data_7GV5
# 
_entry.id   7GV5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7GV5         pdb_00007gv5 10.2210/pdb7gv5/pdb 
WWPDB D_1001406676 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-12-04 
2 'Structure model' 1 1 2025-01-01 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_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.country'                 
2 2 'Structure model' '_citation.journal_id_CSD'          
3 2 'Structure model' '_citation.journal_id_ISSN'         
4 2 'Structure model' '_citation.journal_volume'          
5 2 'Structure model' '_citation.page_first'              
6 2 'Structure model' '_citation.page_last'               
7 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8 2 'Structure model' '_citation.title'                   
9 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.entry_id                        7GV5 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              Rob.vanMontfort@icr.ac.uk 
_pdbx_contact_author.name_first         Rob 
_pdbx_contact_author.name_last          'van Montfort' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodrigues, M.J.'      1 0000-0003-1243-903X 
'Le Bihan, Y.V.'       2 0000-0002-6850-9706 
'van Montfort, R.L.M.' 3 0000-0002-5688-3450 
# 
_citation.id                        primary 
_citation.title                     
'Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.' 
_citation.journal_abbrev            J.Appl.Crystallogr. 
_citation.journal_volume            57 
_citation.page_first                1951 
_citation.page_last                 1965 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39628887 
_citation.pdbx_database_id_DOI      10.1107/S1600576724010549 
_citation.journal_id_ASTM           JACGAR 
_citation.country                   DK 
_citation.journal_id_ISSN           0021-8898 
_citation.journal_id_CSD            0228 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodrigues, M.J.'      1 0000-0003-1243-903X 
primary 'Cabry, M.'            2 0000-0002-9070-5498 
primary 'Collie, G.'           3 0000-0002-0406-922X 
primary 'Carter, M.'           4 ?                   
primary 'McAndrew, C.'         5 0000-0002-1366-088X 
primary 'Owen, R.L.'           6 0000-0002-2104-7057 
primary 'Bellenie, B.R.'       7 0000-0001-9987-3079 
primary 'Le Bihan, Y.V.'       8 0000-0002-6850-9706 
primary 'van Montfort, R.L.M.' 9 0000-0002-5688-3450 
# 
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 'B-cell lymphoma 6 protein'                                            14536.915 1   ? ? ? ? 
2 polymer     syn 'WVIP tetrapeptide'                                                    610.744   1   ? ? ? ? 
3 non-polymer syn '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' 339.575   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                         35.453    1   ? ? ? ? 
5 non-polymer nat 'DIMETHYL SULFOXIDE'                                                   78.133    1   ? ? ? ? 
6 water       nat water                                                                  18.015    185 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'BCL-6,B-cell lymphoma 5 protein,BCL-5,Protein LAZ-3,Zinc finger and BTB domain-containing protein 27,Zinc finger protein 51' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
A ? 
2 'polypeptide(L)' no yes '(ACE)WVIPA' XWVIPA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' A1ACA 
4 'CHLORIDE ION'                                                         CL    
5 'DIMETHYL SULFOXIDE'                                                   DMS   
6 water                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   ALA n 
1 5   ASP n 
1 6   SER n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  PHE n 
1 11  THR n 
1 12  ARG n 
1 13  HIS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  LEU n 
1 19  LEU n 
1 20  ASN n 
1 21  LEU n 
1 22  ASN n 
1 23  ARG n 
1 24  LEU n 
1 25  ARG n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  THR n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  ILE n 
1 36  VAL n 
1 37  VAL n 
1 38  SER n 
1 39  ARG n 
1 40  GLU n 
1 41  GLN n 
1 42  PHE n 
1 43  ARG n 
1 44  ALA n 
1 45  HIS n 
1 46  LYS n 
1 47  THR n 
1 48  VAL n 
1 49  LEU n 
1 50  MET n 
1 51  ALA n 
1 52  CYS n 
1 53  SER n 
1 54  GLY n 
1 55  LEU n 
1 56  PHE n 
1 57  TYR n 
1 58  SER n 
1 59  ILE n 
1 60  PHE n 
1 61  THR n 
1 62  ASP n 
1 63  GLN n 
1 64  LEU n 
1 65  LYS n 
1 66  CYS n 
1 67  ASN n 
1 68  LEU n 
1 69  SER n 
1 70  VAL n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ASP n 
1 75  PRO n 
1 76  GLU n 
1 77  ILE n 
1 78  ASN n 
1 79  PRO n 
1 80  GLU n 
1 81  GLY n 
1 82  PHE n 
1 83  CYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  ASP n 
1 88  PHE n 
1 89  MET n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ARG n 
1 94  LEU n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLU n 
1 99  GLY n 
1 100 ASN n 
1 101 ILE n 
1 102 MET n 
1 103 ALA n 
1 104 VAL n 
1 105 MET n 
1 106 ALA n 
1 107 THR n 
1 108 ALA n 
1 109 MET n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 MET n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 VAL n 
1 118 ASP n 
1 119 THR n 
1 120 CYS n 
1 121 ARG n 
1 122 LYS n 
1 123 PHE n 
1 124 ILE n 
1 125 LYS n 
1 126 ALA n 
1 127 SER n 
1 128 GLU n 
2 1   ACE n 
2 2   TRP n 
2 3   VAL n 
2 4   ILE n 
2 5   PRO n 
2 6   ALA 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                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCL6, BCL5, LAZ3, ZBTB27, ZNF51' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21-AI 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET48b 
_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_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 6 'synthetic construct' ? 32630 ? 
3 2 sample ? ? 'synthetic construct' ? 32630 ? 
# 
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 
A1ACA non-polymer         . '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' ? 'C12 H8 Br Cl N4 O' 339.575 
ACE   non-polymer         . 'ACETYL GROUP'                                                         ? 'C2 H4 O'           44.053  
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 
CL    non-polymer         . 'CHLORIDE ION'                                                         ? 'Cl -1'             35.453  
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'      121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                   ? 'C2 H6 O S'         78.133  
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   GLY 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLY 3   4   ?   ?   ?   A . n 
A 1 4   ALA 4   5   ?   ?   ?   A . n 
A 1 5   ASP 5   6   6   ASP ASP A . n 
A 1 6   SER 6   7   7   SER SER A . n 
A 1 7   CYS 7   8   8   CYS CYS A . n 
A 1 8   ILE 8   9   9   ILE ILE A . n 
A 1 9   GLN 9   10  10  GLN GLN A . n 
A 1 10  PHE 10  11  11  PHE PHE A . n 
A 1 11  THR 11  12  12  THR THR A . n 
A 1 12  ARG 12  13  13  ARG ARG A . n 
A 1 13  HIS 13  14  14  HIS HIS A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ASP 16  17  17  ASP ASP A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  ASN 20  21  21  ASN ASN A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  ARG 23  24  24  ARG ARG A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  ARG 25  26  26  ARG ARG A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  THR 31  32  32  THR THR A . n 
A 1 32  ASP 32  33  33  ASP ASP A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  VAL 36  37  37  VAL VAL A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  SER 38  39  39  SER SER A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLN 41  42  42  GLN GLN A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  ALA 44  45  45  ALA ALA A . n 
A 1 45  HIS 45  46  46  HIS HIS A . n 
A 1 46  LYS 46  47  47  LYS LYS A . n 
A 1 47  THR 47  48  48  THR THR A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  MET 50  51  51  MET MET A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  CYS 52  53  53  CYS CYS A . n 
A 1 53  SER 53  54  54  SER SER A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  PHE 60  61  61  PHE PHE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  ASN 67  68  68  ASN ASN A . n 
A 1 68  LEU 68  69  69  LEU LEU A . n 
A 1 69  SER 69  70  70  SER SER A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ILE 71  72  72  ILE ILE A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  ASP 74  75  75  ASP ASP A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLU 76  77  77  GLU GLU A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  PRO 79  80  80  PRO PRO A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  CYS 83  84  84  CYS CYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  LEU 85  86  86  LEU LEU A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  PHE 88  89  89  PHE PHE A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  ASN 95  96  96  ASN ASN A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ARG 97  98  98  ARG ARG A . n 
A 1 98  GLU 98  99  99  GLU GLU A . n 
A 1 99  GLY 99  100 100 GLY GLY A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 MET 102 103 103 MET MET A . n 
A 1 103 ALA 103 104 104 ALA ALA A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 MET 105 106 106 MET MET A . n 
A 1 106 ALA 106 107 107 ALA ALA A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 MET 109 110 110 MET MET A . n 
A 1 110 TYR 110 111 111 TYR TYR A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLN 112 113 113 GLN GLN A . n 
A 1 113 MET 113 114 114 MET MET A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 HIS 115 116 116 HIS HIS A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 VAL 117 118 118 VAL VAL A . n 
A 1 118 ASP 118 119 119 ASP ASP A . n 
A 1 119 THR 119 120 120 THR THR A . n 
A 1 120 CYS 120 121 121 CYS CYS A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 PHE 123 124 124 PHE PHE A . n 
A 1 124 ILE 124 125 125 ILE ILE A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 SER 127 128 128 SER SER A . n 
A 1 128 GLU 128 129 129 GLU GLU A . n 
B 2 1   ACE 1   0   0   ACE ACE D . n 
B 2 2   TRP 2   1   1   TRP TRP D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ILE 4   3   3   ILE ILE D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   ALA 6   5   5   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1ACA 1   201 1   A1ACA 763 A . 
D 4 CL    1   202 1   CL    CL  A . 
E 5 DMS   1   101 1   DMS   DMS D . 
F 6 HOH   1   301 7   HOH   HOH A . 
F 6 HOH   2   302 178 HOH   HOH A . 
F 6 HOH   3   303 45  HOH   HOH A . 
F 6 HOH   4   304 19  HOH   HOH A . 
F 6 HOH   5   305 166 HOH   HOH A . 
F 6 HOH   6   306 94  HOH   HOH A . 
F 6 HOH   7   307 140 HOH   HOH A . 
F 6 HOH   8   308 173 HOH   HOH A . 
F 6 HOH   9   309 29  HOH   HOH A . 
F 6 HOH   10  310 47  HOH   HOH A . 
F 6 HOH   11  311 90  HOH   HOH A . 
F 6 HOH   12  312 139 HOH   HOH A . 
F 6 HOH   13  313 100 HOH   HOH A . 
F 6 HOH   14  314 179 HOH   HOH A . 
F 6 HOH   15  315 83  HOH   HOH A . 
F 6 HOH   16  316 84  HOH   HOH A . 
F 6 HOH   17  317 142 HOH   HOH A . 
F 6 HOH   18  318 99  HOH   HOH A . 
F 6 HOH   19  319 106 HOH   HOH A . 
F 6 HOH   20  320 40  HOH   HOH A . 
F 6 HOH   21  321 132 HOH   HOH A . 
F 6 HOH   22  322 101 HOH   HOH A . 
F 6 HOH   23  323 87  HOH   HOH A . 
F 6 HOH   24  324 75  HOH   HOH A . 
F 6 HOH   25  325 27  HOH   HOH A . 
F 6 HOH   26  326 202 HOH   HOH A . 
F 6 HOH   27  327 247 HOH   HOH A . 
F 6 HOH   28  328 14  HOH   HOH A . 
F 6 HOH   29  329 37  HOH   HOH A . 
F 6 HOH   30  330 193 HOH   HOH A . 
F 6 HOH   31  331 237 HOH   HOH A . 
F 6 HOH   32  332 91  HOH   HOH A . 
F 6 HOH   33  333 119 HOH   HOH A . 
F 6 HOH   34  334 5   HOH   HOH A . 
F 6 HOH   35  335 42  HOH   HOH A . 
F 6 HOH   36  336 17  HOH   HOH A . 
F 6 HOH   37  337 239 HOH   HOH A . 
F 6 HOH   38  338 117 HOH   HOH A . 
F 6 HOH   39  339 34  HOH   HOH A . 
F 6 HOH   40  340 242 HOH   HOH A . 
F 6 HOH   41  341 243 HOH   HOH A . 
F 6 HOH   42  342 144 HOH   HOH A . 
F 6 HOH   43  343 86  HOH   HOH A . 
F 6 HOH   44  344 6   HOH   HOH A . 
F 6 HOH   45  345 30  HOH   HOH A . 
F 6 HOH   46  346 44  HOH   HOH A . 
F 6 HOH   47  347 4   HOH   HOH A . 
F 6 HOH   48  348 180 HOH   HOH A . 
F 6 HOH   49  349 12  HOH   HOH A . 
F 6 HOH   50  350 89  HOH   HOH A . 
F 6 HOH   51  351 96  HOH   HOH A . 
F 6 HOH   52  352 133 HOH   HOH A . 
F 6 HOH   53  353 145 HOH   HOH A . 
F 6 HOH   54  354 20  HOH   HOH A . 
F 6 HOH   55  355 85  HOH   HOH A . 
F 6 HOH   56  356 24  HOH   HOH A . 
F 6 HOH   57  357 124 HOH   HOH A . 
F 6 HOH   58  358 175 HOH   HOH A . 
F 6 HOH   59  359 97  HOH   HOH A . 
F 6 HOH   60  360 244 HOH   HOH A . 
F 6 HOH   61  361 141 HOH   HOH A . 
F 6 HOH   62  362 170 HOH   HOH A . 
F 6 HOH   63  363 93  HOH   HOH A . 
F 6 HOH   64  364 51  HOH   HOH A . 
F 6 HOH   65  365 196 HOH   HOH A . 
F 6 HOH   66  366 207 HOH   HOH A . 
F 6 HOH   67  367 28  HOH   HOH A . 
F 6 HOH   68  368 122 HOH   HOH A . 
F 6 HOH   69  369 192 HOH   HOH A . 
F 6 HOH   70  370 103 HOH   HOH A . 
F 6 HOH   71  371 50  HOH   HOH A . 
F 6 HOH   72  372 15  HOH   HOH A . 
F 6 HOH   73  373 76  HOH   HOH A . 
F 6 HOH   74  374 131 HOH   HOH A . 
F 6 HOH   75  375 25  HOH   HOH A . 
F 6 HOH   76  376 151 HOH   HOH A . 
F 6 HOH   77  377 186 HOH   HOH A . 
F 6 HOH   78  378 157 HOH   HOH A . 
F 6 HOH   79  379 21  HOH   HOH A . 
F 6 HOH   80  380 241 HOH   HOH A . 
F 6 HOH   81  381 245 HOH   HOH A . 
F 6 HOH   82  382 55  HOH   HOH A . 
F 6 HOH   83  383 167 HOH   HOH A . 
F 6 HOH   84  384 70  HOH   HOH A . 
F 6 HOH   85  385 177 HOH   HOH A . 
F 6 HOH   86  386 39  HOH   HOH A . 
F 6 HOH   87  387 108 HOH   HOH A . 
F 6 HOH   88  388 194 HOH   HOH A . 
F 6 HOH   89  389 105 HOH   HOH A . 
F 6 HOH   90  390 16  HOH   HOH A . 
F 6 HOH   91  391 229 HOH   HOH A . 
F 6 HOH   92  392 191 HOH   HOH A . 
F 6 HOH   93  393 185 HOH   HOH A . 
F 6 HOH   94  394 69  HOH   HOH A . 
F 6 HOH   95  395 169 HOH   HOH A . 
F 6 HOH   96  396 74  HOH   HOH A . 
F 6 HOH   97  397 205 HOH   HOH A . 
F 6 HOH   98  398 129 HOH   HOH A . 
F 6 HOH   99  399 64  HOH   HOH A . 
F 6 HOH   100 400 32  HOH   HOH A . 
F 6 HOH   101 401 22  HOH   HOH A . 
F 6 HOH   102 402 92  HOH   HOH A . 
F 6 HOH   103 403 165 HOH   HOH A . 
F 6 HOH   104 404 212 HOH   HOH A . 
F 6 HOH   105 405 223 HOH   HOH A . 
F 6 HOH   106 406 120 HOH   HOH A . 
F 6 HOH   107 407 82  HOH   HOH A . 
F 6 HOH   108 408 35  HOH   HOH A . 
F 6 HOH   109 409 43  HOH   HOH A . 
F 6 HOH   110 410 174 HOH   HOH A . 
F 6 HOH   111 411 26  HOH   HOH A . 
F 6 HOH   112 412 176 HOH   HOH A . 
F 6 HOH   113 413 60  HOH   HOH A . 
F 6 HOH   114 414 36  HOH   HOH A . 
F 6 HOH   115 415 46  HOH   HOH A . 
F 6 HOH   116 416 61  HOH   HOH A . 
F 6 HOH   117 417 190 HOH   HOH A . 
F 6 HOH   118 418 236 HOH   HOH A . 
F 6 HOH   119 419 67  HOH   HOH A . 
F 6 HOH   120 420 215 HOH   HOH A . 
F 6 HOH   121 421 88  HOH   HOH A . 
F 6 HOH   122 422 65  HOH   HOH A . 
F 6 HOH   123 423 204 HOH   HOH A . 
F 6 HOH   124 424 57  HOH   HOH A . 
F 6 HOH   125 425 56  HOH   HOH A . 
F 6 HOH   126 426 41  HOH   HOH A . 
F 6 HOH   127 427 110 HOH   HOH A . 
F 6 HOH   128 428 68  HOH   HOH A . 
F 6 HOH   129 429 95  HOH   HOH A . 
F 6 HOH   130 430 214 HOH   HOH A . 
F 6 HOH   131 431 147 HOH   HOH A . 
F 6 HOH   132 432 200 HOH   HOH A . 
F 6 HOH   133 433 116 HOH   HOH A . 
F 6 HOH   134 434 187 HOH   HOH A . 
F 6 HOH   135 435 135 HOH   HOH A . 
F 6 HOH   136 436 168 HOH   HOH A . 
F 6 HOH   137 437 228 HOH   HOH A . 
F 6 HOH   138 438 248 HOH   HOH A . 
F 6 HOH   139 439 123 HOH   HOH A . 
F 6 HOH   140 440 227 HOH   HOH A . 
F 6 HOH   141 441 121 HOH   HOH A . 
F 6 HOH   142 442 231 HOH   HOH A . 
F 6 HOH   143 443 171 HOH   HOH A . 
F 6 HOH   144 444 225 HOH   HOH A . 
F 6 HOH   145 445 63  HOH   HOH A . 
F 6 HOH   146 446 71  HOH   HOH A . 
F 6 HOH   147 447 220 HOH   HOH A . 
F 6 HOH   148 448 234 HOH   HOH A . 
F 6 HOH   149 449 203 HOH   HOH A . 
F 6 HOH   150 450 125 HOH   HOH A . 
F 6 HOH   151 451 217 HOH   HOH A . 
F 6 HOH   152 452 181 HOH   HOH A . 
F 6 HOH   153 453 235 HOH   HOH A . 
F 6 HOH   154 454 158 HOH   HOH A . 
F 6 HOH   155 455 114 HOH   HOH A . 
F 6 HOH   156 456 79  HOH   HOH A . 
F 6 HOH   157 457 81  HOH   HOH A . 
F 6 HOH   158 458 238 HOH   HOH A . 
F 6 HOH   159 459 221 HOH   HOH A . 
F 6 HOH   160 460 246 HOH   HOH A . 
F 6 HOH   161 461 115 HOH   HOH A . 
F 6 HOH   162 462 216 HOH   HOH A . 
F 6 HOH   163 463 107 HOH   HOH A . 
F 6 HOH   164 464 230 HOH   HOH A . 
F 6 HOH   165 465 183 HOH   HOH A . 
F 6 HOH   166 466 182 HOH   HOH A . 
F 6 HOH   167 467 188 HOH   HOH A . 
F 6 HOH   168 468 201 HOH   HOH A . 
F 6 HOH   169 469 213 HOH   HOH A . 
F 6 HOH   170 470 48  HOH   HOH A . 
F 6 HOH   171 471 148 HOH   HOH A . 
F 6 HOH   172 472 113 HOH   HOH A . 
F 6 HOH   173 473 206 HOH   HOH A . 
F 6 HOH   174 474 172 HOH   HOH A . 
F 6 HOH   175 475 211 HOH   HOH A . 
G 6 HOH   1   201 62  HOH   HOH D . 
G 6 HOH   2   202 23  HOH   HOH D . 
G 6 HOH   3   203 78  HOH   HOH D . 
G 6 HOH   4   204 38  HOH   HOH D . 
G 6 HOH   5   205 73  HOH   HOH D . 
G 6 HOH   6   206 53  HOH   HOH D . 
G 6 HOH   7   207 240 HOH   HOH D . 
G 6 HOH   8   208 49  HOH   HOH D . 
G 6 HOH   9   209 58  HOH   HOH D . 
G 6 HOH   10  210 195 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 A LYS 126 ? CG  ? A LYS 125 CG  
8  1 Y 1 A LYS 126 ? CD  ? A LYS 125 CD  
9  1 Y 1 A LYS 126 ? CE  ? A LYS 125 CE  
10 1 Y 1 A LYS 126 ? NZ  ? A LYS 125 NZ  
11 1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
12 1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
13 1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
14 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com phasing           
http://www.globalphasing.com/buster/                ?   ? 
5 PDB_EXTRACT 3.24   'Sep. 1, 2017' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.entry_id           7GV5 
_cell.length_a           67.660 
_cell.length_b           67.660 
_cell.length_c           166.650 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        120.000 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7GV5 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_H-M             'P 61 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.entry_id          7GV5 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.63 
_exptl_crystal.density_percent_sol   66.16 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    '1.0 M K2HPO4, 0.7 M NaH2PO4, 75 mM sodium acetate pH 4.5, 2% DMSO' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2017-07-31 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9686 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I24' 
_diffrn_source.pdbx_wavelength_list        0.9686 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7GV5 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.950 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23668 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.082 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.300 
_reflns.B_iso_Wilson_estimate        34.800 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.086 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     214435 
_reflns.pdbx_scaling_rejects         881 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.750 1.780  ? 11921 1283 ? 3.211 ? ? ? 9.300 ? 0.800  ? ? ? ? ? ? 100.000 3.395 1.090 0.355 ? 
1 2 9.090 33.950 ? 1487  222  ? 0.027 ? ? ? 6.700 ? 46.300 ? ? ? ? ? ? 98.600  0.029 0.011 0.999 ? 
# 
_refine.entry_id                                 7GV5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             33.9500 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.9000 
_refine.ls_number_reflns_obs                     23620 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1780 
_refine.ls_R_factor_R_work                       0.1760 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2010 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1400 
_refine.ls_number_reflns_R_free                  1215 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               40.0100 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.0109 
_refine.aniso_B[2][2]                            -0.0109 
_refine.aniso_B[3][3]                            0.0218 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9660 
_refine.correlation_coeff_Fo_to_Fc_free          0.9450 
_refine.overall_SU_R_Cruickshank_DPI             0.0850 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0850 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0970 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0930 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                131.700 
_refine.B_iso_min                                21.190 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_analyze.entry_id                        7GV5 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.230 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.7500 
_refine_hist.d_res_low                        33.9500 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             185 
_refine_hist.number_atoms_total               1231 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           34.83 
_refine_hist.pdbx_B_iso_mean_solvent          58.04 
_refine_hist.pdbx_number_atoms_protein        1022 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' t_dihedral_angle_d        445  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              235  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1233 ?      ? 20.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 162  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        8    ?      ? 1.000  HARMONIC     
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1659 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1233 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1689 0.880  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.250  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.760 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.7500 
_refine_ls_shell.d_res_low                        1.8300 
_refine_ls_shell.pdbx_total_number_of_bins_used   12 
_refine_ls_shell.percent_reflns_obs               99.7200 
_refine_ls_shell.number_reflns_R_work             2686 
_refine_ls_shell.R_factor_all                     0.3287 
_refine_ls_shell.R_factor_R_work                  0.3286 
_refine_ls_shell.R_factor_R_free                  0.3314 
_refine_ls_shell.percent_reflns_R_free            4.5800 
_refine_ls_shell.number_reflns_R_free             129 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2815 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GV5 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 17.50 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GV5 
_struct_keywords.text            'transcription factor, radiation damage, ligand, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP BCL6_HUMAN P41182 ? 1 
;ADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPEGFC
ILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
5 
2 PDB 7GV5       7GV5   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7GV5 A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GV5 D 1 ? 6   ? 7GV5   0 ? 5   ? 0 5   
# 
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 7GV5 GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GV5 PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GV5 GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7400  ? 
1 MORE         -64   ? 
1 'SSA (A^2)'  13000 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_545 x,x-y-1,-z+1/6 0.5000000000 0.8660254038 0.0000000000 33.8300000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5952788201 0.0000000000 0.0000000000 -1.0000000000 27.7750000000 
# 
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 ARG A 12  ? ARG A 27  ? ARG A 13  ARG A 28  1 ? 16 
HELX_P HELX_P2 AA2 HIS A 45  ? SER A 53  ? HIS A 46  SER A 54  1 ? 9  
HELX_P HELX_P3 AA3 SER A 53  ? ASP A 62  ? SER A 54  ASP A 63  1 ? 10 
HELX_P HELX_P4 AA4 LEU A 64  ? LEU A 68  ? LEU A 65  LEU A 69  5 ? 5  
HELX_P HELX_P5 AA5 ASN A 78  ? SER A 92  ? ASN A 79  SER A 93  1 ? 15 
HELX_P HELX_P6 AA6 ASN A 100 ? GLN A 112 ? ASN A 101 GLN A 113 1 ? 13 
HELX_P HELX_P7 AA7 MET A 113 ? GLU A 128 ? MET A 114 GLU A 129 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N A ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
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 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
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 PHE A 42 ? O PHE A 43 N ILE A 35 ? N ILE A 36 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GV5 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 39  ? A 61.47   -119.48 
2 1 SER A 39  ? B 37.36   65.78   
3 1 ARG A 40  ? B 75.73   -23.29  
4 1 SER A 93  ? A 74.79   -3.36   
5 1 MET A 114 ? ? -115.03 79.78   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 362 ? F HOH . 
2 1 A HOH 395 ? F HOH . 
3 1 A HOH 453 ? F HOH . 
4 1 A HOH 464 ? F HOH . 
5 1 A HOH 465 ? F HOH . 
6 1 A HOH 468 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.2144 -16.5503 24.6837 0.0123  -0.0514 -0.0662 -0.0408 0.0297  -0.0236 1.0289 1.8592  2.0503 
0.4411 -0.3182 1.2548 0.1358 -0.0758 -0.0599 -0.0526 0.1061  0.0923 0.2529  -0.0036 -0.0174 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1227 0.1110  -0.0438 -0.0270 -0.0159 -0.0951 1.0040 -0.2713 0.0000 
0.0549 -0.0790 0.5245 0.0416 -0.0272 -0.0144 -0.0219 -0.0034 0.0302 -0.0267 -0.0046 -0.0133 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 6 A 129 '{A|6 - 129}' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 D 1 D 5   '{D|1 - 5}'   ? ? ? ? ? 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 2 ? A GLY 1 
2 1 Y 1 A PRO 3 ? A PRO 2 
3 1 Y 1 A GLY 4 ? A GLY 3 
4 1 Y 1 A ALA 5 ? A ALA 4 
# 
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 
A1ACA C4   C  Y N 1   
A1ACA C5   C  Y N 2   
A1ACA C6   C  Y N 3   
A1ACA C7   C  Y N 4   
A1ACA C8   C  N N 5   
A1ACA C10  C  Y N 6   
A1ACA C1   C  Y N 7   
A1ACA C2   C  Y N 8   
A1ACA C3   C  Y N 9   
A1ACA C9   C  N N 10  
A1ACA O    O  N N 11  
A1ACA N2   N  N N 12  
A1ACA C11  C  Y N 13  
A1ACA N1   N  N N 14  
A1ACA N3   N  Y N 15  
A1ACA C    C  Y N 16  
A1ACA CL   CL N N 17  
A1ACA BR   BR N N 18  
A1ACA N    N  Y N 19  
A1ACA H1   H  N N 20  
A1ACA H2   H  N N 21  
A1ACA H3   H  N N 22  
A1ACA H4   H  N N 23  
A1ACA H5   H  N N 24  
A1ACA H6   H  N N 25  
A1ACA H7   H  N N 26  
A1ACA H8   H  N N 27  
ACE   C    C  N N 28  
ACE   O    O  N N 29  
ACE   CH3  C  N N 30  
ACE   H    H  N N 31  
ACE   H1   H  N N 32  
ACE   H2   H  N N 33  
ACE   H3   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CL    CL   CL N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
DMS   S    S  N N 123 
DMS   O    O  N N 124 
DMS   C1   C  N N 125 
DMS   C2   C  N N 126 
DMS   H11  H  N N 127 
DMS   H12  H  N N 128 
DMS   H13  H  N N 129 
DMS   H21  H  N N 130 
DMS   H22  H  N N 131 
DMS   H23  H  N N 132 
GLN   N    N  N N 133 
GLN   CA   C  N S 134 
GLN   C    C  N N 135 
GLN   O    O  N N 136 
GLN   CB   C  N N 137 
GLN   CG   C  N N 138 
GLN   CD   C  N N 139 
GLN   OE1  O  N N 140 
GLN   NE2  N  N N 141 
GLN   OXT  O  N N 142 
GLN   H    H  N N 143 
GLN   H2   H  N N 144 
GLN   HA   H  N N 145 
GLN   HB2  H  N N 146 
GLN   HB3  H  N N 147 
GLN   HG2  H  N N 148 
GLN   HG3  H  N N 149 
GLN   HE21 H  N N 150 
GLN   HE22 H  N N 151 
GLN   HXT  H  N N 152 
GLU   N    N  N N 153 
GLU   CA   C  N S 154 
GLU   C    C  N N 155 
GLU   O    O  N N 156 
GLU   CB   C  N N 157 
GLU   CG   C  N N 158 
GLU   CD   C  N N 159 
GLU   OE1  O  N N 160 
GLU   OE2  O  N N 161 
GLU   OXT  O  N N 162 
GLU   H    H  N N 163 
GLU   H2   H  N N 164 
GLU   HA   H  N N 165 
GLU   HB2  H  N N 166 
GLU   HB3  H  N N 167 
GLU   HG2  H  N N 168 
GLU   HG3  H  N N 169 
GLU   HE2  H  N N 170 
GLU   HXT  H  N N 171 
GLY   N    N  N N 172 
GLY   CA   C  N N 173 
GLY   C    C  N N 174 
GLY   O    O  N N 175 
GLY   OXT  O  N N 176 
GLY   H    H  N N 177 
GLY   H2   H  N N 178 
GLY   HA2  H  N N 179 
GLY   HA3  H  N N 180 
GLY   HXT  H  N N 181 
HIS   N    N  N N 182 
HIS   CA   C  N S 183 
HIS   C    C  N N 184 
HIS   O    O  N N 185 
HIS   CB   C  N N 186 
HIS   CG   C  Y N 187 
HIS   ND1  N  Y N 188 
HIS   CD2  C  Y N 189 
HIS   CE1  C  Y N 190 
HIS   NE2  N  Y N 191 
HIS   OXT  O  N N 192 
HIS   H    H  N N 193 
HIS   H2   H  N N 194 
HIS   HA   H  N N 195 
HIS   HB2  H  N N 196 
HIS   HB3  H  N N 197 
HIS   HD1  H  N N 198 
HIS   HD2  H  N N 199 
HIS   HE1  H  N N 200 
HIS   HE2  H  N N 201 
HIS   HXT  H  N N 202 
HOH   O    O  N N 203 
HOH   H1   H  N N 204 
HOH   H2   H  N N 205 
ILE   N    N  N N 206 
ILE   CA   C  N S 207 
ILE   C    C  N N 208 
ILE   O    O  N N 209 
ILE   CB   C  N S 210 
ILE   CG1  C  N N 211 
ILE   CG2  C  N N 212 
ILE   CD1  C  N N 213 
ILE   OXT  O  N N 214 
ILE   H    H  N N 215 
ILE   H2   H  N N 216 
ILE   HA   H  N N 217 
ILE   HB   H  N N 218 
ILE   HG12 H  N N 219 
ILE   HG13 H  N N 220 
ILE   HG21 H  N N 221 
ILE   HG22 H  N N 222 
ILE   HG23 H  N N 223 
ILE   HD11 H  N N 224 
ILE   HD12 H  N N 225 
ILE   HD13 H  N N 226 
ILE   HXT  H  N N 227 
LEU   N    N  N N 228 
LEU   CA   C  N S 229 
LEU   C    C  N N 230 
LEU   O    O  N N 231 
LEU   CB   C  N N 232 
LEU   CG   C  N N 233 
LEU   CD1  C  N N 234 
LEU   CD2  C  N N 235 
LEU   OXT  O  N N 236 
LEU   H    H  N N 237 
LEU   H2   H  N N 238 
LEU   HA   H  N N 239 
LEU   HB2  H  N N 240 
LEU   HB3  H  N N 241 
LEU   HG   H  N N 242 
LEU   HD11 H  N N 243 
LEU   HD12 H  N N 244 
LEU   HD13 H  N N 245 
LEU   HD21 H  N N 246 
LEU   HD22 H  N N 247 
LEU   HD23 H  N N 248 
LEU   HXT  H  N N 249 
LYS   N    N  N N 250 
LYS   CA   C  N S 251 
LYS   C    C  N N 252 
LYS   O    O  N N 253 
LYS   CB   C  N N 254 
LYS   CG   C  N N 255 
LYS   CD   C  N N 256 
LYS   CE   C  N N 257 
LYS   NZ   N  N N 258 
LYS   OXT  O  N N 259 
LYS   H    H  N N 260 
LYS   H2   H  N N 261 
LYS   HA   H  N N 262 
LYS   HB2  H  N N 263 
LYS   HB3  H  N N 264 
LYS   HG2  H  N N 265 
LYS   HG3  H  N N 266 
LYS   HD2  H  N N 267 
LYS   HD3  H  N N 268 
LYS   HE2  H  N N 269 
LYS   HE3  H  N N 270 
LYS   HZ1  H  N N 271 
LYS   HZ2  H  N N 272 
LYS   HZ3  H  N N 273 
LYS   HXT  H  N N 274 
MET   N    N  N N 275 
MET   CA   C  N S 276 
MET   C    C  N N 277 
MET   O    O  N N 278 
MET   CB   C  N N 279 
MET   CG   C  N N 280 
MET   SD   S  N N 281 
MET   CE   C  N N 282 
MET   OXT  O  N N 283 
MET   H    H  N N 284 
MET   H2   H  N N 285 
MET   HA   H  N N 286 
MET   HB2  H  N N 287 
MET   HB3  H  N N 288 
MET   HG2  H  N N 289 
MET   HG3  H  N N 290 
MET   HE1  H  N N 291 
MET   HE2  H  N N 292 
MET   HE3  H  N N 293 
MET   HXT  H  N N 294 
PHE   N    N  N N 295 
PHE   CA   C  N S 296 
PHE   C    C  N N 297 
PHE   O    O  N N 298 
PHE   CB   C  N N 299 
PHE   CG   C  Y N 300 
PHE   CD1  C  Y N 301 
PHE   CD2  C  Y N 302 
PHE   CE1  C  Y N 303 
PHE   CE2  C  Y N 304 
PHE   CZ   C  Y N 305 
PHE   OXT  O  N N 306 
PHE   H    H  N N 307 
PHE   H2   H  N N 308 
PHE   HA   H  N N 309 
PHE   HB2  H  N N 310 
PHE   HB3  H  N N 311 
PHE   HD1  H  N N 312 
PHE   HD2  H  N N 313 
PHE   HE1  H  N N 314 
PHE   HE2  H  N N 315 
PHE   HZ   H  N N 316 
PHE   HXT  H  N N 317 
PRO   N    N  N N 318 
PRO   CA   C  N S 319 
PRO   C    C  N N 320 
PRO   O    O  N N 321 
PRO   CB   C  N N 322 
PRO   CG   C  N N 323 
PRO   CD   C  N N 324 
PRO   OXT  O  N N 325 
PRO   H    H  N N 326 
PRO   HA   H  N N 327 
PRO   HB2  H  N N 328 
PRO   HB3  H  N N 329 
PRO   HG2  H  N N 330 
PRO   HG3  H  N N 331 
PRO   HD2  H  N N 332 
PRO   HD3  H  N N 333 
PRO   HXT  H  N N 334 
SER   N    N  N N 335 
SER   CA   C  N S 336 
SER   C    C  N N 337 
SER   O    O  N N 338 
SER   CB   C  N N 339 
SER   OG   O  N N 340 
SER   OXT  O  N N 341 
SER   H    H  N N 342 
SER   H2   H  N N 343 
SER   HA   H  N N 344 
SER   HB2  H  N N 345 
SER   HB3  H  N N 346 
SER   HG   H  N N 347 
SER   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TRP   N    N  N N 366 
TRP   CA   C  N S 367 
TRP   C    C  N N 368 
TRP   O    O  N N 369 
TRP   CB   C  N N 370 
TRP   CG   C  Y N 371 
TRP   CD1  C  Y N 372 
TRP   CD2  C  Y N 373 
TRP   NE1  N  Y N 374 
TRP   CE2  C  Y N 375 
TRP   CE3  C  Y N 376 
TRP   CZ2  C  Y N 377 
TRP   CZ3  C  Y N 378 
TRP   CH2  C  Y N 379 
TRP   OXT  O  N N 380 
TRP   H    H  N N 381 
TRP   H2   H  N N 382 
TRP   HA   H  N N 383 
TRP   HB2  H  N N 384 
TRP   HB3  H  N N 385 
TRP   HD1  H  N N 386 
TRP   HE1  H  N N 387 
TRP   HE3  H  N N 388 
TRP   HZ2  H  N N 389 
TRP   HZ3  H  N N 390 
TRP   HH2  H  N N 391 
TRP   HXT  H  N N 392 
TYR   N    N  N N 393 
TYR   CA   C  N S 394 
TYR   C    C  N N 395 
TYR   O    O  N N 396 
TYR   CB   C  N N 397 
TYR   CG   C  Y N 398 
TYR   CD1  C  Y N 399 
TYR   CD2  C  Y N 400 
TYR   CE1  C  Y N 401 
TYR   CE2  C  Y N 402 
TYR   CZ   C  Y N 403 
TYR   OH   O  N N 404 
TYR   OXT  O  N N 405 
TYR   H    H  N N 406 
TYR   H2   H  N N 407 
TYR   HA   H  N N 408 
TYR   HB2  H  N N 409 
TYR   HB3  H  N N 410 
TYR   HD1  H  N N 411 
TYR   HD2  H  N N 412 
TYR   HE1  H  N N 413 
TYR   HE2  H  N N 414 
TYR   HH   H  N N 415 
TYR   HXT  H  N N 416 
VAL   N    N  N N 417 
VAL   CA   C  N S 418 
VAL   C    C  N N 419 
VAL   O    O  N N 420 
VAL   CB   C  N N 421 
VAL   CG1  C  N N 422 
VAL   CG2  C  N N 423 
VAL   OXT  O  N N 424 
VAL   H    H  N N 425 
VAL   H2   H  N N 426 
VAL   HA   H  N N 427 
VAL   HB   H  N N 428 
VAL   HG11 H  N N 429 
VAL   HG12 H  N N 430 
VAL   HG13 H  N N 431 
VAL   HG21 H  N N 432 
VAL   HG22 H  N N 433 
VAL   HG23 H  N N 434 
VAL   HXT  H  N N 435 
# 
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 
A1ACA N   C1   doub Y N 1   
A1ACA N   C    sing Y N 2   
A1ACA CL  C    sing N N 3   
A1ACA C1  C2   sing Y N 4   
A1ACA C   N3   doub Y N 5   
A1ACA C2  BR   sing N N 6   
A1ACA C2  C3   doub Y N 7   
A1ACA N3  C3   sing Y N 8   
A1ACA C3  N1   sing N N 9   
A1ACA N1  C4   sing N N 10  
A1ACA C4  C5   doub Y N 11  
A1ACA C4  C11  sing Y N 12  
A1ACA C5  C6   sing Y N 13  
A1ACA C11 C10  doub Y N 14  
A1ACA C6  C7   doub Y N 15  
A1ACA C10 C7   sing Y N 16  
A1ACA C10 C9   sing N N 17  
A1ACA C7  N2   sing N N 18  
A1ACA C9  C8   sing N N 19  
A1ACA N2  C8   sing N N 20  
A1ACA C8  O    doub N N 21  
A1ACA C5  H1   sing N N 22  
A1ACA C6  H2   sing N N 23  
A1ACA C1  H3   sing N N 24  
A1ACA C9  H4   sing N N 25  
A1ACA C9  H5   sing N N 26  
A1ACA N2  H6   sing N N 27  
A1ACA C11 H7   sing N N 28  
A1ACA N1  H8   sing N N 29  
ACE   C   O    doub N N 30  
ACE   C   CH3  sing N N 31  
ACE   C   H    sing N N 32  
ACE   CH3 H1   sing N N 33  
ACE   CH3 H2   sing N N 34  
ACE   CH3 H3   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
DMS   S   O    doub N N 118 
DMS   S   C1   sing N N 119 
DMS   S   C2   sing N N 120 
DMS   C1  H11  sing N N 121 
DMS   C1  H12  sing N N 122 
DMS   C1  H13  sing N N 123 
DMS   C2  H21  sing N N 124 
DMS   C2  H22  sing N N 125 
DMS   C2  H23  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
_pdbx_deposit_group.group_id            G_1002065 
_pdbx_deposit_group.group_title         'X-ray dose series of B-cell lymphoma 6 protein BTB domain in complex with ligand 2' 
_pdbx_deposit_group.group_description   
;Crystal structures of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 solved at increasing X-ray dose using Many Structures One Crystal (MSOX) crystallography.
;
_pdbx_deposit_group.group_type          undefined 
# 
_atom_sites.entry_id                    7GV5 
_atom_sites.fract_transf_matrix[1][1]   0.014780 
_atom_sites.fract_transf_matrix[1][2]   0.008533 
_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]   0.017066 
_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]   0.006001 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
BR 
C  
CL 
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   . ASP   A 1 5   ? 17.278 -21.250 -4.853 1.00 71.53  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.212 -22.131 -5.557 1.00 70.30  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.770 -23.612 -5.486 1.00 69.70  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.737 -23.928 -4.886 1.00 70.37  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.640 -21.957 -4.982 1.00 71.06  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.743 -22.004 -6.029 1.00 85.02  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.883 -23.055 -6.707 1.00 85.33  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.476 -20.996 -6.166 1.00 92.15  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.552 -24.510 -6.107 1.00 61.04  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.304 -25.949 -6.093 1.00 58.22  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.290 -26.673 -5.122 1.00 53.46  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.562 -27.861 -5.290 1.00 52.34  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.403 -26.511 -7.509 1.00 63.92  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.683 -26.280 -8.074 1.00 75.51  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.788 -25.964 -4.090 1.00 44.48  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.724 -26.529 -3.113 1.00 41.38  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.105 -27.683 -2.309 1.00 40.32  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.887 -27.732 -2.136 1.00 40.35  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.215 -25.436 -2.162 1.00 42.40  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.363 -24.236 -2.898 1.00 47.81  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.945 -28.578 -1.789 1.00 31.40  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.571 -29.569 -0.773 1.00 28.52  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.176 -29.044 0.526  1.00 30.45  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.124 -28.257 0.474  1.00 29.04  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.920 -31.048 -1.081 1.00 31.65  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.436 -31.232 -1.364 1.00 31.76  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.064 -31.556 -2.244 1.00 31.34  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.922 -32.676 -1.536 1.00 38.04  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.696 -29.481 1.693  0.66 25.58  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.572 -29.396 1.658  0.34 26.93  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.267 -28.981 2.952  0.66 24.73  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 20.997 -28.901 2.955  0.34 26.22  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.607 -30.128 3.889  0.66 27.65  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.391 -30.036 3.877  0.34 29.74  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.846 -31.092 3.965  0.66 28.93  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.689 -31.044 3.952  0.34 30.28  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.288 -27.988 3.623  0.66 26.35  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.872 -28.067 3.575  0.34 27.67  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.579 -27.699 5.112  0.66 31.22  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.358 -27.073 4.628  0.34 29.49  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.012 -26.406 5.635  0.66 53.41  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.612 -27.192 5.936  0.34 44.88  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.325 -25.660 4.933  0.66 48.35  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.395 -27.401 5.976  0.34 36.49  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.309 -26.103 6.896  0.66 47.30  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.330 -27.035 7.042  0.34 40.79  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.741 -30.028 4.593  0.66 25.55  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.512 -29.867 4.575  0.34 26.57  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.116 -31.042 5.571  0.66 24.80  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.019 -30.847 5.528  0.34 25.97  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.648 -30.546 6.929  0.66 27.07  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.529 -30.399 6.881  0.34 28.36  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.243 -29.612 7.500  0.66 25.45  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.963 -29.354 7.390  0.34 27.47  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.633 -31.345 5.531  0.66 25.42  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.553 -30.942 5.433  0.34 27.12  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 25.007 -32.553 6.356  0.66 26.32  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.029 -31.715 4.222  0.34 29.10  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.620 -33.832 5.965  0.66 29.28  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.721 -31.286 2.933  0.34 32.90  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.783 -32.420 7.503  0.66 26.85  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.816 -32.849 4.367  0.34 32.19  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 24.955 -34.950 6.743  0.66 30.16  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.161 -31.998 1.814  0.34 34.20  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.093 -33.532 8.292  0.66 28.59  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.265 -33.557 3.243  0.34 35.86  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.697 -34.790 7.897  0.66 27.11  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.932 -33.128 1.977  0.34 33.92  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.549 -31.140 7.427  1.00 25.17  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.892 -30.757 8.692  1.00 25.30  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.855 -30.519 9.880  1.00 27.52  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.730 -29.499 10.566 1.00 27.13  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.815 -31.779 9.060  1.00 32.58  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.918 -31.919 7.938  1.00 32.55  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.015 -31.367 10.320 1.00 37.01  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.789 -31.457 10.106 1.00 24.47  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.704 -31.387 11.261 1.00 25.35  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.949 -30.491 11.062 1.00 26.49  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.784 -30.408 11.980 1.00 25.06  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.157 -32.810 11.654 1.00 31.07  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.053 -33.759 12.179 1.00 41.54  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.476 -33.323 13.516 1.00 63.10  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.446 -33.405 14.612 1.00 75.14  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.307 -32.792 15.784 1.00 84.47  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.231 -32.929 16.724 1.00 73.19  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.250 -32.024 16.019 1.00 65.39  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.096 -29.847 9.894  1.00 22.18  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.324 -29.095 9.604  1.00 23.37  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.614 -27.995 10.618 1.00 25.11  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.753 -27.911 11.111 1.00 24.86  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.307 -28.523 8.176  1.00 23.50  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.570 -27.780 7.859  1.00 25.23  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.749 -28.456 7.642  1.00 25.69  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.791 -26.449 7.723  1.00 25.56  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.660 -27.527 7.389  1.00 25.14  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.131 -26.305 7.412  1.00 24.77  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.621 -27.115 10.889 1.00 22.49  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.853 -25.985 11.833 1.00 22.23  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.284 -26.490 13.229 1.00 24.56  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.214 -25.938 13.827 1.00 22.18  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.601 -25.107 11.925 1.00 23.22  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.616 -27.536 13.732 0.42 23.71  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.617 -27.544 13.728 0.30 23.17  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.613 -27.536 13.740 0.28 22.95  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.917 -28.125 15.034 0.42 24.06  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.906 -28.154 15.026 0.30 23.43  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.926 -28.112 15.049 0.28 23.08  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.321 -28.729 15.050 0.42 27.79  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.310 -28.746 15.052 0.30 27.69  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.319 -28.745 15.061 0.28 27.55  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.051 -28.548 16.032 0.42 25.56  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.029 -28.573 16.042 0.30 26.02  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.043 -28.594 16.050 0.28 25.93  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.871 -29.175 15.399 0.42 28.39  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.876 -29.233 15.346 0.30 27.12  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.859 -29.120 15.466 0.28 26.49  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.142 -29.744 16.669 0.42 33.16  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.575 -28.679 15.425 0.30 30.75  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.832 -30.230 14.586 0.28 28.82  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.706 -29.417 13.955 1.00 25.32  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.038 -30.037 13.814 1.00 26.03  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.116 -28.946 13.787 1.00 26.12  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.152 -29.101 14.435 1.00 25.20  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.100 -30.892 12.543 1.00 27.94  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.328 -32.214 12.628 1.00 38.62  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.801 -32.532 13.725 1.00 36.62  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.251 -32.930 11.597 1.00 40.44  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.861 -27.829 13.068 1.00 21.36  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.824 -26.715 13.036 1.00 21.19  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.038 -26.171 14.469 1.00 24.89  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.171 -25.995 14.916 1.00 23.02  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.341 -25.596 12.063 1.00 23.89  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.124 -24.303 12.270 1.00 24.15  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.385 -26.056 10.599 1.00 23.88  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.943 -25.909 15.177 1.00 22.97  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.031 -25.347 16.529 1.00 23.71  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.763 -26.310 17.491 1.00 24.10  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.618 -25.864 18.276 1.00 22.61  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.638 -24.972 17.037 1.00 24.29  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.633 -24.087 18.300 1.00 27.82  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.216 -22.703 18.011 1.00 27.84  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.214 -23.949 18.847 1.00 30.68  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.472 -27.610 17.380 1.00 22.96  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.143 -28.650 18.169 1.00 24.15  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.654 -28.564 17.918 1.00 26.35  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.439 -28.534 18.883 1.00 25.66  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.608 -30.029 17.773 1.00 25.98  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.154 -31.230 18.554 1.00 34.39  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.771 -31.135 20.034 1.00 36.94  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.565 -32.519 18.006 1.00 38.55  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.057 -28.440 16.634 1.00 22.86  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.485 -28.331 16.302 1.00 22.50  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.112 -27.034 16.806 1.00 25.13  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.252 -27.051 17.276 1.00 24.87  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.727 -28.553 14.818 1.00 24.68  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.705 -30.014 14.455 1.00 35.63  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.916 -30.893 15.304 1.00 31.10  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.444 -30.305 13.188 1.00 28.61  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.371 -25.921 16.734 1.00 23.21  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.866 -24.644 17.264 1.00 23.87  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.089 -24.784 18.772 1.00 25.55  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.077 -24.262 19.303 1.00 24.93  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.887 -23.508 16.956 1.00 24.01  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.755 -23.143 15.463 1.00 26.10  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.667 -22.083 15.259 1.00 27.50  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.106 -22.706 14.850 1.00 28.15  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.173 -25.481 19.468 1.00 23.57  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.340 -25.697 20.918 1.00 24.46  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.570 -26.577 21.220 1.00 27.94  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.272 -26.328 22.207 1.00 28.23  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.084 -26.308 21.543 1.00 25.64  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.087 -26.176 23.054 1.00 33.02  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.597 -25.205 23.621 1.00 29.87  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.526 -27.156 23.721 1.00 32.21  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.849 -27.583 20.358 1.00 25.91  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.031 -28.445 20.507 1.00 26.72  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.289 -27.592 20.363 1.00 30.39  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.237 -27.786 21.111 1.00 30.88  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 37.029 -29.564 19.454 1.00 27.24  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 36.024 -30.659 19.795 1.00 28.86  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.814 -31.589 18.602 1.00 31.89  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 34.952 -32.707 18.968 1.00 40.12  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.311 -33.480 18.100 1.00 56.29  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.372 -33.222 16.797 1.00 41.71  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.577 -34.494 18.527 1.00 50.54  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.291 -26.628 19.416 1.00 26.12  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.441 -25.735 19.254 1.00 26.18  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.596 -24.869 20.498 1.00 30.16  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.720 -24.670 20.983 1.00 30.68  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.254 -24.829 18.044 1.00 25.63  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.256 -25.519 16.664 1.00 29.56  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.144 -24.468 15.560 1.00 29.06  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.539 -26.354 16.465 1.00 30.53  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.460 -24.364 21.034 1.00 26.61  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.512 -23.567 22.259 1.00 26.92  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.131 -24.377 23.431 1.00 32.31  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 40.015 -23.856 24.131 1.00 33.28  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.120 -23.063 22.662 1.00 27.48  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.238 -22.163 23.896 1.00 30.99  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.949 -21.527 24.302 1.00 37.60  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.934 -22.509 24.671 1.00 33.27  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.317 -22.555 25.848 1.00 44.51  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.669 -21.727 26.827 1.00 37.30  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.365 -23.446 26.066 1.00 32.30  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.654 -25.615 23.643 0.39 30.28  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.657 -25.626 23.622 0.28 30.14  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.654 -25.615 23.644 0.33 30.44  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.119 -26.511 24.711 0.39 31.71  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.099 -26.579 24.650 0.28 31.54  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.119 -26.516 24.706 0.33 31.97  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.630 -26.791 24.638 0.39 37.81  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.614 -26.788 24.624 0.28 37.54  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.632 -26.780 24.635 0.33 37.80  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.276 -26.919 25.680 0.39 39.24  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.241 -26.883 25.680 0.28 38.78  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.278 -26.891 25.679 0.33 39.11  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.324 -27.813 24.707 0.39 35.04  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.424 -27.931 24.438 0.28 34.95  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.351 -27.833 24.660 0.33 35.81  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.677 -28.671 23.634 0.39 40.80  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.074 -27.947 24.864 0.28 41.95  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.785 -28.724 25.676 0.33 45.29  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.191 -26.866 23.413 1.00 33.87  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.628 -27.112 23.196 1.00 35.28  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.421 -25.817 23.001 1.00 37.61  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.630 -25.861 22.755 1.00 39.01  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.803 -28.071 22.014 1.00 36.31  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.062 -29.396 22.217 1.00 43.14  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.051 -30.247 20.970 1.00 48.18  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.410 -30.593 20.551 1.00 62.64  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.764 -30.798 19.289 1.00 77.95  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 45.022 -31.091 18.985 1.00 67.79  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.871 -30.687 18.318 1.00 61.04  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.743 -24.666 23.140 1.00 32.19  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.302 -23.327 22.991 1.00 32.58  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.922 -23.099 21.585 1.00 36.99  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 44.982 -22.482 21.453 1.00 39.03  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.312 -23.024 24.131 1.00 36.11  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.595 -21.548 24.301 1.00 47.02  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.657 -20.737 24.110 1.00 46.67  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.756 -21.199 24.616 1.00 53.78  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.266 -23.613 20.545 1.00 30.33  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.767 -23.502 19.173 1.00 30.22  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.156 -22.305 18.470 1.00 32.86  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 41.919 -22.173 18.399 1.00 28.92  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.578 -24.818 18.376 1.00 33.42  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.370 -25.993 19.013 1.00 35.43  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.916 -24.631 16.875 1.00 33.55  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.866 -27.375 18.530 1.00 37.76  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.041 -21.415 17.971 1.00 32.00  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.688 -20.211 17.215 1.00 32.53  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.785 -19.229 17.981 1.00 33.75  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.167 -18.364 17.363 1.00 31.74  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.114 -20.531 15.829 1.00 33.07  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.140 -21.077 14.797 1.00 40.67  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.534 -21.125 13.446 1.00 41.08  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.384 -20.226 14.722 1.00 47.33  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.794 -19.300 19.320 1.00 30.33  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.113 -18.303 20.150 1.00 29.45  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.925 -17.017 19.958 1.00 35.62  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.157 -17.073 19.838 1.00 35.86  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 42.017 -18.753 21.603 1.00 34.52  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.332 -19.082 22.044 1.00 35.65  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.061 -19.962 21.778 1.00 31.45  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.242 -15.889 19.789 1.00 32.48  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.910 -14.636 19.444 1.00 32.34  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.588 -13.481 20.354 1.00 33.46  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.971 -12.346 20.058 1.00 33.11  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.609 -14.266 17.982 1.00 33.94  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.135 -14.304 17.584 1.00 43.25  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.271 -14.420 18.486 1.00 38.18  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.850 -14.216 16.379 1.00 54.55  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.903 -13.752 21.467 1.00 27.91  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.588 -12.705 22.441 1.00 27.37  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.421 -13.305 23.834 1.00 30.44  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 41.002 -14.467 23.975 1.00 29.45  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.318 -11.872 22.011 1.00 29.70  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 39.017 -12.674 22.151 1.00 27.76  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.211 -10.527 22.761 1.00 30.32  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.730 -12.498 24.855 0.60 28.05  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.729 -12.512 24.867 0.40 27.40  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.510 -12.819 26.256 0.60 27.92  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.473 -12.894 26.248 0.40 27.00  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.426 -11.837 26.723 0.60 30.68  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.502 -11.861 26.845 0.40 30.76  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.533 -10.633 26.456 0.60 30.76  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.732 -10.652 26.739 0.40 31.42  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.809 -12.678 27.110 0.60 33.29  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.728 -13.203 27.116 0.40 31.67  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.538 -12.905 28.600 0.60 33.57  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.603 -11.975 27.343 0.40 32.19  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.900 -13.621 26.618 0.60 33.88  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.342 -13.850 28.443 0.40 31.66  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.383 -12.349 27.386 1.00 26.32  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.321 -11.538 27.986 1.00 26.98  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.602 -11.560 29.476 1.00 32.06  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.606 -12.643 30.089 1.00 31.71  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.882 -12.037 27.665 1.00 28.87  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.660 -12.211 26.137 1.00 28.71  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.842 -11.097 28.288 1.00 30.20  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.919 -10.930 25.246 1.00 29.17  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.853 -10.382 30.044 1.00 29.04  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.159 -10.250 31.473 1.00 29.16  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.888 -9.825  32.210 1.00 33.80  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.297 -8.785  31.890 1.00 31.85  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.347 -9.280  31.736 1.00 33.76  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.634 -9.149  33.234 1.00 34.28  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.609 -9.735  31.003 1.00 34.48  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.486 -10.626 33.209 1.00 31.23  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.298 -10.403 34.026 1.00 31.72  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.803 -10.449 35.454 1.00 39.45  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 36.975 -11.534 36.021 1.00 36.51  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.175 -11.436 33.740 1.00 34.68  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.867 -10.995 34.392 1.00 34.50  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 34.989 -11.638 32.235 1.00 33.58  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.169 -9.272  35.993 0.54 40.02  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.013 -9.249  36.028 0.46 38.98  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.772 -9.104  37.322 0.54 41.67  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.543 -8.994  37.368 0.46 40.29  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.128 -9.863  37.384 0.54 43.04  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.642 -10.002 37.742 0.46 42.54  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 40.014 -9.572  36.581 0.54 42.24  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.459 -10.879 38.594 0.46 42.23  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.808 -9.531  38.433 0.54 47.95  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.424 -8.897  38.397 0.46 45.21  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.531 -8.926  38.300 0.54 62.04  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.753 -7.655  38.253 0.46 54.51  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.264 -10.850 38.294 0.54 38.81  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.753 -9.899  36.987 0.46 37.34  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.476 -11.653 38.481 0.54 38.95  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 41.009 -10.655 37.036 0.46 37.59  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.566 -12.841 37.517 0.54 41.08  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.898 -12.069 36.442 0.46 39.86  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.586 -13.539 37.509 0.54 40.54  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.921 -12.579 35.975 0.46 39.91  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.579 -12.150 39.938 0.54 39.37  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.664 -10.665 38.430 0.46 39.24  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 41.053 -11.091 40.924 0.54 46.29  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.180 -9.282  38.831 0.46 51.14  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.363 -11.709 42.273 0.54 47.06  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.167 -9.330  39.976 0.46 58.72  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.555 -10.701 43.314 0.54 51.86  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.620 -7.990  40.358 0.46 66.98  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.722 -10.153 43.641 0.54 65.33  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.041 -7.236  41.289 0.46 80.11  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.789 -9.252  44.608 0.54 52.99  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 41.973 -7.677  41.942 0.46 66.34  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.830 -10.498 42.997 0.54 51.50  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.523 -6.034  41.571 0.46 67.77  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.499 -13.093 36.730 0.54 36.21  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.677 -12.671 36.385 0.46 35.54  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.465 -14.224 35.800 0.54 35.27  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.448 -13.992 35.766 0.46 34.77  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.737 -13.818 34.354 0.54 37.46  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.597 -13.833 34.247 0.46 37.01  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.376 -12.721 33.929 0.54 35.85  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 39.041 -12.894 33.677 0.46 34.94  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.133 -14.998 35.905 0.54 36.36  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.059 -14.555 36.126 0.46 35.99  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.855 -15.573 37.288 0.54 52.32  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.955 -15.079 37.549 0.46 49.46  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.174 -17.046 37.449 0.54 88.74  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.167 -16.574 37.680 0.46 84.88  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.432 -17.883 36.884 0.54 88.79  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.216 -16.977 38.234 0.46 87.31  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.162 -17.364 38.150 0.54 89.54  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.288 -17.343 37.228 0.46 85.18  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.352 -14.735 33.596 1.00 33.37  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.678 -14.592 32.186 1.00 32.48  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.039 -15.705 31.393 1.00 35.12  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.076 -16.852 31.835 1.00 35.40  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.204 -14.636 32.011 1.00 35.30  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.920 -13.425 32.590 1.00 52.85  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.385 -13.335 32.234 1.00 73.11  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.944 -14.146 31.479 1.00 66.84  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 45.039 -12.325 32.778 1.00 75.22  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.449 -15.376 30.227 1.00 28.74  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.802 -16.389 29.369 1.00 28.52  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.303 -16.205 27.961 1.00 32.32  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.158 -15.112 27.407 1.00 32.09  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.272 -16.218 29.379 1.00 29.63  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.647 -16.318 30.748 1.00 31.56  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.524 -15.191 31.561 1.00 33.75  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.158 -17.533 31.219 1.00 34.26  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 35.950 -15.286 32.832 1.00 35.78  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.593 -17.626 32.496 1.00 37.67  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.490 -16.502 33.292 1.00 35.31  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.912 -17.249 27.386 1.00 29.46  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.421 -17.211 26.016 1.00 28.16  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.287 -17.614 25.060 1.00 30.99  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.481 -18.501 25.372 1.00 29.97  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.634 -18.140 25.848 1.00 29.28  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.869 -17.685 26.676 1.00 36.94  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.183 -18.109 26.030 1.00 44.82  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.205 -17.718 24.616 1.00 59.09  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.794 -16.631 24.130 1.00 71.73  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.510 -15.845 24.921 1.00 64.96  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.713 -16.350 22.838 1.00 52.79  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.204 -16.962 23.903 1.00 27.30  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.128 -17.269 22.945 1.00 26.87  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.506 -16.845 21.540 1.00 28.74  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.593 -16.296 21.320 1.00 27.51  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.824 -16.571 23.371 1.00 27.58  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.611 -17.130 20.588 1.00 25.40  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.760 -16.710 19.202 1.00 24.79  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.893 -15.461 19.026 1.00 27.30  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.681 -15.491 19.308 1.00 25.71  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.289 -17.821 18.245 1.00 24.64  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.053 -19.097 18.426 1.00 28.08  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.575 -20.117 19.241 1.00 29.81  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.289 -19.436 17.981 1.00 29.15  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.500 -21.073 19.205 1.00 29.58  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.559 -20.698 18.478 1.00 29.33  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.499 -14.377 18.555 1.00 25.76  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.771 -13.116 18.298 1.00 25.22  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.527 -13.371 17.425 1.00 27.15  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.461 -12.842 17.731 1.00 24.74  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.681 -12.113 17.567 1.00 27.51  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.658 -11.445 18.516 1.00 30.13  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.617 -10.562 17.723 1.00 28.75  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.676 -10.012 18.637 1.00 35.22  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.663 -9.213  17.883 1.00 37.44  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.655 -14.168 16.361 1.00 24.13  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.516 -14.396 15.456 1.00 24.78  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.334 -15.038 16.152 1.00 26.27  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.197 -14.658 15.887 1.00 26.08  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.930 -15.170 14.207 1.00 32.95  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.557 -16.378 14.630 1.00 32.94  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.813 -14.342 13.281 1.00 33.86  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.587 -16.008 17.028 1.00 22.86  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.502 -16.690 17.741 1.00 22.39  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.828 -15.711 18.697 1.00 24.56  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.584 -15.674 18.782 1.00 23.25  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 33.009 -17.965 18.467 1.00 24.47  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.900 -18.561 19.345 1.00 25.16  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.502 -19.004 17.442 1.00 24.64  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.635 -14.917 19.427 1.00 23.54  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.066 -13.907 20.328 1.00 22.51  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.160 -12.919 19.571 1.00 25.10  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.055 -12.618 20.031 1.00 25.69  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.188 -13.131 21.049 1.00 22.15  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.147 -13.936 21.970 1.00 26.09  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.220 -13.010 22.576 1.00 27.07  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.366 -14.666 23.087 1.00 28.26  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.616 -12.431 18.411 1.00 22.48  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.834 -11.505 17.582 1.00 24.40  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.559 -12.149 17.075 1.00 28.53  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.510 -11.501 17.035 1.00 29.06  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.641 -11.048 16.376 1.00 26.46  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.858 -10.248 16.753 1.00 29.37  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.897 -10.141 15.290 1.00 33.84  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.101 -8.821  14.466 1.00 30.47  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.632 -13.441 16.714 1.00 24.97  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.472 -14.174 16.187 1.00 24.46  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.367 -14.382 17.257 1.00 28.34  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.211 -14.591 16.901 1.00 29.18  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.924 -15.527 15.614 1.00 25.26  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.735 -14.335 18.549 1.00 24.28  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.823 -14.590 19.664 1.00 24.90  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.369 -13.366 20.450 1.00 28.33  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.413 -13.486 21.226 1.00 26.92  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.472 -15.593 20.618 1.00 25.02  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.842 -17.197 19.880 1.00 28.22  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.133 -12.262 20.386 1.00 24.31  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.921 -11.119 21.282 1.00 23.66  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.934 -9.813  20.538 1.00 28.81  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.907 -9.527  19.827 1.00 27.10  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.038 -11.141 22.326 1.00 24.39  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.349 -9.901  22.946 1.00 28.38  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.898 -8.997  20.757 1.00 26.24  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.813 -7.665  20.160 1.00 26.52  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.926 -6.769  20.673 1.00 29.23  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.482 -5.969  19.911 1.00 28.90  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.328 -6.963  21.952 1.00 27.08  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.442 -6.180  22.516 1.00 27.74  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.777 -6.526  21.815 1.00 29.82  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.459 -5.610  21.339 1.00 28.13  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.553 -6.384  24.041 1.00 27.56  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.624 -5.509  24.722 1.00 32.33  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.216 -4.014  24.729 1.00 33.31  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.917 -6.004  26.116 1.00 31.42  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.124 -7.829  21.705 1.00 25.11  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.382 -8.208  21.029 1.00 24.48  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.356 -7.860  19.559 1.00 28.09  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.382 -7.458  19.020 1.00 27.56  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.763 -9.670  21.272 1.00 25.28  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.185 -9.901  22.708 1.00 26.43  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.255 -9.195  23.263 1.00 29.69  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.540 -10.853 23.495 1.00 27.59  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.629 -9.391  24.606 1.00 30.43  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.946 -11.080 24.822 1.00 29.88  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 32.976 -10.339 25.372 1.00 27.87  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.179 -7.938  18.920 1.00 25.75  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.058 -7.541  17.506 1.00 26.30  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.479 -6.066  17.345 1.00 30.51  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.260 -5.748  16.441 1.00 29.02  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.616 -7.764  17.031 1.00 28.55  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.355 -7.232  15.644 1.00 32.35  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 28.977 -7.793  14.532 1.00 33.82  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.483 -6.167  15.442 1.00 36.30  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.738 -7.302  13.246 1.00 36.66  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.230 -5.675  14.167 1.00 39.65  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.847 -6.257  13.072 1.00 46.25  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.581 -5.766  11.830 1.00 51.80  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.965 -5.178  18.217 0.53 28.51  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.961 -5.188  18.221 0.47 28.30  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.293 -3.748  18.202 0.53 29.83  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.281 -3.761  18.228 0.47 29.54  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.784 -3.516  18.514 0.53 34.97  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.782 -3.552  18.490 0.47 34.60  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.428 -2.727  17.829 0.53 36.20  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.427 -2.813  17.751 0.47 35.47  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.403 -2.992  19.182 0.53 32.67  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.453 -3.043  19.291 0.47 32.26  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 28.066 -2.979  18.712 0.53 36.21  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.786 -1.666  19.321 0.47 37.20  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.335 -4.235  19.512 1.00 30.96  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.753 -4.124  19.907 1.00 30.53  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.700 -4.517  18.772 1.00 33.67  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.585 -3.732  18.420 1.00 34.73  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.087 -4.946  21.207 1.00 32.20  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.352 -4.403  22.464 1.00 32.17  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.613 -5.012  21.452 1.00 31.04  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.407 -5.438  23.671 1.00 33.98  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.509 -5.708  18.186 1.00 28.91  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.480 -6.147  17.197 1.00 29.03  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.242 -5.610  15.782 1.00 33.59  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.087 -5.860  14.924 1.00 34.13  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.658 -7.670  17.224 1.00 29.01  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.075 -8.167  18.593 1.00 29.56  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.280 -7.759  19.166 1.00 33.47  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.258 -9.024  19.317 1.00 30.16  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.658 -8.211  20.437 1.00 34.24  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.653 -9.500  20.573 1.00 32.83  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.840 -9.080  21.131 1.00 32.20  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.177 -4.811  15.548 1.00 31.38  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 34.009 -4.120  14.256 1.00 32.27  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.571 -2.704  14.368 1.00 38.85  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.675 -1.988  13.362 1.00 38.63  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.582 -4.153  13.706 1.00 38.14  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.680 -3.647  14.687 1.00 35.51  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.164 -5.547  13.224 1.00 35.42  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 34.973 -2.301  15.592 1.00 35.38  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.594 -0.992  15.796 1.00 37.00  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 37.029 -1.067  15.266 1.00 42.61  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.770 -1.969  15.647 1.00 40.17  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.570 -0.591  17.282 1.00 38.68  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.335 0.691   17.526 1.00 52.01  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.737 1.771   17.376 1.00 56.84  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.549 0.612   17.812 1.00 53.57  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.425 -0.097  14.422 1.00 44.10  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.737 -0.055  13.764 1.00 45.48  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.939 -0.080  14.724 1.00 49.19  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 41.001 -0.552  14.320 1.00 52.10  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.838 1.127   12.788 1.00 49.06  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.950 0.970   11.554 1.00 64.72  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.789 0.409   15.972 1.00 41.66  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.869 0.343   16.957 1.00 40.98  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.788 -0.914  17.808 1.00 44.02  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.811 -1.540  18.069 1.00 45.53  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.857 1.560   17.908 1.00 41.93  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.456 2.853   17.394 1.00 49.24  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.320 3.938   18.433 1.00 50.41  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 42.935 2.694   17.015 1.00 54.08  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.589 -1.237  18.320 1.00 37.49  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.411 -2.365  19.239 1.00 35.83  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.540 -3.720  18.557 1.00 40.72  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.918 -4.682  19.221 1.00 39.46  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.092 -2.258  20.020 1.00 35.95  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 37.981 -1.016  20.910 1.00 36.68  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.710 -1.103  21.750 1.00 36.03  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.364 0.202   22.430 1.00 39.60  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.871 1.236   21.489 1.00 41.77  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.279 -3.791  17.233 1.00 40.06  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.400 -5.046  16.468 1.00 41.04  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.797 -5.673  16.611 1.00 45.28  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 40.932 -6.884  16.430 1.00 45.32  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.036 -4.836  14.999 1.00 43.48  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.194 -3.776  14.078 1.00 50.07  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.824 -4.834  16.911 1.00 41.22  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.231 -5.222  17.027 1.00 41.95  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.716 -5.520  18.445 1.00 44.48  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.886 -5.875  18.637 1.00 43.68  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.129 -4.164  16.364 1.00 44.50  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 43.908 -4.080  14.865 1.00 61.24  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.807 -2.994  14.291 1.00 59.61  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.780 -5.224  14.199 1.00 50.82  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.840 -5.366  19.442 1.00 40.30  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.231 -5.636  20.818 1.00 39.32  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.232 -7.135  21.093 1.00 40.99  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.348 -7.853  20.596 1.00 38.51  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.287 -4.922  21.804 1.00 39.38  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.265 -3.387  21.730 1.00 44.92  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.192 -2.831  22.649 1.00 44.88  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.636 -2.782  22.067 1.00 47.27  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.219 -7.610  21.872 0.51 37.96  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.223 -7.601  21.873 0.49 37.92  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.316 -9.025  22.248 0.51 37.44  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.357 -9.009  22.264 0.49 37.43  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.688 -9.252  23.634 0.51 38.37  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.714 -9.247  23.639 0.49 38.41  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.486 -10.397 24.037 0.51 36.17  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.524 -10.394 24.040 0.49 36.22  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.769 -9.491  22.230 0.51 42.78  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.828 -9.417  22.290 0.49 42.73  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.555 -8.761  23.157 0.51 50.72  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.381 -9.416  20.985 0.49 49.88  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.411 -8.153  24.370 1.00 35.23  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.795 -8.182  25.706 1.00 34.97  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.604 -7.206  25.741 1.00 36.38  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.743 -6.042  25.333 1.00 36.10  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.823 -7.841  26.832 1.00 41.07  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.172 -7.886  28.217 1.00 41.30  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 45.049 -8.759  26.783 1.00 41.80  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.451 -7.684  26.243 1.00 29.63  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.235 -6.889  26.443 1.00 29.10  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.841 -7.008  27.915 1.00 32.63  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.600 -8.119  28.399 1.00 32.34  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.070 -7.272  25.474 1.00 31.25  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.469 -7.112  23.967 1.00 32.77  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.761 -6.518  25.810 1.00 32.66  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.876 -5.678  23.480 1.00 36.45  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.736 -5.860  28.610 1.00 29.52  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.339 -5.822  30.005 1.00 29.95  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.859 -5.513  30.113 1.00 32.85  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.424 -4.450  29.663 1.00 32.18  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.147 -4.762  30.775 1.00 34.48  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.630 -4.950  30.700 1.00 53.70  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.161 -5.989  31.074 1.00 44.59  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.333 -3.935  30.232 1.00 49.76  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.090 -6.411  30.734 1.00 28.94  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.663 -6.168  30.921 1.00 28.02  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.422 -5.262  32.131 1.00 31.50  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.292 -5.121  33.007 1.00 31.80  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.840 -7.470  31.060 1.00 27.22  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.902 -8.498  29.893 1.00 30.00  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.769 -9.530  30.040 1.00 31.01  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.870 -7.813  28.494 1.00 28.15  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.228 -4.679  32.196 1.00 29.37  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.804 -3.805  33.300 1.00 30.61  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 33.017 -4.550  34.640 1.00 35.15  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.699 -5.739  34.709 1.00 33.92  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.318 -3.457  33.112 1.00 32.31  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.767 -2.434  34.089 1.00 43.99  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.633 -2.765  35.292 1.00 44.76  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.430 -1.321  33.649 1.00 45.11  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.553 -3.894  35.695 1.00 36.53  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.793 -4.616  36.969 1.00 37.08  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.569 -5.232  37.638 1.00 40.41  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.736 -6.123  38.466 1.00 41.15  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.452 -3.567  37.879 1.00 40.25  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.177 -2.248  37.243 1.00 44.91  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.021 -2.491  35.770 1.00 38.77  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.352 -4.790  37.281 1.00 37.15  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.113 -5.330  37.849 1.00 38.23  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.819 -6.740  37.285 1.00 37.51  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 28.991 -7.457  37.845 1.00 36.44  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.931 -4.390  37.527 1.00 41.12  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.790 -4.433  38.530 1.00 62.53  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 27.982 -3.539  39.740 1.00 93.53  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.022 -2.299  39.565 1.00 94.24  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.090 -4.078  40.866 1.00 89.81  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.478 -7.128  36.178 1.00 31.93  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.229 -8.439  35.557 1.00 31.41  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.803 -9.568  36.394 1.00 35.79  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 31.972 -9.550  36.776 1.00 34.44  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.694 -8.482  34.074 1.00 33.41  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 29.985 -7.383  33.233 1.00 34.27  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.489 -9.876  33.450 1.00 30.38  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.375 -7.364  33.318 1.00 40.14  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 29.964 -10.547 36.661 1.00 36.06  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.296 -11.726 37.442 1.00 36.39  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.050 -12.754 36.569 1.00 36.30  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.517 -13.157 35.540 1.00 33.89  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 29.002 -12.314 38.010 1.00 38.34  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.217 -13.592 38.760 1.00 54.82  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.907 -14.663 38.255 1.00 44.73  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.780 -13.506 39.964 1.00 46.47  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.267 -13.209 36.974 1.00 33.80  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 33.002 -14.203 36.158 1.00 33.13  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.246 -15.513 35.906 1.00 36.59  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.362 -16.081 34.815 1.00 35.04  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.275 -14.455 36.971 1.00 36.70  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.424 -13.242 37.846 1.00 41.98  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 33.028 -12.838 38.185 1.00 37.48  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.471 -15.994 36.905 1.00 33.25  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.710 -17.232 36.706 1.00 32.80  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.608 -17.038 35.646 1.00 34.27  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.452 -17.898 34.784 1.00 32.27  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.139 -17.778 38.024 1.00 35.72  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.626 -19.201 37.839 1.00 45.92  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.739 -19.792 38.922 1.00 74.55  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.713 -21.038 39.033 1.00 75.25  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.057 -19.026 39.643 1.00 66.84  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.884 -15.911 35.709 1.00 31.70  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.861 -15.587 34.717 1.00 30.70  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.479 -15.546 33.330 1.00 31.38  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.923 -16.099 32.367 1.00 29.10  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.661 -14.912 33.222 1.00 27.67  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.362 -14.854 31.935 1.00 26.21  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.749 -16.267 31.462 1.00 28.60  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.544 -16.611 30.295 1.00 27.16  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.620 -13.951 32.006 1.00 27.70  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.228 -13.810 30.629 1.00 28.45  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.642 -12.981 29.674 1.00 31.27  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.281 -14.627 30.229 1.00 29.18  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.142 -12.922 28.372 1.00 32.03  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.785 -14.557 28.931 1.00 31.00  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.188 -13.735 27.999 1.00 29.54  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.321 -17.070 32.354 1.00 29.78  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.721 -18.435 32.026 1.00 31.90  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.543 -19.268 31.448 1.00 32.19  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.698 -19.964 30.427 1.00 30.05  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.333 -19.113 33.245 1.00 35.88  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.017 -20.748 32.884 1.00 41.63  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.362 -19.177 32.108 1.00 28.95  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.141 -19.881 31.699 1.00 27.34  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.742 -19.427 30.292 1.00 27.56  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.414 -20.263 29.436 1.00 26.01  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 27.019 -19.654 32.755 1.00 30.53  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.329 -20.450 34.068 1.00 32.05  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.605 -19.968 32.195 1.00 30.09  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.622 -19.916 35.262 1.00 37.32  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.809 -18.119 30.046 1.00 24.95  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.459 -17.573 28.732 1.00 24.98  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.476 -17.924 27.657 1.00 27.76  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.081 -18.212 26.530 1.00 26.28  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.181 -16.082 28.804 1.00 25.46  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.887 -15.744 29.587 1.00 31.19  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.785 -14.288 29.790 1.00 32.49  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.632 -16.235 28.858 1.00 32.80  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.775 -17.933 27.996 1.00 25.28  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.812 -18.347 27.042 1.00 24.45  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.566 -19.821 26.652 1.00 26.89  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.577 -20.159 25.473 1.00 25.52  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.198 -18.130 27.653 1.00 24.94  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.366 -18.424 26.693 1.00 29.27  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.321 -17.489 25.455 1.00 28.45  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.714 -18.298 27.434 1.00 31.91  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.292 -20.690 27.641 1.00 25.00  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 29.944 -22.080 27.356 1.00 25.22  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.731 -22.164 26.420 1.00 26.86  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.756 -22.945 25.475 1.00 27.12  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.646 -22.802 28.669 1.00 28.56  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.884 -23.166 29.473 1.00 43.98  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.008 -23.121 28.900 1.00 45.54  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.733 -23.510 30.668 1.00 45.43  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.666 -21.383 26.689 1.00 24.72  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.476 -21.336 25.820 1.00 22.94  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.853 -20.947 24.376 1.00 24.28  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.374 -21.549 23.399 1.00 22.20  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.425 -20.355 26.375 1.00 23.61  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.313 -20.076 25.384 1.00 24.06  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.355 -21.045 25.096 1.00 27.09  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.293 -18.885 24.652 1.00 26.80  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.359 -20.805 24.153 1.00 27.06  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.298 -18.652 23.692 1.00 29.48  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.339 -19.609 23.451 1.00 27.76  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.687 -19.915 24.230 1.00 21.55  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.084 -19.476 22.876 1.00 21.44  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.653 -20.614 22.043 1.00 25.00  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.325 -20.737 20.864 1.00 24.64  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.160 -18.384 22.979 1.00 22.19  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.643 -17.107 23.574 1.00 24.49  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 29.983 -15.869 23.471 1.00 28.75  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.297 -14.574 24.583 1.00 28.98  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.510 -21.439 22.665 1.00 21.80  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.199 -22.539 21.986 1.00 21.74  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.456 -23.853 21.966 1.00 26.25  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.941 -24.810 21.352 1.00 25.38  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.584 -22.754 22.612 1.00 23.97  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.630 -21.768 22.129 1.00 25.22  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.786 -20.528 22.746 1.00 26.79  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.473 -22.083 21.060 1.00 26.21  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.764 -19.623 22.313 1.00 26.07  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.489 -21.214 20.658 1.00 26.64  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.609 -19.975 21.265 1.00 29.42  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.637 -19.166 20.866 1.00 27.93  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.307 -23.941 22.658 1.00 23.14  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.619 -25.243 22.728 1.00 23.65  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.100 -25.236 22.509 1.00 26.56  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.539 -26.327 22.306 1.00 26.77  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.819 -25.926 24.123 1.00 28.00  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.150 -25.173 25.137 1.00 27.77  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.287 -26.163 24.516 1.00 29.18  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.445 -24.053 22.578 0.67 22.70  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.447 -24.055 22.611 0.33 22.79  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 23.973 -23.862 22.540 0.67 22.58  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 23.985 -23.844 22.556 0.33 22.75  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.325 -24.274 23.884 0.67 25.53  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.295 -24.355 23.846 0.33 26.89  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.135 -24.059 24.055 0.67 25.41  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.068 -24.365 23.917 0.33 27.38  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.307 -24.651 21.404 0.67 23.63  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.359 -24.474 21.306 0.33 24.61  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.975 -24.509 20.164 0.67 23.72  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.065 -25.852 21.473 0.33 27.50  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.110 -24.798 24.858 0.67 23.58  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.092 -24.742 24.872 0.33 24.16  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.555 -25.228 26.145 0.67 24.59  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.597 -25.269 26.147 0.33 25.05  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.793 -24.186 27.211 0.67 28.59  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.814 -24.237 27.250 0.33 28.89  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.926 -23.726 27.397 0.67 26.86  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.949 -23.802 27.473 0.33 27.58  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.128 -26.581 26.603 0.67 26.48  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.291 -26.604 26.505 0.33 26.44  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.811 -27.739 25.651 0.67 30.81  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.168 -27.688 25.424 0.33 32.55  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.803 -28.878 25.855 0.67 42.97  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.076 -28.695 25.727 0.33 37.72  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.739 -29.415 27.217 0.67 51.78  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.924 -29.690 24.660 0.33 38.22  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 23.955 -30.423 27.584 0.67 64.88  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.219 -30.982 24.784 0.33 50.92  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.177 -31.026 26.694 0.67 53.46  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.038 -31.811 23.764 0.33 42.11  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 23.948 -30.841 28.840 0.67 49.54  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.677 -31.458 25.933 0.33 33.51  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.725 -23.838 27.928 1.00 26.32  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.781 -22.829 28.986 1.00 25.97  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.563 -23.470 30.346 1.00 31.68  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.498 -24.051 30.591 1.00 30.37  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.718 -21.756 28.708 1.00 26.78  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.762 -20.530 29.641 1.00 30.32  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.038 -19.704 29.389 1.00 28.13  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.499 -19.690 29.490 1.00 31.78  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.562 -23.355 31.244 1.00 30.61  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.462 -23.928 32.592 1.00 32.33  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.761 -22.926 33.530 1.00 36.84  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.411 -22.245 34.318 1.00 36.65  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.852 -24.352 33.110 1.00 36.36  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.822 -24.963 34.501 1.00 55.16  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.820 -25.531 34.937 1.00 42.39  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.916 -24.846 35.234 1.00 48.67  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.446 -22.786 33.364 1.00 33.69  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.628 -21.845 34.121 1.00 35.17  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.105 -22.501 35.394 1.00 39.63  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.463 -23.552 35.328 1.00 39.45  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.490 -21.363 33.212 1.00 36.14  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.794 -20.062 33.541 1.00 42.34  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.800 -18.888 33.590 1.00 42.59  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.688 -19.800 32.520 1.00 42.06  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.452 -21.918 36.565 1.00 36.59  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.077 -22.447 37.886 1.00 38.74  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.562 -21.323 38.770 1.00 40.55  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.924 -20.156 38.556 1.00 37.24  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.284 -23.124 38.572 1.00 41.02  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.939 -24.250 37.759 1.00 47.00  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.178 -24.833 38.429 1.00 66.21  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.889 -25.457 39.726 1.00 87.02  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.478 -26.713 39.891 1.00 108.23 ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.235 -27.182 41.109 1.00 95.87  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.295 -27.505 38.840 1.00 99.18  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.720 -21.653 39.757 1.00 38.91  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.188 -20.647 40.694 1.00 39.61  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.303 -19.754 41.283 1.00 44.09  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.128 -18.536 41.383 1.00 44.38  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.376 -21.332 41.819 1.00 43.05  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.712 -20.365 42.785 1.00 54.72  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.007 -21.011 43.966 1.00 87.32  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.597 -21.913 44.607 1.00 81.85  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.860 -20.603 44.257 1.00 89.22  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.440 -20.363 41.621 1.00 41.71  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.578 -19.655 42.205 1.00 42.55  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.373 -18.778 41.253 1.00 43.30  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.143 -17.924 41.700 1.00 43.38  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.206 -18.958 39.933 1.00 38.56  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 22.995 -18.145 39.001 1.00 36.04  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.152 -17.293 38.038 1.00 38.63  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.725 -16.488 37.293 1.00 36.28  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 23.984 -19.050 38.235 1.00 34.08  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.339 -19.989 37.233 1.00 42.41  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.284 -19.697 36.663 1.00 33.44  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 23.977 -21.122 36.961 1.00 36.71  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.809 -17.495 38.016 1.00 35.93  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.927 -16.834 37.039 1.00 35.54  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.055 -15.301 37.026 1.00 36.74  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.074 -14.718 35.934 1.00 33.53  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.449 -17.278 37.112 1.00 40.00  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.651 -16.724 35.892 1.00 40.62  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.796 -16.965 38.467 1.00 39.81  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.463 -17.533 35.476 1.00 44.24  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.162 -14.657 38.196 1.00 35.45  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.301 -13.198 38.227 1.00 36.40  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.603 -12.722 37.582 1.00 38.02  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.567 -11.779 36.785 1.00 35.88  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.127 -12.625 39.647 1.00 40.85  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.758 -12.928 40.270 1.00 48.14  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.325 -12.579 39.204 1.00 54.65  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.247 -10.787 39.329 1.00 52.73  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.746 -13.391 37.893 1.00 35.32  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.056 -13.042 37.307 1.00 34.46  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.062 -13.337 35.815 1.00 35.46  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.595 -12.548 35.037 1.00 33.37  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.175 -13.818 37.988 1.00 35.68  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.483 -14.481 35.406 1.00 30.62  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.427 -14.843 33.978 1.00 28.36  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.615 -13.800 33.196 1.00 31.12  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.097 -13.333 32.159 1.00 29.13  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.906 -16.296 33.777 1.00 31.57  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.574 -16.592 32.302 1.00 29.38  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.925 -17.301 34.303 1.00 32.19  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.412 -13.426 33.690 0.20 29.95  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.415 -13.420 33.691 0.80 30.72  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.556 -12.435 33.027 0.20 30.78  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.587 -12.430 32.990 0.80 32.14  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.261 -11.085 32.883 0.20 34.86  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.291 -11.078 32.870 0.80 35.26  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.237 -10.505 31.796 0.20 33.95  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.281 -10.479 31.793 0.80 33.95  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.219 -12.262 33.761 0.20 34.62  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.224 -12.250 33.662 0.80 36.22  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.242 -11.387 33.005 0.20 39.03  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.298 -11.327 32.873 0.80 40.80  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.724 -11.086 33.916 0.20 45.17  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.607 -11.351 33.488 0.80 47.17  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.168 -9.633  33.100 0.20 42.58  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.762 -10.316 35.025 0.80 45.28  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.890 -10.599 33.972 1.00 32.21  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.623 -9.316  33.987 1.00 32.77  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.785 -9.347  32.979 1.00 33.04  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 23.973 -8.383  32.212 1.00 31.35  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.133 -9.023  35.392 1.00 34.29  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.525 -10.479 32.937 1.00 29.09  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.630 -10.646 31.988 1.00 28.82  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.088 -10.689 30.539 1.00 31.23  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.666 -10.039 29.667 1.00 28.71  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.539 -11.852 32.355 1.00 32.32  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.854 -11.829 33.750 1.00 31.42  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.849 -11.876 31.548 1.00 31.96  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 23.978 -11.439 30.283 1.00 27.83  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.384 -11.522 28.937 1.00 26.76  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.868 -10.150 28.479 1.00 30.22  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.024 -9.798  27.310 1.00 28.66  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.276 -12.578 28.896 1.00 27.61  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.337 -9.328  29.409 1.00 28.06  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.898 -7.979  29.017 1.00 28.77  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.095 -7.104  28.576 1.00 31.40  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.047 -6.438  27.541 1.00 31.47  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.115 -7.316  30.162 1.00 32.10  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.732 -7.933  30.367 1.00 37.48  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 18.976 -7.373  31.914 1.00 45.62  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.731 -5.620  31.530 1.00 43.46  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.175 -7.141  29.351 1.00 28.76  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.408 -6.399  29.078 1.00 27.89  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 26.022 -6.887  27.744 1.00 30.61  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.407 -6.071  26.907 1.00 29.46  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.374 -6.660  30.229 1.00 28.93  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.787 -6.167  30.001 1.00 29.72  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.097 -4.809  30.080 1.00 32.96  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.825 -7.063  29.745 1.00 29.61  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.405 -4.354  29.897 1.00 31.59  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.138 -6.623  29.587 1.00 29.84  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.417 -5.266  29.646 1.00 32.22  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.714 -4.857  29.546 1.00 30.20  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.057 -8.210  27.533 1.00 27.20  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.619 -8.800  26.310 1.00 25.25  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.708 -8.670  25.088 1.00 28.69  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.137 -8.947  23.960 1.00 28.23  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.028 -10.263 26.542 1.00 24.14  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.177 -10.545 27.543 1.00 26.97  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.435 -12.076 27.638 1.00 27.47  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.481 -9.816  27.142 1.00 29.66  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.438 -8.293  25.309 1.00 26.69  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.441 -8.157  24.241 1.00 27.41  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.186 -9.509  23.556 1.00 30.98  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.426 -9.682  22.361 1.00 29.80  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.812 -7.045  23.245 1.00 28.65  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 23.953 -5.671  23.904 1.00 31.52  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.652 -4.701  22.981 1.00 42.73  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.550 -4.791  21.763 1.00 36.31  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.406 -3.775  23.535 1.00 39.31  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.756 -10.477 24.369 1.00 27.82  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.404 -11.846 23.953 1.00 27.33  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.907 -11.999 24.215 1.00 33.64  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.470 -12.496 25.268 1.00 30.91  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.261 -12.852 24.731 1.00 28.49  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.755 -12.680 24.443 1.00 29.54  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.786 -13.762 25.447 1.00 32.67  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.428 -15.415 24.620 1.00 29.87  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.116 -11.456 23.279 1.00 33.34  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.649 -11.344 23.373 1.00 35.23  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.896 -12.631 23.720 1.00 35.86  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 16.994 -12.577 24.551 1.00 35.22  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.056 -10.739 22.090 1.00 38.45  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.532 -9.317  21.833 1.00 52.56  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.244 -13.774 23.101 1.00 32.55  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.515 -15.015 23.396 1.00 34.10  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.746 -15.500 24.828 1.00 34.98  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.797 -15.969 25.473 1.00 36.13  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.823 -16.098 22.363 1.00 35.93  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.392 -15.731 20.976 1.00 40.89  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.066 -15.469 20.680 1.00 44.64  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.122 -15.638 19.840 1.00 42.70  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 16.034 -15.195 19.385 1.00 44.61  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.244 -15.297 18.836 1.00 43.74  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 18.981 -15.330 25.346 1.00 29.09  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.308 -15.697 26.733 1.00 28.64  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.519 -14.800 27.699 1.00 34.27  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.910 -15.312 28.645 1.00 32.02  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.834 -15.681 27.030 1.00 30.88  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.100 -15.945 28.512 1.00 30.93  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.576 -16.691 26.160 1.00 30.00  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.519 -13.470 27.454 1.00 31.13  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.759 -12.500 28.275 1.00 31.66  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.272 -12.922 28.347 1.00 37.97  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.718 -12.987 29.441 1.00 36.62  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.938 -11.033 27.777 1.00 34.96  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.086 -10.051 28.599 1.00 35.45  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.402 -10.614 27.821 1.00 33.88  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.674 -13.266 27.193 0.61 36.52  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.647 -13.185 27.181 0.39 36.21  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.284 -13.713 27.073 0.61 37.88  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.243 -13.590 27.043 0.39 37.63  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 13.980 -14.951 27.935 0.61 40.72  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.882 -14.802 27.907 0.39 41.34  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 12.993 -14.926 28.673 0.61 41.77  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.867 -14.767 28.603 0.39 42.64  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.931 -13.965 25.595 0.61 40.12  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.910 -13.882 25.565 0.39 39.71  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.497 -14.412 25.359 0.61 54.49  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.666 -12.667 24.685 0.39 52.32  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.573 -13.625 25.656 0.61 58.37  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.259 -11.614 25.222 0.39 55.27  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.303 -15.545 24.871 0.61 60.12  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.858 -12.778 23.454 0.39 58.32  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.816 -16.022 27.865 0.61 35.21  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.715 -15.864 27.870 0.39 36.19  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.544 -17.224 28.681 0.61 35.52  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.469 -17.095 28.631 0.39 36.42  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.732 -16.944 30.174 0.61 38.70  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.669 -16.865 30.136 0.39 39.44  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.021 -17.531 30.985 0.61 38.63  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.890 -17.401 30.925 0.39 39.74  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.304 -18.480 28.213 0.61 36.98  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.273 -18.269 28.062 0.39 41.09  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.702 -19.615 28.845 0.61 37.13  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.224 -18.210 26.635 0.39 38.91  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.795 -18.450 28.554 0.61 32.02  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.724 -19.611 28.508 0.39 40.97  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.682 -16.054 30.530 1.00 35.16  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.928 -15.691 31.942 1.00 35.91  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.702 -14.986 32.497 1.00 42.39  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.241 -15.352 33.587 1.00 41.40  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.172 -14.822 32.078 1.00 35.20  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.723 -15.719 31.848 1.00 37.69  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.153 -14.009 31.732 0.48 40.42  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.158 -13.996 31.749 0.52 40.72  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.949 -13.243 32.084 0.48 42.22  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 12.957 -13.249 32.142 0.52 42.66  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.757 -14.175 32.335 0.48 46.62  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.750 -14.179 32.348 0.52 46.77  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.019 -13.985 33.304 0.48 47.13  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 10.999 -13.998 33.308 0.52 47.22  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.589 -12.249 30.966 0.48 43.54  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.627 -12.158 31.117 0.52 44.73  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.533 -11.064 30.861 0.48 56.07  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.396 -10.860 31.339 0.52 59.12  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.931 -9.927  30.054 0.48 68.97  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.685 -9.671  30.711 0.52 70.82  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.942 -8.929  29.695 0.48 74.45  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.814 -9.659  29.250 0.52 76.27  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.294 -7.898  30.457 0.48 84.56  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.605 -8.834  28.570 0.52 86.28  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.713 -7.705  31.635 0.48 74.72  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.339 -7.928  29.207 0.52 70.89  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.228 -7.052  30.047 0.48 66.22  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.661 -8.902  27.246 0.52 70.84  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.589 -15.188 31.466 1.00 42.66  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.499 -16.173 31.552 1.00 44.51  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.652 -17.087 32.765 1.00 47.87  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.670  -17.316 33.468 1.00 48.02  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.374 -16.982 30.251 1.00 46.53  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.820  -16.140 29.110 1.00 66.44  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.682  -16.903 27.811 1.00 79.21  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.264  -15.969 26.701 1.00 93.10  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.428  -16.657 25.685 1.00 106.05 ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.890 -17.572 33.033 1.00 42.50  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.163 -18.438 34.186 1.00 42.77  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 11.974 -17.673 35.490 1.00 47.93  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.444 -18.236 36.449 1.00 47.66  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.564 -19.052 34.100 1.00 42.86  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.689 -20.330 33.287 1.00 44.74  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.114 -20.434 32.022 1.00 47.97  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.449 -21.398 33.753 1.00 47.65  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.250 -21.607 31.265 1.00 48.97  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.592 -22.568 32.989 1.00 49.63  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 13.987 -22.665 31.756 1.00 47.36  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.356 -16.382 35.512 1.00 44.15  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.166 -15.524 36.696 1.00 45.70  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.666 -15.267 36.960 1.00 52.98  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.218 -15.412 38.106 1.00 54.11  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.021 -14.234 36.599 1.00 47.85  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.509 -14.591 36.787 1.00 46.73  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.582 -13.170 37.645 1.00 50.00  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.488 -13.606 36.208 1.00 51.06  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.887  -14.949 35.896 1.00 50.97  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.443  -14.700 35.993 1.00 53.70  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.687  -15.930 36.527 1.00 58.55  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.728  -15.771 37.276 1.00 59.57  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.864  -14.258 34.642 1.00 56.77  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.143  -17.147 36.173 1.00 53.70  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.522  -18.394 36.636 1.00 55.21  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.699  -18.631 38.145 1.00 61.10  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.828  -19.233 38.759 1.00 61.55  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.076  -19.577 35.853 1.00 54.37  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.825  -18.187 38.730 1.00 59.60  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.129  -18.397 40.150 1.00 62.56  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.508  -17.363 41.106 1.00 71.61  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.439  -17.630 42.310 1.00 74.16  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.637 -18.490 40.370 1.00 65.85  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 11.093 -19.824 40.198 1.00 76.10  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.030  -16.210 40.584 1.00 68.43  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.426  -15.149 41.404 1.00 89.22  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 5.990  -15.466 41.860 1.00 131.70 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.614  -16.626 42.022 1.00 98.39  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.502  -13.781 40.696 1.00 89.70  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.481  -13.572 39.586 1.00 100.00 ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.641  -12.336 38.718 1.00 121.73 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.771  -11.802 38.619 1.00 115.88 ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.627  -11.912 38.117 1.00 115.43 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.227 -35.074 5.836  1.00 32.56  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.291 -33.934 6.322  1.00 33.23  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.439 -36.302 6.708  1.00 31.73  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.954 -35.312 4.555  0.66 29.99  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.974 -35.312 4.548  0.34 30.80  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.735 -34.256 3.569  0.66 28.93  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.697 -34.240 3.593  0.34 30.24  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.230 -34.115 3.285  0.66 33.02  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.192 -34.093 3.421  0.34 32.77  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.520 -35.126 3.224  0.66 33.17  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.453 -35.080 3.523  0.34 32.29  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.520 -34.575 2.274  0.66 27.74  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.381 -34.478 2.222  0.34 29.45  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.021 -34.565 2.459  0.66 27.94  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.765 -35.557 1.382  0.34 30.63  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.803 -35.601 2.880  0.66 30.52  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.134 -36.868 1.337  0.34 33.80  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.907 -33.454 2.248  0.66 27.45  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.683 -35.413 0.446  0.34 30.58  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.119 -35.198 2.963  0.66 29.49  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.319 -37.562 0.475  0.34 33.31  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.213 -33.890 2.569  0.66 30.47  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.428 -36.692 -0.098 0.34 34.50  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.720 -32.116 1.856  0.66 28.17  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.869 -34.335 0.050  0.34 31.51  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.333 -33.055 2.452  0.66 29.93  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.410 -36.919 -1.032 0.34 33.91  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.831 -31.298 1.721  0.66 29.12  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.857 -34.564 -0.870 0.34 33.08  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.115 -31.762 2.034  0.66 29.67  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.642 -35.840 -1.408 0.34 33.63  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.740 -32.871 3.132  1.00 27.86  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.311 -32.572 2.887  1.00 27.83  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.171 -31.506 1.794  1.00 30.58  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.148 -30.800 1.478  1.00 29.70  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.605 -32.072 4.196  1.00 31.34  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.626 -33.131 5.301  1.00 31.54  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.190 -30.732 4.699  1.00 30.37  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.940 -31.339 1.300  1.00 28.61  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.552 -30.254 0.420  1.00 28.62  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.185 -29.117 1.401  1.00 33.23  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.174 -29.240 2.107  1.00 32.53  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.334 -30.631 -0.462 1.00 30.46  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.631 -31.901 -1.329 1.00 28.74  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.891 -29.401 -1.313 1.00 32.03  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.922 -31.792 -2.309 1.00 32.90  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.971 -28.017 1.470  1.00 32.57  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.650 -26.952 2.442  1.00 33.34  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.395 -26.151 2.088  1.00 37.87  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.084 -25.982 0.911  1.00 36.46  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.913 -26.081 2.443  1.00 35.24  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.487 -26.267 1.065  1.00 38.62  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.211 -27.707 0.719  1.00 34.35  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.725 -25.586 3.108  1.00 36.49  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.495 -10.128 16.467 1.00 29.33  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.894 -8.866  16.498 1.00 29.64  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.872 -8.585  17.398 1.00 30.89  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.437 -9.600  18.247 1.00 32.34  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.274 -10.785 19.815 1.00 36.09  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.987 -10.877 18.190 1.00 31.02  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.278 -10.246 11.910 1.00 33.14  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.409 -10.579 13.244 1.00 30.17  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.378 -10.219 14.135 1.00 31.01  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.279 -11.734 19.198 1.00 34.31  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.456 -11.046 20.693 1.00 36.62  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.433 -9.572  19.221 1.00 33.95  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 25.017 -11.148 17.296 1.00 29.15  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.393 -10.535 15.459 1.00 27.98  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.288 -9.603  13.646 1.00 33.73  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.279 -9.360  12.347 1.00 34.75  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.839 -8.588  11.756 0.41 35.11  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 28.952 -11.479 13.837 0.63 27.88  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.194 -9.623  11.432 1.00 34.26  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.331 -15.342 22.670 1.00 42.68  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.525 -35.352 -1.282 0.66 51.44  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.237 -35.139 -0.637 0.66 52.24  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.648 -34.456 -0.245 0.66 50.73  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 17.962 -36.987 -0.807 0.66 51.35  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 25.819 -3.546  26.484 1.00 38.42  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 35.721 -25.789 25.550 1.00 44.07  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 26.801 -32.108 16.149 1.00 49.26  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 38.464 -15.050 15.537 1.00 39.32  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 22.692 -5.451  19.966 1.00 57.85  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 20.791 -5.868  26.232 1.00 43.76  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 41.108 -21.643 25.149 1.00 47.18  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 44.392 -0.873  17.911 1.00 56.67  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 37.798 2.398   19.788 1.00 46.02  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 37.680 -20.497 26.973 1.00 38.97  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 29.834 -32.226 9.550  1.00 54.23  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 23.411 -5.867  32.969 1.00 39.18  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 45.015 -11.136 18.798 1.00 68.85  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 33.309 -20.873 29.608 1.00 53.40  ? 314 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 6 .   ? 21.698 -29.499 -5.245 1.00 42.63  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 19.853 -9.720  37.086 1.00 43.75  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 43.605 -6.642  32.008 1.00 54.36  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 15.464 -10.066 25.095 1.00 54.17  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 16.459 -27.492 -3.287 1.00 58.05  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 17.895 -29.434 7.697  1.00 38.56  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 30.353 1.361   33.937 1.00 70.26  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 22.679 -27.712 17.781 1.00 52.21  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 31.658 -0.965  15.929 1.00 48.20  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 20.449 -13.550 20.529 1.00 51.08  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 27.220 -10.271 35.930 1.00 41.48  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 37.228 -12.563 40.324 1.00 67.18  ? 326 HOH   A O   1 
HETATM 1227 O  O   A HOH   F 6 .   ? 19.064 -23.013 4.409  0.67 47.35  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 27.302 -28.234 18.633 1.00 29.88  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 28.284 -8.953  39.997 1.00 52.05  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 32.621 -24.667 32.239 1.00 67.72  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 28.775 -21.761 41.651 1.00 75.11  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 25.713 -2.982  20.101 1.00 62.43  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 21.465 -27.150 14.652 0.50 42.36  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 29.398 -27.391 20.658 1.00 27.88  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 28.223 -23.782 31.700 1.00 45.19  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 41.232 -16.916 15.243 1.00 43.38  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 41.322 -12.790 14.096 1.00 113.44 ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 23.279 -17.122 44.310 1.00 67.04  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 30.368 -0.709  37.078 1.00 60.59  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 21.535 -30.036 14.204 1.00 71.99  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 34.416 -23.953 29.907 1.00 81.92  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 12.232 -18.086 25.902 1.00 64.42  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 24.894 -26.848 19.057 1.00 38.57  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 22.965 -28.275 12.700 1.00 27.52  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 37.325 -6.440  34.324 1.00 45.80  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 23.951 -15.825 21.299 1.00 35.32  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 21.933 -25.019 18.374 1.00 27.51  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 14.354 -16.825 23.520 1.00 47.15  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 26.106 -22.655 29.933 1.00 30.84  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 10.745 -11.486 34.474 1.00 54.71  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 20.872 -7.379  19.900 1.00 54.84  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 12.704 -20.639 42.507 1.00 62.47  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 28.886 -0.359  17.041 1.00 78.20  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 36.873 -5.731  12.261 1.00 42.22  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 29.060 -31.190 7.245  1.00 39.25  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 18.011 -34.520 8.321  1.00 37.03  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 44.375 -12.701 41.385 1.00 59.90  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 46.001 -14.207 21.603 1.00 62.48  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 30.662 -28.966 22.705 1.00 47.06  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 26.922 -16.643 38.739 1.00 58.85  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 28.523 -24.250 34.429 1.00 57.64  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 34.804 -18.970 13.888 0.50 27.69  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 42.418 -10.496 15.508 1.00 58.61  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 46.835 -21.669 18.091 1.00 52.59  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 26.908 -35.396 11.642 1.00 63.60  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 46.222 -15.925 27.639 1.00 76.32  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 37.956 -16.634 13.183 0.50 32.17  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 43.996 -4.438  25.849 1.00 49.29  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 37.499 3.336   15.839 1.00 47.60  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 41.277 -7.807  46.492 1.00 60.57  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 26.070 -21.942 38.674 1.00 45.79  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 20.212 -15.973 40.935 1.00 38.95  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 43.832 -10.696 35.104 1.00 75.93  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 27.135 -2.359  16.121 1.00 64.94  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 34.106 -7.970  35.717 1.00 41.96  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 41.053 -1.488  11.655 1.00 71.63  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 21.029 -23.447 6.248  1.00 59.73  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 29.647 -22.670 36.917 1.00 71.13  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 39.064 -18.972 33.417 1.00 50.39  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 17.350 -24.578 -2.198 1.00 68.09  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 11.618 -15.274 40.565 1.00 81.48  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 41.200 -7.061  35.964 1.00 49.30  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 26.187 -8.063  9.052  1.00 50.18  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 46.324 -18.913 19.614 1.00 55.45  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 47.181 -25.241 21.610 1.00 59.42  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 45.273 -12.634 23.675 1.00 51.89  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 26.385 -30.786 19.031 1.00 63.77  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 34.797 -29.197 26.077 1.00 68.97  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 26.087 -19.277 41.717 1.00 65.33  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 31.847 -31.885 14.557 1.00 41.92  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 45.491 -10.884 30.331 1.00 59.93  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 19.851 -25.565 41.338 1.00 83.67  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 36.935 -2.264  11.573 1.00 62.05  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 4.295  -20.374 37.939 1.00 62.58  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 27.690 -23.077 13.888 0.50 30.84  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 44.599 -16.467 29.763 1.00 56.81  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 42.200 -5.863  11.840 1.00 75.09  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 44.655 -8.649  17.772 1.00 78.94  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 46.026 -8.985  44.180 1.00 55.76  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 23.673 -15.726 17.813 1.00 46.10  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 40.369 -19.630 29.045 1.00 40.97  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 33.079 -29.799 21.521 1.00 45.57  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 16.711 -6.515  27.554 1.00 67.35  ? 403 HOH   A O   1 
HETATM 1304 O  O   A HOH   F 6 .   ? 12.219 -20.936 27.931 0.66 47.54  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 10.368 -11.677 40.048 1.00 68.32  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 45.853 -17.098 17.400 1.00 71.64  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 25.681 -4.578  17.927 1.00 56.36  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 30.439 -10.660 40.624 1.00 47.71  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 41.301 -17.083 35.198 1.00 49.51  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 47.438 -6.688  20.295 1.00 70.27  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 22.922 -14.989 40.449 1.00 37.45  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 46.867 -20.149 21.955 1.00 72.25  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 35.103 -29.783 23.437 1.00 50.35  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 32.120 -15.684 39.869 1.00 40.01  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 27.090 -1.677  22.052 1.00 56.94  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 27.338 -25.525 28.358 1.00 61.81  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 35.189 1.843   13.535 1.00 60.29  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 33.499 -33.037 12.096 1.00 52.40  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 21.188 -23.322 42.133 1.00 50.05  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 19.611 -27.293 10.072 1.00 58.06  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 32.420 -8.985  39.791 1.00 63.68  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 34.540 -18.873 36.326 1.00 69.01  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 42.054 -8.048  13.756 1.00 64.41  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 25.652 -16.117 41.129 1.00 56.91  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 33.523 -0.349  20.121 1.00 48.02  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 45.785 -5.556  23.759 1.00 51.93  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 33.958 -32.842 21.999 1.00 71.15  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 29.569 -0.798  22.392 1.00 63.89  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 39.893 -5.565  33.984 1.00 47.34  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 37.196 -31.511 23.476 1.00 88.68  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 23.471 -30.557 19.308 1.00 70.12  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 44.369 -4.204  29.094 1.00 71.98  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 42.783 -18.276 30.718 1.00 54.11  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 26.400 -29.455 22.652 1.00 61.73  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 31.756 -26.107 27.093 1.00 63.88  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 22.300 -10.559 14.669 1.00 48.76  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 28.825 -2.600  13.239 1.00 83.19  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 26.912 -34.525 18.001 1.00 69.52  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 23.078 -3.133  26.845 1.00 67.50  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 31.864 -0.044  13.366 1.00 69.78  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 30.599 -34.301 14.851 1.00 66.12  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 19.465 -31.760 13.825 1.00 77.85  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 35.340 -4.226  10.662 1.00 51.64  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 19.740 -8.147  24.616 1.00 58.40  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 48.003 -23.464 19.743 1.00 65.90  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 36.833 -24.507 27.679 1.00 60.47  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 47.417 -28.493 17.655 1.00 62.58  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 46.689 -14.639 18.295 1.00 68.40  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 24.518 -21.807 41.139 1.00 65.99  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 47.232 -11.864 25.404 1.00 77.54  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 47.036 -12.666 28.551 1.00 65.40  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 32.216 -1.138  22.355 1.00 62.84  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 43.886 -13.726 13.888 0.50 100.25 ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 12.053 -18.871 22.738 1.00 70.83  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 35.829 -21.244 30.603 1.00 65.39  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 19.445 -7.732  35.301 1.00 58.97  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 25.313 -5.717  34.913 1.00 64.84  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 34.033 -17.620 39.675 1.00 69.68  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 17.073 -7.930  25.042 1.00 69.43  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 45.572 -8.399  31.348 1.00 66.33  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 17.063 -28.143 9.913  1.00 56.25  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 43.140 -3.013  33.964 1.00 62.12  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 19.942 -14.880 43.402 1.00 57.33  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 19.109 -28.254 13.803 0.50 74.50  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 33.830 -11.145 41.662 0.50 71.25  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 32.572 -20.670 36.941 1.00 80.25  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 28.274 -29.830 24.601 1.00 73.36  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 33.830 -14.019 41.662 0.50 44.57  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 12.568 -18.279 20.017 1.00 66.69  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 21.237 -5.756  34.735 1.00 56.02  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 16.743 -6.865  34.974 1.00 81.87  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 32.021 -23.914 35.065 1.00 77.96  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 45.143 -12.377 15.903 1.00 80.22  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 39.500 -5.547  11.559 1.00 76.94  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 16.699 -30.127 12.431 1.00 61.40  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   G 6 .   ? 12.193 -24.255 0.004  1.00 57.51  ? 201 HOH   D O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 22.624 -34.013 8.845  1.00 38.51  ? 202 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 14.933 -25.801 -1.819 1.00 48.52  ? 203 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 17.725 -36.261 6.036  1.00 46.12  ? 204 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 11.568 -23.520 2.953  1.00 56.28  ? 205 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 20.768 -38.309 4.030  1.00 51.30  ? 206 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 20.795 -39.512 -2.045 1.00 67.23  ? 207 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 10.743 -24.621 5.405  1.00 64.28  ? 208 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 20.105 -35.339 10.110 1.00 46.10  ? 209 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.632 -36.496 9.992  1.00 56.64  ? 210 HOH   D 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   . ASP A 5   ? 0.8877 1.0674 0.7625 0.0366  -0.1386 -0.0239 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8800 1.0535 0.7375 0.0195  -0.1288 -0.0259 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8530 1.0583 0.7369 0.0077  -0.1237 -0.0427 6   ASP A C   
4    O O   . ASP A 5   ? 0.8424 1.0743 0.7569 0.0119  -0.1272 -0.0527 6   ASP A O   
5    C CB  . ASP A 5   ? 0.9025 1.0468 0.7506 0.0102  -0.1110 -0.0185 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0980 1.2210 0.9112 -0.0009 -0.1053 -0.0135 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0981 1.2342 0.9100 -0.0124 -0.1021 -0.0225 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.2071 1.2999 0.9944 0.0009  -0.1028 -0.0017 6   ASP A OD2 
9    N N   . SER A 6   ? 0.7487 0.9504 0.6203 -0.0075 -0.1144 -0.0466 7   SER A N   
10   C CA  . SER A 6   ? 0.6983 0.9234 0.5901 -0.0203 -0.1074 -0.0620 7   SER A CA  
11   C C   . SER A 6   ? 0.6378 0.8506 0.5427 -0.0315 -0.0877 -0.0641 7   SER A C   
12   O O   . SER A 6   ? 0.6195 0.8389 0.5302 -0.0441 -0.0788 -0.0740 7   SER A O   
13   C CB  . SER A 6   ? 0.7761 1.0068 0.6456 -0.0288 -0.1117 -0.0667 7   SER A CB  
14   O OG  . SER A 6   ? 0.9423 1.1450 0.7819 -0.0359 -0.1036 -0.0583 7   SER A OG  
15   N N   . CYS A 7   ? 0.5286 0.7234 0.4379 -0.0261 -0.0819 -0.0553 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4899 0.6722 0.4100 -0.0340 -0.0661 -0.0563 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4616 0.6611 0.4093 -0.0403 -0.0597 -0.0686 8   CYS A C   
18   O O   . CYS A 7   ? 0.4494 0.6704 0.4133 -0.0364 -0.0664 -0.0752 8   CYS A O   
19   C CB  . CYS A 7   ? 0.5098 0.6721 0.4291 -0.0261 -0.0634 -0.0452 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5995 0.7325 0.4844 -0.0243 -0.0634 -0.0315 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3506 0.5394 0.3029 -0.0496 -0.0467 -0.0720 9   ILE A N   
22   C CA  . ILE A 8   ? 0.3054 0.4995 0.2786 -0.0556 -0.0383 -0.0807 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3349 0.5102 0.3121 -0.0510 -0.0323 -0.0725 9   ILE A C   
24   O O   . ILE A 8   ? 0.3267 0.4855 0.2911 -0.0470 -0.0321 -0.0630 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3446 0.5387 0.3193 -0.0683 -0.0292 -0.0912 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3574 0.5308 0.3185 -0.0715 -0.0221 -0.0871 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3333 0.5503 0.3071 -0.0735 -0.0355 -0.1013 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.4375 0.6066 0.4012 -0.0822 -0.0125 -0.0973 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2675 0.4438 0.2606 -0.0531 -0.0266 -0.0768 10  GLN A N   
30   N N   B GLN A 9   ? 0.2837 0.4620 0.2773 -0.0523 -0.0277 -0.0768 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2623 0.4204 0.2570 -0.0492 -0.0215 -0.0693 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2792 0.4411 0.2761 -0.0484 -0.0227 -0.0701 10  GLN A CA  
33   C C   A GLN A 9   ? 0.3016 0.4477 0.3012 -0.0572 -0.0109 -0.0741 10  GLN A C   
34   C C   B GLN A 9   ? 0.3265 0.4758 0.3277 -0.0566 -0.0119 -0.0745 10  GLN A C   
35   O O   A GLN A 9   ? 0.3121 0.4672 0.3199 -0.0648 -0.0071 -0.0839 10  GLN A O   
36   O O   B GLN A 9   ? 0.3280 0.4856 0.3370 -0.0646 -0.0077 -0.0844 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2763 0.4432 0.2815 -0.0408 -0.0263 -0.0672 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2892 0.4632 0.2987 -0.0410 -0.0274 -0.0700 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.3417 0.4931 0.3515 -0.0395 -0.0194 -0.0630 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3185 0.4755 0.3264 -0.0342 -0.0253 -0.0605 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.6198 0.7741 0.6353 -0.0294 -0.0240 -0.0583 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.5075 0.6674 0.5303 -0.0358 -0.0196 -0.0652 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.5507 0.7183 0.5679 -0.0214 -0.0336 -0.0577 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3894 0.5699 0.4272 -0.0370 -0.0208 -0.0745 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.5465 0.6869 0.5639 -0.0290 -0.0178 -0.0549 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.4637 0.6037 0.4826 -0.0363 -0.0130 -0.0598 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2840 0.4092 0.2777 -0.0555 -0.0065 -0.0677 11  PHE A N   
48   N N   B PHE A 10  ? 0.2953 0.4238 0.2903 -0.0547 -0.0076 -0.0676 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2793 0.3888 0.2742 -0.0608 0.0017  -0.0705 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2933 0.4049 0.2886 -0.0598 0.0006  -0.0699 11  PHE A CA  
51   C C   A PHE A 10  ? 0.3085 0.4121 0.3081 -0.0583 0.0037  -0.0673 11  PHE A C   
52   C C   B PHE A 10  ? 0.3237 0.4298 0.3242 -0.0576 0.0029  -0.0671 11  PHE A C   
53   O O   A PHE A 10  ? 0.2921 0.3864 0.2884 -0.0518 0.0021  -0.0592 11  PHE A O   
54   O O   B PHE A 10  ? 0.3155 0.4148 0.3136 -0.0507 0.0007  -0.0591 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2957 0.3878 0.2825 -0.0598 0.0040  -0.0674 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.3161 0.4113 0.3029 -0.0580 0.0022  -0.0656 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.3133 0.3877 0.2992 -0.0638 0.0104  -0.0710 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3413 0.4403 0.3241 -0.0628 0.0032  -0.0715 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3507 0.4248 0.3370 -0.0718 0.0148  -0.0799 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3858 0.5000 0.3642 -0.0633 -0.0018 -0.0725 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3273 0.3831 0.3097 -0.0595 0.0114  -0.0655 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3850 0.4709 0.3670 -0.0663 0.0086  -0.0763 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3706 0.4229 0.3523 -0.0748 0.0206  -0.0824 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.4029 0.5204 0.3762 -0.0690 0.0000  -0.0788 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3576 0.3933 0.3353 -0.0619 0.0157  -0.0677 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.4312 0.5209 0.4106 -0.0709 0.0105  -0.0831 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3404 0.3727 0.3170 -0.0692 0.0203  -0.0757 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.4026 0.5086 0.3776 -0.0731 0.0068  -0.0846 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2798 0.3898 0.2870 -0.0647 0.0082  -0.0748 12  THR A N   
70   C CA  . THR A 11  ? 0.2807 0.3877 0.2929 -0.0649 0.0121  -0.0745 12  THR A CA  
71   C C   . THR A 11  ? 0.3206 0.4023 0.3229 -0.0620 0.0149  -0.0662 12  THR A C   
72   O O   . THR A 11  ? 0.3151 0.3963 0.3194 -0.0568 0.0138  -0.0615 12  THR A O   
73   C CB  . THR A 11  ? 0.3691 0.4812 0.3874 -0.0763 0.0200  -0.0858 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3559 0.4954 0.3854 -0.0786 0.0160  -0.0947 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.4235 0.5351 0.4476 -0.0784 0.0257  -0.0877 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2921 0.3537 0.2840 -0.0647 0.0180  -0.0653 13  ARG A N   
77   C CA  . ARG A 12  ? 0.3146 0.3524 0.2962 -0.0617 0.0192  -0.0586 13  ARG A CA  
78   C C   . ARG A 12  ? 0.3305 0.3659 0.3101 -0.0527 0.0131  -0.0512 13  ARG A C   
79   O O   . ARG A 12  ? 0.3204 0.3390 0.2929 -0.0496 0.0128  -0.0467 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3983 0.4135 0.3689 -0.0668 0.0237  -0.0612 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.5344 0.5427 0.5014 -0.0781 0.0325  -0.0682 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.8120 0.8114 0.7742 -0.0810 0.0372  -0.0663 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.9796 0.9506 0.9249 -0.0769 0.0360  -0.0586 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.1030 1.0649 1.0416 -0.0769 0.0378  -0.0547 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.9743 0.9107 0.8960 -0.0730 0.0352  -0.0481 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8522 0.8311 0.8012 -0.0804 0.0419  -0.0582 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2692 0.3201 0.2534 -0.0493 0.0086  -0.0504 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2865 0.3340 0.2674 -0.0436 0.0052  -0.0451 14  HIS A CA  
89   C C   . HIS A 13  ? 0.3115 0.3517 0.2907 -0.0389 0.0044  -0.0388 14  HIS A C   
90   O O   . HIS A 13  ? 0.3132 0.3425 0.2887 -0.0365 0.0038  -0.0365 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2831 0.3453 0.2645 -0.0425 0.0016  -0.0449 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.3082 0.3656 0.2848 -0.0393 0.0005  -0.0409 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.3161 0.3681 0.2921 -0.0406 0.0023  -0.0444 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.3136 0.3710 0.2864 -0.0356 -0.0014 -0.0350 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.3103 0.3615 0.2835 -0.0388 0.0021  -0.0415 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.3064 0.3589 0.2758 -0.0363 0.0003  -0.0354 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2747 0.3221 0.2578 -0.0373 0.0041  -0.0370 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2744 0.3145 0.2558 -0.0332 0.0042  -0.0316 15  ALA A CA  
99   C C   . ALA A 14  ? 0.3114 0.3348 0.2869 -0.0353 0.0072  -0.0313 15  ALA A C   
100  O O   . ALA A 14  ? 0.2857 0.3001 0.2569 -0.0326 0.0061  -0.0278 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2812 0.3318 0.2695 -0.0306 0.0038  -0.0317 15  ALA A CB  
102  N N   A SER A 15  ? 0.3029 0.3213 0.2766 -0.0409 0.0111  -0.0354 16  SER A N   
103  N N   B SER A 15  ? 0.2961 0.3145 0.2698 -0.0409 0.0111  -0.0354 16  SER A N   
104  N N   C SER A 15  ? 0.2933 0.3116 0.2670 -0.0409 0.0111  -0.0354 16  SER A N   
105  C CA  A SER A 15  ? 0.3177 0.3161 0.2805 -0.0435 0.0137  -0.0346 16  SER A CA  
106  C CA  B SER A 15  ? 0.3097 0.3080 0.2724 -0.0436 0.0138  -0.0347 16  SER A CA  
107  C CA  C SER A 15  ? 0.3053 0.3035 0.2680 -0.0434 0.0137  -0.0345 16  SER A CA  
108  C C   A SER A 15  ? 0.3715 0.3571 0.3274 -0.0401 0.0096  -0.0330 16  SER A C   
109  C C   B SER A 15  ? 0.3702 0.3558 0.3261 -0.0401 0.0096  -0.0331 16  SER A C   
110  C C   C SER A 15  ? 0.3686 0.3540 0.3243 -0.0401 0.0096  -0.0330 16  SER A C   
111  O O   A SER A 15  ? 0.3503 0.3226 0.2982 -0.0374 0.0074  -0.0299 16  SER A O   
112  O O   B SER A 15  ? 0.3563 0.3284 0.3041 -0.0375 0.0075  -0.0300 16  SER A O   
113  O O   C SER A 15  ? 0.3554 0.3271 0.3029 -0.0375 0.0075  -0.0300 16  SER A O   
114  C CB  A SER A 15  ? 0.3754 0.3686 0.3348 -0.0518 0.0201  -0.0398 16  SER A CB  
115  C CB  B SER A 15  ? 0.3592 0.3526 0.3187 -0.0520 0.0201  -0.0401 16  SER A CB  
116  C CB  C SER A 15  ? 0.3515 0.3444 0.3107 -0.0518 0.0202  -0.0397 16  SER A CB  
117  O OG  A SER A 15  ? 0.4492 0.4181 0.3926 -0.0549 0.0228  -0.0380 16  SER A OG  
118  O OG  B SER A 15  ? 0.3969 0.4051 0.3661 -0.0551 0.0242  -0.0438 16  SER A OG  
119  O OG  C SER A 15  ? 0.3800 0.3748 0.3402 -0.0550 0.0206  -0.0441 16  SER A OG  
120  N N   . ASP A 16  ? 0.3369 0.3283 0.2969 -0.0398 0.0080  -0.0362 17  ASP A N   
121  C CA  . ASP A 16  ? 0.3495 0.3325 0.3072 -0.0356 0.0040  -0.0371 17  ASP A CA  
122  C C   . ASP A 16  ? 0.3470 0.3363 0.3091 -0.0302 0.0001  -0.0347 17  ASP A C   
123  O O   . ASP A 16  ? 0.3393 0.3195 0.2987 -0.0259 -0.0037 -0.0346 17  ASP A O   
124  C CB  . ASP A 16  ? 0.3693 0.3600 0.3323 -0.0375 0.0048  -0.0425 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.5100 0.4900 0.4672 -0.0434 0.0091  -0.0465 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.4935 0.4574 0.4405 -0.0464 0.0118  -0.0448 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.5296 0.5160 0.4908 -0.0462 0.0106  -0.0520 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2799 0.2838 0.2479 -0.0305 0.0010  -0.0331 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2758 0.2834 0.2460 -0.0276 -0.0006 -0.0313 18  VAL A CA  
130  C C   . VAL A 17  ? 0.3278 0.3250 0.2930 -0.0258 -0.0017 -0.0282 18  VAL A C   
131  O O   . VAL A 17  ? 0.3048 0.2993 0.2704 -0.0231 -0.0046 -0.0294 18  VAL A O   
132  C CB  . VAL A 17  ? 0.3056 0.3244 0.2776 -0.0285 0.0009  -0.0288 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.3098 0.3274 0.2806 -0.0273 0.0013  -0.0263 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.3017 0.3303 0.2754 -0.0307 0.0012  -0.0321 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.3061 0.2990 0.2674 -0.0277 0.0010  -0.0255 19  LEU A N   
136  C CA  . LEU A 18  ? 0.3211 0.3038 0.2759 -0.0273 0.0011  -0.0231 19  LEU A CA  
137  C C   . LEU A 18  ? 0.3344 0.3017 0.2797 -0.0259 -0.0029 -0.0238 19  LEU A C   
138  O O   . LEU A 18  ? 0.3183 0.2807 0.2600 -0.0233 -0.0065 -0.0233 19  LEU A O   
139  C CB  . LEU A 18  ? 0.3290 0.3113 0.2827 -0.0305 0.0060  -0.0220 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3784 0.3525 0.3262 -0.0309 0.0078  -0.0201 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.3749 0.3551 0.3277 -0.0280 0.0071  -0.0184 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.4145 0.3887 0.3625 -0.0349 0.0140  -0.0215 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.3243 0.2833 0.2648 -0.0271 -0.0028 -0.0254 20  LEU A N   
144  C CA  . LEU A 19  ? 0.3496 0.2897 0.2782 -0.0241 -0.0077 -0.0254 20  LEU A CA  
145  C C   . LEU A 19  ? 0.3729 0.3191 0.3092 -0.0168 -0.0151 -0.0282 20  LEU A C   
146  O O   . LEU A 19  ? 0.3695 0.3065 0.2988 -0.0123 -0.0214 -0.0277 20  LEU A O   
147  C CB  . LEU A 19  ? 0.3777 0.3081 0.3013 -0.0268 -0.0052 -0.0274 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4983 0.4028 0.4054 -0.0233 -0.0100 -0.0267 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.5447 0.4279 0.4309 -0.0262 -0.0093 -0.0221 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.5558 0.4503 0.4585 -0.0274 -0.0057 -0.0294 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.3181 0.2815 0.2689 -0.0162 -0.0142 -0.0321 21  ASN A N   
152  C CA  . ASN A 20  ? 0.3069 0.2799 0.2683 -0.0109 -0.0193 -0.0373 21  ASN A CA  
153  C C   . ASN A 20  ? 0.3366 0.3171 0.3012 -0.0107 -0.0204 -0.0372 21  ASN A C   
154  O O   . ASN A 20  ? 0.3312 0.3138 0.2999 -0.0057 -0.0268 -0.0414 21  ASN A O   
155  C CB  . ASN A 20  ? 0.3255 0.3133 0.2990 -0.0124 -0.0162 -0.0424 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.4672 0.4468 0.4397 -0.0102 -0.0174 -0.0458 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.4185 0.3807 0.3825 -0.0051 -0.0225 -0.0453 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3727 0.3627 0.3517 -0.0140 -0.0128 -0.0494 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.3112 0.2959 0.2747 -0.0158 -0.0146 -0.0332 22  LEU A N   
160  C CA  . LEU A 21  ? 0.3179 0.3065 0.2825 -0.0169 -0.0142 -0.0331 22  LEU A CA  
161  C C   . LEU A 21  ? 0.3469 0.3228 0.3011 -0.0143 -0.0196 -0.0319 22  LEU A C   
162  O O   . LEU A 21  ? 0.3367 0.3169 0.2937 -0.0127 -0.0236 -0.0355 22  LEU A O   
163  C CB  . LEU A 21  ? 0.3194 0.3102 0.2826 -0.0214 -0.0072 -0.0285 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.3404 0.3418 0.3096 -0.0237 -0.0031 -0.0289 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.3597 0.3598 0.3254 -0.0254 0.0015  -0.0235 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.3608 0.3716 0.3373 -0.0251 -0.0024 -0.0346 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.3316 0.2917 0.2724 -0.0149 -0.0194 -0.0275 23  ASN A N   
168  C CA  . ASN A 22  ? 0.3534 0.2973 0.2788 -0.0133 -0.0245 -0.0257 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3993 0.3389 0.3236 -0.0050 -0.0357 -0.0293 23  ASN A C   
170  O O   . ASN A 22  ? 0.4065 0.3419 0.3241 -0.0018 -0.0428 -0.0303 23  ASN A O   
171  C CB  . ASN A 22  ? 0.3800 0.3055 0.2887 -0.0178 -0.0200 -0.0210 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4857 0.3939 0.3750 -0.0189 -0.0225 -0.0185 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.4439 0.3571 0.3339 -0.0189 -0.0243 -0.0196 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4895 0.3754 0.3589 -0.0211 -0.0221 -0.0156 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.3704 0.3120 0.3020 -0.0010 -0.0378 -0.0322 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3806 0.3199 0.3150 0.0090  -0.0488 -0.0371 24  ARG A CA  
177  C C   . ARG A 23  ? 0.4135 0.3753 0.3660 0.0117  -0.0529 -0.0449 24  ARG A C   
178  O O   . ARG A 23  ? 0.4201 0.3811 0.3721 0.0194  -0.0638 -0.0487 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3847 0.3240 0.3264 0.0117  -0.0478 -0.0401 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.4207 0.3337 0.3423 0.0099  -0.0457 -0.0342 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.4554 0.3708 0.3855 0.0095  -0.0416 -0.0378 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.5753 0.4636 0.4855 0.0071  -0.0392 -0.0335 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.7801 0.6664 0.6921 0.0025  -0.0324 -0.0354 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.5809 0.4912 0.5128 0.0000  -0.0279 -0.0407 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.7228 0.5823 0.6151 -0.0010 -0.0294 -0.0324 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.3480 0.3291 0.3152 0.0050  -0.0442 -0.0477 25  LEU A N   
187  C CA  . LEU A 24  ? 0.3365 0.3382 0.3198 0.0045  -0.0452 -0.0562 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3911 0.3892 0.3658 0.0031  -0.0483 -0.0549 25  LEU A C   
189  O O   . LEU A 24  ? 0.3913 0.4002 0.3742 0.0070  -0.0560 -0.0628 25  LEU A O   
190  C CB  . LEU A 24  ? 0.3216 0.3373 0.3150 -0.0042 -0.0336 -0.0576 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.3658 0.3890 0.3685 -0.0047 -0.0296 -0.0609 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.3543 0.3883 0.3616 -0.0138 -0.0189 -0.0616 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.3690 0.4037 0.3875 0.0027  -0.0366 -0.0723 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.3559 0.3402 0.3150 -0.0026 -0.0425 -0.0462 26  ARG A N   
195  C CA  . ARG A 25  ? 0.3651 0.3439 0.3138 -0.0049 -0.0444 -0.0452 26  ARG A CA  
196  C C   . ARG A 25  ? 0.4410 0.4088 0.3777 0.0034  -0.0582 -0.0461 26  ARG A C   
197  O O   . ARG A 25  ? 0.4499 0.4257 0.3889 0.0049  -0.0649 -0.0518 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3816 0.3465 0.3160 -0.0116 -0.0355 -0.0369 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.4310 0.3911 0.3553 -0.0149 -0.0362 -0.0372 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.5219 0.4712 0.4357 -0.0216 -0.0264 -0.0315 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.4778 0.4098 0.3765 -0.0217 -0.0254 -0.0257 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.6324 0.5474 0.5114 -0.0253 -0.0240 -0.0228 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.5442 0.4573 0.4157 -0.0280 -0.0250 -0.0249 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4874 0.3868 0.3530 -0.0275 -0.0209 -0.0187 26  ARG A NH2 
205  N N   A SER A 26  ? 0.4266 0.3750 0.3490 0.0083  -0.0625 -0.0408 27  SER A N   
206  N N   B SER A 26  ? 0.4247 0.3732 0.3474 0.0084  -0.0625 -0.0408 27  SER A N   
207  N N   C SER A 26  ? 0.4286 0.3769 0.3509 0.0083  -0.0625 -0.0408 27  SER A N   
208  C CA  A SER A 26  ? 0.4566 0.3871 0.3614 0.0172  -0.0763 -0.0396 27  SER A CA  
209  C CA  B SER A 26  ? 0.4543 0.3845 0.3594 0.0174  -0.0762 -0.0395 27  SER A CA  
210  C CA  C SER A 26  ? 0.4597 0.3902 0.3646 0.0172  -0.0763 -0.0396 27  SER A CA  
211  C C   A SER A 26  ? 0.5227 0.4698 0.4442 0.0283  -0.0899 -0.0496 27  SER A C   
212  C C   B SER A 26  ? 0.5192 0.4663 0.4407 0.0282  -0.0897 -0.0496 27  SER A C   
213  C C   C SER A 26  ? 0.5224 0.4697 0.4440 0.0282  -0.0898 -0.0497 27  SER A C   
214  O O   A SER A 26  ? 0.5463 0.4875 0.4572 0.0351  -0.1029 -0.0512 27  SER A O   
215  O O   B SER A 26  ? 0.5406 0.4817 0.4513 0.0347  -0.1024 -0.0510 27  SER A O   
216  O O   C SER A 26  ? 0.5444 0.4860 0.4555 0.0350  -0.1028 -0.0513 27  SER A O   
217  C CB  A SER A 26  ? 0.5135 0.4179 0.4001 0.0193  -0.0760 -0.0324 27  SER A CB  
218  C CB  B SER A 26  ? 0.5097 0.4173 0.4011 0.0204  -0.0761 -0.0336 27  SER A CB  
219  C CB  C SER A 26  ? 0.5227 0.4278 0.4102 0.0195  -0.0761 -0.0327 27  SER A CB  
220  O OG  A SER A 26  ? 0.5791 0.4901 0.4809 0.0253  -0.0774 -0.0363 27  SER A OG  
221  O OG  B SER A 26  ? 0.6117 0.4996 0.4827 0.0113  -0.0663 -0.0254 27  SER A OG  
222  O OG  C SER A 26  ? 0.6576 0.5398 0.5234 0.0287  -0.0897 -0.0303 27  SER A OG  
223  N N   . ARG A 27  ? 0.4568 0.4257 0.4045 0.0299  -0.0870 -0.0574 28  ARG A N   
224  C CA  . ARG A 27  ? 0.4602 0.4503 0.4299 0.0397  -0.0979 -0.0701 28  ARG A CA  
225  C C   . ARG A 27  ? 0.4728 0.4924 0.4636 0.0329  -0.0938 -0.0805 28  ARG A C   
226  O O   . ARG A 27  ? 0.4753 0.5181 0.4887 0.0386  -0.1005 -0.0937 28  ARG A O   
227  C CB  . ARG A 27  ? 0.4665 0.4617 0.4514 0.0447  -0.0963 -0.0742 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.5706 0.5346 0.5339 0.0507  -0.0998 -0.0650 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.6284 0.5965 0.6057 0.0527  -0.0949 -0.0689 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.7958 0.7855 0.7989 0.0635  -0.1037 -0.0829 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.9758 0.9843 1.0018 0.0620  -0.0967 -0.0919 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.8315 0.8614 0.8828 0.0716  -0.1042 -0.1066 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.7625 0.7701 0.7868 0.0507  -0.0822 -0.0875 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.4073 0.4252 0.3907 0.0207  -0.0823 -0.0756 29  ASP A N   
235  C CA  . ASP A 28  ? 0.4003 0.4395 0.3982 0.0115  -0.0754 -0.0838 29  ASP A CA  
236  C C   . ASP A 28  ? 0.4399 0.5023 0.4632 0.0073  -0.0668 -0.0936 29  ASP A C   
237  O O   . ASP A 28  ? 0.4518 0.5373 0.4936 0.0040  -0.0663 -0.1066 29  ASP A O   
238  C CB  . ASP A 28  ? 0.4411 0.4901 0.4406 0.0158  -0.0880 -0.0924 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.5727 0.6354 0.5784 0.0037  -0.0793 -0.0984 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.5753 0.6268 0.5710 -0.0065 -0.0657 -0.0904 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.6457 0.7304 0.6671 0.0046  -0.0859 -0.1120 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.3576 0.4140 0.3808 0.0061  -0.0594 -0.0884 30  ILE A N   
243  C CA  . ILE A 29  ? 0.3435 0.4185 0.3862 0.0013  -0.0506 -0.0969 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3791 0.4526 0.4168 -0.0121 -0.0351 -0.0923 30  ILE A C   
245  O O   . ILE A 29  ? 0.3406 0.3964 0.3620 -0.0147 -0.0300 -0.0798 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3842 0.4553 0.4304 0.0082  -0.0526 -0.0962 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.4073 0.4791 0.4598 0.0234  -0.0688 -0.1025 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.3750 0.4628 0.4370 0.0007  -0.0410 -0.1040 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.4437 0.5003 0.4909 0.0308  -0.0712 -0.0979 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.3575 0.4491 0.4091 -0.0206 -0.0277 -0.1032 31  LEU A N   
251  C CA  . LEU A 30  ? 0.3673 0.4557 0.4131 -0.0336 -0.0128 -0.1004 31  LEU A CA  
252  C C   . LEU A 30  ? 0.3948 0.4653 0.4223 -0.0376 -0.0094 -0.0897 31  LEU A C   
253  O O   . LEU A 30  ? 0.3757 0.4365 0.3938 -0.0452 0.0014  -0.0836 31  LEU A O   
254  C CB  . LEU A 30  ? 0.3765 0.4608 0.4191 -0.0366 -0.0047 -0.0957 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.4599 0.5640 0.5213 -0.0382 -0.0019 -0.1094 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.4699 0.5678 0.5231 -0.0442 0.0078  -0.1044 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.5331 0.6563 0.6091 -0.0474 0.0044  -0.1246 31  LEU A CD2 
258  N N   . THR A 31  ? 0.3546 0.4208 0.3770 -0.0325 -0.0186 -0.0887 32  THR A N   
259  C CA  . THR A 31  ? 0.3531 0.4050 0.3607 -0.0371 -0.0147 -0.0817 32  THR A CA  
260  C C   . THR A 31  ? 0.4257 0.4875 0.4403 -0.0483 -0.0055 -0.0912 32  THR A C   
261  O O   . THR A 31  ? 0.4163 0.4986 0.4477 -0.0501 -0.0076 -0.1051 32  THR A O   
262  C CB  . THR A 31  ? 0.4228 0.4676 0.4211 -0.0303 -0.0264 -0.0797 32  THR A CB  
263  O OG1 . THR A 31  ? 0.4265 0.4895 0.4384 -0.0262 -0.0366 -0.0923 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3933 0.4222 0.3796 -0.0218 -0.0325 -0.0693 32  THR A CG2 
265  N N   . ASP A 32  ? 0.3946 0.4420 0.3974 -0.0560 0.0056  -0.0848 33  ASP A N   
266  C CA  . ASP A 32  ? 0.3909 0.4415 0.3962 -0.0682 0.0170  -0.0926 33  ASP A CA  
267  C C   . ASP A 32  ? 0.4131 0.4508 0.4073 -0.0737 0.0217  -0.0907 33  ASP A C   
268  O O   . ASP A 32  ? 0.4105 0.4448 0.4028 -0.0847 0.0331  -0.0955 33  ASP A O   
269  C CB  . ASP A 32  ? 0.4154 0.4584 0.4157 -0.0742 0.0286  -0.0884 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.5453 0.5680 0.5302 -0.0689 0.0298  -0.0725 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.4866 0.4996 0.4645 -0.0628 0.0247  -0.0651 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.6919 0.7091 0.6715 -0.0714 0.0359  -0.0684 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.3487 0.3777 0.3342 -0.0671 0.0143  -0.0843 34  VAL A N   
274  C CA  . VAL A 33  ? 0.3492 0.3663 0.3243 -0.0723 0.0187  -0.0837 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3902 0.4068 0.3595 -0.0660 0.0072  -0.0829 34  VAL A C   
276  O O   . VAL A 33  ? 0.3791 0.3941 0.3457 -0.0567 -0.0021 -0.0771 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3910 0.3849 0.3526 -0.0737 0.0295  -0.0721 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.3720 0.3562 0.3265 -0.0640 0.0243  -0.0604 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.4059 0.3871 0.3590 -0.0814 0.0379  -0.0744 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3619 0.3773 0.3266 -0.0719 0.0084  -0.0888 35  VAL A N   
281  N N   B VAL A 34  ? 0.3537 0.3691 0.3183 -0.0718 0.0082  -0.0888 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3656 0.3762 0.3190 -0.0684 -0.0006 -0.0880 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.3541 0.3645 0.3073 -0.0678 -0.0011 -0.0874 35  VAL A CA  
284  C C   A VAL A 34  ? 0.4122 0.4021 0.3515 -0.0733 0.0102  -0.0817 35  VAL A C   
285  C C   B VAL A 34  ? 0.4130 0.4038 0.3520 -0.0734 0.0092  -0.0825 35  VAL A C   
286  O O   A VAL A 34  ? 0.4143 0.3998 0.3548 -0.0818 0.0218  -0.0852 35  VAL A O   
287  O O   B VAL A 34  ? 0.4219 0.4099 0.3622 -0.0824 0.0198  -0.0875 35  VAL A O   
288  C CB  A VAL A 34  ? 0.4254 0.4541 0.3853 -0.0714 -0.0090 -0.1021 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.4051 0.4339 0.3643 -0.0669 -0.0138 -0.0997 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.4377 0.4577 0.3803 -0.0688 -0.0181 -0.1005 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.4058 0.4452 0.3721 -0.0787 -0.0068 -0.1129 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.4193 0.4709 0.3970 -0.0650 -0.0201 -0.1103 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.4144 0.4329 0.3557 -0.0608 -0.0254 -0.0952 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.3659 0.3422 0.2919 -0.0684 0.0075  -0.0732 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3840 0.3428 0.2983 -0.0721 0.0170  -0.0690 36  ILE A CA  
296  C C   . ILE A 35  ? 0.4532 0.4102 0.3548 -0.0750 0.0111  -0.0741 36  ILE A C   
297  O O   . ILE A 35  ? 0.4519 0.4083 0.3444 -0.0696 -0.0001 -0.0716 36  ILE A O   
298  C CB  . ILE A 35  ? 0.4136 0.3603 0.3232 -0.0663 0.0201  -0.0581 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.4066 0.3568 0.3273 -0.0622 0.0229  -0.0530 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.4382 0.3697 0.3396 -0.0699 0.0306  -0.0566 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.4115 0.3590 0.3377 -0.0674 0.0333  -0.0550 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.4167 0.3711 0.3157 -0.0838 0.0184  -0.0812 37  VAL A N   
303  C CA  . VAL A 36  ? 0.4232 0.3762 0.3087 -0.0883 0.0136  -0.0874 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4935 0.4268 0.3641 -0.0911 0.0230  -0.0828 37  VAL A C   
305  O O   . VAL A 36  ? 0.4706 0.3946 0.3450 -0.0949 0.0365  -0.0826 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4750 0.4404 0.3674 -0.0975 0.0152  -0.1010 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4870 0.4516 0.3638 -0.1023 0.0091  -0.1078 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4704 0.4590 0.3808 -0.0952 0.0066  -0.1080 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.4693 0.3949 0.3223 -0.0893 0.0161  -0.0798 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4864 0.3947 0.3241 -0.0931 0.0250  -0.0771 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5923 0.4973 0.4092 -0.0988 0.0182  -0.0831 38  VAL A C   
312  O O   . VAL A 37  ? 0.5616 0.4631 0.3625 -0.0951 0.0060  -0.0798 38  VAL A O   
313  C CB  . VAL A 37  ? 0.5282 0.4278 0.3616 -0.0870 0.0252  -0.0672 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.5338 0.4190 0.3580 -0.0920 0.0383  -0.0670 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.5050 0.4124 0.3586 -0.0798 0.0266  -0.0617 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5994 0.5053 0.4158 -0.1078 0.0250  -0.0925 39  SER A N   
317  N N   B SER A 38  ? 0.5873 0.4912 0.4027 -0.1080 0.0264  -0.0920 39  SER A N   
318  C CA  A SER A 38  ? 0.6266 0.5321 0.4243 -0.1148 0.0188  -0.1006 39  SER A CA  
319  C CA  B SER A 38  ? 0.6107 0.5130 0.4072 -0.1157 0.0218  -0.1002 39  SER A CA  
320  C C   A SER A 38  ? 0.6379 0.5605 0.4368 -0.1095 -0.0010 -0.1042 39  SER A C   
321  C C   B SER A 38  ? 0.6381 0.5514 0.4266 -0.1103 0.0010  -0.1014 39  SER A C   
322  O O   A SER A 38  ? 0.6146 0.5553 0.4352 -0.1083 -0.0031 -0.1097 39  SER A O   
323  O O   B SER A 38  ? 0.6460 0.5483 0.4103 -0.1082 -0.0085 -0.0972 39  SER A O   
324  C CB  A SER A 38  ? 0.7217 0.6078 0.4923 -0.1181 0.0213  -0.0969 39  SER A CB  
325  C CB  B SER A 38  ? 0.6868 0.5695 0.4614 -0.1217 0.0309  -0.0988 39  SER A CB  
326  O OG  A SER A 38  ? 0.9029 0.7770 0.6772 -0.1214 0.0391  -0.0951 39  SER A OG  
327  O OG  B SER A 38  ? 0.8035 0.6799 0.5878 -0.1275 0.0489  -0.1029 39  SER A OG  
328  N N   A ARG A 39  ? 0.5944 0.5105 0.3699 -0.1059 -0.0153 -0.1013 40  ARG A N   
329  N N   B ARG A 39  ? 0.5582 0.4924 0.3681 -0.1074 -0.0057 -0.1070 40  ARG A N   
330  C CA  A ARG A 39  ? 0.5919 0.5220 0.3662 -0.0981 -0.0366 -0.1046 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.5538 0.5063 0.3680 -0.1007 -0.0251 -0.1118 40  ARG A CA  
332  C C   A ARG A 39  ? 0.6139 0.5479 0.3992 -0.0851 -0.0458 -0.0963 40  ARG A C   
333  C C   B ARG A 39  ? 0.5828 0.5339 0.3979 -0.0874 -0.0364 -0.1015 40  ARG A C   
334  O O   A ARG A 39  ? 0.6012 0.5485 0.3906 -0.0765 -0.0636 -0.0995 40  ARG A O   
335  O O   B ARG A 39  ? 0.5721 0.5421 0.4023 -0.0802 -0.0491 -0.1060 40  ARG A O   
336  C CB  A ARG A 39  ? 0.6133 0.5301 0.3525 -0.0993 -0.0491 -0.1047 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.5812 0.5354 0.3744 -0.1041 -0.0377 -0.1197 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.7020 0.6241 0.4327 -0.1107 -0.0472 -0.1172 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.7265 0.6906 0.5261 -0.1172 -0.0289 -0.1339 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.7274 0.6385 0.4221 -0.1099 -0.0639 -0.1173 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.8231 0.7987 0.6094 -0.1194 -0.0451 -0.1448 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.7925 0.7041 0.4737 -0.1230 -0.0595 -0.1285 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.9226 0.9074 0.7150 -0.1337 -0.0350 -0.1595 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.9525 0.8870 0.6426 -0.1258 -0.0693 -0.1425 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 1.1008 1.0696 0.8732 -0.1449 -0.0244 -0.1622 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.8017 0.7344 0.4772 -0.1389 -0.0638 -0.1527 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.9438 0.8874 0.6892 -0.1440 -0.0218 -0.1517 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.7603 0.7212 0.4753 -0.1162 -0.0840 -0.1480 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.9395 0.9168 0.7187 -0.1580 -0.0151 -0.1765 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.5540 0.4771 0.3447 -0.0832 -0.0344 -0.0865 41  GLU A N   
351  N N   B GLU A 40  ? 0.5393 0.4697 0.3413 -0.0848 -0.0307 -0.0895 41  GLU A N   
352  C CA  A GLU A 40  ? 0.5384 0.4633 0.3383 -0.0722 -0.0412 -0.0787 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.5308 0.4570 0.3331 -0.0738 -0.0387 -0.0798 41  GLU A CA  
354  C C   A GLU A 40  ? 0.5495 0.4922 0.3815 -0.0705 -0.0342 -0.0808 41  GLU A C   
355  C C   B GLU A 40  ? 0.5440 0.4855 0.3766 -0.0704 -0.0328 -0.0797 41  GLU A C   
356  O O   A GLU A 40  ? 0.5251 0.4690 0.3681 -0.0777 -0.0194 -0.0831 41  GLU A O   
357  O O   B GLU A 40  ? 0.5144 0.4551 0.3581 -0.0762 -0.0174 -0.0797 41  GLU A O   
358  C CB  A GLU A 40  ? 0.5662 0.4674 0.3481 -0.0713 -0.0352 -0.0671 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.5619 0.4629 0.3427 -0.0751 -0.0312 -0.0693 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.7879 0.6670 0.5329 -0.0738 -0.0415 -0.0640 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.7509 0.6325 0.4958 -0.0775 -0.0392 -0.0676 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.2589 1.1265 0.9864 -0.0635 -0.0583 -0.0572 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.2093 1.0789 0.9368 -0.0674 -0.0550 -0.0600 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.2637 1.1201 0.9899 -0.0601 -0.0544 -0.0488 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.2421 1.1154 0.9598 -0.0612 -0.0733 -0.0633 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.2728 1.1420 0.9873 -0.0585 -0.0757 -0.0606 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.2189 1.0752 0.9426 -0.0653 -0.0495 -0.0514 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4897 0.4437 0.3344 -0.0608 -0.0450 -0.0798 42  GLN A N   
369  C CA  . GLN A 41  ? 0.4641 0.4341 0.3360 -0.0587 -0.0400 -0.0816 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4996 0.4621 0.3726 -0.0505 -0.0412 -0.0715 42  GLN A C   
371  O O   . GLN A 41  ? 0.5106 0.4644 0.3700 -0.0429 -0.0533 -0.0672 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4853 0.4809 0.3752 -0.0558 -0.0515 -0.0938 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.7021 0.7097 0.5962 -0.0660 -0.0482 -0.1065 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.9409 0.9784 0.8587 -0.0653 -0.0561 -0.1212 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.8514 0.9028 0.7854 -0.0566 -0.0640 -0.1230 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.9623 1.0116 0.8841 -0.0754 -0.0532 -0.1338 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.4137 0.3776 0.3007 -0.0521 -0.0291 -0.0677 43  PHE A N   
378  C CA  . PHE A 42  ? 0.4118 0.3705 0.3014 -0.0455 -0.0293 -0.0592 43  PHE A CA  
379  C C   . PHE A 42  ? 0.4467 0.4219 0.3595 -0.0445 -0.0256 -0.0623 43  PHE A C   
380  O O   . PHE A 42  ? 0.4402 0.4180 0.3611 -0.0510 -0.0141 -0.0640 43  PHE A O   
381  C CB  . PHE A 42  ? 0.4346 0.3765 0.3146 -0.0489 -0.0174 -0.0508 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.4730 0.3973 0.3289 -0.0525 -0.0172 -0.0486 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.5041 0.4248 0.3536 -0.0605 -0.0101 -0.0531 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.5183 0.4274 0.3560 -0.0492 -0.0229 -0.0425 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.5433 0.4474 0.3689 -0.0652 -0.0089 -0.0520 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.5765 0.4668 0.3881 -0.0544 -0.0214 -0.0409 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.5489 0.4378 0.3549 -0.0625 -0.0144 -0.0458 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.4044 0.3888 0.3262 -0.0367 -0.0350 -0.0635 44  ARG A N   
389  C CA  . ARG A 43  ? 0.3757 0.3759 0.3183 -0.0364 -0.0313 -0.0673 44  ARG A CA  
390  C C   . ARG A 43  ? 0.4151 0.4058 0.3566 -0.0350 -0.0240 -0.0576 44  ARG A C   
391  O O   . ARG A 43  ? 0.4105 0.3879 0.3402 -0.0307 -0.0271 -0.0503 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3802 0.3967 0.3354 -0.0285 -0.0445 -0.0753 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.4700 0.5023 0.4312 -0.0296 -0.0528 -0.0879 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.5531 0.6113 0.5387 -0.0249 -0.0600 -0.1005 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.7256 0.7928 0.7269 -0.0313 -0.0466 -0.1026 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.8771 0.9577 0.8907 -0.0423 -0.0359 -0.1120 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.7868 0.8779 0.8036 -0.0482 -0.0372 -0.1223 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.6337 0.7168 0.6553 -0.0481 -0.0237 -0.1119 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.3629 0.3594 0.3151 -0.0392 -0.0142 -0.0579 45  ALA A N   
400  C CA  . ALA A 44  ? 0.3599 0.3495 0.3113 -0.0376 -0.0084 -0.0495 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3767 0.3757 0.3397 -0.0407 -0.0018 -0.0519 45  ALA A C   
402  O O   . ALA A 44  ? 0.3543 0.3647 0.3262 -0.0454 0.0000  -0.0606 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3776 0.3522 0.3180 -0.0404 -0.0005 -0.0425 45  ALA A CB  
404  N N   . HIS A 45  ? 0.3362 0.3308 0.2982 -0.0389 0.0020  -0.0450 46  HIS A N   
405  C CA  . HIS A 45  ? 0.3253 0.3243 0.2924 -0.0423 0.0087  -0.0453 46  HIS A CA  
406  C C   . HIS A 45  ? 0.3643 0.3502 0.3229 -0.0456 0.0174  -0.0392 46  HIS A C   
407  O O   . HIS A 45  ? 0.3491 0.3259 0.3018 -0.0419 0.0177  -0.0323 46  HIS A O   
408  C CB  . HIS A 45  ? 0.3215 0.3234 0.2912 -0.0377 0.0061  -0.0417 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.3594 0.3706 0.3368 -0.0329 -0.0026 -0.0473 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.3857 0.3896 0.3573 -0.0269 -0.0100 -0.0439 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.3638 0.3897 0.3538 -0.0331 -0.0049 -0.0568 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.3775 0.3895 0.3570 -0.0221 -0.0175 -0.0502 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.3647 0.3921 0.3575 -0.0252 -0.0151 -0.0589 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.3455 0.3297 0.3034 -0.0524 0.0249  -0.0425 47  LYS A N   
415  C CA  . LYS A 46  ? 0.3476 0.3154 0.2953 -0.0546 0.0332  -0.0368 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3757 0.3372 0.3189 -0.0483 0.0325  -0.0274 47  LYS A C   
417  O O   . LYS A 46  ? 0.3503 0.3011 0.2886 -0.0444 0.0340  -0.0219 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3788 0.3430 0.3233 -0.0639 0.0421  -0.0414 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.4099 0.3773 0.3575 -0.0715 0.0452  -0.0510 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.3941 0.3590 0.3391 -0.0829 0.0557  -0.0574 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.4712 0.4444 0.4226 -0.0916 0.0584  -0.0696 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.5002 0.4723 0.4500 -0.1050 0.0702  -0.0781 47  LYS A NZ  
423  N N   . THR A 47  ? 0.3337 0.3032 0.2797 -0.0472 0.0301  -0.0269 48  THR A N   
424  C CA  . THR A 47  ? 0.3448 0.3105 0.2864 -0.0417 0.0286  -0.0192 48  THR A CA  
425  C C   . THR A 47  ? 0.3619 0.3292 0.3070 -0.0349 0.0237  -0.0158 48  THR A C   
426  O O   . THR A 47  ? 0.3624 0.3240 0.3046 -0.0302 0.0239  -0.0104 48  THR A O   
427  C CB  . THR A 47  ? 0.4447 0.4194 0.3878 -0.0432 0.0275  -0.0206 48  THR A CB  
428  O OG1 . THR A 47  ? 0.4362 0.4247 0.3906 -0.0425 0.0224  -0.0269 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.4608 0.4299 0.3959 -0.0513 0.0350  -0.0229 48  THR A CG2 
430  N N   . VAL A 48  ? 0.3145 0.2888 0.2652 -0.0344 0.0192  -0.0194 49  VAL A N   
431  C CA  . VAL A 48  ? 0.3085 0.2822 0.2599 -0.0304 0.0164  -0.0172 49  VAL A CA  
432  C C   . VAL A 48  ? 0.3403 0.3046 0.2882 -0.0303 0.0205  -0.0159 49  VAL A C   
433  O O   . VAL A 48  ? 0.3237 0.2867 0.2729 -0.0268 0.0215  -0.0134 49  VAL A O   
434  C CB  . VAL A 48  ? 0.3330 0.3107 0.2859 -0.0302 0.0108  -0.0206 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.3448 0.3171 0.2939 -0.0288 0.0102  -0.0186 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.3304 0.3170 0.2885 -0.0291 0.0072  -0.0225 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.3301 0.2894 0.2750 -0.0343 0.0231  -0.0191 50  LEU A N   
438  C CA  . LEU A 49  ? 0.3216 0.2709 0.2627 -0.0350 0.0282  -0.0191 50  LEU A CA  
439  C C   . LEU A 49  ? 0.3572 0.2989 0.2977 -0.0309 0.0324  -0.0146 50  LEU A C   
440  O O   . LEU A 49  ? 0.3651 0.3034 0.3075 -0.0272 0.0344  -0.0137 50  LEU A O   
441  C CB  . LEU A 49  ? 0.3194 0.2651 0.2571 -0.0412 0.0308  -0.0243 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.3669 0.3199 0.3044 -0.0437 0.0247  -0.0297 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.3801 0.3324 0.3161 -0.0503 0.0274  -0.0365 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3977 0.3467 0.3295 -0.0421 0.0219  -0.0285 50  LEU A CD2 
445  N N   . MET A 50  ? 0.3262 0.2647 0.2634 -0.0312 0.0335  -0.0122 51  MET A N   
446  C CA  . MET A 50  ? 0.3557 0.2834 0.2882 -0.0259 0.0356  -0.0067 51  MET A CA  
447  C C   . MET A 50  ? 0.4031 0.3391 0.3417 -0.0179 0.0304  -0.0035 51  MET A C   
448  O O   . MET A 50  ? 0.4111 0.3418 0.3512 -0.0108 0.0306  -0.0013 51  MET A O   
449  C CB  . MET A 50  ? 0.3873 0.3079 0.3103 -0.0295 0.0377  -0.0045 51  MET A CB  
450  C CG  . MET A 50  ? 0.4286 0.3410 0.3461 -0.0388 0.0446  -0.0092 51  MET A CG  
451  S SD  . MET A 50  ? 0.4896 0.3989 0.3974 -0.0460 0.0480  -0.0091 51  MET A SD  
452  C CE  . MET A 50  ? 0.4622 0.3441 0.3514 -0.0412 0.0516  0.0001  51  MET A CE  
453  N N   . ALA A 51  ? 0.3519 0.3016 0.2954 -0.0186 0.0256  -0.0044 52  ALA A N   
454  C CA  . ALA A 51  ? 0.3397 0.2999 0.2899 -0.0129 0.0210  -0.0031 52  ALA A CA  
455  C C   . ALA A 51  ? 0.3845 0.3491 0.3433 -0.0107 0.0223  -0.0064 52  ALA A C   
456  O O   . ALA A 51  ? 0.3898 0.3628 0.3562 -0.0053 0.0199  -0.0068 52  ALA A O   
457  C CB  . ALA A 51  ? 0.3452 0.3169 0.2975 -0.0159 0.0171  -0.0045 52  ALA A CB  
458  N N   . CYS A 52  ? 0.3351 0.2950 0.2923 -0.0156 0.0262  -0.0097 53  CYS A N   
459  C CA  . CYS A 52  ? 0.3407 0.3028 0.3027 -0.0164 0.0293  -0.0138 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3867 0.3401 0.3495 -0.0149 0.0352  -0.0158 53  CYS A C   
461  O O   . CYS A 52  ? 0.3657 0.3227 0.3345 -0.0151 0.0390  -0.0204 53  CYS A O   
462  C CB  . CYS A 52  ? 0.3445 0.3057 0.3005 -0.0235 0.0290  -0.0162 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.3822 0.3517 0.3383 -0.0246 0.0228  -0.0154 53  CYS A SG  
464  N N   . SER A 53  ? 0.3421 0.2833 0.2982 -0.0152 0.0374  -0.0140 54  SER A N   
465  C CA  . SER A 53  ? 0.3380 0.2681 0.2928 -0.0154 0.0441  -0.0169 54  SER A CA  
466  C C   . SER A 53  ? 0.4088 0.3256 0.3602 -0.0097 0.0455  -0.0132 54  SER A C   
467  O O   . SER A 53  ? 0.3926 0.3022 0.3350 -0.0123 0.0447  -0.0096 54  SER A O   
468  C CB  . SER A 53  ? 0.3520 0.2767 0.2979 -0.0248 0.0467  -0.0201 54  SER A CB  
469  O OG  . SER A 53  ? 0.4085 0.3201 0.3496 -0.0274 0.0531  -0.0226 54  SER A OG  
470  N N   . GLY A 54  ? 0.3758 0.2877 0.3335 -0.0024 0.0484  -0.0149 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3873 0.2811 0.3392 0.0047  0.0497  -0.0111 55  GLY A CA  
472  C C   . GLY A 54  ? 0.4319 0.3075 0.3712 -0.0037 0.0570  -0.0121 55  GLY A C   
473  O O   . GLY A 54  ? 0.4374 0.2959 0.3648 -0.0034 0.0582  -0.0074 55  GLY A O   
474  N N   . LEU A 55  ? 0.4032 0.2824 0.3433 -0.0129 0.0619  -0.0186 56  LEU A N   
475  C CA  . LEU A 55  ? 0.4195 0.2853 0.3490 -0.0224 0.0684  -0.0215 56  LEU A CA  
476  C C   . LEU A 55  ? 0.4478 0.3156 0.3695 -0.0296 0.0658  -0.0192 56  LEU A C   
477  O O   . LEU A 55  ? 0.4350 0.2871 0.3468 -0.0333 0.0704  -0.0181 56  LEU A O   
478  C CB  . LEU A 55  ? 0.4155 0.2860 0.3458 -0.0303 0.0726  -0.0293 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4831 0.3417 0.4037 -0.0405 0.0792  -0.0343 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.5038 0.3405 0.4213 -0.0373 0.0879  -0.0354 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.4697 0.3362 0.3881 -0.0489 0.0800  -0.0412 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3808 0.2667 0.3067 -0.0319 0.0591  -0.0191 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3725 0.2631 0.2944 -0.0380 0.0568  -0.0189 57  PHE A CA  
484  C C   . PHE A 56  ? 0.4228 0.3054 0.3390 -0.0344 0.0563  -0.0126 57  PHE A C   
485  O O   . PHE A 56  ? 0.4207 0.2972 0.3292 -0.0415 0.0599  -0.0135 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3744 0.2840 0.3021 -0.0398 0.0495  -0.0209 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3881 0.3012 0.3149 -0.0455 0.0495  -0.0272 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.4319 0.3415 0.3545 -0.0536 0.0531  -0.0332 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.4002 0.3196 0.3285 -0.0437 0.0458  -0.0276 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.4412 0.3541 0.3610 -0.0584 0.0517  -0.0392 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.4311 0.3507 0.3536 -0.0491 0.0450  -0.0326 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.4079 0.3247 0.3262 -0.0558 0.0472  -0.0382 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3927 0.2745 0.3113 -0.0239 0.0524  -0.0069 58  TYR A N   
494  C CA  . TYR A 57  ? 0.4065 0.2775 0.3154 -0.0193 0.0507  0.0001  58  TYR A CA  
495  C C   . TYR A 57  ? 0.4740 0.3177 0.3676 -0.0222 0.0587  0.0017  58  TYR A C   
496  O O   . TYR A 57  ? 0.4633 0.2959 0.3433 -0.0279 0.0616  0.0042  58  TYR A O   
497  C CB  . TYR A 57  ? 0.4312 0.3069 0.3466 -0.0061 0.0439  0.0044  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4885 0.3499 0.3908 0.0006  0.0404  0.0123  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.5088 0.3737 0.4024 -0.0036 0.0376  0.0155  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.5463 0.3896 0.4434 0.0118  0.0396  0.0163  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.5557 0.4048 0.4325 0.0019  0.0342  0.0232  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5997 0.4264 0.4805 0.0191  0.0347  0.0246  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6861 0.5156 0.5555 0.0137  0.0320  0.0283  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.7693 0.5803 0.6187 0.0204  0.0271  0.0368  58  TYR A OH  
505  N N   A SER A 58  ? 0.4523 0.2838 0.3471 -0.0192 0.0635  -0.0005 59  SER A N   
506  N N   B SER A 58  ? 0.4496 0.2813 0.3445 -0.0192 0.0634  -0.0005 59  SER A N   
507  C CA  A SER A 58  ? 0.4838 0.2860 0.3635 -0.0220 0.0722  0.0002  59  SER A CA  
508  C CA  B SER A 58  ? 0.4799 0.2826 0.3601 -0.0219 0.0721  0.0001  59  SER A CA  
509  C C   A SER A 58  ? 0.5519 0.3519 0.4250 -0.0385 0.0804  -0.0061 59  SER A C   
510  C C   B SER A 58  ? 0.5469 0.3475 0.4202 -0.0384 0.0801  -0.0060 59  SER A C   
511  O O   A SER A 58  ? 0.5799 0.3590 0.4365 -0.0448 0.0869  -0.0042 59  SER A O   
512  O O   B SER A 58  ? 0.5703 0.3506 0.4270 -0.0445 0.0862  -0.0038 59  SER A O   
513  C CB  A SER A 58  ? 0.5207 0.3139 0.4066 -0.0152 0.0757  -0.0028 59  SER A CB  
514  C CB  B SER A 58  ? 0.5146 0.3095 0.4015 -0.0161 0.0759  -0.0036 59  SER A CB  
515  O OG  A SER A 58  ? 0.5635 0.3568 0.4555 0.0009  0.0686  0.0020  59  SER A OG  
516  O OG  B SER A 58  ? 0.5924 0.3569 0.4643 -0.0191 0.0851  -0.0035 59  SER A OG  
517  N N   . ILE A 59  ? 0.4898 0.3115 0.3751 -0.0458 0.0796  -0.0141 60  ILE A N   
518  C CA  . ILE A 59  ? 0.4833 0.3098 0.3670 -0.0605 0.0852  -0.0226 60  ILE A CA  
519  C C   . ILE A 59  ? 0.5228 0.3544 0.4020 -0.0670 0.0851  -0.0221 60  ILE A C   
520  O O   . ILE A 59  ? 0.5443 0.3626 0.4128 -0.0779 0.0942  -0.0256 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4923 0.3420 0.3890 -0.0642 0.0810  -0.0307 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4938 0.3365 0.3920 -0.0621 0.0844  -0.0337 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.4734 0.3343 0.3717 -0.0776 0.0835  -0.0404 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.5071 0.3706 0.4136 -0.0637 0.0782  -0.0390 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.4540 0.3039 0.3407 -0.0617 0.0762  -0.0189 61  PHE A N   
526  C CA  . PHE A 60  ? 0.4537 0.3113 0.3381 -0.0690 0.0770  -0.0207 61  PHE A CA  
527  C C   . PHE A 60  ? 0.5245 0.3610 0.3906 -0.0679 0.0802  -0.0124 61  PHE A C   
528  O O   . PHE A 60  ? 0.5316 0.3719 0.3932 -0.0761 0.0832  -0.0149 61  PHE A O   
529  C CB  . PHE A 60  ? 0.4387 0.3248 0.3386 -0.0661 0.0674  -0.0232 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.4361 0.3387 0.3486 -0.0681 0.0638  -0.0313 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.4829 0.3907 0.3980 -0.0789 0.0685  -0.0417 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.4379 0.3501 0.3579 -0.0598 0.0559  -0.0290 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.4848 0.4071 0.4090 -0.0798 0.0632  -0.0488 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.4658 0.3893 0.3922 -0.0618 0.0520  -0.0354 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.4558 0.3840 0.3837 -0.0709 0.0548  -0.0448 61  PHE A CZ  
536  N N   . THR A 61  ? 0.5083 0.3214 0.3627 -0.0583 0.0800  -0.0036 62  THR A N   
537  C CA  . THR A 61  ? 0.5363 0.3226 0.3672 -0.0572 0.0828  0.0050  62  THR A CA  
538  C C   . THR A 61  ? 0.6365 0.3912 0.4485 -0.0667 0.0957  0.0035  62  THR A C   
539  O O   . THR A 61  ? 0.6516 0.3777 0.4385 -0.0694 0.1009  0.0098  62  THR A O   
540  C CB  . THR A 61  ? 0.6144 0.3932 0.4414 -0.0399 0.0730  0.0156  62  THR A CB  
541  O OG1 . THR A 61  ? 0.5798 0.3539 0.4156 -0.0303 0.0717  0.0155  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.5662 0.3731 0.4066 -0.0339 0.0621  0.0168  62  THR A CG2 
543  N N   . ASP A 62  ? 0.5881 0.3464 0.4100 -0.0730 0.1016  -0.0053 63  ASP A N   
544  C CA  . ASP A 62  ? 0.6233 0.3534 0.4290 -0.0845 0.1153  -0.0091 63  ASP A CA  
545  C C   . ASP A 62  ? 0.6942 0.4298 0.4948 -0.1033 0.1245  -0.0175 63  ASP A C   
546  O O   . ASP A 62  ? 0.6455 0.4145 0.4662 -0.1092 0.1215  -0.0270 63  ASP A O   
547  C CB  . ASP A 62  ? 0.6387 0.3737 0.4572 -0.0862 0.1184  -0.0173 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.8214 0.5300 0.6247 -0.1006 0.1336  -0.0236 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.9004 0.5732 0.6859 -0.0957 0.1389  -0.0173 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.8344 0.5577 0.6435 -0.1168 0.1402  -0.0354 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.7335 0.4354 0.5069 -0.1128 0.1360  -0.0147 64  GLN A N   
552  C CA  . GLN A 63  ? 0.7530 0.4565 0.5185 -0.1325 0.1475  -0.0233 64  GLN A CA  
553  C C   . GLN A 63  ? 0.7850 0.5136 0.5705 -0.1482 0.1548  -0.0413 64  GLN A C   
554  O O   . GLN A 63  ? 0.8126 0.5614 0.6057 -0.1612 0.1594  -0.0517 64  GLN A O   
555  C CB  . GLN A 63  ? 0.8271 0.4825 0.5545 -0.1407 0.1603  -0.0165 64  GLN A CB  
556  C CG  . GLN A 63  ? 1.0397 0.6745 0.7448 -0.1278 0.1521  -0.0002 64  GLN A CG  
557  N N   . LEU A 64  ? 0.6864 0.4152 0.4812 -0.1472 0.1556  -0.0463 65  LEU A N   
558  C CA  . LEU A 64  ? 0.6625 0.4179 0.4768 -0.1606 0.1599  -0.0638 65  LEU A CA  
559  C C   . LEU A 64  ? 0.6776 0.4743 0.5207 -0.1507 0.1444  -0.0677 65  LEU A C   
560  O O   . LEU A 64  ? 0.6801 0.5083 0.5414 -0.1588 0.1426  -0.0807 65  LEU A O   
561  C CB  . LEU A 64  ? 0.6843 0.4176 0.4911 -0.1671 0.1698  -0.0688 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.7975 0.4943 0.5789 -0.1846 0.1890  -0.0724 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.8207 0.4975 0.5973 -0.1889 0.1973  -0.0775 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.8499 0.5670 0.6379 -0.2062 0.1991  -0.0886 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.5939 0.3897 0.4409 -0.1337 0.1337  -0.0579 66  LYS A N   
566  C CA  . LYS A 65  ? 0.5547 0.3830 0.4238 -0.1251 0.1202  -0.0607 66  LYS A CA  
567  C C   . LYS A 65  ? 0.6046 0.4577 0.4850 -0.1193 0.1099  -0.0586 66  LYS A C   
568  O O   . LYS A 65  ? 0.5731 0.4547 0.4713 -0.1171 0.1008  -0.0650 66  LYS A O   
569  C CB  . LYS A 65  ? 0.5594 0.3782 0.4283 -0.1113 0.1146  -0.0527 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.5782 0.3761 0.4394 -0.1166 0.1243  -0.0571 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.5694 0.3646 0.4349 -0.1032 0.1184  -0.0517 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.6265 0.3954 0.4825 -0.1058 0.1287  -0.0543 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.6725 0.4047 0.5100 -0.1019 0.1362  -0.0456 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.6041 0.4451 0.4727 -0.1171 0.1114  -0.0502 67  CYS A N   
575  C CA  . CYS A 66  ? 0.6062 0.4689 0.4843 -0.1127 0.1031  -0.0488 67  CYS A CA  
576  C C   . CYS A 66  ? 0.6441 0.5365 0.5397 -0.1231 0.1035  -0.0640 67  CYS A C   
577  O O   . CYS A 66  ? 0.6320 0.5481 0.5420 -0.1173 0.0941  -0.0654 67  CYS A O   
578  C CB  . CYS A 66  ? 0.6505 0.4926 0.5089 -0.1119 0.1067  -0.0389 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.7479 0.5687 0.5859 -0.1325 0.1249  -0.0455 67  CYS A SG  
580  N N   . ASN A 67  ? 0.5933 0.4844 0.4885 -0.1384 0.1146  -0.0762 68  ASN A N   
581  C CA  . ASN A 67  ? 0.5866 0.5070 0.5002 -0.1496 0.1164  -0.0936 68  ASN A CA  
582  C C   . ASN A 67  ? 0.6041 0.5491 0.5370 -0.1483 0.1082  -0.1046 68  ASN A C   
583  O O   . ASN A 67  ? 0.5785 0.5514 0.5298 -0.1555 0.1072  -0.1204 68  ASN A O   
584  C CB  . ASN A 67  ? 0.6275 0.5341 0.5294 -0.1693 0.1346  -0.1027 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.8530 0.7391 0.7349 -0.1723 0.1419  -0.0941 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.8522 0.7043 0.7084 -0.1816 0.1552  -0.0895 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.7123 0.6158 0.6029 -0.1642 0.1332  -0.0909 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.5556 0.4911 0.4845 -0.1393 0.1022  -0.0973 69  LEU A N   
589  C CA  . LEU A 68  ? 0.5323 0.4875 0.4742 -0.1382 0.0939  -0.1065 69  LEU A CA  
590  C C   . LEU A 68  ? 0.5402 0.5203 0.4970 -0.1257 0.0772  -0.1058 69  LEU A C   
591  O O   . LEU A 68  ? 0.5118 0.4863 0.4651 -0.1145 0.0714  -0.0934 69  LEU A O   
592  C CB  . LEU A 68  ? 0.5439 0.4783 0.4740 -0.1347 0.0951  -0.1000 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.6287 0.5348 0.5431 -0.1462 0.1113  -0.1014 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.6380 0.5244 0.5428 -0.1397 0.1115  -0.0944 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.6519 0.5708 0.5733 -0.1637 0.1197  -0.1199 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4875 0.4945 0.4604 -0.1272 0.0690  -0.1193 70  SER A N   
597  N N   B SER A 69  ? 0.4870 0.4939 0.4598 -0.1273 0.0691  -0.1193 70  SER A N   
598  C CA  A SER A 69  ? 0.4700 0.4976 0.4549 -0.1145 0.0521  -0.1192 70  SER A CA  
599  C CA  B SER A 69  ? 0.4695 0.4977 0.4549 -0.1149 0.0522  -0.1197 70  SER A CA  
600  C C   A SER A 69  ? 0.4860 0.5084 0.4635 -0.1068 0.0421  -0.1143 70  SER A C   
601  C C   B SER A 69  ? 0.4862 0.5090 0.4640 -0.1070 0.0421  -0.1146 70  SER A C   
602  O O   A SER A 69  ? 0.4548 0.4848 0.4348 -0.0955 0.0286  -0.1104 70  SER A O   
603  O O   B SER A 69  ? 0.4550 0.4856 0.4354 -0.0956 0.0285  -0.1109 70  SER A O   
604  C CB  A SER A 69  ? 0.5196 0.5795 0.5264 -0.1183 0.0469  -0.1371 70  SER A CB  
605  C CB  B SER A 69  ? 0.5187 0.5791 0.5257 -0.1192 0.0473  -0.1381 70  SER A CB  
606  O OG  A SER A 69  ? 0.6149 0.6854 0.6266 -0.1275 0.0481  -0.1510 70  SER A OG  
607  O OG  B SER A 69  ? 0.6045 0.6716 0.6191 -0.1261 0.0565  -0.1433 70  SER A OG  
608  N N   . VAL A 70  ? 0.4548 0.4625 0.4215 -0.1139 0.0497  -0.1152 71  VAL A N   
609  C CA  . VAL A 70  ? 0.4572 0.4575 0.4140 -0.1095 0.0435  -0.1117 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4899 0.4612 0.4312 -0.1110 0.0552  -0.1019 71  VAL A C   
611  O O   . VAL A 70  ? 0.4919 0.4505 0.4291 -0.1206 0.0686  -0.1048 71  VAL A O   
612  C CB  . VAL A 70  ? 0.5275 0.5439 0.4890 -0.1169 0.0391  -0.1271 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.5384 0.5450 0.4856 -0.1134 0.0331  -0.1234 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.5203 0.5678 0.5001 -0.1137 0.0262  -0.1387 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.4108 0.3713 0.3435 -0.1017 0.0505  -0.0914 72  ILE A N   
616  C CA  . ILE A 71  ? 0.4159 0.3525 0.3372 -0.1008 0.0596  -0.0837 72  ILE A CA  
617  C C   . ILE A 71  ? 0.4640 0.3986 0.3773 -0.1003 0.0555  -0.0854 72  ILE A C   
618  O O   . ILE A 71  ? 0.4587 0.4000 0.3700 -0.0935 0.0446  -0.0820 72  ILE A O   
619  C CB  . ILE A 71  ? 0.4470 0.3732 0.3670 -0.0909 0.0603  -0.0704 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.4652 0.3910 0.3889 -0.0923 0.0648  -0.0683 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.4746 0.3799 0.3863 -0.0876 0.0678  -0.0643 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.5196 0.4289 0.4365 -0.1026 0.0786  -0.0720 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.4310 0.3534 0.3372 -0.1081 0.0649  -0.0907 73  ASN A N   
624  C CA  . ASN A 72  ? 0.4413 0.3594 0.3374 -0.1097 0.0634  -0.0934 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4863 0.3854 0.3764 -0.1046 0.0710  -0.0854 73  ASN A C   
626  O O   . ASN A 72  ? 0.4831 0.3664 0.3732 -0.1059 0.0825  -0.0843 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4996 0.4178 0.3926 -0.1223 0.0695  -0.1064 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.7325 0.6731 0.6348 -0.1283 0.0627  -0.1175 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.6102 0.5688 0.5153 -0.1236 0.0482  -0.1195 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.6813 0.6208 0.5885 -0.1389 0.0734  -0.1259 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.4385 0.3380 0.3230 -0.0990 0.0650  -0.0807 74  LEU A N   
632  C CA  . LEU A 73  ? 0.4326 0.3181 0.3142 -0.0948 0.0727  -0.0757 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4833 0.3580 0.3555 -0.1027 0.0814  -0.0835 74  LEU A C   
634  O O   . LEU A 73  ? 0.4881 0.3676 0.3526 -0.1110 0.0786  -0.0917 74  LEU A O   
635  C CB  . LEU A 73  ? 0.4219 0.3112 0.3011 -0.0879 0.0657  -0.0689 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.4509 0.3501 0.3390 -0.0798 0.0574  -0.0613 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.4648 0.3629 0.3504 -0.0745 0.0552  -0.0554 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.4246 0.3214 0.3236 -0.0763 0.0625  -0.0576 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.4603 0.3219 0.3338 -0.0996 0.0914  -0.0820 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4824 0.3323 0.3482 -0.1063 0.1017  -0.0899 75  ASP A CA  
641  C C   . ASP A 74  ? 0.5431 0.3986 0.3937 -0.1131 0.0959  -0.0943 75  ASP A C   
642  O O   . ASP A 74  ? 0.5269 0.3883 0.3736 -0.1089 0.0879  -0.0887 75  ASP A O   
643  C CB  . ASP A 74  ? 0.5048 0.3447 0.3779 -0.0987 0.1106  -0.0872 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.6586 0.4854 0.5275 -0.1042 0.1234  -0.0962 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.6717 0.5000 0.5291 -0.1116 0.1246  -0.1020 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.6751 0.4883 0.5506 -0.1008 0.1325  -0.0975 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.5655 0.4174 0.4051 -0.1237 0.0997  -0.1042 76  PRO A N   
648  C CA  . PRO A 75  ? 0.5778 0.4328 0.3983 -0.1299 0.0926  -0.1077 76  PRO A CA  
649  C C   . PRO A 75  ? 0.6260 0.4733 0.4362 -0.1293 0.0964  -0.1051 76  PRO A C   
650  O O   . PRO A 75  ? 0.6415 0.4890 0.4329 -0.1326 0.0883  -0.1045 76  PRO A O   
651  C CB  . PRO A 75  ? 0.6221 0.4734 0.4339 -0.1420 0.0984  -0.1200 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.6802 0.5209 0.5053 -0.1422 0.1127  -0.1228 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5961 0.4395 0.4376 -0.1312 0.1101  -0.1127 76  PRO A CD  
654  N N   . GLU A 76  ? 0.5833 0.4235 0.4049 -0.1250 0.1084  -0.1041 77  GLU A N   
655  C CA  . GLU A 76  ? 0.6004 0.4358 0.4163 -0.1254 0.1145  -0.1040 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5886 0.4311 0.4053 -0.1185 0.1047  -0.0942 77  GLU A C   
657  O O   . GLU A 76  ? 0.5796 0.4183 0.3864 -0.1214 0.1079  -0.0941 77  GLU A O   
658  C CB  . GLU A 76  ? 0.6331 0.4628 0.4666 -0.1210 0.1292  -0.1077 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.9082 0.7325 0.7352 -0.1269 0.1410  -0.1151 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.3088 1.1229 1.1218 -0.1389 0.1509  -0.1267 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.3163 1.1241 1.1402 -0.1378 0.1594  -0.1323 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.2710 1.0814 1.0600 -0.1496 0.1504  -0.1301 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.5112 0.3629 0.3389 -0.1106 0.0943  -0.0869 78  ILE A N   
664  C CA  . ILE A 77  ? 0.5020 0.3597 0.3316 -0.1039 0.0855  -0.0782 78  ILE A CA  
665  C C   . ILE A 77  ? 0.5662 0.4213 0.3723 -0.1082 0.0748  -0.0764 78  ILE A C   
666  O O   . ILE A 77  ? 0.5515 0.4090 0.3482 -0.1107 0.0655  -0.0785 78  ILE A O   
667  C CB  . ILE A 77  ? 0.5178 0.3855 0.3662 -0.0944 0.0790  -0.0718 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.5232 0.3886 0.3903 -0.0889 0.0890  -0.0722 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4768 0.3508 0.3267 -0.0883 0.0701  -0.0639 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.5954 0.4587 0.4708 -0.0855 0.0986  -0.0736 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.5747 0.4243 0.3712 -0.1089 0.0760  -0.0731 79  ASN A N   
672  C CA  . ASN A 78  ? 0.5908 0.4314 0.3604 -0.1123 0.0666  -0.0697 79  ASN A CA  
673  C C   . ASN A 78  ? 0.5857 0.4334 0.3601 -0.1030 0.0515  -0.0617 79  ASN A C   
674  O O   . ASN A 78  ? 0.5474 0.4015 0.3387 -0.0967 0.0528  -0.0572 79  ASN A O   
675  C CB  . ASN A 78  ? 0.6236 0.4527 0.3805 -0.1186 0.0771  -0.0702 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.8482 0.6618 0.5728 -0.1225 0.0689  -0.0654 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.7216 0.5328 0.4452 -0.1188 0.0653  -0.0591 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.7562 0.5575 0.4520 -0.1300 0.0651  -0.0682 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.5589 0.4063 0.3190 -0.1016 0.0367  -0.0609 80  PRO A N   
680  C CA  . PRO A 79  ? 0.5459 0.4005 0.3123 -0.0919 0.0224  -0.0549 80  PRO A CA  
681  C C   . PRO A 79  ? 0.5959 0.4404 0.3538 -0.0891 0.0215  -0.0474 80  PRO A C   
682  O O   . PRO A 79  ? 0.5679 0.4212 0.3421 -0.0812 0.0168  -0.0430 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5973 0.4511 0.3460 -0.0915 0.0070  -0.0574 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.6662 0.5197 0.4091 -0.1008 0.0138  -0.0660 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.6145 0.4563 0.3531 -0.1083 0.0316  -0.0667 80  PRO A CD  
686  N N   . GLU A 80  ? 0.5690 0.3941 0.3004 -0.0969 0.0271  -0.0466 81  GLU A N   
687  C CA  . GLU A 80  ? 0.5706 0.3838 0.2920 -0.0966 0.0285  -0.0406 81  GLU A CA  
688  C C   . GLU A 80  ? 0.5756 0.4013 0.3252 -0.0953 0.0407  -0.0411 81  GLU A C   
689  O O   . GLU A 80  ? 0.5464 0.3752 0.3045 -0.0898 0.0371  -0.0364 81  GLU A O   
690  C CB  . GLU A 80  ? 0.6290 0.4160 0.3124 -0.1074 0.0334  -0.0403 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.7687 0.5394 0.4368 -0.1073 0.0325  -0.0337 81  GLU A CG  
692  C CD  . GLU A 80  ? 1.1525 0.8956 0.7845 -0.1206 0.0429  -0.0338 81  GLU A CD  
693  O OE1 . GLU A 80  ? 1.1766 0.8982 0.7843 -0.1207 0.0379  -0.0273 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 1.0570 0.7984 0.6843 -0.1316 0.0569  -0.0408 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.5358 0.3689 0.2999 -0.0996 0.0540  -0.0474 82  GLY A N   
696  C CA  . GLY A 81  ? 0.5092 0.3559 0.3014 -0.0963 0.0637  -0.0489 82  GLY A CA  
697  C C   . GLY A 81  ? 0.5048 0.3671 0.3204 -0.0852 0.0549  -0.0444 82  GLY A C   
698  O O   . GLY A 81  ? 0.4687 0.3386 0.2983 -0.0806 0.0552  -0.0416 82  GLY A O   
699  N N   . PHE A 82  ? 0.4550 0.3225 0.2740 -0.0820 0.0473  -0.0448 83  PHE A N   
700  C CA  . PHE A 82  ? 0.4252 0.3066 0.2640 -0.0734 0.0400  -0.0417 83  PHE A CA  
701  C C   . PHE A 82  ? 0.4571 0.3382 0.2914 -0.0685 0.0293  -0.0361 83  PHE A C   
702  O O   . PHE A 82  ? 0.4303 0.3209 0.2808 -0.0629 0.0284  -0.0331 83  PHE A O   
703  C CB  . PHE A 82  ? 0.4411 0.3282 0.2832 -0.0734 0.0353  -0.0453 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.4395 0.3399 0.3016 -0.0667 0.0312  -0.0432 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.4680 0.3729 0.3470 -0.0641 0.0393  -0.0425 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.4460 0.3536 0.3092 -0.0624 0.0192  -0.0419 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.4699 0.3842 0.3629 -0.0591 0.0361  -0.0400 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.4590 0.3788 0.3399 -0.0577 0.0172  -0.0409 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.4354 0.3576 0.3294 -0.0568 0.0260  -0.0395 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.4836 0.3528 0.2951 -0.0701 0.0209  -0.0349 84  CYS A N   
711  C CA  . CYS A 83  ? 0.5143 0.3790 0.3188 -0.0646 0.0103  -0.0299 84  CYS A CA  
712  C C   . CYS A 83  ? 0.5181 0.3792 0.3256 -0.0654 0.0172  -0.0266 84  CYS A C   
713  O O   . CYS A 83  ? 0.4849 0.3529 0.3040 -0.0592 0.0125  -0.0237 84  CYS A O   
714  C CB  . CYS A 83  ? 0.5809 0.4275 0.3549 -0.0659 0.0005  -0.0287 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.6598 0.4977 0.4243 -0.0564 -0.0150 -0.0229 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4835 0.3351 0.2814 -0.0739 0.0293  -0.0286 85  ILE A N   
717  C CA  . ILE A 84  ? 0.4622 0.3125 0.2639 -0.0771 0.0379  -0.0283 85  ILE A CA  
718  C C   . ILE A 84  ? 0.4469 0.3195 0.2807 -0.0707 0.0403  -0.0290 85  ILE A C   
719  O O   . ILE A 84  ? 0.4232 0.3004 0.2648 -0.0681 0.0389  -0.0270 85  ILE A O   
720  C CB  . ILE A 84  ? 0.5107 0.3503 0.2989 -0.0888 0.0520  -0.0333 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.5527 0.3641 0.3010 -0.0962 0.0492  -0.0309 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4973 0.3453 0.3007 -0.0925 0.0638  -0.0371 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.6286 0.4292 0.3604 -0.1083 0.0619  -0.0368 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.4045 0.2889 0.2547 -0.0683 0.0434  -0.0318 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3903 0.2920 0.2666 -0.0616 0.0447  -0.0316 86  LEU A CA  
726  C C   . LEU A 85  ? 0.4203 0.3298 0.3044 -0.0544 0.0343  -0.0274 86  LEU A C   
727  O O   . LEU A 85  ? 0.3935 0.3133 0.2916 -0.0501 0.0338  -0.0258 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3910 0.2976 0.2787 -0.0608 0.0516  -0.0354 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.4643 0.3684 0.3522 -0.0666 0.0638  -0.0417 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.4774 0.3828 0.3743 -0.0652 0.0698  -0.0458 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.4755 0.3912 0.3794 -0.0647 0.0682  -0.0437 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3930 0.2990 0.2685 -0.0533 0.0260  -0.0266 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3768 0.2914 0.2607 -0.0472 0.0168  -0.0247 87  LEU A CA  
734  C C   . LEU A 86  ? 0.4102 0.3214 0.2901 -0.0452 0.0127  -0.0217 87  LEU A C   
735  O O   . LEU A 86  ? 0.3851 0.3064 0.2782 -0.0412 0.0110  -0.0206 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3856 0.2994 0.2626 -0.0468 0.0087  -0.0271 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.4322 0.3584 0.3214 -0.0412 0.0003  -0.0280 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.4118 0.3501 0.3193 -0.0406 0.0063  -0.0284 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.4667 0.3949 0.3508 -0.0406 -0.0087 -0.0326 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3986 0.2931 0.2580 -0.0490 0.0121  -0.0207 88  ASP A N   
741  C CA  . ASP A 87  ? 0.4065 0.2928 0.2588 -0.0487 0.0102  -0.0182 88  ASP A CA  
742  C C   . ASP A 87  ? 0.4184 0.3156 0.2865 -0.0504 0.0187  -0.0192 88  ASP A C   
743  O O   . ASP A 87  ? 0.4175 0.3198 0.2930 -0.0472 0.0157  -0.0181 88  ASP A O   
744  C CB  . ASP A 87  ? 0.4668 0.3286 0.2899 -0.0548 0.0113  -0.0169 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.6730 0.5214 0.4768 -0.0506 -0.0013 -0.0149 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.6844 0.5448 0.5009 -0.0423 -0.0115 -0.0155 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.7080 0.5344 0.4838 -0.0558 -0.0013 -0.0134 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3879 0.2896 0.2618 -0.0550 0.0288  -0.0223 89  PHE A N   
749  C CA  . PHE A 88  ? 0.3546 0.2705 0.2465 -0.0553 0.0355  -0.0249 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3594 0.2924 0.2709 -0.0472 0.0302  -0.0231 89  PHE A C   
751  O O   . PHE A 88  ? 0.3267 0.2690 0.2478 -0.0457 0.0297  -0.0234 89  PHE A O   
752  C CB  . PHE A 88  ? 0.3594 0.2797 0.2578 -0.0591 0.0458  -0.0300 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.3512 0.2905 0.2726 -0.0561 0.0498  -0.0335 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3866 0.3309 0.3117 -0.0605 0.0540  -0.0373 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3761 0.3277 0.3144 -0.0482 0.0482  -0.0331 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.3719 0.3369 0.3196 -0.0568 0.0557  -0.0416 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3978 0.3664 0.3558 -0.0432 0.0492  -0.0359 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3713 0.3485 0.3350 -0.0472 0.0523  -0.0405 89  PHE A CZ  
759  N N   . MET A 89  ? 0.3222 0.2586 0.2380 -0.0432 0.0271  -0.0219 90  MET A N   
760  C CA  . MET A 89  ? 0.3118 0.2608 0.2418 -0.0372 0.0234  -0.0201 90  MET A CA  
761  C C   . MET A 89  ? 0.3556 0.3078 0.2864 -0.0351 0.0171  -0.0186 90  MET A C   
762  O O   . MET A 89  ? 0.3442 0.3069 0.2852 -0.0324 0.0165  -0.0181 90  MET A O   
763  C CB  . MET A 89  ? 0.3217 0.2698 0.2516 -0.0358 0.0217  -0.0197 90  MET A CB  
764  C CG  . MET A 89  ? 0.3516 0.2963 0.2826 -0.0370 0.0284  -0.0214 90  MET A CG  
765  S SD  . MET A 89  ? 0.4062 0.3492 0.3369 -0.0370 0.0273  -0.0219 90  MET A SD  
766  C CE  . MET A 89  ? 0.4130 0.3471 0.3409 -0.0399 0.0363  -0.0251 90  MET A CE  
767  N N   . TYR A 90  ? 0.3222 0.2646 0.2414 -0.0357 0.0119  -0.0183 91  TYR A N   
768  C CA  . TYR A 90  ? 0.3208 0.2643 0.2408 -0.0326 0.0054  -0.0180 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3826 0.3185 0.2961 -0.0350 0.0068  -0.0179 91  TYR A C   
770  O O   . TYR A 90  ? 0.3713 0.3070 0.2858 -0.0324 0.0023  -0.0182 91  TYR A O   
771  C CB  . TYR A 90  ? 0.3537 0.2910 0.2662 -0.0297 -0.0027 -0.0188 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.3615 0.3113 0.2853 -0.0275 -0.0047 -0.0212 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3817 0.3316 0.3045 -0.0301 -0.0017 -0.0222 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.3667 0.3276 0.3017 -0.0242 -0.0084 -0.0236 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.3664 0.3260 0.2981 -0.0301 -0.0021 -0.0254 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.3654 0.3371 0.3095 -0.0244 -0.0087 -0.0274 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.4016 0.3722 0.3438 -0.0278 -0.0052 -0.0281 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.3770 0.3571 0.3273 -0.0297 -0.0043 -0.0329 91  TYR A OH  
779  N N   . THR A 91  ? 0.3478 0.2768 0.2544 -0.0410 0.0140  -0.0187 92  THR A N   
780  C CA  . THR A 91  ? 0.3606 0.2796 0.2585 -0.0457 0.0170  -0.0196 92  THR A CA  
781  C C   . THR A 91  ? 0.3916 0.3196 0.2978 -0.0520 0.0266  -0.0238 92  THR A C   
782  O O   . THR A 91  ? 0.3973 0.3203 0.2994 -0.0569 0.0299  -0.0260 92  THR A O   
783  C CB  . THR A 91  ? 0.4333 0.3259 0.3048 -0.0499 0.0167  -0.0179 92  THR A CB  
784  O OG1 . THR A 91  ? 0.4340 0.3225 0.2988 -0.0561 0.0241  -0.0193 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.4551 0.3373 0.3162 -0.0428 0.0052  -0.0149 92  THR A CG2 
786  N N   A SER A 92  ? 0.3348 0.2752 0.2527 -0.0518 0.0312  -0.0259 93  SER A N   
787  N N   B SER A 92  ? 0.3361 0.2761 0.2536 -0.0519 0.0313  -0.0259 93  SER A N   
788  C CA  A SER A 92  ? 0.3255 0.2776 0.2547 -0.0565 0.0400  -0.0320 93  SER A CA  
789  C CA  B SER A 92  ? 0.3278 0.2797 0.2568 -0.0565 0.0400  -0.0319 93  SER A CA  
790  C C   A SER A 92  ? 0.3735 0.3098 0.2867 -0.0671 0.0493  -0.0356 93  SER A C   
791  C C   B SER A 92  ? 0.3907 0.3270 0.3038 -0.0674 0.0494  -0.0358 93  SER A C   
792  O O   A SER A 92  ? 0.3653 0.3117 0.2883 -0.0723 0.0582  -0.0427 93  SER A O   
793  O O   B SER A 92  ? 0.3906 0.3368 0.3131 -0.0733 0.0583  -0.0430 93  SER A O   
794  C CB  A SER A 92  ? 0.3302 0.2962 0.2714 -0.0573 0.0400  -0.0354 93  SER A CB  
795  C CB  B SER A 92  ? 0.3412 0.3092 0.2845 -0.0559 0.0392  -0.0350 93  SER A CB  
796  O OG  A SER A 92  ? 0.3248 0.3013 0.2751 -0.0494 0.0318  -0.0320 93  SER A OG  
797  O OG  B SER A 92  ? 0.3850 0.3423 0.3175 -0.0638 0.0430  -0.0375 93  SER A OG  
798  N N   A ARG A 93  ? 0.3654 0.2771 0.2535 -0.0701 0.0473  -0.0314 94  ARG A N   
799  N N   B ARG A 93  ? 0.3724 0.2847 0.2610 -0.0701 0.0475  -0.0316 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3921 0.2838 0.2585 -0.0813 0.0564  -0.0340 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3985 0.2894 0.2641 -0.0812 0.0560  -0.0337 94  ARG A CA  
802  C C   A ARG A 93  ? 0.4474 0.3332 0.3058 -0.0822 0.0582  -0.0338 94  ARG A C   
803  C C   B ARG A 93  ? 0.4522 0.3366 0.3091 -0.0824 0.0582  -0.0336 94  ARG A C   
804  O O   A ARG A 93  ? 0.4289 0.3100 0.2817 -0.0755 0.0492  -0.0287 94  ARG A O   
805  O O   B ARG A 93  ? 0.4395 0.3185 0.2899 -0.0760 0.0492  -0.0285 94  ARG A O   
806  C CB  A ARG A 93  ? 0.4351 0.2981 0.2730 -0.0848 0.0532  -0.0295 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.4343 0.2975 0.2727 -0.0833 0.0513  -0.0286 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4876 0.3524 0.3306 -0.0862 0.0536  -0.0309 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.5082 0.3750 0.3537 -0.0824 0.0496  -0.0292 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.6589 0.4961 0.4775 -0.0833 0.0454  -0.0245 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5816 0.4362 0.4155 -0.0958 0.0617  -0.0346 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.7936 0.5969 0.5770 -0.0918 0.0497  -0.0223 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.5837 0.4428 0.4255 -0.0959 0.0608  -0.0364 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.9730 0.7552 0.7369 -0.1040 0.0600  -0.0248 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.7610 0.5932 0.5805 -0.0993 0.0604  -0.0339 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.8196 0.6134 0.5983 -0.1092 0.0668  -0.0306 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.6442 0.4826 0.4732 -0.0998 0.0606  -0.0369 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.8023 0.5502 0.5297 -0.1121 0.0638  -0.0218 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5634 0.3605 0.3493 -0.1022 0.0598  -0.0286 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.4183 0.3050 0.2766 -0.0913 0.0706  -0.0408 95  LEU A N   
821  C CA  . LEU A 94  ? 0.4181 0.2995 0.2691 -0.0939 0.0749  -0.0426 95  LEU A CA  
822  C C   . LEU A 94  ? 0.5106 0.3645 0.3284 -0.1071 0.0828  -0.0437 95  LEU A C   
823  O O   . LEU A 94  ? 0.4961 0.3472 0.3104 -0.1184 0.0951  -0.0504 95  LEU A O   
824  C CB  . LEU A 94  ? 0.4109 0.3165 0.2902 -0.0928 0.0833  -0.0511 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.4574 0.3603 0.3344 -0.0939 0.0881  -0.0541 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.4295 0.3320 0.3074 -0.0836 0.0766  -0.0468 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.4599 0.3840 0.3638 -0.0937 0.0983  -0.0646 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.5124 0.3459 0.3047 -0.1064 0.0762  -0.0380 96  ASN A N   
829  C CA  . ASN A 95  ? 0.5572 0.3600 0.3114 -0.1185 0.0820  -0.0376 96  ASN A CA  
830  C C   . ASN A 95  ? 0.6133 0.4191 0.3672 -0.1275 0.0951  -0.0458 96  ASN A C   
831  O O   . ASN A 95  ? 0.6181 0.4158 0.3585 -0.1269 0.0914  -0.0442 96  ASN A O   
832  C CB  . ASN A 95  ? 0.6256 0.4051 0.3511 -0.1125 0.0668  -0.0282 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.8908 0.6340 0.5709 -0.1238 0.0705  -0.0261 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.7390 0.4680 0.4036 -0.1376 0.0846  -0.0302 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.8216 0.5491 0.4784 -0.1189 0.0580  -0.0205 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.5622 0.3831 0.3348 -0.1352 0.1099  -0.0560 97  LEU A N   
837  C CA  . LEU A 96  ? 0.5763 0.4046 0.3554 -0.1432 0.1240  -0.0664 97  LEU A CA  
838  C C   . LEU A 96  ? 0.6542 0.4548 0.3968 -0.1620 0.1376  -0.0706 97  LEU A C   
839  O O   . LEU A 96  ? 0.6582 0.4497 0.3911 -0.1719 0.1456  -0.0731 97  LEU A O   
840  C CB  . LEU A 96  ? 0.5633 0.4252 0.3848 -0.1399 0.1315  -0.0767 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.6284 0.5081 0.4724 -0.1396 0.1412  -0.0874 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.6306 0.5103 0.4772 -0.1282 0.1312  -0.0813 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5999 0.5127 0.4855 -0.1337 0.1452  -0.0969 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.6290 0.4135 0.3478 -0.1677 0.1403  -0.0710 98  ARG A N   
845  C CA  . ARG A 97  ? 0.6804 0.4341 0.3575 -0.1864 0.1529  -0.0741 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6999 0.4602 0.3807 -0.1945 0.1664  -0.0852 98  ARG A C   
847  O O   . ARG A 97  ? 0.6438 0.4230 0.3484 -0.1837 0.1610  -0.0864 98  ARG A O   
848  C CB  . ARG A 97  ? 0.7371 0.4543 0.3672 -0.1853 0.1388  -0.0607 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.8179 0.5255 0.4425 -0.1755 0.1241  -0.0496 98  ARG A CG  
850  C CD  . ARG A 97  ? 1.0867 0.7605 0.6684 -0.1710 0.1077  -0.0374 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.3812 1.0145 0.9106 -0.1877 0.1166  -0.0366 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.6703 1.2729 1.1689 -0.1977 0.1227  -0.0336 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.5442 1.1070 0.9913 -0.2138 0.1315  -0.0327 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.5473 1.1568 1.0642 -0.1927 0.1209  -0.0319 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.6927 0.4363 0.3492 -0.2143 0.1851  -0.0942 99  GLU A N   
856  C CA  . GLU A 98  ? 0.7000 0.4479 0.3573 -0.2242 0.2002  -0.1066 99  GLU A CA  
857  C C   . GLU A 98  ? 0.7644 0.5038 0.4071 -0.2170 0.1884  -0.1002 99  GLU A C   
858  O O   . GLU A 98  ? 0.7535 0.5120 0.4208 -0.2135 0.1933  -0.1086 99  GLU A O   
859  C CB  . GLU A 98  ? 0.7650 0.4863 0.3844 -0.2492 0.2209  -0.1149 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.9104 0.6371 0.5315 -0.2616 0.2395  -0.1302 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.3475 1.0447 0.9257 -0.2883 0.2609  -0.1385 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.3102 0.9660 0.8337 -0.2965 0.2558  -0.1267 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.3587 1.0737 0.9574 -0.3009 0.2830  -0.1574 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.7560 0.4679 0.3609 -0.2140 0.1724  -0.0863 100 GLY A N   
865  C CA  . GLY A 99  ? 0.7747 0.4787 0.3633 -0.2079 0.1595  -0.0809 100 GLY A CA  
866  C C   . GLY A 99  ? 0.7624 0.4937 0.3889 -0.1884 0.1445  -0.0772 100 GLY A C   
867  O O   . GLY A 99  ? 0.7648 0.4966 0.3869 -0.1850 0.1380  -0.0770 100 GLY A O   
868  N N   . ASN A 100 ? 0.6830 0.4366 0.3455 -0.1765 0.1396  -0.0748 101 ASN A N   
869  C CA  . ASN A 100 ? 0.6330 0.4091 0.3273 -0.1593 0.1262  -0.0709 101 ASN A CA  
870  C C   . ASN A 100 ? 0.6397 0.4467 0.3814 -0.1522 0.1340  -0.0787 101 ASN A C   
871  O O   . ASN A 100 ? 0.5967 0.4194 0.3624 -0.1394 0.1251  -0.0761 101 ASN A O   
872  C CB  . ASN A 100 ? 0.6109 0.3830 0.3008 -0.1479 0.1073  -0.0585 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.7087 0.4883 0.4143 -0.1456 0.1089  -0.0568 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5786 0.3783 0.3136 -0.1465 0.1201  -0.0646 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.6475 0.4122 0.3353 -0.1416 0.0970  -0.0474 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5983 0.4138 0.3531 -0.1602 0.1499  -0.0886 102 ILE A N   
877  C CA  . ILE A 101 ? 0.5681 0.4139 0.3685 -0.1516 0.1551  -0.0963 102 ILE A CA  
878  C C   . ILE A 101 ? 0.5720 0.4301 0.3941 -0.1435 0.1562  -0.1011 102 ILE A C   
879  O O   . ILE A 101 ? 0.5146 0.3915 0.3677 -0.1291 0.1494  -0.0993 102 ILE A O   
880  C CB  . ILE A 101 ? 0.6170 0.4731 0.4298 -0.1621 0.1723  -0.1091 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5972 0.4873 0.4590 -0.1490 0.1721  -0.1155 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.6238 0.4691 0.4195 -0.1792 0.1911  -0.1216 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.6324 0.5379 0.5107 -0.1552 0.1814  -0.1248 102 ILE A CD1 
884  N N   . MET A 102 ? 0.5657 0.4113 0.3698 -0.1526 0.1644  -0.1070 103 MET A N   
885  C CA  . MET A 102 ? 0.5686 0.4227 0.3916 -0.1458 0.1665  -0.1122 103 MET A CA  
886  C C   . MET A 102 ? 0.5884 0.4422 0.4138 -0.1332 0.1497  -0.1011 103 MET A C   
887  O O   . MET A 102 ? 0.5476 0.4147 0.4010 -0.1214 0.1477  -0.1018 103 MET A O   
888  C CB  . MET A 102 ? 0.6364 0.4769 0.4387 -0.1598 0.1801  -0.1222 103 MET A CB  
889  C CG  . MET A 102 ? 0.7272 0.5706 0.5313 -0.1733 0.2000  -0.1364 103 MET A CG  
890  S SD  . MET A 102 ? 0.7803 0.6575 0.6387 -0.1628 0.2081  -0.1481 103 MET A SD  
891  C CE  . MET A 102 ? 0.7448 0.6302 0.6285 -0.1533 0.2133  -0.1574 103 MET A CE  
892  N N   . ALA A 103 ? 0.5691 0.4076 0.3653 -0.1356 0.1375  -0.0913 104 ALA A N   
893  C CA  . ALA A 103 ? 0.5566 0.3972 0.3556 -0.1253 0.1219  -0.0827 104 ALA A CA  
894  C C   . ALA A 103 ? 0.5555 0.4116 0.3802 -0.1123 0.1133  -0.0760 104 ALA A C   
895  O O   . ALA A 103 ? 0.5203 0.3850 0.3625 -0.1027 0.1075  -0.0735 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5893 0.4128 0.3536 -0.1298 0.1102  -0.0757 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4933 0.3517 0.3184 -0.1131 0.1130  -0.0736 105 VAL A N   
898  C CA  . VAL A 104 ? 0.4519 0.3255 0.3001 -0.1018 0.1052  -0.0680 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4697 0.3613 0.3512 -0.0931 0.1107  -0.0735 105 VAL A C   
900  O O   . VAL A 104 ? 0.4369 0.3365 0.3336 -0.0821 0.1023  -0.0681 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4961 0.3670 0.3364 -0.1062 0.1053  -0.0659 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.4531 0.3429 0.3203 -0.0958 0.0998  -0.0631 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.5216 0.3723 0.3293 -0.1099 0.0954  -0.0578 105 VAL A CG2 
904  N N   A MET A 105 ? 0.4498 0.3467 0.3417 -0.0978 0.1245  -0.0845 106 MET A N   
905  N N   B MET A 105 ? 0.4595 0.3564 0.3514 -0.0978 0.1245  -0.0845 106 MET A N   
906  C CA  A MET A 105 ? 0.4439 0.3575 0.3680 -0.0878 0.1289  -0.0909 106 MET A CA  
907  C CA  B MET A 105 ? 0.4611 0.3747 0.3854 -0.0874 0.1284  -0.0905 106 MET A CA  
908  C C   A MET A 105 ? 0.4957 0.4043 0.4245 -0.0800 0.1259  -0.0888 106 MET A C   
909  C C   B MET A 105 ? 0.5010 0.4093 0.4295 -0.0799 0.1256  -0.0885 106 MET A C   
910  O O   A MET A 105 ? 0.4751 0.3917 0.4230 -0.0672 0.1200  -0.0853 106 MET A O   
911  O O   B MET A 105 ? 0.4755 0.3916 0.4230 -0.0671 0.1198  -0.0850 106 MET A O   
912  C CB  A MET A 105 ? 0.4869 0.4074 0.4213 -0.0951 0.1451  -0.1055 106 MET A CB  
913  C CB  B MET A 105 ? 0.5063 0.4278 0.4423 -0.0940 0.1443  -0.1051 106 MET A CB  
914  C CG  A MET A 105 ? 0.5240 0.4643 0.4946 -0.0823 0.1476  -0.1131 106 MET A CG  
915  C CG  B MET A 105 ? 0.5458 0.4866 0.5180 -0.0805 0.1461  -0.1120 106 MET A CG  
916  S SD  A MET A 105 ? 0.5922 0.5442 0.5797 -0.0903 0.1673  -0.1335 106 MET A SD  
917  S SD  B MET A 105 ? 0.6136 0.5716 0.6070 -0.0872 0.1639  -0.1318 106 MET A SD  
918  C CE  A MET A 105 ? 0.5425 0.5088 0.5667 -0.0697 0.1647  -0.1386 106 MET A CE  
919  C CE  B MET A 105 ? 0.6006 0.5412 0.5786 -0.0976 0.1783  -0.1412 106 MET A CE  
920  N N   . ALA A 106 ? 0.4737 0.3674 0.3826 -0.0885 0.1300  -0.0910 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4829 0.3693 0.3930 -0.0843 0.1291  -0.0906 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4866 0.3728 0.3959 -0.0767 0.1152  -0.0793 107 ALA A C   
923  O O   . ALA A 106 ? 0.4609 0.3471 0.3832 -0.0677 0.1135  -0.0774 107 ALA A O   
924  C CB  . ALA A 106 ? 0.5151 0.3869 0.4009 -0.0971 0.1351  -0.0957 107 ALA A CB  
925  N N   . THR A 107 ? 0.4422 0.3271 0.3360 -0.0801 0.1057  -0.0723 108 THR A N   
926  C CA  . THR A 107 ? 0.4378 0.3250 0.3323 -0.0739 0.0933  -0.0634 108 THR A CA  
927  C C   . THR A 107 ? 0.4570 0.3562 0.3733 -0.0624 0.0897  -0.0591 108 THR A C   
928  O O   . THR A 107 ? 0.4228 0.3221 0.3460 -0.0558 0.0852  -0.0549 108 THR A O   
929  C CB  . THR A 107 ? 0.4904 0.3734 0.3644 -0.0789 0.0837  -0.0584 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4905 0.3615 0.3417 -0.0891 0.0866  -0.0627 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4839 0.3708 0.3598 -0.0737 0.0720  -0.0524 108 THR A CG2 
932  N N   . ALA A 108 ? 0.4076 0.3163 0.3335 -0.0611 0.0920  -0.0609 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3830 0.3048 0.3290 -0.0503 0.0876  -0.0579 109 ALA A CA  
934  C C   . ALA A 108 ? 0.4210 0.3435 0.3837 -0.0406 0.0910  -0.0605 109 ALA A C   
935  O O   . ALA A 108 ? 0.3978 0.3227 0.3685 -0.0308 0.0843  -0.0547 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3874 0.3207 0.3408 -0.0527 0.0905  -0.0619 109 ALA A CB  
937  N N   . MET A 109 ? 0.3945 0.3121 0.3596 -0.0433 0.1014  -0.0692 110 MET A N   
938  C CA  . MET A 109 ? 0.3998 0.3141 0.3793 -0.0328 0.1043  -0.0718 110 MET A CA  
939  C C   . MET A 109 ? 0.4417 0.3406 0.4109 -0.0305 0.1002  -0.0646 110 MET A C   
940  O O   . MET A 109 ? 0.4414 0.3367 0.4177 -0.0196 0.0960  -0.0598 110 MET A O   
941  C CB  . MET A 109 ? 0.4411 0.3530 0.4257 -0.0369 0.1174  -0.0841 110 MET A CB  
942  C CG  . MET A 109 ? 0.4975 0.4273 0.4992 -0.0372 0.1232  -0.0937 110 MET A CG  
943  S SD  . MET A 109 ? 0.6012 0.5280 0.6042 -0.0471 0.1409  -0.1099 110 MET A SD  
944  C CE  . MET A 109 ? 0.5707 0.4896 0.5911 -0.0316 0.1428  -0.1132 110 MET A CE  
945  N N   . TYR A 110 ? 0.4174 0.3070 0.3684 -0.0414 0.1012  -0.0643 111 TYR A N   
946  C CA  . TYR A 110 ? 0.4138 0.2911 0.3548 -0.0429 0.0989  -0.0601 111 TYR A CA  
947  C C   . TYR A 110 ? 0.4464 0.3284 0.3881 -0.0376 0.0885  -0.0505 111 TYR A C   
948  O O   . TYR A 110 ? 0.4350 0.3078 0.3766 -0.0326 0.0875  -0.0464 111 TYR A O   
949  C CB  . TYR A 110 ? 0.4343 0.3073 0.3576 -0.0560 0.1000  -0.0634 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.4497 0.3159 0.3638 -0.0600 0.0965  -0.0610 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4958 0.3481 0.4085 -0.0613 0.1037  -0.0646 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.4481 0.3217 0.3554 -0.0631 0.0868  -0.0568 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.4828 0.3300 0.3876 -0.0672 0.1022  -0.0644 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.4536 0.3248 0.3554 -0.0679 0.0844  -0.0574 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4884 0.3469 0.3890 -0.0707 0.0926  -0.0614 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4647 0.3223 0.3603 -0.0776 0.0916  -0.0640 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3993 0.2937 0.3403 -0.0390 0.0817  -0.0473 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3724 0.2727 0.3143 -0.0349 0.0725  -0.0396 112 LEU A CA  
959  C C   . LEU A 111 ? 0.4099 0.3155 0.3647 -0.0233 0.0694  -0.0358 112 LEU A C   
960  O O   . LEU A 111 ? 0.4035 0.3116 0.3577 -0.0197 0.0627  -0.0294 112 LEU A O   
961  C CB  . LEU A 111 ? 0.3574 0.2667 0.2931 -0.0402 0.0662  -0.0381 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3998 0.3046 0.3205 -0.0495 0.0645  -0.0403 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.4062 0.3170 0.3204 -0.0514 0.0569  -0.0377 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.4360 0.3371 0.3537 -0.0511 0.0624  -0.0396 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3795 0.2882 0.3464 -0.0174 0.0739  -0.0406 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3814 0.2976 0.3625 -0.0047 0.0695  -0.0387 113 GLN A CA  
967  C C   . GLN A 112 ? 0.4192 0.3528 0.4051 -0.0044 0.0622  -0.0361 113 GLN A C   
968  O O   . GLN A 112 ? 0.4039 0.3396 0.3889 0.0010  0.0546  -0.0294 113 GLN A O   
969  C CB  . GLN A 112 ? 0.4039 0.3046 0.3801 0.0038  0.0666  -0.0320 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.4483 0.3293 0.4200 0.0038  0.0749  -0.0354 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.6014 0.4615 0.5606 0.0077  0.0734  -0.0279 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.5210 0.3804 0.4783 0.0155  0.0658  -0.0207 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.5680 0.4094 0.5161 0.0009  0.0810  -0.0299 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3752 0.3188 0.3632 -0.0119 0.0656  -0.0417 114 MET A N   
975  C CA  . MET A 113 ? 0.3628 0.3211 0.3546 -0.0141 0.0613  -0.0413 114 MET A CA  
976  C C   . MET A 113 ? 0.4318 0.4050 0.4415 -0.0119 0.0662  -0.0507 114 MET A C   
977  O O   . MET A 113 ? 0.3969 0.3721 0.4053 -0.0213 0.0743  -0.0580 114 MET A O   
978  C CB  . MET A 113 ? 0.3848 0.3375 0.3602 -0.0258 0.0618  -0.0402 114 MET A CB  
979  C CG  . MET A 113 ? 0.4058 0.3485 0.3681 -0.0272 0.0563  -0.0334 114 MET A CG  
980  S SD  . MET A 113 ? 0.4538 0.3899 0.3977 -0.0379 0.0544  -0.0331 114 MET A SD  
981  C CE  . MET A 113 ? 0.4136 0.3606 0.3607 -0.0372 0.0485  -0.0306 114 MET A CE  
982  N N   . GLU A 114 ? 0.4192 0.4022 0.4453 0.0007  0.0616  -0.0514 115 GLU A N   
983  C CA  . GLU A 114 ? 0.4295 0.4305 0.4786 0.0063  0.0648  -0.0622 115 GLU A CA  
984  C C   . GLU A 114 ? 0.4289 0.4477 0.4857 -0.0032 0.0693  -0.0706 115 GLU A C   
985  O O   . GLU A 114 ? 0.4140 0.4415 0.4826 -0.0073 0.0789  -0.0824 115 GLU A O   
986  C CB  . GLU A 114 ? 0.4627 0.4722 0.5259 0.0233  0.0547  -0.0599 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.6510 0.6395 0.7067 0.0334  0.0525  -0.0535 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3878 0.4112 0.4377 -0.0077 0.0637  -0.0656 116 HIS A N   
989  C CA  . HIS A 115 ? 0.4011 0.4383 0.4563 -0.0179 0.0690  -0.0738 116 HIS A CA  
990  C C   . HIS A 115 ? 0.4224 0.4457 0.4608 -0.0334 0.0806  -0.0774 116 HIS A C   
991  O O   . HIS A 115 ? 0.4315 0.4641 0.4772 -0.0421 0.0906  -0.0887 116 HIS A O   
992  C CB  . HIS A 115 ? 0.4235 0.4668 0.4748 -0.0186 0.0607  -0.0681 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.4760 0.5349 0.5428 -0.0048 0.0498  -0.0664 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.5073 0.5895 0.5994 0.0025  0.0492  -0.0771 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.5031 0.5574 0.5619 0.0022  0.0391  -0.0560 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.5028 0.5923 0.5997 0.0148  0.0368  -0.0717 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.5045 0.5767 0.5805 0.0142  0.0311  -0.0589 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.3629 0.3642 0.3784 -0.0372 0.0794  -0.0688 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3694 0.3544 0.3643 -0.0507 0.0882  -0.0709 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.4375 0.4239 0.4408 -0.0531 0.0998  -0.0816 117 VAL A C   
1001 O O   . VAL A 116 ? 0.4112 0.3964 0.4091 -0.0653 0.1110  -0.0902 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.4126 0.3772 0.3834 -0.0526 0.0821  -0.0605 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.4267 0.3739 0.3746 -0.0652 0.0898  -0.0630 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.4039 0.3680 0.3678 -0.0511 0.0721  -0.0522 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3933 0.3807 0.4087 -0.0421 0.0981  -0.0817 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3957 0.3849 0.4224 -0.0420 0.1090  -0.0929 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.4602 0.4723 0.5100 -0.0443 0.1171  -0.1073 118 VAL A C   
1008 O O   . VAL A 117 ? 0.4440 0.4554 0.4921 -0.0556 0.1306  -0.1183 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.4353 0.4204 0.4725 -0.0272 0.1045  -0.0901 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.4360 0.4234 0.4875 -0.0259 0.1160  -0.1031 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.4364 0.3999 0.4510 -0.0284 0.0994  -0.0787 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.4284 0.4608 0.4983 -0.0351 0.1091  -0.1079 119 ASP A N   
1013 N N   B ASP A 118 ? 0.4240 0.4568 0.4951 -0.0342 0.1091  -0.1082 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.4280 0.4873 0.5238 -0.0364 0.1148  -0.1228 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.4239 0.4840 0.5217 -0.0349 0.1145  -0.1231 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.4688 0.5265 0.5517 -0.0570 0.1273  -0.1300 119 ASP A C   
1017 C C   B ASP A 118 ? 0.4748 0.5347 0.5613 -0.0553 0.1273  -0.1311 119 ASP A C   
1018 O O   A ASP A 118 ? 0.4741 0.5432 0.5697 -0.0650 0.1410  -0.1457 119 ASP A O   
1019 O O   B ASP A 118 ? 0.4823 0.5548 0.5831 -0.0627 0.1407  -0.1472 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.4436 0.5231 0.5578 -0.0234 0.1012  -0.1200 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.4378 0.5177 0.5532 -0.0223 0.1008  -0.1201 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.6048 0.7167 0.7491 -0.0238 0.1052  -0.1368 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.5890 0.6758 0.7230 -0.0010 0.0900  -0.1180 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.6403 0.7678 0.8097 -0.0171 0.1103  -0.1501 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.6230 0.7086 0.7684 0.0054  0.0953  -0.1252 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.6725 0.7951 0.8168 -0.0307 0.1035  -0.1377 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.6628 0.7547 0.7984 0.0095  0.0763  -0.1096 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.4131 0.4549 0.4697 -0.0657 0.1235  -0.1192 120 THR A N   
1029 N N   B THR A 119 ? 0.4237 0.4676 0.4838 -0.0645 0.1239  -0.1205 120 THR A N   
1030 C CA  A THR A 119 ? 0.4255 0.4595 0.4646 -0.0853 0.1352  -0.1247 120 THR A CA  
1031 C CA  B THR A 119 ? 0.4349 0.4713 0.4775 -0.0838 0.1351  -0.1256 120 THR A CA  
1032 C C   A THR A 119 ? 0.4802 0.4931 0.4970 -0.0981 0.1480  -0.1281 120 THR A C   
1033 C C   B THR A 119 ? 0.4881 0.5030 0.5076 -0.0971 0.1481  -0.1289 120 THR A C   
1034 O O   A THR A 119 ? 0.4818 0.4936 0.4924 -0.1140 0.1627  -0.1392 120 THR A O   
1035 O O   B THR A 119 ? 0.4928 0.5085 0.5086 -0.1126 0.1630  -0.1408 120 THR A O   
1036 C CB  A THR A 119 ? 0.4556 0.4765 0.4728 -0.0900 0.1276  -0.1132 120 THR A CB  
1037 C CB  B THR A 119 ? 0.5048 0.5292 0.5271 -0.0869 0.1262  -0.1133 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.4631 0.4793 0.4685 -0.1081 0.1403  -0.1214 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4643 0.5074 0.5068 -0.0727 0.1131  -0.1093 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.4126 0.4050 0.3990 -0.0892 0.1198  -0.0978 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.5085 0.5292 0.5189 -0.1047 0.1371  -0.1203 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.4455 0.4415 0.4490 -0.0923 0.1432  -0.1195 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.4692 0.4451 0.4502 -0.1039 0.1541  -0.1228 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.5381 0.5302 0.5423 -0.1068 0.1691  -0.1409 121 CYS A C   
1045 O O   . CYS A 120 ? 0.5329 0.5171 0.5228 -0.1238 0.1844  -0.1505 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.4705 0.4295 0.4373 -0.0965 0.1451  -0.1116 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.5197 0.4575 0.4547 -0.0971 0.1305  -0.0937 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4942 0.5082 0.5333 -0.0902 0.1648  -0.1461 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4982 0.5119 0.5371 -0.0903 0.1649  -0.1461 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.5004 0.5344 0.5694 -0.0883 0.1767  -0.1646 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.5067 0.5397 0.5745 -0.0890 0.1773  -0.1648 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.5456 0.5987 0.6270 -0.1020 0.1900  -0.1809 122 ARG A C   
1053 C C   B ARG A 121 ? 0.5476 0.6006 0.6289 -0.1023 0.1902  -0.1811 122 ARG A C   
1054 O O   A ARG A 121 ? 0.5493 0.6063 0.6352 -0.1137 0.2073  -0.1970 122 ARG A O   
1055 O O   B ARG A 121 ? 0.5502 0.6075 0.6364 -0.1139 0.2075  -0.1973 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4992 0.5526 0.6025 -0.0648 0.1652  -0.1650 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.5157 0.5667 0.6170 -0.0658 0.1665  -0.1654 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.6672 0.7015 0.7618 -0.0526 0.1571  -0.1538 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.7069 0.7388 0.8005 -0.0563 0.1631  -0.1585 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.8149 0.8639 0.9416 -0.0310 0.1502  -0.1580 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.8385 0.8860 0.9663 -0.0359 0.1590  -0.1654 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.8958 0.9229 1.0099 -0.0196 0.1408  -0.1443 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.9011 0.9571 1.0399 -0.0185 0.1411  -0.1547 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 1.0325 1.0417 1.1388 -0.0202 0.1478  -0.1462 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 1.0358 1.0756 1.1670 -0.0048 0.1294  -0.1412 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.9060 0.9171 1.0159 -0.0309 0.1640  -0.1611 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.8541 0.8700 0.9692 -0.0061 0.1337  -0.1374 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.8109 0.8000 0.9052 -0.0113 0.1398  -0.1341 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.8355 0.8823 0.9738 0.0093  0.1140  -0.1321 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4901 0.5545 0.5761 -0.1021 0.1830  -0.1777 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.5032 0.5866 0.6012 -0.1162 0.1951  -0.1931 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.5672 0.6244 0.6273 -0.1416 0.2110  -0.1947 123 LYS A C   
1073 O O   . LYS A 122 ? 0.5634 0.6304 0.6308 -0.1569 0.2296  -0.2130 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.5190 0.6193 0.6298 -0.1094 0.1826  -0.1885 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.7470 0.8786 0.8987 -0.0865 0.1697  -0.1926 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.8991 1.0483 1.0623 -0.0801 0.1569  -0.1888 123 LYS A CD  
1077 C CE  . LYS A 122 ? 1.0555 1.2298 1.2522 -0.0557 0.1415  -0.1900 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.1998 1.4071 1.4224 -0.0528 0.1354  -0.1993 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.5243 0.5474 0.5431 -0.1458 0.2038  -0.1761 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.5525 0.5443 0.5283 -0.1678 0.2158  -0.1746 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.6249 0.6062 0.5899 -0.1778 0.2308  -0.1841 124 PHE A C   
1082 O O   . PHE A 123 ? 0.6320 0.6017 0.5772 -0.1989 0.2488  -0.1943 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.5767 0.5370 0.5146 -0.1657 0.2012  -0.1529 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.6035 0.5616 0.5350 -0.1672 0.1942  -0.1459 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.6219 0.6112 0.5896 -0.1568 0.1878  -0.1502 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.6662 0.5897 0.5546 -0.1775 0.1925  -0.1345 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.6375 0.6244 0.5989 -0.1588 0.1819  -0.1445 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.6946 0.6141 0.5772 -0.1782 0.1863  -0.1284 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.6428 0.5945 0.5623 -0.1697 0.1819  -0.1339 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.5718 0.5564 0.5493 -0.1636 0.2247  -0.1819 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5964 0.5730 0.5671 -0.1717 0.2388  -0.1923 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.6677 0.6728 0.6725 -0.1785 0.2578  -0.2173 125 ILE A C   
1093 O O   . ILE A 124 ? 0.6911 0.6860 0.6786 -0.1985 0.2773  -0.2295 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.6244 0.5950 0.5987 -0.1551 0.2274  -0.1834 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.6343 0.5738 0.5675 -0.1560 0.2141  -0.1631 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.6502 0.6202 0.6293 -0.1607 0.2431  -0.1982 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.6875 0.6250 0.6275 -0.1380 0.1984  -0.1514 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.6146 0.6555 0.6666 -0.1626 0.2521  -0.2257 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.6243 0.6992 0.7166 -0.1657 0.2674  -0.2513 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.6893 0.7656 0.7699 -0.1916 0.2862  -0.2644 126 LYS A C   
1101 O O   . LYS A 125 ? 0.6933 0.7829 0.7873 -0.2051 0.3069  -0.2865 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.6345 0.7463 0.7760 -0.1417 0.2531  -0.2552 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.6422 0.7024 0.6959 -0.1995 0.2802  -0.2515 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.6690 0.7236 0.7052 -0.2252 0.2979  -0.2617 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.7713 0.7898 0.7605 -0.2501 0.3170  -0.2640 127 ALA A C   
1106 O O   . ALA A 126 ? 0.7780 0.7983 0.7623 -0.2731 0.3391  -0.2814 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.6693 0.7108 0.6859 -0.2253 0.2851  -0.2455 127 ALA A CB  
1108 N N   . SER A 127 ? 0.7751 0.7606 0.7286 -0.2465 0.3089  -0.2471 128 SER A N   
1109 C CA  . SER A 127 ? 0.8420 0.7898 0.7451 -0.2686 0.3236  -0.2467 128 SER A CA  
1110 C C   . SER A 127 ? 0.9494 0.9065 0.8648 -0.2758 0.3420  -0.2660 128 SER A C   
1111 O O   . SER A 127 ? 1.0037 0.9340 0.8800 -0.2988 0.3595  -0.2713 128 SER A O   
1112 C CB  . SER A 127 ? 0.9118 0.8209 0.7694 -0.2623 0.3055  -0.2210 128 SER A CB  
1113 O OG  . SER A 127 ? 1.0619 0.9452 0.8845 -0.2700 0.2996  -0.2075 128 SER A OG  
1114 N N   . GLU A 128 ? 0.8798 0.8728 0.8473 -0.2568 0.3387  -0.2770 129 GLU A N   
1115 C CA  . GLU A 128 ? 1.1335 1.1377 1.1186 -0.2608 0.3556  -0.2966 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.6561 1.6845 1.6635 -0.2806 0.3825  -0.3260 129 GLU A C   
1117 O O   . GLU A 128 ? 1.2429 1.2641 1.2312 -0.3009 0.3936  -0.3298 129 GLU A O   
1118 C CB  . GLU A 128 ? 1.1168 1.1451 1.1461 -0.2318 0.3413  -0.2967 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.2116 1.2864 1.3016 -0.2148 0.3370  -0.3106 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.4683 1.5608 1.5960 -0.1838 0.3190  -0.3063 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.4097 1.4776 1.5156 -0.1726 0.3043  -0.2864 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.3588 1.4895 1.5375 -0.1706 0.3193  -0.3234 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.2734 0.5119 0.3540 -0.0302 -0.0167 -0.0914 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2838 0.5222 0.3643 -0.0302 -0.0167 -0.0914 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.2612 0.4976 0.3404 -0.0292 -0.0162 -0.0933 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2778 0.5142 0.3570 -0.0292 -0.0161 -0.0933 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.3126 0.5489 0.3932 -0.0291 -0.0166 -0.0936 1   TRP D C   
1131 C C   B TRP B 2   ? 0.3092 0.5458 0.3900 -0.0292 -0.0166 -0.0935 1   TRP D C   
1132 O O   A TRP B 2   ? 0.3139 0.5500 0.3963 -0.0293 -0.0177 -0.0930 1   TRP D O   
1133 O O   B TRP B 2   ? 0.3025 0.5393 0.3851 -0.0297 -0.0176 -0.0928 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.2476 0.4809 0.3255 -0.0281 -0.0172 -0.0943 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.2693 0.5026 0.3472 -0.0280 -0.0172 -0.0944 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.2510 0.4840 0.3266 -0.0282 -0.0168 -0.0954 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2833 0.5164 0.3641 -0.0275 -0.0191 -0.0944 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2834 0.5167 0.3596 -0.0285 -0.0180 -0.0951 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.3223 0.5556 0.4063 -0.0279 -0.0206 -0.0942 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.2461 0.4783 0.3186 -0.0278 -0.0150 -0.0973 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2822 0.5157 0.3641 -0.0264 -0.0194 -0.0952 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2714 0.5044 0.3444 -0.0284 -0.0172 -0.0973 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.3144 0.5488 0.4025 -0.0272 -0.0215 -0.0952 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2849 0.5172 0.3555 -0.0280 -0.0151 -0.0988 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.3299 0.5648 0.4162 -0.0262 -0.0207 -0.0960 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.2557 0.4871 0.3275 -0.0274 -0.0131 -0.0979 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2945 0.5278 0.3748 -0.0254 -0.0186 -0.0955 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2794 0.5110 0.3468 -0.0278 -0.0131 -0.1017 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.3208 0.5579 0.4096 -0.0248 -0.0209 -0.0977 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.2688 0.4993 0.3382 -0.0272 -0.0110 -0.1000 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.3135 0.5483 0.3953 -0.0240 -0.0191 -0.0966 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2766 0.5073 0.3436 -0.0275 -0.0109 -0.1022 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.3183 0.5554 0.4041 -0.0236 -0.0200 -0.0980 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.2472 0.4837 0.3276 -0.0287 -0.0157 -0.0947 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.2465 0.4830 0.3279 -0.0285 -0.0163 -0.0957 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2824 0.5166 0.3629 -0.0266 -0.0161 -0.0963 2   VAL D C   
1157 O O   . VAL B 3   ? 0.2720 0.5050 0.3515 -0.0261 -0.0150 -0.0958 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2887 0.5295 0.3724 -0.0306 -0.0159 -0.0968 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2899 0.5341 0.3745 -0.0326 -0.0162 -0.0954 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2749 0.5184 0.3607 -0.0310 -0.0142 -0.0979 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.2574 0.4913 0.3382 -0.0256 -0.0169 -0.0973 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.2582 0.4907 0.3386 -0.0237 -0.0168 -0.0974 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.3150 0.5488 0.3987 -0.0251 -0.0162 -0.0987 3   ILE D C   
1164 O O   . ILE B 4   ? 0.3050 0.5410 0.3902 -0.0264 -0.0171 -0.1009 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.2816 0.5144 0.3613 -0.0218 -0.0179 -0.0986 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.2595 0.4937 0.3387 -0.0207 -0.0183 -0.0986 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.3020 0.5337 0.3814 -0.0195 -0.0180 -0.0980 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.3125 0.5469 0.3905 -0.0199 -0.0182 -0.0966 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.3063 0.5396 0.3918 -0.0251 -0.0147 -0.0980 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.3131 0.5494 0.4044 -0.0266 -0.0140 -0.1002 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.3698 0.6054 0.4637 -0.0257 -0.0154 -0.1015 4   PRO D C   
1172 O O   . PRO B 5   ? 0.3541 0.5860 0.4453 -0.0232 -0.0160 -0.0997 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.3366 0.5725 0.4300 -0.0264 -0.0114 -0.0994 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.3828 0.6136 0.4710 -0.0243 -0.0114 -0.0964 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.3303 0.5610 0.4139 -0.0240 -0.0133 -0.0960 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.3489 0.5890 0.4486 -0.0278 -0.0159 -0.1050 5   ALA D N   
# 
