 142 ASP ASP A . n 
A 1 145 ALA 145 143 143 ALA ALA A . n 
A 1 146 ASP 146 144 144 ASP ASP A . n 
A 1 147 ALA 147 145 145 ALA ALA A . n 
A 1 148 GLN 148 146 146 GLN GLN A . n 
A 1 149 ASN 149 147 147 ASN ASN A . n 
A 1 150 SER 150 148 148 SER SER A . n 
A 1 151 HIS 151 149 149 HIS HIS A . n 
A 1 152 SER 152 150 150 SER SER A . n 
A 1 153 TYR 153 151 151 TYR TYR A . n 
A 1 154 CYS 154 152 152 CYS CYS A . n 
A 1 155 PHE 155 153 153 PHE PHE A . n 
A 1 156 GLU 156 154 154 GLU GLU A . n 
A 1 157 ILE 157 155 155 ILE ILE A . n 
A 1 158 LEU 158 156 156 LEU LEU A . n 
A 1 159 GLU 159 157 157 GLU GLU A . n 
A 1 160 ARG 160 158 158 ARG ARG A . n 
A 1 161 ARG 161 159 159 ARG ARG A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        1CY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   1CY 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 1CY 1  201 201 1CY 1CY A . 
C 3 FLC 1  202 202 FLC FLC A . 
D 4 HOH 1  301 347 HOH HOH A . 
D 4 HOH 2  302 310 HOH HOH A . 
D 4 HOH 3  303 307 HOH HOH A . 
D 4 HOH 4  304 311 HOH HOH A . 
D 4 HOH 5  305 340 HOH HOH A . 
D 4 HOH 6  306 322 HOH HOH A . 
D 4 HOH 7  307 343 HOH HOH A . 
D 4 HOH 8  308 348 HOH HOH A . 
D 4 HOH 9  309 309 HOH HOH A . 
D 4 HOH 10 310 341 HOH HOH A . 
D 4 HOH 11 311 320 HOH HOH A . 
D 4 HOH 12 312 346 HOH HOH A . 
D 4 HOH 13 313 327 HOH HOH A . 
D 4 HOH 14 314 336 HOH HOH A . 
D 4 HOH 15 315 323 HOH HOH A . 
D 4 HOH 16 316 315 HOH HOH A . 
D 4 HOH 17 317 302 HOH HOH A . 
D 4 HOH 18 318 301 HOH HOH A . 
D 4 HOH 19 319 331 HOH HOH A . 
D 4 HOH 20 320 328 HOH HOH A . 
D 4 HOH 21 321 306 HOH HOH A . 
D 4 HOH 22 322 317 HOH HOH A . 
D 4 HOH 23 323 325 HOH HOH A . 
D 4 HOH 24 324 314 HOH HOH A . 
D 4 HOH 25 325 338 HOH HOH A . 
D 4 HOH 26 326 319 HOH HOH A . 
D 4 HOH 27 327 334 HOH HOH A . 
D 4 HOH 28 328 345 HOH HOH A . 
D 4 HOH 29 329 318 HOH HOH A . 
D 4 HOH 30 330 308 HOH HOH A . 
D 4 HOH 31 331 303 HOH HOH A . 
D 4 HOH 32 332 344 HOH HOH A . 
D 4 HOH 33 333 335 HOH HOH A . 
D 4 HOH 34 334 305 HOH HOH A . 
D 4 HOH 35 335 333 HOH HOH A . 
D 4 HOH 36 336 329 HOH HOH A . 
D 4 HOH 37 337 304 HOH HOH A . 
D 4 HOH 38 338 342 HOH HOH A . 
D 4 HOH 39 339 321 HOH HOH A . 
D 4 HOH 40 340 330 HOH HOH A . 
D 4 HOH 41 341 312 HOH HOH A . 
D 4 HOH 42 342 332 HOH HOH A . 
D 4 HOH 43 343 339 HOH HOH A . 
D 4 HOH 44 344 316 HOH HOH A . 
D 4 HOH 45 345 337 HOH HOH A . 
D 4 HOH 46 346 326 HOH HOH A . 
D 4 HOH 47 347 324 HOH HOH A . 
D 4 HOH 48 348 313 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 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.18.2_3874: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DAR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.076 
_cell.length_a_esd                 ? 
_cell.length_b                     68.076 
_cell.length_b_esd                 ? 
_cell.length_c                     212.602 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9DAR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 61 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                   9DAR 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.90 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          68.44 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M ammonium citrate dibasic, 20% (w/v) PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.920 
_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                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.920 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DAR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.17 
_reflns.d_resolution_low                               34.5 
_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                                     12722 
_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                           94.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                23.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.17 
_reflns_shell.d_res_low                                     2.38 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             636 
_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                               19.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.438 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.768 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          56.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DAR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.17 
_refine.ls_d_res_low                             34.49 
_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                     12720 
_refine.ls_number_reflns_R_free                  590 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    78.04 
_refine.ls_percent_reflns_R_free                 4.64 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2116 
_refine.ls_R_factor_R_free                       0.2519 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2096 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 32.66 
_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                            0.25 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.17 
_refine_hist.d_res_low                        34.49 
_refine_hist.number_atoms_solvent             48 
_refine_hist.number_atoms_total               1362 
_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        1284 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_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' ? 0.009  ? 1365 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.292  ? 1866 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.048 ? 192  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.066  ? 194  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 246  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.17 2.39  . . 26  647  17.00  . . . . 0.2874 . . . . . . . . . . . 0.3064 
'X-RAY DIFFRACTION' 2.39 2.73  . . 157 3534 92.00  . . . . 0.2832 . . . . . . . . . . . 0.3205 
'X-RAY DIFFRACTION' 2.73 3.44  . . 199 3833 100.00 . . . . 0.2357 . . . . . . . . . . . 0.2601 
'X-RAY DIFFRACTION' 3.44 34.49 . . 208 4116 100.00 . . . . 0.1834 . . . . . . . . . . . 0.2361 
# 
_struct.entry_id                     9DAR 
_struct.title                        
'Structure of E. coli dihydrofolate reductase (DHFR) in an occluded conformation and in complex with cycloguanil' 
_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        9DAR 
_struct_keywords.text            'dihydrofolate reductase, occluded, cycloguanil, DHFR, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DYR_ECOL6 
_struct_ref.pdbx_db_accession          P0ABQ5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDE
AIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DAR 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 161 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0ABQ5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  159 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_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 9DAR SER A 1 ? UNP P0ABQ5 ? ? 'expression tag' -1 1 
1 9DAR HIS A 2 ? UNP P0ABQ5 ? ? 'expression tag' 0  2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ALA A 21  ? LEU A 26  ? ALA A 19  LEU A 24  1 ? 6  
HELX_P HELX_P2 AA2 LEU A 26  ? LEU A 38  ? LEU A 24  LEU A 36  1 ? 13 
HELX_P HELX_P3 AA3 ARG A 46  ? SER A 51  ? ARG A 44  SER A 49  1 ? 6  
HELX_P HELX_P4 AA4 SER A 79  ? CYS A 87  ? SER A 77  CYS A 85  1 ? 9  
HELX_P HELX_P5 AA5 GLY A 98  ? LEU A 106 ? GLY A 96  LEU A 104 1 ? 9  
HELX_P HELX_P6 AA6 GLU A 131 ? ASP A 133 ? GLU A 129 ASP A 131 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? 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 ARG A 14  ? ILE A 16  ? ARG A 12  ILE A 14  
AA1 2 MET A 3   ? ALA A 11  ? MET A 1   ALA A 9   
AA1 3 GLU A 92  ? GLY A 97  ? GLU A 90  GLY A 95  
AA1 4 VAL A 42  ? GLY A 45  ? VAL A 40  GLY A 43  
AA1 5 ASN A 61  ? LEU A 64  ? ASN A 59  LEU A 62  
AA1 6 THR A 75  ? VAL A 77  ? THR A 73  VAL A 75  
AA2 1 ARG A 14  ? ILE A 16  ? ARG A 12  ILE A 14  
AA2 2 MET A 3   ? ALA A 11  ? MET A 1   ALA A 9   
AA2 3 ALA A 109 ? ILE A 117 ? ALA A 107 ILE A 115 
AA2 4 TYR A 153 ? ARG A 160 ? TYR A 151 ARG A 158 
AA2 5 TRP A 135 ? HIS A 143 ? TRP A 133 HIS A 141 
# 
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 O ILE A 16  ? O ILE A 14  N ALA A 9   ? N ALA A 7   
AA1 2 3 N MET A 3   ? N MET A 1   O ILE A 93  ? O ILE A 91  
AA1 3 4 O ILE A 96  ? O ILE A 94  N ILE A 43  ? N ILE A 41  
AA1 4 5 N MET A 44  ? N MET A 42  O LEU A 64  ? O LEU A 62  
AA1 5 6 N ILE A 63  ? N ILE A 61  O THR A 75  ? O THR A 73  
AA2 1 2 O ILE A 16  ? O ILE A 14  N ALA A 9   ? N ALA A 7   
AA2 2 3 N LEU A 10  ? N LEU A 8   O THR A 115 ? O THR A 113 
AA2 3 4 N LEU A 114 ? N LEU A 112 O GLU A 156 ? O GLU A 154 
AA2 4 5 O TYR A 153 ? O TYR A 151 N HIS A 143 ? N HIS A 141 
# 
_pdbx_entry_details.entry_id                   9DAR 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 CD  A GLU 118 ? ? 1_555 OE2 A GLU 118 ? ? 10_554 1.14 
2 1 CD  A GLU 118 ? ? 1_555 CD  A GLU 118 ? ? 10_554 2.06 
3 1 OE1 A GLU 118 ? ? 1_555 OE2 A GLU 118 ? ? 10_554 2.12 
4 1 O   A HOH 323 ? ? 1_555 O   A HOH 340 ? ? 8_565  2.13 
# 
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 ASP A 11  ? ? 76.17   -2.90   
2 1 ASP A 144 ? ? -148.44 -159.82 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    95 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    96 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -138.00 
# 
_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    GLU 
_pdbx_struct_special_symmetry.auth_seq_id     118 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   A 
_pdbx_struct_special_symmetry.label_comp_id   GLU 
_pdbx_struct_special_symmetry.label_seq_id    120 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -19.7232 21.7327 -6.9764  0.4174 ? -0.0058 ? 0.0209  ? 0.5856 ? -0.1543 ? 0.5319 ? 3.8669 ? 0.8440 
? 1.7542 ? 3.2162 ? -0.0323 ? 6.0342 ? 0.1861 ? -0.0904 ? 0.2009  ? -0.2847 ? 0.3022  ? -0.3449 ? -0.0333 ? 1.3137 ? -0.3361 ? 
2 'X-RAY DIFFRACTION' ? refined -17.8416 29.4077 3.5308   0.3201 ? -0.0080 ? 0.0680  ? 0.3945 ? -0.1432 ? 0.3738 ? 2.0891 ? 1.2898 
? 2.2008 ? 1.8669 ? 0.1365  ? 4.8952 ? 0.0125 ? 0.0576  ? 0.1497  ? 0.0167  ? -0.0063 ? -0.0191 ? -0.2929 ? 0.5831 ? -0.0275 ? 
3 'X-RAY DIFFRACTION' ? refined -22.5789 15.7944 -3.5257  0.4738 ? 0.0644  ? -0.0230 ? 0.4091 ? -0.0879 ? 0.4452 ? 1.4282 ? 1.1302 
? 2.0945 ? 2.1945 ? -0.2429 ? 6.1665 ? 0.2852 ? 0.0854  ? -0.3818 ? 0.2207  ? -0.0139 ? -0.1531 ? 1.0044  ? 0.4948 ? -0.3424 ? 
4 'X-RAY DIFFRACTION' ? refined -30.6377 20.4055 -11.7779 0.2987 ? -0.0226 ? -0.0657 ? 0.2993 ? -0.0758 ? 0.4601 ? 3.3440 ? 
-0.0979 ? 1.0309 ? 2.2665 ? 0.0119  ? 6.8232 ? 0.2824 ? 0.2302  ? -0.5707 ? -0.1800 ? -0.0145 ? 0.0432  ? 0.2830  ? 0.1175 ? 
-0.1699 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid -1 through 24 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 25 through 96 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 97 through 129 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 130 through 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 
1CY N1   N  N N 1   
1CY C2   C  N N 2   
1CY N3   N  N N 3   
1CY C4   C  N N 4   
1CY N5   N  N N 5   
1CY C6   C  N N 6   
1CY N7   N  N N 7   
1CY N8   N  N N 8   
1CY C9   C  N N 9   
1CY C10  C  N N 10  
1CY C11  C  Y N 11  
1CY C12  C  Y N 12  
1CY C13  C  Y N 13  
1CY C14  C  Y N 14  
1CY C15  C  Y N 15  
1CY C16  C  Y N 16  
1CY CL17 CL N N 17  
1CY HN7  H  N N 18  
1CY HN7A H  N N 19  
1CY HN8  H  N N 20  
1CY HN8A H  N N 21  
1CY H9   H  N N 22  
1CY H9A  H  N N 23  
1CY H9B  H  N N 24  
1CY H10  H  N N 25  
1CY H10A H  N N 26  
1CY H10B H  N N 27  
1CY H12  H  N N 28  
1CY H13  H  N N 29  
1CY H15  H  N N 30  
1CY H16  H  N N 31  
ALA N    N  N N 32  
ALA CA   C  N S 33  
ALA C    C  N N 34  
ALA O    O  N N 35  
ALA CB   C  N N 36  
ALA OXT  O  N N 37  
ALA H    H  N N 38  
ALA H2   H  N N 39  
ALA HA   H  N N 40  
ALA HB1  H  N N 41  
ALA HB2  H  N N 42  
ALA HB3  H  N N 43  
ALA HXT  H  N N 44  
ARG N    N  N N 45  
ARG CA   C  N S 46  
ARG C    C  N N 47  
ARG O    O  N N 48  
ARG CB   C  N N 49  
ARG CG   C  N N 50  
ARG CD   C  N N 51  
ARG NE   N  N N 52  
ARG CZ   C  N N 53  
ARG NH1  N  N N 54  
ARG NH2  N  N N 55  
ARG OXT  O  N N 56  
ARG H    H  N N 57  
ARG H2   H  N N 58  
ARG HA   H  N N 59  
ARG HB2  H  N N 60  
ARG HB3  H  N N 61  
ARG HG2  H  N N 62  
ARG HG3  H  N N 63  
ARG HD2  H  N N 64  
ARG HD3  H  N N 65  
ARG HE   H  N N 66  
ARG HH11 H  N N 67  
ARG HH12 H  N N 68  
ARG HH21 H  N N 69  
ARG HH22 H  N N 70  
ARG HXT  H  N N 71  
ASN N    N  N N 72  
ASN CA   C  N S 73  
ASN C    C  N N 74  
ASN O    O  N N 75  
ASN CB   C  N N 76  
ASN CG   C  N N 77  
ASN OD1  O  N N 78  
ASN ND2  N  N N 79  
ASN OXT  O  N N 80  
ASN H    H  N N 81  
ASN H2   H  N N 82  
ASN HA   H  N N 83  
ASN HB2  H  N N 84  
ASN HB3  H  N N 85  
ASN HD21 H  N N 86  
ASN HD22 H  N N 87  
ASN HXT  H  N N 88  
ASP N    N  N N 89  
ASP CA   C  N S 90  
ASP C    C  N N 91  
ASP O    O  N N 92  
ASP CB   C  N N 93  
ASP CG   C  N N 94  
ASP OD1  O  N N 95  
ASP OD2  O  N N 96  
ASP OXT  O  N N 97  
ASP H    H  N N 98  
ASP H2   H  N N 99  
ASP HA   H  N N 100 
ASP HB2  H  N N 101 
ASP HB3  H  N N 102 
ASP HD2  H  N N 103 
ASP HXT  H  N N 104 
CYS N    N  N N 105 
CYS CA   C  N R 106 
CYS C    C  N N 107 
CYS O    O  N N 108 
CYS CB   C  N N 109 
CYS SG   S  N N 110 
CYS OXT  O  N N 111 
CYS H    H  N N 112 
CYS H2   H  N N 113 
CYS HA   H  N N 114 
CYS HB2  H  N N 115 
CYS HB3  H  N N 116 
CYS HG   H  N N 117 
CYS HXT  H  N N 118 
FLC CAC  C  N N 119 
FLC CA   C  N N 120 
FLC CB   C  N N 121 
FLC CBC  C  N N 122 
FLC CG   C  N N 123 
FLC CGC  C  N N 124 
FLC OA1  O  N N 125 
FLC OA2  O  N N 126 
FLC OB1  O  N N 127 
FLC OB2  O  N N 128 
FLC OG1  O  N N 129 
FLC OG2  O  N N 130 
FLC OHB  O  N N 131 
FLC HA1  H  N N 132 
FLC HA2  H  N N 133 
FLC HG1  H  N N 134 
FLC HG2  H  N N 135 
FLC HOB  H  N N 136 
GLN N    N  N N 137 
GLN CA   C  N S 138 
GLN C    C  N N 139 
GLN O    O  N N 140 
GLN CB   C  N N 141 
GLN CG   C  N N 142 
GLN CD   C  N N 143 
GLN OE1  O  N N 144 
GLN NE2  N  N N 145 
GLN OXT  O  N N 146 
GLN H    H  N N 147 
GLN H2   H  N N 148 
GLN HA   H  N N 149 
GLN HB2  H  N N 150 
GLN HB3  H  N N 151 
GLN HG2  H  N N 152 
GLN HG3  H  N N 153 
GLN HE21 H  N N 154 
GLN HE22 H  N N 155 
GLN HXT  H  N N 156 
GLU N    N  N N 157 
GLU CA   C  N S 158 
GLU C    C  N N 159 
GLU O    O  N N 160 
GLU CB   C  N N 161 
GLU CG   C  N N 162 
GLU CD   C  N N 163 
GLU OE1  O  N N 164 
GLU OE2  O  N N 165 
GLU OXT  O  N N 166 
GLU H    H  N N 167 
GLU H2   H  N N 168 
GLU HA   H  N N 169 
GLU HB2  H  N N 170 
GLU HB3  H  N N 171 
GLU HG2  H  N N 172 
GLU HG3  H  N N 173 
GLU HE2  H  N N 174 
GLU HXT  H  N N 175 
GLY N    N  N N 176 
GLY CA   C  N N 177 
GLY C    C  N N 178 
GLY O    O  N N 179 
GLY OXT  O  N N 180 
GLY H    H  N N 181 
GLY H2   H  N N 182 
GLY HA2  H  N N 183 
GLY HA3  H  N N 184 
GLY HXT  H  N N 185 
HIS N    N  N N 186 
HIS CA   C  N S 187 
HIS C    C  N N 188 
HIS O    O  N N 189 
HIS CB   C  N N 190 
HIS CG   C  Y N 191 
HIS ND1  N  Y N 192 
HIS CD2  C  Y N 193 
HIS CE1  C  Y N 194 
HIS NE2  N  Y N 195 
HIS OXT  O  N N 196 
HIS H    H  N N 197 
HIS H2   H  N N 198 
HIS HA   H  N N 199 
HIS HB2  H  N N 200 
HIS HB3  H  N N 201 
HIS HD1  H  N N 202 
HIS HD2  H  N N 203 
HIS HE1  H  N N 204 
HIS HE2  H  N N 205 
HIS HXT  H  N N 206 
HOH O    O  N N 207 
HOH H1   H  N N 208 
HOH H2   H  N N 209 
ILE N    N  N N 210 
ILE CA   C  N S 211 
ILE C    C  N N 212 
ILE O    O  N N 213 
ILE CB   C  N S 214 
ILE CG1  C  N N 215 
ILE CG2  C  N N 216 
ILE CD1  C  N N 217 
ILE OXT  O  N N 218 
ILE H    H  N N 219 
ILE H2   H  N N 220 
ILE HA   H  N N 221 
ILE HB   H  N N 222 
ILE HG12 H  N N 223 
ILE HG13 H  N N 224 
ILE HG21 H  N N 225 
ILE HG22 H  N N 226 
ILE HG23 H  N N 227 
ILE HD11 H  N N 228 
ILE HD12 H  N N 229 
ILE HD13 H  N N 230 
ILE HXT  H  N N 231 
LEU N    N  N N 232 
LEU CA   C  N S 233 
LEU C    C  N N 234 
LEU O    O  N N 235 
LEU CB   C  N N 236 
LEU CG   C  N N 237 
LEU CD1  C  N N 238 
LEU CD2  C  N N 239 
LEU OXT  O  N N 240 
LEU H    H  N N 241 
LEU H2   H  N N 242 
LEU HA   H  N N 243 
LEU HB2  H  N N 244 
LEU HB3  H  N N 245 
LEU HG   H  N N 246 
LEU HD11 H  N N 247 
LEU HD12 H  N N 248 
LEU HD13 H  N N 249 
LEU HD21 H  N N 250 
LEU HD22 H  N N 251 
LEU HD23 H  N N 252 
LEU HXT  H  N N 253 
LYS N    N  N N 254 
LYS CA   C  N S 255 
LYS C    C  N N 256 
LYS O    O  N N 257 
LYS CB   C  N N 258 
LYS CG   C  N N 259 
LYS CD   C  N N 260 
LYS CE   C  N N 261 
LYS NZ   N  N N 262 
LYS OXT  O  N N 263 
LYS H    H  N N 264 
LYS H2   H  N N 265 
LYS HA   H  N N 266 
LYS HB2  H  N N 267 
LYS HB3  H  N N 268 
LYS HG2  H  N N 269 
LYS HG3  H  N N 270 
LYS HD2  H  N N 271 
LYS HD3  H  N N 272 
LYS HE2  H  N N 273 
LYS HE3  H  N N 274 
LYS HZ1  H  N N 275 
LYS HZ2  H  N N 276 
LYS HZ3  H  N N 277 
LYS HXT  H  N N 278 
MET N    N  N N 279 
MET CA   C  N S 280 
MET C    C  N N 281 
MET O    O  N N 282 
MET CB   C  N N 283 
MET CG   C  N N 284 
MET SD   S  N N 285 
MET CE   C  N N 286 
MET OXT  O  N N 287 
MET H    H  N N 288 
MET H2   H  N N 289 
MET HA   H  N N 290 
MET HB2  H  N N 291 
MET HB3  H  N N 292 
MET HG2  H  N N 293 
MET HG3  H  N N 294 
MET HE1  H  N N 295 
MET HE2  H  N N 296 
MET HE3  H  N N 297 
MET HXT  H  N N 298 
PHE N    N  N N 299 
PHE CA   C  N S 300 
PHE C    C  N N 301 
PHE O    O  N N 302 
PHE CB   C  N N 303 
PHE CG   C  Y N 304 
PHE CD1  C  Y N 305 
PHE CD2  C  Y N 306 
PHE CE1  C  Y N 307 
PHE CE2  C  Y N 308 
PHE CZ   C  Y N 309 
PHE OXT  O  N N 310 
PHE H    H  N N 311 
PHE H2   H  N N 312 
PHE HA   H  N N 313 
PHE HB2  H  N N 314 
PHE HB3  H  N N 315 
PHE HD1  H  N N 316 
PHE HD2  H  N N 317 
PHE HE1  H  N N 318 
PHE HE2  H  N N 319 
PHE HZ   H  N N 320 
PHE HXT  H  N N 321 
PRO N    N  N N 322 
PRO CA   C  N S 323 
PRO C    C  N N 324 
PRO O    O  N N 325 
PRO CB   C  N N 326 
PRO CG   C  N N 327 
PRO CD   C  N N 328 
PRO OXT  O  N N 329 
PRO H    H  N N 330 
PRO HA   H  N N 331 
PRO HB2  H  N N 332 
PRO HB3  H  N N 333 
PRO HG2  H  N N 334 
PRO HG3  H  N N 335 
PRO HD2  H  N N 336 
PRO HD3  H  N N 337 
PRO HXT  H  N N 338 
SER N    N  N N 339 
SER CA   C  N S 340 
SER C    C  N N 341 
SER O    O  N N 342 
SER CB   C  N N 343 
SER OG   O  N N 344 
SER OXT  O  N N 345 
SER H    H  N N 346 
SER H2   H  N N 347 
SER HA   H  N N 348 
SER HB2  H  N N 349 
SER HB3  H  N N 350 
SER HG   H  N N 351 
SER HXT  H  N N 352 
THR N    N  N N 353 
THR CA   C  N S 354 
THR C    C  N N 355 
THR O    O  N N 356 
THR CB   C  N R 357 
THR OG1  O  N N 358 
THR CG2  C  N N 359 
THR OXT  O  N N 360 
THR H    H  N N 361 
THR H2   H  N N 362 
THR HA   H  N N 363 
THR HB   H  N N 364 
THR HG1  H  N N 365 
THR HG21 H  N N 366 
THR HG22 H  N N 367 
THR HG23 H  N N 368 
THR HXT  H  N N 369 
TRP N    N  N N 370 
TRP CA   C  N S 371 
TRP C    C  N N 372 
TRP O    O  N N 373 
TRP CB   C  N N 374 
TRP CG   C  Y N 375 
TRP CD1  C  Y N 376 
TRP CD2  C  Y N 377 
TRP NE1  N  Y N 378 
TRP CE2  C  Y N 379 
TRP CE3  C  Y N 380 
TRP CZ2  C  Y N 381 
TRP CZ3  C  Y N 382 
TRP CH2  C  Y N 383 
TRP OXT  O  N N 384 
TRP H    H  N N 385 
TRP H2   H  N N 386 
TRP HA   H  N N 387 
TRP HB2  H  N N 388 
TRP HB3  H  N N 389 
TRP HD1  H  N N 390 
TRP HE1  H  N N 391 
TRP HE3  H  N N 392 
TRP HZ2  H  N N 393 
TRP HZ3  H  N N 394 
TRP HH2  H  N N 395 
TRP HXT  H  N N 396 
TYR N    N  N N 397 
TYR CA   C  N S 398 
TYR C    C  N N 399 
TYR O    O  N N 400 
TYR CB   C  N N 401 
TYR CG   C  Y N 402 
TYR CD1  C  Y N 403 
TYR CD2  C  Y N 404 
TYR CE1  C  Y N 405 
TYR CE2  C  Y N 406 
TYR CZ   C  Y N 407 
TYR OH   O  N N 408 
TYR OXT  O  N N 409 
TYR H    H  N N 410 
TYR H2   H  N N 411 
TYR HA   H  N N 412 
TYR HB2  H  N N 413 
TYR HB3  H  N N 414 
TYR HD1  H  N N 415 
TYR HD2  H  N N 416 
TYR HE1  H  N N 417 
TYR HE2  H  N N 418 
TYR HH   H  N N 419 
TYR HXT  H  N N 420 
VAL N    N  N N 421 
VAL CA   C  N S 422 
VAL C    C  N N 423 
VAL O    O  N N 424 
VAL CB   C  N N 425 
VAL CG1  C  N N 426 
VAL CG2  C  N N 427 
VAL OXT  O  N N 428 
VAL H    H  N N 429 
VAL H2   H  N N 430 
VAL HA   H  N N 431 
VAL HB   H  N N 432 
VAL HG11 H  N N 433 
VAL HG12 H  N N 434 
VAL HG13 H  N N 435 
VAL HG21 H  N N 436 
VAL HG22 H  N N 437 
VAL HG23 H  N N 438 
VAL HXT  H  N N 439 
# 
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 
1CY C6   N1   sing N N 1   
1CY C2   N1   doub N N 2   
1CY N3   C2   sing N N 3   
1CY C2   N7   sing N N 4   
1CY C4   N3   doub N N 5   
1CY N8   C4   sing N N 6   
1CY C4   N5   sing N N 7   
1CY C11  N5   sing N N 8   
1CY N5   C6   sing N N 9   
1CY C6   C10  sing N N 10  
1CY C6   C9   sing N N 11  
1CY N7   HN7  sing N N 12  
1CY N7   HN7A sing N N 13  
1CY N8   HN8  sing N N 14  
1CY N8   HN8A sing N N 15  
1CY C9   H9   sing N N 16  
1CY C9   H9A  sing N N 17  
1CY C9   H9B  sing N N 18  
1CY C10  H10  sing N N 19  
1CY C10  H10A sing N N 20  
1CY C10  H10B sing N N 21  
1CY C16  C11  doub Y N 22  
1CY C12  C11  sing Y N 23  
1CY C13  C12  doub Y N 24  
1CY C12  H12  sing N N 25  
1CY C14  C13  sing Y N 26  
1CY C13  H13  sing N N 27  
1CY CL17 C14  sing N N 28  
1CY C14  C15  doub Y N 29  
1CY C15  C16  sing Y N 30  
1CY C15  H15  sing N N 31  
1CY C16  H16  sing N N 32  
ALA N    CA   sing N N 33  
ALA N    H    sing N N 34  
ALA N    H2   sing N N 35  
ALA CA   C    sing N N 36  
ALA CA   CB   sing N N 37  
ALA CA   HA   sing N N 38  
ALA C    O    doub N N 39  
ALA C    OXT  sing N N 40  
ALA CB   HB1  sing N N 41  
ALA CB   HB2  sing N N 42  
ALA CB   HB3  sing N N 43  
ALA OXT  HXT  sing N N 44  
ARG N    CA   sing N N 45  
ARG N    H    sing N N 46  
ARG N    H2   sing N N 47  
ARG CA   C    sing N N 48  
ARG CA   CB   sing N N 49  
ARG CA   HA   sing N N 50  
ARG C    O    doub N N 51  
ARG C    OXT  sing N N 52  
ARG CB   CG   sing N N 53  
ARG CB   HB2  sing N N 54  
ARG CB   HB3  sing N N 55  
ARG CG   CD   sing N N 56  
ARG CG   HG2  sing N N 57  
ARG CG   HG3  sing N N 58  
ARG CD   NE   sing N N 59  
ARG CD   HD2  sing N N 60  
ARG CD   HD3  sing N N 61  
ARG NE   CZ   sing N N 62  
ARG NE   HE   sing N N 63  
ARG CZ   NH1  sing N N 64  
ARG CZ   NH2  doub N N 65  
ARG NH1  HH11 sing N N 66  
ARG NH1  HH12 sing N N 67  
ARG NH2  HH21 sing N N 68  
ARG NH2  HH22 sing N N 69  
ARG OXT  HXT  sing N N 70  
ASN N    CA   sing N N 71  
ASN N    H    sing N N 72  
ASN N    H2   sing N N 73  
ASN CA   C    sing N N 74  
ASN CA   CB   sing N N 75  
ASN CA   HA   sing N N 76  
ASN C    O    doub N N 77  
ASN C    OXT  sing N N 78  
ASN CB   CG   sing N N 79  
ASN CB   HB2  sing N N 80  
ASN CB   HB3  sing N N 81  
ASN CG   OD1  doub N N 82  
ASN CG   ND2  sing N N 83  
ASN ND2  HD21 sing N N 84  
ASN ND2  HD22 sing N N 85  
ASN OXT  HXT  sing N N 86  
ASP N    CA   sing N N 87  
ASP N    H    sing N N 88  
ASP N    H2   sing N N 89  
ASP CA   C    sing N N 90  
ASP CA   CB   sing N N 91  
ASP CA   HA   sing N N 92  
ASP C    O    doub N N 93  
ASP C    OXT  sing N N 94  
ASP CB   CG   sing N N 95  
ASP CB   HB2  sing N N 96  
ASP CB   HB3  sing N N 97  
ASP CG   OD1  doub N N 98  
ASP CG   OD2  sing N N 99  
ASP OD2  HD2  sing N N 100 
ASP OXT  HXT  sing N N 101 
CYS N    CA   sing N N 102 
CYS N    H    sing N N 103 
CYS N    H2   sing N N 104 
CYS CA   C    sing N N 105 
CYS CA   CB   sing N N 106 
CYS CA   HA   sing N N 107 
CYS C    O    doub N N 108 
CYS C    OXT  sing N N 109 
CYS CB   SG   sing N N 110 
CYS CB   HB2  sing N N 111 
CYS CB   HB3  sing N N 112 
CYS SG   HG   sing N N 113 
CYS OXT  HXT  sing N N 114 
FLC CAC  CA   sing N N 115 
FLC CAC  OA1  doub N N 116 
FLC CAC  OA2  sing N N 117 
FLC CA   CB   sing N N 118 
FLC CA   HA1  sing N N 119 
FLC CA   HA2  sing N N 120 
FLC CB   CBC  sing N N 121 
FLC CB   CG   sing N N 122 
FLC CB   OHB  sing N N 123 
FLC CBC  OB1  doub N N 124 
FLC CBC  OB2  sing N N 125 
FLC CG   CGC  sing N N 126 
FLC CG   HG1  sing N N 127 
FLC CG   HG2  sing N N 128 
FLC CGC  OG1  doub N N 129 
FLC CGC  OG2  sing N N 130 
FLC OHB  HOB  sing N N 131 
GLN N    CA   sing N N 132 
GLN N    H    sing N N 133 
GLN N    H2   sing N N 134 
GLN CA   C    sing N N 135 
GLN CA   CB   sing N N 136 
GLN CA   HA   sing N N 137 
GLN C    O    doub N N 138 
GLN C    OXT  sing N N 139 
GLN CB   CG   sing N N 140 
GLN CB   HB2  sing N N 141 
GLN CB   HB3  sing N N 142 
GLN CG   CD   sing N N 143 
GLN CG   HG2  sing N N 144 
GLN CG   HG3  sing N N 145 
GLN CD   OE1  doub N N 146 
GLN CD   NE2  sing N N 147 
GLN NE2  HE21 sing N N 148 
GLN NE2  HE22 sing N N 149 
GLN OXT  HXT  sing N N 150 
GLU N    CA   sing N N 151 
GLU N    H    sing N N 152 
GLU N    H2   sing N N 153 
GLU CA   C    sing N N 154 
GLU CA   CB   sing N N 155 
GLU CA   HA   sing N N 156 
GLU C    O    doub N N 157 
GLU C    OXT  sing N N 158 
GLU CB   CG   sing N N 159 
GLU CB   HB2  sing N N 160 
GLU CB   HB3  sing N N 161 
GLU CG   CD   sing N N 162 
GLU CG   HG2  sing N N 163 
GLU CG   HG3  sing N N 164 
GLU CD   OE1  doub N N 165 
GLU CD   OE2  sing N N 166 
GLU OE2  HE2  sing N N 167 
GLU OXT  HXT  sing N N 168 
GLY N    CA   sing N N 169 
GLY N    H    sing N N 170 
GLY N    H2   sing N N 171 
GLY CA   C    sing N N 172 
GLY CA   HA2  sing N N 173 
GLY CA   HA3  sing N N 174 
GLY C    O    doub N N 175 
GLY C    OXT  sing N N 176 
GLY OXT  HXT  sing N N 177 
HIS N    CA   sing N N 178 
HIS N    H    sing N N 179 
HIS N    H2   sing N N 180 
HIS CA   C    sing N N 181 
HIS CA   CB   sing N N 182 
HIS CA   HA   sing N N 183 
HIS C    O    doub N N 184 
HIS C    OXT  sing N N 185 
HIS CB   CG   sing N N 186 
HIS CB   HB2  sing N N 187 
HIS CB   HB3  sing N N 188 
HIS CG   ND1  sing Y N 189 
HIS CG   CD2  doub Y N 190 
HIS ND1  CE1  doub Y N 191 
HIS ND1  HD1  sing N N 192 
HIS CD2  NE2  sing Y N 193 
HIS CD2  HD2  sing N N 194 
HIS CE1  NE2  sing Y N 195 
HIS CE1  HE1  sing N N 196 
HIS NE2  HE2  sing N N 197 
HIS OXT  HXT  sing N N 198 
HOH O    H1   sing N N 199 
HOH O    H2   sing N N 200 
ILE N    CA   sing N N 201 
ILE N    H    sing N N 202 
ILE N    H2   sing N N 203 
ILE CA   C    sing N N 204 
ILE CA   CB   sing N N 205 
ILE CA   HA   sing N N 206 
ILE C    O    doub N N 207 
ILE C    OXT  sing N N 208 
ILE CB   CG1  sing N N 209 
ILE CB   CG2  sing N N 210 
ILE CB   HB   sing N N 211 
ILE CG1  CD1  sing N N 212 
ILE CG1  HG12 sing N N 213 
ILE CG1  HG13 sing N N 214 
ILE CG2  HG21 sing N N 215 
ILE CG2  HG22 sing N N 216 
ILE CG2  HG23 sing N N 217 
ILE CD1  HD11 sing N N 218 
ILE CD1  HD12 sing N N 219 
ILE CD1  HD13 sing N N 220 
ILE OXT  HXT  sing N N 221 
LEU N    CA   sing N N 222 
LEU N    H    sing N N 223 
LEU N    H2   sing N N 224 
LEU CA   C    sing N N 225 
LEU CA   CB   sing N N 226 
LEU CA   HA   sing N N 227 
LEU C    O    doub N N 228 
LEU C    OXT  sing N N 229 
LEU CB   CG   sing N N 230 
LEU CB   HB2  sing N N 231 
LEU CB   HB3  sing N N 232 
LEU CG   CD1  sing N N 233 
LEU CG   CD2  sing N N 234 
LEU CG   HG   sing N N 235 
LEU CD1  HD11 sing N N 236 
LEU CD1  HD12 sing N N 237 
LEU CD1  HD13 sing N N 238 
LEU CD2  HD21 sing N N 239 
LEU CD2  HD22 sing N N 240 
LEU CD2  HD23 sing N N 241 
LEU OXT  HXT  sing N N 242 
LYS N    CA   sing N N 243 
LYS N    H    sing N N 244 
LYS N    H2   sing N N 245 
LYS CA   C    sing N N 246 
LYS CA   CB   sing N N 247 
LYS CA   HA   sing N N 248 
LYS C    O    doub N N 249 
LYS C    OXT  sing N N 250 
LYS CB   CG   sing N N 251 
LYS CB   HB2  sing N N 252 
LYS CB   HB3  sing N N 253 
LYS CG   CD   sing N N 254 
LYS CG   HG2  sing N N 255 
LYS CG   HG3  sing N N 256 
LYS CD   CE   sing N N 257 
LYS CD   HD2  sing N N 258 
LYS CD   HD3  sing N N 259 
LYS CE   NZ   sing N N 260 
LYS CE   HE2  sing N N 261 
LYS CE   HE3  sing N N 262 
LYS NZ   HZ1  sing N N 263 
LYS NZ   HZ2  sing N N 264 
LYS NZ   HZ3  sing N N 265 
LYS OXT  HXT  sing N N 266 
MET N    CA   sing N N 267 
MET N    H    sing N N 268 
MET N    H2   sing N N 269 
MET CA   C    sing N N 270 
MET CA   CB   sing N N 271 
MET CA   HA   sing N N 272 
MET C    O    doub N N 273 
MET C    OXT  sing N N 274 
MET CB   CG   sing N N 275 
MET CB   HB2  sing N N 276 
MET CB   HB3  sing N N 277 
MET CG   SD   sing N N 278 
MET CG   HG2  sing N N 279 
MET CG   HG3  sing N N 280 
MET SD   CE   sing N N 281 
MET CE   HE1  sing N N 282 
MET CE   HE2  sing N N 283 
MET CE   HE3  sing N N 284 
MET OXT  HXT  sing N N 285 
PHE N    CA   sing N N 286 
PHE N    H    sing N N 287 
PHE N    H2   sing N N 288 
PHE CA   C    sing N N 289 
PHE CA   CB   sing N N 290 
PHE CA   HA   sing N N 291 
PHE C    O    doub N N 292 
PHE C    OXT  sing N N 293 
PHE CB   CG   sing N N 294 
PHE CB   HB2  sing N N 295 
PHE CB   HB3  sing N N 296 
PHE CG   CD1  doub Y N 297 
PHE CG   CD2  sing Y N 298 
PHE CD1  CE1  sing Y N 299 
PHE CD1  HD1  sing N N 300 
PHE CD2  CE2  doub Y N 301 
PHE CD2  HD2  sing N N 302 
PHE CE1  CZ   doub Y N 303 
PHE CE1  HE1  sing N N 304 
PHE CE2  CZ   sing Y N 305 
PHE CE2  HE2  sing N N 306 
PHE CZ   HZ   sing N N 307 
PHE OXT  HXT  sing N N 308 
PRO N    CA   sing N N 309 
PRO N    CD   sing N N 310 
PRO N    H    sing N N 311 
PRO CA   C    sing N N 312 
PRO CA   CB   sing N N 313 
PRO CA   HA   sing N N 314 
PRO C    O    doub N N 315 
PRO C    OXT  sing N N 316 
PRO CB   CG   sing N N 317 
PRO CB   HB2  sing N N 318 
PRO CB   HB3  sing N N 319 
PRO CG   CD   sing N N 320 
PRO CG   HG2  sing N N 321 
PRO CG   HG3  sing N N 322 
PRO CD   HD2  sing N N 323 
PRO CD   HD3  sing N N 324 
PRO OXT  HXT  sing N N 325 
SER N    CA   sing N N 326 
SER N    H    sing N N 327 
SER N    H2   sing N N 328 
SER CA   C    sing N N 329 
SER CA   CB   sing N N 330 
SER CA   HA   sing N N 331 
SER C    O    doub N N 332 
SER C    OXT  sing N N 333 
SER CB   OG   sing N N 334 
SER CB   HB2  sing N N 335 
SER CB   HB3  sing N N 336 
SER OG   HG   sing N N 337 
SER OXT  HXT  sing N N 338 
THR N    CA   sing N N 339 
THR N    H    sing N N 340 
THR N    H2   sing N N 341 
THR CA   C    sing N N 342 
THR CA   CB   sing N N 343 
THR CA   HA   sing N N 344 
THR C    O    doub N N 345 
THR C    OXT  sing N N 346 
THR CB   OG1  sing N N 347 
THR CB   CG2  sing N N 348 
THR CB   HB   sing N N 349 
THR OG1  HG1  sing N N 350 
THR CG2  HG21 sing N N 351 
THR CG2  HG22 sing N N 352 
THR CG2  HG23 sing N N 353 
THR OXT  HXT  sing N N 354 
TRP N    CA   sing N N 355 
TRP N    H    sing N N 356 
TRP N    H2   sing N N 357 
TRP CA   C    sing N N 358 
TRP CA   CB   sing N N 359 
TRP CA   HA   sing N N 360 
TRP C    O    doub N N 361 
TRP C    OXT  sing N N 362 
TRP CB   CG   sing N N 363 
TRP CB   HB2  sing N N 364 
TRP CB   HB3  sing N N 365 
TRP CG   CD1  doub Y N 366 
TRP CG   CD2  sing Y N 367 
TRP CD1  NE1  sing Y N 368 
TRP CD1  HD1  sing N N 369 
TRP CD2  CE2  doub Y N 370 
TRP CD2  CE3  sing Y N 371 
TRP NE1  CE2  sing Y N 372 
TRP NE1  HE1  sing N N 373 
TRP CE2  CZ2  sing Y N 374 
TRP CE3  CZ3  doub Y N 375 
TRP CE3  HE3  sing N N 376 
TRP CZ2  CH2  doub Y N 377 
TRP CZ2  HZ2  sing N N 378 
TRP CZ3  CH2  sing Y N 379 
TRP CZ3  HZ3  sing N N 380 
TRP CH2  HH2  sing N N 381 
TRP OXT  HXT  sing N N 382 
TYR N    CA   sing N N 383 
TYR N    H    sing N N 384 
TYR N    H2   sing N N 385 
TYR CA   C    sing N N 386 
TYR CA   CB   sing N N 387 
TYR CA   HA   sing N N 388 
TYR C    O    doub N N 389 
TYR C    OXT  sing N N 390 
TYR CB   CG   sing N N 391 
TYR CB   HB2  sing N N 392 
TYR CB   HB3  sing N N 393 
TYR CG   CD1  doub Y N 394 
TYR CG   CD2  sing Y N 395 
TYR CD1  CE1  sing Y N 396 
TYR CD1  HD1  sing N N 397 
TYR CD2  CE2  doub Y N 398 
TYR CD2  HD2  sing N N 399 
TYR CE1  CZ   doub Y N 400 
TYR CE1  HE1  sing N N 401 
TYR CE2  CZ   sing Y N 402 
TYR CE2  HE2  sing N N 403 
TYR CZ   OH   sing N N 404 
TYR OH   HH   sing N N 405 
TYR OXT  HXT  sing N N 406 
VAL N    CA   sing N N 407 
VAL N    H    sing N N 408 
VAL N    H2   sing N N 409 
VAL CA   C    sing N N 410 
VAL CA   CB   sing N N 411 
VAL CA   HA   sing N N 412 
VAL C    O    doub N N 413 
VAL C    OXT  sing N N 414 
VAL CB   CG1  sing N N 415 
VAL CB   CG2  sing N N 416 
VAL CB   HB   sing N N 417 
VAL CG1  HG11 sing N N 418 
VAL CG1  HG12 sing N N 419 
VAL CG1  HG13 sing N N 420 
VAL CG2  HG21 sing N N 421 
VAL CG2  HG22 sing N N 422 
VAL CG2  HG23 sing N N 423 
VAL OXT  HXT  sing N N 424 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)'        'United States' 1P30GM124169 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 1R01AI171514 2 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 2U01AI123394 3 
# 
_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   1DDR 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DAR 
_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]   0.014689 
_atom_sites.fract_transf_matrix[1][2]   0.008481 
_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]   0.016962 
_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]   0.004704 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . SER A 1 1   ? -36.147 27.631 9.685   1.00 80.65  ? -1  SER A N    1 
ATOM   2    C  CA   . SER A 1 1   ? -35.034 28.578 9.762   1.00 75.58  ? -1  SER A CA   1 
ATOM   3    C  C    . SER A 1 1   ? -33.708 27.887 10.115  1.00 74.41  ? -1  SER A C    1 
ATOM   4    O  O    . SER A 1 1   ? -33.679 26.740 10.557  1.00 77.45  ? -1  SER A O    1 
ATOM   5    C  CB   . SER A 1 1   ? -35.348 29.678 10.772  1.00 80.42  ? -1  SER A CB   1 
ATOM   6    O  OG   . SER A 1 1   ? -35.063 29.244 12.088  1.00 92.00  ? -1  SER A OG   1 
ATOM   7    N  N    . HIS A 1 2   ? -32.600 28.593 9.911   1.00 82.14  ? 0   HIS A N    1 
ATOM   8    C  CA   . HIS A 1 2   ? -31.271 27.984 10.001  1.00 79.57  ? 0   HIS A CA   1 
ATOM   9    C  C    . HIS A 1 2   ? -31.210 26.733 9.132   1.00 75.02  ? 0   HIS A C    1 
ATOM   10   O  O    . HIS A 1 2   ? -30.510 25.772 9.456   1.00 78.42  ? 0   HIS A O    1 
ATOM   11   C  CB   . HIS A 1 2   ? -30.880 27.639 11.448  1.00 79.11  ? 0   HIS A CB   1 
ATOM   12   C  CG   . HIS A 1 2   ? -31.065 28.761 12.428  1.00 82.58  ? 0   HIS A CG   1 
ATOM   13   N  ND1  . HIS A 1 2   ? -30.838 28.607 13.780  1.00 88.62  ? 0   HIS A ND1  1 
ATOM   14   C  CD2  . HIS A 1 2   ? -31.484 30.041 12.265  1.00 83.48  ? 0   HIS A CD2  1 
ATOM   15   C  CE1  . HIS A 1 2   ? -31.091 29.745 14.405  1.00 86.30  ? 0   HIS A CE1  1 
ATOM   16   N  NE2  . HIS A 1 2   ? -31.487 30.631 13.508  1.00 85.99  ? 0   HIS A NE2  1 
ATOM   17   N  N    . MET A 1 3   ? -31.967 26.732 8.033   1.00 67.17  ? 1   MET A N    1 
ATOM   18   C  CA   . MET A 1 3   ? -32.016 25.582 7.142   1.00 58.54  ? 1   MET A CA   1 
ATOM   19   C  C    . MET A 1 3   ? -30.658 25.343 6.474   1.00 54.15  ? 1   MET A C    1 
ATOM   20   O  O    . MET A 1 3   ? -29.987 26.278 6.025   1.00 51.56  ? 1   MET A O    1 
ATOM   21   C  CB   . MET A 1 3   ? -33.098 25.804 6.088   1.00 51.51  ? 1   MET A CB   1 
ATOM   22   C  CG   . MET A 1 3   ? -32.833 24.998 4.826   1.00 59.93  ? 1   MET A CG   1 
ATOM   23   S  SD   . MET A 1 3   ? -34.162 25.017 3.612   1.00 62.23  ? 1   MET A SD   1 
ATOM   24   C  CE   . MET A 1 3   ? -33.922 26.603 2.801   1.00 50.46  ? 1   MET A CE   1 
ATOM   25   N  N    . ILE A 1 4   ? -30.242 24.080 6.408   1.00 51.79  ? 2   ILE A N    1 
ATOM   26   C  CA   . ILE A 1 4   ? -28.947 23.718 5.837   1.00 49.88  ? 2   ILE A CA   1 
ATOM   27   C  C    . ILE A 1 4   ? -29.135 23.281 4.390   1.00 48.01  ? 2   ILE A C    1 
ATOM   28   O  O    . ILE A 1 4   ? -29.999 22.439 4.086   1.00 46.04  ? 2   ILE A O    1 
ATOM   29   C  CB   . ILE A 1 4   ? -28.257 22.601 6.637   1.00 50.36  ? 2   ILE A CB   1 
ATOM   30   C  CG1  . ILE A 1 4   ? -28.140 22.937 8.130   1.00 55.74  ? 2   ILE A CG1  1 
ATOM   31   C  CG2  . ILE A 1 4   ? -26.881 22.331 6.052   1.00 44.37  ? 2   ILE A CG2  1 
ATOM   32   C  CD1  . ILE A 1 4   ? -27.320 24.148 8.421   1.00 53.50  ? 2   ILE A CD1  1 
ATOM   33   N  N    . SER A 1 5   ? -28.297 23.823 3.504   1.00 42.13  ? 3   SER A N    1 
ATOM   34   C  CA   . SER A 1 5   ? -28.350 23.529 2.075   1.00 42.57  ? 3   SER A CA   1 
ATOM   35   C  C    . SER A 1 5   ? -26.955 23.157 1.601   1.00 40.15  ? 3   SER A C    1 
ATOM   36   O  O    . SER A 1 5   ? -25.952 23.683 2.105   1.00 40.25  ? 3   SER A O    1 
ATOM   37   C  CB   . SER A 1 5   ? -28.841 24.735 1.271   1.00 40.27  ? 3   SER A CB   1 
ATOM   38   O  OG   . SER A 1 5   ? -30.202 25.021 1.528   1.00 41.69  ? 3   SER A OG   1 
ATOM   39   N  N    . LEU A 1 6   ? -26.899 22.245 0.640   1.00 37.05  ? 4   LEU A N    1 
ATOM   40   C  CA   . LEU A 1 6   ? -25.663 21.862 -0.032  1.00 38.99  ? 4   LEU A CA   1 
ATOM   41   C  C    . LEU A 1 6   ? -25.730 22.359 -1.473  1.00 39.70  ? 4   LEU A C    1 
ATOM   42   O  O    . LEU A 1 6   ? -26.762 22.188 -2.136  1.00 35.67  ? 4   LEU A O    1 
ATOM   43   C  CB   . LEU A 1 6   ? -25.500 20.344 -0.014  1.00 37.31  ? 4   LEU A CB   1 
ATOM   44   C  CG   . LEU A 1 6   ? -24.839 19.660 1.173   1.00 42.81  ? 4   LEU A CG   1 
ATOM   45   C  CD1  . LEU A 1 6   ? -25.484 20.101 2.466   1.00 38.71  ? 4   LEU A CD1  1 
ATOM   46   C  CD2  . LEU A 1 6   ? -25.013 18.186 0.991   1.00 38.80  ? 4   LEU A CD2  1 
ATOM   47   N  N    . ILE A 1 7   ? -24.647 22.966 -1.964  1.00 36.39  ? 5   ILE A N    1 
ATOM   48   C  CA   . ILE A 1 7   ? -24.575 23.377 -3.361  1.00 37.87  ? 5   ILE A CA   1 
ATOM   49   C  C    . ILE A 1 7   ? -23.289 22.836 -3.986  1.00 39.46  ? 5   ILE A C    1 
ATOM   50   O  O    . ILE A 1 7   ? -22.185 23.118 -3.495  1.00 39.76  ? 5   ILE A O    1 
ATOM   51   C  CB   . ILE A 1 7   ? -24.686 24.902 -3.514  1.00 37.27  ? 5   ILE A CB   1 
ATOM   52   C  CG1  . ILE A 1 7   ? -24.671 25.281 -5.003  1.00 36.82  ? 5   ILE A CG1  1 
ATOM   53   C  CG2  . ILE A 1 7   ? -23.647 25.622 -2.677  1.00 38.57  ? 5   ILE A CG2  1 
ATOM   54   C  CD1  . ILE A 1 7   ? -25.132 26.695 -5.274  1.00 38.54  ? 5   ILE A CD1  1 
ATOM   55   N  N    . ALA A 1 8   ? -23.430 22.046 -5.060  1.00 36.98  ? 6   ALA A N    1 
ATOM   56   C  CA   . ALA A 1 8   ? -22.296 21.349 -5.663  1.00 37.10  ? 6   ALA A CA   1 
ATOM   57   C  C    . ALA A 1 8   ? -22.435 21.293 -7.180  1.00 41.10  ? 6   ALA A C    1 
ATOM   58   O  O    . ALA A 1 8   ? -23.548 21.351 -7.723  1.00 38.64  ? 6   ALA A O    1 
ATOM   59   C  CB   . ALA A 1 8   ? -22.171 19.915 -5.133  1.00 36.91  ? 6   ALA A CB   1 
ATOM   60   N  N    . ALA A 1 9   ? -21.291 21.178 -7.859  1.00 42.91  ? 7   ALA A N    1 
ATOM   61   C  CA   . ALA A 1 9   ? -21.233 20.904 -9.290  1.00 44.25  ? 7   ALA A CA   1 
ATOM   62   C  C    . ALA A 1 9   ? -20.751 19.477 -9.468  1.00 46.75  ? 7   ALA A C    1 
ATOM   63   O  O    . ALA A 1 9   ? -19.725 19.096 -8.902  1.00 47.64  ? 7   ALA A O    1 
ATOM   64   C  CB   . ALA A 1 9   ? -20.300 21.874 -10.013 1.00 42.61  ? 7   ALA A CB   1 
ATOM   65   N  N    . LEU A 1 10  ? -21.493 18.685 -10.234 1.00 45.86  ? 8   LEU A N    1 
ATOM   66   C  CA   . LEU A 1 10  ? -21.227 17.259 -10.346 1.00 48.09  ? 8   LEU A CA   1 
ATOM   67   C  C    . LEU A 1 10  ? -20.972 16.916 -11.801 1.00 49.30  ? 8   LEU A C    1 
ATOM   68   O  O    . LEU A 1 10  ? -21.664 17.412 -12.692 1.00 49.39  ? 8   LEU A O    1 
ATOM   69   C  CB   . LEU A 1 10  ? -22.405 16.435 -9.824  1.00 49.78  ? 8   LEU A CB   1 
ATOM   70   C  CG   . LEU A 1 10  ? -22.742 16.626 -8.338  1.00 48.76  ? 8   LEU A CG   1 
ATOM   71   C  CD1  . LEU A 1 10  ? -23.755 15.593 -7.931  1.00 49.12  ? 8   LEU A CD1  1 
ATOM   72   C  CD2  . LEU A 1 10  ? -21.512 16.570 -7.433  1.00 51.63  ? 8   LEU A CD2  1 
ATOM   73   N  N    . ALA A 1 11  ? -19.962 16.101 -12.044 1.00 52.92  ? 9   ALA A N    1 
ATOM   74   C  CA   . ALA A 1 11  ? -19.784 15.449 -13.331 1.00 52.31  ? 9   ALA A CA   1 
ATOM   75   C  C    . ALA A 1 11  ? -19.946 13.967 -13.041 1.00 61.46  ? 9   ALA A C    1 
ATOM   76   O  O    . ALA A 1 11  ? -19.007 13.333 -12.555 1.00 71.72  ? 9   ALA A O    1 
ATOM   77   C  CB   . ALA A 1 11  ? -18.422 15.755 -13.944 1.00 55.97  ? 9   ALA A CB   1 
ATOM   78   N  N    . VAL A 1 12  ? -21.140 13.422 -13.285 1.00 62.87  ? 10  VAL A N    1 
ATOM   79   C  CA   . VAL A 1 12  ? -21.381 11.996 -13.076 1.00 68.37  ? 10  VAL A CA   1 
ATOM   80   C  C    . VAL A 1 12  ? -21.096 11.574 -11.634 1.00 80.08  ? 10  VAL A C    1 
ATOM   81   O  O    . VAL A 1 12  ? -20.394 10.577 -11.401 1.00 81.76  ? 10  VAL A O    1 
ATOM   82   C  CB   . VAL A 1 12  ? -20.517 11.144 -14.012 1.00 63.66  ? 10  VAL A CB   1 
ATOM   83   C  CG1  . VAL A 1 12  ? -20.817 9.666  -13.776 1.00 72.12  ? 10  VAL A CG1  1 
ATOM   84   C  CG2  . VAL A 1 12  ? -20.681 11.568 -15.474 1.00 64.10  ? 10  VAL A CG2  1 
ATOM   85   N  N    . ASP A 1 13  ? -21.617 12.330 -10.667 1.00 64.50  ? 11  ASP A N    1 
ATOM   86   C  CA   A ASP A 1 13  ? -21.459 12.068 -9.228  0.52 65.95  ? 11  ASP A CA   1 
ATOM   87   C  CA   B ASP A 1 13  ? -21.476 12.138 -9.221  0.48 66.30  ? 11  ASP A CA   1 
ATOM   88   C  C    . ASP A 1 13  ? -20.079 12.447 -8.681  1.00 62.96  ? 11  ASP A C    1 
ATOM   89   O  O    . ASP A 1 13  ? -19.861 12.327 -7.474  1.00 63.43  ? 11  ASP A O    1 
ATOM   90   C  CB   A ASP A 1 13  ? -21.744 10.599 -8.862  0.52 67.43  ? 11  ASP A CB   1 
ATOM   91   C  CB   B ASP A 1 13  ? -21.932 10.737 -8.758  0.48 67.49  ? 11  ASP A CB   1 
ATOM   92   C  CG   A ASP A 1 13  ? -22.489 10.456 -7.534  0.52 65.13  ? 11  ASP A CG   1 
ATOM   93   C  CG   B ASP A 1 13  ? -20.981 9.614  -9.150  0.48 67.87  ? 11  ASP A CG   1 
ATOM   94   O  OD1  A ASP A 1 13  ? -23.597 11.017 -7.406  0.52 65.65  ? 11  ASP A OD1  1 
ATOM   95   O  OD1  B ASP A 1 13  ? -19.785 9.668  -8.807  0.48 70.04  ? 11  ASP A OD1  1 
ATOM   96   O  OD2  A ASP A 1 13  ? -21.985 9.764  -6.626  0.52 64.17  ? 11  ASP A OD2  1 
ATOM   97   O  OD2  B ASP A 1 13  ? -21.443 8.659  -9.808  0.48 69.03  ? 11  ASP A OD2  1 
ATOM   98   N  N    . ARG A 1 14  ? -19.139 12.907 -9.503  1.00 60.77  ? 12  ARG A N    1 
ATOM   99   C  CA   . ARG A 1 14  ? -17.836 13.324 -8.988  1.00 63.76  ? 12  ARG A CA   1 
ATOM   100  C  C    . ARG A 1 14  ? -17.798 14.836 -8.770  1.00 59.98  ? 12  ARG A C    1 
ATOM   101  O  O    . ARG A 1 14  ? -18.234 15.600 -9.633  1.00 60.38  ? 12  ARG A O    1 
ATOM   102  C  CB   . ARG A 1 14  ? -16.722 12.858 -9.923  1.00 62.29  ? 12  ARG A CB   1 
ATOM   103  C  CG   . ARG A 1 14  ? -16.345 11.457 -9.571  1.00 67.77  ? 12  ARG A CG   1 
ATOM   104  C  CD   . ARG A 1 14  ? -15.480 10.747 -10.572 1.00 80.35  ? 12  ARG A CD   1 
ATOM   105  N  NE   . ARG A 1 14  ? -15.405 9.340  -10.172 1.00 85.61  ? 12  ARG A NE   1 
ATOM   106  C  CZ   . ARG A 1 14  ? -14.596 8.423  -10.692 1.00 86.85  ? 12  ARG A CZ   1 
ATOM   107  N  NH1  . ARG A 1 14  ? -13.760 8.732  -11.677 1.00 90.84  ? 12  ARG A NH1  1 
ATOM   108  N  NH2  . ARG A 1 14  ? -14.635 7.182  -10.221 1.00 89.40  ? 12  ARG A NH2  1 
ATOM   109  N  N    . VAL A 1 15  ? -17.279 15.263 -7.618  1.00 62.87  ? 13  VAL A N    1 
ATOM   110  C  CA   . VAL A 1 15  ? -17.394 16.654 -7.176  1.00 60.01  ? 13  VAL A CA   1 
ATOM   111  C  C    . VAL A 1 15  ? -16.340 17.517 -7.863  1.00 63.90  ? 13  VAL A C    1 
ATOM   112  O  O    . VAL A 1 15  ? -15.144 17.179 -7.877  1.00 56.79  ? 13  VAL A O    1 
ATOM   113  C  CB   . VAL A 1 15  ? -17.267 16.749 -5.648  1.00 61.28  ? 13  VAL A CB   1 
ATOM   114  C  CG1  . VAL A 1 15  ? -17.166 18.223 -5.194  1.00 55.58  ? 13  VAL A CG1  1 
ATOM   115  C  CG2  . VAL A 1 15  ? -18.453 16.067 -4.986  1.00 63.20  ? 13  VAL A CG2  1 
ATOM   116  N  N    . ILE A 1 16  ? -16.786 18.652 -8.420  1.00 64.35  ? 14  ILE A N    1 
ATOM   117  C  CA   . ILE A 1 16  ? -15.935 19.615 -9.120  1.00 69.84  ? 14  ILE A CA   1 
ATOM   118  C  C    . ILE A 1 16  ? -15.754 20.842 -8.236  1.00 70.35  ? 14  ILE A C    1 
ATOM   119  O  O    . ILE A 1 16  ? -16.736 21.411 -7.751  1.00 64.82  ? 14  ILE A O    1 
ATOM   120  C  CB   . ILE A 1 16  ? -16.522 20.017 -10.491 1.00 68.70  ? 14  ILE A CB   1 
ATOM   121  C  CG1  . ILE A 1 16  ? -16.651 18.806 -11.414 1.00 60.28  ? 14  ILE A CG1  1 
ATOM   122  C  CG2  . ILE A 1 16  ? -15.691 21.118 -11.158 1.00 78.78  ? 14  ILE A CG2  1 
ATOM   123  C  CD1  . ILE A 1 16  ? -17.848 18.881 -12.288 1.00 55.73  ? 14  ILE A CD1  1 
ATOM   124  N  N    . GLY A 1 17  ? -14.500 21.246 -8.027  1.00 75.81  ? 15  GLY A N    1 
ATOM   125  C  CA   . GLY A 1 17  ? -14.184 22.438 -7.277  1.00 77.43  ? 15  GLY A CA   1 
ATOM   126  C  C    . GLY A 1 17  ? -13.353 23.402 -8.110  1.00 89.55  ? 15  GLY A C    1 
ATOM   127  O  O    . GLY A 1 17  ? -13.026 23.137 -9.266  1.00 94.30  ? 15  GLY A O    1 
ATOM   128  N  N    . MET A 1 18  ? -13.017 24.533 -7.487  1.00 86.18  ? 16  MET A N    1 
ATOM   129  C  CA   . MET A 1 18  ? -12.189 25.530 -8.156  1.00 87.55  ? 16  MET A CA   1 
ATOM   130  C  C    . MET A 1 18  ? -10.826 24.983 -8.534  1.00 93.68  ? 16  MET A C    1 
ATOM   131  O  O    . MET A 1 18  ? -10.111 25.626 -9.310  1.00 99.37  ? 16  MET A O    1 
ATOM   132  C  CB   . MET A 1 18  ? -12.031 26.762 -7.257  1.00 79.98  ? 16  MET A CB   1 
ATOM   133  C  CG   . MET A 1 18  ? -13.365 27.220 -6.709  1.00 79.75  ? 16  MET A CG   1 
ATOM   134  S  SD   . MET A 1 18  ? -14.462 27.809 -8.020  1.00 83.12  ? 16  MET A SD   1 
ATOM   135  C  CE   . MET A 1 18  ? -13.791 29.442 -8.294  1.00 89.20  ? 16  MET A CE   1 
ATOM   136  N  N    . GLU A 1 19  ? -10.450 23.816 -8.005  1.00 97.66  ? 17  GLU A N    1 
ATOM   137  C  CA   . GLU A 1 19  ? -9.142  23.252 -8.314  1.00 103.62 ? 17  GLU A CA   1 
ATOM   138  C  C    . GLU A 1 19  ? -9.055  22.858 -9.782  1.00 106.79 ? 17  GLU A C    1 
ATOM   139  O  O    . GLU A 1 19  ? -7.979  22.941 -10.385 1.00 108.14 ? 17  GLU A O    1 
ATOM   140  C  CB   . GLU A 1 19  ? -8.864  22.038 -7.417  1.00 104.75 ? 17  GLU A CB   1 
ATOM   141  C  CG   . GLU A 1 19  ? -9.018  22.282 -5.900  1.00 100.71 ? 17  GLU A CG   1 
ATOM   142  C  CD   . GLU A 1 19  ? -10.441 21.988 -5.391  1.00 102.41 ? 17  GLU A CD   1 
ATOM   143  O  OE1  . GLU A 1 19  ? -11.269 21.510 -6.203  1.00 106.35 ? 17  GLU A OE1  1 
ATOM   144  O  OE2  . GLU A 1 19  ? -10.732 22.223 -4.186  1.00 91.26  ? 17  GLU A OE2  1 
ATOM   145  N  N    . ASN A 1 20  ? -10.201 22.513 -10.371 1.00 111.60 ? 18  ASN A N    1 
ATOM   146  C  CA   . ASN A 1 20  ? -10.226 22.094 -11.797 1.00 116.05 ? 18  ASN A CA   1 
ATOM   147  C  C    . ASN A 1 20  ? -10.481 23.305 -12.699 1.00 113.60 ? 18  ASN A C    1 
ATOM   148  O  O    . ASN A 1 20  ? -11.002 24.316 -12.196 1.00 112.60 ? 18  ASN A O    1 
ATOM   149  C  CB   . ASN A 1 20  ? -11.237 20.975 -12.052 1.00 111.46 ? 18  ASN A CB   1 
ATOM   150  C  CG   . ASN A 1 20  ? -11.312 19.975 -10.918 1.00 112.23 ? 18  ASN A CG   1 
ATOM   151  O  OD1  . ASN A 1 20  ? -12.386 19.717 -10.382 1.00 102.48 ? 18  ASN A OD1  1 
ATOM   152  N  ND2  . ASN A 1 20  ? -10.176 19.407 -10.549 1.00 116.82 ? 18  ASN A ND2  1 
ATOM   153  N  N    . ALA A 1 21  ? -10.079 23.215 -13.969 1.00 110.37 ? 19  ALA A N    1 
ATOM   154  C  CA   . ALA A 1 21  ? -10.305 24.304 -14.947 1.00 107.56 ? 19  ALA A CA   1 
ATOM   155  C  C    . ALA A 1 21  ? -11.785 24.419 -15.305 1.00 110.41 ? 19  ALA A C    1 
ATOM   156  O  O    . ALA A 1 21  ? -12.212 25.517 -15.698 1.00 112.14 ? 19  ALA A O    1 
ATOM   157  C  CB   . ALA A 1 21  ? -9.489  24.029 -16.182 1.00 98.49  ? 19  ALA A CB   1 
ATOM   158  N  N    . MET A 1 22  ? -12.535 23.327 -15.187 1.00 106.71 ? 20  MET A N    1 
ATOM   159  C  CA   . MET A 1 22  ? -13.943 23.328 -15.661 1.00 106.63 ? 20  MET A CA   1 
ATOM   160  C  C    . MET A 1 22  ? -14.826 24.357 -14.942 1.00 106.32 ? 20  MET A C    1 
ATOM   161  O  O    . MET A 1 22  ? -15.680 24.924 -15.634 1.00 105.66 ? 20  MET A O    1 
ATOM   162  C  CB   . MET A 1 22  ? -14.559 21.935 -15.525 1.00 102.02 ? 20  MET A CB   1 
ATOM   163  C  CG   . MET A 1 22  ? -15.028 21.359 -16.833 1.00 95.22  ? 20  MET A CG   1 
ATOM   164  S  SD   . MET A 1 22  ? -16.383 20.234 -16.490 1.00 100.07 ? 20  MET A SD   1 
ATOM   165  C  CE   . MET A 1 22  ? -16.811 20.769 -14.836 1.00 82.95  ? 20  MET A CE   1 
ATOM   166  N  N    . PRO A 1 23  ? -14.749 24.586 -13.613 1.00 104.37 ? 21  PRO A N    1 
ATOM   167  C  CA   . PRO A 1 23  ? -15.581 25.611 -12.986 1.00 101.32 ? 21  PRO A CA   1 
ATOM   168  C  C    . PRO A 1 23  ? -15.505 26.908 -13.790 1.00 98.04  ? 21  PRO A C    1 
ATOM   169  O  O    . PRO A 1 23  ? -16.524 27.409 -14.196 1.00 92.58  ? 21  PRO A O    1 
ATOM   170  C  CB   . PRO A 1 23  ? -14.905 25.782 -11.628 1.00 90.84  ? 21  PRO A CB   1 
ATOM   171  C  CG   . PRO A 1 23  ? -14.442 24.391 -11.314 1.00 93.21  ? 21  PRO A CG   1 
ATOM   172  C  CD   . PRO A 1 23  ? -13.950 23.846 -12.638 1.00 102.70 ? 21  PRO A CD   1 
ATOM   173  N  N    . TRP A 1 24  ? -14.293 27.400 -14.009 1.00 107.75 ? 22  TRP A N    1 
ATOM   174  C  CA   . TRP A 1 24  ? -14.103 28.619 -14.780 1.00 107.84 ? 22  TRP A CA   1 
ATOM   175  C  C    . TRP A 1 24  ? -14.567 28.454 -16.225 1.00 105.16 ? 22  TRP A C    1 
ATOM   176  O  O    . TRP A 1 24  ? -14.915 29.447 -16.874 1.00 100.33 ? 22  TRP A O    1 
ATOM   177  C  CB   . TRP A 1 24  ? -12.634 29.028 -14.726 1.00 112.35 ? 22  TRP A CB   1 
ATOM   178  C  CG   . TRP A 1 24  ? -12.044 29.033 -13.329 1.00 119.21 ? 22  TRP A CG   1 
ATOM   179  C  CD1  . TRP A 1 24  ? -11.165 28.120 -12.816 1.00 120.01 ? 22  TRP A CD1  1 
ATOM   180  C  CD2  . TRP A 1 24  ? -12.256 30.014 -12.286 1.00 123.80 ? 22  TRP A CD2  1 
ATOM   181  N  NE1  . TRP A 1 24  ? -10.833 28.455 -11.521 1.00 127.16 ? 22  TRP A NE1  1 
ATOM   182  C  CE2  . TRP A 1 24  ? -11.483 29.613 -11.173 1.00 124.85 ? 22  TRP A CE2  1 
ATOM   183  C  CE3  . TRP A 1 24  ? -13.025 31.186 -12.186 1.00 117.38 ? 22  TRP A CE3  1 
ATOM   184  C  CZ2  . TRP A 1 24  ? -11.450 30.346 -9.978  1.00 119.27 ? 22  TRP A CZ2  1 
ATOM   185  C  CZ3  . TRP A 1 24  ? -12.997 31.906 -10.994 1.00 111.21 ? 22  TRP A CZ3  1 
ATOM   186  C  CH2  . TRP A 1 24  ? -12.214 31.483 -9.910  1.00 117.03 ? 22  TRP A CH2  1 
ATOM   187  N  N    . ASN A 1 25  ? -14.573 27.222 -16.748 1.00 113.25 ? 23  ASN A N    1 
ATOM   188  C  CA   . ASN A 1 25  ? -15.074 26.953 -18.097 1.00 108.90 ? 23  ASN A CA   1 
ATOM   189  C  C    . ASN A 1 25  ? -16.598 26.899 -18.183 1.00 101.50 ? 23  ASN A C    1 
ATOM   190  O  O    . ASN A 1 25  ? -17.124 26.789 -19.300 1.00 92.53  ? 23  ASN A O    1 
ATOM   191  C  CB   . ASN A 1 25  ? -14.489 25.644 -18.650 1.00 107.16 ? 23  ASN A CB   1 
ATOM   192  C  CG   . ASN A 1 25  ? -13.076 25.816 -19.198 1.00 109.97 ? 23  ASN A CG   1 
ATOM   193  O  OD1  . ASN A 1 25  ? -12.462 26.874 -19.039 1.00 109.69 ? 23  ASN A OD1  1 
ATOM   194  N  ND2  . ASN A 1 25  ? -12.573 24.791 -19.883 1.00 110.01 ? 23  ASN A ND2  1 
ATOM   195  N  N    . LEU A 1 26  ? -17.311 26.965 -17.041 1.00 86.09  ? 24  LEU A N    1 
ATOM   196  C  CA   . LEU A 1 26  ? -18.768 27.093 -17.000 1.00 69.15  ? 24  LEU A CA   1 
ATOM   197  C  C    . LEU A 1 26  ? -19.183 28.329 -16.216 1.00 60.14  ? 24  LEU A C    1 
ATOM   198  O  O    . LEU A 1 26  ? -19.675 28.226 -15.087 1.00 54.56  ? 24  LEU A O    1 
ATOM   199  C  CB   . LEU A 1 26  ? -19.464 25.863 -16.433 1.00 59.42  ? 24  LEU A CB   1 
ATOM   200  C  CG   . LEU A 1 26  ? -19.302 24.641 -17.323 1.00 65.68  ? 24  LEU A CG   1 
ATOM   201  C  CD1  . LEU A 1 26  ? -20.041 23.483 -16.708 1.00 60.12  ? 24  LEU A CD1  1 
ATOM   202  C  CD2  . LEU A 1 26  ? -19.728 24.921 -18.739 1.00 62.08  ? 24  LEU A CD2  1 
ATOM   203  N  N    . PRO A 1 27  ? -19.036 29.509 -16.805 1.00 57.87  ? 25  PRO A N    1 
ATOM   204  C  CA   . PRO A 1 27  ? -19.574 30.717 -16.172 1.00 54.51  ? 25  PRO A CA   1 
ATOM   205  C  C    . PRO A 1 27  ? -21.014 30.604 -15.732 1.00 53.48  ? 25  PRO A C    1 
ATOM   206  O  O    . PRO A 1 27  ? -21.378 31.213 -14.720 1.00 55.66  ? 25  PRO A O    1 
ATOM   207  C  CB   . PRO A 1 27  ? -19.402 31.788 -17.269 1.00 52.65  ? 25  PRO A CB   1 
ATOM   208  C  CG   . PRO A 1 27  ? -19.045 31.032 -18.541 1.00 58.89  ? 25  PRO A CG   1 
ATOM   209  C  CD   . PRO A 1 27  ? -18.296 29.832 -18.035 1.00 59.48  ? 25  PRO A CD   1 
ATOM   210  N  N    . ALA A 1 28  ? -21.861 29.881 -16.468 1.00 52.43  ? 26  ALA A N    1 
ATOM   211  C  CA   . ALA A 1 28  ? -23.263 29.806 -16.089 1.00 47.31  ? 26  ALA A CA   1 
ATOM   212  C  C    . ALA A 1 28  ? -23.424 29.133 -14.742 1.00 48.31  ? 26  ALA A C    1 
ATOM   213  O  O    . ALA A 1 28  ? -24.315 29.498 -13.967 1.00 48.94  ? 26  ALA A O    1 
ATOM   214  C  CB   . ALA A 1 28  ? -24.051 29.058 -17.155 1.00 40.90  ? 26  ALA A CB   1 
ATOM   215  N  N    . ASP A 1 29  ? -22.581 28.140 -14.453 1.00 47.47  ? 27  ASP A N    1 
ATOM   216  C  CA   . ASP A 1 29  ? -22.596 27.517 -13.137 1.00 46.73  ? 27  ASP A CA   1 
ATOM   217  C  C    . ASP A 1 29  ? -22.188 28.508 -12.069 1.00 48.19  ? 27  ASP A C    1 
ATOM   218  O  O    . ASP A 1 29  ? -22.743 28.509 -10.964 1.00 49.89  ? 27  ASP A O    1 
ATOM   219  C  CB   . ASP A 1 29  ? -21.635 26.339 -13.079 1.00 46.59  ? 27  ASP A CB   1 
ATOM   220  C  CG   . ASP A 1 29  ? -21.574 25.738 -11.699 1.00 45.58  ? 27  ASP A CG   1 
ATOM   221  O  OD1  . ASP A 1 29  ? -20.456 25.527 -11.202 1.00 50.04  ? 27  ASP A OD1  1 
ATOM   222  O  OD2  . ASP A 1 29  ? -22.643 25.414 -11.135 1.00 43.48  ? 27  ASP A OD2  1 
ATOM   223  N  N    . LEU A 1 30  ? -21.182 29.336 -12.369 1.00 49.62  ? 28  LEU A N    1 
ATOM   224  C  CA   . LEU A 1 30  ? -20.738 30.336 -11.407 1.00 48.04  ? 28  LEU A CA   1 
ATOM   225  C  C    . LEU A 1 30  ? -21.846 31.330 -11.123 1.00 47.34  ? 28  LEU A C    1 
ATOM   226  O  O    . LEU A 1 30  ? -22.088 31.685 -9.967  1.00 47.91  ? 28  LEU A O    1 
ATOM   227  C  CB   . LEU A 1 30  ? -19.496 31.048 -11.932 1.00 49.75  ? 28  LEU A CB   1 
ATOM   228  C  CG   . LEU A 1 30  ? -18.206 30.282 -11.658 1.00 53.92  ? 28  LEU A CG   1 
ATOM   229  C  CD1  . LEU A 1 30  ? -17.984 30.198 -10.157 1.00 62.57  ? 28  LEU A CD1  1 
ATOM   230  C  CD2  . LEU A 1 30  ? -18.244 28.897 -12.256 1.00 63.45  ? 28  LEU A CD2  1 
ATOM   231  N  N    . ALA A 1 31  ? -22.548 31.776 -12.166 1.00 44.71  ? 29  ALA A N    1 
ATOM   232  C  CA   . ALA A 1 31  ? -23.653 32.696 -11.951 1.00 45.08  ? 29  ALA A CA   1 
ATOM   233  C  C    . ALA A 1 31  ? -24.717 32.052 -11.083 1.00 47.66  ? 29  ALA A C    1 
ATOM   234  O  O    . ALA A 1 31  ? -25.285 32.700 -10.197 1.00 48.58  ? 29  ALA A O    1 
ATOM   235  C  CB   . ALA A 1 31  ? -24.231 33.130 -13.293 1.00 43.15  ? 29  ALA A CB   1 
ATOM   236  N  N    . TRP A 1 32  ? -24.995 30.769 -11.323 1.00 46.84  ? 30  TRP A N    1 
ATOM   237  C  CA   . TRP A 1 32  ? -25.950 30.035 -10.498 1.00 44.07  ? 30  TRP A CA   1 
ATOM   238  C  C    . TRP A 1 32  ? -25.449 29.926 -9.069  1.00 44.88  ? 30  TRP A C    1 
ATOM   239  O  O    . TRP A 1 32  ? -26.209 30.141 -8.123  1.00 46.44  ? 30  TRP A O    1 
ATOM   240  C  CB   . TRP A 1 32  ? -26.187 28.666 -11.120 1.00 43.86  ? 30  TRP A CB   1 
ATOM   241  C  CG   . TRP A 1 32  ? -26.814 27.589 -10.284 1.00 42.89  ? 30  TRP A CG   1 
ATOM   242  C  CD1  . TRP A 1 32  ? -26.165 26.634 -9.547  1.00 41.54  ? 30  TRP A CD1  1 
ATOM   243  C  CD2  . TRP A 1 32  ? -28.211 27.286 -10.184 1.00 39.09  ? 30  TRP A CD2  1 
ATOM   244  N  NE1  . TRP A 1 32  ? -27.075 25.779 -8.958  1.00 36.03  ? 30  TRP A NE1  1 
ATOM   245  C  CE2  . TRP A 1 32  ? -28.338 26.160 -9.341  1.00 39.52  ? 30  TRP A CE2  1 
ATOM   246  C  CE3  . TRP A 1 32  ? -29.365 27.866 -10.714 1.00 41.26  ? 30  TRP A CE3  1 
ATOM   247  C  CZ2  . TRP A 1 32  ? -29.575 25.608 -9.021  1.00 39.14  ? 30  TRP A CZ2  1 
ATOM   248  C  CZ3  . TRP A 1 32  ? -30.587 27.327 -10.388 1.00 37.78  ? 30  TRP A CZ3  1 
ATOM   249  C  CH2  . TRP A 1 32  ? -30.684 26.206 -9.552  1.00 36.65  ? 30  TRP A CH2  1 
ATOM   250  N  N    . PHE A 1 33  ? -24.153 29.658 -8.890  1.00 45.45  ? 31  PHE A N    1 
ATOM   251  C  CA   . PHE A 1 33  ? -23.592 29.642 -7.545  1.00 45.19  ? 31  PHE A CA   1 
ATOM   252  C  C    . PHE A 1 33  ? -23.734 31.001 -6.865  1.00 47.25  ? 31  PHE A C    1 
ATOM   253  O  O    . PHE A 1 33  ? -24.183 31.092 -5.715  1.00 45.09  ? 31  PHE A O    1 
ATOM   254  C  CB   . PHE A 1 33  ? -22.122 29.235 -7.576  1.00 40.68  ? 31  PHE A CB   1 
ATOM   255  C  CG   . PHE A 1 33  ? -21.502 29.208 -6.206  1.00 44.36  ? 31  PHE A CG   1 
ATOM   256  C  CD1  . PHE A 1 33  ? -21.633 28.089 -5.398  1.00 37.92  ? 31  PHE A CD1  1 
ATOM   257  C  CD2  . PHE A 1 33  ? -20.859 30.323 -5.695  1.00 43.00  ? 31  PHE A CD2  1 
ATOM   258  C  CE1  . PHE A 1 33  ? -21.082 28.053 -4.131  1.00 40.13  ? 31  PHE A CE1  1 
ATOM   259  C  CE2  . PHE A 1 33  ? -20.319 30.306 -4.403  1.00 44.49  ? 31  PHE A CE2  1 
ATOM   260  C  CZ   . PHE A 1 33  ? -20.433 29.164 -3.621  1.00 37.71  ? 31  PHE A CZ   1 
ATOM   261  N  N    . LYS A 1 34  ? -23.316 32.073 -7.542  1.00 45.11  ? 32  LYS A N    1 
ATOM   262  C  CA   . LYS A 1 34  ? -23.457 33.400 -6.944  1.00 47.61  ? 32  LYS A CA   1 
ATOM   263  C  C    . LYS A 1 34  ? -24.922 33.716 -6.633  1.00 50.23  ? 32  LYS A C    1 
ATOM   264  O  O    . LYS A 1 34  ? -25.243 34.207 -5.543  1.00 48.90  ? 32  LYS A O    1 
ATOM   265  C  CB   . LYS A 1 34  ? -22.853 34.457 -7.873  1.00 48.48  ? 32  LYS A CB   1 
ATOM   266  C  CG   . LYS A 1 34  ? -22.927 35.884 -7.329  1.00 54.31  ? 32  LYS A CG   1 
ATOM   267  C  CD   . LYS A 1 34  ? -21.911 36.800 -8.007  1.00 60.95  ? 32  LYS A CD   1 
ATOM   268  C  CE   . LYS A 1 34  ? -22.360 38.275 -8.000  1.00 67.94  ? 32  LYS A CE   1 
ATOM   269  N  NZ   . LYS A 1 34  ? -21.629 39.139 -8.998  1.00 69.24  ? 32  LYS A NZ   1 
ATOM   270  N  N    . ARG A 1 35  ? -25.829 33.425 -7.576  1.00 51.50  ? 33  ARG A N    1 
ATOM   271  C  CA   . ARG A 1 35  ? -27.236 33.766 -7.381  1.00 49.25  ? 33  ARG A CA   1 
ATOM   272  C  C    . ARG A 1 35  ? -27.791 33.104 -6.125  1.00 49.83  ? 33  ARG A C    1 
ATOM   273  O  O    . ARG A 1 35  ? -28.524 33.739 -5.357  1.00 49.96  ? 33  ARG A O    1 
ATOM   274  C  CB   . ARG A 1 35  ? -28.052 33.369 -8.619  1.00 49.17  ? 33  ARG A CB   1 
ATOM   275  C  CG   . ARG A 1 35  ? -29.586 33.500 -8.453  1.00 58.98  ? 33  ARG A CG   1 
ATOM   276  C  CD   . ARG A 1 35  ? -30.379 33.017 -9.708  1.00 67.77  ? 33  ARG A CD   1 
ATOM   277  N  NE   . ARG A 1 35  ? -30.912 31.642 -9.588  1.00 72.09  ? 33  ARG A NE   1 
ATOM   278  C  CZ   . ARG A 1 35  ? -32.050 31.308 -8.961  1.00 75.83  ? 33  ARG A CZ   1 
ATOM   279  N  NH1  . ARG A 1 35  ? -32.804 32.258 -8.393  1.00 76.99  ? 33  ARG A NH1  1 
ATOM   280  N  NH2  . ARG A 1 35  ? -32.442 30.021 -8.901  1.00 59.40  ? 33  ARG A NH2  1 
ATOM   281  N  N    . ASN A 1 36  ? -27.428 31.844 -5.876  1.00 48.31  ? 34  ASN A N    1 
ATOM   282  C  CA   . ASN A 1 36  ? -28.021 31.094 -4.772  1.00 47.22  ? 34  ASN A CA   1 
ATOM   283  C  C    . ASN A 1 36  ? -27.245 31.186 -3.466  1.00 48.15  ? 34  ASN A C    1 
ATOM   284  O  O    . ASN A 1 36  ? -27.703 30.626 -2.460  1.00 48.89  ? 34  ASN A O    1 
ATOM   285  C  CB   . ASN A 1 36  ? -28.192 29.624 -5.149  1.00 42.37  ? 34  ASN A CB   1 
ATOM   286  C  CG   . ASN A 1 36  ? -29.261 29.426 -6.196  1.00 45.82  ? 34  ASN A CG   1 
ATOM   287  O  OD1  . ASN A 1 36  ? -28.975 29.100 -7.352  1.00 48.54  ? 34  ASN A OD1  1 
ATOM   288  N  ND2  . ASN A 1 36  ? -30.493 29.646 -5.808  1.00 45.24  ? 34  ASN A ND2  1 
ATOM   289  N  N    . THR A 1 37  ? -26.097 31.867 -3.436  1.00 46.11  ? 35  THR A N    1 
ATOM   290  C  CA   . THR A 1 37  ? -25.380 32.056 -2.184  1.00 43.70  ? 35  THR A CA   1 
ATOM   291  C  C    . THR A 1 37  ? -25.234 33.523 -1.820  1.00 48.07  ? 35  THR A C    1 
ATOM   292  O  O    . THR A 1 37  ? -24.646 33.835 -0.785  1.00 52.31  ? 35  THR A O    1 
ATOM   293  C  CB   . THR A 1 37  ? -23.989 31.415 -2.248  1.00 47.83  ? 35  THR A CB   1 
ATOM   294  O  OG1  . THR A 1 37  ? -23.230 32.056 -3.278  1.00 45.94  ? 35  THR A OG1  1 
ATOM   295  C  CG2  . THR A 1 37  ? -24.087 29.918 -2.572  1.00 39.93  ? 35  THR A CG2  1 
ATOM   296  N  N    . LEU A 1 38  ? -25.751 34.435 -2.622  1.00 49.38  ? 36  LEU A N    1 
ATOM   297  C  CA   . LEU A 1 38  ? -25.550 35.841 -2.324  1.00 52.74  ? 36  LEU A CA   1 
ATOM   298  C  C    . LEU A 1 38  ? -26.122 36.175 -0.952  1.00 52.48  ? 36  LEU A C    1 
ATOM   299  O  O    . LEU A 1 38  ? -27.229 35.755 -0.615  1.00 48.00  ? 36  LEU A O    1 
ATOM   300  C  CB   . LEU A 1 38  ? -26.196 36.699 -3.412  1.00 57.11  ? 36  LEU A CB   1 
ATOM   301  C  CG   . LEU A 1 38  ? -25.486 38.020 -3.735  1.00 59.96  ? 36  LEU A CG   1 
ATOM   302  C  CD1  . LEU A 1 38  ? -24.048 37.793 -4.197  1.00 59.59  ? 36  LEU A CD1  1 
ATOM   303  C  CD2  . LEU A 1 38  ? -26.288 38.761 -4.800  1.00 61.28  ? 36  LEU A CD2  1 
ATOM   304  N  N    . ASN A 1 39  ? -25.354 36.917 -0.148  1.00 55.01  ? 37  ASN A N    1 
ATOM   305  C  CA   . ASN A 1 39  ? -25.808 37.353 1.170   1.00 52.68  ? 37  ASN A CA   1 
ATOM   306  C  C    . ASN A 1 39  ? -26.217 36.184 2.065   1.00 52.59  ? 37  ASN A C    1 
ATOM   307  O  O    . ASN A 1 39  ? -27.045 36.337 2.980   1.00 56.25  ? 37  ASN A O    1 
ATOM   308  C  CB   . ASN A 1 39  ? -26.959 38.353 1.036   1.00 59.51  ? 37  ASN A CB   1 
ATOM   309  C  CG   . ASN A 1 39  ? -26.603 39.528 0.142   1.00 63.15  ? 37  ASN A CG   1 
ATOM   310  O  OD1  . ASN A 1 39  ? -27.373 39.904 -0.747  1.00 69.50  ? 37  ASN A OD1  1 
ATOM   311  N  ND2  . ASN A 1 39  ? -25.450 40.148 0.409   1.00 63.42  ? 37  ASN A ND2  1 
ATOM   312  N  N    . LYS A 1 40  ? -25.653 35.010 1.809   1.00 49.26  ? 38  LYS A N    1 
ATOM   313  C  CA   . LYS A 1 40  ? -25.836 33.863 2.672   1.00 45.86  ? 38  LYS A CA   1 
ATOM   314  C  C    . LYS A 1 40  ? -24.488 33.439 3.223   1.00 48.63  ? 38  LYS A C    1 
ATOM   315  O  O    . LYS A 1 40  ? -23.480 33.552 2.517   1.00 45.98  ? 38  LYS A O    1 
ATOM   316  C  CB   . LYS A 1 40  ? -26.474 32.705 1.908   1.00 42.74  ? 38  LYS A CB   1 
ATOM   317  C  CG   . LYS A 1 40  ? -27.881 33.030 1.438   1.00 47.02  ? 38  LYS A CG   1 
ATOM   318  C  CD   . LYS A 1 40  ? -28.579 31.854 0.780   1.00 43.07  ? 38  LYS A CD   1 
ATOM   319  C  CE   . LYS A 1 40  ? -29.475 32.311 -0.380  1.00 45.08  ? 38  LYS A CE   1 
ATOM   320  N  NZ   . LYS A 1 40  ? -30.146 31.168 -1.054  1.00 44.09  ? 38  LYS A NZ   1 
ATOM   321  N  N    . PRO A 1 41  ? -24.406 33.012 4.482   1.00 44.74  ? 39  PRO A N    1 
ATOM   322  C  CA   . PRO A 1 41  ? -23.146 32.475 4.996   1.00 43.73  ? 39  PRO A CA   1 
ATOM   323  C  C    . PRO A 1 41  ? -22.796 31.178 4.285   1.00 43.35  ? 39  PRO A C    1 
ATOM   324  O  O    . PRO A 1 41  ? -23.678 30.377 3.962   1.00 44.13  ? 39  PRO A O    1 
ATOM   325  C  CB   . PRO A 1 41  ? -23.439 32.245 6.485   1.00 40.31  ? 39  PRO A CB   1 
ATOM   326  C  CG   . PRO A 1 41  ? -24.907 32.118 6.559   1.00 42.78  ? 39  PRO A CG   1 
ATOM   327  C  CD   . PRO A 1 41  ? -25.411 33.119 5.552   1.00 45.70  ? 39  PRO A CD   1 
ATOM   328  N  N    . VAL A 1 42  ? -21.503 30.976 4.027   1.00 42.34  ? 40  VAL A N    1 
ATOM   329  C  CA   . VAL A 1 42  ? -21.019 29.787 3.330   1.00 40.74  ? 40  VAL A CA   1 
ATOM   330  C  C    . VAL A 1 42  ? -20.072 29.029 4.257   1.00 40.20  ? 40  VAL A C    1 
ATOM   331  O  O    . VAL A 1 42  ? -19.275 29.642 4.982   1.00 39.48  ? 40  VAL A O    1 
ATOM   332  C  CB   . VAL A 1 42  ? -20.313 30.157 2.006   1.00 41.78  ? 40  VAL A CB   1 
ATOM   333  C  CG1  . VAL A 1 42  ? -21.341 30.626 0.947   1.00 38.65  ? 40  VAL A CG1  1 
ATOM   334  C  CG2  . VAL A 1 42  ? -19.219 31.219 2.242   1.00 37.41  ? 40  VAL A CG2  1 
ATOM   335  N  N    . ILE A 1 43  ? -20.180 27.700 4.246   1.00 33.35  ? 41  ILE A N    1 
ATOM   336  C  CA   . ILE A 1 43  ? -19.307 26.806 4.997   1.00 37.32  ? 41  ILE A CA   1 
ATOM   337  C  C    . ILE A 1 43  ? -18.536 25.972 4.000   1.00 40.20  ? 41  ILE A C    1 
ATOM   338  O  O    . ILE A 1 43  ? -19.132 25.378 3.093   1.00 36.28  ? 41  ILE A O    1 
ATOM   339  C  CB   . ILE A 1 43  ? -20.093 25.881 5.941   1.00 38.12  ? 41  ILE A CB   1 
ATOM   340  C  CG1  . ILE A 1 43  ? -20.838 26.677 6.998   1.00 34.47  ? 41  ILE A CG1  1 
ATOM   341  C  CG2  . ILE A 1 43  ? -19.177 24.888 6.616   1.00 39.01  ? 41  ILE A CG2  1 
ATOM   342  C  CD1  . ILE A 1 43  ? -21.735 25.785 7.802   1.00 31.22  ? 41  ILE A CD1  1 
ATOM   343  N  N    . MET A 1 44  ? -17.219 25.899 4.181   1.00 39.88  ? 42  MET A N    1 
ATOM   344  C  CA   . MET A 1 44  ? -16.365 25.173 3.256   1.00 39.62  ? 42  MET A CA   1 
ATOM   345  C  C    . MET A 1 44  ? -15.282 24.485 4.074   1.00 42.50  ? 42  MET A C    1 
ATOM   346  O  O    . MET A 1 44  ? -15.044 24.842 5.226   1.00 40.97  ? 42  MET A O    1 
ATOM   347  C  CB   . MET A 1 44  ? -15.774 26.124 2.210   1.00 36.99  ? 42  MET A CB   1 
ATOM   348  C  CG   . MET A 1 44  ? -14.568 26.895 2.716   1.00 39.64  ? 42  MET A CG   1 
ATOM   349  S  SD   . MET A 1 44  ? -14.201 28.364 1.706   1.00 41.21  ? 42  MET A SD   1 
ATOM   350  C  CE   . MET A 1 44  ? -15.537 29.445 2.274   1.00 38.05  ? 42  MET A CE   1 
ATOM   351  N  N    . GLY A 1 45  ? -14.662 23.452 3.500   1.00 42.65  ? 43  GLY A N    1 
ATOM   352  C  CA   . GLY A 1 45  ? -13.583 22.789 4.197   1.00 42.69  ? 43  GLY A CA   1 
ATOM   353  C  C    . GLY A 1 45  ? -12.275 23.512 3.973   1.00 44.26  ? 43  GLY A C    1 
ATOM   354  O  O    . GLY A 1 45  ? -12.176 24.426 3.154   1.00 44.31  ? 43  GLY A O    1 
ATOM   355  N  N    . ARG A 1 46  ? -11.241 23.083 4.698   1.00 47.45  ? 44  ARG A N    1 
ATOM   356  C  CA   . ARG A 1 46  ? -9.946  23.751 4.566   1.00 49.79  ? 44  ARG A CA   1 
ATOM   357  C  C    . ARG A 1 46  ? -9.410  23.690 3.138   1.00 52.68  ? 44  ARG A C    1 
ATOM   358  O  O    . ARG A 1 46  ? -8.827  24.663 2.646   1.00 49.74  ? 44  ARG A O    1 
ATOM   359  C  CB   . ARG A 1 46  ? -8.927  23.140 5.518   1.00 53.11  ? 44  ARG A CB   1 
ATOM   360  C  CG   . ARG A 1 46  ? -7.646  23.960 5.614   1.00 54.01  ? 44  ARG A CG   1 
ATOM   361  C  CD   . ARG A 1 46  ? -6.774  23.399 6.705   1.00 56.01  ? 44  ARG A CD   1 
ATOM   362  N  NE   . ARG A 1 46  ? -7.040  21.975 6.908   1.00 57.29  ? 44  ARG A NE   1 
ATOM   363  C  CZ   . ARG A 1 46  ? -6.296  20.992 6.409   1.00 63.66  ? 44  ARG A CZ   1 
ATOM   364  N  NH1  . ARG A 1 46  ? -5.220  21.265 5.677   1.00 63.91  ? 44  ARG A NH1  1 
ATOM   365  N  NH2  . ARG A 1 46  ? -6.621  19.729 6.657   1.00 67.09  ? 44  ARG A NH2  1 
ATOM   366  N  N    . HIS A 1 47  ? -9.548  22.542 2.472   1.00 49.21  ? 45  HIS A N    1 
ATOM   367  C  CA   . HIS A 1 47  ? -9.032  22.430 1.114   1.00 52.43  ? 45  HIS A CA   1 
ATOM   368  C  C    . HIS A 1 47  ? -9.793  23.345 0.158   1.00 52.79  ? 45  HIS A C    1 
ATOM   369  O  O    . HIS A 1 47  ? -9.202  23.938 -0.751  1.00 49.72  ? 45  HIS A O    1 
ATOM   370  C  CB   . HIS A 1 47  ? -9.093  20.976 0.649   1.00 52.42  ? 45  HIS A CB   1 
ATOM   371  C  CG   . HIS A 1 47  ? -8.211  20.053 1.437   1.00 58.30  ? 45  HIS A CG   1 
ATOM   372  N  ND1  . HIS A 1 47  ? -8.568  18.753 1.738   1.00 60.80  ? 45  HIS A ND1  1 
ATOM   373  C  CD2  . HIS A 1 47  ? -6.972  20.231 1.958   1.00 60.90  ? 45  HIS A CD2  1 
ATOM   374  C  CE1  . HIS A 1 47  ? -7.597  18.180 2.427   1.00 56.86  ? 45  HIS A CE1  1 
ATOM   375  N  NE2  . HIS A 1 47  ? -6.616  19.055 2.573   1.00 62.71  ? 45  HIS A NE2  1 
ATOM   376  N  N    . THR A 1 48  ? -11.098 23.502 0.352   1.00 50.13  ? 46  THR A N    1 
ATOM   377  C  CA   . THR A 1 48  ? -11.809 24.428 -0.518  1.00 47.19  ? 46  THR A CA   1 
ATOM   378  C  C    . THR A 1 48  ? -11.339 25.856 -0.275  1.00 48.25  ? 46  THR A C    1 
ATOM   379  O  O    . THR A 1 48  ? -11.105 26.615 -1.222  1.00 45.02  ? 46  THR A O    1 
ATOM   380  C  CB   . THR A 1 48  ? -13.307 24.306 -0.291  1.00 47.59  ? 46  THR A CB   1 
ATOM   381  O  OG1  . THR A 1 48  ? -13.727 23.014 -0.740  1.00 47.45  ? 46  THR A OG1  1 
ATOM   382  C  CG2  . THR A 1 48  ? -14.030 25.384 -1.082  1.00 41.48  ? 46  THR A CG2  1 
ATOM   383  N  N    . TRP A 1 49  ? -11.167 26.232 0.991   1.00 49.06  ? 47  TRP A N    1 
ATOM   384  C  CA   . TRP A 1 49  ? -10.605 27.544 1.298   1.00 47.99  ? 47  TRP A CA   1 
ATOM   385  C  C    . TRP A 1 49  ? -9.268  27.735 0.591   1.00 49.12  ? 47  TRP A C    1 
ATOM   386  O  O    . TRP A 1 49  ? -9.019  28.778 -0.029  1.00 51.54  ? 47  TRP A O    1 
ATOM   387  C  CB   . TRP A 1 49  ? -10.445 27.706 2.820   1.00 46.91  ? 47  TRP A CB   1 
ATOM   388  C  CG   . TRP A 1 49  ? -9.581  28.871 3.189   1.00 42.93  ? 47  TRP A CG   1 
ATOM   389  C  CD1  . TRP A 1 49  ? -8.347  28.826 3.757   1.00 44.15  ? 47  TRP A CD1  1 
ATOM   390  C  CD2  . TRP A 1 49  ? -9.886  30.258 2.992   1.00 47.17  ? 47  TRP A CD2  1 
ATOM   391  N  NE1  . TRP A 1 49  ? -7.853  30.101 3.926   1.00 46.43  ? 47  TRP A NE1  1 
ATOM   392  C  CE2  . TRP A 1 49  ? -8.781  30.998 3.465   1.00 47.06  ? 47  TRP A CE2  1 
ATOM   393  C  CE3  . TRP A 1 49  ? -10.985 30.947 2.449   1.00 48.63  ? 47  TRP A CE3  1 
ATOM   394  C  CZ2  . TRP A 1 49  ? -8.737  32.395 3.418   1.00 47.14  ? 47  TRP A CZ2  1 
ATOM   395  C  CZ3  . TRP A 1 49  ? -10.943 32.342 2.402   1.00 45.76  ? 47  TRP A CZ3  1 
ATOM   396  C  CH2  . TRP A 1 49  ? -9.825  33.047 2.887   1.00 48.63  ? 47  TRP A CH2  1 
ATOM   397  N  N    . GLU A 1 50  ? -8.397  26.726 0.646   1.00 50.14  ? 48  GLU A N    1 
ATOM   398  C  CA   . GLU A 1 50  ? -7.064  26.894 0.082   1.00 50.37  ? 48  GLU A CA   1 
ATOM   399  C  C    . GLU A 1 50  ? -7.099  27.067 -1.427  1.00 49.77  ? 48  GLU A C    1 
ATOM   400  O  O    . GLU A 1 50  ? -6.131  27.576 -2.002  1.00 57.58  ? 48  GLU A O    1 
ATOM   401  C  CB   . GLU A 1 50  ? -6.169  25.706 0.452   1.00 49.95  ? 48  GLU A CB   1 
ATOM   402  C  CG   . GLU A 1 50  ? -5.764  25.663 1.935   1.00 55.50  ? 48  GLU A CG   1 
ATOM   403  C  CD   . GLU A 1 50  ? -5.152  24.321 2.388   1.00 62.64  ? 48  GLU A CD   1 
ATOM   404  O  OE1  . GLU A 1 50  ? -5.129  23.341 1.599   1.00 64.59  ? 48  GLU A OE1  1 
ATOM   405  O  OE2  . GLU A 1 50  ? -4.698  24.251 3.556   1.00 65.69  ? 48  GLU A OE2  1 
ATOM   406  N  N    . SER A 1 51  ? -8.179  26.680 -2.090  1.00 53.37  ? 49  SER A N    1 
ATOM   407  C  CA   . SER A 1 51  ? -8.188  26.810 -3.543  1.00 53.25  ? 49  SER A CA   1 
ATOM   408  C  C    . SER A 1 51  ? -8.635  28.192 -4.011  1.00 55.98  ? 49  SER A C    1 
ATOM   409  O  O    . SER A 1 51  ? -8.657  28.437 -5.217  1.00 62.53  ? 49  SER A O    1 
ATOM   410  C  CB   . SER A 1 51  ? -9.083  25.734 -4.170  1.00 52.74  ? 49  SER A CB   1 
ATOM   411  O  OG   . SER A 1 51  ? -10.437 25.966 -3.833  1.00 57.20  ? 49  SER A OG   1 
ATOM   412  N  N    . ILE A 1 52  ? -9.017  29.095 -3.106  1.00 54.89  ? 50  ILE A N    1 
ATOM   413  C  CA   . ILE A 1 52  ? -9.409  30.443 -3.476  1.00 52.60  ? 50  ILE A CA   1 
ATOM   414  C  C    . ILE A 1 52  ? -8.577  31.492 -2.745  1.00 53.70  ? 50  ILE A C    1 
ATOM   415  O  O    . ILE A 1 52  ? -8.197  32.507 -3.336  1.00 52.09  ? 50  ILE A O    1 
ATOM   416  C  CB   . ILE A 1 52  ? -10.916 30.678 -3.227  1.00 54.19  ? 50  ILE A CB   1 
ATOM   417  C  CG1  . ILE A 1 52  ? -11.319 30.243 -1.826  1.00 52.31  ? 50  ILE A CG1  1 
ATOM   418  C  CG2  . ILE A 1 52  ? -11.748 29.881 -4.210  1.00 52.41  ? 50  ILE A CG2  1 
ATOM   419  C  CD1  . ILE A 1 52  ? -12.684 30.766 -1.428  1.00 45.35  ? 50  ILE A CD1  1 
ATOM   420  N  N    . GLY A 1 53  ? -8.294  31.273 -1.455  1.00 56.38  ? 51  GLY A N    1 
ATOM   421  C  CA   . GLY A 1 53  ? -7.370  32.095 -0.675  1.00 51.67  ? 51  GLY A CA   1 
ATOM   422  C  C    . GLY A 1 53  ? -7.840  33.497 -0.326  1.00 58.27  ? 51  GLY A C    1 
ATOM   423  O  O    . GLY A 1 53  ? -7.111  34.219 0.368   1.00 59.50  ? 51  GLY A O    1 
ATOM   424  N  N    . ARG A 1 54  ? -9.019  33.904 -0.791  1.00 61.41  ? 52  ARG A N    1 
ATOM   425  C  CA   . ARG A 1 54  ? -9.736  35.149 -0.588  1.00 55.15  ? 52  ARG A CA   1 
ATOM   426  C  C    . ARG A 1 54  ? -11.194 34.856 -0.257  1.00 53.43  ? 52  ARG A C    1 
ATOM   427  O  O    . ARG A 1 54  ? -11.818 34.029 -0.927  1.00 52.84  ? 52  ARG A O    1 
ATOM   428  C  CB   . ARG A 1 54  ? -9.621  36.011 -1.864  1.00 58.82  ? 52  ARG A CB   1 
ATOM   429  C  CG   . ARG A 1 54  ? -10.442 37.296 -1.828  1.00 66.99  ? 52  ARG A CG   1 
ATOM   430  C  CD   . ARG A 1 54  ? -10.253 38.168 -3.067  1.00 75.14  ? 52  ARG A CD   1 
ATOM   431  N  NE   . ARG A 1 54  ? -8.941  38.781 -3.096  1.00 88.70  ? 52  ARG A NE   1 
ATOM   432  C  CZ   . ARG A 1 54  ? -7.950  38.451 -3.918  1.00 93.46  ? 52  ARG A CZ   1 
ATOM   433  N  NH1  . ARG A 1 54  ? -8.058  37.439 -4.788  1.00 94.94  ? 52  ARG A NH1  1 
ATOM   434  N  NH2  . ARG A 1 54  ? -6.820  39.139 -3.847  1.00 85.81  ? 52  ARG A NH2  1 
ATOM   435  N  N    . PRO A 1 55  ? -11.764 35.498 0.769   1.00 50.89  ? 53  PRO A N    1 
ATOM   436  C  CA   . PRO A 1 55  ? -13.172 35.252 1.104   1.00 49.02  ? 53  PRO A CA   1 
ATOM   437  C  C    . PRO A 1 55  ? -14.070 35.510 -0.091  1.00 51.50  ? 53  PRO A C    1 
ATOM   438  O  O    . PRO A 1 55  ? -13.831 36.429 -0.874  1.00 52.72  ? 53  PRO A O    1 
ATOM   439  C  CB   . PRO A 1 55  ? -13.448 36.267 2.223   1.00 45.70  ? 53  PRO A CB   1 
ATOM   440  C  CG   . PRO A 1 55  ? -12.118 36.521 2.812   1.00 49.47  ? 53  PRO A CG   1 
ATOM   441  C  CD   . PRO A 1 55  ? -11.175 36.513 1.655   1.00 48.92  ? 53  PRO A CD   1 
ATOM   442  N  N    . LEU A 1 56  ? -15.117 34.708 -0.222  1.00 49.61  ? 54  LEU A N    1 
ATOM   443  C  CA   . LEU A 1 56  ? -16.197 35.082 -1.118  1.00 49.52  ? 54  LEU A CA   1 
ATOM   444  C  C    . LEU A 1 56  ? -16.846 36.356 -0.578  1.00 49.99  ? 54  LEU A C    1 
ATOM   445  O  O    . LEU A 1 56  ? -17.187 36.411 0.604   1.00 48.47  ? 54  LEU A O    1 
ATOM   446  C  CB   . LEU A 1 56  ? -17.226 33.972 -1.220  1.00 46.64  ? 54  LEU A CB   1 
ATOM   447  C  CG   . LEU A 1 56  ? -16.641 32.616 -1.590  1.00 45.72  ? 54  LEU A CG   1 
ATOM   448  C  CD1  . LEU A 1 56  ? -17.769 31.607 -1.705  1.00 42.86  ? 54  LEU A CD1  1 
ATOM   449  C  CD2  . LEU A 1 56  ? -15.811 32.699 -2.850  1.00 49.94  ? 54  LEU A CD2  1 
ATOM   450  N  N    . PRO A 1 57  ? -17.020 37.386 -1.397  1.00 51.54  ? 55  PRO A N    1 
ATOM   451  C  CA   . PRO A 1 57  ? -17.441 38.692 -0.867  1.00 50.25  ? 55  PRO A CA   1 
ATOM   452  C  C    . PRO A 1 57  ? -18.911 38.735 -0.502  1.00 53.87  ? 55  PRO A C    1 
ATOM   453  O  O    . PRO A 1 57  ? -19.742 38.034 -1.076  1.00 56.06  ? 55  PRO A O    1 
ATOM   454  C  CB   . PRO A 1 57  ? -17.167 39.659 -2.024  1.00 51.04  ? 55  PRO A CB   1 
ATOM   455  C  CG   . PRO A 1 57  ? -16.991 38.817 -3.240  1.00 52.29  ? 55  PRO A CG   1 
ATOM   456  C  CD   . PRO A 1 57  ? -16.847 37.376 -2.855  1.00 51.53  ? 55  PRO A CD   1 
ATOM   457  N  N    . GLY A 1 58  ? -19.229 39.618 0.438   1.00 57.50  ? 56  GLY A N    1 
ATOM   458  C  CA   . GLY A 1 58  ? -20.607 39.799 0.841   1.00 63.94  ? 56  GLY A CA   1 
ATOM   459  C  C    . GLY A 1 58  ? -21.225 38.581 1.476   1.00 65.13  ? 56  GLY A C    1 
ATOM   460  O  O    . GLY A 1 58  ? -22.414 38.306 1.252   1.00 68.92  ? 56  GLY A O    1 
ATOM   461  N  N    . ARG A 1 59  ? -20.443 37.823 2.245   1.00 59.07  ? 57  ARG A N    1 
ATOM   462  C  CA   . ARG A 1 59  ? -20.928 36.627 2.917   1.00 52.82  ? 57  ARG A CA   1 
ATOM   463  C  C    . ARG A 1 59  ? -20.042 36.340 4.108   1.00 50.24  ? 57  ARG A C    1 
ATOM   464  O  O    . ARG A 1 59  ? -18.838 36.591 4.074   1.00 57.63  ? 57  ARG A O    1 
ATOM   465  C  CB   . ARG A 1 59  ? -20.921 35.407 2.014   1.00 48.83  ? 57  ARG A CB   1 
ATOM   466  C  CG   . ARG A 1 59  ? -21.633 35.611 0.726   1.00 52.29  ? 57  ARG A CG   1 
ATOM   467  C  CD   . ARG A 1 59  ? -21.470 34.382 -0.079  1.00 46.43  ? 57  ARG A CD   1 
ATOM   468  N  NE   . ARG A 1 59  ? -21.968 34.553 -1.430  1.00 51.14  ? 57  ARG A NE   1 
ATOM   469  C  CZ   . ARG A 1 59  ? -21.299 35.140 -2.414  1.00 55.26  ? 57  ARG A CZ   1 
ATOM   470  N  NH1  . ARG A 1 59  ? -20.092 35.648 -2.202  1.00 53.53  ? 57  ARG A NH1  1 
ATOM   471  N  NH2  . ARG A 1 59  ? -21.854 35.221 -3.617  1.00 61.86  ? 57  ARG A NH2  1 
ATOM   472  N  N    . LYS A 1 60  ? -20.647 35.818 5.166   1.00 53.25  ? 58  LYS A N    1 
ATOM   473  C  CA   . LYS A 1 60  ? -19.848 35.247 6.228   1.00 46.29  ? 58  LYS A CA   1 
ATOM   474  C  C    . LYS A 1 60  ? -19.292 33.926 5.728   1.00 47.63  ? 58  LYS A C    1 
ATOM   475  O  O    . LYS A 1 60  ? -20.038 33.027 5.336   1.00 45.43  ? 58  LYS A O    1 
ATOM   476  C  CB   . LYS A 1 60  ? -20.633 35.060 7.514   1.00 43.15  ? 58  LYS A CB   1 
ATOM   477  C  CG   . LYS A 1 60  ? -19.716 34.713 8.662   1.00 46.66  ? 58  LYS A CG   1 
ATOM   478  C  CD   . LYS A 1 60  ? -20.405 34.858 10.020  1.00 52.38  ? 58  LYS A CD   1 
ATOM   479  C  CE   . LYS A 1 60  ? -19.396 34.747 11.200  1.00 52.53  ? 58  LYS A CE   1 
ATOM   480  N  NZ   . LYS A 1 60  ? -19.978 34.075 12.437  1.00 57.58  ? 58  LYS A NZ   1 
ATOM   481  N  N    . ASN A 1 61  ? -17.969 33.863 5.678   1.00 46.83  ? 59  ASN A N    1 
ATOM   482  C  CA   . ASN A 1 61  ? -17.135 32.727 5.272   1.00 40.38  ? 59  ASN A CA   1 
ATOM   483  C  C    . ASN A 1 61  ? -16.704 31.949 6.520   1.00 41.24  ? 59  ASN A C    1 
ATOM   484  O  O    . ASN A 1 61  ? -15.958 32.475 7.355   1.00 43.42  ? 59  ASN A O    1 
ATOM   485  C  CB   . ASN A 1 61  ? -15.927 33.285 4.496   1.00 40.91  ? 59  ASN A CB   1 
ATOM   486  C  CG   . ASN A 1 61  ? -16.191 33.615 3.041   1.00 47.02  ? 59  ASN A CG   1 
ATOM   487  O  OD1  . ASN A 1 61  ? -16.615 32.788 2.277   1.00 62.12  ? 59  ASN A OD1  1 
ATOM   488  N  ND2  . ASN A 1 61  ? -16.205 34.877 2.746   1.00 58.24  ? 59  ASN A ND2  1 
ATOM   489  N  N    . ILE A 1 62  ? -17.212 30.723 6.666   1.00 40.91  ? 60  ILE A N    1 
ATOM   490  C  CA   . ILE A 1 62  ? -16.867 29.811 7.761   1.00 38.93  ? 60  ILE A CA   1 
ATOM   491  C  C    . ILE A 1 62  ? -16.073 28.623 7.224   1.00 39.35  ? 60  ILE A C    1 
ATOM   492  O  O    . ILE A 1 62  ? -16.527 27.943 6.304   1.00 39.07  ? 60  ILE A O    1 
ATOM   493  C  CB   . ILE A 1 62  ? -18.118 29.323 8.523   1.00 43.85  ? 60  ILE A CB   1 
ATOM   494  C  CG1  . ILE A 1 62  ? -18.800 30.452 9.320   1.00 42.98  ? 60  ILE A CG1  1 
ATOM   495  C  CG2  . ILE A 1 62  ? -17.804 28.118 9.433   1.00 39.30  ? 60  ILE A CG2  1 
ATOM   496  C  CD1  . ILE A 1 62  ? -19.862 31.192 8.561   1.00 46.91  ? 60  ILE A CD1  1 
ATOM   497  N  N    . ILE A 1 63  ? -14.908 28.346 7.821   1.00 44.86  ? 61  ILE A N    1 
ATOM   498  C  CA   . ILE A 1 63  ? -14.007 27.283 7.360   1.00 41.15  ? 61  ILE A CA   1 
ATOM   499  C  C    . ILE A 1 63  ? -14.032 26.158 8.388   1.00 44.65  ? 61  ILE A C    1 
ATOM   500  O  O    . ILE A 1 63  ? -13.637 26.362 9.542   1.00 43.38  ? 61  ILE A O    1 
ATOM   501  C  CB   . ILE A 1 63  ? -12.572 27.797 7.182   1.00 41.59  ? 61  ILE A CB   1 
ATOM   502  C  CG1  . ILE A 1 63  ? -12.570 29.152 6.462   1.00 37.17  ? 61  ILE A CG1  1 
ATOM   503  C  CG2  . ILE A 1 63  ? -11.748 26.769 6.414   1.00 42.81  ? 61  ILE A CG2  1 
ATOM   504  C  CD1  . ILE A 1 63  ? -13.237 29.151 5.095   1.00 39.67  ? 61  ILE A CD1  1 
ATOM   505  N  N    . LEU A 1 64  ? -14.509 24.978 7.994   1.00 42.61  ? 62  LEU A N    1 
ATOM   506  C  CA   . LEU A 1 64  ? -14.468 23.816 8.885   1.00 44.54  ? 62  LEU A CA   1 
ATOM   507  C  C    . LEU A 1 64  ? -13.097 23.171 8.741   1.00 49.78  ? 62  LEU A C    1 
ATOM   508  O  O    . LEU A 1 64  ? -12.767 22.639 7.678   1.00 46.92  ? 62  LEU A O    1 
ATOM   509  C  CB   . LEU A 1 64  ? -15.578 22.830 8.538   1.00 43.65  ? 62  LEU A CB   1 
ATOM   510  C  CG   . LEU A 1 64  ? -15.623 21.514 9.314   1.00 44.30  ? 62  LEU A CG   1 
ATOM   511  C  CD1  . LEU A 1 64  ? -15.801 21.744 10.811  1.00 46.99  ? 62  LEU A CD1  1 
ATOM   512  C  CD2  . LEU A 1 64  ? -16.729 20.638 8.775   1.00 45.40  ? 62  LEU A CD2  1 
ATOM   513  N  N    . SER A 1 65  ? -12.284 23.233 9.789   1.00 48.45  ? 63  SER A N    1 
ATOM   514  C  CA   . SER A 1 65  ? -10.890 22.834 9.669   1.00 51.80  ? 63  SER A CA   1 
ATOM   515  C  C    . SER A 1 65  ? -10.460 22.015 10.870  1.00 51.65  ? 63  SER A C    1 
ATOM   516  O  O    . SER A 1 65  ? -10.835 22.316 12.001  1.00 47.04  ? 63  SER A O    1 
ATOM   517  C  CB   . SER A 1 65  ? -9.962  24.046 9.548   1.00 49.38  ? 63  SER A CB   1 
ATOM   518  O  OG   . SER A 1 65  ? -8.612  23.610 9.549   1.00 54.08  ? 63  SER A OG   1 
ATOM   519  N  N    . SER A 1 66  ? -9.637  21.008 10.615  1.00 54.46  ? 64  SER A N    1 
ATOM   520  C  CA   . SER A 1 66  ? -9.015  20.220 11.663  1.00 56.06  ? 64  SER A CA   1 
ATOM   521  C  C    . SER A 1 66  ? -7.678  20.795 12.107  1.00 58.39  ? 64  SER A C    1 
ATOM   522  O  O    . SER A 1 66  ? -6.956  20.148 12.871  1.00 62.58  ? 64  SER A O    1 
ATOM   523  C  CB   . SER A 1 66  ? -8.832  18.791 11.176  1.00 56.45  ? 64  SER A CB   1 
ATOM   524  O  OG   . SER A 1 66  ? -7.967  18.769 10.057  1.00 62.79  ? 64  SER A OG   1 
ATOM   525  N  N    . GLN A 1 67  ? -7.330  21.982 11.643  1.00 56.68  ? 65  GLN A N    1 
ATOM   526  C  CA   . GLN A 1 67  ? -6.069  22.620 11.978  1.00 55.22  ? 65  GLN A CA   1 
ATOM   527  C  C    . GLN A 1 67  ? -6.346  24.072 12.360  1.00 52.85  ? 65  GLN A C    1 
ATOM   528  O  O    . GLN A 1 67  ? -7.413  24.605 12.050  1.00 51.59  ? 65  GLN A O    1 
ATOM   529  C  CB   . GLN A 1 67  ? -5.099  22.542 10.795  1.00 57.81  ? 65  GLN A CB   1 
ATOM   530  C  CG   . GLN A 1 67  ? -4.695  21.115 10.448  1.00 61.95  ? 65  GLN A CG   1 
ATOM   531  C  CD   . GLN A 1 67  ? -3.848  21.045 9.178   1.00 71.92  ? 65  GLN A CD   1 
ATOM   532  O  OE1  . GLN A 1 67  ? -3.342  22.070 8.707   1.00 71.79  ? 65  GLN A OE1  1 
ATOM   533  N  NE2  . GLN A 1 67  ? -3.672  19.833 8.631   1.00 67.84  ? 65  GLN A NE2  1 
ATOM   534  N  N    . PRO A 1 68  ? -5.423  24.708 13.069  1.00 52.84  ? 66  PRO A N    1 
ATOM   535  C  CA   . PRO A 1 68  ? -5.693  26.073 13.537  1.00 55.11  ? 66  PRO A CA   1 
ATOM   536  C  C    . PRO A 1 68  ? -5.823  27.025 12.354  1.00 53.25  ? 66  PRO A C    1 
ATOM   537  O  O    . PRO A 1 68  ? -5.236  26.819 11.293  1.00 54.82  ? 66  PRO A O    1 
ATOM   538  C  CB   . PRO A 1 68  ? -4.458  26.400 14.385  1.00 53.11  ? 66  PRO A CB   1 
ATOM   539  C  CG   . PRO A 1 68  ? -3.855  25.058 14.709  1.00 53.35  ? 66  PRO A CG   1 
ATOM   540  C  CD   . PRO A 1 68  ? -4.076  24.272 13.458  1.00 55.51  ? 66  PRO A CD   1 
ATOM   541  N  N    . GLY A 1 69  ? -6.596  28.088 12.542  1.00 49.21  ? 67  GLY A N    1 
ATOM   542  C  CA   . GLY A 1 69  ? -6.838  29.009 11.449  1.00 50.17  ? 67  GLY A CA   1 
ATOM   543  C  C    . GLY A 1 69  ? -5.593  29.775 11.047  1.00 52.65  ? 67  GLY A C    1 
ATOM   544  O  O    . GLY A 1 69  ? -4.676  29.972 11.837  1.00 51.21  ? 67  GLY A O    1 
ATOM   545  N  N    . THR A 1 70  ? -5.570  30.231 9.782   1.00 49.53  ? 68  THR A N    1 
ATOM   546  C  CA   . THR A 1 70  ? -4.426  30.966 9.248   1.00 48.35  ? 68  THR A CA   1 
ATOM   547  C  C    . THR A 1 70  ? -4.796  32.281 8.560   1.00 48.93  ? 68  THR A C    1 
ATOM   548  O  O    . THR A 1 70  ? -3.940  32.877 7.894   1.00 52.07  ? 68  THR A O    1 
ATOM   549  C  CB   . THR A 1 70  ? -3.639  30.082 8.268   1.00 49.24  ? 68  THR A CB   1 
ATOM   550  O  OG1  . THR A 1 70  ? -4.545  29.388 7.385   1.00 48.47  ? 68  THR A OG1  1 
ATOM   551  C  CG2  . THR A 1 70  ? -2.831  29.087 9.034   1.00 52.96  ? 68  THR A CG2  1 
ATOM   552  N  N    . ASP A 1 71  ? -6.028  32.759 8.708   1.00 47.16  ? 69  ASP A N    1 
ATOM   553  C  CA   . ASP A 1 71  ? -6.494  33.960 8.012   1.00 52.70  ? 69  ASP A CA   1 
ATOM   554  C  C    . ASP A 1 71  ? -7.603  34.595 8.830   1.00 48.66  ? 69  ASP A C    1 
ATOM   555  O  O    . ASP A 1 71  ? -8.642  33.966 9.035   1.00 49.75  ? 69  ASP A O    1 
ATOM   556  C  CB   . ASP A 1 71  ? -7.009  33.624 6.608   1.00 48.81  ? 69  ASP A CB   1 
ATOM   557  C  CG   . ASP A 1 71  ? -7.187  34.854 5.737   1.00 51.38  ? 69  ASP A CG   1 
ATOM   558  O  OD1  . ASP A 1 71  ? -8.016  35.712 6.130   1.00 50.00  ? 69  ASP A OD1  1 
ATOM   559  O  OD2  . ASP A 1 71  ? -6.556  34.943 4.650   1.00 49.39  ? 69  ASP A OD2  1 
ATOM   560  N  N    . ASP A 1 72  ? -7.412  35.839 9.252   1.00 51.31  ? 70  ASP A N    1 
ATOM   561  C  CA   . ASP A 1 72  ? -8.330  36.466 10.199  1.00 53.39  ? 70  ASP A CA   1 
ATOM   562  C  C    . ASP A 1 72  ? -9.501  37.188 9.514   1.00 53.22  ? 70  ASP A C    1 
ATOM   563  O  O    . ASP A 1 72  ? -10.251 37.906 10.178  1.00 62.14  ? 70  ASP A O    1 
ATOM   564  C  CB   . ASP A 1 72  ? -7.530  37.394 11.139  1.00 53.46  ? 70  ASP A CB   1 
ATOM   565  C  CG   . ASP A 1 72  ? -6.267  36.672 11.773  1.00 63.19  ? 70  ASP A CG   1 
ATOM   566  O  OD1  . ASP A 1 72  ? -5.331  37.326 12.327  1.00 64.16  ? 70  ASP A OD1  1 
ATOM   567  O  OD2  . ASP A 1 72  ? -6.197  35.422 11.703  1.00 65.28  ? 70  ASP A OD2  1 
ATOM   568  N  N    . ARG A 1 73  ? -9.695  36.977 8.217   1.00 51.69  ? 71  ARG A N    1 
ATOM   569  C  CA   . ARG A 1 73  ? -10.856 37.456 7.478   1.00 50.22  ? 71  ARG A CA   1 
ATOM   570  C  C    . ARG A 1 73  ? -11.989 36.446 7.425   1.00 54.43  ? 71  ARG A C    1 
ATOM   571  O  O    . ARG A 1 73  ? -13.020 36.728 6.797   1.00 55.60  ? 71  ARG A O    1 
ATOM   572  C  CB   . ARG A 1 73  ? -10.473 37.793 6.030   1.00 50.51  ? 71  ARG A CB   1 
ATOM   573  C  CG   . ARG A 1 73  ? -9.399  38.852 5.869   1.00 49.64  ? 71  ARG A CG   1 
ATOM   574  C  CD   . ARG A 1 73  ? -8.951  38.933 4.414   1.00 51.39  ? 71  ARG A CD   1 
ATOM   575  N  NE   . ARG A 1 73  ? -8.250  37.725 3.983   1.00 52.02  ? 71  ARG A NE   1 
ATOM   576  C  CZ   . ARG A 1 73  ? -7.813  37.517 2.745   1.00 49.80  ? 71  ARG A CZ   1 
ATOM   577  N  NH1  . ARG A 1 73  ? -8.006  38.437 1.804   1.00 56.42  ? 71  ARG A NH1  1 
ATOM   578  N  NH2  . ARG A 1 73  ? -7.175  36.392 2.447   1.00 45.97  ? 71  ARG A NH2  1 
ATOM   579  N  N    . VAL A 1 74  ? -11.809 35.255 8.004   1.00 49.73  ? 72  VAL A N    1 
ATOM   580  C  CA   . VAL A 1 74  ? -12.805 34.195 7.912   1.00 48.62  ? 72  VAL A CA   1 
ATOM   581  C  C    . VAL A 1 74  ? -12.887 33.542 9.285   1.00 47.61  ? 72  VAL A C    1 
ATOM   582  O  O    . VAL A 1 74  ? -12.009 33.720 10.131  1.00 48.17  ? 72  VAL A O    1 
ATOM   583  C  CB   . VAL A 1 74  ? -12.477 33.154 6.807   1.00 43.21  ? 72  VAL A CB   1 
ATOM   584  C  CG1  . VAL A 1 74  ? -12.504 33.819 5.419   1.00 43.21  ? 72  VAL A CG1  1 
ATOM   585  C  CG2  . VAL A 1 74  ? -11.165 32.406 7.066   1.00 38.57  ? 72  VAL A CG2  1 
ATOM   586  N  N    . THR A 1 75  ? -13.968 32.808 9.521   1.00 45.96  ? 73  THR A N    1 
ATOM   587  C  CA   . THR A 1 75  ? -14.238 32.241 10.836  1.00 41.23  ? 73  THR A CA   1 
ATOM   588  C  C    . THR A 1 75  ? -13.848 30.775 10.782  1.00 42.50  ? 73  THR A C    1 
ATOM   589  O  O    . THR A 1 75  ? -14.368 30.025 9.945   1.00 43.98  ? 73  THR A O    1 
ATOM   590  C  CB   . THR A 1 75  ? -15.712 32.392 11.205  1.00 41.87  ? 73  THR A CB   1 
ATOM   591  O  OG1  . THR A 1 75  ? -16.005 33.767 11.429  1.00 44.30  ? 73  THR A OG1  1 
ATOM   592  C  CG2  . THR A 1 75  ? -16.041 31.652 12.481  1.00 38.84  ? 73  THR A CG2  1 
ATOM   593  N  N    . TRP A 1 76  ? -12.926 30.371 11.647  1.00 39.13  ? 74  TRP A N    1 
ATOM   594  C  CA   . TRP A 1 76  ? -12.458 28.993 11.688  1.00 40.47  ? 74  TRP A CA   1 
ATOM   595  C  C    . TRP A 1 76  ? -13.192 28.229 12.777  1.00 42.04  ? 74  TRP A C    1 
ATOM   596  O  O    . TRP A 1 76  ? -13.404 28.750 13.879  1.00 43.02  ? 74  TRP A O    1 
ATOM   597  C  CB   . TRP A 1 76  ? -10.957 28.949 11.938  1.00 44.53  ? 74  TRP A CB   1 
ATOM   598  C  CG   . TRP A 1 76  ? -10.176 29.597 10.830  1.00 45.70  ? 74  TRP A CG   1 
ATOM   599  C  CD1  . TRP A 1 76  ? -9.937  30.939 10.657  1.00 42.66  ? 74  TRP A CD1  1 
ATOM   600  C  CD2  . TRP A 1 76  ? -9.560  28.933 9.720   1.00 45.34  ? 74  TRP A CD2  1 
ATOM   601  N  NE1  . TRP A 1 76  ? -9.195  31.140 9.512   1.00 45.67  ? 74  TRP A NE1  1 
ATOM   602  C  CE2  . TRP A 1 76  ? -8.947  29.925 8.926   1.00 45.45  ? 74  TRP A CE2  1 
ATOM   603  C  CE3  . TRP A 1 76  ? -9.452  27.591 9.332   1.00 45.98  ? 74  TRP A CE3  1 
ATOM   604  C  CZ2  . TRP A 1 76  ? -8.248  29.616 7.768   1.00 44.95  ? 74  TRP A CZ2  1 
ATOM   605  C  CZ3  . TRP A 1 76  ? -8.761  27.289 8.190   1.00 42.25  ? 74  TRP A CZ3  1 
ATOM   606  C  CH2  . TRP A 1 76  ? -8.169  28.297 7.413   1.00 43.02  ? 74  TRP A CH2  1 
ATOM   607  N  N    . VAL A 1 77  ? -13.598 26.995 12.460  1.00 42.56  ? 75  VAL A N    1 
ATOM   608  C  CA   . VAL A 1 77  ? -14.335 26.152 13.397  1.00 41.18  ? 75  VAL A CA   1 
ATOM   609  C  C    . VAL A 1 77  ? -13.855 24.714 13.271  1.00 47.93  ? 75  VAL A C    1 
ATOM   610  O  O    . VAL A 1 77  ? -13.227 24.314 12.282  1.00 47.75  ? 75  VAL A O    1 
ATOM   611  C  CB   . VAL A 1 77  ? -15.858 26.222 13.173  1.00 43.24  ? 75  VAL A CB   1 
ATOM   612  C  CG1  . VAL A 1 77  ? -16.367 27.623 13.462  1.00 42.53  ? 75  VAL A CG1  1 
ATOM   613  C  CG2  . VAL A 1 77  ? -16.194 25.815 11.792  1.00 39.84  ? 75  VAL A CG2  1 
ATOM   614  N  N    . LYS A 1 78  ? -14.217 23.922 14.278  1.00 45.86  ? 76  LYS A N    1 
ATOM   615  C  CA   . LYS A 1 78  ? -13.692 22.585 14.490  1.00 43.67  ? 76  LYS A CA   1 
ATOM   616  C  C    . LYS A 1 78  ? -14.745 21.500 14.354  1.00 43.94  ? 76  LYS A C    1 
ATOM   617  O  O    . LYS A 1 78  ? -14.389 20.318 14.321  1.00 49.65  ? 76  LYS A O    1 
ATOM   618  C  CB   . LYS A 1 78  ? -13.086 22.523 15.888  1.00 46.46  ? 76  LYS A CB   1 
ATOM   619  C  CG   . LYS A 1 78  ? -11.870 23.418 16.075  1.00 58.92  ? 76  LYS A CG   1 
ATOM   620  C  CD   . LYS A 1 78  ? -11.475 23.222 17.463  1.00 60.12  ? 76  LYS A CD   1 
ATOM   621  C  CE   . LYS A 1 78  ? -12.659 23.955 18.196  1.00 63.07  ? 76  LYS A CE   1 
ATOM   622  N  NZ   . LYS A 1 78  ? -12.766 24.148 19.664  1.00 60.70  ? 76  LYS A NZ   1 
ATOM   623  N  N    . SER A 1 79  ? -16.025 21.856 14.298  1.00 41.35  ? 77  SER A N    1 
ATOM   624  C  CA   . SER A 1 79  ? -17.081 20.857 14.276  1.00 39.89  ? 77  SER A CA   1 
ATOM   625  C  C    . SER A 1 79  ? -18.236 21.397 13.465  1.00 42.75  ? 77  SER A C    1 
ATOM   626  O  O    . SER A 1 79  ? -18.366 22.613 13.255  1.00 38.22  ? 77  SER A O    1 
ATOM   627  C  CB   . SER A 1 79  ? -17.586 20.482 15.681  1.00 44.90  ? 77  SER A CB   1 
ATOM   628  O  OG   . SER A 1 79  ? -18.285 21.565 16.291  1.00 41.68  ? 77  SER A OG   1 
ATOM   629  N  N    . VAL A 1 80  ? -19.075 20.453 13.019  1.00 42.53  ? 78  VAL A N    1 
ATOM   630  C  CA   . VAL A 1 80  ? -20.307 20.789 12.318  1.00 40.86  ? 78  VAL A CA   1 
ATOM   631  C  C    . VAL A 1 80  ? -21.150 21.750 13.146  1.00 43.77  ? 78  VAL A C    1 
ATOM   632  O  O    . VAL A 1 80  ? -21.652 22.761 12.638  1.00 43.65  ? 78  VAL A O    1 
ATOM   633  C  CB   . VAL A 1 80  ? -21.089 19.509 11.987  1.00 41.54  ? 78  VAL A CB   1 
ATOM   634  C  CG1  . VAL A 1 80  ? -22.521 19.868 11.639  1.00 40.52  ? 78  VAL A CG1  1 
ATOM   635  C  CG2  . VAL A 1 80  ? -20.431 18.776 10.833  1.00 45.14  ? 78  VAL A CG2  1 
ATOM   636  N  N    . ASP A 1 81  ? -21.338 21.452 14.438  1.00 45.12  ? 79  ASP A N    1 
ATOM   637  C  CA   . ASP A 1 81  ? -22.221 22.307 15.222  1.00 44.86  ? 79  ASP A CA   1 
ATOM   638  C  C    . ASP A 1 81  ? -21.624 23.695 15.388  1.00 42.88  ? 79  ASP A C    1 
ATOM   639  O  O    . ASP A 1 81  ? -22.346 24.702 15.337  1.00 45.07  ? 79  ASP A O    1 
ATOM   640  C  CB   . ASP A 1 81  ? -22.509 21.691 16.593  1.00 48.54  ? 79  ASP A CB   1 
ATOM   641  C  CG   . ASP A 1 81  ? -23.420 20.491 16.507  1.00 49.25  ? 79  ASP A CG   1 
ATOM   642  O  OD1  . ASP A 1 81  ? -24.225 20.418 15.546  1.00 48.09  ? 79  ASP A OD1  1 
ATOM   643  O  OD2  . ASP A 1 81  ? -23.339 19.640 17.419  1.00 54.80  ? 79  ASP A OD2  1 
ATOM   644  N  N    . GLU A 1 82  ? -20.311 23.767 15.618  1.00 39.35  ? 80  GLU A N    1 
ATOM   645  C  CA   . GLU A 1 82  ? -19.654 25.065 15.667  1.00 40.86  ? 80  GLU A CA   1 
ATOM   646  C  C    . GLU A 1 82  ? -19.878 25.826 14.364  1.00 43.69  ? 80  GLU A C    1 
ATOM   647  O  O    . GLU A 1 82  ? -20.140 27.035 14.375  1.00 38.32  ? 80  GLU A O    1 
ATOM   648  C  CB   . GLU A 1 82  ? -18.162 24.882 15.952  1.00 40.89  ? 80  GLU A CB   1 
ATOM   649  C  CG   . GLU A 1 82  ? -17.839 24.670 17.423  1.00 43.86  ? 80  GLU A CG   1 
ATOM   650  C  CD   . GLU A 1 82  ? -16.352 24.513 17.671  1.00 48.32  ? 80  GLU A CD   1 
ATOM   651  O  OE1  . GLU A 1 82  ? -15.585 24.646 16.694  1.00 52.25  ? 80  GLU A OE1  1 
ATOM   652  O  OE2  . GLU A 1 82  ? -15.937 24.298 18.838  1.00 51.63  ? 80  GLU A OE2  1 
ATOM   653  N  N    . ALA A 1 83  ? -19.820 25.119 13.229  1.00 41.28  ? 81  ALA A N    1 
ATOM   654  C  CA   . ALA A 1 83  ? -20.053 25.766 11.944  1.00 41.81  ? 81  ALA A CA   1 
ATOM   655  C  C    . ALA A 1 83  ? -21.482 26.286 11.837  1.00 42.80  ? 81  ALA A C    1 
ATOM   656  O  O    . ALA A 1 83  ? -21.707 27.420 11.399  1.00 44.28  ? 81  ALA A O    1 
ATOM   657  C  CB   . ALA A 1 83  ? -19.747 24.790 10.812  1.00 36.17  ? 81  ALA A CB   1 
ATOM   658  N  N    . ILE A 1 84  ? -22.470 25.469 12.226  1.00 41.80  ? 82  ILE A N    1 
ATOM   659  C  CA   . ILE A 1 84  ? -23.855 25.918 12.143  1.00 41.05  ? 82  ILE A CA   1 
ATOM   660  C  C    . ILE A 1 84  ? -24.058 27.147 13.014  1.00 47.38  ? 82  ILE A C    1 
ATOM   661  O  O    . ILE A 1 84  ? -24.822 28.062 12.670  1.00 45.73  ? 82  ILE A O    1 
ATOM   662  C  CB   . ILE A 1 84  ? -24.827 24.796 12.563  1.00 47.64  ? 82  ILE A CB   1 
ATOM   663  C  CG1  . ILE A 1 84  ? -24.620 23.521 11.736  1.00 40.57  ? 82  ILE A CG1  1 
ATOM   664  C  CG2  . ILE A 1 84  ? -26.282 25.303 12.486  1.00 44.24  ? 82  ILE A CG2  1 
ATOM   665  C  CD1  . ILE A 1 84  ? -24.849 23.745 10.336  1.00 48.30  ? 82  ILE A CD1  1 
ATOM   666  N  N    . ALA A 1 85  ? -23.439 27.154 14.191  1.00 44.09  ? 83  ALA A N    1 
ATOM   667  C  CA   . ALA A 1 85  ? -23.749 28.214 15.133  1.00 44.46  ? 83  ALA A CA   1 
ATOM   668  C  C    . ALA A 1 85  ? -23.074 29.506 14.725  1.00 44.90  ? 83  ALA A C    1 
ATOM   669  O  O    . ALA A 1 85  ? -23.593 30.593 15.020  1.00 42.62  ? 83  ALA A O    1 
ATOM   670  C  CB   . ALA A 1 85  ? -23.337 27.808 16.546  1.00 39.35  ? 83  ALA A CB   1 
ATOM   671  N  N    . ALA A 1 86  ? -21.926 29.406 14.048  1.00 40.91  ? 84  ALA A N    1 
ATOM   672  C  CA   . ALA A 1 86  ? -21.212 30.597 13.599  1.00 46.60  ? 84  ALA A CA   1 
ATOM   673  C  C    . ALA A 1 86  ? -22.006 31.389 12.569  1.00 48.18  ? 84  ALA A C    1 
ATOM   674  O  O    . ALA A 1 86  ? -21.680 32.556 12.319  1.00 47.25  ? 84  ALA A O    1 
ATOM   675  C  CB   . ALA A 1 86  ? -19.850 30.210 13.005  1.00 38.34  ? 84  ALA A CB   1 
ATOM   676  N  N    . CYS A 1 87  ? -23.026 30.779 11.957  1.00 43.59  ? 85  CYS A N    1 
ATOM   677  C  CA   . CYS A 1 87  ? -23.796 31.453 10.920  1.00 45.50  ? 85  CYS A CA   1 
ATOM   678  C  C    . CYS A 1 87  ? -24.828 32.389 11.489  1.00 46.03  ? 85  CYS A C    1 
ATOM   679  O  O    . CYS A 1 87  ? -25.246 33.321 10.793  1.00 52.28  ? 85  CYS A O    1 
ATOM   680  C  CB   . CYS A 1 87  ? -24.509 30.439 10.027  1.00 43.71  ? 85  CYS A CB   1 
ATOM   681  S  SG   . CYS A 1 87  ? -23.404 29.438 9.043   1.00 50.82  ? 85  CYS A SG   1 
ATOM   682  N  N    . GLY A 1 88  ? -25.273 32.139 12.713  1.00 49.06  ? 86  GLY A N    1 
ATOM   683  C  CA   . GLY A 1 88  ? -26.186 33.033 13.382  1.00 45.78  ? 86  GLY A CA   1 
ATOM   684  C  C    . GLY A 1 88  ? -27.628 32.766 13.003  1.00 50.99  ? 86  GLY A C    1 
ATOM   685  O  O    . GLY A 1 88  ? -27.989 31.697 12.513  1.00 53.46  ? 86  GLY A O    1 
ATOM   686  N  N    . ASP A 1 89  ? -28.463 33.778 13.248  1.00 52.14  ? 87  ASP A N    1 
ATOM   687  C  CA   . ASP A 1 89  ? -29.884 33.753 12.919  1.00 55.95  ? 87  ASP A CA   1 
ATOM   688  C  C    . ASP A 1 89  ? -30.089 34.143 11.454  1.00 53.61  ? 87  ASP A C    1 
ATOM   689  O  O    . ASP A 1 89  ? -30.381 35.294 11.118  1.00 58.63  ? 87  ASP A O    1 
ATOM   690  C  CB   . ASP A 1 89  ? -30.649 34.682 13.852  1.00 54.28  ? 87  ASP A CB   1 
ATOM   691  C  CG   . ASP A 1 89  ? -32.130 34.431 13.816  1.00 63.71  ? 87  ASP A CG   1 
ATOM   692  O  OD1  . ASP A 1 89  ? -32.516 33.406 13.206  1.00 64.72  ? 87  ASP A OD1  1 
ATOM   693  O  OD2  . ASP A 1 89  ? -32.905 35.244 14.386  1.00 68.03  ? 87  ASP A OD2  1 
ATOM   694  N  N    . VAL A 1 90  ? -29.942 33.164 10.570  1.00 52.21  ? 88  VAL A N    1 
ATOM   695  C  CA   . VAL A 1 90  ? -30.185 33.376 9.140   1.00 50.70  ? 88  VAL A CA   1 
ATOM   696  C  C    . VAL A 1 90  ? -31.155 32.314 8.648   1.00 55.60  ? 88  VAL A C    1 
ATOM   697  O  O    . VAL A 1 90  ? -31.287 31.235 9.258   1.00 60.18  ? 88  VAL A O    1 
ATOM   698  C  CB   . VAL A 1 90  ? -28.873 33.343 8.315   1.00 52.08  ? 88  VAL A CB   1 
ATOM   699  C  CG1  . VAL A 1 90  ? -27.911 34.447 8.750   1.00 49.76  ? 88  VAL A CG1  1 
ATOM   700  C  CG2  . VAL A 1 90  ? -28.215 31.983 8.405   1.00 48.63  ? 88  VAL A CG2  1 
ATOM   701  N  N    . PRO A 1 91  ? -31.850 32.573 7.532   1.00 54.88  ? 89  PRO A N    1 
ATOM   702  C  CA   . PRO A 1 91  ? -32.830 31.595 7.028   1.00 52.32  ? 89  PRO A CA   1 
ATOM   703  C  C    . PRO A 1 91  ? -32.209 30.369 6.396   1.00 53.60  ? 89  PRO A C    1 
ATOM   704  O  O    . PRO A 1 91  ? -32.801 29.283 6.481   1.00 54.15  ? 89  PRO A O    1 
ATOM   705  C  CB   . PRO A 1 91  ? -33.628 32.401 5.996   1.00 46.03  ? 89  PRO A CB   1 
ATOM   706  C  CG   . PRO A 1 91  ? -33.389 33.829 6.368   1.00 48.69  ? 89  PRO A CG   1 
ATOM   707  C  CD   . PRO A 1 91  ? -31.977 33.865 6.839   1.00 49.50  ? 89  PRO A CD   1 
ATOM   708  N  N    . GLU A 1 92  ? -31.047 30.512 5.749   1.00 52.86  ? 90  GLU A N    1 
ATOM   709  C  CA   . GLU A 1 92  ? -30.455 29.444 4.952   1.00 46.21  ? 90  GLU A CA   1 
ATOM   710  C  C    . GLU A 1 92  ? -28.934 29.503 5.032   1.00 47.62  ? 90  GLU A C    1 
ATOM   711  O  O    . GLU A 1 92  ? -28.337 30.560 4.797   1.00 44.96  ? 90  GLU A O    1 
ATOM   712  C  CB   . GLU A 1 92  ? -30.900 29.546 3.488   1.00 44.77  ? 90  GLU A CB   1 
ATOM   713  C  CG   . GLU A 1 92  ? -30.463 28.363 2.649   1.00 43.75  ? 90  GLU A CG   1 
ATOM   714  C  CD   . GLU A 1 92  ? -31.009 28.400 1.235   1.00 45.16  ? 90  GLU A CD   1 
ATOM   715  O  OE1  . GLU A 1 92  ? -31.530 29.459 0.808   1.00 42.87  ? 90  GLU A OE1  1 
ATOM   716  O  OE2  . GLU A 1 92  ? -30.907 27.355 0.544   1.00 43.27  ? 90  GLU A OE2  1 
ATOM   717  N  N    . ILE A 1 93  ? -28.314 28.364 5.341   1.00 44.98  ? 91  ILE A N    1 
ATOM   718  C  CA   . ILE A 1 93  ? -26.864 28.214 5.406   1.00 42.65  ? 91  ILE A CA   1 
ATOM   719  C  C    . ILE A 1 93  ? -26.407 27.401 4.200   1.00 41.58  ? 91  ILE A C    1 
ATOM   720  O  O    . ILE A 1 93  ? -26.967 26.331 3.926   1.00 41.41  ? 91  ILE A O    1 
ATOM   721  C  CB   . ILE A 1 93  ? -26.449 27.523 6.715   1.00 42.87  ? 91  ILE A CB   1 
ATOM   722  C  CG1  . ILE A 1 93  ? -26.672 28.448 7.905   1.00 42.87  ? 91  ILE A CG1  1 
ATOM   723  C  CG2  . ILE A 1 93  ? -25.023 27.073 6.650   1.00 40.31  ? 91  ILE A CG2  1 
ATOM   724  C  CD1  . ILE A 1 93  ? -26.659 27.713 9.228   1.00 50.04  ? 91  ILE A CD1  1 
ATOM   725  N  N    . MET A 1 94  ? -25.377 27.881 3.493   1.00 39.12  ? 92  MET A N    1 
ATOM   726  C  CA   . MET A 1 94  ? -24.920 27.233 2.265   1.00 39.35  ? 92  MET A CA   1 
ATOM   727  C  C    . MET A 1 94  ? -23.586 26.526 2.484   1.00 37.27  ? 92  MET A C    1 
ATOM   728  O  O    . MET A 1 94  ? -22.568 27.180 2.730   1.00 39.08  ? 92  MET A O    1 
ATOM   729  C  CB   . MET A 1 94  ? -24.796 28.229 1.110   1.00 37.17  ? 92  MET A CB   1 
ATOM   730  C  CG   . MET A 1 94  ? -25.997 29.113 0.894   1.00 36.32  ? 92  MET A CG   1 
ATOM   731  S  SD   . MET A 1 94  ? -27.440 28.153 0.351   1.00 40.10  ? 92  MET A SD   1 
ATOM   732  C  CE   . MET A 1 94  ? -26.892 27.563 -1.230  1.00 34.82  ? 92  MET A CE   1 
ATOM   733  N  N    . VAL A 1 95  ? -23.595 25.199 2.362   1.00 36.86  ? 93  VAL A N    1 
ATOM   734  C  CA   . VAL A 1 95  ? -22.387 24.382 2.423   1.00 35.87  ? 93  VAL A CA   1 
ATOM   735  C  C    . VAL A 1 95  ? -21.864 24.191 1.010   1.00 41.00  ? 93  VAL A C    1 
ATOM   736  O  O    . VAL A 1 95  ? -22.551 23.612 0.162   1.00 42.34  ? 93  VAL A O    1 
ATOM   737  C  CB   . VAL A 1 95  ? -22.673 23.030 3.080   1.00 37.21  ? 93  VAL A CB   1 
ATOM   738  C  CG1  . VAL A 1 95  ? -21.392 22.230 3.172   1.00 34.87  ? 93  VAL A CG1  1 
ATOM   739  C  CG2  . VAL A 1 95  ? -23.292 23.250 4.470   1.00 32.87  ? 93  VAL A CG2  1 
ATOM   740  N  N    . ILE A 1 96  ? -20.652 24.678 0.740   1.00 38.14  ? 94  ILE A N    1 
ATOM   741  C  CA   . ILE A 1 96  ? -20.209 24.842 -0.636  1.00 36.84  ? 94  ILE A CA   1 
ATOM   742  C  C    . ILE A 1 96  ? -19.098 23.900 -1.004  1.00 39.25  ? 94  ILE A C    1 
ATOM   743  O  O    . ILE A 1 96  ? -18.568 23.986 -2.125  1.00 38.63  ? 94  ILE A O    1 
ATOM   744  C  CB   . ILE A 1 96  ? -19.784 26.287 -0.918  1.00 38.58  ? 94  ILE A CB   1 
ATOM   745  C  CG1  . ILE A 1 96  ? -18.549 26.640 -0.081  1.00 37.65  ? 94  ILE A CG1  1 
ATOM   746  C  CG2  . ILE A 1 96  ? -20.954 27.223 -0.628  1.00 37.04  ? 94  ILE A CG2  1 
ATOM   747  C  CD1  . ILE A 1 96  ? -17.877 27.922 -0.549  1.00 37.11  ? 94  ILE A CD1  1 
ATOM   748  N  N    . GLY A 1 97  ? -18.715 22.999 -0.119  1.00 40.85  ? 95  GLY A N    1 
ATOM   749  C  CA   . GLY A 1 97  ? -17.830 22.004 -0.649  1.00 39.43  ? 95  GLY A CA   1 
ATOM   750  C  C    . GLY A 1 97  ? -16.653 21.582 0.183   1.00 44.35  ? 95  GLY A C    1 
ATOM   751  O  O    . GLY A 1 97  ? -16.367 22.122 1.254   1.00 41.32  ? 95  GLY A O    1 
ATOM   752  N  N    . GLY A 1 98  ? -15.903 20.673 -0.419  1.00 46.22  ? 96  GLY A N    1 
ATOM   753  C  CA   . GLY A 1 98  ? -15.374 19.552 0.290   1.00 49.10  ? 96  GLY A CA   1 
ATOM   754  C  C    . GLY A 1 98  ? -16.365 18.416 0.105   1.00 45.64  ? 96  GLY A C    1 
ATOM   755  O  O    . GLY A 1 98  ? -17.497 18.496 0.597   1.00 46.49  ? 96  GLY A O    1 
ATOM   756  N  N    . GLY A 1 99  ? -15.983 17.372 -0.627  1.00 40.85  ? 97  GLY A N    1 
ATOM   757  C  CA   . GLY A 1 99  ? -16.755 16.142 -0.572  1.00 44.37  ? 97  GLY A CA   1 
ATOM   758  C  C    . GLY A 1 99  ? -16.900 15.639 0.850   1.00 45.10  ? 97  GLY A C    1 
ATOM   759  O  O    . GLY A 1 99  ? -17.981 15.207 1.263   1.00 43.51  ? 97  GLY A O    1 
ATOM   760  N  N    . ARG A 1 100 ? -15.826 15.720 1.632   1.00 43.75  ? 98  ARG A N    1 
ATOM   761  C  CA   . ARG A 1 100 ? -15.912 15.333 3.037   1.00 51.65  ? 98  ARG A CA   1 
ATOM   762  C  C    . ARG A 1 100 ? -16.819 16.283 3.814   1.00 47.66  ? 98  ARG A C    1 
ATOM   763  O  O    . ARG A 1 100 ? -17.554 15.865 4.716   1.00 50.34  ? 98  ARG A O    1 
ATOM   764  C  CB   . ARG A 1 100 ? -14.510 15.292 3.644   1.00 48.90  ? 98  ARG A CB   1 
ATOM   765  C  CG   . ARG A 1 100 ? -14.461 15.119 5.152   1.00 59.89  ? 98  ARG A CG   1 
ATOM   766  C  CD   . ARG A 1 100 ? -14.641 13.665 5.580   1.00 63.36  ? 98  ARG A CD   1 
ATOM   767  N  NE   . ARG A 1 100 ? -14.805 13.527 7.033   1.00 72.62  ? 98  ARG A NE   1 
ATOM   768  C  CZ   . ARG A 1 100 ? -15.783 12.832 7.618   1.00 76.56  ? 98  ARG A CZ   1 
ATOM   769  N  NH1  . ARG A 1 100 ? -16.698 12.210 6.871   1.00 70.72  ? 98  ARG A NH1  1 
ATOM   770  N  NH2  . ARG A 1 100 ? -15.849 12.762 8.949   1.00 73.39  ? 98  ARG A NH2  1 
ATOM   771  N  N    . VAL A 1 101 ? -16.778 17.567 3.481   1.00 48.05  ? 99  VAL A N    1 
ATOM   772  C  CA   . VAL A 1 101 ? -17.681 18.521 4.111   1.00 44.98  ? 99  VAL A CA   1 
ATOM   773  C  C    . VAL A 1 101 ? -19.127 18.206 3.739   1.00 44.99  ? 99  VAL A C    1 
ATOM   774  O  O    . VAL A 1 101 ? -20.006 18.150 4.605   1.00 45.31  ? 99  VAL A O    1 
ATOM   775  C  CB   . VAL A 1 101 ? -17.270 19.952 3.725   1.00 44.29  ? 99  VAL A CB   1 
ATOM   776  C  CG1  . VAL A 1 101 ? -18.290 20.933 4.191   1.00 42.03  ? 99  VAL A CG1  1 
ATOM   777  C  CG2  . VAL A 1 101 ? -15.892 20.274 4.336   1.00 42.97  ? 99  VAL A CG2  1 
ATOM   778  N  N    . TYR A 1 102 ? -19.395 17.972 2.447   1.00 43.96  ? 100 TYR A N    1 
ATOM   779  C  CA   . TYR A 1 102 ? -20.732 17.560 2.025   1.00 41.40  ? 100 TYR A CA   1 
ATOM   780  C  C    . TYR A 1 102 ? -21.214 16.364 2.837   1.00 44.59  ? 100 TYR A C    1 
ATOM   781  O  O    . TYR A 1 102 ? -22.366 16.317 3.296   1.00 41.65  ? 100 TYR A O    1 
ATOM   782  C  CB   . TYR A 1 102 ? -20.730 17.194 0.541   1.00 41.10  ? 100 TYR A CB   1 
ATOM   783  C  CG   . TYR A 1 102 ? -20.550 18.345 -0.433  1.00 39.95  ? 100 TYR A CG   1 
ATOM   784  C  CD1  . TYR A 1 102 ? -21.186 19.554 -0.231  1.00 37.62  ? 100 TYR A CD1  1 
ATOM   785  C  CD2  . TYR A 1 102 ? -19.764 18.194 -1.580  1.00 42.14  ? 100 TYR A CD2  1 
ATOM   786  C  CE1  . TYR A 1 102 ? -21.033 20.595 -1.136  1.00 38.64  ? 100 TYR A CE1  1 
ATOM   787  C  CE2  . TYR A 1 102 ? -19.608 19.225 -2.488  1.00 38.26  ? 100 TYR A CE2  1 
ATOM   788  C  CZ   . TYR A 1 102 ? -20.241 20.422 -2.257  1.00 39.48  ? 100 TYR A CZ   1 
ATOM   789  O  OH   . TYR A 1 102 ? -20.100 21.455 -3.155  1.00 36.59  ? 100 TYR A OH   1 
ATOM   790  N  N    . GLU A 1 103 ? -20.345 15.367 3.002   1.00 39.31  ? 101 GLU A N    1 
ATOM   791  C  CA   . GLU A 1 103 ? -20.749 14.164 3.713   1.00 43.14  ? 101 GLU A CA   1 
ATOM   792  C  C    . GLU A 1 103 ? -21.168 14.486 5.141   1.00 49.39  ? 101 GLU A C    1 
ATOM   793  O  O    . GLU A 1 103 ? -22.095 13.870 5.676   1.00 48.72  ? 101 GLU A O    1 
ATOM   794  C  CB   . GLU A 1 103 ? -19.602 13.160 3.715   1.00 50.60  ? 101 GLU A CB   1 
ATOM   795  C  CG   . GLU A 1 103 ? -19.961 11.789 4.245   1.00 57.15  ? 101 GLU A CG   1 
ATOM   796  C  CD   . GLU A 1 103 ? -18.792 10.829 4.122   1.00 77.75  ? 101 GLU A CD   1 
ATOM   797  O  OE1  . GLU A 1 103 ? -18.846 9.731  4.729   1.00 85.59  ? 101 GLU A OE1  1 
ATOM   798  O  OE2  . GLU A 1 103 ? -17.802 11.192 3.437   1.00 76.59  ? 101 GLU A OE2  1 
ATOM   799  N  N    . GLN A 1 104 ? -20.494 15.446 5.780   1.00 44.51  ? 102 GLN A N    1 
ATOM   800  C  CA   . GLN A 1 104 ? -20.764 15.716 7.185   1.00 47.07  ? 102 GLN A CA   1 
ATOM   801  C  C    . GLN A 1 104 ? -22.050 16.510 7.391   1.00 45.43  ? 102 GLN A C    1 
ATOM   802  O  O    . GLN A 1 104 ? -22.724 16.338 8.417   1.00 42.26  ? 102 GLN A O    1 
ATOM   803  C  CB   . GLN A 1 104 ? -19.585 16.456 7.797   1.00 44.59  ? 102 GLN A CB   1 
ATOM   804  C  CG   . GLN A 1 104 ? -18.401 15.567 8.055   1.00 48.57  ? 102 GLN A CG   1 
ATOM   805  C  CD   . GLN A 1 104 ? -17.258 16.341 8.691   1.00 58.32  ? 102 GLN A CD   1 
ATOM   806  O  OE1  . GLN A 1 104 ? -16.383 16.880 7.994   1.00 61.13  ? 102 GLN A OE1  1 
ATOM   807  N  NE2  . GLN A 1 104 ? -17.279 16.435 10.028  1.00 57.24  ? 102 GLN A NE2  1 
ATOM   808  N  N    . PHE A 1 105 ? -22.417 17.363 6.436   1.00 44.55  ? 103 PHE A N    1 
ATOM   809  C  CA   . PHE A 1 105 ? -23.648 18.141 6.534   1.00 41.81  ? 103 PHE A CA   1 
ATOM   810  C  C    . PHE A 1 105 ? -24.858 17.476 5.898   1.00 43.14  ? 103 PHE A C    1 
ATOM   811  O  O    . PHE A 1 105 ? -25.985 17.825 6.248   1.00 48.09  ? 103 PHE A O    1 
ATOM   812  C  CB   . PHE A 1 105 ? -23.436 19.516 5.913   1.00 40.36  ? 103 PHE A CB   1 
ATOM   813  C  CG   . PHE A 1 105 ? -22.576 20.410 6.767   1.00 45.13  ? 103 PHE A CG   1 
ATOM   814  C  CD1  . PHE A 1 105 ? -21.192 20.400 6.638   1.00 41.17  ? 103 PHE A CD1  1 
ATOM   815  C  CD2  . PHE A 1 105 ? -23.143 21.199 7.756   1.00 43.60  ? 103 PHE A CD2  1 
ATOM   816  C  CE1  . PHE A 1 105 ? -20.385 21.204 7.449   1.00 40.98  ? 103 PHE A CE1  1 
ATOM   817  C  CE2  . PHE A 1 105 ? -22.338 22.008 8.574   1.00 44.22  ? 103 PHE A CE2  1 
ATOM   818  C  CZ   . PHE A 1 105 ? -20.956 22.010 8.412   1.00 36.88  ? 103 PHE A CZ   1 
ATOM   819  N  N    . LEU A 1 106 ? -24.674 16.507 5.013   1.00 43.80  ? 104 LEU A N    1 
ATOM   820  C  CA   . LEU A 1 106 ? -25.829 15.913 4.351   1.00 45.81  ? 104 LEU A CA   1 
ATOM   821  C  C    . LEU A 1 106 ? -26.933 15.516 5.322   1.00 49.79  ? 104 LEU A C    1 
ATOM   822  O  O    . LEU A 1 106 ? -28.105 15.824 5.038   1.00 52.04  ? 104 LEU A O    1 
ATOM   823  C  CB   . LEU A 1 106 ? -25.400 14.697 3.524   1.00 45.77  ? 104 LEU A CB   1 
ATOM   824  C  CG   . LEU A 1 106 ? -26.541 14.144 2.668   1.00 47.51  ? 104 LEU A CG   1 
ATOM   825  C  CD1  . LEU A 1 106 ? -27.174 15.271 1.876   1.00 46.22  ? 104 LEU A CD1  1 
ATOM   826  C  CD2  . LEU A 1 106 ? -26.074 13.041 1.755   1.00 47.50  ? 104 LEU A CD2  1 
ATOM   827  N  N    . PRO A 1 107 ? -26.656 14.866 6.454   1.00 49.04  ? 105 PRO A N    1 
ATOM   828  C  CA   . PRO A 1 107 ? -27.754 14.449 7.337   1.00 46.76  ? 105 PRO A CA   1 
ATOM   829  C  C    . PRO A 1 107 ? -28.492 15.615 7.947   1.00 50.07  ? 105 PRO A C    1 
ATOM   830  O  O    . PRO A 1 107 ? -29.636 15.443 8.386   1.00 56.04  ? 105 PRO A O    1 
ATOM   831  C  CB   . PRO A 1 107 ? -27.043 13.622 8.417   1.00 47.32  ? 105 PRO A CB   1 
ATOM   832  C  CG   . PRO A 1 107 ? -25.775 13.171 7.756   1.00 48.26  ? 105 PRO A CG   1 
ATOM   833  C  CD   . PRO A 1 107 ? -25.361 14.361 6.933   1.00 49.16  ? 105 PRO A CD   1 
ATOM   834  N  N    . LYS A 1 108 ? -27.881 16.795 8.005   1.00 48.41  ? 106 LYS A N    1 
ATOM   835  C  CA   . LYS A 1 108 ? -28.546 17.977 8.532   1.00 49.62  ? 106 LYS A CA   1 
ATOM   836  C  C    . LYS A 1 108 ? -29.166 18.864 7.454   1.00 54.00  ? 106 LYS A C    1 
ATOM   837  O  O    . LYS A 1 108 ? -29.705 19.927 7.782   1.00 58.25  ? 106 LYS A O    1 
ATOM   838  C  CB   . LYS A 1 108 ? -27.564 18.798 9.378   1.00 48.49  ? 106 LYS A CB   1 
ATOM   839  C  CG   . LYS A 1 108 ? -27.105 18.078 10.641  1.00 47.15  ? 106 LYS A CG   1 
ATOM   840  C  CD   . LYS A 1 108 ? -26.540 19.044 11.667  1.00 45.44  ? 106 LYS A CD   1 
ATOM   841  C  CE   . LYS A 1 108 ? -26.455 18.416 13.051  1.00 48.71  ? 106 LYS A CE   1 
ATOM   842  N  NZ   . LYS A 1 108 ? -27.314 19.135 14.047  1.00 58.37  ? 106 LYS A NZ   1 
ATOM   843  N  N    . ALA A 1 109 ? -29.124 18.461 6.188   1.00 51.77  ? 107 ALA A N    1 
ATOM   844  C  CA   . ALA A 1 109 ? -29.516 19.331 5.090   1.00 51.25  ? 107 ALA A CA   1 
ATOM   845  C  C    . ALA A 1 109 ? -30.950 19.044 4.684   1.00 51.46  ? 107 ALA A C    1 
ATOM   846  O  O    . ALA A 1 109 ? -31.379 17.887 4.697   1.00 54.85  ? 107 ALA A O    1 
ATOM   847  C  CB   . ALA A 1 109 ? -28.586 19.147 3.889   1.00 45.53  ? 107 ALA A CB   1 
ATOM   848  N  N    . GLN A 1 110 ? -31.687 20.109 4.332   1.00 46.85  ? 108 GLN A N    1 
ATOM   849  C  CA   . GLN A 1 110 ? -33.048 20.012 3.807   1.00 52.77  ? 108 GLN A CA   1 
ATOM   850  C  C    . GLN A 1 110 ? -33.153 20.353 2.334   1.00 48.77  ? 108 GLN A C    1 
ATOM   851  O  O    . GLN A 1 110 ? -34.231 20.170 1.761   1.00 52.75  ? 108 GLN A O    1 
ATOM   852  C  CB   . GLN A 1 110 ? -34.019 20.953 4.548   1.00 59.33  ? 108 GLN A CB   1 
ATOM   853  C  CG   . GLN A 1 110 ? -34.615 20.485 5.863   1.00 67.29  ? 108 GLN A CG   1 
ATOM   854  C  CD   . GLN A 1 110 ? -33.569 20.327 6.927   1.00 76.36  ? 108 GLN A CD   1 
ATOM   855  O  OE1  . GLN A 1 110 ? -32.911 21.311 7.322   1.00 77.64  ? 108 GLN A OE1  1 
ATOM   856  N  NE2  . GLN A 1 110 ? -33.444 19.092 7.460   1.00 76.28  ? 108 GLN A NE2  1 
ATOM   857  N  N    . LYS A 1 111 ? -32.084 20.849 1.712   1.00 44.70  ? 109 LYS A N    1 
ATOM   858  C  CA   . LYS A 1 111 ? -32.134 21.351 0.346   1.00 43.88  ? 109 LYS A CA   1 
ATOM   859  C  C    . LYS A 1 111 ? -30.794 21.098 -0.345  1.00 45.20  ? 109 LYS A C    1 
ATOM   860  O  O    . LYS A 1 111 ? -29.733 21.271 0.266   1.00 46.18  ? 109 LYS A O    1 
ATOM   861  C  CB   . LYS A 1 111 ? -32.475 22.846 0.366   1.00 45.00  ? 109 LYS A CB   1 
ATOM   862  C  CG   . LYS A 1 111 ? -32.941 23.418 -0.935  1.00 46.28  ? 109 LYS A CG   1 
ATOM   863  C  CD   . LYS A 1 111 ? -33.471 24.835 -0.738  1.00 46.01  ? 109 LYS A CD   1 
ATOM   864  C  CE   . LYS A 1 111 ? -34.158 25.311 -2.006  1.00 46.30  ? 109 LYS A CE   1 
ATOM   865  N  NZ   . LYS A 1 111 ? -34.555 26.755 -1.950  1.00 51.61  ? 109 LYS A NZ   1 
ATOM   866  N  N    . LEU A 1 112 ? -30.836 20.684 -1.615  1.00 46.17  ? 110 LEU A N    1 
ATOM   867  C  CA   . LEU A 1 112 ? -29.626 20.469 -2.407  1.00 40.54  ? 110 LEU A CA   1 
ATOM   868  C  C    . LEU A 1 112 ? -29.733 21.252 -3.705  1.00 39.03  ? 110 LEU A C    1 
ATOM   869  O  O    . LEU A 1 112 ? -30.762 21.183 -4.381  1.00 42.49  ? 110 LEU A O    1 
ATOM   870  C  CB   . LEU A 1 112 ? -29.426 18.990 -2.742  1.00 40.76  ? 110 LEU A CB   1 
ATOM   871  C  CG   . LEU A 1 112 ? -29.492 17.994 -1.588  1.00 44.70  ? 110 LEU A CG   1 
ATOM   872  C  CD1  . LEU A 1 112 ? -29.653 16.579 -2.146  1.00 43.51  ? 110 LEU A CD1  1 
ATOM   873  C  CD2  . LEU A 1 112 ? -28.260 18.114 -0.734  1.00 42.73  ? 110 LEU A CD2  1 
ATOM   874  N  N    . TYR A 1 113 ? -28.671 21.980 -4.058  1.00 39.94  ? 111 TYR A N    1 
ATOM   875  C  CA   . TYR A 1 113 ? -28.544 22.658 -5.346  1.00 36.43  ? 111 TYR A CA   1 
ATOM   876  C  C    . TYR A 1 113 ? -27.457 21.930 -6.128  1.00 40.86  ? 111 TYR A C    1 
ATOM   877  O  O    . TYR A 1 113 ? -26.274 22.003 -5.771  1.00 41.23  ? 111 TYR A O    1 
ATOM   878  C  CB   . TYR A 1 113 ? -28.160 24.134 -5.185  1.00 35.86  ? 111 TYR A CB   1 
ATOM   879  C  CG   . TYR A 1 113 ? -29.086 24.986 -4.346  1.00 38.37  ? 111 TYR A CG   1 
ATOM   880  C  CD1  . TYR A 1 113 ? -29.127 24.844 -2.959  1.00 40.23  ? 111 TYR A CD1  1 
ATOM   881  C  CD2  . TYR A 1 113 ? -29.922 25.932 -4.936  1.00 41.42  ? 111 TYR A CD2  1 
ATOM   882  C  CE1  . TYR A 1 113 ? -29.969 25.628 -2.172  1.00 40.34  ? 111 TYR A CE1  1 
ATOM   883  C  CE2  . TYR A 1 113 ? -30.772 26.723 -4.163  1.00 42.17  ? 111 TYR A CE2  1 
ATOM   884  C  CZ   . TYR A 1 113 ? -30.787 26.559 -2.784  1.00 43.88  ? 111 TYR A CZ   1 
ATOM   885  O  OH   . TYR A 1 113 ? -31.610 27.332 -2.001  1.00 43.69  ? 111 TYR A OH   1 
ATOM   886  N  N    . LEU A 1 114 ? -27.836 21.246 -7.199  1.00 39.61  ? 112 LEU A N    1 
ATOM   887  C  CA   . LEU A 1 114 ? -26.893 20.432 -7.945  1.00 39.85  ? 112 LEU A CA   1 
ATOM   888  C  C    . LEU A 1 114 ? -26.806 20.937 -9.376  1.00 38.16  ? 112 LEU A C    1 
ATOM   889  O  O    . LEU A 1 114 ? -27.831 21.263 -9.983  1.00 39.05  ? 112 LEU A O    1 
ATOM   890  C  CB   . LEU A 1 114 ? -27.317 18.965 -7.945  1.00 39.25  ? 112 LEU A CB   1 
ATOM   891  C  CG   . LEU A 1 114 ? -27.417 18.276 -6.587  1.00 40.28  ? 112 LEU A CG   1 
ATOM   892  C  CD1  . LEU A 1 114 ? -27.781 16.828 -6.800  1.00 41.09  ? 112 LEU A CD1  1 
ATOM   893  C  CD2  . LEU A 1 114 ? -26.140 18.413 -5.794  1.00 41.54  ? 112 LEU A CD2  1 
ATOM   894  N  N    . THR A 1 115 ? -25.578 21.007 -9.908  1.00 38.29  ? 113 THR A N    1 
ATOM   895  C  CA   . THR A 1 115 ? -25.333 21.246 -11.326 1.00 39.78  ? 113 THR A CA   1 
ATOM   896  C  C    . THR A 1 115 ? -24.799 19.952 -11.917 1.00 41.68  ? 113 THR A C    1 
ATOM   897  O  O    . THR A 1 115 ? -23.701 19.520 -11.560 1.00 43.09  ? 113 THR A O    1 
ATOM   898  C  CB   . THR A 1 115 ? -24.325 22.363 -11.560 1.00 42.14  ? 113 THR A CB   1 
ATOM   899  O  OG1  . THR A 1 115 ? -24.747 23.560 -10.890 1.00 44.05  ? 113 THR A OG1  1 
ATOM   900  C  CG2  . THR A 1 115 ? -24.247 22.631 -13.055 1.00 43.30  ? 113 THR A CG2  1 
ATOM   901  N  N    . HIS A 1 116 ? -25.574 19.334 -12.807 1.00 41.86  ? 114 HIS A N    1 
ATOM   902  C  CA   . HIS A 1 116 ? -25.163 18.126 -13.508 1.00 43.54  ? 114 HIS A CA   1 
ATOM   903  C  C    . HIS A 1 116 ? -24.495 18.547 -14.805 1.00 44.43  ? 114 HIS A C    1 
ATOM   904  O  O    . HIS A 1 116 ? -25.158 19.058 -15.716 1.00 45.10  ? 114 HIS A O    1 
ATOM   905  C  CB   . HIS A 1 116 ? -26.355 17.217 -13.798 1.00 41.57  ? 114 HIS A CB   1 
ATOM   906  C  CG   . HIS A 1 116 ? -27.166 16.873 -12.585 1.00 43.18  ? 114 HIS A CG   1 
ATOM   907  N  ND1  . HIS A 1 116 ? -26.872 15.800 -11.768 1.00 41.10  ? 114 HIS A ND1  1 
ATOM   908  C  CD2  . HIS A 1 116 ? -28.278 17.447 -12.063 1.00 40.70  ? 114 HIS A CD2  1 
ATOM   909  C  CE1  . HIS A 1 116 ? -27.758 15.738 -10.791 1.00 40.04  ? 114 HIS A CE1  1 
ATOM   910  N  NE2  . HIS A 1 116 ? -28.621 16.729 -10.944 1.00 40.97  ? 114 HIS A NE2  1 
ATOM   911  N  N    . ILE A 1 117 ? -23.189 18.318 -14.893 1.00 44.94  ? 115 ILE A N    1 
ATOM   912  C  CA   . ILE A 1 117 ? -22.382 18.714 -16.035 1.00 44.21  ? 115 ILE A CA   1 
ATOM   913  C  C    . ILE A 1 117 ? -22.125 17.479 -16.878 1.00 48.41  ? 115 ILE A C    1 
ATOM   914  O  O    . ILE A 1 117 ? -21.716 16.430 -16.365 1.00 47.34  ? 115 ILE A O    1 
ATOM   915  C  CB   . ILE A 1 117 ? -21.077 19.380 -15.572 1.00 47.19  ? 115 ILE A CB   1 
ATOM   916  C  CG1  . ILE A 1 117 ? -21.411 20.555 -14.664 1.00 43.55  ? 115 ILE A CG1  1 
ATOM   917  C  CG2  . ILE A 1 117 ? -20.212 19.804 -16.742 1.00 48.93  ? 115 ILE A CG2  1 
ATOM   918  C  CD1  . ILE A 1 117 ? -20.201 21.162 -14.020 1.00 50.11  ? 115 ILE A CD1  1 
ATOM   919  N  N    . ASP A 1 118 ? -22.430 17.580 -18.165 1.00 50.15  ? 116 ASP A N    1 
ATOM   920  C  CA   A ASP A 1 118 ? -22.202 16.459 -19.078 0.65 52.50  ? 116 ASP A CA   1 
ATOM   921  C  CA   B ASP A 1 118 ? -22.198 16.499 -19.113 0.35 52.52  ? 116 ASP A CA   1 
ATOM   922  C  C    . ASP A 1 118 ? -20.729 16.506 -19.514 1.00 56.65  ? 116 ASP A C    1 
ATOM   923  O  O    . ASP A 1 118 ? -20.358 16.881 -20.625 1.00 61.36  ? 116 ASP A O    1 
ATOM   924  C  CB   A ASP A 1 118 ? -23.216 16.485 -20.228 0.65 50.20  ? 116 ASP A CB   1 
ATOM   925  C  CB   B ASP A 1 118 ? -23.085 16.659 -20.337 0.35 50.23  ? 116 ASP A CB   1 
ATOM   926  C  CG   A ASP A 1 118 ? -24.677 16.179 -19.742 0.65 52.61  ? 116 ASP A CG   1 
ATOM   927  C  CG   B ASP A 1 118 ? -22.872 15.569 -21.340 0.35 54.19  ? 116 ASP A CG   1 
ATOM   928  O  OD1  A ASP A 1 118 ? -24.902 15.143 -19.062 0.65 48.63  ? 116 ASP A OD1  1 
ATOM   929  O  OD1  B ASP A 1 118 ? -22.118 14.622 -21.036 0.35 57.11  ? 116 ASP A OD1  1 
ATOM   930  O  OD2  A ASP A 1 118 ? -25.590 17.011 -19.984 0.65 48.02  ? 116 ASP A OD2  1 
ATOM   931  O  OD2  B ASP A 1 118 ? -23.428 15.680 -22.446 0.35 56.55  ? 116 ASP A OD2  1 
ATOM   932  N  N    . ALA A 1 119 ? -19.879 16.092 -18.583 1.00 57.43  ? 117 ALA A N    1 
ATOM   933  C  CA   . ALA A 1 119 ? -18.441 16.014 -18.795 1.00 62.09  ? 117 ALA A CA   1 
ATOM   934  C  C    . ALA A 1 119 ? -17.895 14.866 -17.951 1.00 65.29  ? 117 ALA A C    1 
ATOM   935  O  O    . ALA A 1 119 ? -18.545 14.460 -16.989 1.00 64.12  ? 117 ALA A O    1 
ATOM   936  C  CB   . ALA A 1 119 ? -17.789 17.316 -18.364 1.00 64.70  ? 117 ALA A CB   1 
ATOM   937  N  N    . GLU A 1 120 ? -16.710 14.375 -18.303 1.00 71.29  ? 118 GLU A N    1 
ATOM   938  C  CA   . GLU A 1 120 ? -16.057 13.308 -17.510 1.00 75.17  ? 118 GLU A CA   1 
ATOM   939  C  C    . GLU A 1 120 ? -14.856 13.910 -16.785 1.00 75.59  ? 118 GLU A C    1 
ATOM   940  O  O    . GLU A 1 120 ? -14.086 14.635 -17.430 1.00 77.01  ? 118 GLU A O    1 
ATOM   941  C  CB   . GLU A 1 120 ? -15.616 12.168 -18.422 1.00 81.78  ? 118 GLU A CB   1 
ATOM   942  C  CG   . GLU A 1 120 ? -16.085 10.806 -17.945 1.00 89.29  ? 118 GLU A CG   1 
ATOM   943  C  CD   . GLU A 1 120 ? -15.268 9.635  -18.461 1.00 101.17 ? 118 GLU A CD   1 
ATOM   944  O  OE1  . GLU A 1 120 ? -14.739 9.737  -19.586 1.00 99.75  ? 118 GLU A OE1  1 
ATOM   945  O  OE2  . GLU A 1 120 ? -15.163 8.626  -17.737 0.50 104.75 ? 118 GLU A OE2  1 
ATOM   946  N  N    . VAL A 1 121 ? -14.728 13.632 -15.490 1.00 76.47  ? 119 VAL A N    1 
ATOM   947  C  CA   . VAL A 1 121 ? -13.577 14.138 -14.691 1.00 74.78  ? 119 VAL A CA   1 
ATOM   948  C  C    . VAL A 1 121 ? -12.976 12.933 -13.971 1.00 83.75  ? 119 VAL A C    1 
ATOM   949  O  O    . VAL A 1 121 ? -13.754 12.053 -13.571 1.00 86.68  ? 119 VAL A O    1 
ATOM   950  C  CB   . VAL A 1 121 ? -14.001 15.264 -13.728 1.00 75.11  ? 119 VAL A CB   1 
ATOM   951  C  CG1  . VAL A 1 121 ? -12.991 15.509 -12.620 1.00 79.46  ? 119 VAL A CG1  1 
ATOM   952  C  CG2  . VAL A 1 121 ? -14.303 16.558 -14.466 1.00 69.02  ? 119 VAL A CG2  1 
ATOM   953  N  N    . GLU A 1 122 ? -11.651 12.886 -13.834 1.00 87.04  ? 120 GLU A N    1 
ATOM   954  C  CA   . GLU A 1 122 ? -10.977 11.697 -13.244 1.00 92.79  ? 120 GLU A CA   1 
ATOM   955  C  C    . GLU A 1 122 ? -10.792 11.839 -11.731 1.00 93.64  ? 120 GLU A C    1 
ATOM   956  O  O    . GLU A 1 122 ? -10.275 10.889 -11.127 1.00 101.14 ? 120 GLU A O    1 
ATOM   957  C  CB   . GLU A 1 122 ? -9.626  11.477 -13.921 1.00 92.52  ? 120 GLU A CB   1 
ATOM   958  C  CG   . GLU A 1 122 ? -9.741  11.066 -15.377 1.00 96.87  ? 120 GLU A CG   1 
ATOM   959  C  CD   . GLU A 1 122 ? -8.617  11.574 -16.262 1.00 105.63 ? 120 GLU A CD   1 
ATOM   960  O  OE1  . GLU A 1 122 ? -7.775  12.345 -15.761 1.00 110.62 ? 120 GLU A OE1  1 
ATOM   961  O  OE2  . GLU A 1 122 ? -8.586  11.198 -17.450 1.00 104.56 ? 120 GLU A OE2  1 
ATOM   962  N  N    . GLY A 1 123 ? -11.230 12.952 -11.139 1.00 93.37  ? 121 GLY A N    1 
ATOM   963  C  CA   . GLY A 1 123 ? -11.029 13.184 -9.696  1.00 95.63  ? 121 GLY A CA   1 
ATOM   964  C  C    . GLY A 1 123 ? -11.671 12.082 -8.875  1.00 99.84  ? 121 GLY A C    1 
ATOM   965  O  O    . GLY A 1 123 ? -12.699 11.553 -9.314  1.00 97.34  ? 121 GLY A O    1 
ATOM   966  N  N    . ASP A 1 124 ? -11.062 11.703 -7.752  1.00 99.59  ? 122 ASP A N    1 
ATOM   967  C  CA   . ASP A 1 124 ? -11.584 10.555 -6.962  1.00 97.27  ? 122 ASP A CA   1 
ATOM   968  C  C    . ASP A 1 124 ? -12.665 11.001 -5.966  1.00 94.03  ? 122 ASP A C    1 
ATOM   969  O  O    . ASP A 1 124 ? -13.250 10.119 -5.314  1.00 90.26  ? 122 ASP A O    1 
ATOM   970  C  CB   . ASP A 1 124 ? -10.445 9.809  -6.270  1.00 101.13 ? 122 ASP A CB   1 
ATOM   971  C  CG   . ASP A 1 124 ? -9.695  8.866  -7.194  1.00 116.14 ? 122 ASP A CG   1 
ATOM   972  O  OD1  . ASP A 1 124 ? -10.072 7.679  -7.250  1.00 120.27 ? 122 ASP A OD1  1 
ATOM   973  O  OD2  . ASP A 1 124 ? -8.740  9.327  -7.848  1.00 119.78 ? 122 ASP A OD2  1 
ATOM   974  N  N    . THR A 1 125 ? -12.906 12.307 -5.831  1.00 82.17  ? 123 THR A N    1 
ATOM   975  C  CA   . THR A 1 125 ? -13.886 12.782 -4.821  1.00 73.22  ? 123 THR A CA   1 
ATOM   976  C  C    . THR A 1 125 ? -15.302 12.579 -5.353  1.00 73.05  ? 123 THR A C    1 
ATOM   977  O  O    . THR A 1 125 ? -15.563 12.979 -6.489  1.00 74.89  ? 123 THR A O    1 
ATOM   978  C  CB   . THR A 1 125 ? -13.618 14.234 -4.425  1.00 67.25  ? 123 THR A CB   1 
ATOM   979  O  OG1  . THR A 1 125 ? -12.221 14.480 -4.576  1.00 81.28  ? 123 THR A OG1  1 
ATOM   980  C  CG2  . THR A 1 125 ? -14.046 14.543 -3.008  1.00 66.99  ? 123 THR A CG2  1 
ATOM   981  N  N    . HIS A 1 126 ? -16.179 12.002 -4.542  1.00 68.20  ? 124 HIS A N    1 
ATOM   982  C  CA   . HIS A 1 126 ? -17.562 11.714 -4.982  1.00 64.19  ? 124 HIS A CA   1 
ATOM   983  C  C    . HIS A 1 126 ? -18.565 12.431 -4.081  1.00 61.12  ? 124 HIS A C    1 
ATOM   984  O  O    . HIS A 1 126 ? -18.304 12.526 -2.874  1.00 57.54  ? 124 HIS A O    1 
ATOM   985  C  CB   . HIS A 1 126 ? -17.825 10.211 -4.906  1.00 68.32  ? 124 HIS A CB   1 
ATOM   986  C  CG   . HIS A 1 126 ? -17.279 9.419  -6.042  1.00 75.76  ? 124 HIS A CG   1 
ATOM   987  N  ND1  . HIS A 1 126 ? -18.083 8.933  -7.049  1.00 75.30  ? 124 HIS A ND1  1 
ATOM   988  C  CD2  . HIS A 1 126 ? -16.027 8.998  -6.315  1.00 81.29  ? 124 HIS A CD2  1 
ATOM   989  C  CE1  . HIS A 1 126 ? -17.347 8.255  -7.904  1.00 80.68  ? 124 HIS A CE1  1 
ATOM   990  N  NE2  . HIS A 1 126 ? -16.082 8.281  -7.475  1.00 83.86  ? 124 HIS A NE2  1 
ATOM   991  N  N    . PHE A 1 127 ? -19.662 12.920 -4.652  1.00 57.60  ? 125 PHE A N    1 
ATOM   992  C  CA   . PHE A 1 127 ? -20.704 13.522 -3.852  1.00 50.24  ? 125 PHE A CA   1 
ATOM   993  C  C    . PHE A 1 127 ? -21.328 12.426 -2.998  1.00 52.54  ? 125 PHE A C    1 
ATOM   994  O  O    . PHE A 1 127 ? -21.436 11.282 -3.445  1.00 55.85  ? 125 PHE A O    1 
ATOM   995  C  CB   . PHE A 1 127 ? -21.758 14.179 -4.737  1.00 52.55  ? 125 PHE A CB   1 
ATOM   996  C  CG   . PHE A 1 127 ? -22.707 15.069 -3.990  1.00 48.06  ? 125 PHE A CG   1 
ATOM   997  C  CD1  . PHE A 1 127 ? -22.307 16.309 -3.541  1.00 46.87  ? 125 PHE A CD1  1 
ATOM   998  C  CD2  . PHE A 1 127 ? -24.006 14.673 -3.756  1.00 42.97  ? 125 PHE A CD2  1 
ATOM   999  C  CE1  . PHE A 1 127 ? -23.184 17.140 -2.860  1.00 43.12  ? 125 PHE A CE1  1 
ATOM   1000 C  CE2  . PHE A 1 127 ? -24.880 15.496 -3.075  1.00 46.87  ? 125 PHE A CE2  1 
ATOM   1001 C  CZ   . PHE A 1 127 ? -24.463 16.730 -2.620  1.00 43.92  ? 125 PHE A CZ   1 
ATOM   1002 N  N    . PRO A 1 128 ? -21.673 12.723 -1.752  1.00 50.81  ? 126 PRO A N    1 
ATOM   1003 C  CA   . PRO A 1 128 ? -22.213 11.683 -0.872  1.00 53.70  ? 126 PRO A CA   1 
ATOM   1004 C  C    . PRO A 1 128 ? -23.517 11.155 -1.430  1.00 58.71  ? 126 PRO A C    1 
ATOM   1005 O  O    . PRO A 1 128 ? -24.256 11.866 -2.113  1.00 61.48  ? 126 PRO A O    1 
ATOM   1006 C  CB   . PRO A 1 128 ? -22.441 12.422 0.452   1.00 51.17  ? 126 PRO A CB   1 
ATOM   1007 C  CG   . PRO A 1 128 ? -22.472 13.890 0.060   1.00 47.44  ? 126 PRO A CG   1 
ATOM   1008 C  CD   . PRO A 1 128 ? -21.473 13.993 -1.045  1.00 46.87  ? 126 PRO A CD   1 
ATOM   1009 N  N    . ASP A 1 129 ? -23.820 9.907  -1.117  1.00 62.37  ? 127 ASP A N    1 
ATOM   1010 C  CA   . ASP A 1 129 ? -25.057 9.330  -1.617  1.00 70.15  ? 127 ASP A CA   1 
ATOM   1011 C  C    . ASP A 1 129 ? -26.265 9.787  -0.802  1.00 75.21  ? 127 ASP A C    1 
ATOM   1012 O  O    . ASP A 1 129 ? -26.224 9.854  0.433   1.00 73.91  ? 127 ASP A O    1 
ATOM   1013 C  CB   . ASP A 1 129 ? -24.966 7.815  -1.621  1.00 72.86  ? 127 ASP A CB   1 
ATOM   1014 C  CG   . ASP A 1 129 ? -24.358 7.298  -2.891  1.00 79.23  ? 127 ASP A CG   1 
ATOM   1015 O  OD1  . ASP A 1 129 ? -24.949 7.557  -3.968  1.00 84.46  ? 127 ASP A OD1  1 
ATOM   1016 O  OD2  . ASP A 1 129 ? -23.306 6.629  -2.812  1.00 81.44  ? 127 ASP A OD2  1 
ATOM   1017 N  N    . TYR A 1 130 ? -27.342 10.116 -1.502  1.00 77.92  ? 128 TYR A N    1 
ATOM   1018 C  CA   . TYR A 1 130 ? -28.605 10.407 -0.849  1.00 82.01  ? 128 TYR A CA   1 
ATOM   1019 C  C    . TYR A 1 130 ? -29.665 9.387  -1.254  1.00 90.54  ? 128 TYR A C    1 
ATOM   1020 O  O    . TYR A 1 130 ? -29.670 8.855  -2.370  1.00 89.26  ? 128 TYR A O    1 
ATOM   1021 C  CB   . TYR A 1 130 ? -29.078 11.837 -1.143  1.00 72.51  ? 128 TYR A CB   1 
ATOM   1022 C  CG   . TYR A 1 130 ? -29.100 12.247 -2.597  1.00 70.18  ? 128 TYR A CG   1 
ATOM   1023 C  CD1  . TYR A 1 130 ? -27.945 12.701 -3.212  1.00 68.13  ? 128 TYR A CD1  1 
ATOM   1024 C  CD2  . TYR A 1 130 ? -30.282 12.236 -3.337  1.00 67.34  ? 128 TYR A CD2  1 
ATOM   1025 C  CE1  . TYR A 1 130 ? -27.943 13.100 -4.535  1.00 64.86  ? 128 TYR A CE1  1 
ATOM   1026 C  CE2  . TYR A 1 130 ? -30.292 12.643 -4.669  1.00 67.41  ? 128 TYR A CE2  1 
ATOM   1027 C  CZ   . TYR A 1 130 ? -29.110 13.073 -5.265  1.00 67.25  ? 128 TYR A CZ   1 
ATOM   1028 O  OH   . TYR A 1 130 ? -29.062 13.475 -6.594  1.00 68.36  ? 128 TYR A OH   1 
ATOM   1029 N  N    . GLU A 1 131 ? -30.548 9.116  -0.310  1.00 101.26 ? 129 GLU A N    1 
ATOM   1030 C  CA   . GLU A 1 131 ? -31.623 8.143  -0.382  1.00 104.31 ? 129 GLU A CA   1 
ATOM   1031 C  C    . GLU A 1 131 ? -32.735 8.717  -1.248  1.00 103.25 ? 129 GLU A C    1 
ATOM   1032 O  O    . GLU A 1 131 ? -33.502 9.568  -0.778  1.00 105.95 ? 129 GLU A O    1 
ATOM   1033 C  CB   . GLU A 1 131 ? -32.141 7.832  1.026   1.00 105.13 ? 129 GLU A CB   1 
ATOM   1034 C  CG   . GLU A 1 131 ? -31.045 7.602  2.087   1.00 110.25 ? 129 GLU A CG   1 
ATOM   1035 C  CD   . GLU A 1 131 ? -30.178 8.845  2.374   1.00 114.65 ? 129 GLU A CD   1 
ATOM   1036 O  OE1  . GLU A 1 131 ? -30.697 9.991  2.316   1.00 109.28 ? 129 GLU A OE1  1 
ATOM   1037 O  OE2  . GLU A 1 131 ? -28.966 8.671  2.647   1.00 111.55 ? 129 GLU A OE2  1 
ATOM   1038 N  N    . PRO A 1 132 ? -32.855 8.294  -2.507  1.00 94.55  ? 130 PRO A N    1 
ATOM   1039 C  CA   . PRO A 1 132 ? -33.858 8.910  -3.395  1.00 89.03  ? 130 PRO A CA   1 
ATOM   1040 C  C    . PRO A 1 132 ? -35.239 9.009  -2.772  1.00 86.06  ? 130 PRO A C    1 
ATOM   1041 O  O    . PRO A 1 132 ? -35.969 9.972  -3.032  1.00 87.19  ? 130 PRO A O    1 
ATOM   1042 C  CB   . PRO A 1 132 ? -33.850 7.977  -4.614  1.00 88.35  ? 130 PRO A CB   1 
ATOM   1043 C  CG   . PRO A 1 132 ? -32.481 7.368  -4.599  1.00 87.81  ? 130 PRO A CG   1 
ATOM   1044 C  CD   . PRO A 1 132 ? -32.199 7.138  -3.138  1.00 92.78  ? 130 PRO A CD   1 
ATOM   1045 N  N    . ASP A 1 133 ? -35.608 8.044  -1.936  1.00 89.30  ? 131 ASP A N    1 
ATOM   1046 C  CA   . ASP A 1 133 ? -36.922 8.020  -1.310  1.00 94.14  ? 131 ASP A CA   1 
ATOM   1047 C  C    . ASP A 1 133 ? -37.097 9.106  -0.246  1.00 86.21  ? 131 ASP A C    1 
ATOM   1048 O  O    . ASP A 1 133 ? -38.235 9.394  0.139   1.00 86.55  ? 131 ASP A O    1 
ATOM   1049 C  CB   . ASP A 1 133 ? -37.156 6.620  -0.722  1.00 92.88  ? 131 ASP A CB   1 
ATOM   1050 C  CG   . ASP A 1 133 ? -38.555 6.431  -0.181  1.00 100.89 ? 131 ASP A CG   1 
ATOM   1051 O  OD1  . ASP A 1 133 ? -38.898 7.088  0.827   1.00 105.40 ? 131 ASP A OD1  1 
ATOM   1052 O  OD2  . ASP A 1 133 ? -39.309 5.611  -0.754  1.00 107.75 ? 131 ASP A OD2  1 
ATOM   1053 N  N    . ASP A 1 134 ? -36.020 9.718  0.240   1.00 84.78  ? 132 ASP A N    1 
ATOM   1054 C  CA   . ASP A 1 134 ? -36.142 10.814 1.195   1.00 80.91  ? 132 ASP A CA   1 
ATOM   1055 C  C    . ASP A 1 134 ? -35.973 12.184 0.554   1.00 72.03  ? 132 ASP A C    1 
ATOM   1056 O  O    . ASP A 1 134 ? -36.029 13.191 1.267   1.00 68.89  ? 132 ASP A O    1 
ATOM   1057 C  CB   . ASP A 1 134 ? -35.127 10.662 2.334   1.00 80.40  ? 132 ASP A CB   1 
ATOM   1058 C  CG   . ASP A 1 134 ? -35.675 9.874  3.506   1.00 92.82  ? 132 ASP A CG   1 
ATOM   1059 O  OD1  . ASP A 1 134 ? -34.854 9.393  4.313   1.00 94.87  ? 132 ASP A OD1  1 
ATOM   1060 O  OD2  . ASP A 1 134 ? -36.917 9.719  3.617   1.00 94.31  ? 132 ASP A OD2  1 
ATOM   1061 N  N    . TRP A 1 135 ? -35.775 12.253 -0.762  1.00 67.41  ? 133 TRP A N    1 
ATOM   1062 C  CA   . TRP A 1 135 ? -35.536 13.520 -1.434  1.00 63.81  ? 133 TRP A CA   1 
ATOM   1063 C  C    . TRP A 1 135 ? -36.499 13.666 -2.602  1.00 65.11  ? 133 TRP A C    1 
ATOM   1064 O  O    . TRP A 1 135 ? -36.799 12.694 -3.301  1.00 69.14  ? 133 TRP A O    1 
ATOM   1065 C  CB   . TRP A 1 135 ? -34.083 13.620 -1.907  1.00 61.86  ? 133 TRP A CB   1 
ATOM   1066 C  CG   . TRP A 1 135 ? -33.126 13.805 -0.761  1.00 61.21  ? 133 TRP A CG   1 
ATOM   1067 C  CD1  . TRP A 1 135 ? -32.461 12.821 -0.080  1.00 66.22  ? 133 TRP A CD1  1 
ATOM   1068 C  CD2  . TRP A 1 135 ? -32.715 15.045 -0.171  1.00 55.46  ? 133 TRP A CD2  1 
ATOM   1069 N  NE1  . TRP A 1 135 ? -31.679 13.371 0.909   1.00 61.54  ? 133 TRP A NE1  1 
ATOM   1070 C  CE2  . TRP A 1 135 ? -31.813 14.735 0.869   1.00 56.61  ? 133 TRP A CE2  1 
ATOM   1071 C  CE3  . TRP A 1 135 ? -33.022 16.386 -0.417  1.00 49.56  ? 133 TRP A CE3  1 
ATOM   1072 C  CZ2  . TRP A 1 135 ? -31.216 15.715 1.655   1.00 50.25  ? 133 TRP A CZ2  1 
ATOM   1073 C  CZ3  . TRP A 1 135 ? -32.424 17.356 0.366   1.00 49.13  ? 133 TRP A CZ3  1 
ATOM   1074 C  CH2  . TRP A 1 135 ? -31.535 17.016 1.387   1.00 47.42  ? 133 TRP A CH2  1 
ATOM   1075 N  N    . GLU A 1 136 ? -36.989 14.884 -2.795  1.00 56.09  ? 134 GLU A N    1 
ATOM   1076 C  CA   . GLU A 1 136 ? -37.892 15.209 -3.883  1.00 49.31  ? 134 GLU A CA   1 
ATOM   1077 C  C    . GLU A 1 136 ? -37.229 16.229 -4.780  1.00 49.72  ? 134 GLU A C    1 
ATOM   1078 O  O    . GLU A 1 136 ? -36.654 17.202 -4.290  1.00 49.04  ? 134 GLU A O    1 
ATOM   1079 C  CB   . GLU A 1 136 ? -39.211 15.770 -3.363  1.00 56.00  ? 134 GLU A CB   1 
ATOM   1080 C  CG   . GLU A 1 136 ? -40.178 16.132 -4.461  1.00 56.48  ? 134 GLU A CG   1 
ATOM   1081 C  CD   . GLU A 1 136 ? -41.545 16.489 -3.925  1.00 60.35  ? 134 GLU A CD   1 
ATOM   1082 O  OE1  . GLU A 1 136 ? -41.707 16.605 -2.684  1.00 64.12  ? 134 GLU A OE1  1 
ATOM   1083 O  OE2  . GLU A 1 136 ? -42.466 16.623 -4.752  1.00 63.00  ? 134 GLU A OE2  1 
ATOM   1084 N  N    . SER A 1 137 ? -37.292 16.003 -6.082  1.00 48.36  ? 135 SER A N    1 
ATOM   1085 C  CA   . SER A 1 137 ? -36.755 16.954 -7.036  1.00 45.18  ? 135 SER A CA   1 
ATOM   1086 C  C    . SER A 1 137 ? -37.853 17.969 -7.332  1.00 50.24  ? 135 SER A C    1 
ATOM   1087 O  O    . SER A 1 137 ? -38.959 17.589 -7.730  1.00 46.44  ? 135 SER A O    1 
ATOM   1088 C  CB   . SER A 1 137 ? -36.288 16.240 -8.304  1.00 47.39  ? 135 SER A CB   1 
ATOM   1089 O  OG   . SER A 1 137 ? -35.683 17.148 -9.228  1.00 46.60  ? 135 SER A OG   1 
ATOM   1090 N  N    . VAL A 1 138 ? -37.563 19.251 -7.124  1.00 47.48  ? 136 VAL A N    1 
ATOM   1091 C  CA   . VAL A 1 138 ? -38.574 20.293 -7.260  1.00 47.31  ? 136 VAL A CA   1 
ATOM   1092 C  C    . VAL A 1 138 ? -38.264 21.282 -8.372  1.00 52.67  ? 136 VAL A C    1 
ATOM   1093 O  O    . VAL A 1 138 ? -39.148 22.083 -8.728  1.00 52.18  ? 136 VAL A O    1 
ATOM   1094 C  CB   . VAL A 1 138 ? -38.776 21.049 -5.932  1.00 49.82  ? 136 VAL A CB   1 
ATOM   1095 C  CG1  . VAL A 1 138 ? -39.289 20.097 -4.870  1.00 48.48  ? 136 VAL A CG1  1 
ATOM   1096 C  CG2  . VAL A 1 138 ? -37.486 21.705 -5.509  1.00 42.40  ? 136 VAL A CG2  1 
ATOM   1097 N  N    . PHE A 1 139 ? -37.054 21.250 -8.942  1.00 48.36  ? 137 PHE A N    1 
ATOM   1098 C  CA   . PHE A 1 139 ? -36.666 22.161 -10.015 1.00 46.28  ? 137 PHE A CA   1 
ATOM   1099 C  C    . PHE A 1 139 ? -35.506 21.571 -10.817 1.00 49.36  ? 137 PHE A C    1 
ATOM   1100 O  O    . PHE A 1 139 ? -34.508 21.126 -10.228 1.00 46.13  ? 137 PHE A O    1 
ATOM   1101 C  CB   . PHE A 1 139 ? -36.267 23.520 -9.431  1.00 45.26  ? 137 PHE A CB   1 
ATOM   1102 C  CG   . PHE A 1 139 ? -35.760 24.490 -10.449 1.00 44.41  ? 137 PHE A CG   1 
ATOM   1103 C  CD1  . PHE A 1 139 ? -36.649 25.260 -11.197 1.00 48.26  ? 137 PHE A CD1  1 
ATOM   1104 C  CD2  . PHE A 1 139 ? -34.396 24.633 -10.675 1.00 42.58  ? 137 PHE A CD2  1 
ATOM   1105 C  CE1  . PHE A 1 139 ? -36.191 26.163 -12.169 1.00 44.28  ? 137 PHE A CE1  1 
ATOM   1106 C  CE2  . PHE A 1 139 ? -33.922 25.544 -11.632 1.00 42.60  ? 137 PHE A CE2  1 
ATOM   1107 C  CZ   . PHE A 1 139 ? -34.830 26.304 -12.382 1.00 42.61  ? 137 PHE A CZ   1 
ATOM   1108 N  N    . SER A 1 140 ? -35.623 21.583 -12.151 1.00 40.10  ? 138 SER A N    1 
ATOM   1109 C  CA   . SER A 1 140 ? -34.496 21.234 -13.001 1.00 42.05  ? 138 SER A CA   1 
ATOM   1110 C  C    . SER A 1 140 ? -34.516 22.110 -14.239 1.00 43.36  ? 138 SER A C    1 
ATOM   1111 O  O    . SER A 1 140 ? -35.569 22.548 -14.705 1.00 45.63  ? 138 SER A O    1 
ATOM   1112 C  CB   . SER A 1 140 ? -34.506 19.754 -13.381 1.00 43.77  ? 138 SER A CB   1 
ATOM   1113 O  OG   . SER A 1 140 ? -35.720 19.383 -13.992 1.00 39.55  ? 138 SER A OG   1 
ATOM   1114 N  N    . GLU A 1 141 ? -33.319 22.394 -14.764 1.00 43.32  ? 139 GLU A N    1 
ATOM   1115 C  CA   . GLU A 1 141 ? -33.187 23.298 -15.917 1.00 45.46  ? 139 GLU A CA   1 
ATOM   1116 C  C    . GLU A 1 141 ? -31.999 22.897 -16.785 1.00 44.13  ? 139 GLU A C    1 
ATOM   1117 O  O    . GLU A 1 141 ? -30.849 23.088 -16.378 1.00 45.80  ? 139 GLU A O    1 
ATOM   1118 C  CB   . GLU A 1 141 ? -33.014 24.738 -15.461 1.00 45.58  ? 139 GLU A CB   1 
ATOM   1119 C  CG   . GLU A 1 141 ? -33.512 25.756 -16.454 1.00 46.38  ? 139 GLU A CG   1 
ATOM   1120 C  CD   . GLU A 1 141 ? -33.358 27.148 -15.923 1.00 47.36  ? 139 GLU A CD   1 
ATOM   1121 O  OE1  . GLU A 1 141 ? -34.387 27.786 -15.584 1.00 55.12  ? 139 GLU A OE1  1 
ATOM   1122 O  OE2  . GLU A 1 141 ? -32.207 27.603 -15.859 1.00 43.80  ? 139 GLU A OE2  1 
ATOM   1123 N  N    . PHE A 1 142 ? -32.261 22.409 -17.995 1.00 45.44  ? 140 PHE A N    1 
ATOM   1124 C  CA   . PHE A 1 142 ? -31.192 21.981 -18.895 1.00 43.44  ? 140 PHE A CA   1 
ATOM   1125 C  C    . PHE A 1 142 ? -30.685 23.141 -19.743 1.00 43.94  ? 140 PHE A C    1 
ATOM   1126 O  O    . PHE A 1 142 ? -31.473 23.953 -20.232 1.00 45.56  ? 140 PHE A O    1 
ATOM   1127 C  CB   . PHE A 1 142 ? -31.673 20.870 -19.829 1.00 40.54  ? 140 PHE A CB   1 
ATOM   1128 C  CG   . PHE A 1 142 ? -30.575 20.284 -20.658 1.00 42.80  ? 140 PHE A CG   1 
ATOM   1129 C  CD1  . PHE A 1 142 ? -29.715 19.340 -20.120 1.00 46.54  ? 140 PHE A CD1  1 
ATOM   1130 C  CD2  . PHE A 1 142 ? -30.386 20.684 -21.977 1.00 47.21  ? 140 PHE A CD2  1 
ATOM   1131 C  CE1  . PHE A 1 142 ? -28.677 18.806 -20.880 1.00 47.41  ? 140 PHE A CE1  1 
ATOM   1132 C  CE2  . PHE A 1 142 ? -29.367 20.143 -22.746 1.00 44.27  ? 140 PHE A CE2  1 
ATOM   1133 C  CZ   . PHE A 1 142 ? -28.504 19.214 -22.190 1.00 45.87  ? 140 PHE A CZ   1 
ATOM   1134 N  N    . HIS A 1 143 ? -29.370 23.185 -19.961 1.00 44.77  ? 141 HIS A N    1 
ATOM   1135 C  CA   . HIS A 1 143 ? -28.770 24.126 -20.901 1.00 46.29  ? 141 HIS A CA   1 
ATOM   1136 C  C    . HIS A 1 143 ? -27.775 23.401 -21.803 1.00 45.35  ? 141 HIS A C    1 
ATOM   1137 O  O    . HIS A 1 143 ? -26.995 22.566 -21.335 1.00 45.72  ? 141 HIS A O    1 
ATOM   1138 C  CB   . HIS A 1 143 ? -28.084 25.283 -20.147 1.00 45.37  ? 141 HIS A CB   1 
ATOM   1139 C  CG   . HIS A 1 143 ? -29.033 26.119 -19.345 1.00 48.43  ? 141 HIS A CG   1 
ATOM   1140 N  ND1  . HIS A 1 143 ? -29.624 27.264 -19.845 1.00 48.31  ? 141 HIS A ND1  1 
ATOM   1141 C  CD2  . HIS A 1 143 ? -29.503 25.978 -18.082 1.00 47.77  ? 141 HIS A CD2  1 
ATOM   1142 C  CE1  . HIS A 1 143 ? -30.410 27.791 -18.923 1.00 48.82  ? 141 HIS A CE1  1 
ATOM   1143 N  NE2  . HIS A 1 143 ? -30.359 27.029 -17.843 1.00 43.09  ? 141 HIS A NE2  1 
ATOM   1144 N  N    . ASP A 1 144 ? -27.812 23.700 -23.102 1.00 47.04  ? 142 ASP A N    1 
ATOM   1145 C  CA   . ASP A 1 144 ? -26.770 23.190 -23.983 1.00 41.94  ? 142 ASP A CA   1 
ATOM   1146 C  C    . ASP A 1 144 ? -25.449 23.906 -23.700 1.00 45.76  ? 142 ASP A C    1 
ATOM   1147 O  O    . ASP A 1 144 ? -25.415 24.964 -23.073 1.00 46.97  ? 142 ASP A O    1 
ATOM   1148 C  CB   . ASP A 1 144 ? -27.111 23.418 -25.457 1.00 43.94  ? 142 ASP A CB   1 
ATOM   1149 C  CG   . ASP A 1 144 ? -28.373 22.724 -25.902 1.00 48.10  ? 142 ASP A CG   1 
ATOM   1150 O  OD1  . ASP A 1 144 ? -28.490 21.492 -25.752 1.00 49.58  ? 142 ASP A OD1  1 
ATOM   1151 O  OD2  . ASP A 1 144 ? -29.235 23.419 -26.468 1.00 54.53  ? 142 ASP A OD2  1 
ATOM   1152 N  N    . ALA A 1 145 ? -24.354 23.336 -24.207 1.00 45.94  ? 143 ALA A N    1 
ATOM   1153 C  CA   . ALA A 1 145 ? -23.114 24.091 -24.316 1.00 48.76  ? 143 ALA A CA   1 
ATOM   1154 C  C    . ALA A 1 145 ? -23.271 25.222 -25.328 1.00 51.62  ? 143 ALA A C    1 
ATOM   1155 O  O    . ALA A 1 145 ? -24.064 25.143 -26.271 1.00 51.38  ? 143 ALA A O    1 
ATOM   1156 C  CB   . ALA A 1 145 ? -21.959 23.185 -24.753 1.00 46.75  ? 143 ALA A CB   1 
ATOM   1157 N  N    . ASP A 1 146 ? -22.493 26.278 -25.136 1.00 53.18  ? 144 ASP A N    1 
ATOM   1158 C  CA   . ASP A 1 146 ? -22.540 27.401 -26.053 1.00 56.49  ? 144 ASP A CA   1 
ATOM   1159 C  C    . ASP A 1 146 ? -21.150 28.021 -26.106 1.00 63.38  ? 144 ASP A C    1 
ATOM   1160 O  O    . ASP A 1 146 ? -20.153 27.380 -25.751 1.00 65.96  ? 144 ASP A O    1 
ATOM   1161 C  CB   . ASP A 1 146 ? -23.628 28.406 -25.635 1.00 55.82  ? 144 ASP A CB   1 
ATOM   1162 C  CG   . ASP A 1 146 ? -23.383 29.000 -24.276 1.00 56.38  ? 144 ASP A CG   1 
ATOM   1163 O  OD1  . ASP A 1 146 ? -22.220 29.018 -23.826 1.00 63.16  ? 144 ASP A OD1  1 
ATOM   1164 O  OD2  . ASP A 1 146 ? -24.354 29.462 -23.646 1.00 54.19  ? 144 ASP A OD2  1 
ATOM   1165 N  N    . ALA A 1 147 ? -21.082 29.278 -26.548 1.00 67.71  ? 145 ALA A N    1 
ATOM   1166 C  CA   . ALA A 1 147 ? -19.787 29.939 -26.665 1.00 68.62  ? 145 ALA A CA   1 
ATOM   1167 C  C    . ALA A 1 147 ? -19.054 29.973 -25.323 1.00 69.94  ? 145 ALA A C    1 
ATOM   1168 O  O    . ALA A 1 147 ? -17.837 29.744 -25.271 1.00 76.30  ? 145 ALA A O    1 
ATOM   1169 C  CB   . ALA A 1 147 ? -19.950 31.358 -27.211 1.00 69.60  ? 145 ALA A CB   1 
ATOM   1170 N  N    . GLN A 1 148 ? -19.755 30.269 -24.216 1.00 64.35  ? 146 GLN A N    1 
ATOM   1171 C  CA   . GLN A 1 148 ? -18.970 30.467 -23.003 1.00 64.53  ? 146 GLN A CA   1 
ATOM   1172 C  C    . GLN A 1 148 ? -18.956 29.224 -22.122 1.00 60.30  ? 146 GLN A C    1 
ATOM   1173 O  O    . GLN A 1 148 ? -18.084 29.104 -21.254 1.00 65.40  ? 146 GLN A O    1 
ATOM   1174 C  CB   . GLN A 1 148 ? -19.517 31.623 -22.138 1.00 64.55  ? 146 GLN A CB   1 
ATOM   1175 C  CG   . GLN A 1 148 ? -19.466 33.030 -22.699 1.00 71.24  ? 146 GLN A CG   1 
ATOM   1176 C  CD   . GLN A 1 148 ? -20.587 33.175 -23.736 1.00 76.94  ? 146 GLN A CD   1 
ATOM   1177 O  OE1  . GLN A 1 148 ? -20.334 33.428 -24.925 1.00 78.89  ? 146 GLN A OE1  1 
ATOM   1178 N  NE2  . GLN A 1 148 ? -21.846 33.101 -23.263 1.00 74.41  ? 146 GLN A NE2  1 
ATOM   1179 N  N    . ASN A 1 149 ? -19.865 28.276 -22.352 1.00 57.62  ? 147 ASN A N    1 
ATOM   1180 C  CA   . ASN A 1 149 ? -19.965 27.074 -21.538 1.00 59.41  ? 147 ASN A CA   1 
ATOM   1181 C  C    . ASN A 1 149 ? -19.636 25.869 -22.404 1.00 58.14  ? 147 ASN A C    1 
ATOM   1182 O  O    . ASN A 1 149 ? -20.384 25.521 -23.326 1.00 56.46  ? 147 ASN A O    1 
ATOM   1183 C  CB   . ASN A 1 149 ? -21.343 26.988 -20.901 1.00 55.80  ? 147 ASN A CB   1 
ATOM   1184 C  CG   . ASN A 1 149 ? -21.659 28.231 -20.101 1.00 55.47  ? 147 ASN A CG   1 
ATOM   1185 O  OD1  . ASN A 1 149 ? -21.267 28.339 -18.950 1.00 55.02  ? 147 ASN A OD1  1 
ATOM   1186 N  ND2  . ASN A 1 149 ? -22.310 29.202 -20.731 1.00 58.32  ? 147 ASN A ND2  1 
ATOM   1187 N  N    . SER A 1 150 ? -18.483 25.268 -22.128 1.00 57.69  ? 148 SER A N    1 
ATOM   1188 C  CA   . SER A 1 150 ? -17.916 24.231 -22.977 1.00 59.06  ? 148 SER A CA   1 
ATOM   1189 C  C    . SER A 1 150 ? -18.635 22.904 -22.849 1.00 58.02  ? 148 SER A C    1 
ATOM   1190 O  O    . SER A 1 150 ? -18.364 22.006 -23.643 1.00 57.89  ? 148 SER A O    1 
ATOM   1191 C  CB   . SER A 1 150 ? -16.432 24.069 -22.639 1.00 64.50  ? 148 SER A CB   1 
ATOM   1192 O  OG   . SER A 1 150 ? -16.267 23.883 -21.232 1.00 74.89  ? 148 SER A OG   1 
ATOM   1193 N  N    . HIS A 1 151 ? -19.520 22.747 -21.868 1.00 53.55  ? 149 HIS A N    1 
ATOM   1194 C  CA   . HIS A 1 151 ? -20.276 21.517 -21.719 1.00 51.50  ? 149 HIS A CA   1 
ATOM   1195 C  C    . HIS A 1 151 ? -21.734 21.862 -21.462 1.00 51.87  ? 149 HIS A C    1 
ATOM   1196 O  O    . HIS A 1 151 ? -22.044 22.930 -20.927 1.00 51.56  ? 149 HIS A O    1 
ATOM   1197 C  CB   . HIS A 1 151 ? -19.763 20.624 -20.555 1.00 55.12  ? 149 HIS A CB   1 
ATOM   1198 C  CG   . HIS A 1 151 ? -18.308 20.267 -20.641 1.00 62.16  ? 149 HIS A CG   1 
ATOM   1199 N  ND1  . HIS A 1 151 ? -17.296 21.202 -20.527 1.00 70.71  ? 149 HIS A ND1  1 
ATOM   1200 C  CD2  . HIS A 1 151 ? -17.696 19.094 -20.939 1.00 68.31  ? 149 HIS A CD2  1 
ATOM   1201 C  CE1  . HIS A 1 151 ? -16.124 20.604 -20.680 1.00 75.24  ? 149 HIS A CE1  1 
ATOM   1202 N  NE2  . HIS A 1 151 ? -16.339 19.325 -20.939 1.00 72.49  ? 149 HIS A NE2  1 
ATOM   1203 N  N    . SER A 1 152 ? -22.631 20.955 -21.843 1.00 47.34  ? 150 SER A N    1 
ATOM   1204 C  CA   . SER A 1 152 ? -24.013 21.135 -21.427 1.00 48.52  ? 150 SER A CA   1 
ATOM   1205 C  C    . SER A 1 152 ? -24.162 20.758 -19.946 1.00 48.33  ? 150 SER A C    1 
ATOM   1206 O  O    . SER A 1 152 ? -23.332 20.047 -19.373 1.00 46.60  ? 150 SER A O    1 
ATOM   1207 C  CB   . SER A 1 152 ? -24.957 20.331 -22.325 1.00 48.66  ? 150 SER A CB   1 
ATOM   1208 O  OG   . SER A 1 152 ? -24.778 18.922 -22.196 1.00 55.27  ? 150 SER A OG   1 
ATOM   1209 N  N    . TYR A 1 153 ? -25.219 21.278 -19.322 1.00 43.35  ? 151 TYR A N    1 
ATOM   1210 C  CA   . TYR A 1 153 ? -25.381 21.202 -17.877 1.00 46.66  ? 151 TYR A CA   1 
ATOM   1211 C  C    . TYR A 1 153 ? -26.856 21.358 -17.530 1.00 44.45  ? 151 TYR A C    1 
ATOM   1212 O  O    . TYR A 1 153 ? -27.622 21.965 -18.279 1.00 46.29  ? 151 TYR A O    1 
ATOM   1213 C  CB   . TYR A 1 153 ? -24.553 22.281 -17.167 1.00 45.49  ? 151 TYR A CB   1 
ATOM   1214 C  CG   . TYR A 1 153 ? -24.798 23.674 -17.701 1.00 45.59  ? 151 TYR A CG   1 
ATOM   1215 C  CD1  . TYR A 1 153 ? -24.167 24.117 -18.864 1.00 47.33  ? 151 TYR A CD1  1 
ATOM   1216 C  CD2  . TYR A 1 153 ? -25.670 24.540 -17.060 1.00 44.84  ? 151 TYR A CD2  1 
ATOM   1217 C  CE1  . TYR A 1 153 ? -24.406 25.391 -19.376 1.00 46.91  ? 151 TYR A CE1  1 
ATOM   1218 C  CE2  . TYR A 1 153 ? -25.905 25.820 -17.555 1.00 45.33  ? 151 TYR A CE2  1 
ATOM   1219 C  CZ   . TYR A 1 153 ? -25.279 26.232 -18.713 1.00 47.27  ? 151 TYR A CZ   1 
ATOM   1220 O  OH   . TYR A 1 153 ? -25.531 27.489 -19.207 1.00 49.32  ? 151 TYR A OH   1 
ATOM   1221 N  N    . CYS A 1 154 ? -27.244 20.808 -16.383 1.00 42.67  ? 152 CYS A N    1 
ATOM   1222 C  CA   . CYS A 1 154 ? -28.626 20.847 -15.916 1.00 40.27  ? 152 CYS A CA   1 
ATOM   1223 C  C    . CYS A 1 154 ? -28.636 21.221 -14.441 1.00 43.51  ? 152 CYS A C    1 
ATOM   1224 O  O    . CYS A 1 154 ? -28.081 20.491 -13.608 1.00 40.69  ? 152 CYS A O    1 
ATOM   1225 C  CB   . CYS A 1 154 ? -29.306 19.495 -16.119 1.00 39.93  ? 152 CYS A CB   1 
ATOM   1226 S  SG   . CYS A 1 154 ? -31.080 19.609 -15.940 1.00 41.56  ? 152 CYS A SG   1 
ATOM   1227 N  N    . PHE A 1 155 ? -29.219 22.368 -14.117 1.00 42.06  ? 153 PHE A N    1 
ATOM   1228 C  CA   . PHE A 1 155 ? -29.386 22.710 -12.717 1.00 39.40  ? 153 PHE A CA   1 
ATOM   1229 C  C    . PHE A 1 155 ? -30.507 21.866 -12.126 1.00 41.60  ? 153 PHE A C    1 
ATOM   1230 O  O    . PHE A 1 155 ? -31.494 21.544 -12.802 1.00 42.56  ? 153 PHE A O    1 
ATOM   1231 C  CB   . PHE A 1 155 ? -29.716 24.187 -12.559 1.00 37.49  ? 153 PHE A CB   1 
ATOM   1232 C  CG   . PHE A 1 155 ? -28.688 25.092 -13.123 1.00 38.03  ? 153 PHE A CG   1 
ATOM   1233 C  CD1  . PHE A 1 155 ? -27.358 24.982 -12.730 1.00 38.82  ? 153 PHE A CD1  1 
ATOM   1234 C  CD2  . PHE A 1 155 ? -29.041 26.063 -14.061 1.00 39.24  ? 153 PHE A CD2  1 
ATOM   1235 C  CE1  . PHE A 1 155 ? -26.388 25.831 -13.271 1.00 42.54  ? 153 PHE A CE1  1 
ATOM   1236 C  CE2  . PHE A 1 155 ? -28.072 26.928 -14.614 1.00 41.89  ? 153 PHE A CE2  1 
ATOM   1237 C  CZ   . PHE A 1 155 ? -26.744 26.805 -14.223 1.00 42.46  ? 153 PHE A CZ   1 
ATOM   1238 N  N    . GLU A 1 156 ? -30.346 21.494 -10.858 1.00 35.51  ? 154 GLU A N    1 
ATOM   1239 C  CA   . GLU A 1 156 ? -31.389 20.769 -10.157 1.00 41.51  ? 154 GLU A CA   1 
ATOM   1240 C  C    . GLU A 1 156 ? -31.421 21.204 -8.701  1.00 40.10  ? 154 GLU A C    1 
ATOM   1241 O  O    . GLU A 1 156 ? -30.366 21.388 -8.085  1.00 39.73  ? 154 GLU A O    1 
ATOM   1242 C  CB   . GLU A 1 156 ? -31.162 19.256 -10.239 1.00 38.12  ? 154 GLU A CB   1 
ATOM   1243 C  CG   . GLU A 1 156 ? -32.393 18.462 -9.848  1.00 38.51  ? 154 GLU A CG   1 
ATOM   1244 C  CD   . GLU A 1 156 ? -32.099 17.024 -9.523  1.00 40.27  ? 154 GLU A CD   1 
ATOM   1245 O  OE1  . GLU A 1 156 ? -30.901 16.642 -9.454  1.00 39.06  ? 154 GLU A OE1  1 
ATOM   1246 O  OE2  . GLU A 1 156 ? -33.082 16.271 -9.347  1.00 41.21  ? 154 GLU A OE2  1 
ATOM   1247 N  N    . ILE A 1 157 ? -32.629 21.332 -8.147  1.00 39.79  ? 155 ILE A N    1 
ATOM   1248 C  CA   . ILE A 1 157 ? -32.841 21.575 -6.720  1.00 39.02  ? 155 ILE A CA   1 
ATOM   1249 C  C    . ILE A 1 157 ? -33.690 20.441 -6.160  1.00 42.09  ? 155 ILE A C    1 
ATOM   1250 O  O    . ILE A 1 157 ? -34.750 20.127 -6.710  1.00 45.76  ? 155 ILE A O    1 
ATOM   1251 C  CB   . ILE A 1 157 ? -33.541 22.918 -6.453  1.00 39.39  ? 155 ILE A CB   1 
ATOM   1252 C  CG1  . ILE A 1 157 ? -32.706 24.085 -6.977  1.00 41.01  ? 155 ILE A CG1  1 
ATOM   1253 C  CG2  . ILE A 1 157 ? -33.812 23.067 -4.959  1.00 38.73  ? 155 ILE A CG2  1 
ATOM   1254 C  CD1  . ILE A 1 157 ? -33.443 25.418 -6.928  1.00 39.50  ? 155 ILE A CD1  1 
ATOM   1255 N  N    . LEU A 1 158 ? -33.238 19.840 -5.065  1.00 38.69  ? 156 LEU A N    1 
ATOM   1256 C  CA   . LEU A 1 158 ? -33.995 18.817 -4.363  1.00 40.99  ? 156 LEU A CA   1 
ATOM   1257 C  C    . LEU A 1 158 ? -34.286 19.301 -2.951  1.00 46.95  ? 156 LEU A C    1 
ATOM   1258 O  O    . LEU A 1 158 ? -33.519 20.087 -2.384  1.00 43.75  ? 156 LEU A O    1 
ATOM   1259 C  CB   . LEU A 1 158 ? -33.214 17.490 -4.308  1.00 42.82  ? 156 LEU A CB   1 
ATOM   1260 C  CG   . LEU A 1 158 ? -32.877 16.841 -5.657  1.00 44.31  ? 156 LEU A CG   1 
ATOM   1261 C  CD1  . LEU A 1 158 ? -31.474 17.236 -6.065  1.00 40.86  ? 156 LEU A CD1  1 
ATOM   1262 C  CD2  . LEU A 1 158 ? -32.981 15.307 -5.551  1.00 41.56  ? 156 LEU A CD2  1 
ATOM   1263 N  N    . GLU A 1 159 ? -35.374 18.798 -2.362  1.00 48.39  ? 157 GLU A N    1 
ATOM   1264 C  CA   . GLU A 1 159 ? -35.723 19.128 -0.988  1.00 45.14  ? 157 GLU A CA   1 
ATOM   1265 C  C    . GLU A 1 159 ? -36.105 17.861 -0.239  1.00 53.04  ? 157 GLU A C    1 
ATOM   1266 O  O    . GLU A 1 159 ? -36.728 16.956 -0.809  1.00 53.21  ? 157 GLU A O    1 
ATOM   1267 C  CB   . GLU A 1 159 ? -36.862 20.151 -0.954  1.00 45.13  ? 157 GLU A CB   1 
ATOM   1268 C  CG   . GLU A 1 159 ? -36.339 21.577 -1.077  1.00 49.25  ? 157 GLU A CG   1 
ATOM   1269 C  CD   . GLU A 1 159 ? -37.422 22.615 -1.221  1.00 45.76  ? 157 GLU A CD   1 
ATOM   1270 O  OE1  . GLU A 1 159 ? -38.586 22.268 -0.977  1.00 53.46  ? 157 GLU A OE1  1 
ATOM   1271 O  OE2  . GLU A 1 159 ? -37.112 23.776 -1.586  1.00 45.94  ? 157 GLU A OE2  1 
ATOM   1272 N  N    . ARG A 1 160 ? -35.739 17.805 1.042   1.00 49.00  ? 158 ARG A N    1 
ATOM   1273 C  CA   . ARG A 1 160 ? -36.023 16.628 1.855   1.00 53.93  ? 158 ARG A CA   1 
ATOM   1274 C  C    . ARG A 1 160 ? -37.516 16.462 2.122   1.00 59.80  ? 158 ARG A C    1 
ATOM   1275 O  O    . ARG A 1 160 ? -38.219 17.415 2.475   1.00 60.74  ? 158 ARG A O    1 
ATOM   1276 C  CB   . ARG A 1 160 ? -35.278 16.703 3.187   1.00 54.34  ? 158 ARG A CB   1 
ATOM   1277 C  CG   . ARG A 1 160 ? -35.148 15.351 3.849   1.00 56.07  ? 158 ARG A CG   1 
ATOM   1278 C  CD   . ARG A 1 160 ? -34.553 15.455 5.229   1.00 56.25  ? 158 ARG A CD   1 
ATOM   1279 N  NE   . ARG A 1 160 ? -33.100 15.569 5.145   1.00 57.30  ? 158 ARG A NE   1 
ATOM   1280 C  CZ   . ARG A 1 160 ? -32.262 14.543 4.990   1.00 55.28  ? 158 ARG A CZ   1 
ATOM   1281 N  NH1  . ARG A 1 160 ? -32.721 13.300 4.895   1.00 59.43  ? 158 ARG A NH1  1 
ATOM   1282 N  NH2  . ARG A 1 160 ? -30.951 14.768 4.922   1.00 56.28  ? 158 ARG A NH2  1 
ATOM   1283 N  N    . ARG A 1 161 ? -38.002 15.238 1.950   1.00 59.92  ? 159 ARG A N    1 
ATOM   1284 C  CA   . ARG A 1 161 ? -39.361 14.930 2.332   1.00 59.94  ? 159 ARG A CA   1 
ATOM   1285 C  C    . ARG A 1 161 ? -39.438 14.890 3.855   1.00 70.47  ? 159 ARG A C    1 
ATOM   1286 O  O    . ARG A 1 161 ? -39.548 13.830 4.466   1.00 79.24  ? 159 ARG A O    1 
ATOM   1287 C  CB   . ARG A 1 161 ? -39.805 13.607 1.716   1.00 66.00  ? 159 ARG A CB   1 
ATOM   1288 C  CG   . ARG A 1 161 ? -39.678 13.565 0.210   1.00 63.12  ? 159 ARG A CG   1 
ATOM   1289 C  CD   . ARG A 1 161 ? -40.404 12.353 -0.371  1.00 65.22  ? 159 ARG A CD   1 
ATOM   1290 N  NE   . ARG A 1 161 ? -39.890 12.046 -1.705  1.00 73.20  ? 159 ARG A NE   1 
ATOM   1291 C  CZ   . ARG A 1 161 ? -40.556 12.275 -2.836  1.00 74.12  ? 159 ARG A CZ   1 
ATOM   1292 N  NH1  . ARG A 1 161 ? -41.782 12.795 -2.780  1.00 67.68  ? 159 ARG A NH1  1 
ATOM   1293 N  NH2  . ARG A 1 161 ? -40.004 11.977 -4.020  1.00 70.24  ? 159 ARG A NH2  1 
ATOM   1294 O  OXT  . ARG A 1 161 ? -39.369 15.924 4.522   1.00 85.31  ? 159 ARG A OXT  1 
HETATM 1295 N  N1   . 1CY B 2 .   ? -20.417 25.548 -8.514  1.00 42.06  ? 201 1CY A N1   1 
HETATM 1296 C  C2   . 1CY B 2 .   ? -21.394 24.974 -7.795  1.00 40.12  ? 201 1CY A C2   1 
HETATM 1297 N  N3   . 1CY B 2 .   ? -21.283 24.506 -6.532  1.00 42.53  ? 201 1CY A N3   1 
HETATM 1298 C  C4   . 1CY B 2 .   ? -20.221 24.914 -5.840  1.00 36.30  ? 201 1CY A C4   1 
HETATM 1299 N  N5   . 1CY B 2 .   ? -19.185 25.571 -6.443  1.00 43.84  ? 201 1CY A N5   1 
HETATM 1300 C  C6   . 1CY B 2 .   ? -19.086 25.692 -7.912  1.00 41.68  ? 201 1CY A C6   1 
HETATM 1301 N  N7   . 1CY B 2 .   ? -22.596 24.838 -8.338  1.00 42.88  ? 201 1CY A N7   1 
HETATM 1302 N  N8   . 1CY B 2 .   ? -20.152 24.616 -4.560  1.00 38.86  ? 201 1CY A N8   1 
HETATM 1303 C  C9   . 1CY B 2 .   ? -18.168 24.580 -8.387  1.00 46.77  ? 201 1CY A C9   1 
HETATM 1304 C  C10  . 1CY B 2 .   ? -18.533 27.043 -8.329  1.00 47.65  ? 201 1CY A C10  1 
HETATM 1305 C  C11  . 1CY B 2 .   ? -18.116 26.122 -5.656  1.00 44.96  ? 201 1CY A C11  1 
HETATM 1306 C  C12  . 1CY B 2 .   ? -18.086 27.474 -5.352  1.00 46.65  ? 201 1CY A C12  1 
HETATM 1307 C  C13  . 1CY B 2 .   ? -17.063 28.002 -4.584  1.00 43.52  ? 201 1CY A C13  1 
HETATM 1308 C  C14  . 1CY B 2 .   ? -16.083 27.160 -4.114  1.00 48.55  ? 201 1CY A C14  1 
HETATM 1309 C  C15  . 1CY B 2 .   ? -16.105 25.810 -4.375  1.00 48.39  ? 201 1CY A C15  1 
HETATM 1310 C  C16  . 1CY B 2 .   ? -17.126 25.295 -5.152  1.00 48.84  ? 201 1CY A C16  1 
HETATM 1311 CL CL17 . 1CY B 2 .   ? -14.800 27.816 -3.148  1.00 58.94  ? 201 1CY A CL17 1 
HETATM 1312 C  CAC  . FLC C 3 .   ? -12.649 19.215 7.802   1.00 63.96  ? 202 FLC A CAC  1 
HETATM 1313 C  CA   . FLC C 3 .   ? -12.059 20.074 6.659   1.00 52.25  ? 202 FLC A CA   1 
HETATM 1314 C  CB   . FLC C 3 .   ? -10.784 19.362 6.244   1.00 62.32  ? 202 FLC A CB   1 
HETATM 1315 C  CBC  . FLC C 3 .   ? -9.741  19.522 7.361   1.00 61.85  ? 202 FLC A CBC  1 
HETATM 1316 C  CG   . FLC C 3 .   ? -10.285 19.860 4.882   1.00 59.15  ? 202 FLC A CG   1 
HETATM 1317 C  CGC  . FLC C 3 .   ? -11.287 19.626 3.743   1.00 52.63  ? 202 FLC A CGC  1 
HETATM 1318 O  OA1  . FLC C 3 .   ? -12.343 19.489 9.000   1.00 66.21  ? 202 FLC A OA1  1 
HETATM 1319 O  OA2  . FLC C 3 .   ? -13.419 18.226 7.571   1.00 60.79  ? 202 FLC A OA2  1 
HETATM 1320 O  OB1  . FLC C 3 .   ? -9.249  20.662 7.626   1.00 61.75  ? 202 FLC A OB1  1 
HETATM 1321 O  OB2  . FLC C 3 .   ? -9.384  18.495 8.016   1.00 57.13  ? 202 FLC A OB2  1 
HETATM 1322 O  OG1  . FLC C 3 .   ? -11.947 18.555 3.684   1.00 48.88  ? 202 FLC A OG1  1 
HETATM 1323 O  OG2  . FLC C 3 .   ? -11.469 20.511 2.863   1.00 53.84  ? 202 FLC A OG2  1 
HETATM 1324 O  OHB  . FLC C 3 .   ? -11.098 17.995 6.153   1.00 68.36  ? 202 FLC A OHB  1 
HETATM 1325 O  O    . HOH D 4 .   ? -23.261 32.837 -24.968 1.00 68.29  ? 301 HOH A O    1 
HETATM 1326 O  O    . HOH D 4 .   ? -24.796 13.768 -23.107 1.00 49.89  ? 302 HOH A O    1 
HETATM 1327 O  O    . HOH D 4 .   ? -15.833 35.225 9.439   1.00 53.91  ? 303 HOH A O    1 
HETATM 1328 O  O    . HOH D 4 .   ? -12.754 21.190 0.847   1.00 48.92  ? 304 HOH A O    1 
HETATM 1329 O  O    . HOH D 4 .   ? -21.589 19.674 19.214  1.00 56.66  ? 305 HOH A O    1 
HETATM 1330 O  O    . HOH D 4 .   ? -27.111 17.025 -17.966 1.00 49.69  ? 306 HOH A O    1 
HETATM 1331 O  O    . HOH D 4 .   ? -24.206 31.771 -22.478 1.00 59.84  ? 307 HOH A O    1 
HETATM 1332 O  O    . HOH D 4 .   ? -13.976 18.353 2.084   1.00 50.84  ? 308 HOH A O    1 
HETATM 1333 O  O    . HOH D 4 .   ? -18.932 21.473 -6.364  1.00 44.41  ? 309 HOH A O    1 
HETATM 1334 O  O    . HOH D 4 .   ? -8.165  28.507 14.588  1.00 50.55  ? 310 HOH A O    1 
HETATM 1335 O  O    . HOH D 4 .   ? -25.471 31.590 16.587  1.00 46.53  ? 311 HOH A O    1 
HETATM 1336 O  O    . HOH D 4 .   ? -3.650  19.993 3.968   1.00 63.43  ? 312 HOH A O    1 
HETATM 1337 O  O    . HOH D 4 .   ? -32.966 16.759 8.652   1.00 61.84  ? 313 HOH A O    1 
HETATM 1338 O  O    . HOH D 4 .   ? -20.409 33.706 -14.739 1.00 56.28  ? 314 HOH A O    1 
HETATM 1339 O  O    . HOH D 4 .   ? -37.061 17.582 -11.491 1.00 51.15  ? 315 HOH A O    1 
HETATM 1340 O  O    . HOH D 4 .   ? -27.428 29.170 13.301  1.00 50.95  ? 316 HOH A O    1 
HETATM 1341 O  O    . HOH D 4 .   ? -25.369 27.584 -21.915 1.00 48.74  ? 317 HOH A O    1 
HETATM 1342 O  O    . HOH D 4 .   ? -29.580 32.999 4.775   1.00 45.22  ? 318 HOH A O    1 
HETATM 1343 O  O    . HOH D 4 .   ? -5.344  30.638 4.897   1.00 47.87  ? 319 HOH A O    1 
HETATM 1344 O  O    . HOH D 4 .   ? -24.554 12.934 -20.652 1.00 44.89  ? 320 HOH A O    1 
HETATM 1345 O  O    . HOH D 4 .   ? -33.944 28.985 -0.468  1.00 47.97  ? 321 HOH A O    1 
HETATM 1346 O  O    . HOH D 4 .   ? -9.839  25.430 13.050  1.00 54.04  ? 322 HOH A O    1 
HETATM 1347 O  O    . HOH D 4 .   ? -40.364 17.331 -0.385  1.00 57.59  ? 323 HOH A O    1 
HETATM 1348 O  O    . HOH D 4 .   ? -10.394 34.078 12.344  1.00 52.47  ? 324 HOH A O    1 
HETATM 1349 O  O    . HOH D 4 .   ? -14.860 30.127 15.826  1.00 51.10  ? 325 HOH A O    1 
HETATM 1350 O  O    . HOH D 4 .   ? -28.243 35.292 5.306   1.00 48.53  ? 326 HOH A O    1 
HETATM 1351 O  O    . HOH D 4 .   ? -4.634  32.937 4.144   1.00 50.27  ? 327 HOH A O    1 
HETATM 1352 O  O    . HOH D 4 .   ? -29.740 24.635 11.926  1.00 65.05  ? 328 HOH A O    1 
HETATM 1353 O  O    . HOH D 4 .   ? -15.785 36.186 6.540   1.00 52.19  ? 329 HOH A O    1 
HETATM 1354 O  O    . HOH D 4 .   ? -18.378 17.771 13.609  1.00 49.94  ? 330 HOH A O    1 
HETATM 1355 O  O    . HOH D 4 .   ? -25.335 23.609 -8.114  1.00 37.71  ? 331 HOH A O    1 
HETATM 1356 O  O    . HOH D 4 .   ? -26.822 30.749 -14.527 1.00 54.56  ? 332 HOH A O    1 
HETATM 1357 O  O    . HOH D 4 .   ? -2.736  33.148 5.265   1.00 49.45  ? 333 HOH A O    1 
HETATM 1358 O  O    . HOH D 4 .   ? -19.496 28.919 16.526  1.00 42.32  ? 334 HOH A O    1 
HETATM 1359 O  O    . HOH D 4 .   ? -28.756 27.738 -22.629 1.00 50.83  ? 335 HOH A O    1 
HETATM 1360 O  O    . HOH D 4 .   ? -35.078 21.438 -18.418 1.00 40.56  ? 336 HOH A O    1 
HETATM 1361 O  O    . HOH D 4 .   ? -11.514 31.871 13.903  1.00 40.60  ? 337 HOH A O    1 
HETATM 1362 O  O    . HOH D 4 .   ? -35.333 27.848 -4.717  1.00 48.97  ? 338 HOH A O    1 
HETATM 1363 O  O    . HOH D 4 .   ? -20.364 18.763 15.652  1.00 48.83  ? 339 HOH A O    1 
HETATM 1364 O  O    . HOH D 4 .   ? -6.679  39.911 -0.830  1.00 63.96  ? 340 HOH A O    1 
HETATM 1365 O  O    . HOH D 4 .   ? -30.103 25.740 -23.838 1.00 49.53  ? 341 HOH A O    1 
HETATM 1366 O  O    . HOH D 4 .   ? -10.387 17.143 -0.503  1.00 59.56  ? 342 HOH A O    1 
HETATM 1367 O  O    . HOH D 4 .   ? -28.248 31.841 -12.514 1.00 55.60  ? 343 HOH A O    1 
HETATM 1368 O  O    . HOH D 4 .   ? -15.883 27.942 19.714  1.00 48.10  ? 344 HOH A O    1 
HETATM 1369 O  O    . HOH D 4 .   ? -14.163 37.071 10.732  1.00 56.76  ? 345 HOH A O    1 
HETATM 1370 O  O    . HOH D 4 .   ? -12.104 19.226 -1.204  1.00 52.89  ? 346 HOH A O    1 
HETATM 1371 O  O    . HOH D 4 .   ? -31.094 33.797 2.842   1.00 47.87  ? 347 HOH A O    1 
HETATM 1372 O  O    . HOH D 4 .   ? -9.483  30.582 14.945  1.00 48.35  ? 348 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   . SER A 1   ? 0.8422 1.2460 0.9763 0.0641  0.1841  -0.2306 -1  SER A N   
2    C CA  . SER A 1   ? 0.8034 1.1526 0.9158 0.0644  0.1811  -0.2671 -1  SER A CA  
3    C C   . SER A 1   ? 0.8027 1.1474 0.8773 0.0375  0.1628  -0.2604 -1  SER A C   
4    O O   . SER A 1   ? 0.8336 1.2182 0.8909 0.0217  0.1545  -0.2329 -1  SER A O   
5    C CB  . SER A 1   ? 0.8643 1.2279 0.9635 0.0823  0.2053  -0.3148 -1  SER A CB  
6    O OG  . SER A 1   ? 1.0075 1.4237 1.0643 0.0673  0.2126  -0.3245 -1  SER A OG  
7    N N   . HIS A 2   ? 0.9208 1.2166 0.9834 0.0317  0.1545  -0.2846 0   HIS A N   
8    C CA  . HIS A 2   ? 0.8978 1.1894 0.9361 0.0092  0.1341  -0.2770 0   HIS A CA  
9    C C   . HIS A 2   ? 0.8359 1.1266 0.8879 0.0026  0.1149  -0.2320 0   HIS A C   
10   O O   . HIS A 2   ? 0.8796 1.1892 0.9110 -0.0110 0.0983  -0.2154 0   HIS A O   
11   C CB  . HIS A 2   ? 0.8898 1.2303 0.8857 -0.0034 0.1354  -0.2893 0   HIS A CB  
12   C CG  . HIS A 2   ? 0.9387 1.2855 0.9134 0.0037  0.1555  -0.3355 0   HIS A CG  
13   N ND1 . HIS A 2   ? 1.0147 1.4064 0.9461 -0.0067 0.1598  -0.3516 0   HIS A ND1 
14   C CD2 . HIS A 2   ? 0.9580 1.2686 0.9451 0.0216  0.1713  -0.3699 0   HIS A CD2 
15   C CE1 . HIS A 2   ? 0.9927 1.3768 0.9095 0.0042  0.1787  -0.3967 0   HIS A CE1 
16   N NE2 . HIS A 2   ? 0.9945 1.3271 0.9454 0.0228  0.1855  -0.4091 0   HIS A NE2 
17   N N   . MET A 3   ? 0.7335 1.0002 0.8186 0.0136  0.1151  -0.2127 1   MET A N   
18   C CA  . MET A 3   ? 0.6231 0.8825 0.7187 0.0082  0.0967  -0.1727 1   MET A CA  
19   C C   . MET A 3   ? 0.5808 0.8075 0.6691 -0.0015 0.0781  -0.1712 1   MET A C   
20   O O   . MET A 3   ? 0.5574 0.7505 0.6509 -0.0025 0.0805  -0.1933 1   MET A O   
21   C CB  . MET A 3   ? 0.5290 0.7681 0.6602 0.0214  0.1002  -0.1569 1   MET A CB  
22   C CG  . MET A 3   ? 0.6439 0.8502 0.7831 0.0158  0.0793  -0.1263 1   MET A CG  
23   S SD  . MET A 3   ? 0.6663 0.8556 0.8424 0.0271  0.0775  -0.1009 1   MET A SD  
24   C CE  . MET A 3   ? 0.5309 0.6637 0.7229 0.0399  0.0851  -0.1271 1   MET A CE  
25   N N   . ILE A 4   ? 0.5516 0.7886 0.6276 -0.0089 0.0590  -0.1451 2   ILE A N   
26   C CA  . ILE A 4   ? 0.5353 0.7535 0.6065 -0.0138 0.0417  -0.1444 2   ILE A CA  
27   C C   . ILE A 4   ? 0.5178 0.6995 0.6068 -0.0088 0.0321  -0.1219 2   ILE A C   
28   O O   . ILE A 4   ? 0.4926 0.6724 0.5843 -0.0065 0.0247  -0.0937 2   ILE A O   
29   C CB  . ILE A 4   ? 0.5404 0.7877 0.5854 -0.0198 0.0233  -0.1327 2   ILE A CB  
30   C CG1 . ILE A 4   ? 0.6036 0.8906 0.6236 -0.0270 0.0309  -0.1519 2   ILE A CG1 
31   C CG2 . ILE A 4   ? 0.4674 0.7040 0.5144 -0.0197 0.0072  -0.1371 2   ILE A CG2 
32   C CD1 . ILE A 4   ? 0.5761 0.8614 0.5954 -0.0318 0.0401  -0.1904 2   ILE A CD1 
33   N N   . SER A 5   ? 0.4495 0.6038 0.5475 -0.0102 0.0313  -0.1338 3   SER A N   
34   C CA  . SER A 5   ? 0.4630 0.5823 0.5723 -0.0068 0.0238  -0.1166 3   SER A CA  
35   C C   . SER A 5   ? 0.4337 0.5540 0.5376 -0.0097 0.0130  -0.1222 3   SER A C   
36   O O   . SER A 5   ? 0.4292 0.5692 0.5309 -0.0174 0.0163  -0.1448 3   SER A O   
37   C CB  . SER A 5   ? 0.4398 0.5240 0.5665 -0.0059 0.0368  -0.1245 3   SER A CB  
38   O OG  . SER A 5   ? 0.4530 0.5393 0.5919 0.0027  0.0454  -0.1179 3   SER A OG  
39   N N   . LEU A 6   ? 0.4011 0.5034 0.5032 -0.0035 -0.0001 -0.1029 4   LEU A N   
40   C CA  . LEU A 6   ? 0.4253 0.5304 0.5258 -0.0014 -0.0083 -0.1086 4   LEU A CA  
41   C C   . LEU A 6   ? 0.4432 0.5142 0.5510 -0.0042 -0.0016 -0.1059 4   LEU A C   
42   O O   . LEU A 6   ? 0.4026 0.4426 0.5102 -0.0010 -0.0040 -0.0875 4   LEU A O   
43   C CB  . LEU A 6   ? 0.4084 0.5150 0.4944 0.0115  -0.0303 -0.0911 4   LEU A CB  
44   C CG  . LEU A 6   ? 0.4704 0.6114 0.5448 0.0160  -0.0439 -0.0939 4   LEU A CG  
45   C CD1 . LEU A 6   ? 0.4136 0.5754 0.4819 0.0062  -0.0360 -0.0958 4   LEU A CD1 
46   C CD2 . LEU A 6   ? 0.4322 0.5528 0.4893 0.0292  -0.0680 -0.0709 4   LEU A CD2 
47   N N   . ILE A 7   ? 0.3965 0.4762 0.5099 -0.0128 0.0058  -0.1225 5   ILE A N   
48   C CA  . ILE A 7   ? 0.4246 0.4753 0.5387 -0.0187 0.0117  -0.1182 5   ILE A CA  
49   C C   . ILE A 7   ? 0.4366 0.5135 0.5493 -0.0162 0.0088  -0.1259 5   ILE A C   
50   O O   . ILE A 7   ? 0.4235 0.5419 0.5455 -0.0233 0.0126  -0.1444 5   ILE A O   
51   C CB  . ILE A 7   ? 0.4217 0.4513 0.5430 -0.0367 0.0271  -0.1285 5   ILE A CB  
52   C CG1 . ILE A 7   ? 0.4290 0.4250 0.5451 -0.0452 0.0310  -0.1184 5   ILE A CG1 
53   C CG2 . ILE A 7   ? 0.4254 0.4874 0.5527 -0.0516 0.0342  -0.1534 5   ILE A CG2 
54   C CD1 . ILE A 7   ? 0.4635 0.4190 0.5820 -0.0598 0.0405  -0.1198 5   ILE A CD1 
55   N N   . ALA A 8   ? 0.4159 0.4723 0.5170 -0.0054 0.0017  -0.1134 6   ALA A N   
56   C CA  . ALA A 8   ? 0.4091 0.4929 0.5076 0.0046  -0.0012 -0.1225 6   ALA A CA  
57   C C   . ALA A 8   ? 0.4745 0.5288 0.5582 0.0032  0.0028  -0.1147 6   ALA A C   
58   O O   . ALA A 8   ? 0.4631 0.4703 0.5348 0.0009  -0.0009 -0.0970 6   ALA A O   
59   C CB  . ALA A 8   ? 0.4063 0.4990 0.4972 0.0302  -0.0220 -0.1189 6   ALA A CB  
60   N N   . ALA A 9   ? 0.4859 0.5739 0.5705 0.0044  0.0105  -0.1284 7   ALA A N   
61   C CA  . ALA A 9   ? 0.5157 0.5856 0.5800 0.0067  0.0142  -0.1247 7   ALA A CA  
62   C C   . ALA A 9   ? 0.5466 0.6287 0.6011 0.0386  0.0004  -0.1325 7   ALA A C   
63   O O   . ALA A 9   ? 0.5349 0.6688 0.6065 0.0525  -0.0010 -0.1493 7   ALA A O   
64   C CB  . ALA A 9   ? 0.4823 0.5847 0.5519 -0.0174 0.0361  -0.1350 7   ALA A CB  
65   N N   . LEU A 10  ? 0.5611 0.5935 0.5877 0.0511  -0.0123 -0.1209 8   LEU A N   
66   C CA  . LEU A 10  ? 0.5974 0.6217 0.6083 0.0835  -0.0308 -0.1275 8   LEU A CA  
67   C C   . LEU A 10  ? 0.6262 0.6376 0.6095 0.0909  -0.0253 -0.1351 8   LEU A C   
68   O O   . LEU A 10  ? 0.6457 0.6218 0.6093 0.0721  -0.0198 -0.1224 8   LEU A O   
69   C CB  . LEU A 10  ? 0.6422 0.6111 0.6381 0.0912  -0.0564 -0.1071 8   LEU A CB  
70   C CG  . LEU A 10  ? 0.6179 0.6005 0.6345 0.0851  -0.0623 -0.0986 8   LEU A CG  
71   C CD1 . LEU A 10  ? 0.6446 0.5792 0.6425 0.0927  -0.0883 -0.0782 8   LEU A CD1 
72   C CD2 . LEU A 10  ? 0.6269 0.6692 0.6657 0.0969  -0.0605 -0.1175 8   LEU A CD2 
73   N N   . ALA A 11  ? 0.6623 0.7049 0.6434 0.1193  -0.0269 -0.1569 9   ALA A N   
74   C CA  . ALA A 11  ? 0.6722 0.6960 0.6194 0.1357  -0.0263 -0.1680 9   ALA A CA  
75   C C   . ALA A 11  ? 0.8084 0.7902 0.7369 0.1726  -0.0566 -0.1719 9   ALA A C   
76   O O   . ALA A 11  ? 0.9208 0.9393 0.8649 0.2032  -0.0625 -0.1908 9   ALA A O   
77   C CB  . ALA A 11  ? 0.6892 0.7887 0.6488 0.1405  -0.0005 -0.1939 9   ALA A CB  
78   N N   . VAL A 12  ? 0.8627 0.7671 0.7591 0.1688  -0.0783 -0.1527 10  VAL A N   
79   C CA  . VAL A 12  ? 0.9590 0.8088 0.8301 0.1984  -0.1107 -0.1534 10  VAL A CA  
80   C C   . VAL A 12  ? 1.0932 0.9597 0.9899 0.2125  -0.1268 -0.1496 10  VAL A C   
81   O O   . VAL A 12  ? 1.1169 0.9812 1.0084 0.2489  -0.1439 -0.1653 10  VAL A O   
82   C CB  . VAL A 12  ? 0.9080 0.7575 0.7534 0.2347  -0.1116 -0.1838 10  VAL A CB  
83   C CG1 . VAL A 12  ? 1.0495 0.8267 0.8640 0.2653  -0.1498 -0.1840 10  VAL A CG1 
84   C CG2 . VAL A 12  ? 0.9268 0.7674 0.7411 0.2202  -0.0934 -0.1897 10  VAL A CG2 
85   N N   . ASP A 13  ? 0.8820 0.7646 0.8040 0.1856  -0.1223 -0.1299 11  ASP A N   
86   C CA  A ASP A 13  ? 0.8878 0.7884 0.8297 0.1917  -0.1362 -0.1228 11  ASP A CA  
87   C CA  B ASP A 13  ? 0.8911 0.7936 0.8344 0.1899  -0.1349 -0.1224 11  ASP A CA  
88   C C   . ASP A 13  ? 0.8110 0.7928 0.7883 0.2055  -0.1225 -0.1455 11  ASP A C   
89   O O   . ASP A 13  ? 0.8043 0.8079 0.7978 0.2089  -0.1337 -0.1406 11  ASP A O   
90   C CB  A ASP A 13  ? 0.9364 0.7761 0.8494 0.2157  -0.1736 -0.1139 11  ASP A CB  
91   C CB  B ASP A 13  ? 0.9367 0.7759 0.8516 0.2089  -0.1724 -0.1093 11  ASP A CB  
92   C CG  A ASP A 13  ? 0.9106 0.7365 0.8274 0.1991  -0.1904 -0.0866 11  ASP A CG  
93   C CG  B ASP A 13  ? 0.9512 0.7778 0.8497 0.2532  -0.1894 -0.1323 11  ASP A CG  
94   O OD1 A ASP A 13  ? 0.9214 0.7335 0.8396 0.1673  -0.1841 -0.0651 11  ASP A OD1 
95   O OD1 B ASP A 13  ? 0.9495 0.8375 0.8742 0.2767  -0.1826 -0.1536 11  ASP A OD1 
96   O OD2 A ASP A 13  ? 0.8970 0.7270 0.8142 0.2186  -0.2104 -0.0862 11  ASP A OD2 
97   O OD2 B ASP A 13  ? 1.0031 0.7575 0.8622 0.2655  -0.2113 -0.1303 11  ASP A OD2 
98   N N   . ARG A 14  ? 0.7623 0.7945 0.7520 0.2108  -0.0993 -0.1690 12  ARG A N   
99   C CA  . ARG A 14  ? 0.7582 0.8775 0.7869 0.2190  -0.0862 -0.1893 12  ARG A CA  
100  C C   . ARG A 14  ? 0.6864 0.8510 0.7416 0.1778  -0.0586 -0.1862 12  ARG A C   
101  O O   . ARG A 14  ? 0.7000 0.8492 0.7450 0.1523  -0.0398 -0.1809 12  ARG A O   
102  C CB  . ARG A 14  ? 0.7252 0.8852 0.7561 0.2507  -0.0774 -0.2186 12  ARG A CB  
103  C CG  . ARG A 14  ? 0.8051 0.9433 0.8266 0.2990  -0.1083 -0.2277 12  ARG A CG  
104  C CD  . ARG A 14  ? 0.9604 1.1182 0.9745 0.3399  -0.1046 -0.2581 12  ARG A CD  
105  N NE  . ARG A 14  ? 1.0500 1.1568 1.0458 0.3864  -0.1421 -0.2617 12  ARG A NE  
106  C CZ  . ARG A 14  ? 1.0647 1.1797 1.0555 0.4373  -0.1505 -0.2904 12  ARG A CZ  
107  N NH1 . ARG A 14  ? 1.0881 1.2713 1.0920 0.4490  -0.1206 -0.3198 12  ARG A NH1 
108  N NH2 . ARG A 14  ? 1.1246 1.1778 1.0943 0.4729  -0.1890 -0.2873 12  ARG A NH2 
109  N N   . VAL A 15  ? 0.6960 0.9112 0.7816 0.1710  -0.0589 -0.1892 13  VAL A N   
110  C CA  . VAL A 15  ? 0.6445 0.8859 0.7497 0.1311  -0.0391 -0.1853 13  VAL A CA  
111  C C   . VAL A 15  ? 0.6640 0.9723 0.7917 0.1151  -0.0120 -0.2039 13  VAL A C   
112  O O   . VAL A 15  ? 0.5435 0.9201 0.6943 0.1345  -0.0103 -0.2239 13  VAL A O   
113  C CB  . VAL A 15  ? 0.6465 0.9130 0.7688 0.1282  -0.0516 -0.1828 13  VAL A CB  
114  C CG1 . VAL A 15  ? 0.5571 0.8553 0.6995 0.0891  -0.0310 -0.1865 13  VAL A CG1 
115  C CG2 . VAL A 15  ? 0.7010 0.9024 0.7979 0.1335  -0.0739 -0.1597 13  VAL A CG2 
116  N N   . ILE A 16  ? 0.6773 0.9682 0.7995 0.0787  0.0082  -0.1960 14  ILE A N   
117  C CA  . ILE A 16  ? 0.7242 1.0682 0.8612 0.0522  0.0345  -0.2073 14  ILE A CA  
118  C C   . ILE A 16  ? 0.7151 1.0831 0.8749 0.0165  0.0425  -0.2076 14  ILE A C   
119  O O   . ILE A 16  ? 0.6664 0.9807 0.8159 0.0000  0.0389  -0.1936 14  ILE A O   
120  C CB  . ILE A 16  ? 0.7349 1.0337 0.8417 0.0348  0.0488  -0.1963 14  ILE A CB  
121  C CG1 . ILE A 16  ? 0.6458 0.9200 0.7247 0.0690  0.0406  -0.2000 14  ILE A CG1 
122  C CG2 . ILE A 16  ? 0.8419 1.1916 0.9596 -0.0010 0.0759  -0.2028 14  ILE A CG2 
123  C CD1 . ILE A 16  ? 0.6272 0.8226 0.6677 0.0585  0.0380  -0.1803 14  ILE A CD1 
124  N N   . GLY A 17  ? 0.7464 1.1967 0.9373 0.0049  0.0528  -0.2250 15  GLY A N   
125  C CA  . GLY A 17  ? 0.7524 1.2273 0.9624 -0.0331 0.0598  -0.2286 15  GLY A CA  
126  C C   . GLY A 17  ? 0.8869 1.4079 1.1078 -0.0709 0.0840  -0.2344 15  GLY A C   
127  O O   . GLY A 17  ? 0.9432 1.4833 1.1566 -0.0668 0.0975  -0.2356 15  GLY A O   
128  N N   . MET A 18  ? 0.8337 1.3715 1.0692 -0.1103 0.0889  -0.2381 16  MET A N   
129  C CA  . MET A 18  ? 0.8330 1.4146 1.0789 -0.1549 0.1097  -0.2412 16  MET A CA  
130  C C   . MET A 18  ? 0.8624 1.5559 1.1410 -0.1450 0.1191  -0.2581 16  MET A C   
131  O O   . MET A 18  ? 0.9161 1.6573 1.2021 -0.1802 0.1397  -0.2590 16  MET A O   
132  C CB  . MET A 18  ? 0.7359 1.3120 0.9910 -0.1980 0.1078  -0.2450 16  MET A CB  
133  C CG  . MET A 18  ? 0.7762 1.2502 1.0037 -0.1982 0.0977  -0.2338 16  MET A CG  
134  S SD  . MET A 18  ? 0.8640 1.2419 1.0524 -0.2127 0.1085  -0.2094 16  MET A SD  
135  C CE  . MET A 18  ? 0.9409 1.3193 1.1291 -0.2786 0.1219  -0.2089 16  MET A CE  
136  N N   . GLU A 19  ? 0.8913 1.6294 1.1899 -0.0979 0.1040  -0.2707 17  GLU A N   
137  C CA  . GLU A 19  ? 0.9167 1.7680 1.2524 -0.0805 0.1113  -0.2895 17  GLU A CA  
138  C C   . GLU A 19  ? 0.9597 1.8196 1.2782 -0.0690 0.1318  -0.2898 17  GLU A C   
139  O O   . GLU A 19  ? 0.9358 1.8926 1.2805 -0.0781 0.1512  -0.3028 17  GLU A O   
140  C CB  . GLU A 19  ? 0.9140 1.7958 1.2703 -0.0262 0.0857  -0.3012 17  GLU A CB  
141  C CG  . GLU A 19  ? 0.8635 1.7341 1.2288 -0.0334 0.0627  -0.3001 17  GLU A CG  
142  C CD  . GLU A 19  ? 0.9365 1.6938 1.2607 -0.0188 0.0461  -0.2829 17  GLU A CD  
143  O OE1 . GLU A 19  ? 1.0189 1.7097 1.3120 -0.0009 0.0492  -0.2717 17  GLU A OE1 
144  O OE2 . GLU A 19  ? 0.8019 1.5412 1.1244 -0.0263 0.0301  -0.2809 17  GLU A OE2 
145  N N   . ASN A 20  ? 1.0673 1.8316 1.3414 -0.0509 0.1279  -0.2762 18  ASN A N   
146  C CA  . ASN A 20  ? 1.1343 1.8936 1.3816 -0.0394 0.1446  -0.2765 18  ASN A CA  
147  C C   . ASN A 20  ? 1.1165 1.8587 1.3411 -0.0960 0.1686  -0.2610 18  ASN A C   
148  O O   . ASN A 20  ? 1.1217 1.8166 1.3399 -0.1380 0.1670  -0.2455 18  ASN A O   
149  C CB  . ASN A 20  ? 1.1225 1.7837 1.3287 0.0003  0.1266  -0.2675 18  ASN A CB  
150  C CG  . ASN A 20  ? 1.1297 1.7850 1.3496 0.0497  0.0981  -0.2758 18  ASN A CG  
151  O OD1 . ASN A 20  ? 1.0365 1.6166 1.2408 0.0549  0.0773  -0.2610 18  ASN A OD1 
152  N ND2 . ASN A 20  ? 1.1506 1.8877 1.4001 0.0865  0.0964  -0.2988 18  ASN A ND2 
153  N N   . ALA A 21  ? 1.0687 1.8473 1.2776 -0.0956 0.1902  -0.2658 19  ALA A N   
154  C CA  . ALA A 21  ? 1.0488 1.8099 1.2279 -0.1485 0.2122  -0.2481 19  ALA A CA  
155  C C   . ALA A 21  ? 1.1453 1.7786 1.2712 -0.1545 0.2018  -0.2226 19  ALA A C   
156  O O   . ALA A 21  ? 1.1877 1.7897 1.2833 -0.1980 0.2150  -0.2034 19  ALA A O   
157  C CB  . ALA A 21  ? 0.9069 1.7536 1.0815 -0.1452 0.2400  -0.2617 19  ALA A CB  
158  N N   . MET A 22  ? 1.1265 1.6874 1.2406 -0.1147 0.1774  -0.2200 20  MET A N   
159  C CA  . MET A 22  ? 1.1762 1.6338 1.2413 -0.1162 0.1692  -0.1978 20  MET A CA  
160  C C   . MET A 22  ? 1.2019 1.5751 1.2628 -0.1374 0.1537  -0.1763 20  MET A C   
161  O O   . MET A 22  ? 1.2302 1.5286 1.2557 -0.1545 0.1513  -0.1541 20  MET A O   
162  C CB  . MET A 22  ? 1.1359 1.5587 1.1817 -0.0624 0.1523  -0.2055 20  MET A CB  
163  C CG  . MET A 22  ? 1.0981 1.4238 1.0958 -0.0656 0.1422  -0.1833 20  MET A CG  
164  S SD  . MET A 22  ? 1.1765 1.4673 1.1585 -0.0059 0.1182  -0.1953 20  MET A SD  
165  C CE  . MET A 22  ? 0.9541 1.2240 0.9737 0.0039  0.0949  -0.1898 20  MET A CE  
166  N N   . PRO A 23  ? 1.1629 1.5452 1.2573 -0.1356 0.1425  -0.1826 21  PRO A N   
167  C CA  . PRO A 23  ? 1.1495 1.4606 1.2396 -0.1608 0.1335  -0.1661 21  PRO A CA  
168  C C   . PRO A 23  ? 1.1210 1.4104 1.1937 -0.2124 0.1479  -0.1508 21  PRO A C   
169  O O   . PRO A 23  ? 1.0888 1.2948 1.1342 -0.2246 0.1414  -0.1295 21  PRO A O   
170  C CB  . PRO A 23  ? 0.9903 1.3426 1.1189 -0.1575 0.1255  -0.1821 21  PRO A CB  
171  C CG  . PRO A 23  ? 0.9957 1.4045 1.1414 -0.1127 0.1181  -0.1994 21  PRO A CG  
172  C CD  . PRO A 23  ? 1.1121 1.5494 1.2407 -0.0997 0.1312  -0.2033 21  PRO A CD  
173  N N   . TRP A 24  ? 1.2138 1.5789 1.3011 -0.2434 0.1666  -0.1596 22  TRP A N   
174  C CA  . TRP A 24  ? 1.2283 1.5750 1.2943 -0.2979 0.1803  -0.1423 22  TRP A CA  
175  C C   . TRP A 24  ? 1.2216 1.5324 1.2415 -0.3001 0.1875  -0.1239 22  TRP A C   
176  O O   . TRP A 24  ? 1.1894 1.4445 1.1784 -0.3392 0.1900  -0.1003 22  TRP A O   
177  C CB  . TRP A 24  ? 1.2412 1.6909 1.3366 -0.3331 0.1990  -0.1558 22  TRP A CB  
178  C CG  . TRP A 24  ? 1.2958 1.7960 1.4375 -0.3283 0.1901  -0.1768 22  TRP A CG  
179  C CD1 . TRP A 24  ? 1.2605 1.8578 1.4414 -0.2978 0.1908  -0.2009 22  TRP A CD1 
180  C CD2 . TRP A 24  ? 1.3654 1.8222 1.5163 -0.3548 0.1777  -0.1765 22  TRP A CD2 
181  N NE1 . TRP A 24  ? 1.3332 1.9519 1.5462 -0.3054 0.1785  -0.2133 22  TRP A NE1 
182  C CE2 . TRP A 24  ? 1.3388 1.8726 1.5325 -0.3411 0.1714  -0.2002 22  TRP A CE2 
183  C CE3 . TRP A 24  ? 1.3254 1.6835 1.4509 -0.3864 0.1699  -0.1600 22  TRP A CE3 
184  C CZ2 . TRP A 24  ? 1.2691 1.7857 1.4769 -0.3611 0.1588  -0.2087 22  TRP A CZ2 
185  C CZ3 . TRP A 24  ? 1.2488 1.5869 1.3897 -0.4026 0.1582  -0.1708 22  TRP A CZ3 
186  C CH2 . TRP A 24  ? 1.2831 1.7007 1.4629 -0.3916 0.1533  -0.1953 22  TRP A CH2 
187  N N   . ASN A 25  ? 1.3184 1.6556 1.3290 -0.2592 0.1890  -0.1341 23  ASN A N   
188  C CA  . ASN A 25  ? 1.2921 1.5924 1.2533 -0.2577 0.1933  -0.1194 23  ASN A CA  
189  C C   . ASN A 25  ? 1.2442 1.4354 1.1770 -0.2414 0.1697  -0.0983 23  ASN A C   
190  O O   . ASN A 25  ? 1.1588 1.3099 1.0471 -0.2444 0.1691  -0.0826 23  ASN A O   
191  C CB  . ASN A 25  ? 1.2492 1.6155 1.2072 -0.2187 0.2029  -0.1424 23  ASN A CB  
192  C CG  . ASN A 25  ? 1.2440 1.7203 1.2140 -0.2423 0.2331  -0.1567 23  ASN A CG  
193  O OD1 . ASN A 25  ? 1.2242 1.7336 1.2101 -0.2907 0.2455  -0.1493 23  ASN A OD1 
194  N ND2 . ASN A 25  ? 1.2289 1.7617 1.1894 -0.2095 0.2452  -0.1775 23  ASN A ND2 
195  N N   . LEU A 26  ? 1.0551 1.2036 1.0122 -0.2247 0.1505  -0.0979 24  LEU A N   
196  C CA  . LEU A 26  ? 0.8777 0.9323 0.8174 -0.2135 0.1292  -0.0772 24  LEU A CA  
197  C C   . LEU A 26  ? 0.7739 0.7823 0.7290 -0.2371 0.1228  -0.0673 24  LEU A C   
198  O O   . LEU A 26  ? 0.6994 0.6931 0.6805 -0.2168 0.1107  -0.0747 24  LEU A O   
199  C CB  . LEU A 26  ? 0.7556 0.7970 0.7049 -0.1657 0.1109  -0.0853 24  LEU A CB  
200  C CG  . LEU A 26  ? 0.8374 0.8974 0.7609 -0.1395 0.1115  -0.0934 24  LEU A CG  
201  C CD1 . LEU A 26  ? 0.7733 0.8078 0.7034 -0.0980 0.0894  -0.0980 24  LEU A CD1 
202  C CD2 . LEU A 26  ? 0.8215 0.8412 0.6962 -0.1584 0.1141  -0.0738 24  LEU A CD2 
203  N N   . PRO A 27  ? 0.7566 0.8558 0.5864 -0.1589 0.0605  -0.0792 25  PRO A N   
204  C CA  . PRO A 27  ? 0.7258 0.7829 0.5623 -0.1710 0.0447  -0.0622 25  PRO A CA  
205  C C   . PRO A 27  ? 0.7263 0.7280 0.5777 -0.1507 0.0308  -0.0559 25  PRO A C   
206  O O   . PRO A 27  ? 0.7555 0.7338 0.6256 -0.1431 0.0236  -0.0521 25  PRO A O   
207  C CB  . PRO A 27  ? 0.7163 0.7654 0.5185 -0.2137 0.0343  -0.0448 25  PRO A CB  
208  C CG  . PRO A 27  ? 0.7922 0.8753 0.5699 -0.2226 0.0452  -0.0520 25  PRO A CG  
209  C CD  . PRO A 27  ? 0.7757 0.9100 0.5744 -0.1911 0.0661  -0.0768 25  PRO A CD  
210  N N   . ALA A 28  ? 0.7226 0.7044 0.5651 -0.1430 0.0263  -0.0548 26  ALA A N   
211  C CA  . ALA A 28  ? 0.6674 0.6046 0.5256 -0.1268 0.0125  -0.0474 26  ALA A CA  
212  C C   . ALA A 28  ? 0.6676 0.6112 0.5566 -0.0965 0.0196  -0.0591 26  ALA A C   
213  O O   . ALA A 28  ? 0.6774 0.5956 0.5865 -0.0859 0.0107  -0.0540 26  ALA A O   
214  C CB  . ALA A 28  ? 0.5979 0.5177 0.4386 -0.1271 0.0064  -0.0438 26  ALA A CB  
215  N N   . ASP A 29  ? 0.6445 0.6226 0.5365 -0.0822 0.0346  -0.0754 27  ASP A N   
216  C CA  . ASP A 29  ? 0.6250 0.6087 0.5420 -0.0571 0.0396  -0.0854 27  ASP A CA  
217  C C   . ASP A 29  ? 0.6359 0.6251 0.5700 -0.0607 0.0407  -0.0838 27  ASP A C   
218  O O   . ASP A 29  ? 0.6550 0.6311 0.6095 -0.0465 0.0383  -0.0846 27  ASP A O   
219  C CB  . ASP A 29  ? 0.6127 0.6301 0.5272 -0.0409 0.0520  -0.1033 27  ASP A CB  
220  C CG  . ASP A 29  ? 0.5916 0.6118 0.5284 -0.0183 0.0541  -0.1117 27  ASP A CG  
221  O OD1 . ASP A 29  ? 0.6341 0.6887 0.5784 -0.0108 0.0633  -0.1233 27  ASP A OD1 
222  O OD2 . ASP A 29  ? 0.5717 0.5628 0.5176 -0.0089 0.0460  -0.1066 27  ASP A OD2 
223  N N   . LEU A 30  ? 0.6503 0.6613 0.5739 -0.0817 0.0445  -0.0819 28  LEU A N   
224  C CA  . LEU A 30  ? 0.6266 0.6384 0.5605 -0.0889 0.0434  -0.0795 28  LEU A CA  
225  C C   . LEU A 30  ? 0.6327 0.5958 0.5702 -0.0916 0.0274  -0.0678 28  LEU A C   
226  O O   . LEU A 30  ? 0.6380 0.5897 0.5926 -0.0804 0.0259  -0.0708 28  LEU A O   
227  C CB  . LEU A 30  ? 0.6432 0.6871 0.5599 -0.1170 0.0477  -0.0768 28  LEU A CB  
228  C CG  . LEU A 30  ? 0.6733 0.7769 0.5986 -0.1089 0.0645  -0.0922 28  LEU A CG  
229  C CD1 . LEU A 30  ? 0.7735 0.8807 0.7232 -0.0915 0.0671  -0.0990 28  LEU A CD1 
230  C CD2 . LEU A 30  ? 0.7886 0.9098 0.7124 -0.0881 0.0726  -0.1049 28  LEU A CD2 
231  N N   . ALA A 31  ? 0.6144 0.5487 0.5357 -0.1049 0.0145  -0.0555 29  ALA A N   
232  C CA  . ALA A 31  ? 0.6326 0.5208 0.5594 -0.1028 -0.0033 -0.0459 29  ALA A CA  
233  C C   . ALA A 31  ? 0.6580 0.5398 0.6129 -0.0735 -0.0020 -0.0524 29  ALA A C   
234  O O   . ALA A 31  ? 0.6706 0.5339 0.6415 -0.0625 -0.0084 -0.0538 29  ALA A O   
235  C CB  . ALA A 31  ? 0.6250 0.4850 0.5296 -0.1210 -0.0194 -0.0310 29  ALA A CB  
236  N N   . TRP A 32  ? 0.6410 0.5388 0.5998 -0.0617 0.0054  -0.0570 30  TRP A N   
237  C CA  . TRP A 32  ? 0.5986 0.4954 0.5803 -0.0393 0.0066  -0.0617 30  TRP A CA  
238  C C   . TRP A 32  ? 0.5974 0.5119 0.5958 -0.0272 0.0171  -0.0730 30  TRP A C   
239  O O   . TRP A 32  ? 0.6130 0.5211 0.6305 -0.0148 0.0151  -0.0753 30  TRP A O   
240  C CB  . TRP A 32  ? 0.5962 0.5008 0.5696 -0.0342 0.0097  -0.0633 30  TRP A CB  
241  C CG  . TRP A 32  ? 0.5770 0.4871 0.5656 -0.0164 0.0124  -0.0686 30  TRP A CG  
242  C CD1 . TRP A 32  ? 0.5535 0.4812 0.5435 -0.0057 0.0220  -0.0795 30  TRP A CD1 
243  C CD2 . TRP A 32  ? 0.5285 0.4272 0.5294 -0.0102 0.0033  -0.0618 30  TRP A CD2 
244  N NE1 . TRP A 32  ? 0.4823 0.4055 0.4813 0.0041  0.0184  -0.0788 30  TRP A NE1 
245  C CE2 . TRP A 32  ? 0.5285 0.4380 0.5351 0.0006  0.0082  -0.0681 30  TRP A CE2 
246  C CE3 . TRP A 32  ? 0.5591 0.4416 0.5671 -0.0134 -0.0100 -0.0506 30  TRP A CE3 
247  C CZ2 . TRP A 32  ? 0.5206 0.4285 0.5381 0.0045  0.0015  -0.0625 30  TRP A CZ2 
248  C CZ3 . TRP A 32  ? 0.5086 0.3944 0.5324 -0.0060 -0.0157 -0.0466 30  TRP A CZ3 
249  C CH2 . TRP A 32  ? 0.4883 0.3884 0.5159 0.0010  -0.0092 -0.0522 30  TRP A CH2 
250  N N   . PHE A 33  ? 0.5985 0.5384 0.5898 -0.0313 0.0281  -0.0804 31  PHE A N   
251  C CA  . PHE A 33  ? 0.5855 0.5411 0.5905 -0.0227 0.0361  -0.0896 31  PHE A CA  
252  C C   . PHE A 33  ? 0.6161 0.5530 0.6261 -0.0277 0.0302  -0.0875 31  PHE A C   
253  O O   . PHE A 33  ? 0.5847 0.5184 0.6101 -0.0154 0.0317  -0.0932 31  PHE A O   
254  C CB  . PHE A 33  ? 0.5193 0.5092 0.5173 -0.0270 0.0466  -0.0971 31  PHE A CB  
255  C CG  . PHE A 33  ? 0.5562 0.5621 0.5674 -0.0196 0.0527  -0.1052 31  PHE A CG  
256  C CD1 . PHE A 33  ? 0.4686 0.4822 0.4899 -0.0018 0.0560  -0.1126 31  PHE A CD1 
257  C CD2 . PHE A 33  ? 0.5387 0.5463 0.5487 -0.0327 0.0524  -0.1041 31  PHE A CD2 
258  C CE1 . PHE A 33  ? 0.4890 0.5156 0.5202 0.0032  0.0599  -0.1189 31  PHE A CE1 
259  C CE2 . PHE A 33  ? 0.5498 0.5704 0.5701 -0.0273 0.0570  -0.1110 31  PHE A CE2 
260  C CZ  . PHE A 33  ? 0.4566 0.4879 0.4882 -0.0090 0.0612  -0.1184 31  PHE A CZ  
261  N N   . LYS A 34  ? 0.5991 0.5222 0.5926 -0.0472 0.0227  -0.0800 32  LYS A N   
262  C CA  . LYS A 34  ? 0.6407 0.5354 0.6328 -0.0518 0.0129  -0.0784 32  LYS A CA  
263  C C   . LYS A 34  ? 0.6782 0.5447 0.6857 -0.0338 0.0030  -0.0787 32  LYS A C   
264  O O   . LYS A 34  ? 0.6605 0.5179 0.6795 -0.0218 0.0025  -0.0866 32  LYS A O   
265  C CB  . LYS A 34  ? 0.6665 0.5437 0.6319 -0.0796 0.0016  -0.0672 32  LYS A CB  
266  C CG  . LYS A 34  ? 0.7568 0.5937 0.7129 -0.0864 -0.0133 -0.0650 32  LYS A CG  
267  C CD  . LYS A 34  ? 0.8544 0.6825 0.7787 -0.1213 -0.0227 -0.0537 32  LYS A CD  
268  C CE  . LYS A 34  ? 0.9703 0.7358 0.8751 -0.1302 -0.0481 -0.0463 32  LYS A CE  
269  N NZ  . LYS A 34  ? 1.0057 0.7530 0.8722 -0.1701 -0.0635 -0.0297 32  LYS A NZ  
270  N N   . ARG A 35  ? 0.6973 0.5536 0.7059 -0.0313 -0.0048 -0.0710 33  ARG A N   
271  C CA  . ARG A 35  ? 0.6693 0.5062 0.6958 -0.0141 -0.0157 -0.0709 33  ARG A CA  
272  C C   . ARG A 35  ? 0.6602 0.5211 0.7119 0.0067  -0.0041 -0.0825 33  ARG A C   
273  O O   . ARG A 35  ? 0.6595 0.5122 0.7267 0.0215  -0.0082 -0.0896 33  ARG A O   
274  C CB  . ARG A 35  ? 0.6717 0.5010 0.6956 -0.0169 -0.0254 -0.0595 33  ARG A CB  
275  C CG  . ARG A 35  ? 0.7901 0.6123 0.8386 0.0025  -0.0358 -0.0592 33  ARG A CG  
276  C CD  . ARG A 35  ? 0.9043 0.7212 0.9495 -0.0028 -0.0466 -0.0462 33  ARG A CD  
277  N NE  . ARG A 35  ? 0.9453 0.7914 1.0023 0.0038  -0.0367 -0.0473 33  ARG A NE  
278  C CZ  . ARG A 35  ? 0.9775 0.8419 1.0617 0.0198  -0.0369 -0.0503 33  ARG A CZ  
279  N NH1 . ARG A 35  ? 0.9860 0.8469 1.0926 0.0358  -0.0448 -0.0554 33  ARG A NH1 
280  N NH2 . ARG A 35  ? 0.7608 0.6478 0.8484 0.0195  -0.0303 -0.0488 33  ARG A NH2 
281  N N   . ASN A 36  ? 0.6305 0.5206 0.6845 0.0077  0.0095  -0.0856 34  ASN A N   
282  C CA  . ASN A 36  ? 0.6030 0.5150 0.6760 0.0222  0.0181  -0.0935 34  ASN A CA  
283  C C   . ASN A 36  ? 0.6103 0.5345 0.6848 0.0243  0.0285  -0.1042 34  ASN A C   
284  O O   . ASN A 36  ? 0.6095 0.5517 0.6965 0.0333  0.0353  -0.1105 34  ASN A O   
285  C CB  . ASN A 36  ? 0.5371 0.4653 0.6075 0.0218  0.0220  -0.0898 34  ASN A CB  
286  C CG  . ASN A 36  ? 0.5833 0.5022 0.6554 0.0210  0.0113  -0.0796 34  ASN A CG  
287  O OD1 . ASN A 36  ? 0.6266 0.5363 0.6814 0.0112  0.0072  -0.0724 34  ASN A OD1 
288  N ND2 . ASN A 36  ? 0.5671 0.4916 0.6601 0.0309  0.0066  -0.0794 34  ASN A ND2 
289  N N   . THR A 37  ? 0.5916 0.5082 0.6520 0.0136  0.0292  -0.1055 35  THR A N   
290  C CA  . THR A 37  ? 0.5577 0.4839 0.6187 0.0140  0.0370  -0.1148 35  THR A CA  
291  C C   . THR A 37  ? 0.6246 0.5236 0.6783 0.0107  0.0295  -0.1182 35  THR A C   
292  O O   . THR A 37  ? 0.6784 0.5803 0.7290 0.0091  0.0342  -0.1259 35  THR A O   
293  C CB  . THR A 37  ? 0.6062 0.5540 0.6570 0.0039  0.0444  -0.1146 35  THR A CB  
294  O OG1 . THR A 37  ? 0.5901 0.5307 0.6248 -0.0127 0.0394  -0.1076 35  THR A OG1 
295  C CG2 . THR A 37  ? 0.4989 0.4657 0.5525 0.0103  0.0488  -0.1135 35  THR A CG2 
296  N N   . LEU A 38  ? 0.6534 0.5216 0.7013 0.0090  0.0155  -0.1125 36  LEU A N   
297  C CA  . LEU A 38  ? 0.7123 0.5448 0.7469 0.0050  0.0040  -0.1154 36  LEU A CA  
298  C C   . LEU A 38  ? 0.7053 0.5366 0.7522 0.0238  0.0080  -0.1312 36  LEU A C   
299  O O   . LEU A 38  ? 0.6360 0.4833 0.7047 0.0428  0.0122  -0.1375 36  LEU A O   
300  C CB  . LEU A 38  ? 0.7833 0.5771 0.8095 0.0031  -0.0160 -0.1064 36  LEU A CB  
301  C CG  . LEU A 38  ? 0.8441 0.5941 0.8402 -0.0164 -0.0332 -0.1005 36  LEU A CG  
302  C CD1 . LEU A 38  ? 0.8398 0.6091 0.8153 -0.0464 -0.0269 -0.0910 36  LEU A CD1 
303  C CD2 . LEU A 38  ? 0.8774 0.5856 0.8655 -0.0161 -0.0563 -0.0907 36  LEU A CD2 
304  N N   . ASN A 39  ? 0.7476 0.5634 0.7791 0.0166  0.0071  -0.1377 37  ASN A N   
305  C CA  . ASN A 39  ? 0.7178 0.5290 0.7549 0.0330  0.0107  -0.1548 37  ASN A CA  
306  C C   . ASN A 39  ? 0.6941 0.5516 0.7524 0.0440  0.0291  -0.1624 37  ASN A C   
307  O O   . ASN A 39  ? 0.7340 0.5992 0.8040 0.0613  0.0339  -0.1766 37  ASN A O   
308  C CB  . ASN A 39  ? 0.8143 0.5908 0.8562 0.0535  -0.0044 -0.1627 37  ASN A CB  
309  C CG  . ASN A 39  ? 0.8875 0.6088 0.9032 0.0408  -0.0277 -0.1533 37  ASN A CG  
310  O OD1 . ASN A 39  ? 0.9744 0.6725 0.9937 0.0489  -0.0433 -0.1477 37  ASN A OD1 
311  N ND2 . ASN A 39  ? 0.9082 0.6063 0.8951 0.0191  -0.0327 -0.1507 37  ASN A ND2 
312  N N   . LYS A 40  ? 0.6407 0.5288 0.7020 0.0337  0.0384  -0.1535 38  LYS A N   
313  C CA  . LYS A 40  ? 0.5815 0.5061 0.6547 0.0383  0.0519  -0.1579 38  LYS A CA  
314  C C   . LYS A 40  ? 0.6162 0.5537 0.6776 0.0242  0.0577  -0.1565 38  LYS A C   
315  O O   . LYS A 40  ? 0.5876 0.5213 0.6382 0.0108  0.0539  -0.1484 38  LYS A O   
316  C CB  . LYS A 40  ? 0.5310 0.4761 0.6169 0.0415  0.0536  -0.1489 38  LYS A CB  
317  C CG  . LYS A 40  ? 0.5814 0.5221 0.6831 0.0554  0.0475  -0.1496 38  LYS A CG  
318  C CD  . LYS A 40  ? 0.5211 0.4823 0.6332 0.0558  0.0483  -0.1401 38  LYS A CD  
319  C CE  . LYS A 40  ? 0.5487 0.4951 0.6690 0.0618  0.0362  -0.1332 38  LYS A CE  
320  N NZ  . LYS A 40  ? 0.5280 0.4921 0.6552 0.0595  0.0354  -0.1230 38  LYS A NZ  
321  N N   . PRO A 41  ? 0.5608 0.5159 0.6233 0.0255  0.0660  -0.1643 39  PRO A N   
322  C CA  . PRO A 41  ? 0.5459 0.5160 0.5998 0.0135  0.0692  -0.1619 39  PRO A CA  
323  C C   . PRO A 41  ? 0.5324 0.5230 0.5915 0.0126  0.0699  -0.1526 39  PRO A C   
324  O O   . PRO A 41  ? 0.5373 0.5347 0.6049 0.0204  0.0706  -0.1498 39  PRO A O   
325  C CB  . PRO A 41  ? 0.4989 0.4808 0.5521 0.0159  0.0762  -0.1718 39  PRO A CB  
326  C CG  . PRO A 41  ? 0.5235 0.5120 0.5898 0.0291  0.0796  -0.1769 39  PRO A CG  
327  C CD  . PRO A 41  ? 0.5676 0.5310 0.6377 0.0369  0.0720  -0.1767 39  PRO A CD  
328  N N   . VAL A 42  ? 0.5180 0.5194 0.5711 0.0035  0.0688  -0.1485 40  VAL A N   
329  C CA  . VAL A 42  ? 0.4904 0.5107 0.5467 0.0062  0.0686  -0.1432 40  VAL A CA  
330  C C   . VAL A 42  ? 0.4773 0.5176 0.5326 0.0053  0.0690  -0.1455 40  VAL A C   
331  O O   . VAL A 42  ? 0.4681 0.5130 0.5190 -0.0037 0.0693  -0.1481 40  VAL A O   
332  C CB  . VAL A 42  ? 0.5039 0.5276 0.5561 -0.0013 0.0664  -0.1377 40  VAL A CB  
333  C CG1 . VAL A 42  ? 0.4718 0.4733 0.5235 0.0003  0.0627  -0.1330 40  VAL A CG1 
334  C CG2 . VAL A 42  ? 0.4504 0.4771 0.4940 -0.0174 0.0652  -0.1375 40  VAL A CG2 
335  N N   . ILE A 43  ? 0.3872 0.4355 0.4445 0.0140  0.0665  -0.1442 41  ILE A N   
336  C CA  . ILE A 43  ? 0.4330 0.4962 0.4887 0.0163  0.0624  -0.1456 41  ILE A CA  
337  C C   . ILE A 43  ? 0.4638 0.5414 0.5220 0.0256  0.0586  -0.1454 41  ILE A C   
338  O O   . ILE A 43  ? 0.4180 0.4861 0.4742 0.0331  0.0569  -0.1436 41  ILE A O   
339  C CB  . ILE A 43  ? 0.4479 0.5023 0.4983 0.0185  0.0584  -0.1446 41  ILE A CB  
340  C CG1 . ILE A 43  ? 0.4044 0.4529 0.4524 0.0103  0.0643  -0.1479 41  ILE A CG1 
341  C CG2 . ILE A 43  ? 0.4579 0.5205 0.5037 0.0215  0.0493  -0.1445 41  ILE A CG2 
342  C CD1 . ILE A 43  ? 0.3662 0.4126 0.4076 0.0081  0.0617  -0.1458 41  ILE A CD1 
343  N N   . MET A 44  ? 0.4501 0.5529 0.5124 0.0259  0.0570  -0.1483 42  MET A N   
344  C CA  . MET A 44  ? 0.4377 0.5633 0.5045 0.0377  0.0547  -0.1519 42  MET A CA  
345  C C   . MET A 44  ? 0.4652 0.6122 0.5374 0.0457  0.0468  -0.1560 42  MET A C   
346  O O   . MET A 44  ? 0.4459 0.5932 0.5176 0.0365  0.0449  -0.1543 42  MET A O   
347  C CB  . MET A 44  ? 0.3958 0.5437 0.4660 0.0275  0.0625  -0.1516 42  MET A CB  
348  C CG  . MET A 44  ? 0.4171 0.5963 0.4929 0.0143  0.0642  -0.1519 42  MET A CG  
349  S SD  . MET A 44  ? 0.4347 0.6261 0.5050 -0.0101 0.0708  -0.1464 42  MET A SD  
350  C CE  . MET A 44  ? 0.4173 0.5533 0.4751 -0.0207 0.0694  -0.1411 42  MET A CE  
351  N N   . GLY A 45  ? 0.4607 0.6231 0.5366 0.0647  0.0407  -0.1623 43  GLY A N   
352  C CA  . GLY A 45  ? 0.4513 0.6359 0.5349 0.0764  0.0305  -0.1673 43  GLY A CA  
353  C C   . GLY A 45  ? 0.4480 0.6856 0.5479 0.0706  0.0372  -0.1709 43  GLY A C   
354  O O   . GLY A 45  ? 0.4421 0.6975 0.5439 0.0570  0.0490  -0.1695 43  GLY A O   
355  N N   . ARG A 46  ? 0.4757 0.7406 0.5867 0.0793  0.0278  -0.1746 44  ARG A N   
356  C CA  . ARG A 46  ? 0.4796 0.8038 0.6083 0.0714  0.0332  -0.1771 44  ARG A CA  
357  C C   . ARG A 46  ? 0.4985 0.8659 0.6371 0.0804  0.0426  -0.1859 44  ARG A C   
358  O O   . ARG A 46  ? 0.4460 0.8534 0.5904 0.0604  0.0534  -0.1835 44  ARG A O   
359  C CB  . ARG A 46  ? 0.5085 0.8587 0.6506 0.0837  0.0191  -0.1805 44  ARG A CB  
360  C CG  . ARG A 46  ? 0.4926 0.9064 0.6530 0.0690  0.0238  -0.1800 44  ARG A CG  
361  C CD  . ARG A 46  ? 0.5072 0.9408 0.6801 0.0794  0.0073  -0.1812 44  ARG A CD  
362  N NE  . ARG A 46  ? 0.5347 0.9376 0.7044 0.1112  -0.0097 -0.1878 44  ARG A NE  
363  C CZ  . ARG A 46  ? 0.5989 1.0341 0.7856 0.1444  -0.0190 -0.2013 44  ARG A CZ  
364  N NH1 . ARG A 46  ? 0.5687 1.0789 0.7808 0.1505  -0.0101 -0.2107 44  ARG A NH1 
365  N NH2 . ARG A 46  ? 0.6600 1.0528 0.8365 0.1714  -0.0386 -0.2060 44  ARG A NH2 
366  N N   . HIS A 47  ? 0.4571 0.8180 0.5948 0.1088  0.0376  -0.1964 45  HIS A N   
367  C CA  . HIS A 47  ? 0.4809 0.8857 0.6256 0.1185  0.0475  -0.2074 45  HIS A CA  
368  C C   . HIS A 47  ? 0.4953 0.8849 0.6256 0.0945  0.0616  -0.1995 45  HIS A C   
369  O O   . HIS A 47  ? 0.4392 0.8759 0.5740 0.0823  0.0733  -0.2017 45  HIS A O   
370  C CB  . HIS A 47  ? 0.4866 0.8772 0.6279 0.1560  0.0368  -0.2221 45  HIS A CB  
371  C CG  . HIS A 47  ? 0.5508 0.9582 0.7063 0.1831  0.0194  -0.2312 45  HIS A CG  
372  N ND1 . HIS A 47  ? 0.6033 0.9612 0.7457 0.2105  -0.0012 -0.2364 45  HIS A ND1 
373  C CD2 . HIS A 47  ? 0.5564 1.0216 0.7357 0.1855  0.0165  -0.2344 45  HIS A CD2 
374  C CE1 . HIS A 47  ? 0.5404 0.9221 0.6981 0.2305  -0.0168 -0.2431 45  HIS A CE1 
375  N NE2 . HIS A 47  ? 0.5838 1.0331 0.7658 0.2164  -0.0058 -0.2421 45  HIS A NE2 
376  N N   . THR A 48  ? 0.4883 0.8154 0.6010 0.0858  0.0597  -0.1897 46  THR A N   
377  C CA  . THR A 48  ? 0.4604 0.7718 0.5608 0.0640  0.0699  -0.1817 46  THR A CA  
378  C C   . THR A 48  ? 0.4662 0.7986 0.5685 0.0329  0.0762  -0.1723 46  THR A C   
379  O O   . THR A 48  ? 0.4198 0.7738 0.5169 0.0143  0.0841  -0.1691 46  THR A O   
380  C CB  . THR A 48  ? 0.4921 0.7386 0.5775 0.0631  0.0654  -0.1739 46  THR A CB  
381  O OG1 . THR A 48  ? 0.4996 0.7255 0.5777 0.0871  0.0583  -0.1810 46  THR A OG1 
382  C CG2 . THR A 48  ? 0.4239 0.6531 0.4989 0.0412  0.0729  -0.1647 46  THR A CG2 
383  N N   . TRP A 49  ? 0.4779 0.8024 0.5837 0.0248  0.0710  -0.1676 47  TRP A N   
384  C CA  . TRP A 49  ? 0.4592 0.8010 0.5633 -0.0050 0.0739  -0.1594 47  TRP A CA  
385  C C   . TRP A 49  ? 0.4456 0.8594 0.5612 -0.0136 0.0797  -0.1628 47  TRP A C   
386  O O   . TRP A 49  ? 0.4746 0.9029 0.5807 -0.0420 0.0846  -0.1552 47  TRP A O   
387  C CB  . TRP A 49  ? 0.4492 0.7779 0.5551 -0.0091 0.0665  -0.1565 47  TRP A CB  
388  C CG  . TRP A 49  ? 0.3911 0.7451 0.4951 -0.0381 0.0668  -0.1498 47  TRP A CG  
389  C CD1 . TRP A 49  ? 0.3852 0.7892 0.5032 -0.0425 0.0632  -0.1508 47  TRP A CD1 
390  C CD2 . TRP A 49  ? 0.4598 0.7878 0.5447 -0.0679 0.0682  -0.1404 47  TRP A CD2 
391  N NE1 . TRP A 49  ? 0.4148 0.8272 0.5223 -0.0763 0.0630  -0.1416 47  TRP A NE1 
392  C CE2 . TRP A 49  ? 0.4470 0.8092 0.5320 -0.0921 0.0651  -0.1353 47  TRP A CE2 
393  C CE3 . TRP A 49  ? 0.5011 0.7786 0.5679 -0.0760 0.0693  -0.1355 47  TRP A CE3 
394  C CZ2 . TRP A 49  ? 0.4624 0.8035 0.5254 -0.1258 0.0619  -0.1252 47  TRP A CZ2 
395  C CZ3 . TRP A 49  ? 0.4785 0.7346 0.5256 -0.1060 0.0655  -0.1266 47  TRP A CZ3 
396  C CH2 . TRP A 49  ? 0.5066 0.7915 0.5497 -0.1313 0.0614  -0.1215 47  TRP A CH2 
397  N N   . GLU A 50  ? 0.4361 0.8976 0.5715 0.0105  0.0780  -0.1746 48  GLU A N   
398  C CA  . GLU A 50  ? 0.4063 0.9498 0.5576 0.0036  0.0843  -0.1798 48  GLU A CA  
399  C C   . GLU A 50  ? 0.3933 0.9611 0.5365 -0.0041 0.0959  -0.1825 48  GLU A C   
400  O O   . GLU A 50  ? 0.4678 1.1030 0.6171 -0.0234 0.1035  -0.1825 48  GLU A O   
401  C CB  . GLU A 50  ? 0.3768 0.9671 0.5538 0.0378  0.0783  -0.1948 48  GLU A CB  
402  C CG  . GLU A 50  ? 0.4453 1.0311 0.6322 0.0385  0.0658  -0.1905 48  GLU A CG  
403  C CD  . GLU A 50  ? 0.5209 1.1301 0.7290 0.0783  0.0535  -0.2046 48  GLU A CD  
404  O OE1 . GLU A 50  ? 0.5426 1.1579 0.7536 0.1086  0.0526  -0.2182 48  GLU A OE1 
405  O OE2 . GLU A 50  ? 0.5557 1.1677 0.7726 0.0782  0.0416  -0.2008 48  GLU A OE2 
406  N N   . SER A 51  ? 0.4608 0.9787 0.5886 0.0071  0.0970  -0.1838 49  SER A N   
407  C CA  . SER A 51  ? 0.4550 0.9961 0.5722 -0.0014 0.1072  -0.1865 49  SER A CA  
408  C C   . SER A 51  ? 0.5056 1.0212 0.6000 -0.0426 0.1090  -0.1688 49  SER A C   
409  O O   . SER A 51  ? 0.5876 1.1196 0.6687 -0.0566 0.1159  -0.1677 49  SER A O   
410  C CB  . SER A 51  ? 0.4647 0.9660 0.5731 0.0280  0.1059  -0.1960 49  SER A CB  
411  O OG  . SER A 51  ? 0.5529 0.9752 0.6453 0.0230  0.0991  -0.1843 49  SER A OG  
412  N N   . ILE A 52  ? 0.5090 0.9811 0.5955 -0.0620 0.1015  -0.1555 50  ILE A N   
413  C CA  . ILE A 52  ? 0.4987 0.9387 0.5611 -0.0990 0.0986  -0.1395 50  ILE A CA  
414  C C   . ILE A 52  ? 0.5073 0.9663 0.5668 -0.1300 0.0939  -0.1298 50  ILE A C   
415  O O   . ILE A 52  ? 0.4889 0.9603 0.5301 -0.1667 0.0926  -0.1184 50  ILE A O   
416  C CB  . ILE A 52  ? 0.5522 0.9064 0.6004 -0.0929 0.0912  -0.1332 50  ILE A CB  
417  C CG1 . ILE A 52  ? 0.5349 0.8581 0.5944 -0.0720 0.0860  -0.1373 50  ILE A CG1 
418  C CG2 . ILE A 52  ? 0.5371 0.8728 0.5813 -0.0737 0.0943  -0.1383 50  ILE A CG2 
419  C CD1 . ILE A 52  ? 0.4753 0.7259 0.5220 -0.0723 0.0795  -0.1310 50  ILE A CD1 
420  N N   . GLY A 53  ? 0.5369 0.9949 0.6104 -0.1187 0.0893  -0.1329 51  GLY A N   
421  C CA  . GLY A 53  ? 0.4692 0.9522 0.5419 -0.1458 0.0841  -0.1253 51  GLY A CA  
422  C C   . GLY A 53  ? 0.5831 1.0049 0.6259 -0.1785 0.0739  -0.1108 51  GLY A C   
423  O O   . GLY A 53  ? 0.5967 1.0306 0.6335 -0.2033 0.0674  -0.1039 51  GLY A O   
424  N N   . ARG A 54  ? 0.6514 1.0073 0.6746 -0.1786 0.0705  -0.1066 52  ARG A N   
425  C CA  . ARG A 54  ? 0.6059 0.8900 0.5997 -0.1998 0.0584  -0.0962 52  ARG A CA  
426  C C   . ARG A 54  ? 0.6058 0.8242 0.6003 -0.1707 0.0569  -0.1021 52  ARG A C   
427  O O   . ARG A 54  ? 0.5946 0.8138 0.5993 -0.1486 0.0632  -0.1071 52  ARG A O   
428  C CB  . ARG A 54  ? 0.6614 0.9438 0.6297 -0.2336 0.0538  -0.0836 52  ARG A CB  
429  C CG  . ARG A 54  ? 0.8041 1.0028 0.7386 -0.2527 0.0368  -0.0730 52  ARG A CG  
430  C CD  . ARG A 54  ? 0.9193 1.1123 0.8234 -0.2909 0.0279  -0.0578 52  ARG A CD  
431  N NE  . ARG A 54  ? 1.0795 1.3204 0.9703 -0.3325 0.0244  -0.0474 52  ARG A NE  
432  C CZ  . ARG A 54  ? 1.1099 1.4334 1.0076 -0.3516 0.0348  -0.0448 52  ARG A CZ  
433  N NH1 . ARG A 54  ? 1.1073 1.4750 1.0248 -0.3296 0.0506  -0.0541 52  ARG A NH1 
434  N NH2 . ARG A 54  ? 1.0040 1.3690 0.8876 -0.3938 0.0294  -0.0335 52  ARG A NH2 
435  N N   . PRO A 55  ? 0.5953 0.7597 0.5787 -0.1703 0.0487  -0.1024 53  PRO A N   
436  C CA  . PRO A 55  ? 0.5882 0.7001 0.5744 -0.1436 0.0484  -0.1090 53  PRO A CA  
437  C C   . PRO A 55  ? 0.6329 0.7141 0.6096 -0.1431 0.0451  -0.1040 53  PRO A C   
438  O O   . PRO A 55  ? 0.6598 0.7283 0.6149 -0.1696 0.0366  -0.0936 53  PRO A O   
439  C CB  . PRO A 55  ? 0.5684 0.6312 0.5368 -0.1517 0.0388  -0.1100 53  PRO A CB  
440  C CG  . PRO A 55  ? 0.6054 0.7039 0.5704 -0.1739 0.0370  -0.1066 53  PRO A CG  
441  C CD  . PRO A 55  ? 0.5814 0.7305 0.5469 -0.1953 0.0390  -0.0976 53  PRO A CD  
442  N N   . LEU A 56  ? 0.6090 0.6765 0.5994 -0.1155 0.0499  -0.1100 54  LEU A N   
443  C CA  . LEU A 56  ? 0.6242 0.6516 0.6055 -0.1131 0.0437  -0.1054 54  LEU A CA  
444  C C   . LEU A 56  ? 0.6558 0.6238 0.6197 -0.1187 0.0304  -0.1043 54  LEU A C   
445  O O   . LEU A 56  ? 0.6400 0.5926 0.6090 -0.1057 0.0314  -0.1131 54  LEU A O   
446  C CB  . LEU A 56  ? 0.5822 0.6079 0.5818 -0.0838 0.0502  -0.1116 54  LEU A CB  
447  C CG  . LEU A 56  ? 0.5494 0.6242 0.5636 -0.0724 0.0607  -0.1160 54  LEU A CG  
448  C CD1 . LEU A 56  ? 0.5142 0.5753 0.5392 -0.0478 0.0629  -0.1200 54  LEU A CD1 
449  C CD2 . LEU A 56  ? 0.5951 0.7021 0.6003 -0.0904 0.0627  -0.1106 54  LEU A CD2 
450  N N   . PRO A 57  ? 0.6950 0.6272 0.6360 -0.1376 0.0164  -0.0945 55  PRO A N   
451  C CA  . PRO A 57  ? 0.7064 0.5774 0.6256 -0.1437 -0.0003 -0.0946 55  PRO A CA  
452  C C   . PRO A 57  ? 0.7615 0.5933 0.6919 -0.1127 -0.0033 -0.1044 55  PRO A C   
453  O O   . PRO A 57  ? 0.7806 0.6209 0.7285 -0.0948 0.0017  -0.1049 55  PRO A O   
454  C CB  . PRO A 57  ? 0.7355 0.5796 0.6243 -0.1747 -0.0174 -0.0790 55  PRO A CB  
455  C CG  . PRO A 57  ? 0.7336 0.6212 0.6319 -0.1788 -0.0077 -0.0724 55  PRO A CG  
456  C CD  . PRO A 57  ? 0.6945 0.6381 0.6254 -0.1543 0.0138  -0.0833 55  PRO A CD  
457  N N   . GLY A 58  ? 0.8256 0.6151 0.7442 -0.1075 -0.0126 -0.1126 56  GLY A N   
458  C CA  . GLY A 58  ? 0.9142 0.6715 0.8438 -0.0772 -0.0157 -0.1246 56  GLY A CA  
459  C C   . GLY A 58  ? 0.9050 0.7030 0.8667 -0.0511 0.0036  -0.1351 56  GLY A C   
460  O O   . GLY A 58  ? 0.9485 0.7425 0.9275 -0.0290 0.0043  -0.1394 56  GLY A O   
461  N N   . ARG A 59  ? 0.8124 0.6503 0.7817 -0.0551 0.0174  -0.1381 57  ARG A N   
462  C CA  . ARG A 59  ? 0.7134 0.5864 0.7071 -0.0353 0.0327  -0.1461 57  ARG A CA  
463  C C   . ARG A 59  ? 0.6743 0.5691 0.6653 -0.0423 0.0401  -0.1512 57  ARG A C   
464  O O   . ARG A 59  ? 0.7686 0.6735 0.7476 -0.0631 0.0374  -0.1449 57  ARG A O   
465  C CB  . ARG A 59  ? 0.6460 0.5538 0.6556 -0.0321 0.0402  -0.1383 57  ARG A CB  
466  C CG  . ARG A 59  ? 0.6957 0.5857 0.7053 -0.0301 0.0324  -0.1307 57  ARG A CG  
467  C CD  . ARG A 59  ? 0.6068 0.5304 0.6269 -0.0286 0.0400  -0.1248 57  ARG A CD  
468  N NE  . ARG A 59  ? 0.6729 0.5816 0.6886 -0.0319 0.0322  -0.1157 57  ARG A NE  
469  C CZ  . ARG A 59  ? 0.7334 0.6351 0.7310 -0.0531 0.0249  -0.1059 57  ARG A CZ  
470  N NH1 . ARG A 59  ? 0.7132 0.6243 0.6965 -0.0736 0.0245  -0.1037 57  ARG A NH1 
471  N NH2 . ARG A 59  ? 0.8237 0.7107 0.8159 -0.0563 0.0172  -0.0973 57  ARG A NH2 
472  N N   . LYS A 60  ? 0.7055 0.6106 0.7071 -0.0268 0.0488  -0.1619 58  LYS A N   
473  C CA  . LYS A 60  ? 0.6088 0.5399 0.6099 -0.0331 0.0555  -0.1645 58  LYS A CA  
474  C C   . LYS A 60  ? 0.6077 0.5787 0.6235 -0.0329 0.0609  -0.1564 58  LYS A C   
475  O O   . LYS A 60  ? 0.5716 0.5533 0.6011 -0.0194 0.0649  -0.1555 58  LYS A O   
476  C CB  . LYS A 60  ? 0.5682 0.4994 0.5718 -0.0206 0.0624  -0.1775 58  LYS A CB  
477  C CG  . LYS A 60  ? 0.6094 0.5583 0.6053 -0.0318 0.0654  -0.1792 58  LYS A CG  
478  C CD  . LYS A 60  ? 0.6859 0.6291 0.6751 -0.0252 0.0712  -0.1933 58  LYS A CD  
479  C CE  . LYS A 60  ? 0.6894 0.6421 0.6643 -0.0407 0.0710  -0.1942 58  LYS A CE  
480  N NZ  . LYS A 60  ? 0.7484 0.7172 0.7223 -0.0367 0.0793  -0.2026 58  LYS A NZ  
481  N N   . ASN A 61  ? 0.5916 0.5842 0.6034 -0.0480 0.0593  -0.1509 59  ASN A N   
482  C CA  . ASN A 61  ? 0.4921 0.5258 0.5165 -0.0467 0.0626  -0.1460 59  ASN A CA  
483  C C   . ASN A 61  ? 0.4953 0.5481 0.5238 -0.0433 0.0643  -0.1500 59  ASN A C   
484  O O   . ASN A 61  ? 0.5251 0.5801 0.5445 -0.0563 0.0616  -0.1510 59  ASN A O   
485  C CB  . ASN A 61  ? 0.4946 0.5468 0.5128 -0.0664 0.0590  -0.1386 59  ASN A CB  
486  C CG  . ASN A 61  ? 0.5757 0.6205 0.5904 -0.0710 0.0571  -0.1321 59  ASN A CG  
487  O OD1 . ASN A 61  ? 0.7601 0.8151 0.7850 -0.0580 0.0609  -0.1317 59  ASN A OD1 
488  N ND2 . ASN A 61  ? 0.7340 0.7486 0.7301 -0.0883 0.0489  -0.1275 59  ASN A ND2 
489  N N   . ILE A 62  ? 0.4847 0.5466 0.5232 -0.0279 0.0666  -0.1513 60  ILE A N   
490  C CA  . ILE A 62  ? 0.4544 0.5305 0.4943 -0.0248 0.0646  -0.1531 60  ILE A CA  
491  C C   . ILE A 62  ? 0.4465 0.5510 0.4975 -0.0152 0.0607  -0.1502 60  ILE A C   
492  O O   . ILE A 62  ? 0.4416 0.5452 0.4978 -0.0035 0.0610  -0.1492 60  ILE A O   
493  C CB  . ILE A 62  ? 0.5230 0.5833 0.5598 -0.0175 0.0670  -0.1566 60  ILE A CB  
494  C CG1 . ILE A 62  ? 0.5225 0.5616 0.5488 -0.0235 0.0714  -0.1640 60  ILE A CG1 
495  C CG2 . ILE A 62  ? 0.4622 0.5342 0.4971 -0.0157 0.0613  -0.1550 60  ILE A CG2 
496  C CD1 . ILE A 62  ? 0.5779 0.5973 0.6072 -0.0165 0.0745  -0.1668 60  ILE A CD1 
497  N N   . ILE A 63  ? 0.5072 0.6362 0.5612 -0.0187 0.0555  -0.1500 61  ILE A N   
498  C CA  . ILE A 63  ? 0.4456 0.6057 0.5122 -0.0057 0.0500  -0.1504 61  ILE A CA  
499  C C   . ILE A 63  ? 0.4929 0.6468 0.5567 0.0034  0.0399  -0.1507 61  ILE A C   
500  O O   . ILE A 63  ? 0.4782 0.6333 0.5365 -0.0068 0.0354  -0.1497 61  ILE A O   
501  C CB  . ILE A 63  ? 0.4348 0.6356 0.5101 -0.0155 0.0494  -0.1499 61  ILE A CB  
502  C CG1 . ILE A 63  ? 0.3820 0.5798 0.4506 -0.0346 0.0562  -0.1466 61  ILE A CG1 
503  C CG2 . ILE A 63  ? 0.4319 0.6712 0.5236 0.0031  0.0461  -0.1539 61  ILE A CG2 
504  C CD1 . ILE A 63  ? 0.4167 0.6053 0.4853 -0.0286 0.0617  -0.1461 61  ILE A CD1 
505  N N   . LEU A 64  ? 0.4708 0.6138 0.5344 0.0201  0.0341  -0.1512 62  LEU A N   
506  C CA  . LEU A 64  ? 0.5013 0.6333 0.5579 0.0274  0.0196  -0.1497 62  LEU A CA  
507  C C   . LEU A 64  ? 0.5530 0.7158 0.6227 0.0422  0.0087  -0.1534 62  LEU A C   
508  O O   . LEU A 64  ? 0.5091 0.6859 0.5879 0.0601  0.0078  -0.1588 62  LEU A O   
509  C CB  . LEU A 64  ? 0.5037 0.6053 0.5494 0.0365  0.0145  -0.1476 62  LEU A CB  
510  C CG  . LEU A 64  ? 0.5235 0.6045 0.5553 0.0420  -0.0049 -0.1441 62  LEU A CG  
511  C CD1 . LEU A 64  ? 0.5645 0.6376 0.5833 0.0229  -0.0079 -0.1392 62  LEU A CD1 
512  C CD2 . LEU A 64  ? 0.5520 0.6025 0.5704 0.0470  -0.0103 -0.1407 62  LEU A CD2 
513  N N   . SER A 65  ? 0.5312 0.7076 0.6022 0.0357  0.0003  -0.1517 63  SER A N   
514  C CA  . SER A 65  ? 0.5540 0.7708 0.6433 0.0494  -0.0092 -0.1560 63  SER A CA  
515  C C   . SER A 65  ? 0.5572 0.7646 0.6405 0.0532  -0.0301 -0.1528 63  SER A C   
516  O O   . SER A 65  ? 0.5114 0.6974 0.5784 0.0337  -0.0323 -0.1462 63  SER A O   
517  C CB  . SER A 65  ? 0.5044 0.7643 0.6073 0.0334  0.0013  -0.1560 63  SER A CB  
518  O OG  . SER A 65  ? 0.5411 0.8490 0.6647 0.0463  -0.0087 -0.1601 63  SER A OG  
519  N N   . SER A 66  ? 0.5831 0.8076 0.6787 0.0788  -0.0461 -0.1584 64  SER A N   
520  C CA  . SER A 66  ? 0.6060 0.8252 0.6988 0.0855  -0.0704 -0.1555 64  SER A CA  
521  C C   . SER A 66  ? 0.6105 0.8830 0.7252 0.0806  -0.0726 -0.1559 64  SER A C   
522  O O   . SER A 66  ? 0.6606 0.9382 0.7788 0.0898  -0.0948 -0.1544 64  SER A O   
523  C CB  . SER A 66  ? 0.6157 0.8200 0.7090 0.1196  -0.0913 -0.1626 64  SER A CB  
524  O OG  . SER A 66  ? 0.6701 0.9247 0.7910 0.1437  -0.0847 -0.1759 64  SER A OG  
525  N N   . GLN A 67  ? 0.5716 0.8825 0.6993 0.0648  -0.0526 -0.1569 65  GLN A N   
526  C CA  . GLN A 67  ? 0.5282 0.8944 0.6756 0.0549  -0.0538 -0.1558 65  GLN A CA  
527  C C   . GLN A 67  ? 0.5049 0.8647 0.6385 0.0181  -0.0379 -0.1483 65  GLN A C   
528  O O   . GLN A 67  ? 0.5066 0.8304 0.6231 0.0072  -0.0236 -0.1474 65  GLN A O   
529  C CB  . GLN A 67  ? 0.5284 0.9607 0.7073 0.0745  -0.0479 -0.1663 65  GLN A CB  
530  C CG  . GLN A 67  ? 0.5734 1.0140 0.7665 0.1160  -0.0657 -0.1776 65  GLN A CG  
531  C CD  . GLN A 67  ? 0.6665 1.1765 0.8895 0.1373  -0.0559 -0.1918 65  GLN A CD  
532  O OE1 . GLN A 67  ? 0.6432 1.2055 0.8789 0.1166  -0.0385 -0.1904 65  GLN A OE1 
533  N NE2 . GLN A 67  ? 0.6118 1.1227 0.8433 0.1777  -0.0683 -0.2059 65  GLN A NE2 
534  N N   . PRO A 68  ? 0.4924 0.8836 0.6315 -0.0007 -0.0426 -0.1433 66  PRO A N   
535  C CA  . PRO A 68  ? 0.5335 0.9079 0.6527 -0.0357 -0.0314 -0.1369 66  PRO A CA  
536  C C   . PRO A 68  ? 0.5041 0.8929 0.6263 -0.0457 -0.0128 -0.1387 66  PRO A C   
537  O O   . PRO A 68  ? 0.5008 0.9363 0.6457 -0.0331 -0.0085 -0.1433 66  PRO A O   
538  C CB  . PRO A 68  ? 0.4924 0.9059 0.6198 -0.0515 -0.0437 -0.1311 66  PRO A CB  
539  C CG  . PRO A 68  ? 0.4828 0.9156 0.6287 -0.0234 -0.0645 -0.1333 66  PRO A CG  
540  C CD  . PRO A 68  ? 0.5007 0.9445 0.6639 0.0088  -0.0594 -0.1434 66  PRO A CD  
541  N N   . GLY A 69  ? 0.4747 0.8228 0.5722 -0.0686 -0.0028 -0.1358 67  GLY A N   
542  C CA  . GLY A 69  ? 0.4875 0.8368 0.5821 -0.0794 0.0109  -0.1360 67  GLY A CA  
543  C C   . GLY A 69  ? 0.4968 0.9014 0.6022 -0.1001 0.0108  -0.1312 67  GLY A C   
544  O O   . GLY A 69  ? 0.4686 0.9001 0.5770 -0.1143 0.0013  -0.1265 67  GLY A O   
545  N N   . THR A 70  ? 0.4497 0.8730 0.5592 -0.1050 0.0209  -0.1313 68  THR A N   
546  C CA  . THR A 70  ? 0.4127 0.8943 0.5302 -0.1292 0.0218  -0.1255 68  THR A CA  
547  C C   . THR A 70  ? 0.4377 0.8916 0.5299 -0.1590 0.0278  -0.1188 68  THR A C   
548  O O   . THR A 70  ? 0.4604 0.9624 0.5556 -0.1825 0.0290  -0.1126 68  THR A O   
549  C CB  . THR A 70  ? 0.3879 0.9438 0.5392 -0.1072 0.0256  -0.1324 68  THR A CB  
550  O OG1 . THR A 70  ? 0.3859 0.9170 0.5386 -0.0804 0.0336  -0.1406 68  THR A OG1 
551  C CG2 . THR A 70  ? 0.4133 1.0092 0.5898 -0.0858 0.0137  -0.1368 68  THR A CG2 
552  N N   . ASP A 71  ? 0.4485 0.8282 0.5151 -0.1596 0.0301  -0.1196 69  ASP A N   
553  C CA  . ASP A 71  ? 0.5394 0.8825 0.5804 -0.1830 0.0320  -0.1140 69  ASP A CA  
554  C C   . ASP A 71  ? 0.5242 0.7878 0.5369 -0.1844 0.0290  -0.1167 69  ASP A C   
555  O O   . ASP A 71  ? 0.5473 0.7795 0.5634 -0.1587 0.0338  -0.1244 69  ASP A O   
556  C CB  . ASP A 71  ? 0.4853 0.8345 0.5346 -0.1691 0.0413  -0.1164 69  ASP A CB  
557  C CG  . ASP A 71  ? 0.5345 0.8592 0.5586 -0.1981 0.0398  -0.1077 69  ASP A CG  
558  O OD1 . ASP A 71  ? 0.5491 0.8045 0.5461 -0.2062 0.0341  -0.1065 69  ASP A OD1 
559  O OD2 . ASP A 71  ? 0.4915 0.8639 0.5213 -0.2114 0.0434  -0.1029 69  ASP A OD2 
560  N N   . ASP A 72  ? 0.5781 0.8099 0.5615 -0.2144 0.0207  -0.1112 70  ASP A N   
561  C CA  . ASP A 72  ? 0.6373 0.7984 0.5929 -0.2140 0.0171  -0.1173 70  ASP A CA  
562  C C   . ASP A 72  ? 0.6610 0.7630 0.5982 -0.2093 0.0181  -0.1204 70  ASP A C   
563  O O   . ASP A 72  ? 0.8019 0.8449 0.7142 -0.2091 0.0141  -0.1273 70  ASP A O   
564  C CB  . ASP A 72  ? 0.6505 0.8006 0.5801 -0.2460 0.0050  -0.1121 70  ASP A CB  
565  C CG  . ASP A 72  ? 0.7440 0.9611 0.6957 -0.2518 0.0016  -0.1072 70  ASP A CG  
566  O OD1 . ASP A 72  ? 0.7575 0.9862 0.6942 -0.2823 -0.0092 -0.0994 70  ASP A OD1 
567  O OD2 . ASP A 72  ? 0.7461 1.0041 0.7300 -0.2252 0.0077  -0.1110 70  ASP A OD2 
568  N N   . ARG A 73  ? 0.6324 0.7498 0.5817 -0.2035 0.0229  -0.1168 71  ARG A N   
569  C CA  . ARG A 73  ? 0.6344 0.7014 0.5722 -0.1945 0.0230  -0.1191 71  ARG A CA  
570  C C   . ARG A 73  ? 0.6827 0.7441 0.6413 -0.1589 0.0336  -0.1286 71  ARG A C   
571  O O   . ARG A 73  ? 0.7110 0.7366 0.6650 -0.1484 0.0338  -0.1307 71  ARG A O   
572  C CB  . ARG A 73  ? 0.6326 0.7183 0.5683 -0.2116 0.0209  -0.1082 71  ARG A CB  
573  C CG  . ARG A 73  ? 0.6275 0.7201 0.5386 -0.2535 0.0088  -0.0956 71  ARG A CG  
574  C CD  . ARG A 73  ? 0.6372 0.7656 0.5498 -0.2713 0.0097  -0.0847 71  ARG A CD  
575  N NE  . ARG A 73  ? 0.6053 0.8172 0.5542 -0.2582 0.0237  -0.0870 71  ARG A NE  
576  C CZ  . ARG A 73  ? 0.5586 0.8182 0.5151 -0.2677 0.0292  -0.0816 71  ARG A CZ  
577  N NH1 . ARG A 73  ? 0.6613 0.8924 0.5899 -0.2944 0.0212  -0.0708 71  ARG A NH1 
578  N NH2 . ARG A 73  ? 0.4741 0.8088 0.4638 -0.2504 0.0415  -0.0878 71  ARG A NH2 
579  N N   . VAL A 74  ? 0.6042 0.7006 0.5846 -0.1416 0.0401  -0.1329 72  VAL A N   
580  C CA  . VAL A 74  ? 0.5854 0.6791 0.5827 -0.1124 0.0479  -0.1394 72  VAL A CA  
581  C C   . VAL A 74  ? 0.5715 0.6667 0.5709 -0.1037 0.0485  -0.1453 72  VAL A C   
582  O O   . VAL A 74  ? 0.5761 0.6847 0.5695 -0.1178 0.0434  -0.1436 72  VAL A O   
583  C CB  . VAL A 74  ? 0.4949 0.6318 0.5150 -0.0999 0.0528  -0.1366 72  VAL A CB  
584  C CG1 . VAL A 74  ? 0.4980 0.6319 0.5118 -0.1113 0.0527  -0.1304 72  VAL A CG1 
585  C CG2 . VAL A 74  ? 0.4117 0.6053 0.4485 -0.1005 0.0514  -0.1353 72  VAL A CG2 
586  N N   . THR A 75  ? 0.5533 0.6343 0.5586 -0.0835 0.0536  -0.1510 73  THR A N   
587  C CA  . THR A 75  ? 0.4959 0.5732 0.4975 -0.0789 0.0536  -0.1559 73  THR A CA  
588  C C   . THR A 75  ? 0.4953 0.6047 0.5147 -0.0657 0.0512  -0.1527 73  THR A C   
589  O O   . THR A 75  ? 0.5091 0.6219 0.5400 -0.0499 0.0538  -0.1521 73  THR A O   
590  C CB  . THR A 75  ? 0.5173 0.5621 0.5114 -0.0684 0.0598  -0.1643 73  THR A CB  
591  O OG1 . THR A 75  ? 0.5656 0.5766 0.5409 -0.0771 0.0591  -0.1704 73  THR A OG1 
592  C CG2 . THR A 75  ? 0.4797 0.5274 0.4687 -0.0664 0.0607  -0.1682 73  THR A CG2 
593  N N   . TRP A 76  ? 0.4457 0.5755 0.4655 -0.0717 0.0441  -0.1505 74  TRP A N   
594  C CA  . TRP A 76  ? 0.4493 0.6046 0.4838 -0.0573 0.0370  -0.1482 74  TRP A CA  
595  C C   . TRP A 76  ? 0.4799 0.6144 0.5031 -0.0538 0.0333  -0.1492 74  TRP A C   
596  O O   . TRP A 76  ? 0.5035 0.6219 0.5090 -0.0678 0.0338  -0.1513 74  TRP A O   
597  C CB  . TRP A 76  ? 0.4843 0.6790 0.5287 -0.0645 0.0283  -0.1445 74  TRP A CB  
598  C CG  . TRP A 76  ? 0.4850 0.7108 0.5406 -0.0714 0.0321  -0.1424 74  TRP A CG  
599  C CD1 . TRP A 76  ? 0.4527 0.6723 0.4959 -0.0947 0.0350  -0.1395 74  TRP A CD1 
600  C CD2 . TRP A 76  ? 0.4592 0.7265 0.5370 -0.0566 0.0327  -0.1433 74  TRP A CD2 
601  N NE1 . TRP A 76  ? 0.4737 0.7319 0.5297 -0.0991 0.0373  -0.1364 74  TRP A NE1 
602  C CE2 . TRP A 76  ? 0.4522 0.7437 0.5309 -0.0750 0.0376  -0.1398 74  TRP A CE2 
603  C CE3 . TRP A 76  ? 0.4560 0.7409 0.5502 -0.0299 0.0283  -0.1474 74  TRP A CE3 
604  C CZ2 . TRP A 76  ? 0.4234 0.7639 0.5206 -0.0683 0.0411  -0.1411 74  TRP A CZ2 
605  C CZ3 . TRP A 76  ? 0.3880 0.7169 0.5006 -0.0191 0.0313  -0.1509 74  TRP A CZ3 
606  C CH2 . TRP A 76  ? 0.3863 0.7468 0.5014 -0.0387 0.0392  -0.1480 74  TRP A CH2 
607  N N   . VAL A 77  ? 0.4848 0.6181 0.5144 -0.0370 0.0286  -0.1479 75  VAL A N   
608  C CA  . VAL A 77  ? 0.4786 0.5921 0.4940 -0.0374 0.0227  -0.1463 75  VAL A CA  
609  C C   . VAL A 77  ? 0.5600 0.6797 0.5813 -0.0222 0.0065  -0.1422 75  VAL A C   
610  O O   . VAL A 77  ? 0.5459 0.6840 0.5842 -0.0059 0.0032  -0.1435 75  VAL A O   
611  C CB  . VAL A 77  ? 0.5144 0.6056 0.5228 -0.0358 0.0331  -0.1489 75  VAL A CB  
612  C CG1 . VAL A 77  ? 0.5114 0.5924 0.5123 -0.0467 0.0461  -0.1557 75  VAL A CG1 
613  C CG2 . VAL A 77  ? 0.4666 0.5586 0.4884 -0.0199 0.0353  -0.1482 75  VAL A CG2 
614  N N   . LYS A 78  ? 0.5455 0.6473 0.5496 -0.0279 -0.0048 -0.1378 76  LYS A N   
615  C CA  . LYS A 78  ? 0.5200 0.6173 0.5218 -0.0166 -0.0267 -0.1329 76  LYS A CA  
616  C C   . LYS A 78  ? 0.5386 0.6057 0.5251 -0.0124 -0.0347 -0.1286 76  LYS A C   
617  O O   . LYS A 78  ? 0.6170 0.6710 0.5986 0.0002  -0.0560 -0.1250 76  LYS A O   
618  C CB  . LYS A 78  ? 0.5599 0.6570 0.5482 -0.0321 -0.0397 -0.1280 76  LYS A CB  
619  C CG  . LYS A 78  ? 0.7027 0.8310 0.7050 -0.0374 -0.0375 -0.1302 76  LYS A CG  
620  C CD  . LYS A 78  ? 0.7261 0.8476 0.7106 -0.0538 -0.0521 -0.1242 76  LYS A CD  
621  C CE  . LYS A 78  ? 0.7793 0.8786 0.7383 -0.0766 -0.0359 -0.1263 76  LYS A CE  
622  N NZ  . LYS A 78  ? 0.7626 0.8502 0.6935 -0.1017 -0.0401 -0.1234 76  LYS A NZ  
623  N N   . SER A 79  ? 0.5127 0.5681 0.4903 -0.0228 -0.0205 -0.1288 77  SER A N   
624  C CA  . SER A 79  ? 0.5083 0.5388 0.4686 -0.0253 -0.0286 -0.1225 77  SER A CA  
625  C C   . SER A 79  ? 0.5414 0.5738 0.5091 -0.0247 -0.0097 -0.1260 77  SER A C   
626  O O   . SER A 79  ? 0.4748 0.5221 0.4551 -0.0264 0.0088  -0.1330 77  SER A O   
627  C CB  . SER A 79  ? 0.5854 0.6029 0.5176 -0.0496 -0.0369 -0.1152 77  SER A CB  
628  O OG  . SER A 79  ? 0.5411 0.5724 0.4701 -0.0666 -0.0159 -0.1206 77  SER A OG  
629  N N   . VAL A 80  ? 0.5483 0.5619 0.5057 -0.0230 -0.0178 -0.1201 78  VAL A N   
630  C CA  . VAL A 80  ? 0.5245 0.5404 0.4876 -0.0243 -0.0034 -0.1211 78  VAL A CA  
631  C C   . VAL A 80  ? 0.5564 0.5885 0.5180 -0.0411 0.0142  -0.1251 78  VAL A C   
632  O O   . VAL A 80  ? 0.5457 0.5898 0.5232 -0.0363 0.0313  -0.1324 78  VAL A O   
633  C CB  . VAL A 80  ? 0.5470 0.5389 0.4924 -0.0267 -0.0187 -0.1116 78  VAL A CB  
634  C CG1 . VAL A 80  ? 0.5295 0.5310 0.4788 -0.0355 -0.0044 -0.1106 78  VAL A CG1 
635  C CG2 . VAL A 80  ? 0.5967 0.5721 0.5463 -0.0038 -0.0315 -0.1128 78  VAL A CG2 
636  N N   . ASP A 81  ? 0.5804 0.6125 0.5213 -0.0607 0.0091  -0.1213 79  ASP A N   
637  C CA  . ASP A 81  ? 0.5715 0.6234 0.5097 -0.0751 0.0270  -0.1281 79  ASP A CA  
638  C C   . ASP A 81  ? 0.5390 0.6008 0.4895 -0.0692 0.0412  -0.1405 79  ASP A C   
639  O O   . ASP A 81  ? 0.5599 0.6334 0.5193 -0.0668 0.0583  -0.1509 79  ASP A O   
640  C CB  . ASP A 81  ? 0.6273 0.6803 0.5366 -0.1008 0.0191  -0.1216 79  ASP A CB  
641  C CG  . ASP A 81  ? 0.6447 0.6897 0.5369 -0.1139 0.0069  -0.1088 79  ASP A CG  
642  O OD1 . ASP A 81  ? 0.6243 0.6734 0.5296 -0.1057 0.0123  -0.1082 79  ASP A OD1 
643  O OD2 . ASP A 81  ? 0.7285 0.7618 0.5918 -0.1350 -0.0098 -0.0982 79  ASP A OD2 
644  N N   . GLU A 82  ? 0.4963 0.5526 0.4460 -0.0671 0.0323  -0.1397 80  GLU A N   
645  C CA  . GLU A 82  ? 0.5105 0.5728 0.4690 -0.0644 0.0425  -0.1492 80  GLU A CA  
646  C C   . GLU A 82  ? 0.5392 0.6020 0.5188 -0.0486 0.0528  -0.1543 80  GLU A C   
647  O O   . GLU A 82  ? 0.4703 0.5328 0.4529 -0.0483 0.0648  -0.1639 80  GLU A O   
648  C CB  . GLU A 82  ? 0.5110 0.5736 0.4689 -0.0650 0.0290  -0.1450 80  GLU A CB  
649  C CG  . GLU A 82  ? 0.5569 0.6179 0.4918 -0.0843 0.0209  -0.1423 80  GLU A CG  
650  C CD  . GLU A 82  ? 0.6110 0.6762 0.5489 -0.0837 0.0057  -0.1377 80  GLU A CD  
651  O OE1 . GLU A 82  ? 0.6501 0.7255 0.6096 -0.0682 0.0042  -0.1382 80  GLU A OE1 
652  O OE2 . GLU A 82  ? 0.6601 0.7225 0.5793 -0.0995 -0.0046 -0.1337 80  GLU A OE2 
653  N N   . ALA A 83  ? 0.5058 0.5657 0.4968 -0.0357 0.0465  -0.1484 81  ALA A N   
654  C CA  . ALA A 83  ? 0.5071 0.5666 0.5149 -0.0235 0.0546  -0.1514 81  ALA A CA  
655  C C   . ALA A 83  ? 0.5188 0.5778 0.5297 -0.0231 0.0662  -0.1563 81  ALA A C   
656  O O   . ALA A 83  ? 0.5359 0.5916 0.5549 -0.0181 0.0747  -0.1632 81  ALA A O   
657  C CB  . ALA A 83  ? 0.4341 0.4910 0.4493 -0.0107 0.0454  -0.1451 81  ALA A CB  
658  N N   . ILE A 84  ? 0.5071 0.5701 0.5111 -0.0286 0.0649  -0.1525 82  ILE A N   
659  C CA  . ILE A 84  ? 0.4918 0.5649 0.5029 -0.0273 0.0761  -0.1578 82  ILE A CA  
660  C C   . ILE A 84  ? 0.5706 0.6503 0.5795 -0.0295 0.0882  -0.1719 82  ILE A C   
661  O O   . ILE A 84  ? 0.5448 0.6273 0.5655 -0.0194 0.0972  -0.1814 82  ILE A O   
662  C CB  . ILE A 84  ? 0.5751 0.6587 0.5763 -0.0390 0.0721  -0.1501 82  ILE A CB  
663  C CG1 . ILE A 84  ? 0.4926 0.5598 0.4892 -0.0368 0.0564  -0.1368 82  ILE A CG1 
664  C CG2 . ILE A 84  ? 0.5204 0.6266 0.5340 -0.0370 0.0848  -0.1567 82  ILE A CG2 
665  C CD1 . ILE A 84  ? 0.5869 0.6482 0.6001 -0.0220 0.0580  -0.1363 82  ILE A CD1 
666  N N   . ALA A 85  ? 0.5342 0.6149 0.5261 -0.0420 0.0869  -0.1743 83  ALA A N   
667  C CA  . ALA A 85  ? 0.5397 0.6257 0.5240 -0.0450 0.0983  -0.1895 83  ALA A CA  
668  C C   . ALA A 85  ? 0.5507 0.6165 0.5387 -0.0361 0.0995  -0.1975 83  ALA A C   
669  O O   . ALA A 85  ? 0.5239 0.5852 0.5102 -0.0298 0.1079  -0.2126 83  ALA A O   
670  C CB  . ALA A 85  ? 0.4809 0.5729 0.4413 -0.0645 0.0959  -0.1890 83  ALA A CB  
671  N N   . ALA A 86  ? 0.5030 0.5569 0.4944 -0.0358 0.0901  -0.1882 84  ALA A N   
672  C CA  . ALA A 86  ? 0.5811 0.6169 0.5725 -0.0334 0.0889  -0.1924 84  ALA A CA  
673  C C   . ALA A 86  ? 0.6011 0.6246 0.6049 -0.0192 0.0923  -0.1972 84  ALA A C   
674  O O   . ALA A 86  ? 0.5987 0.5999 0.5967 -0.0185 0.0901  -0.2025 84  ALA A O   
675  C CB  . ALA A 86  ? 0.4745 0.5125 0.4699 -0.0376 0.0790  -0.1807 84  ALA A CB  
676  N N   . CYS A 87  ? 0.5344 0.5690 0.5527 -0.0096 0.0950  -0.1942 85  CYS A N   
677  C CA  . CYS A 87  ? 0.5579 0.5816 0.5895 0.0042  0.0956  -0.1970 85  CYS A CA  
678  C C   . CYS A 87  ? 0.5651 0.5865 0.5971 0.0145  0.1025  -0.2139 85  CYS A C   
679  O O   . CYS A 87  ? 0.6489 0.6506 0.6871 0.0269  0.0993  -0.2191 85  CYS A O   
680  C CB  . CYS A 87  ? 0.5255 0.5630 0.5722 0.0098  0.0944  -0.1869 85  CYS A CB  
681  S SG  . CYS A 87  ? 0.6160 0.6519 0.6631 0.0055  0.0853  -0.1711 85  CYS A SG  
682  N N   . GLY A 88  ? 0.5991 0.6409 0.6239 0.0103  0.1108  -0.2231 86  GLY A N   
683  C CA  . GLY A 88  ? 0.5565 0.6024 0.5807 0.0220  0.1190  -0.2435 86  GLY A CA  
684  C C   . GLY A 88  ? 0.6055 0.6799 0.6520 0.0355  0.1235  -0.2442 86  GLY A C   
685  O O   . GLY A 88  ? 0.6255 0.7218 0.6839 0.0306  0.1241  -0.2331 86  GLY A O   
686  N N   . ASP A 89  ? 0.6196 0.6919 0.6697 0.0528  0.1243  -0.2555 87  ASP A N   
687  C CA  . ASP A 89  ? 0.6502 0.7522 0.7236 0.0684  0.1273  -0.2578 87  ASP A CA  
688  C C   . ASP A 89  ? 0.6229 0.7012 0.7129 0.0827  0.1167  -0.2516 87  ASP A C   
689  O O   . ASP A 89  ? 0.6953 0.7464 0.7862 0.1008  0.1092  -0.2590 87  ASP A O   
690  C CB  . ASP A 89  ? 0.6272 0.7385 0.6968 0.0830  0.1323  -0.2746 87  ASP A CB  
691  C CG  . ASP A 89  ? 0.7222 0.8817 0.8167 0.0944  0.1387  -0.2781 87  ASP A CG  
692  O OD1 . ASP A 89  ? 0.7201 0.9077 0.8314 0.0860  0.1399  -0.2665 87  ASP A OD1 
693  O OD2 . ASP A 89  ? 0.7724 0.9428 0.8695 0.1115  0.1424  -0.2930 87  ASP A OD2 
694  N N   . VAL A 90  ? 0.5990 0.6850 0.6997 0.0741  0.1150  -0.2384 88  VAL A N   
695  C CA  . VAL A 90  ? 0.5808 0.6484 0.6972 0.0847  0.1054  -0.2316 88  VAL A CA  
696  C C   . VAL A 90  ? 0.6228 0.7293 0.7604 0.0833  0.1084  -0.2232 88  VAL A C   
697  O O   . VAL A 90  ? 0.6716 0.8097 0.8053 0.0678  0.1152  -0.2172 88  VAL A O   
698  C CB  . VAL A 90  ? 0.6157 0.6451 0.7182 0.0729  0.0961  -0.2186 88  VAL A CB  
699  C CG1 . VAL A 90  ? 0.6057 0.5979 0.6869 0.0709  0.0919  -0.2274 88  VAL A CG1 
700  C CG2 . VAL A 90  ? 0.5691 0.6144 0.6642 0.0540  0.0983  -0.2036 88  VAL A CG2 
701  N N   . PRO A 91  ? 0.6092 0.7107 0.7652 0.0961  0.1001  -0.2184 89  PRO A N   
702  C CA  . PRO A 91  ? 0.5589 0.6964 0.7327 0.0922  0.1001  -0.2069 89  PRO A CA  
703  C C   . PRO A 91  ? 0.5830 0.7101 0.7436 0.0722  0.0948  -0.1855 89  PRO A C   
704  O O   . PRO A 91  ? 0.5791 0.7360 0.7425 0.0605  0.0963  -0.1762 89  PRO A O   
705  C CB  . PRO A 91  ? 0.4754 0.6029 0.6705 0.1128  0.0898  -0.2087 89  PRO A CB  
706  C CG  . PRO A 91  ? 0.5212 0.6180 0.7109 0.1309  0.0867  -0.2264 89  PRO A CG  
707  C CD  . PRO A 91  ? 0.5514 0.6169 0.7126 0.1154  0.0889  -0.2256 89  PRO A CD  
708  N N   . GLU A 92  ? 0.5922 0.6788 0.7373 0.0678  0.0876  -0.1780 90  GLU A N   
709  C CA  . GLU A 92  ? 0.5156 0.5906 0.6495 0.0548  0.0814  -0.1609 90  GLU A CA  
710  C C   . GLU A 92  ? 0.5484 0.5981 0.6629 0.0473  0.0802  -0.1595 90  GLU A C   
711  O O   . GLU A 92  ? 0.5240 0.5500 0.6344 0.0513  0.0777  -0.1642 90  GLU A O   
712  C CB  . GLU A 92  ? 0.4992 0.5600 0.6419 0.0601  0.0714  -0.1510 90  GLU A CB  
713  C CG  . GLU A 92  ? 0.4936 0.5452 0.6235 0.0485  0.0655  -0.1359 90  GLU A CG  
714  C CD  . GLU A 92  ? 0.5135 0.5531 0.6492 0.0513  0.0558  -0.1261 90  GLU A CD  
715  O OE1 . GLU A 92  ? 0.4826 0.5149 0.6314 0.0619  0.0516  -0.1296 90  GLU A OE1 
716  O OE2 . GLU A 92  ? 0.4950 0.5292 0.6198 0.0429  0.0506  -0.1151 90  GLU A OE2 
717  N N   . ILE A 93  ? 0.5176 0.5722 0.6193 0.0359  0.0799  -0.1524 91  ILE A N   
718  C CA  . ILE A 93  ? 0.4978 0.5379 0.5847 0.0300  0.0778  -0.1507 91  ILE A CA  
719  C C   . ILE A 93  ? 0.4893 0.5191 0.5713 0.0290  0.0703  -0.1399 91  ILE A C   
720  O O   . ILE A 93  ? 0.4866 0.5205 0.5664 0.0269  0.0659  -0.1326 91  ILE A O   
721  C CB  . ILE A 93  ? 0.5003 0.5527 0.5759 0.0208  0.0803  -0.1526 91  ILE A CB  
722  C CG1 . ILE A 93  ? 0.4975 0.5583 0.5732 0.0209  0.0888  -0.1656 91  ILE A CG1 
723  C CG2 . ILE A 93  ? 0.4749 0.5178 0.5390 0.0168  0.0752  -0.1487 91  ILE A CG2 
724  C CD1 . ILE A 93  ? 0.5866 0.6644 0.6503 0.0089  0.0916  -0.1666 91  ILE A CD1 
725  N N   . MET A 94  ? 0.4638 0.4813 0.5413 0.0290  0.0685  -0.1392 92  MET A N   
726  C CA  . MET A 94  ? 0.4704 0.4822 0.5426 0.0294  0.0632  -0.1321 92  MET A CA  
727  C C   . MET A 94  ? 0.4447 0.4634 0.5079 0.0282  0.0620  -0.1332 92  MET A C   
728  O O   . MET A 94  ? 0.4663 0.4903 0.5284 0.0245  0.0646  -0.1368 92  MET A O   
729  C CB  . MET A 94  ? 0.4466 0.4459 0.5198 0.0284  0.0614  -0.1298 92  MET A CB  
730  C CG  . MET A 94  ? 0.4360 0.4250 0.5192 0.0326  0.0593  -0.1298 92  MET A CG  
731  S SD  . MET A 94  ? 0.4789 0.4741 0.5705 0.0369  0.0551  -0.1224 92  MET A SD  
732  C CE  . MET A 94  ? 0.4207 0.4036 0.4987 0.0325  0.0490  -0.1135 92  MET A CE  
733  N N   . VAL A 95  ? 0.4423 0.4600 0.4981 0.0315  0.0559  -0.1300 93  VAL A N   
734  C CA  . VAL A 95  ? 0.4305 0.4536 0.4789 0.0361  0.0514  -0.1324 93  VAL A CA  
735  C C   . VAL A 95  ? 0.4962 0.5200 0.5417 0.0419  0.0503  -0.1328 93  VAL A C   
736  O O   . VAL A 95  ? 0.5196 0.5302 0.5587 0.0447  0.0459  -0.1290 93  VAL A O   
737  C CB  . VAL A 95  ? 0.4543 0.4682 0.4913 0.0377  0.0414  -0.1297 93  VAL A CB  
738  C CG1 . VAL A 95  ? 0.4257 0.4426 0.4564 0.0470  0.0336  -0.1340 93  VAL A CG1 
739  C CG2 . VAL A 95  ? 0.3978 0.4160 0.4352 0.0277  0.0439  -0.1289 93  VAL A CG2 
740  N N   . ILE A 96  ? 0.4528 0.4951 0.5014 0.0417  0.0545  -0.1374 94  ILE A N   
741  C CA  . ILE A 96  ? 0.4345 0.4850 0.4804 0.0421  0.0569  -0.1381 94  ILE A CA  
742  C C   . ILE A 96  ? 0.4595 0.5294 0.5025 0.0545  0.0546  -0.1459 94  ILE A C   
743  O O   . ILE A 96  ? 0.4472 0.5331 0.4873 0.0550  0.0585  -0.1491 94  ILE A O   
744  C CB  . ILE A 96  ? 0.4521 0.5124 0.5016 0.0280  0.0633  -0.1362 94  ILE A CB  
745  C CG1 . ILE A 96  ? 0.4302 0.5154 0.4849 0.0237  0.0659  -0.1406 94  ILE A CG1 
746  C CG2 . ILE A 96  ? 0.4397 0.4758 0.4917 0.0212  0.0629  -0.1310 94  ILE A CG2 
747  C CD1 . ILE A 96  ? 0.4200 0.5176 0.4726 0.0061  0.0697  -0.1378 94  ILE A CD1 
748  N N   . GLY A 97  ? 0.4798 0.5499 0.5224 0.0651  0.0474  -0.1500 95  GLY A N   
749  C CA  . GLY A 97  ? 0.4586 0.5419 0.4976 0.0826  0.0424  -0.1595 95  GLY A CA  
750  C C   . GLY A 97  ? 0.5105 0.6169 0.5577 0.0935  0.0373  -0.1668 95  GLY A C   
751  O O   . GLY A 97  ? 0.4666 0.5817 0.5217 0.0843  0.0383  -0.1637 95  GLY A O   
752  N N   . GLY A 98  ? 0.5306 0.6500 0.5757 0.1142  0.0319  -0.1781 96  GLY A N   
753  C CA  . GLY A 98  ? 0.5703 0.6824 0.6130 0.1339  0.0161  -0.1846 96  GLY A CA  
754  C C   . GLY A 98  ? 0.5520 0.6115 0.5708 0.1420  0.0011  -0.1822 96  GLY A C   
755  O O   . GLY A 98  ? 0.5765 0.6043 0.5856 0.1259  -0.0015 -0.1698 96  GLY A O   
756  N N   . GLY A 99  ? 0.4660 0.5895 0.4966 0.1304  -0.0544 -0.0814 97  GLY A N   
757  C CA  . GLY A 99  ? 0.5426 0.5984 0.5450 0.1407  -0.0613 -0.0845 97  GLY A CA  
758  C C   . GLY A 99  ? 0.5780 0.5835 0.5520 0.1353  -0.0748 -0.0738 97  GLY A C   
759  O O   . GLY A 99  ? 0.5858 0.5348 0.5327 0.1189  -0.0749 -0.0688 97  GLY A O   
760  N N   . ARG A 100 ? 0.5513 0.5805 0.5305 0.1455  -0.0869 -0.0687 98  ARG A N   
761  C CA  . ARG A 100 ? 0.6770 0.6588 0.6266 0.1368  -0.1009 -0.0570 98  ARG A CA  
762  C C   . ARG A 100 ? 0.6343 0.6026 0.5739 0.0982  -0.0874 -0.0468 98  ARG A C   
763  O O   . ARG A 100 ? 0.6968 0.6119 0.6042 0.0822  -0.0912 -0.0393 98  ARG A O   
764  C CB  . ARG A 100 ? 0.6269 0.6438 0.5873 0.1561  -0.1179 -0.0534 98  ARG A CB  
765  C CG  . ARG A 100 ? 0.7897 0.7651 0.7206 0.1427  -0.1330 -0.0393 98  ARG A CG  
766  C CD  . ARG A 100 ? 0.8713 0.7728 0.7633 0.1599  -0.1552 -0.0388 98  ARG A CD  
767  N NE  . ARG A 100 ? 1.0163 0.8701 0.8727 0.1385  -0.1682 -0.0239 98  ARG A NE  
768  C CZ  . ARG A 100 ? 1.1062 0.8854 0.9176 0.1194  -0.1738 -0.0175 98  ARG A CZ  
769  N NH1 . ARG A 100 ? 1.0489 0.7921 0.8461 0.1183  -0.1686 -0.0240 98  ARG A NH1 
770  N NH2 . ARG A 100 ? 1.0896 0.8314 0.8676 0.0979  -0.1852 -0.0038 98  ARG A NH2 
771  N N   . VAL A 101 ? 0.6159 0.6307 0.5790 0.0830  -0.0725 -0.0469 99  VAL A N   
772  C CA  . VAL A 101 ? 0.5855 0.5860 0.5375 0.0522  -0.0593 -0.0408 99  VAL A CA  
773  C C   . VAL A 101 ? 0.6003 0.5666 0.5425 0.0417  -0.0473 -0.0441 99  VAL A C   
774  O O   . VAL A 101 ? 0.6234 0.5558 0.5423 0.0233  -0.0431 -0.0385 99  VAL A O   
775  C CB  . VAL A 101 ? 0.5531 0.6030 0.5265 0.0406  -0.0504 -0.0409 99  VAL A CB  
776  C CG1 . VAL A 101 ? 0.5358 0.5657 0.4956 0.0159  -0.0372 -0.0385 99  VAL A CG1 
777  C CG2 . VAL A 101 ? 0.5239 0.6073 0.5016 0.0430  -0.0643 -0.0336 99  VAL A CG2 
778  N N   . TYR A 102 ? 0.5776 0.5560 0.5367 0.0519  -0.0418 -0.0530 100 TYR A N   
779  C CA  . TYR A 102 ? 0.5581 0.5066 0.5084 0.0413  -0.0335 -0.0549 100 TYR A CA  
780  C C   . TYR A 102 ? 0.6289 0.5215 0.5436 0.0365  -0.0445 -0.0487 100 TYR A C   
781  O O   . TYR A 102 ? 0.6042 0.4749 0.5035 0.0140  -0.0369 -0.0435 100 TYR A O   
782  C CB  . TYR A 102 ? 0.5447 0.5059 0.5108 0.0561  -0.0319 -0.0650 100 TYR A CB  
783  C CG  . TYR A 102 ? 0.5037 0.5144 0.4997 0.0534  -0.0203 -0.0702 100 TYR A CG  
784  C CD1 . TYR A 102 ? 0.4677 0.4905 0.4711 0.0332  -0.0088 -0.0669 100 TYR A CD1 
785  C CD2 . TYR A 102 ? 0.5152 0.5579 0.5279 0.0715  -0.0219 -0.0792 100 TYR A CD2 
786  C CE1 . TYR A 102 ? 0.4622 0.5204 0.4855 0.0287  -0.0025 -0.0705 100 TYR A CE1 
787  C CE2 . TYR A 102 ? 0.4446 0.5301 0.4790 0.0640  -0.0130 -0.0825 100 TYR A CE2 
788  C CZ  . TYR A 102 ? 0.4575 0.5468 0.4955 0.0415  -0.0049 -0.0772 100 TYR A CZ  
789  O OH  . TYR A 102 ? 0.4051 0.5275 0.4576 0.0319  0.0001  -0.0793 100 TYR A OH  
790  N N   . GLU A 103 ? 0.5748 0.4447 0.4741 0.0575  -0.0639 -0.0490 101 GLU A N   
791  C CA  . GLU A 103 ? 0.6586 0.4649 0.5157 0.0519  -0.0796 -0.0422 101 GLU A CA  
792  C C   . GLU A 103 ? 0.7503 0.5405 0.5856 0.0247  -0.0773 -0.0303 101 GLU A C   
793  O O   . GLU A 103 ? 0.7667 0.5151 0.5694 0.0025  -0.0795 -0.0229 101 GLU A O   
794  C CB  . GLU A 103 ? 0.7652 0.5488 0.6085 0.0845  -0.1042 -0.0455 101 GLU A CB  
795  C CG  . GLU A 103 ? 0.8919 0.5962 0.6832 0.0819  -0.1265 -0.0394 101 GLU A CG  
796  C CD  . GLU A 103 ? 1.1652 0.8456 0.9434 0.1226  -0.1530 -0.0457 101 GLU A CD  
797  O OE1 . GLU A 103 ? 1.3048 0.9130 1.0344 0.1240  -0.1779 -0.0397 101 GLU A OE1 
798  O OE2 . GLU A 103 ? 1.1196 0.8556 0.9349 0.1533  -0.1499 -0.0567 101 GLU A OE2 
799  N N   . GLN A 104 ? 0.6731 0.4961 0.5222 0.0235  -0.0734 -0.0278 102 GLN A N   
800  C CA  . GLN A 104 ? 0.7206 0.5247 0.5431 -0.0002 -0.0726 -0.0175 102 GLN A CA  
801  C C   . GLN A 104 ? 0.6953 0.5114 0.5194 -0.0266 -0.0488 -0.0176 102 GLN A C   
802  O O   . GLN A 104 ? 0.6734 0.4651 0.4672 -0.0498 -0.0458 -0.0103 102 GLN A O   
803  C CB  . GLN A 104 ? 0.6772 0.5081 0.5089 0.0065  -0.0788 -0.0145 102 GLN A CB  
804  C CG  . GLN A 104 ? 0.7357 0.5514 0.5583 0.0295  -0.1054 -0.0113 102 GLN A CG  
805  C CD  . GLN A 104 ? 0.8444 0.6940 0.6777 0.0318  -0.1124 -0.0061 102 GLN A CD  
806  O OE1 . GLN A 104 ? 0.8505 0.7537 0.7186 0.0479  -0.1117 -0.0110 102 GLN A OE1 
807  N NE2 . GLN A 104 ? 0.8512 0.6717 0.6521 0.0117  -0.1189 0.0048  102 GLN A NE2 
808  N N   . PHE A 105 ? 0.6604 0.5148 0.5176 -0.0231 -0.0323 -0.0259 103 PHE A N   
809  C CA  . PHE A 105 ? 0.6186 0.4886 0.4812 -0.0414 -0.0110 -0.0280 103 PHE A CA  
810  C C   . PHE A 105 ? 0.6376 0.5005 0.5011 -0.0509 -0.0048 -0.0287 103 PHE A C   
811  O O   . PHE A 105 ? 0.6970 0.5715 0.5588 -0.0686 0.0107  -0.0280 103 PHE A O   
812  C CB  . PHE A 105 ? 0.5770 0.4867 0.4699 -0.0337 0.0002  -0.0356 103 PHE A CB  
813  C CG  . PHE A 105 ? 0.6386 0.5539 0.5224 -0.0353 -0.0029 -0.0330 103 PHE A CG  
814  C CD1 . PHE A 105 ? 0.5821 0.5089 0.4730 -0.0228 -0.0181 -0.0308 103 PHE A CD1 
815  C CD2 . PHE A 105 ? 0.6274 0.5369 0.4923 -0.0497 0.0084  -0.0327 103 PHE A CD2 
816  C CE1 . PHE A 105 ? 0.5818 0.5138 0.4614 -0.0288 -0.0234 -0.0261 103 PHE A CE1 
817  C CE2 . PHE A 105 ? 0.6416 0.5482 0.4904 -0.0536 0.0033  -0.0298 103 PHE A CE2 
818  C CZ  . PHE A 105 ? 0.5427 0.4598 0.3987 -0.0452 -0.0136 -0.0253 103 PHE A CZ  
819  N N   . LEU A 106 ? 0.6519 0.4969 0.5154 -0.0401 -0.0170 -0.0299 104 LEU A N   
820  C CA  . LEU A 106 ? 0.6807 0.5177 0.5423 -0.0528 -0.0129 -0.0293 104 LEU A CA  
821  C C   . LEU A 106 ? 0.7452 0.5676 0.5788 -0.0836 -0.0078 -0.0198 104 LEU A C   
822  O O   . LEU A 106 ? 0.7598 0.6097 0.6077 -0.0987 0.0074  -0.0202 104 LEU A O   
823  C CB  . LEU A 106 ? 0.6971 0.4974 0.5446 -0.0387 -0.0320 -0.0308 104 LEU A CB  
824  C CG  . LEU A 106 ? 0.7232 0.5141 0.5677 -0.0533 -0.0296 -0.0299 104 LEU A CG  
825  C CD1 . LEU A 106 ? 0.6751 0.5193 0.5619 -0.0543 -0.0095 -0.0362 104 LEU A CD1 
826  C CD2 . LEU A 106 ? 0.7430 0.4927 0.5692 -0.0362 -0.0486 -0.0341 104 LEU A CD2 
827  N N   . PRO A 107 ? 0.7611 0.5464 0.5557 -0.0954 -0.0198 -0.0108 105 PRO A N   
828  C CA  . PRO A 107 ? 0.7454 0.5212 0.5100 -0.1302 -0.0143 -0.0008 105 PRO A CA  
829  C C   . PRO A 107 ? 0.7647 0.5907 0.5471 -0.1412 0.0119  -0.0043 105 PRO A C   
830  O O   . PRO A 107 ? 0.8386 0.6805 0.6101 -0.1684 0.0234  0.0008  105 PRO A O   
831  C CB  . PRO A 107 ? 0.7866 0.5081 0.5032 -0.1373 -0.0358 0.0091  105 PRO A CB  
832  C CG  . PRO A 107 ? 0.8061 0.5006 0.5269 -0.1036 -0.0574 0.0043  105 PRO A CG  
833  C CD  . PRO A 107 ? 0.7817 0.5313 0.5550 -0.0791 -0.0414 -0.0082 105 PRO A CD  
834  N N   . LYS A 108 ? 0.7272 0.5789 0.5335 -0.1213 0.0209  -0.0131 106 LYS A N   
835  C CA  . LYS A 108 ? 0.7249 0.6167 0.5438 -0.1254 0.0441  -0.0193 106 LYS A CA  
836  C C   . LYS A 108 ? 0.7517 0.6864 0.6137 -0.1115 0.0583  -0.0298 106 LYS A C   
837  O O   . LYS A 108 ? 0.7914 0.7570 0.6646 -0.1081 0.0756  -0.0374 106 LYS A O   
838  C CB  . LYS A 108 ? 0.7170 0.6008 0.5245 -0.1160 0.0426  -0.0217 106 LYS A CB  
839  C CG  . LYS A 108 ? 0.7282 0.5729 0.4903 -0.1329 0.0302  -0.0109 106 LYS A CG  
840  C CD  . LYS A 108 ? 0.7122 0.5558 0.4585 -0.1317 0.0347  -0.0132 106 LYS A CD  
841  C CE  . LYS A 108 ? 0.7814 0.5912 0.4783 -0.1557 0.0274  -0.0025 106 LYS A CE  
842  N NZ  . LYS A 108 ? 0.9035 0.7329 0.5814 -0.1722 0.0506  -0.0071 106 LYS A NZ  
843  N N   . ALA A 109 ? 0.7166 0.6509 0.5996 -0.1025 0.0504  -0.0309 107 ALA A N   
844  C CA  . ALA A 109 ? 0.6856 0.6543 0.6073 -0.0883 0.0594  -0.0399 107 ALA A CA  
845  C C   . ALA A 109 ? 0.6744 0.6711 0.6098 -0.1032 0.0693  -0.0381 107 ALA A C   
846  O O   . ALA A 109 ? 0.7291 0.7090 0.6459 -0.1232 0.0621  -0.0288 107 ALA A O   
847  C CB  . ALA A 109 ? 0.6123 0.5691 0.5486 -0.0705 0.0456  -0.0428 107 ALA A CB  
848  N N   . GLN A 110 ? 0.5923 0.6302 0.5576 -0.0940 0.0836  -0.0465 108 GLN A N   
849  C CA  . GLN A 110 ? 0.6466 0.7238 0.6346 -0.1040 0.0926  -0.0456 108 GLN A CA  
850  C C   . GLN A 110 ? 0.5817 0.6697 0.6016 -0.0905 0.0873  -0.0500 108 GLN A C   
851  O O   . GLN A 110 ? 0.6153 0.7339 0.6549 -0.0998 0.0910  -0.0475 108 GLN A O   
852  C CB  . GLN A 110 ? 0.7098 0.8344 0.7100 -0.1010 0.1131  -0.0529 108 GLN A CB  
853  C CG  . GLN A 110 ? 0.8140 0.9534 0.7892 -0.1239 0.1247  -0.0476 108 GLN A CG  
854  C CD  . GLN A 110 ? 0.9567 1.0517 0.8927 -0.1273 0.1191  -0.0451 108 GLN A CD  
855  O OE1 . GLN A 110 ? 0.9780 1.0623 0.9096 -0.1079 0.1217  -0.0540 108 GLN A OE1 
856  N NE2 . GLN A 110 ? 0.9767 1.0426 0.8789 -0.1542 0.1095  -0.0319 108 GLN A NE2 
857  N N   . LYS A 111 ? 0.5356 0.6029 0.5601 -0.0718 0.0784  -0.0554 109 LYS A N   
858  C CA  . LYS A 111 ? 0.5128 0.5905 0.5639 -0.0602 0.0738  -0.0601 109 LYS A CA  
859  C C   . LYS A 111 ? 0.5421 0.5898 0.5856 -0.0509 0.0602  -0.0610 109 LYS A C   
860  O O   . LYS A 111 ? 0.5651 0.5962 0.5932 -0.0442 0.0567  -0.0619 109 LYS A O   
861  C CB  . LYS A 111 ? 0.5128 0.6149 0.5822 -0.0440 0.0819  -0.0694 109 LYS A CB  
862  C CG  . LYS A 111 ? 0.5146 0.6328 0.6112 -0.0359 0.0776  -0.0730 109 LYS A CG  
863  C CD  . LYS A 111 ? 0.5010 0.6378 0.6094 -0.0185 0.0834  -0.0823 109 LYS A CD  
864  C CE  . LYS A 111 ? 0.4898 0.6439 0.6255 -0.0120 0.0771  -0.0843 109 LYS A CE  
865  N NZ  . LYS A 111 ? 0.5528 0.7133 0.6949 0.0097  0.0770  -0.0944 109 LYS A NZ  
866  N N   . LEU A 112 ? 0.5519 0.5966 0.6058 -0.0508 0.0527  -0.0610 110 LEU A N   
867  C CA  . LEU A 112 ? 0.4880 0.5147 0.5375 -0.0399 0.0421  -0.0641 110 LEU A CA  
868  C C   . LEU A 112 ? 0.4560 0.4996 0.5274 -0.0346 0.0408  -0.0690 110 LEU A C   
869  O O   . LEU A 112 ? 0.4916 0.5464 0.5764 -0.0420 0.0416  -0.0675 110 LEU A O   
870  C CB  . LEU A 112 ? 0.5079 0.5037 0.5370 -0.0444 0.0319  -0.0605 110 LEU A CB  
871  C CG  . LEU A 112 ? 0.5768 0.5453 0.5764 -0.0549 0.0283  -0.0532 110 LEU A CG  
872  C CD1 . LEU A 112 ? 0.5826 0.5131 0.5575 -0.0624 0.0151  -0.0494 110 LEU A CD1 
873  C CD2 . LEU A 112 ? 0.5601 0.5167 0.5467 -0.0424 0.0243  -0.0546 110 LEU A CD2 
874  N N   . TYR A 113 ? 0.4659 0.5126 0.5391 -0.0247 0.0371  -0.0736 111 TYR A N   
875  C CA  . TYR A 113 ? 0.4134 0.4712 0.4997 -0.0229 0.0329  -0.0773 111 TYR A CA  
876  C C   . TYR A 113 ? 0.4738 0.5263 0.5525 -0.0177 0.0266  -0.0802 111 TYR A C   
877  O O   . TYR A 113 ? 0.4794 0.5360 0.5512 -0.0104 0.0243  -0.0817 111 TYR A O   
878  C CB  . TYR A 113 ? 0.4027 0.4691 0.4909 -0.0198 0.0321  -0.0796 111 TYR A CB  
879  C CG  . TYR A 113 ? 0.4328 0.5016 0.5237 -0.0178 0.0379  -0.0803 111 TYR A CG  
880  C CD1 . TYR A 113 ? 0.4619 0.5259 0.5409 -0.0167 0.0450  -0.0793 111 TYR A CD1 
881  C CD2 . TYR A 113 ? 0.4650 0.5406 0.5681 -0.0152 0.0356  -0.0829 111 TYR A CD2 
882  C CE1 . TYR A 113 ? 0.4616 0.5308 0.5405 -0.0120 0.0523  -0.0825 111 TYR A CE1 
883  C CE2 . TYR A 113 ? 0.4726 0.5523 0.5775 -0.0070 0.0410  -0.0863 111 TYR A CE2 
884  C CZ  . TYR A 113 ? 0.4987 0.5770 0.5915 -0.0050 0.0506  -0.0870 111 TYR A CZ  
885  O OH  . TYR A 113 ? 0.4943 0.5794 0.5864 0.0057  0.0578  -0.0928 111 TYR A OH  
886  N N   . LEU A 114 ? 0.4599 0.5060 0.5392 -0.0206 0.0234  -0.0815 112 LEU A N   
887  C CA  . LEU A 114 ? 0.4688 0.5081 0.5371 -0.0118 0.0184  -0.0869 112 LEU A CA  
888  C C   . LEU A 114 ? 0.4401 0.4939 0.5160 -0.0155 0.0167  -0.0911 112 LEU A C   
889  O O   . LEU A 114 ? 0.4488 0.5019 0.5331 -0.0266 0.0158  -0.0884 112 LEU A O   
890  C CB  . LEU A 114 ? 0.4789 0.4847 0.5277 -0.0119 0.0137  -0.0859 112 LEU A CB  
891  C CG  . LEU A 114 ? 0.5046 0.4884 0.5375 -0.0124 0.0124  -0.0804 112 LEU A CG  
892  C CD1 . LEU A 114 ? 0.5382 0.4799 0.5431 -0.0156 0.0030  -0.0789 112 LEU A CD1 
893  C CD2 . LEU A 114 ? 0.5197 0.5098 0.5489 0.0026  0.0111  -0.0827 112 LEU A CD2 
894  N N   . THR A 115 ? 0.4369 0.5081 0.5099 -0.0071 0.0158  -0.0974 113 THR A N   
895  C CA  . THR A 115 ? 0.4509 0.5362 0.5243 -0.0117 0.0146  -0.1025 113 THR A CA  
896  C C   . THR A 115 ? 0.4841 0.5581 0.5414 0.0029  0.0136  -0.1115 113 THR A C   
897  O O   . THR A 115 ? 0.4992 0.5857 0.5524 0.0204  0.0141  -0.1172 113 THR A O   
898  C CB  . THR A 115 ? 0.4672 0.5879 0.5462 -0.0163 0.0148  -0.1031 113 THR A CB  
899  O OG1 . THR A 115 ? 0.4896 0.6093 0.5748 -0.0269 0.0129  -0.0956 113 THR A OG1 
900  C CG2 . THR A 115 ? 0.4787 0.6122 0.5543 -0.0267 0.0133  -0.1069 113 THR A CG2 
901  N N   . HIS A 116 ? 0.4982 0.5476 0.5445 -0.0029 0.0106  -0.1132 114 HIS A N   
902  C CA  . HIS A 116 ? 0.5343 0.5629 0.5571 0.0114  0.0080  -0.1236 114 HIS A CA  
903  C C   . HIS A 116 ? 0.5355 0.5947 0.5580 0.0107  0.0117  -0.1325 114 HIS A C   
904  O O   . HIS A 116 ? 0.5436 0.6025 0.5674 -0.0084 0.0103  -0.1294 114 HIS A O   
905  C CB  . HIS A 116 ? 0.5319 0.5126 0.5351 0.0012  0.0010  -0.1199 114 HIS A CB  
906  C CG  . HIS A 116 ? 0.5603 0.5175 0.5628 -0.0063 -0.0022 -0.1091 114 HIS A CG  
907  N ND1 . HIS A 116 ? 0.5532 0.4762 0.5322 0.0062  -0.0080 -0.1099 114 HIS A ND1 
908  C CD2 . HIS A 116 ? 0.5204 0.4852 0.5406 -0.0252 -0.0006 -0.0974 114 HIS A CD2 
909  C CE1 . HIS A 116 ? 0.5431 0.4545 0.5239 -0.0092 -0.0092 -0.0981 114 HIS A CE1 
910  N NE2 . HIS A 116 ? 0.5360 0.4769 0.5438 -0.0269 -0.0033 -0.0912 114 HIS A NE2 
911  N N   . ILE A 117 ? 0.5328 0.6214 0.5533 0.0309  0.0158  -0.1432 115 ILE A N   
912  C CA  . ILE A 117 ? 0.5096 0.6403 0.5300 0.0299  0.0216  -0.1523 115 ILE A CA  
913  C C   . ILE A 117 ? 0.5791 0.6884 0.5720 0.0508  0.0217  -0.1682 115 ILE A C   
914  O O   . ILE A 117 ? 0.5775 0.6646 0.5567 0.0790  0.0185  -0.1762 115 ILE A O   
915  C CB  . ILE A 117 ? 0.5210 0.7123 0.5598 0.0364  0.0269  -0.1534 115 ILE A CB  
916  C CG1 . ILE A 117 ? 0.4672 0.6640 0.5234 0.0159  0.0241  -0.1380 115 ILE A CG1 
917  C CG2 . ILE A 117 ? 0.5252 0.7705 0.5633 0.0309  0.0339  -0.1618 115 ILE A CG2 
918  C CD1 . ILE A 117 ? 0.5288 0.7765 0.5985 0.0186  0.0260  -0.1360 115 ILE A CD1 
919  N N   . ASP A 118 ? 0.6061 0.7136 0.5857 0.0373  0.0233  -0.1726 116 ASP A N   
920  C CA  A ASP A 118 ? 0.6549 0.7381 0.6017 0.0566  0.0236  -0.1895 116 ASP A CA  
921  C CA  B ASP A 118 ? 0.6545 0.7394 0.6017 0.0557  0.0239  -0.1895 116 ASP A CA  
922  C C   . ASP A 118 ? 0.6843 0.8325 0.6357 0.0787  0.0350  -0.2058 116 ASP A C   
923  O O   . ASP A 118 ? 0.7337 0.9181 0.6795 0.0690  0.0428  -0.2132 116 ASP A O   
924  C CB  A ASP A 118 ? 0.6436 0.6933 0.5703 0.0312  0.0194  -0.1868 116 ASP A CB  
925  C CB  B ASP A 118 ? 0.6394 0.7002 0.5689 0.0295  0.0211  -0.1873 116 ASP A CB  
926  C CG  A ASP A 118 ? 0.6957 0.6856 0.6175 0.0135  0.0072  -0.1717 116 ASP A CG  
927  C CG  B ASP A 118 ? 0.7127 0.7441 0.6021 0.0471  0.0214  -0.2055 116 ASP A CG  
928  O OD1 A ASP A 118 ? 0.6668 0.6105 0.5703 0.0283  0.0001  -0.1725 116 ASP A OD1 
929  O OD1 B ASP A 118 ? 0.7578 0.7805 0.6316 0.0832  0.0223  -0.2204 116 ASP A OD1 
930  O OD2 A ASP A 118 ? 0.6318 0.6243 0.5686 -0.0157 0.0037  -0.1581 116 ASP A OD2 
931  O OD2 B ASP A 118 ? 0.7540 0.7697 0.6249 0.0261  0.0197  -0.2056 116 ASP A OD2 
932  N N   . ALA A 119 ? 0.6847 0.8510 0.6462 0.1084  0.0353  -0.2109 117 ALA A N   
933  C CA  . ALA A 119 ? 0.7172 0.9535 0.6885 0.1354  0.0450  -0.2263 117 ALA A CA  
934  C C   . ALA A 119 ? 0.7684 0.9813 0.7310 0.1800  0.0381  -0.2366 117 ALA A C   
935  O O   . ALA A 119 ? 0.7757 0.9292 0.7315 0.1802  0.0262  -0.2264 117 ALA A O   
936  C CB  . ALA A 119 ? 0.7132 1.0245 0.7207 0.1141  0.0507  -0.2143 117 ALA A CB  
937  N N   . GLU A 120 ? 0.8262 1.0916 0.7909 0.2176  0.0446  -0.2560 118 GLU A N   
938  C CA  . GLU A 120 ? 0.8912 1.1249 0.8401 0.2665  0.0346  -0.2692 118 GLU A CA  
939  C C   . GLU A 120 ? 0.8542 1.1729 0.8450 0.2781  0.0382  -0.2655 118 GLU A C   
940  O O   . GLU A 120 ? 0.8352 1.2411 0.8498 0.2704  0.0501  -0.2665 118 GLU A O   
941  C CB  . GLU A 120 ? 0.9849 1.2164 0.9062 0.2997  0.0372  -0.2902 118 GLU A CB  
942  C CG  . GLU A 120 ? 1.1203 1.2685 1.0039 0.3358  0.0194  -0.2965 118 GLU A CG  
943  C CD  . GLU A 120 ? 1.2798 1.4264 1.1377 0.3682  0.0202  -0.3134 118 GLU A CD  
944  O OE1 . GLU A 120 ? 1.2256 1.4577 1.1066 0.3659  0.0366  -0.3196 118 GLU A OE1 
945  O OE2 . GLU A 120 ? 1.3749 1.4212 1.1840 0.3797  0.0046  -0.3171 118 GLU A OE2 
946  N N   . VAL A 121 ? 0.8716 1.1637 0.8702 0.2861  0.0258  -0.2545 119 VAL A N   
947  C CA  . VAL A 121 ? 0.8122 1.1828 0.8464 0.3005  0.0264  -0.2516 119 VAL A CA  
948  C C   . VAL A 121 ? 0.9429 1.2767 0.9624 0.3436  0.0094  -0.2562 119 VAL A C   
949  O O   . VAL A 121 ? 1.0228 1.2629 1.0076 0.3576  -0.0051 -0.2580 119 VAL A O   
950  C CB  . VAL A 121 ? 0.8028 1.1879 0.8631 0.2612  0.0249  -0.2272 119 VAL A CB  
951  C CG1 . VAL A 121 ? 0.8247 1.2795 0.9150 0.2771  0.0222  -0.2244 119 VAL A CG1 
952  C CG2 . VAL A 121 ? 0.7112 1.1292 0.7823 0.2129  0.0370  -0.2170 119 VAL A CG2 
953  N N   . GLU A 122 ? 0.9521 1.3599 0.9950 0.3621  0.0094  -0.2576 120 GLU A N   
954  C CA  . GLU A 122 ? 1.0359 1.4224 1.0674 0.4049  -0.0073 -0.2634 120 GLU A CA  
955  C C   . GLU A 122 ? 1.0360 1.4339 1.0882 0.4064  -0.0187 -0.2501 120 GLU A C   
956  O O   . GLU A 122 ? 1.1307 1.5315 1.1805 0.4398  -0.0324 -0.2537 120 GLU A O   
957  C CB  . GLU A 122 ? 1.0049 1.4646 1.0460 0.4301  -0.0021 -0.2760 120 GLU A CB  
958  C CG  . GLU A 122 ? 1.0658 1.5266 1.0881 0.4303  0.0102  -0.2902 120 GLU A CG  
959  C CD  . GLU A 122 ? 1.1324 1.7012 1.1798 0.4365  0.0223  -0.2976 120 GLU A CD  
960  O OE1 . GLU A 122 ? 1.1572 1.8062 1.2399 0.4259  0.0240  -0.2877 120 GLU A OE1 
961  O OE2 . GLU A 122 ? 1.1234 1.6966 1.1529 0.4509  0.0295  -0.3131 120 GLU A OE2 
962  N N   . GLY A 123 ? 1.0240 1.4284 1.0952 0.3723  -0.0142 -0.2355 121 GLY A N   
963  C CA  . GLY A 123 ? 1.0505 1.4486 1.1342 0.3746  -0.0272 -0.2230 121 GLY A CA  
964  C C   . GLY A 123 ? 1.1497 1.4486 1.1953 0.4058  -0.0498 -0.2261 121 GLY A C   
965  O O   . GLY A 123 ? 1.1564 1.3802 1.1618 0.4189  -0.0554 -0.2361 121 GLY A O   
966  N N   . ASP A 124 ? 1.1460 1.4395 1.1986 0.4155  -0.0654 -0.2162 122 ASP A N   
967  C CA  . ASP A 124 ? 1.1647 1.3552 1.1757 0.4367  -0.0901 -0.2149 122 ASP A CA  
968  C C   . ASP A 124 ? 1.1491 1.2776 1.1458 0.3892  -0.0941 -0.1912 122 ASP A C   
969  O O   . ASP A 124 ? 1.1416 1.1861 1.1016 0.3950  -0.1149 -0.1850 122 ASP A O   
970  C CB  . ASP A 124 ? 1.2060 1.4159 1.2204 0.4697  -0.1085 -0.2148 122 ASP A CB  
971  C CG  . ASP A 124 ? 1.3967 1.6190 1.3972 0.5051  -0.1106 -0.2325 122 ASP A CG  
972  O OD1 . ASP A 124 ? 1.4959 1.6267 1.4471 0.5257  -0.1265 -0.2407 122 ASP A OD1 
973  O OD2 . ASP A 124 ? 1.3976 1.7201 1.4336 0.5111  -0.0977 -0.2375 122 ASP A OD2 
974  N N   . THR A 125 ? 0.9784 1.1443 0.9993 0.3424  -0.0758 -0.1780 123 THR A N   
975  C CA  . THR A 125 ? 0.8818 1.0059 0.8945 0.3005  -0.0773 -0.1569 123 THR A CA  
976  C C   . THR A 125 ? 0.9105 0.9683 0.8968 0.2728  -0.0707 -0.1544 123 THR A C   
977  O O   . THR A 125 ? 0.9202 1.0060 0.9192 0.2579  -0.0546 -0.1592 123 THR A O   
978  C CB  . THR A 125 ? 0.7682 0.9682 0.8186 0.2686  -0.0638 -0.1446 123 THR A CB  
979  O OG1 . THR A 125 ? 0.9137 1.1844 0.9901 0.2927  -0.0708 -0.1462 123 THR A OG1 
980  C CG2 . THR A 125 ? 0.7840 0.9394 0.8221 0.2324  -0.0662 -0.1256 123 THR A CG2 
981  N N   . HIS A 126 ? 0.8897 0.8630 0.8387 0.2635  -0.0844 -0.1460 124 HIS A N   
982  C CA  . HIS A 126 ? 0.8677 0.7806 0.7904 0.2362  -0.0808 -0.1420 124 HIS A CA  
983  C C   . HIS A 126 ? 0.8302 0.7344 0.7577 0.1926  -0.0736 -0.1233 124 HIS A C   
984  O O   . HIS A 126 ? 0.7850 0.6886 0.7128 0.1864  -0.0796 -0.1127 124 HIS A O   
985  C CB  . HIS A 126 ? 0.9691 0.7890 0.8377 0.2542  -0.1028 -0.1467 124 HIS A CB  
986  C CG  . HIS A 126 ? 1.0693 0.8848 0.9246 0.2971  -0.1084 -0.1683 124 HIS A CG  
987  N ND1 . HIS A 126 ? 1.0869 0.8600 0.9144 0.2944  -0.1070 -0.1772 124 HIS A ND1 
988  C CD2 . HIS A 126 ? 1.1246 0.9749 0.9892 0.3454  -0.1154 -0.1840 124 HIS A CD2 
989  C CE1 . HIS A 126 ? 1.1574 0.9344 0.9739 0.3399  -0.1122 -0.1986 124 HIS A CE1 
990  N NE2 . HIS A 126 ? 1.1728 1.0000 1.0135 0.3733  -0.1168 -0.2037 124 HIS A NE2 
991  N N   . PHE A 127 ? 0.7854 0.6862 0.7168 0.1639  -0.0605 -0.1200 125 PHE A N   
992  C CA  . PHE A 127 ? 0.6960 0.5849 0.6281 0.1271  -0.0537 -0.1048 125 PHE A CA  
993  C C   . PHE A 127 ? 0.7646 0.5787 0.6530 0.1193  -0.0699 -0.0965 125 PHE A C   
994  O O   . PHE A 127 ? 0.8360 0.5961 0.6899 0.1325  -0.0842 -0.1022 125 PHE A O   
995  C CB  . PHE A 127 ? 0.7159 0.6186 0.6622 0.1024  -0.0388 -0.1040 125 PHE A CB  
996  C CG  . PHE A 127 ? 0.6524 0.5638 0.6099 0.0708  -0.0286 -0.0915 125 PHE A CG  
997  C CD1 . PHE A 127 ? 0.6132 0.5710 0.5969 0.0646  -0.0192 -0.0883 125 PHE A CD1 
998  C CD2 . PHE A 127 ? 0.6062 0.4809 0.5457 0.0474  -0.0288 -0.0835 125 PHE A CD2 
999  C CE1 . PHE A 127 ? 0.5619 0.5243 0.5519 0.0407  -0.0099 -0.0797 125 PHE A CE1 
1000 C CE2 . PHE A 127 ? 0.6458 0.5371 0.5978 0.0230  -0.0177 -0.0744 125 PHE A CE2 
1001 C CZ  . PHE A 127 ? 0.5865 0.5192 0.5628 0.0223  -0.0081 -0.0738 125 PHE A CZ  
1002 N N   . PRO A 128 ? 0.7470 0.5531 0.6304 0.0981  -0.0698 -0.0835 126 PRO A N   
1003 C CA  . PRO A 128 ? 0.8223 0.5586 0.6595 0.0859  -0.0865 -0.0738 126 PRO A CA  
1004 C C   . PRO A 128 ? 0.9060 0.6041 0.7204 0.0614  -0.0861 -0.0702 126 PRO A C   
1005 O O   . PRO A 128 ? 0.9207 0.6538 0.7614 0.0452  -0.0691 -0.0707 126 PRO A O   
1006 C CB  . PRO A 128 ? 0.7825 0.5356 0.6260 0.0620  -0.0791 -0.0613 126 PRO A CB  
1007 C CG  . PRO A 128 ? 0.6965 0.5193 0.5868 0.0556  -0.0564 -0.0643 126 PRO A CG  
1008 C CD  . PRO A 128 ? 0.6703 0.5269 0.5834 0.0850  -0.0567 -0.0773 126 PRO A CD  
1009 N N   . ASP A 129 ? 0.9944 0.6184 0.7568 0.0564  -0.1074 -0.0651 127 ASP A N   
1010 C CA  . ASP A 129 ? 1.1150 0.7004 0.8501 0.0280  -0.1103 -0.0592 127 ASP A CA  
1011 C C   . ASP A 129 ? 1.1717 0.7748 0.9111 -0.0164 -0.0980 -0.0433 127 ASP A C   
1012 O O   . ASP A 129 ? 1.1604 0.7590 0.8887 -0.0288 -0.0998 -0.0339 127 ASP A O   
1013 C CB  . ASP A 129 ? 1.2023 0.6945 0.8714 0.0352  -0.1406 -0.0587 127 ASP A CB  
1014 C CG  . ASP A 129 ? 1.2926 0.7649 0.9529 0.0714  -0.1486 -0.0765 127 ASP A CG  
1015 O OD1 . ASP A 129 ? 1.3476 0.8389 1.0224 0.0618  -0.1369 -0.0808 127 ASP A OD1 
1016 O OD2 . ASP A 129 ? 1.3393 0.7777 0.9772 0.1103  -0.1671 -0.0865 127 ASP A OD2 
1017 N N   . TYR A 130 ? 1.1925 0.8198 0.9483 -0.0394 -0.0853 -0.0408 128 TYR A N   
1018 C CA  . TYR A 130 ? 1.2363 0.8847 0.9951 -0.0801 -0.0744 -0.0269 128 TYR A CA  
1019 C C   . TYR A 130 ? 1.3730 0.9756 1.0915 -0.1115 -0.0878 -0.0170 128 TYR A C   
1020 O O   . TYR A 130 ? 1.3716 0.9440 1.0759 -0.1034 -0.0978 -0.0229 128 TYR A O   
1021 C CB  . TYR A 130 ? 1.0696 0.7981 0.8874 -0.0829 -0.0475 -0.0304 128 TYR A CB  
1022 C CG  . TYR A 130 ? 1.0225 0.7750 0.8689 -0.0695 -0.0416 -0.0404 128 TYR A CG  
1023 C CD1 . TYR A 130 ? 0.9841 0.7533 0.8513 -0.0363 -0.0397 -0.0537 128 TYR A CD1 
1024 C CD2 . TYR A 130 ? 0.9798 0.7448 0.8338 -0.0927 -0.0377 -0.0356 128 TYR A CD2 
1025 C CE1 . TYR A 130 ? 0.9276 0.7194 0.8173 -0.0272 -0.0342 -0.0625 128 TYR A CE1 
1026 C CE2 . TYR A 130 ? 0.9662 0.7509 0.8440 -0.0821 -0.0336 -0.0441 128 TYR A CE2 
1027 C CZ  . TYR A 130 ? 0.9552 0.7511 0.8488 -0.0497 -0.0316 -0.0578 128 TYR A CZ  
1028 O OH  . TYR A 130 ? 0.9566 0.7716 0.8692 -0.0416 -0.0277 -0.0662 128 TYR A OH  
1029 N N   . GLU A 131 ? 1.5176 1.1156 1.2141 -0.1497 -0.0884 -0.0014 129 GLU A N   
1030 C CA  . GLU A 131 ? 1.5843 1.1427 1.2363 -0.1911 -0.1026 0.0132  129 GLU A CA  
1031 C C   . GLU A 131 ? 1.5378 1.1556 1.2297 -0.2097 -0.0860 0.0149  129 GLU A C   
1032 O O   . GLU A 131 ? 1.5352 1.2244 1.2661 -0.2267 -0.0643 0.0196  129 GLU A O   
1033 C CB  . GLU A 131 ? 1.6076 1.1586 1.2284 -0.2282 -0.1051 0.0297  129 GLU A CB  
1034 C CG  . GLU A 131 ? 1.6949 1.2053 1.2888 -0.2095 -0.1170 0.0286  129 GLU A CG  
1035 C CD  . GLU A 131 ? 1.7121 1.2823 1.3618 -0.1736 -0.0958 0.0156  129 GLU A CD  
1036 O OE1 . GLU A 131 ? 1.6010 1.2482 1.3030 -0.1766 -0.0686 0.0122  129 GLU A OE1 
1037 O OE2 . GLU A 131 ? 1.6871 1.2256 1.3258 -0.1420 -0.1086 0.0090  129 GLU A OE2 
1038 N N   . PRO A 132 ? 1.2857 0.8870 1.4197 -0.1453 -0.2104 0.1011  130 PRO A N   
1039 C CA  . PRO A 132 ? 1.1943 0.8397 1.3488 -0.1635 -0.1997 0.0863  130 PRO A CA  
1040 C C   . PRO A 132 ? 1.1426 0.8225 1.3050 -0.2071 -0.1914 0.1105  130 PRO A C   
1041 O O   . PRO A 132 ? 1.1276 0.8745 1.3109 -0.2150 -0.1751 0.1047  130 PRO A O   
1042 C CB  . PRO A 132 ? 1.2085 0.7954 1.3532 -0.1581 -0.2180 0.0633  130 PRO A CB  
1043 C CG  . PRO A 132 ? 1.2261 0.7566 1.3536 -0.1199 -0.2324 0.0547  130 PRO A CG  
1044 C CD  . PRO A 132 ? 1.2968 0.8162 1.4121 -0.1247 -0.2339 0.0875  130 PRO A CD  
1045 N N   . ASP A 133 ? 1.2010 0.8501 1.3420 -0.2278 -0.1971 0.1349  131 ASP A N   
1046 C CA  . ASP A 133 ? 1.2463 0.9396 1.3911 -0.2653 -0.1852 0.1560  131 ASP A CA  
1047 C C   . ASP A 133 ? 1.1190 0.8811 1.2756 -0.2702 -0.1654 0.1743  131 ASP A C   
1048 O O   . ASP A 133 ? 1.1005 0.9207 1.2673 -0.2949 -0.1510 0.1857  131 ASP A O   
1049 C CB  . ASP A 133 ? 1.2600 0.8943 1.3749 -0.2857 -0.1980 0.1766  131 ASP A CB  
1050 C CG  . ASP A 133 ? 1.3454 1.0237 1.4644 -0.3271 -0.1873 0.1966  131 ASP A CG  
1051 O OD1 . ASP A 133 ? 1.3810 1.1172 1.5063 -0.3370 -0.1708 0.2163  131 ASP A OD1 
1052 O OD2 . ASP A 133 ? 1.4408 1.0974 1.5558 -0.3497 -0.1955 0.1922  131 ASP A OD2 
1053 N N   . ASP A 134 ? 1.1018 0.8636 1.2559 -0.2453 -0.1633 0.1755  132 ASP A N   
1054 C CA  . ASP A 134 ? 1.0285 0.8600 1.1855 -0.2413 -0.1410 0.1846  132 ASP A CA  
1055 C C   . ASP A 134 ? 0.8924 0.7775 1.0668 -0.2147 -0.1247 0.1565  132 ASP A C   
1056 O O   . ASP A 134 ? 0.8362 0.7721 1.0092 -0.2076 -0.1069 0.1591  132 ASP A O   
1057 C CB  . ASP A 134 ? 1.0376 0.8475 1.1697 -0.2262 -0.1445 0.2011  132 ASP A CB  
1058 C CG  . ASP A 134 ? 1.2066 1.0018 1.3181 -0.2592 -0.1478 0.2392  132 ASP A CG  
1059 O OD1 . ASP A 134 ? 1.2538 1.0113 1.3397 -0.2489 -0.1583 0.2559  132 ASP A OD1 
1060 O OD2 . ASP A 134 ? 1.2125 1.0399 1.3309 -0.2913 -0.1389 0.2502  132 ASP A OD2 
1061 N N   . TRP A 135 ? 0.8347 0.7059 1.0208 -0.2001 -0.1308 0.1301  133 TRP A N   
1062 C CA  . TRP A 135 ? 0.7719 0.6840 0.9687 -0.1757 -0.1170 0.1058  133 TRP A CA  
1063 C C   . TRP A 135 ? 0.7757 0.7076 0.9907 -0.1844 -0.1170 0.0913  133 TRP A C   
1064 O O   . TRP A 135 ? 0.8380 0.7336 1.0554 -0.1984 -0.1332 0.0879  133 TRP A O   
1065 C CB  . TRP A 135 ? 0.7589 0.6429 0.9487 -0.1436 -0.1231 0.0871  133 TRP A CB  
1066 C CG  . TRP A 135 ? 0.7552 0.6399 0.9306 -0.1318 -0.1211 0.0985  133 TRP A CG  
1067 C CD1 . TRP A 135 ? 0.8375 0.6802 0.9984 -0.1292 -0.1361 0.1137  133 TRP A CD1 
1068 C CD2 . TRP A 135 ? 0.6697 0.5967 0.8407 -0.1207 -0.1054 0.0951  133 TRP A CD2 
1069 N NE1 . TRP A 135 ? 0.7744 0.6389 0.9247 -0.1175 -0.1307 0.1205  133 TRP A NE1 
1070 C CE2 . TRP A 135 ? 0.6933 0.6083 0.8492 -0.1139 -0.1120 0.1082  133 TRP A CE2 
1071 C CE3 . TRP A 135 ? 0.5799 0.5484 0.7546 -0.1155 -0.0882 0.0821  133 TRP A CE3 
1072 C CZ2 . TRP A 135 ? 0.6055 0.5524 0.7513 -0.1055 -0.1021 0.1070  133 TRP A CZ2 
1073 C CZ3 . TRP A 135 ? 0.5714 0.5624 0.7330 -0.1067 -0.0782 0.0809  133 TRP A CZ3 
1074 C CH2 . TRP A 135 ? 0.5572 0.5393 0.7053 -0.1035 -0.0852 0.0925  133 TRP A CH2 
1075 N N   . GLU A 136 ? 0.6400 0.6267 0.8644 -0.1754 -0.1004 0.0827  134 GLU A N   
1076 C CA  . GLU A 136 ? 0.5392 0.5543 0.7800 -0.1782 -0.1000 0.0692  134 GLU A CA  
1077 C C   . GLU A 136 ? 0.5447 0.5636 0.7810 -0.1479 -0.0939 0.0459  134 GLU A C   
1078 O O   . GLU A 136 ? 0.5353 0.5669 0.7613 -0.1306 -0.0810 0.0442  134 GLU A O   
1079 C CB  . GLU A 136 ? 0.5972 0.6784 0.8521 -0.1920 -0.0864 0.0814  134 GLU A CB  
1080 C CG  . GLU A 136 ? 0.5845 0.7034 0.8579 -0.1920 -0.0876 0.0685  134 GLU A CG  
1081 C CD  . GLU A 136 ? 0.6027 0.7954 0.8949 -0.2060 -0.0762 0.0818  134 GLU A CD  
1082 O OE1 . GLU A 136 ? 0.6439 0.8604 0.9318 -0.2127 -0.0639 0.0995  134 GLU A OE1 
1083 O OE2 . GLU A 136 ? 0.6169 0.8486 0.9281 -0.2098 -0.0800 0.0744  134 GLU A OE2 
1084 N N   . SER A 137 ? 0.5303 0.5362 0.7709 -0.1438 -0.1036 0.0284  135 SER A N   
1085 C CA  . SER A 137 ? 0.4903 0.5019 0.7242 -0.1187 -0.0976 0.0087  135 SER A CA  
1086 C C   . SER A 137 ? 0.5352 0.5968 0.7768 -0.1157 -0.0877 0.0079  135 SER A C   
1087 O O   . SER A 137 ? 0.4739 0.5594 0.7310 -0.1308 -0.0946 0.0097  135 SER A O   
1088 C CB  . SER A 137 ? 0.5312 0.5079 0.7614 -0.1131 -0.1122 -0.0103 135 SER A CB  
1089 O OG  . SER A 137 ? 0.5219 0.5062 0.7424 -0.0906 -0.1050 -0.0272 135 SER A OG  
1090 N N   . VAL A 138 ? 0.4991 0.5760 0.7290 -0.0963 -0.0730 0.0053  136 VAL A N   
1091 C CA  . VAL A 138 ? 0.4820 0.6012 0.7143 -0.0865 -0.0635 0.0055  136 VAL A CA  
1092 C C   . VAL A 138 ? 0.5577 0.6692 0.7742 -0.0646 -0.0611 -0.0092 136 VAL A C   
1093 O O   . VAL A 138 ? 0.5417 0.6827 0.7580 -0.0524 -0.0571 -0.0102 136 VAL A O   
1094 C CB  . VAL A 138 ? 0.5087 0.6500 0.7341 -0.0814 -0.0480 0.0167  136 VAL A CB  
1095 C CG1 . VAL A 138 ? 0.4812 0.6398 0.7209 -0.1055 -0.0493 0.0346  136 VAL A CG1 
1096 C CG2 . VAL A 138 ? 0.4339 0.5422 0.6350 -0.0695 -0.0411 0.0122  136 VAL A CG2 
1097 N N   . PHE A 139 ? 0.5198 0.5956 0.7220 -0.0585 -0.0633 -0.0195 137 PHE A N   
1098 C CA  . PHE A 139 ? 0.5028 0.5698 0.6858 -0.0421 -0.0602 -0.0308 137 PHE A CA  
1099 C C   . PHE A 139 ? 0.5527 0.5929 0.7298 -0.0418 -0.0663 -0.0429 137 PHE A C   
1100 O O   . PHE A 139 ? 0.5171 0.5409 0.6948 -0.0450 -0.0658 -0.0422 137 PHE A O   
1101 C CB  . PHE A 139 ? 0.4998 0.5599 0.6600 -0.0301 -0.0459 -0.0277 137 PHE A CB  
1102 C CG  . PHE A 139 ? 0.5035 0.5459 0.6380 -0.0179 -0.0423 -0.0355 137 PHE A CG  
1103 C CD1 . PHE A 139 ? 0.5530 0.6044 0.6764 -0.0037 -0.0427 -0.0360 137 PHE A CD1 
1104 C CD2 . PHE A 139 ? 0.4924 0.5126 0.6130 -0.0210 -0.0390 -0.0409 137 PHE A CD2 
1105 C CE1 . PHE A 139 ? 0.5199 0.5491 0.6135 0.0060  -0.0401 -0.0399 137 PHE A CE1 
1106 C CE2 . PHE A 139 ? 0.5063 0.5118 0.6004 -0.0148 -0.0346 -0.0453 137 PHE A CE2 
1107 C CZ  . PHE A 139 ? 0.5118 0.5172 0.5900 -0.0019 -0.0353 -0.0438 137 PHE A CZ  
1108 N N   . SER A 140 ? 0.4378 0.4779 0.6078 -0.0356 -0.0720 -0.0543 138 SER A N   
1109 C CA  . SER A 140 ? 0.4721 0.4942 0.6316 -0.0306 -0.0742 -0.0677 138 SER A CA  
1110 C C   . SER A 140 ? 0.4943 0.5214 0.6317 -0.0198 -0.0707 -0.0744 138 SER A C   
1111 O O   . SER A 140 ? 0.5193 0.5607 0.6536 -0.0159 -0.0740 -0.0720 138 SER A O   
1112 C CB  . SER A 140 ? 0.4942 0.5025 0.6662 -0.0368 -0.0897 -0.0778 138 SER A CB  
1113 O OG  . SER A 140 ? 0.4347 0.4543 0.6138 -0.0440 -0.1013 -0.0806 138 SER A OG  
1114 N N   . GLU A 141 ? 0.5019 0.5210 0.6229 -0.0149 -0.0638 -0.0816 139 GLU A N   
1115 C CA  . GLU A 141 ? 0.5376 0.5586 0.6311 -0.0075 -0.0586 -0.0846 139 GLU A CA  
1116 C C   . GLU A 141 ? 0.5232 0.5464 0.6072 -0.0046 -0.0561 -0.0982 139 GLU A C   
1117 O O   . GLU A 141 ? 0.5437 0.5694 0.6272 -0.0073 -0.0466 -0.0975 139 GLU A O   
1118 C CB  . GLU A 141 ? 0.5494 0.5610 0.6216 -0.0073 -0.0458 -0.0718 139 GLU A CB  
1119 C CG  . GLU A 141 ? 0.5715 0.5775 0.6132 0.0013  -0.0444 -0.0679 139 GLU A CG  
1120 C CD  . GLU A 141 ? 0.6005 0.5830 0.6160 0.0015  -0.0339 -0.0556 139 GLU A CD  
1121 O OE1 . GLU A 141 ? 0.7029 0.6793 0.7120 0.0127  -0.0356 -0.0480 139 GLU A OE1 
1122 O OE2 . GLU A 141 ? 0.5643 0.5354 0.5645 -0.0092 -0.0244 -0.0544 139 GLU A OE2 
1123 N N   . PHE A 142 ? 0.5410 0.5691 0.6163 0.0016  -0.0641 -0.1111 140 PHE A N   
1124 C CA  . PHE A 142 ? 0.5168 0.5527 0.5810 0.0082  -0.0608 -0.1269 140 PHE A CA  
1125 C C   . PHE A 142 ? 0.5304 0.5767 0.5624 0.0082  -0.0475 -0.1218 140 PHE A C   
1126 O O   . PHE A 142 ? 0.5596 0.6007 0.5709 0.0087  -0.0485 -0.1127 140 PHE A O   
1127 C CB  . PHE A 142 ? 0.4814 0.5142 0.5448 0.0149  -0.0762 -0.1461 140 PHE A CB  
1128 C CG  . PHE A 142 ? 0.5108 0.5523 0.5631 0.0267  -0.0730 -0.1661 140 PHE A CG  
1129 C CD1 . PHE A 142 ? 0.5543 0.5900 0.6240 0.0343  -0.0746 -0.1764 140 PHE A CD1 
1130 C CD2 . PHE A 142 ? 0.5712 0.6292 0.5935 0.0330  -0.0680 -0.1744 140 PHE A CD2 
1131 C CE1 . PHE A 142 ? 0.5638 0.6138 0.6238 0.0511  -0.0706 -0.1969 140 PHE A CE1 
1132 C CE2 . PHE A 142 ? 0.5324 0.6063 0.5436 0.0462  -0.0629 -0.1944 140 PHE A CE2 
1133 C CZ  . PHE A 142 ? 0.5464 0.6184 0.5779 0.0567  -0.0637 -0.2065 140 PHE A CZ  
1134 N N   . HIS A 143 ? 0.5370 0.6003 0.5639 0.0079  -0.0357 -0.1272 141 HIS A N   
1135 C CA  . HIS A 143 ? 0.5624 0.6396 0.5567 0.0036  -0.0225 -0.1227 141 HIS A CA  
1136 C C   . HIS A 143 ? 0.5411 0.6498 0.5322 0.0130  -0.0175 -0.1422 141 HIS A C   
1137 O O   . HIS A 143 ? 0.5327 0.6560 0.5483 0.0203  -0.0174 -0.1539 141 HIS A O   
1138 C CB  . HIS A 143 ? 0.5541 0.6283 0.5415 -0.0133 -0.0085 -0.1048 141 HIS A CB  
1139 C CG  . HIS A 143 ? 0.6059 0.6464 0.5878 -0.0181 -0.0120 -0.0880 141 HIS A CG  
1140 N ND1 . HIS A 143 ? 0.6241 0.6412 0.5703 -0.0198 -0.0101 -0.0743 141 HIS A ND1 
1141 C CD2 . HIS A 143 ? 0.5945 0.6213 0.5993 -0.0187 -0.0171 -0.0832 141 HIS A CD2 
1142 C CE1 . HIS A 143 ? 0.6384 0.6296 0.5871 -0.0181 -0.0138 -0.0640 141 HIS A CE1 
1143 N NE2 . HIS A 143 ? 0.5511 0.5508 0.5355 -0.0187 -0.0171 -0.0693 141 HIS A NE2 
1144 N N   . ASP A 144 ? 0.5694 0.6899 0.5280 0.0159  -0.0138 -0.1460 142 ASP A N   
1145 C CA  . ASP A 144 ? 0.4947 0.6534 0.4453 0.0253  -0.0048 -0.1639 142 ASP A CA  
1146 C C   . ASP A 144 ? 0.5313 0.7244 0.4831 0.0108  0.0155  -0.1535 142 ASP A C   
1147 O O   . ASP A 144 ? 0.5531 0.7320 0.4996 -0.0097 0.0219  -0.1315 142 ASP A O   
1148 C CB  . ASP A 144 ? 0.5308 0.6980 0.4408 0.0299  -0.0042 -0.1688 142 ASP A CB  
1149 C CG  . ASP A 144 ? 0.5930 0.7354 0.4991 0.0417  -0.0255 -0.1812 142 ASP A CG  
1150 O OD1 . ASP A 144 ? 0.6075 0.7422 0.5341 0.0543  -0.0382 -0.2031 142 ASP A OD1 
1151 O OD2 . ASP A 144 ? 0.6873 0.8179 0.5667 0.0380  -0.0307 -0.1692 142 ASP A OD2 
1152 N N   . ALA A 145 ? 0.5160 0.7568 0.4727 0.0214  0.0252  -0.1706 143 ALA A N   
1153 C CA  . ALA A 145 ? 0.5370 0.8268 0.4888 0.0042  0.0463  -0.1608 143 ALA A CA  
1154 C C   . ALA A 145 ? 0.5892 0.8784 0.4938 -0.0150 0.0572  -0.1436 143 ALA A C   
1155 O O   . ALA A 145 ? 0.6019 0.8731 0.4771 -0.0051 0.0505  -0.1478 143 ALA A O   
1156 C CB  . ALA A 145 ? 0.4853 0.8379 0.4529 0.0250  0.0550  -0.1849 143 ALA A CB  
1157 N N   . ASP A 146 ? 0.6061 0.9140 0.5006 -0.0443 0.0731  -0.1234 144 ASP A N   
1158 C CA  . ASP A 146 ? 0.6669 0.9681 0.5115 -0.0664 0.0838  -0.1030 144 ASP A CA  
1159 C C   . ASP A 146 ? 0.7355 1.0939 0.5786 -0.0959 0.1057  -0.0923 144 ASP A C   
1160 O O   . ASP A 146 ? 0.7352 1.1549 0.6162 -0.0900 0.1128  -0.1071 144 ASP A O   
1161 C CB  . ASP A 146 ? 0.6922 0.9172 0.5116 -0.0786 0.0732  -0.0794 144 ASP A CB  
1162 C CG  . ASP A 146 ? 0.7010 0.9015 0.5398 -0.0986 0.0731  -0.0663 144 ASP A CG  
1163 O OD1 . ASP A 146 ? 0.7649 1.0099 0.6250 -0.1155 0.0845  -0.0672 144 ASP A OD1 
1164 O OD2 . ASP A 146 ? 0.6954 0.8360 0.5275 -0.0967 0.0613  -0.0560 144 ASP A OD2 
1165 N N   . ALA A 147 ? 0.8119 1.1507 0.6100 -0.1284 0.1154  -0.0656 145 ALA A N   
1166 C CA  . ALA A 147 ? 0.8066 1.2010 0.5995 -0.1650 0.1364  -0.0523 145 ALA A CA  
1167 C C   . ALA A 147 ? 0.8024 1.2153 0.6398 -0.1809 0.1363  -0.0525 145 ALA A C   
1168 O O   . ALA A 147 ? 0.8462 1.3418 0.7110 -0.1918 0.1501  -0.0589 145 ALA A O   
1169 C CB  . ALA A 147 ? 0.8550 1.2033 0.5863 -0.2022 0.1432  -0.0194 145 ALA A CB  
1170 N N   . GLN A 148 ? 0.7522 1.0956 0.5973 -0.1821 0.1208  -0.0459 146 GLN A N   
1171 C CA  . GLN A 148 ? 0.7369 1.0998 0.6151 -0.2036 0.1216  -0.0435 146 GLN A CA  
1172 C C   . GLN A 148 ? 0.6571 1.0432 0.5908 -0.1694 0.1100  -0.0667 146 GLN A C   
1173 O O   . GLN A 148 ? 0.6961 1.1246 0.6642 -0.1799 0.1114  -0.0695 146 GLN A O   
1174 C CB  . GLN A 148 ? 0.7746 1.0520 0.6260 -0.2300 0.1131  -0.0226 146 GLN A CB  
1175 C CG  . GLN A 148 ? 0.8940 1.1272 0.6855 -0.2700 0.1213  0.0046  146 GLN A CG  
1176 C CD  . GLN A 148 ? 0.9982 1.1795 0.7458 -0.2480 0.1163  0.0110  146 GLN A CD  
1177 O OE1 . GLN A 148 ? 1.0268 1.2302 0.7403 -0.2583 0.1277  0.0202  146 GLN A OE1 
1178 N NE2 . GLN A 148 ? 0.9894 1.1029 0.7350 -0.2199 0.0991  0.0082  146 GLN A NE2 
1179 N N   . ASN A 149 ? 0.6290 0.9901 0.5704 -0.1302 0.0978  -0.0828 147 ASN A N   
1180 C CA  . ASN A 149 ? 0.6343 1.0022 0.6209 -0.0989 0.0847  -0.1021 147 ASN A CA  
1181 C C   . ASN A 149 ? 0.5970 1.0149 0.5973 -0.0646 0.0867  -0.1273 147 ASN A C   
1182 O O   . ASN A 149 ? 0.5908 0.9861 0.5683 -0.0466 0.0825  -0.1358 147 ASN A O   
1183 C CB  . ASN A 149 ? 0.6158 0.9051 0.5992 -0.0868 0.0668  -0.0987 147 ASN A CB  
1184 C CG  . ASN A 149 ? 0.6351 0.8739 0.5987 -0.1158 0.0660  -0.0766 147 ASN A CG  
1185 O OD1 . ASN A 149 ? 0.6218 0.8622 0.6067 -0.1265 0.0632  -0.0738 147 ASN A OD1 
1186 N ND2 . ASN A 149 ? 0.7013 0.8946 0.6199 -0.1280 0.0680  -0.0613 147 ASN A ND2 
1187 N N   . SER A 150 ? 0.5560 1.0444 0.5914 -0.0548 0.0926  -0.1401 148 SER A N   
1188 C CA  . SER A 150 ? 0.5506 1.0971 0.5963 -0.0209 0.0978  -0.1657 148 SER A CA  
1189 C C   . SER A 150 ? 0.5474 1.0513 0.6059 0.0211  0.0784  -0.1881 148 SER A C   
1190 O O   . SER A 150 ? 0.5365 1.0693 0.5939 0.0531  0.0797  -0.2126 148 SER A O   
1191 C CB  . SER A 150 ? 0.5761 1.2170 0.6575 -0.0214 0.1096  -0.1714 148 SER A CB  
1192 O OG  . SER A 150 ? 0.7001 1.3291 0.8163 -0.0218 0.0969  -0.1671 148 SER A OG  
1193 N N   . HIS A 151 ? 0.5100 0.9463 0.5784 0.0209  0.0607  -0.1809 149 HIS A N   
1194 C CA  . HIS A 151 ? 0.4967 0.8858 0.5741 0.0530  0.0412  -0.1986 149 HIS A CA  
1195 C C   . HIS A 151 ? 0.5321 0.8458 0.5930 0.0397  0.0283  -0.1851 149 HIS A C   
1196 O O   . HIS A 151 ? 0.5373 0.8311 0.5905 0.0120  0.0317  -0.1624 149 HIS A O   
1197 C CB  . HIS A 151 ? 0.5282 0.9219 0.6444 0.0726  0.0299  -0.2053 149 HIS A CB  
1198 C CG  . HIS A 151 ? 0.5823 1.0581 0.7215 0.0904  0.0405  -0.2183 149 HIS A CG  
1199 N ND1 . HIS A 151 ? 0.6643 1.2099 0.8126 0.0646  0.0579  -0.2055 149 HIS A ND1 
1200 C CD2 . HIS A 151 ? 0.6465 1.1499 0.7990 0.1326  0.0364  -0.2442 149 HIS A CD2 
1201 C CE1 . HIS A 151 ? 0.6879 1.3105 0.8604 0.0902  0.0644  -0.2221 149 HIS A CE1 
1202 N NE2 . HIS A 151 ? 0.6610 1.2581 0.8353 0.1350  0.0517  -0.2464 149 HIS A NE2 
1203 N N   . SER A 152 ? 0.4904 0.7633 0.5452 0.0598  0.0129  -0.2001 150 SER A N   
1204 C CA  . SER A 152 ? 0.5272 0.7399 0.5764 0.0489  -0.0009 -0.1879 150 SER A CA  
1205 C C   . SER A 152 ? 0.5233 0.7102 0.6029 0.0471  -0.0115 -0.1793 150 SER A C   
1206 O O   . SER A 152 ? 0.4875 0.6924 0.5906 0.0614  -0.0137 -0.1873 150 SER A O   
1207 C CB  . SER A 152 ? 0.5444 0.7273 0.5772 0.0645  -0.0151 -0.2055 150 SER A CB  
1208 O OG  . SER A 152 ? 0.6276 0.7967 0.6757 0.0893  -0.0284 -0.2282 150 SER A OG  
1209 N N   . TYR A 153 ? 0.4737 0.6222 0.5512 0.0311  -0.0178 -0.1621 151 TYR A N   
1210 C CA  . TYR A 153 ? 0.5145 0.6437 0.6146 0.0241  -0.0240 -0.1495 151 TYR A CA  
1211 C C   . TYR A 153 ? 0.5016 0.5896 0.5979 0.0157  -0.0341 -0.1387 151 TYR A C   
1212 O O   . TYR A 153 ? 0.5347 0.6144 0.6097 0.0110  -0.0330 -0.1353 151 TYR A O   
1213 C CB  . TYR A 153 ? 0.4910 0.6443 0.5930 0.0054  -0.0107 -0.1341 151 TYR A CB  
1214 C CG  . TYR A 153 ? 0.5039 0.6529 0.5755 -0.0146 0.0008  -0.1209 151 TYR A CG  
1215 C CD1 . TYR A 153 ? 0.5226 0.7023 0.5733 -0.0184 0.0132  -0.1245 151 TYR A CD1 
1216 C CD2 . TYR A 153 ? 0.5105 0.6228 0.5704 -0.0280 -0.0009 -0.1044 151 TYR A CD2 
1217 C CE1 . TYR A 153 ? 0.5332 0.6994 0.5496 -0.0376 0.0222  -0.1094 151 TYR A CE1 
1218 C CE2 . TYR A 153 ? 0.5330 0.6301 0.5592 -0.0426 0.0076  -0.0919 151 TYR A CE2 
1219 C CZ  . TYR A 153 ? 0.5574 0.6776 0.5608 -0.0484 0.0182  -0.0932 151 TYR A CZ  
1220 O OH  . TYR A 153 ? 0.6045 0.7006 0.5689 -0.0636 0.0250  -0.0779 151 TYR A OH  
1221 N N   . CYS A 154 ? 0.4793 0.5463 0.5959 0.0144  -0.0438 -0.1323 152 CYS A N   
1222 C CA  . CYS A 154 ? 0.4574 0.4967 0.5761 0.0060  -0.0525 -0.1218 152 CYS A CA  
1223 C C   . CYS A 154 ? 0.4961 0.5302 0.6268 -0.0044 -0.0500 -0.1050 152 CYS A C   
1224 O O   . CYS A 154 ? 0.4553 0.4881 0.6027 -0.0011 -0.0550 -0.1046 152 CYS A O   
1225 C CB  . CYS A 154 ? 0.4574 0.4739 0.5860 0.0127  -0.0699 -0.1328 152 CYS A CB  
1226 S SG  . CYS A 154 ? 0.4820 0.4838 0.6135 -0.0007 -0.0794 -0.1218 152 CYS A SG  
1227 N N   . PHE A 155 ? 0.4832 0.5131 0.6017 -0.0145 -0.0429 -0.0918 153 PHE A N   
1228 C CA  . PHE A 155 ? 0.4494 0.4728 0.5749 -0.0229 -0.0411 -0.0783 153 PHE A CA  
1229 C C   . PHE A 155 ? 0.4756 0.4874 0.6176 -0.0237 -0.0521 -0.0734 153 PHE A C   
1230 O O   . PHE A 155 ? 0.4884 0.4972 0.6316 -0.0221 -0.0592 -0.0768 153 PHE A O   
1231 C CB  . PHE A 155 ? 0.4355 0.4512 0.5378 -0.0299 -0.0309 -0.0683 153 PHE A CB  
1232 C CG  . PHE A 155 ? 0.4473 0.4690 0.5288 -0.0365 -0.0204 -0.0696 153 PHE A CG  
1233 C CD1 . PHE A 155 ? 0.4476 0.4896 0.5376 -0.0434 -0.0164 -0.0722 153 PHE A CD1 
1234 C CD2 . PHE A 155 ? 0.4763 0.4860 0.5288 -0.0371 -0.0151 -0.0668 153 PHE A CD2 
1235 C CE1 . PHE A 155 ? 0.4963 0.5515 0.5684 -0.0554 -0.0059 -0.0721 153 PHE A CE1 
1236 C CE2 . PHE A 155 ? 0.5166 0.5295 0.5456 -0.0490 -0.0048 -0.0649 153 PHE A CE2 
1237 C CZ  . PHE A 155 ? 0.5116 0.5499 0.5518 -0.0603 0.0005  -0.0677 153 PHE A CZ  
1238 N N   . GLU A 156 ? 0.3954 0.4042 0.5495 -0.0284 -0.0542 -0.0645 154 GLU A N   
1239 C CA  . GLU A 156 ? 0.4696 0.4704 0.6371 -0.0346 -0.0625 -0.0555 154 GLU A CA  
1240 C C   . GLU A 156 ? 0.4507 0.4551 0.6177 -0.0417 -0.0567 -0.0411 154 GLU A C   
1241 O O   . GLU A 156 ? 0.4462 0.4532 0.6102 -0.0414 -0.0537 -0.0399 154 GLU A O   
1242 C CB  . GLU A 156 ? 0.4281 0.4116 0.6087 -0.0325 -0.0770 -0.0608 154 GLU A CB  
1243 C CG  . GLU A 156 ? 0.4330 0.4058 0.6245 -0.0454 -0.0871 -0.0516 154 GLU A CG  
1244 C CD  . GLU A 156 ? 0.4636 0.4052 0.6614 -0.0471 -0.1021 -0.0510 154 GLU A CD  
1245 O OE1 . GLU A 156 ? 0.4525 0.3836 0.6480 -0.0328 -0.1046 -0.0574 154 GLU A OE1 
1246 O OE2 . GLU A 156 ? 0.4778 0.4058 0.6821 -0.0628 -0.1121 -0.0438 154 GLU A OE2 
1247 N N   . ILE A 157 ? 0.4436 0.4542 0.6142 -0.0479 -0.0557 -0.0309 155 ILE A N   
1248 C CA  . ILE A 157 ? 0.4322 0.4492 0.6011 -0.0541 -0.0505 -0.0175 155 ILE A CA  
1249 C C   . ILE A 157 ? 0.4649 0.4840 0.6505 -0.0657 -0.0588 -0.0059 155 ILE A C   
1250 O O   . ILE A 157 ? 0.5047 0.5333 0.7008 -0.0707 -0.0630 -0.0059 155 ILE A O   
1251 C CB  . ILE A 157 ? 0.4386 0.4663 0.5918 -0.0495 -0.0384 -0.0153 155 ILE A CB  
1252 C CG1 . ILE A 157 ? 0.4711 0.4858 0.6012 -0.0432 -0.0312 -0.0241 155 ILE A CG1 
1253 C CG2 . ILE A 157 ? 0.4284 0.4655 0.5776 -0.0545 -0.0328 -0.0037 155 ILE A CG2 
1254 C CD1 . ILE A 157 ? 0.4608 0.4715 0.5685 -0.0343 -0.0219 -0.0237 155 ILE A CD1 
1255 N N   . LEU A 158 ? 0.4240 0.4357 0.6104 -0.0720 -0.0621 0.0051  156 LEU A N   
1256 C CA  . LEU A 158 ? 0.4504 0.4603 0.6467 -0.0875 -0.0691 0.0209  156 LEU A CA  
1257 C C   . LEU A 158 ? 0.5220 0.5521 0.7097 -0.0933 -0.0589 0.0359  156 LEU A C   
1258 O O   . LEU A 158 ? 0.4858 0.5180 0.6585 -0.0851 -0.0519 0.0334  156 LEU A O   
1259 C CB  . LEU A 158 ? 0.4845 0.4591 0.6834 -0.0889 -0.0848 0.0234  156 LEU A CB  
1260 C CG  . LEU A 158 ? 0.5099 0.4602 0.7134 -0.0804 -0.0962 0.0059  156 LEU A CG  
1261 C CD1 . LEU A 158 ? 0.4683 0.4183 0.6660 -0.0600 -0.0937 -0.0085 156 LEU A CD1 
1262 C CD2 . LEU A 158 ? 0.4884 0.3972 0.6936 -0.0896 -0.1144 0.0126  156 LEU A CD2 
1263 N N   . GLU A 159 ? 0.5320 0.5790 0.7277 -0.1095 -0.0584 0.0516  157 GLU A N   
1264 C CA  . GLU A 159 ? 0.4861 0.5573 0.6718 -0.1155 -0.0480 0.0667  157 GLU A CA  
1265 C C   . GLU A 159 ? 0.5868 0.6514 0.7769 -0.1385 -0.0561 0.0892  157 GLU A C   
1266 O O   . GLU A 159 ? 0.5869 0.6428 0.7920 -0.1546 -0.0661 0.0936  157 GLU A O   
1267 C CB  . GLU A 159 ? 0.4710 0.5857 0.6581 -0.1098 -0.0329 0.0637  157 GLU A CB  
1268 C CG  . GLU A 159 ? 0.5311 0.6418 0.6982 -0.0876 -0.0230 0.0476  157 GLU A CG  
1269 C CD  . GLU A 159 ? 0.4769 0.6203 0.6416 -0.0737 -0.0106 0.0418  157 GLU A CD  
1270 O OE1 . GLU A 159 ? 0.5554 0.7393 0.7366 -0.0813 -0.0071 0.0516  157 GLU A OE1 
1271 O OE2 . GLU A 159 ? 0.4905 0.6193 0.6359 -0.0553 -0.0051 0.0279  157 GLU A OE2 
1272 N N   . ARG A 160 ? 0.5406 0.6069 0.7142 -0.1422 -0.0529 0.1040  158 ARG A N   
1273 C CA  . ARG A 160 ? 0.6079 0.6626 0.7784 -0.1652 -0.0608 0.1296  158 ARG A CA  
1274 C C   . ARG A 160 ? 0.6637 0.7619 0.8464 -0.1886 -0.0518 0.1443  158 ARG A C   
1275 O O   . ARG A 160 ? 0.6581 0.8082 0.8415 -0.1826 -0.0343 0.1413  158 ARG A O   
1276 C CB  . ARG A 160 ? 0.6223 0.6741 0.7682 -0.1621 -0.0592 0.1428  158 ARG A CB  
1277 C CG  . ARG A 160 ? 0.6587 0.6766 0.7950 -0.1806 -0.0735 0.1692  158 ARG A CG  
1278 C CD  . ARG A 160 ? 0.6683 0.6912 0.7777 -0.1782 -0.0718 0.1848  158 ARG A CD  
1279 N NE  . ARG A 160 ? 0.6929 0.6896 0.7947 -0.1546 -0.0832 0.1726  158 ARG A NE  
1280 C CZ  . ARG A 160 ? 0.6839 0.6333 0.7831 -0.1478 -0.1035 0.1788  158 ARG A CZ  
1281 N NH1 . ARG A 160 ? 0.7502 0.6592 0.8485 -0.1645 -0.1162 0.1973  158 ARG A NH1 
1282 N NH2 . ARG A 160 ? 0.6997 0.6424 0.7964 -0.1240 -0.1118 0.1659  158 ARG A NH2 
1283 N N   . ARG A 161 ? 0.6693 0.7466 0.8607 -0.2156 -0.0644 0.1598  159 ARG A N   
1284 C CA  . ARG A 161 ? 0.6499 0.7739 0.8537 -0.2456 -0.0570 0.1785  159 ARG A CA  
1285 C C   . ARG A 161 ? 0.7827 0.9291 0.9657 -0.2569 -0.0463 0.2036  159 ARG A C   
1286 O O   . ARG A 161 ? 0.9053 1.0278 1.0778 -0.2852 -0.0548 0.2303  159 ARG A O   
1287 C CB  . ARG A 161 ? 0.7352 0.8228 0.9499 -0.2772 -0.0757 0.1883  159 ARG A CB  
1288 C CG  . ARG A 161 ? 0.7021 0.7643 0.9319 -0.2657 -0.0879 0.1620  159 ARG A CG  
1289 C CD  . ARG A 161 ? 0.7357 0.7715 0.9709 -0.2963 -0.1035 0.1667  159 ARG A CD  
1290 N NE  . ARG A 161 ? 0.8524 0.8390 1.0899 -0.2830 -0.1202 0.1421  159 ARG A NE  
1291 C CZ  . ARG A 161 ? 0.8496 0.8618 1.1048 -0.2829 -0.1222 0.1231  159 ARG A CZ  
1292 N NH1 . ARG A 161 ? 0.7362 0.8240 1.0113 -0.2944 -0.1096 0.1268  159 ARG A NH1 
1293 N NH2 . ARG A 161 ? 0.8171 0.7828 1.0689 -0.2694 -0.1371 0.1001  159 ARG A NH2 
1294 O OXT . ARG A 161 ? 0.9617 1.1465 1.1334 -0.2378 -0.0296 0.1979  159 ARG A OXT 
# 
