data_7GV6
# 
_entry.id   7GV6 
# 
_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   7GV6         pdb_00007gv6 10.2210/pdb7gv6/pdb 
WWPDB D_1001406677 ?            ?                   
# 
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                        7GV6 
_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 47  HOH   HOH A . 
F 6 HOH   4   304 19  HOH   HOH A . 
F 6 HOH   5   305 94  HOH   HOH A . 
F 6 HOH   6   306 90  HOH   HOH A . 
F 6 HOH   7   307 29  HOH   HOH A . 
F 6 HOH   8   308 45  HOH   HOH A . 
F 6 HOH   9   309 140 HOH   HOH A . 
F 6 HOH   10  310 173 HOH   HOH A . 
F 6 HOH   11  311 166 HOH   HOH A . 
F 6 HOH   12  312 40  HOH   HOH A . 
F 6 HOH   13  313 179 HOH   HOH A . 
F 6 HOH   14  314 101 HOH   HOH A . 
F 6 HOH   15  315 247 HOH   HOH A . 
F 6 HOH   16  316 100 HOH   HOH A . 
F 6 HOH   17  317 142 HOH   HOH A . 
F 6 HOH   18  318 106 HOH   HOH A . 
F 6 HOH   19  319 202 HOH   HOH A . 
F 6 HOH   20  320 99  HOH   HOH A . 
F 6 HOH   21  321 139 HOH   HOH A . 
F 6 HOH   22  322 119 HOH   HOH A . 
F 6 HOH   23  323 87  HOH   HOH A . 
F 6 HOH   24  324 132 HOH   HOH A . 
F 6 HOH   25  325 83  HOH   HOH A . 
F 6 HOH   26  326 37  HOH   HOH A . 
F 6 HOH   27  327 75  HOH   HOH A . 
F 6 HOH   28  328 27  HOH   HOH A . 
F 6 HOH   29  329 193 HOH   HOH A . 
F 6 HOH   30  330 84  HOH   HOH A . 
F 6 HOH   31  331 17  HOH   HOH A . 
F 6 HOH   32  332 91  HOH   HOH A . 
F 6 HOH   33  333 237 HOH   HOH A . 
F 6 HOH   34  334 20  HOH   HOH A . 
F 6 HOH   35  335 14  HOH   HOH A . 
F 6 HOH   36  336 42  HOH   HOH A . 
F 6 HOH   37  337 6   HOH   HOH A . 
F 6 HOH   38  338 239 HOH   HOH A . 
F 6 HOH   39  339 50  HOH   HOH A . 
F 6 HOH   40  340 196 HOH   HOH A . 
F 6 HOH   41  341 34  HOH   HOH A . 
F 6 HOH   42  342 243 HOH   HOH A . 
F 6 HOH   43  343 242 HOH   HOH A . 
F 6 HOH   44  344 86  HOH   HOH A . 
F 6 HOH   45  345 244 HOH   HOH A . 
F 6 HOH   46  346 122 HOH   HOH A . 
F 6 HOH   47  347 117 HOH   HOH A . 
F 6 HOH   48  348 44  HOH   HOH A . 
F 6 HOH   49  349 5   HOH   HOH A . 
F 6 HOH   50  350 145 HOH   HOH A . 
F 6 HOH   51  351 133 HOH   HOH A . 
F 6 HOH   52  352 96  HOH   HOH A . 
F 6 HOH   53  353 151 HOH   HOH A . 
F 6 HOH   54  354 89  HOH   HOH A . 
F 6 HOH   55  355 4   HOH   HOH A . 
F 6 HOH   56  356 124 HOH   HOH A . 
F 6 HOH   57  357 51  HOH   HOH A . 
F 6 HOH   58  358 85  HOH   HOH A . 
F 6 HOH   59  359 30  HOH   HOH A . 
F 6 HOH   60  360 93  HOH   HOH A . 
F 6 HOH   61  361 175 HOH   HOH A . 
F 6 HOH   62  362 97  HOH   HOH A . 
F 6 HOH   63  363 21  HOH   HOH A . 
F 6 HOH   64  364 12  HOH   HOH A . 
F 6 HOH   65  365 15  HOH   HOH A . 
F 6 HOH   66  366 141 HOH   HOH A . 
F 6 HOH   67  367 24  HOH   HOH A . 
F 6 HOH   68  368 25  HOH   HOH A . 
F 6 HOH   69  369 144 HOH   HOH A . 
F 6 HOH   70  370 170 HOH   HOH A . 
F 6 HOH   71  371 192 HOH   HOH A . 
F 6 HOH   72  372 207 HOH   HOH A . 
F 6 HOH   73  373 23  HOH   HOH A . 
F 6 HOH   74  374 186 HOH   HOH A . 
F 6 HOH   75  375 16  HOH   HOH A . 
F 6 HOH   76  376 70  HOH   HOH A . 
F 6 HOH   77  377 55  HOH   HOH A . 
F 6 HOH   78  378 131 HOH   HOH A . 
F 6 HOH   79  379 76  HOH   HOH A . 
F 6 HOH   80  380 39  HOH   HOH A . 
F 6 HOH   81  381 167 HOH   HOH A . 
F 6 HOH   82  382 108 HOH   HOH A . 
F 6 HOH   83  383 103 HOH   HOH A . 
F 6 HOH   84  384 245 HOH   HOH A . 
F 6 HOH   85  385 105 HOH   HOH A . 
F 6 HOH   86  386 180 HOH   HOH A . 
F 6 HOH   87  387 177 HOH   HOH A . 
F 6 HOH   88  388 229 HOH   HOH A . 
F 6 HOH   89  389 165 HOH   HOH A . 
F 6 HOH   90  390 169 HOH   HOH A . 
F 6 HOH   91  391 32  HOH   HOH A . 
F 6 HOH   92  392 28  HOH   HOH A . 
F 6 HOH   93  393 194 HOH   HOH A . 
F 6 HOH   94  394 191 HOH   HOH A . 
F 6 HOH   95  395 129 HOH   HOH A . 
F 6 HOH   96  396 69  HOH   HOH A . 
F 6 HOH   97  397 212 HOH   HOH A . 
F 6 HOH   98  398 92  HOH   HOH A . 
F 6 HOH   99  399 241 HOH   HOH A . 
F 6 HOH   100 400 74  HOH   HOH A . 
F 6 HOH   101 401 157 HOH   HOH A . 
F 6 HOH   102 402 82  HOH   HOH A . 
F 6 HOH   103 403 22  HOH   HOH A . 
F 6 HOH   104 404 205 HOH   HOH A . 
F 6 HOH   105 405 176 HOH   HOH A . 
F 6 HOH   106 406 174 HOH   HOH A . 
F 6 HOH   107 407 120 HOH   HOH A . 
F 6 HOH   108 408 67  HOH   HOH A . 
F 6 HOH   109 409 26  HOH   HOH A . 
F 6 HOH   110 410 35  HOH   HOH A . 
F 6 HOH   111 411 43  HOH   HOH A . 
F 6 HOH   112 412 64  HOH   HOH A . 
F 6 HOH   113 413 190 HOH   HOH A . 
F 6 HOH   114 414 204 HOH   HOH A . 
F 6 HOH   115 415 60  HOH   HOH A . 
F 6 HOH   116 416 36  HOH   HOH A . 
F 6 HOH   117 417 88  HOH   HOH A . 
F 6 HOH   118 418 61  HOH   HOH A . 
F 6 HOH   119 419 46  HOH   HOH A . 
F 6 HOH   120 420 215 HOH   HOH A . 
F 6 HOH   121 421 236 HOH   HOH A . 
F 6 HOH   122 422 56  HOH   HOH A . 
F 6 HOH   123 423 185 HOH   HOH A . 
F 6 HOH   124 424 223 HOH   HOH A . 
F 6 HOH   125 425 110 HOH   HOH A . 
F 6 HOH   126 426 65  HOH   HOH A . 
F 6 HOH   127 427 57  HOH   HOH A . 
F 6 HOH   128 428 68  HOH   HOH A . 
F 6 HOH   129 429 135 HOH   HOH A . 
F 6 HOH   130 430 214 HOH   HOH A . 
F 6 HOH   131 431 95  HOH   HOH A . 
F 6 HOH   132 432 147 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 41  HOH   HOH A . 
F 6 HOH   136 436 168 HOH   HOH A . 
F 6 HOH   137 437 200 HOH   HOH A . 
F 6 HOH   138 438 227 HOH   HOH A . 
F 6 HOH   139 439 248 HOH   HOH A . 
F 6 HOH   140 440 121 HOH   HOH A . 
F 6 HOH   141 441 123 HOH   HOH A . 
F 6 HOH   142 442 231 HOH   HOH A . 
F 6 HOH   143 443 171 HOH   HOH A . 
F 6 HOH   144 444 228 HOH   HOH A . 
F 6 HOH   145 445 225 HOH   HOH A . 
F 6 HOH   146 446 71  HOH   HOH A . 
F 6 HOH   147 447 63  HOH   HOH A . 
F 6 HOH   148 448 220 HOH   HOH A . 
F 6 HOH   149 449 234 HOH   HOH A . 
F 6 HOH   150 450 203 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   155 455 238 HOH   HOH A . 
F 6 HOH   156 456 81  HOH   HOH A . 
F 6 HOH   157 457 79  HOH   HOH A . 
F 6 HOH   158 458 125 HOH   HOH A . 
F 6 HOH   159 459 114 HOH   HOH A . 
F 6 HOH   160 460 246 HOH   HOH A . 
F 6 HOH   161 461 58  HOH   HOH A . 
F 6 HOH   162 462 221 HOH   HOH A . 
F 6 HOH   163 463 216 HOH   HOH A . 
F 6 HOH   164 464 115 HOH   HOH A . 
F 6 HOH   165 465 183 HOH   HOH A . 
F 6 HOH   166 466 107 HOH   HOH A . 
F 6 HOH   167 467 188 HOH   HOH A . 
F 6 HOH   168 468 230 HOH   HOH A . 
F 6 HOH   169 469 201 HOH   HOH A . 
F 6 HOH   170 470 182 HOH   HOH A . 
F 6 HOH   171 471 113 HOH   HOH A . 
F 6 HOH   172 472 48  HOH   HOH A . 
F 6 HOH   173 473 148 HOH   HOH A . 
F 6 HOH   174 474 213 HOH   HOH A . 
F 6 HOH   175 475 206 HOH   HOH A . 
F 6 HOH   176 476 172 HOH   HOH A . 
F 6 HOH   177 477 211 HOH   HOH A . 
G 6 HOH   1   201 62  HOH   HOH D . 
G 6 HOH   2   202 78  HOH   HOH D . 
G 6 HOH   3   203 38  HOH   HOH D . 
G 6 HOH   4   204 53  HOH   HOH D . 
G 6 HOH   5   205 73  HOH   HOH D . 
G 6 HOH   6   206 240 HOH   HOH D . 
G 6 HOH   7   207 49  HOH   HOH D . 
G 6 HOH   8   208 195 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           7GV6 
_cell.length_a           67.790 
_cell.length_b           67.790 
_cell.length_c           166.860 
_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                         7GV6 
_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          7GV6 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.65 
_exptl_crystal.density_percent_sol   66.33 
_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                     7GV6 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             34.000 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23801 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.089 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.500 
_reflns.B_iso_Wilson_estimate        34.520 
_reflns.pdbx_redundancy              9.000 
_reflns.pdbx_Rrim_I_all              0.094 
_reflns.pdbx_Rpim_I_all              0.031 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     215122 
_reflns.pdbx_scaling_rejects         735 
_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  ? 11906 1281 ? 2.234 ? ? ? 9.300 ? 1.000  ? ? ? ? ? ? 100.000 2.364 0.764 0.411 ? 
1 2 9.090 34.000 ? 1501  236  ? 0.046 ? ? ? 6.400 ? 29.500 ? ? ? ? ? ? 98.800  0.049 0.019 0.998 ? 
# 
_refine.entry_id                                 7GV6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             34.0000 
_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                     23730 
_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                          0.1790 
_refine.ls_R_factor_R_work                       0.1770 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2020 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1500 
_refine.ls_number_reflns_R_free                  1222 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               39.9600 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.4710 
_refine.aniso_B[2][2]                            -0.4710 
_refine.aniso_B[3][3]                            0.9421 
_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               0.9640 
_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                                133.240 
_refine.B_iso_min                                20.470 
_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                        7GV6 
_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                        34.0000 
_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           34.88 
_refine_hist.pdbx_B_iso_mean_solvent          58.36 
_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      1624 ?      ? 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           ?    3.270  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.620 ? ?      ?            
# 
_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               99.6800 
_refine_ls_shell.number_reflns_R_work             2686 
_refine_ls_shell.R_factor_all                     0.3061 
_refine_ls_shell.R_factor_R_work                  0.3064 
_refine_ls_shell.R_factor_R_free                  0.2984 
_refine_ls_shell.percent_reflns_R_free            4.6500 
_refine_ls_shell.number_reflns_R_free             131 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2817 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GV6 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 18.75 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GV6 
_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 7GV6       7GV6   ? 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 7GV6 A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GV6 D 1 ? 6   ? 7GV6   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 7GV6 GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GV6 PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GV6 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)' 7390  ? 
1 MORE         -65   ? 
1 'SSA (A^2)'  13040 ? 
# 
_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 33.8950000000 0.8660254038 
-0.5000000000 0.0000000000 -58.7078621225 0.0000000000 0.0000000000 -1.0000000000 27.8100000000 
# 
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  ? THR A 61  ? SER A 54  THR A 62  1 ? 9  
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 ? ? ? ? ? ? ? 1.332 ? ? 
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                   7GV6 
_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 61.35 -119.23 
2 1 SER A 39  ? B 36.59 65.86   
3 1 ARG A 40  ? B 76.77 -23.54  
4 1 SER A 93  ? A 76.04 -3.87   
5 1 GLN A 113 ? ? 62.37 60.05   
# 
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 370 ? F HOH . 
2 1 A HOH 390 ? F HOH . 
3 1 A HOH 453 ? F HOH . 
4 1 A HOH 465 ? F HOH . 
5 1 A HOH 468 ? F HOH . 
6 1 A HOH 469 ? 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 0.0069  -0.0645 -0.0484 -0.0428 0.0298  -0.0202 1.0784 1.8515  2.0360 
0.4701 -0.3372 1.2013 0.1469 -0.0857 -0.0611 -0.0577 0.1040  0.0975 0.2524  -0.0109 -0.0053 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1377 0.1197  -0.0306 -0.0428 -0.0091 -0.0799 0.7096 -0.1661 0.0000 
0.0610 -0.0442 0.4271 0.0305 -0.0106 -0.0199 -0.0053 -0.0019 0.0389 -0.0402 -0.0035 -0.0154 
# 
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                    7GV6 
_atom_sites.fract_transf_matrix[1][1]   0.014751 
_atom_sites.fract_transf_matrix[1][2]   0.008517 
_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]   0.017033 
_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]   0.005993 
_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   ? 17.312 -21.296 -4.773 1.00 70.07  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.227 -22.157 -5.523 1.00 69.10  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.775 -23.635 -5.485 1.00 68.61  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.709 -23.947 -4.943 1.00 69.39  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.665 -22.007 -4.963 1.00 69.88  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.748 -22.018 -6.031 1.00 84.14  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.895 -23.056 -6.724 1.00 84.48  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.455 -20.993 -6.168 1.00 91.46  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.582 -24.536 -6.072 1.00 59.85  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.328 -25.975 -6.077 1.00 57.05  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.324 -26.709 -5.125 1.00 52.57  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.625 -27.885 -5.329 1.00 51.72  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.413 -26.518 -7.499 1.00 62.28  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.692 -26.281 -8.064 1.00 73.23  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.809 -26.016 -4.078 1.00 43.84  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.747 -26.581 -3.106 1.00 40.90  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.133 -27.739 -2.298 1.00 40.59  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.908 -27.816 -2.148 1.00 40.89  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.247 -25.486 -2.163 1.00 41.73  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.405 -24.301 -2.910 1.00 47.08  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.985 -28.631 -1.786 1.00 31.82  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.635 -29.636 -0.784 1.00 29.13  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.239 -29.106 0.521  1.00 30.84  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.189 -28.315 0.478  1.00 29.94  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.980 -31.113 -1.101 1.00 32.35  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.502 -31.303 -1.359 1.00 32.53  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.112 -31.633 -2.267 1.00 33.44  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.966 -32.757 -1.548 1.00 38.11  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.760 -29.559 1.678  0.66 26.28  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.619 -29.453 1.647  0.34 27.09  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.289 -29.063 2.951  0.66 25.50  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 21.017 -28.960 2.953  0.34 26.04  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.622 -30.200 3.903  0.66 28.08  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.417 -30.092 3.875  0.34 29.42  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.844 -31.144 4.014  0.66 28.42  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.724 -31.104 3.952  0.34 29.53  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.288 -28.070 3.596  0.66 27.42  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.874 -28.142 3.567  0.34 27.45  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.588 -27.747 5.076  0.66 32.60  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.340 -27.155 4.636  0.34 30.41  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.068 -26.425 5.574  0.66 53.56  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.569 -27.272 5.928  0.34 42.72  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.473 -25.637 4.840  0.66 48.00  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.349 -27.466 5.947  0.34 33.02  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.311 -26.141 6.848  0.66 49.59  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.272 -27.131 7.044  0.34 38.92  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.766 -30.101 4.597  0.66 26.32  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.532 -29.910 4.578  0.34 26.51  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.149 -31.102 5.588  0.66 24.64  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.041 -30.886 5.531  0.34 25.54  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.686 -30.610 6.947  0.66 26.71  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.554 -30.442 6.886  0.34 27.77  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.290 -29.691 7.526  0.66 24.18  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.983 -29.393 7.391  0.34 26.67  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.667 -31.409 5.536  0.66 25.52  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.574 -30.985 5.429  0.34 26.90  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 25.045 -32.626 6.348  0.66 26.57  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.039 -31.782 4.229  0.34 29.27  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.648 -33.900 5.952  0.66 29.70  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.762 -31.352 2.933  0.34 32.94  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.834 -32.505 7.490  0.66 26.99  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.783 -32.943 4.392  0.34 32.54  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 24.978 -35.024 6.723  0.66 30.46  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.193 -32.085 1.826  0.34 34.24  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.145 -33.622 8.266  0.66 28.93  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.220 -33.675 3.278  0.34 36.00  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.723 -34.874 7.878  0.66 27.76  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.921 -33.239 2.005  0.34 33.99  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.586 -31.191 7.437  1.00 24.07  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.932 -30.819 8.710  1.00 24.69  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.891 -30.590 9.902  1.00 27.74  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.783 -29.561 10.572 1.00 27.32  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.849 -31.842 9.075  1.00 33.70  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.954 -31.976 7.960  1.00 35.77  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.047 -31.423 10.322 1.00 37.09  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.822 -31.529 10.133 1.00 25.34  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.742 -31.459 11.280 1.00 25.89  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.984 -30.560 11.067 1.00 27.06  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.801 -30.457 11.992 1.00 25.97  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.210 -32.879 11.663 1.00 30.56  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.108 -33.837 12.178 1.00 41.88  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.508 -33.405 13.506 1.00 63.84  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.459 -33.489 14.620 1.00 77.00  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.327 -32.833 15.770 1.00 87.76  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.231 -32.977 16.729 1.00 76.38  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.296 -32.019 15.965 1.00 68.12  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.140 -29.926 9.884  1.00 23.19  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.367 -29.158 9.609  1.00 23.01  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.656 -28.051 10.630 1.00 25.18  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.791 -27.965 11.126 1.00 23.82  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.352 -28.579 8.172  1.00 23.28  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.608 -27.824 7.867  1.00 25.04  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.797 -28.489 7.664  1.00 25.05  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.812 -26.495 7.712  1.00 25.15  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.697 -27.555 7.400  1.00 24.75  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.159 -26.335 7.435  1.00 24.33  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.666 -27.174 10.902 1.00 21.60  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.900 -26.042 11.843 1.00 22.21  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.319 -26.540 13.251 1.00 24.42  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.243 -25.985 13.861 1.00 22.71  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.653 -25.164 11.917 1.00 23.52  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.655 -27.597 13.740 0.42 23.79  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.655 -27.601 13.741 0.30 23.08  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.653 -27.593 13.756 0.28 23.23  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.940 -28.191 15.044 0.42 23.57  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.934 -28.206 15.044 0.30 22.85  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.963 -28.160 15.070 0.28 23.10  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.356 -28.770 15.060 0.42 26.69  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.341 -28.802 15.072 0.30 26.74  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.356 -28.799 15.081 0.28 26.90  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.085 -28.576 16.039 0.42 23.95  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.053 -28.643 16.068 0.30 24.76  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.074 -28.661 16.075 0.28 25.03  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.918 -29.279 15.369 0.42 28.14  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.899 -29.282 15.363 0.30 26.58  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.895 -29.159 15.503 0.28 27.34  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.193 -29.880 16.624 0.42 33.79  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.605 -28.713 15.471 0.30 30.16  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.807 -30.247 14.599 0.28 32.63  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.746 -29.461 13.968 1.00 24.54  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.076 -30.089 13.828 1.00 25.05  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.163 -29.001 13.792 1.00 25.53  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.208 -29.164 14.421 1.00 25.20  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.146 -30.963 12.563 1.00 27.49  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.366 -32.278 12.650 1.00 39.45  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.839 -32.594 13.749 1.00 38.07  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.279 -32.992 11.618 1.00 41.10  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.900 -27.892 13.080 1.00 21.31  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.857 -26.769 13.038 1.00 20.47  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.084 -26.234 14.469 1.00 25.47  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.220 -26.049 14.898 1.00 23.51  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.403 -25.634 12.072 1.00 22.55  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.199 -24.342 12.311 1.00 22.40  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.495 -26.074 10.606 1.00 23.16  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.999 -25.972 15.189 1.00 22.45  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.103 -25.390 16.540 1.00 23.40  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.813 -26.346 17.515 1.00 24.45  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.660 -25.899 18.301 1.00 23.21  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.720 -24.975 17.053 1.00 24.23  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.724 -24.106 18.327 1.00 27.91  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.305 -22.724 18.060 1.00 27.46  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.299 -23.971 18.876 1.00 30.85  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.524 -27.649 17.396 1.00 22.39  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.181 -28.695 18.185 1.00 24.14  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.704 -28.623 17.930 1.00 26.80  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.482 -28.629 18.892 1.00 26.25  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.637 -30.071 17.793 1.00 26.69  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.202 -31.272 18.565 1.00 35.19  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.780 -31.215 20.044 1.00 37.91  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.672 -32.572 17.985 1.00 39.84  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.120 -28.482 16.652 1.00 22.98  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.556 -28.375 16.342 1.00 21.59  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.175 -27.075 16.839 1.00 25.04  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.319 -27.070 17.296 1.00 24.75  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.813 -28.598 14.857 1.00 23.72  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.752 -30.055 14.476 1.00 35.93  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.930 -30.951 15.314 1.00 31.00  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.518 -30.322 13.199 1.00 28.96  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.433 -25.967 16.757 1.00 23.51  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.948 -24.696 17.280 1.00 23.05  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.157 -24.833 18.795 1.00 24.98  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.128 -24.289 19.334 1.00 24.95  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.983 -23.545 16.974 1.00 22.94  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.831 -23.185 15.476 1.00 25.77  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.760 -22.099 15.297 1.00 26.74  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.176 -22.781 14.842 1.00 27.99  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.234 -25.541 19.492 1.00 22.58  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.385 -25.747 20.945 1.00 23.28  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.619 -26.626 21.260 1.00 27.98  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.317 -26.376 22.245 1.00 28.10  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.125 -26.342 21.567 1.00 25.50  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.134 -26.231 23.080 1.00 33.16  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.643 -25.262 23.654 1.00 30.02  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.580 -27.218 23.746 1.00 34.41  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.909 -27.616 20.405 1.00 25.79  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.096 -28.478 20.542 1.00 26.46  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.365 -27.645 20.382 1.00 30.40  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.320 -27.848 21.124 1.00 30.67  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 37.091 -29.605 19.500 1.00 26.40  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 36.080 -30.702 19.828 1.00 29.30  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.848 -31.604 18.626 1.00 31.82  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 35.037 -32.764 18.991 1.00 38.05  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.407 -33.546 18.122 1.00 54.84  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.448 -33.277 16.821 1.00 43.30  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.715 -34.592 18.547 1.00 46.60  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.363 -26.680 19.437 1.00 26.06  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.506 -25.784 19.260 1.00 26.37  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.651 -24.916 20.514 1.00 30.40  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.777 -24.705 20.990 1.00 30.80  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.302 -24.877 18.059 1.00 25.87  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.320 -25.552 16.679 1.00 30.68  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.198 -24.499 15.583 1.00 30.09  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.588 -26.404 16.501 1.00 31.77  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.513 -24.422 21.060 1.00 26.40  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.569 -23.634 22.292 1.00 27.37  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.200 -24.440 23.466 1.00 32.03  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 40.091 -23.919 24.155 1.00 32.40  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.176 -23.116 22.690 1.00 28.01  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.308 -22.246 23.946 1.00 31.28  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 36.020 -21.590 24.329 1.00 35.41  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 35.000 -22.562 24.702 1.00 34.73  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.378 -22.590 25.876 1.00 46.00  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.723 -21.743 26.841 1.00 37.68  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.423 -23.476 26.102 1.00 35.00  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.733 -25.680 23.683 0.39 29.97  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.737 -25.693 23.658 0.28 29.82  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.734 -25.683 23.676 0.33 30.24  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.207 -26.562 24.756 0.39 31.27  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.186 -26.640 24.688 0.28 31.10  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.198 -26.586 24.737 0.33 31.71  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.716 -26.845 24.681 0.39 37.33  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.699 -26.842 24.666 0.28 37.08  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.709 -26.853 24.675 0.33 37.43  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.359 -26.997 25.723 0.39 38.25  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.323 -26.956 25.723 0.28 37.91  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.343 -27.007 25.721 0.33 38.30  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.411 -27.863 24.776 0.39 34.49  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.520 -27.997 24.478 0.28 34.41  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.427 -27.901 24.688 0.33 35.66  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.700 -28.685 23.658 0.39 39.73  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.166 -28.013 24.891 0.28 40.84  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.816 -28.769 25.741 0.33 45.64  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.277 -26.898 23.457 1.00 33.60  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.708 -27.145 23.238 1.00 35.19  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.487 -25.851 23.025 1.00 38.32  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.686 -25.897 22.750 1.00 40.10  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.869 -28.108 22.056 1.00 36.59  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.163 -29.447 22.285 1.00 43.01  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.111 -30.292 21.033 1.00 46.93  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.456 -30.602 20.549 1.00 61.42  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.759 -30.784 19.270 1.00 77.23  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 45.009 -31.040 18.908 1.00 65.55  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.822 -30.677 18.340 1.00 63.05  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.807 -24.702 23.169 1.00 32.45  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.363 -23.356 23.019 1.00 33.20  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.985 -23.119 21.612 1.00 37.33  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 45.020 -22.460 21.475 1.00 38.84  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.362 -23.051 24.164 1.00 36.55  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.681 -21.579 24.320 1.00 47.62  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.757 -20.747 24.141 1.00 46.62  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.851 -21.256 24.622 1.00 53.15  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.348 -23.667 20.579 1.00 29.98  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.835 -23.557 19.202 1.00 29.63  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.237 -22.352 18.491 1.00 32.19  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 42.009 -22.224 18.400 1.00 28.66  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.625 -24.873 18.417 1.00 32.65  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.455 -26.032 19.031 1.00 34.89  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.925 -24.678 16.901 1.00 31.94  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 44.004 -27.425 18.557 1.00 38.85  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.121 -21.458 17.998 1.00 30.84  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.766 -20.257 17.230 1.00 31.66  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.866 -19.268 17.991 1.00 32.86  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.253 -18.396 17.372 1.00 31.05  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.184 -20.581 15.845 1.00 32.42  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.211 -21.098 14.795 1.00 40.29  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.562 -21.241 13.466 1.00 41.36  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.378 -20.169 14.635 1.00 47.05  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.851 -19.352 19.332 1.00 29.74  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.164 -18.359 20.166 1.00 29.16  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.987 -17.072 19.981 1.00 34.97  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.215 -17.133 19.862 1.00 35.39  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 42.104 -18.803 21.633 1.00 33.37  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.428 -19.115 22.058 1.00 35.73  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.156 -20.004 21.849 1.00 32.57  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.314 -15.935 19.832 1.00 31.16  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.999 -14.686 19.507 1.00 31.04  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.655 -13.535 20.412 1.00 33.63  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 43.004 -12.398 20.100 1.00 33.67  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.711 -14.313 18.040 1.00 32.46  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.229 -14.338 17.645 1.00 42.69  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.367 -14.431 18.548 1.00 37.40  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.940 -14.267 16.438 1.00 53.68  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.980 -13.804 21.532 1.00 28.48  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.663 -12.750 22.498 1.00 27.42  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.492 -13.358 23.881 1.00 31.05  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 41.092 -14.530 24.013 1.00 30.32  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.393 -11.920 22.061 1.00 29.37  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 39.088 -12.721 22.215 1.00 27.36  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.296 -10.567 22.799 1.00 30.18  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.795 -12.550 24.902 0.60 28.55  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.788 -12.567 24.916 0.40 27.93  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.585 -12.859 26.310 0.60 28.55  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.537 -12.949 26.298 0.40 27.63  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.503 -11.876 26.780 0.60 30.69  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.577 -11.911 26.900 0.40 30.84  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.619 -10.669 26.536 0.60 30.69  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.821 -10.703 26.815 0.40 31.27  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.893 -12.710 27.152 0.60 34.11  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.803 -13.263 27.152 0.40 32.53  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.640 -12.957 28.638 0.60 34.22  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.718 -12.055 27.303 0.40 33.02  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.988 -13.639 26.645 0.60 34.85  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.430 -13.839 28.514 0.40 32.62  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.445 -12.390 27.419 1.00 26.87  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.397 -11.569 28.015 1.00 26.43  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.682 -11.581 29.510 1.00 31.63  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.696 -12.659 30.127 1.00 31.19  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.948 -12.051 27.697 1.00 27.76  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.720 -12.215 26.158 1.00 27.73  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.928 -11.070 28.318 1.00 29.12  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.990 -10.942 25.285 1.00 29.73  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.918 -10.397 30.076 1.00 28.51  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.220 -10.262 31.505 1.00 28.57  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.963 -9.835  32.264 1.00 34.08  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.376 -8.788  31.965 1.00 32.05  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.423 -9.309  31.759 1.00 33.45  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.710 -9.179  33.256 1.00 34.14  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.672 -9.807  31.035 1.00 33.82  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.565 -10.645 33.263 1.00 32.26  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.371 -10.429 34.081 1.00 32.09  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.867 -10.479 35.517 1.00 39.27  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 37.054 -11.563 36.076 1.00 36.66  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.264 -11.471 33.764 1.00 35.03  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.942 -11.057 34.397 1.00 35.25  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 35.102 -11.653 32.252 1.00 33.54  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.187 -9.302  36.082 0.54 40.06  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.079 -9.276  36.082 0.46 38.66  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.771 -9.141  37.423 0.54 41.73  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.615 -8.998  37.413 0.46 39.79  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.148 -9.863  37.470 0.54 43.64  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.704 -10.011 37.790 0.46 42.35  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 40.031 -9.529  36.676 0.54 42.76  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.513 -10.887 38.639 0.46 42.06  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.817 -9.644  38.513 0.54 47.62  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.503 -8.870  38.446 0.46 44.29  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.508 -9.115  38.375 0.54 62.07  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.847 -7.624  38.272 0.46 50.76  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.303 -10.872 38.356 0.54 39.48  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.808 -9.927  37.023 0.46 37.13  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.532 -11.649 38.534 0.54 39.59  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 41.056 -10.693 37.078 0.46 37.37  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.635 -12.833 37.569 0.54 41.77  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.937 -12.110 36.487 0.46 39.48  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.667 -13.514 37.557 0.54 41.86  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.958 -12.626 36.026 0.46 39.67  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.651 -12.151 39.989 0.54 40.30  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.701 -10.702 38.476 0.46 38.81  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 41.070 -11.081 40.987 0.54 46.64  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.164 -9.308  38.903 0.46 49.27  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.376 -11.699 42.338 0.54 47.79  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.186 -9.342  40.018 0.46 56.82  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.614 -10.692 43.371 0.54 51.03  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.626 -7.997  40.392 0.46 63.66  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.802 -10.168 43.662 0.54 64.43  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.053 -7.250  41.333 0.46 75.92  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.917 -9.270  44.628 0.54 50.19  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 42.001 -7.704  42.002 0.46 61.82  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.882 -10.531 42.981 0.54 52.39  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.525 -6.041  41.607 0.46 63.13  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.570 -13.099 36.786 0.54 36.15  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.713 -12.710 36.430 0.46 35.18  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.547 -14.229 35.855 0.54 34.98  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.492 -14.033 35.811 0.46 34.43  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.822 -13.818 34.413 0.54 37.29  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.623 -13.874 34.292 0.46 36.90  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.479 -12.713 33.998 0.54 35.68  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 39.011 -12.970 33.718 0.46 34.74  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.212 -15.003 35.946 0.54 35.86  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.113 -14.618 36.180 0.46 35.62  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.928 -15.591 37.321 0.54 52.62  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 38.026 -15.134 37.608 0.46 49.70  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.212 -17.075 37.457 0.54 88.82  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.207 -16.633 37.738 0.46 84.82  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.467 -17.883 36.855 0.54 87.96  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.237 -17.057 38.310 0.46 86.44  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.173 -17.430 38.178 0.54 89.58  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.321 -17.384 37.267 0.46 84.91  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.417 -14.745 33.646 1.00 33.57  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.738 -14.611 32.231 1.00 33.02  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.110 -15.744 31.436 1.00 35.32  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.145 -16.885 31.891 1.00 35.38  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.266 -14.619 32.060 1.00 35.85  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.954 -13.376 32.608 1.00 51.39  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.430 -13.303 32.293 1.00 71.25  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 45.004 -14.134 31.571 1.00 63.89  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 45.080 -12.286 32.835 1.00 73.20  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.511 -15.427 30.268 1.00 29.08  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.857 -16.409 29.390 1.00 28.53  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.365 -16.237 27.979 1.00 32.35  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.210 -15.159 27.400 1.00 32.94  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.330 -16.218 29.394 1.00 29.70  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.717 -16.346 30.766 1.00 31.70  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.578 -15.234 31.590 1.00 33.60  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.252 -17.575 31.224 1.00 34.34  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 36.029 -15.356 32.871 1.00 35.37  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.696 -17.695 32.503 1.00 37.49  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.577 -16.584 33.313 1.00 35.25  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.988 -17.280 27.430 1.00 29.11  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.494 -17.243 26.057 1.00 27.83  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.362 -17.633 25.100 1.00 31.34  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.557 -18.526 25.403 1.00 30.02  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.722 -18.161 25.887 1.00 30.26  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.956 -17.685 26.699 1.00 37.44  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.265 -18.115 26.052 1.00 46.71  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.284 -17.744 24.631 1.00 56.48  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.866 -16.659 24.130 1.00 70.20  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.573 -15.855 24.912 1.00 63.34  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.788 -16.398 22.834 1.00 52.27  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.279 -16.968 23.941 1.00 28.19  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.206 -17.276 22.984 1.00 27.73  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.580 -16.861 21.568 1.00 28.15  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.667 -16.303 21.350 1.00 26.81  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.903 -16.585 23.408 1.00 28.39  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.683 -17.161 20.612 1.00 25.27  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.819 -16.756 19.218 1.00 24.31  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.946 -15.507 19.043 1.00 27.19  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.737 -15.553 19.336 1.00 25.80  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.329 -17.870 18.267 1.00 24.29  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.095 -19.149 18.432 1.00 27.59  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.613 -20.182 19.226 1.00 29.15  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.341 -19.473 18.000 1.00 29.56  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.553 -21.121 19.208 1.00 29.12  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.617 -20.737 18.492 1.00 29.23  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.549 -14.407 18.587 1.00 25.51  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.819 -13.147 18.321 1.00 25.79  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.575 -13.403 17.446 1.00 27.85  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.504 -12.879 17.752 1.00 25.50  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.728 -12.135 17.600 1.00 27.95  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.766 -11.510 18.523 1.00 30.87  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.688 -10.578 17.738 1.00 30.90  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.772 -10.066 18.642 1.00 32.88  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.744 -9.222  17.902 1.00 34.94  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.709 -14.200 16.371 1.00 25.11  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.569 -14.440 15.467 1.00 25.15  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.391 -15.092 16.166 1.00 26.19  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.257 -14.693 15.914 1.00 26.50  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.985 -15.209 14.225 1.00 30.47  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.585 -16.423 14.658 1.00 31.69  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.925 -14.387 13.327 1.00 32.50  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.646 -16.059 17.056 1.00 22.12  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.550 -16.728 17.789 1.00 21.62  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.880 -15.740 18.737 1.00 24.98  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.642 -15.696 18.811 1.00 23.21  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 33.035 -17.998 18.525 1.00 24.59  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.893 -18.596 19.362 1.00 24.80  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.554 -19.029 17.510 1.00 25.21  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.696 -14.931 19.454 1.00 23.55  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.134 -13.926 20.364 1.00 23.11  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.224 -12.939 19.608 1.00 26.32  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.108 -12.668 20.066 1.00 26.71  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.260 -13.160 21.089 1.00 22.99  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.203 -13.969 22.015 1.00 25.92  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.277 -13.038 22.627 1.00 25.95  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.414 -14.682 23.124 1.00 28.19  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.664 -12.471 18.422 1.00 23.40  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.881 -11.543 17.582 1.00 25.05  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.599 -12.178 17.086 1.00 28.38  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.552 -11.531 17.088 1.00 29.14  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.695 -11.074 16.377 1.00 27.07  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.908 -10.280 16.766 1.00 30.15  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.976 -10.175 15.319 1.00 34.08  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.198 -8.872  14.476 1.00 30.44  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.661 -13.467 16.705 1.00 24.39  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.494 -14.193 16.192 1.00 24.25  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.400 -14.410 17.273 1.00 28.53  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.242 -14.637 16.920 1.00 28.45  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.948 -15.549 15.615 1.00 24.54  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.777 -14.360 18.569 1.00 24.33  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.873 -14.619 19.698 1.00 25.27  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.414 -13.400 20.489 1.00 28.33  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.467 -13.535 21.276 1.00 26.70  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.539 -15.607 20.646 1.00 25.31  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.874 -17.219 19.910 1.00 27.73  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.173 -12.298 20.435 1.00 25.06  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.964 -11.154 21.326 1.00 24.79  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.974 -9.845  20.573 1.00 28.81  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.947 -9.544  19.865 1.00 27.70  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.078 -11.166 22.376 1.00 25.63  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.386 -9.916  22.976 1.00 29.59  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.929 -9.043  20.776 1.00 25.99  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.866 -7.713  20.180 1.00 26.01  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.980 -6.815  20.687 1.00 29.18  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.515 -5.993  19.927 1.00 28.60  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.386 -6.995  21.972 1.00 26.78  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.500 -6.192  22.515 1.00 26.22  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.838 -6.550  21.833 1.00 29.12  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.549 -5.647  21.376 1.00 26.19  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.603 -6.374  24.048 1.00 26.02  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.686 -5.507  24.727 1.00 31.36  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.291 -4.018  24.734 1.00 33.01  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.958 -6.001  26.122 1.00 31.19  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.166 -7.847  21.720 1.00 24.89  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.435 -8.216  21.056 1.00 23.97  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.416 -7.879  19.581 1.00 28.11  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.443 -7.498  19.039 1.00 27.50  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.807 -9.680  21.292 1.00 24.87  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.230 -9.925  22.724 1.00 25.51  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.299 -9.221  23.287 1.00 28.24  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.581 -10.878 23.504 1.00 26.84  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.663 -9.419  24.631 1.00 28.83  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.984 -11.112 24.829 1.00 29.16  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 33.010 -10.372 25.384 1.00 26.48  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.238 -7.956  18.941 1.00 26.02  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.114 -7.577  17.531 1.00 27.19  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.534 -6.099  17.369 1.00 30.54  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.324 -5.780  16.476 1.00 28.91  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.670 -7.795  17.071 1.00 29.01  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.411 -7.279  15.679 1.00 33.04  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 29.048 -7.840  14.576 1.00 34.63  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.539 -6.217  15.464 1.00 37.19  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.809 -7.365  13.285 1.00 36.96  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.289 -5.738  14.183 1.00 40.46  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.918 -6.322  13.098 1.00 47.80  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.651 -5.846  11.848 1.00 53.56  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 30.014 -5.216  18.239 0.53 28.98  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 30.013 -5.217  18.239 0.47 29.22  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.334 -3.784  18.235 0.53 30.06  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.339 -3.789  18.235 0.47 30.49  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.823 -3.541  18.533 0.53 35.62  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.835 -3.573  18.502 0.47 35.55  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.448 -2.726  17.861 0.53 37.29  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.473 -2.808  17.784 0.47 36.87  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.453 -3.043  19.240 0.53 32.65  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.505 -3.052  19.281 0.47 33.95  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 28.103 -3.036  18.803 0.53 34.55  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.828 -1.671  19.295 0.47 40.37  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.391 -4.268  19.517 1.00 31.77  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.808 -4.152  19.908 1.00 30.79  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.755 -4.533  18.770 1.00 33.99  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.637 -3.750  18.435 1.00 36.10  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.142 -4.977  21.203 1.00 32.87  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.426 -4.403  22.450 1.00 32.91  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.672 -5.064  21.450 1.00 32.34  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.460 -5.397  23.664 1.00 34.26  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.583 -5.727  18.194 1.00 28.49  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.560 -6.181  17.215 1.00 28.54  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.334 -5.632  15.801 1.00 33.73  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.177 -5.880  14.929 1.00 34.84  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.699 -7.709  17.258 1.00 28.77  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.117 -8.192  18.633 1.00 29.28  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.318 -7.773  19.203 1.00 32.64  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.323 -9.083  19.344 1.00 30.13  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.697 -8.213  20.481 1.00 33.28  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.713 -9.541  20.608 1.00 32.92  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.892 -9.098  21.172 1.00 31.59  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.272 -4.831  15.579 1.00 31.16  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 34.109 -4.147  14.282 1.00 31.74  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.646 -2.720  14.405 1.00 38.63  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.722 -1.991  13.407 1.00 39.39  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.683 -4.188  13.718 1.00 38.58  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.772 -3.654  14.671 1.00 35.64  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.261 -5.581  13.248 1.00 35.44  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 35.051 -2.320  15.629 1.00 34.73  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.652 -0.997  15.823 1.00 35.93  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 37.082 -1.061  15.283 1.00 41.96  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.829 -1.954  15.670 1.00 40.23  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.645 -0.602  17.309 1.00 37.13  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.412 0.677   17.549 1.00 52.08  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.822 1.758   17.381 1.00 56.60  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.622 0.594   17.845 1.00 53.97  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.473 -0.084  14.436 1.00 43.30  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.783 -0.025  13.780 1.00 44.62  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.985 -0.061  14.738 1.00 48.19  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 41.049 -0.517  14.318 1.00 50.75  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.877 1.177   12.824 1.00 48.42  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 38.027 1.009   11.565 1.00 66.29  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.838 0.401   16.002 1.00 40.74  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.929 0.324   16.977 1.00 40.31  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.846 -0.934  17.834 1.00 43.72  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.868 -1.568  18.084 1.00 45.33  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.944 1.550   17.924 1.00 41.49  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.547 2.840   17.408 1.00 48.59  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.377 3.946   18.433 1.00 49.54  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 43.035 2.685   17.071 1.00 53.80  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.646 -1.262  18.347 1.00 36.60  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.481 -2.383  19.273 1.00 35.23  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.610 -3.737  18.591 1.00 40.23  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.977 -4.703  19.257 1.00 39.85  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.173 -2.274  20.082 1.00 35.37  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 38.058 -1.004  20.947 1.00 36.00  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.788 -1.090  21.790 1.00 34.79  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.437 0.214   22.477 1.00 41.68  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.908 1.237   21.544 1.00 41.74  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.358 -3.804  17.263 1.00 39.48  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.484 -5.055  16.487 1.00 40.01  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.880 -5.683  16.633 1.00 44.42  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 41.015 -6.899  16.469 1.00 44.99  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.122 -4.839  15.016 1.00 42.49  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.284 -3.785  14.091 1.00 49.14  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.909 -4.843  16.924 1.00 39.96  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.315 -5.230  17.052 1.00 40.80  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.787 -5.538  18.473 1.00 43.87  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.955 -5.905  18.669 1.00 43.31  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.215 -4.165  16.405 1.00 43.84  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 44.020 -4.097  14.901 1.00 61.36  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.972 -3.018  14.310 1.00 60.28  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.857 -5.247  14.249 1.00 51.10  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.899 -5.388  19.464 1.00 40.07  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.271 -5.661  20.843 1.00 39.54  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.273 -7.161  21.117 1.00 41.56  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.372 -7.872  20.646 1.00 39.76  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.324 -4.935  21.825 1.00 39.61  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.340 -3.394  21.793 1.00 44.85  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.296 -2.831  22.745 1.00 44.88  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.728 -2.829  22.133 1.00 46.87  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.275 -7.642  21.871 0.51 38.73  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.282 -7.632  21.873 0.49 38.63  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.373 -9.058  22.249 0.51 38.31  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.426 -9.038  22.270 0.49 38.22  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.760 -9.286  23.645 0.51 39.43  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.794 -9.279  23.654 0.49 39.41  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.583 -10.429 24.061 0.51 37.32  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.636 -10.426 24.069 0.49 37.28  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.825 -9.526  22.215 0.51 43.59  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.900 -9.432  22.290 0.49 43.31  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.637 -8.759  23.088 0.51 52.70  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.433 -9.487  20.976 0.49 51.18  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.469 -8.188  24.375 1.00 35.82  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.872 -8.215  25.720 1.00 34.86  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.689 -7.240  25.772 1.00 35.98  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.834 -6.062  25.401 1.00 35.88  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.908 -7.884  26.844 1.00 40.30  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.261 -7.895  28.234 1.00 40.61  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 45.116 -8.826  26.808 1.00 41.00  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.543 -7.727  26.269 1.00 29.06  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.339 -6.922  26.476 1.00 28.92  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.940 -7.036  27.944 1.00 32.83  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.694 -8.147  28.424 1.00 31.49  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.169 -7.298  25.507 1.00 30.56  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.562 -7.121  23.996 1.00 31.88  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.855 -6.554  25.855 1.00 31.66  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.957 -5.678  23.502 1.00 34.94  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.820 -5.891  28.633 1.00 30.97  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.407 -5.845  30.029 1.00 30.62  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.930 -5.516  30.140 1.00 32.91  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.496 -4.455  29.690 1.00 31.34  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.225 -4.809  30.816 1.00 34.55  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.707 -4.998  30.736 1.00 53.40  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.241 -6.041  31.088 1.00 43.63  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.405 -3.977  30.287 1.00 48.99  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.158 -6.415  30.752 1.00 27.90  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.738 -6.165  30.951 1.00 27.76  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.499 -5.279  32.178 1.00 32.04  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.379 -5.140  33.046 1.00 32.38  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.939 -7.480  31.080 1.00 27.07  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 34.002 -8.483  29.899 1.00 31.34  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.888 -9.520  30.047 1.00 31.65  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.924 -7.782  28.529 1.00 29.69  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.301 -4.691  32.249 1.00 29.29  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.862 -3.826  33.350 1.00 31.00  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 33.071 -4.578  34.682 1.00 35.82  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.732 -5.762  34.746 1.00 34.49  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.378 -3.490  33.158 1.00 32.64  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.832 -2.462  34.133 1.00 43.25  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.705 -2.789  35.338 1.00 44.18  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.502 -1.347  33.690 1.00 44.93  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.631 -3.938  35.734 1.00 35.68  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.857 -4.666  37.009 1.00 36.66  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.620 -5.254  37.681 1.00 40.13  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.770 -6.133  38.528 1.00 40.94  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.538 -3.624  37.914 1.00 39.96  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.236 -2.304  37.295 1.00 44.69  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.123 -2.543  35.818 1.00 38.36  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.410 -4.808  37.306 1.00 36.84  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.160 -5.330  37.873 1.00 38.68  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.877 -6.747  37.333 1.00 38.36  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 29.053 -7.468  37.901 1.00 37.46  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.983 -4.403  37.504 1.00 41.47  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.824 -4.423  38.488 1.00 63.01  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 28.006 -3.538  39.708 1.00 92.53  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.083 -2.299  39.538 1.00 92.64  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.063 -4.083  40.835 1.00 86.32  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.537 -7.136  36.231 1.00 32.19  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.287 -8.453  35.627 1.00 31.07  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.881 -9.578  36.454 1.00 35.59  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 32.058 -9.553  36.814 1.00 34.74  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.741 -8.490  34.137 1.00 33.26  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 30.019 -7.391  33.307 1.00 34.53  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.547 -9.885  33.512 1.00 30.70  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.421 -7.384  33.369 1.00 39.76  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 30.056 -10.571 36.705 1.00 35.57  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.375 -11.755 37.486 1.00 36.22  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.119 -12.782 36.613 1.00 35.76  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.590 -13.174 35.573 1.00 33.67  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 29.067 -12.341 38.051 1.00 38.72  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.262 -13.620 38.811 1.00 53.50  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.969 -14.698 38.309 1.00 44.75  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.764 -13.525 40.039 1.00 45.47  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.332 -13.244 37.020 1.00 33.21  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 33.066 -14.231 36.200 1.00 32.30  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.315 -15.545 35.953 1.00 36.27  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.421 -16.100 34.858 1.00 34.29  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.354 -14.467 36.999 1.00 35.61  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.500 -13.242 37.868 1.00 41.00  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 33.101 -12.870 38.229 1.00 36.62  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.533 -16.024 36.943 1.00 33.39  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.771 -17.265 36.765 1.00 32.96  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.669 -17.082 35.699 1.00 34.84  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.522 -17.948 34.837 1.00 33.02  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.199 -17.789 38.090 1.00 35.64  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.643 -19.198 37.923 1.00 45.45  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.776 -19.766 39.035 1.00 72.15  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.746 -21.010 39.166 1.00 71.92  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.117 -18.985 39.759 1.00 65.38  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.933 -15.961 35.759 1.00 31.82  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.919 -15.637 34.755 1.00 31.08  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.537 -15.579 33.362 1.00 31.69  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.974 -16.115 32.392 1.00 29.24  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.731 -14.956 33.257 1.00 27.57  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.431 -14.885 31.968 1.00 25.96  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.801 -16.297 31.495 1.00 29.09  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.557 -16.635 30.336 1.00 27.52  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.701 -13.985 32.040 1.00 27.21  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.312 -13.843 30.663 1.00 27.93  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.742 -12.993 29.715 1.00 30.33  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.356 -14.671 30.259 1.00 29.04  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.242 -12.934 28.410 1.00 30.73  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.856 -14.609 28.956 1.00 30.38  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.288 -13.751 28.034 1.00 29.13  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.390 -17.110 32.377 1.00 30.31  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.780 -18.487 32.054 1.00 31.71  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.595 -19.318 31.483 1.00 32.27  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.745 -19.998 30.454 1.00 30.07  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.398 -19.163 33.274 1.00 35.69  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.110 -20.791 32.921 1.00 41.88  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.415 -19.211 32.132 1.00 28.82  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.184 -19.915 31.738 1.00 27.63  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.780 -19.460 30.332 1.00 27.51  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.425 -20.285 29.482 1.00 26.71  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 27.071 -19.679 32.795 1.00 30.78  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.383 -20.492 34.101 1.00 31.85  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.661 -19.996 32.239 1.00 30.45  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.668 -19.995 35.302 1.00 40.13  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.851 -18.154 30.097 1.00 23.90  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.501 -17.610 28.774 1.00 24.37  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.509 -17.962 27.698 1.00 28.28  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.111 -18.228 26.558 1.00 25.99  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.241 -16.119 28.851 1.00 24.77  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.937 -15.759 29.609 1.00 30.97  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.844 -14.280 29.764 1.00 32.51  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.684 -16.290 28.883 1.00 33.30  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.814 -17.992 28.042 1.00 25.48  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.853 -18.401 27.089 1.00 24.67  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.631 -19.869 26.685 1.00 26.85  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.632 -20.204 25.490 1.00 24.86  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.250 -18.160 27.690 1.00 24.62  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.430 -18.445 26.728 1.00 29.49  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.395 -17.516 25.489 1.00 28.40  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.788 -18.326 27.472 1.00 31.58  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.338 -20.725 27.671 1.00 25.37  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 29.989 -22.117 27.402 1.00 25.57  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.773 -22.212 26.458 1.00 27.99  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.806 -22.986 25.503 1.00 27.61  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.706 -22.840 28.723 1.00 29.14  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.957 -23.211 29.510 1.00 43.93  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.074 -23.140 28.931 1.00 44.99  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.820 -23.585 30.702 1.00 44.53  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.711 -21.435 26.718 1.00 24.48  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.525 -21.393 25.846 1.00 23.15  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.903 -21.004 24.402 1.00 24.18  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.418 -21.602 23.442 1.00 23.14  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.468 -20.416 26.403 1.00 24.36  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.358 -20.134 25.415 1.00 24.74  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.387 -21.096 25.139 1.00 26.77  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.340 -18.947 24.684 1.00 27.21  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.398 -20.854 24.189 1.00 27.17  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.352 -18.716 23.717 1.00 29.36  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.377 -19.659 23.496 1.00 27.83  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.740 -19.968 24.241 1.00 20.98  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.140 -19.536 22.889 1.00 20.90  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.706 -20.679 22.068 1.00 24.54  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.383 -20.794 20.886 1.00 23.91  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.225 -18.445 23.000 1.00 21.99  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.704 -17.151 23.583 1.00 24.26  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 30.045 -15.908 23.480 1.00 28.56  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.357 -14.582 24.567 1.00 28.80  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.567 -21.509 22.693 1.00 22.20  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.249 -22.611 22.013 1.00 22.47  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.503 -23.915 21.997 1.00 26.81  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.978 -24.871 21.366 1.00 25.30  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.637 -22.829 22.634 1.00 24.13  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.683 -21.840 22.152 1.00 25.25  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.817 -20.586 22.748 1.00 27.18  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.531 -22.153 21.085 1.00 25.87  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.800 -19.681 22.322 1.00 28.89  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.546 -21.277 20.683 1.00 27.02  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.647 -20.026 21.272 1.00 30.65  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.666 -19.190 20.874 1.00 27.00  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.355 -23.999 22.690 1.00 23.28  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.656 -25.293 22.761 1.00 23.85  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.143 -25.291 22.529 1.00 26.59  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.584 -26.374 22.318 1.00 26.45  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.851 -25.963 24.161 1.00 28.24  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.158 -25.219 25.166 1.00 26.99  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.318 -26.180 24.558 1.00 28.03  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.490 -24.122 22.612 0.67 22.82  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.486 -24.119 22.645 0.33 22.80  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 24.018 -23.930 22.574 0.67 22.81  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 24.022 -23.916 22.588 0.33 22.76  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.366 -24.330 23.921 0.67 25.68  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.334 -24.404 23.888 0.33 26.89  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.169 -24.122 24.085 0.67 24.90  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.107 -24.377 23.975 0.33 26.97  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.344 -24.704 21.436 0.67 24.51  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.396 -24.564 21.349 0.33 24.72  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 24.010 -24.562 20.195 0.67 22.05  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.101 -25.938 21.544 0.33 26.82  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.150 -24.856 24.892 0.67 23.55  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.134 -24.819 24.899 0.33 24.15  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.603 -25.290 26.188 0.67 24.45  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.650 -25.334 26.187 0.33 25.00  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.837 -24.253 27.246 0.67 28.87  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.859 -24.294 27.275 0.33 28.98  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.965 -23.782 27.419 0.67 27.25  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.989 -23.841 27.480 0.33 27.81  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.186 -26.636 26.644 0.67 27.47  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.362 -26.655 26.562 0.33 26.98  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.898 -27.794 25.686 0.67 33.78  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.262 -27.762 25.503 0.33 34.21  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.906 -28.920 25.888 0.67 42.20  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.098 -28.700 25.750 0.33 39.28  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.834 -29.465 27.247 0.67 52.29  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.969 -29.717 24.702 0.33 41.65  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 24.047 -30.475 27.605 0.67 64.72  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.264 -31.005 24.857 0.33 53.79  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.275 -31.074 26.707 0.67 52.10  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.101 -31.854 23.852 0.33 44.03  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 24.033 -30.898 28.860 0.67 49.96  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.702 -31.457 26.025 0.33 36.57  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.774 -23.909 27.964 1.00 25.94  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.826 -22.894 29.018 1.00 26.06  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.601 -23.532 30.381 1.00 31.49  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.540 -24.124 30.615 1.00 30.42  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.774 -21.821 28.725 1.00 26.74  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.770 -20.610 29.673 1.00 30.01  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.044 -19.766 29.469 1.00 27.43  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.526 -19.767 29.478 1.00 32.36  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.601 -23.418 31.277 1.00 30.52  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.502 -23.984 32.631 1.00 31.94  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.800 -22.985 33.566 1.00 36.82  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.451 -22.301 34.362 1.00 36.50  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.893 -24.392 33.161 1.00 35.77  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.852 -25.016 34.549 1.00 52.98  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.854 -25.603 34.970 1.00 44.23  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.933 -24.893 35.294 1.00 47.03  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.482 -22.868 33.415 1.00 33.03  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.663 -21.923 34.168 1.00 34.80  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.147 -22.579 35.437 1.00 39.06  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.510 -23.641 35.379 1.00 38.05  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.532 -21.422 33.259 1.00 35.57  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.838 -20.132 33.604 1.00 41.87  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.852 -18.947 33.658 1.00 42.15  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.718 -19.870 32.603 1.00 41.83  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.501 -21.987 36.599 1.00 36.08  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.143 -22.501 37.929 1.00 38.34  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.609 -21.381 38.815 1.00 40.07  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.959 -20.211 38.605 1.00 37.48  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.363 -23.158 38.608 1.00 40.47  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.994 -24.307 37.818 1.00 46.32  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.229 -24.893 38.491 1.00 64.79  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.929 -25.519 39.784 1.00 84.05  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.494 -26.767 39.942 1.00 105.72 ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.242 -27.239 41.157 1.00 94.10  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.296 -27.549 38.886 1.00 95.91  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.782 -21.722 39.820 1.00 39.02  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.241 -20.708 40.746 1.00 38.97  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.353 -19.806 41.324 1.00 43.83  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.179 -18.588 41.402 1.00 44.32  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.431 -21.376 41.890 1.00 42.62  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.694 -20.391 42.779 1.00 55.01  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 15.984 -20.998 43.978 1.00 86.22  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.548 -21.916 44.619 1.00 81.49  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.860 -20.540 44.285 1.00 87.17  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.481 -20.413 41.687 1.00 41.24  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.620 -19.709 42.268 1.00 42.01  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.414 -18.831 41.318 1.00 43.24  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.187 -17.984 41.772 1.00 44.12  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.249 -19.010 39.991 1.00 37.39  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 23.035 -18.199 39.049 1.00 35.38  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.188 -17.340 38.092 1.00 38.36  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.756 -16.529 37.351 1.00 36.28  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 24.016 -19.108 38.275 1.00 34.78  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.376 -20.041 37.257 1.00 44.30  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.318 -19.752 36.692 1.00 33.99  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 24.018 -21.176 36.976 1.00 37.27  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.845 -17.531 38.076 1.00 36.01  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.971 -16.872 37.089 1.00 35.85  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.098 -15.344 37.072 1.00 37.59  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.145 -14.757 35.982 1.00 34.96  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.489 -17.324 37.164 1.00 40.31  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.682 -16.765 35.955 1.00 40.88  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.833 -17.020 38.527 1.00 39.94  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.525 -17.608 35.501 1.00 42.48  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.197 -14.704 38.241 1.00 35.84  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.327 -13.243 38.265 1.00 36.93  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.626 -12.768 37.614 1.00 38.61  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.590 -11.817 36.829 1.00 36.68  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.158 -12.668 39.689 1.00 41.62  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.790 -12.952 40.318 1.00 49.01  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.337 -12.656 39.263 1.00 55.30  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.325 -10.860 39.199 1.00 52.99  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.763 -13.438 37.916 1.00 35.82  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.080 -13.081 37.357 1.00 34.79  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.112 -13.382 35.860 1.00 35.55  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.649 -12.593 35.084 1.00 34.30  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.188 -13.853 38.066 1.00 36.12  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.524 -14.522 35.451 1.00 30.54  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.479 -14.884 34.023 1.00 28.48  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.656 -13.838 33.241 1.00 31.53  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.119 -13.382 32.189 1.00 30.00  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.951 -16.336 33.834 1.00 32.15  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.621 -16.634 32.371 1.00 29.98  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.955 -17.352 34.365 1.00 32.99  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.455 -13.467 33.744 0.20 30.13  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.454 -13.467 33.742 0.80 30.09  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.598 -12.479 33.083 0.20 31.04  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.621 -12.482 33.048 0.80 31.75  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.300 -11.129 32.947 0.20 34.93  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.323 -11.125 32.938 0.80 34.72  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.271 -10.544 31.864 0.20 33.94  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.299 -10.525 31.865 0.80 33.13  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.253 -12.312 33.805 0.20 34.94  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.255 -12.309 33.713 0.80 35.85  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.285 -11.438 33.035 0.20 39.41  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.325 -11.404 32.910 0.80 40.50  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.748 -11.135 33.911 0.20 45.64  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.640 -11.410 33.542 0.80 46.79  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.224 -9.664  33.098 0.20 42.98  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.828 -10.356 35.070 0.80 44.94  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.937 -10.649 34.035 1.00 32.35  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.668 -9.360  34.037 1.00 32.61  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.827 -9.391  33.023 1.00 33.50  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 24.017 -8.426  32.261 1.00 31.54  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.188 -9.042  35.437 1.00 34.14  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.567 -10.518 32.979 1.00 28.86  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.676 -10.679 32.035 1.00 28.18  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.137 -10.724 30.588 1.00 30.49  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.705 -10.063 29.722 1.00 28.73  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.586 -11.876 32.390 1.00 33.71  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.896 -11.855 33.782 1.00 32.25  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.892 -11.879 31.596 1.00 32.67  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 24.034 -11.479 30.323 1.00 27.04  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.457 -11.536 28.968 1.00 26.21  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.921 -10.171 28.507 1.00 29.08  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.067 -9.821  27.334 1.00 27.88  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.377 -12.613 28.884 1.00 27.54  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.385 -9.357  29.434 1.00 27.81  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.932 -8.008  29.056 1.00 28.99  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.129 -7.143  28.619 1.00 31.74  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.083 -6.482  27.579 1.00 31.95  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.162 -7.352  30.211 1.00 32.60  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.776 -7.955  30.417 1.00 37.56  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 19.024 -7.397  31.973 1.00 45.29  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.806 -5.635  31.613 1.00 43.12  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.209 -7.182  29.397 1.00 29.52  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.447 -6.447  29.120 1.00 28.98  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 26.063 -6.911  27.780 1.00 30.93  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.457 -6.082  26.955 1.00 29.48  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.425 -6.698  30.270 1.00 29.63  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.833 -6.197  30.029 1.00 29.44  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.138 -4.840  30.123 1.00 32.09  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.877 -7.089  29.781 1.00 28.78  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.442 -4.377  29.913 1.00 30.44  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.185 -6.644  29.627 1.00 29.23  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.460 -5.286  29.681 1.00 31.10  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.755 -4.878  29.551 1.00 31.32  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.113 -8.236  27.558 1.00 26.77  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.671 -8.814  26.336 1.00 25.30  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.749 -8.694  25.122 1.00 29.40  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.170 -8.992  23.998 1.00 29.22  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.090 -10.278 26.573 1.00 23.99  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.232 -10.554 27.576 1.00 26.82  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.515 -12.073 27.658 1.00 27.51  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.553 -9.814  27.180 1.00 28.52  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.479 -8.312  25.345 1.00 27.02  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.482 -8.184  24.270 1.00 27.87  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.236 -9.537  23.596 1.00 30.66  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.509 -9.726  22.404 1.00 29.44  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.870 -7.085  23.261 1.00 29.19  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 24.012 -5.700  23.904 1.00 30.90  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.717 -4.733  22.984 1.00 39.88  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.647 -4.844  21.760 1.00 36.29  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.429 -3.777  23.554 1.00 39.40  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.779 -10.498 24.407 1.00 27.20  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.438 -11.874 23.998 1.00 27.29  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.944 -12.023 24.254 1.00 32.96  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.507 -12.490 25.320 1.00 31.04  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.284 -12.880 24.784 1.00 28.40  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.775 -12.741 24.472 1.00 30.02  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.831 -13.762 25.503 1.00 32.33  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.501 -15.448 24.746 1.00 29.04  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.154 -11.512 23.299 1.00 33.36  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.689 -11.386 23.401 1.00 35.35  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.924 -12.665 23.754 1.00 36.89  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 17.021 -12.599 24.582 1.00 35.88  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.100 -10.769 22.123 1.00 38.38  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.581 -9.347  21.883 1.00 53.08  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.262 -13.809 23.142 1.00 33.52  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.545 -15.056 23.431 1.00 34.77  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.771 -15.539 24.865 1.00 35.34  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.830 -16.024 25.502 1.00 35.70  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.873 -16.134 22.400 1.00 36.65  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.416 -15.781 21.019 1.00 41.44  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.086 -15.499 20.749 1.00 45.19  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.120 -15.712 19.865 1.00 43.07  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 16.028 -15.239 19.453 1.00 45.07  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.223 -15.370 18.877 1.00 44.07  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 19.000 -15.363 25.385 1.00 29.01  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.320 -15.725 26.780 1.00 29.46  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.532 -14.820 27.739 1.00 34.65  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.904 -15.324 28.674 1.00 32.27  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.843 -15.705 27.087 1.00 32.24  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.099 -15.973 28.574 1.00 32.04  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.584 -16.722 26.223 1.00 31.48  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.552 -13.493 27.500 1.00 31.22  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.801 -12.526 28.322 1.00 31.84  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.322 -12.952 28.388 1.00 37.93  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.780 -13.050 29.479 1.00 37.92  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.972 -11.063 27.829 1.00 35.26  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.114 -10.088 28.653 1.00 36.35  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.433 -10.643 27.886 1.00 34.00  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.725 -13.285 27.230 0.61 36.25  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.692 -13.189 27.216 0.39 35.98  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.338 -13.737 27.110 0.61 37.50  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.290 -13.597 27.067 0.39 37.28  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 14.020 -14.981 27.959 0.61 40.35  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.918 -14.814 27.920 0.39 41.04  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 13.021 -14.956 28.682 0.61 41.08  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.896 -14.779 28.609 0.39 42.00  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.963 -13.962 25.635 0.61 39.88  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.964 -13.878 25.584 0.39 39.35  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.511 -14.355 25.426 0.61 54.83  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.701 -12.659 24.719 0.39 52.28  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.621 -13.553 25.784 0.61 58.56  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.235 -11.632 25.260 0.39 55.09  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.267 -15.462 24.903 0.61 61.05  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.940 -12.738 23.494 0.39 58.31  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.856 -16.052 27.899 0.61 35.43  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.751 -15.873 27.890 0.39 36.28  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.564 -17.251 28.710 0.61 35.72  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.498 -17.111 28.640 0.39 36.58  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.740 -16.981 30.200 0.61 38.92  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.680 -16.896 30.151 0.39 39.55  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.006 -17.557 31.003 0.61 39.10  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.879 -17.425 30.924 0.39 39.98  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.315 -18.514 28.253 0.61 34.90  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.311 -18.279 28.070 0.39 41.15  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.677 -19.644 28.859 0.61 37.86  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.256 -18.231 26.641 0.39 39.79  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.800 -18.514 28.635 0.61 29.33  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.783 -19.626 28.528 0.39 41.24  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.704 -16.105 30.568 1.00 34.99  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.941 -15.750 31.988 1.00 35.65  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.728 -15.043 32.537 1.00 41.83  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.265 -15.401 33.628 1.00 40.75  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.185 -14.883 32.137 1.00 35.18  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.729 -15.786 31.910 1.00 37.61  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.192 -14.063 31.769 0.48 39.79  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.197 -14.050 31.785 0.52 40.14  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.995 -13.287 32.104 0.48 41.45  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 13.002 -13.294 32.161 0.52 41.94  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.803 -14.216 32.358 0.48 45.53  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.797 -14.222 32.372 0.52 45.72  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.074 -14.026 33.332 0.48 45.92  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.056 -14.041 33.338 0.52 46.06  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.649 -12.303 30.973 0.48 42.96  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.682 -12.220 31.114 0.52 44.27  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.588 -11.114 30.871 0.48 54.56  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.437 -10.914 31.331 0.52 58.47  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.984 -9.986  30.053 0.48 67.69  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.706 -9.736  30.704 0.52 70.59  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.986 -8.980  29.691 0.48 72.33  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.839 -9.714  29.245 0.52 75.98  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.328 -7.942  30.449 0.48 82.88  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.621 -8.876  28.572 0.52 86.12  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.746 -7.749  31.627 0.48 73.42  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.343 -7.965  29.217 0.52 70.63  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.255 -7.089  30.035 0.48 64.96  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.682 -8.934  27.249 0.52 70.72  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.632 -15.233 31.493 1.00 41.42  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.536 -16.217 31.590 1.00 43.08  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.689 -17.133 32.800 1.00 46.96  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.701  -17.380 33.488 1.00 46.61  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.393 -17.026 30.290 1.00 44.84  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.844  -16.179 29.147 1.00 65.25  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.702  -16.933 27.842 1.00 77.22  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.265  -15.993 26.744 1.00 91.40  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.442  -16.681 25.718 1.00 104.94 ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.923 -17.620 33.074 1.00 42.56  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.186 -18.485 34.233 1.00 43.11  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 11.989 -17.717 35.546 1.00 47.53  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.445 -18.274 36.501 1.00 47.19  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.584 -19.110 34.150 1.00 43.51  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.710 -20.381 33.322 1.00 45.46  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.146 -20.469 32.050 1.00 48.54  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.452 -21.463 33.789 1.00 48.30  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.285 -21.633 31.281 1.00 49.09  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.585 -22.630 33.020 1.00 50.13  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 13.997 -22.706 31.776 1.00 47.75  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.376 -16.427 35.576 1.00 43.06  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.178 -15.576 36.760 1.00 44.25  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.684 -15.324 37.012 1.00 52.43  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.233 -15.477 38.151 1.00 53.62  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.027 -14.280 36.675 1.00 46.21  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.520 -14.640 36.804 1.00 44.64  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.617 -13.245 37.758 1.00 49.33  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.486 -13.604 36.284 1.00 49.58  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.915  -15.006 35.943 1.00 50.99  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.471  -14.753 36.021 1.00 53.33  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.702  -15.975 36.555 1.00 58.01  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.739  -15.802 37.291 1.00 58.32  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.914  -14.311 34.661 1.00 56.59  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.155  -17.198 36.216 1.00 53.50  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.534  -18.444 36.677 1.00 55.11  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.704  -18.670 38.190 1.00 61.67  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.837  -19.280 38.802 1.00 62.24  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.102  -19.628 35.907 1.00 54.35  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.824  -18.212 38.776 1.00 60.77  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.125  -18.414 40.196 1.00 63.78  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.510  -17.369 41.143 1.00 72.39  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.446  -17.625 42.349 1.00 74.83  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.632 -18.515 40.416 1.00 67.12  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 11.092 -19.839 40.192 1.00 76.73  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.033  -16.219 40.612 1.00 69.22  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.432  -15.151 41.424 1.00 88.16  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 5.998  -15.463 41.886 1.00 133.24 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.614  -16.623 42.033 1.00 100.87 ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.508  -13.787 40.707 1.00 88.73  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.483  -13.580 39.600 1.00 99.04  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.639  -12.343 38.734 1.00 120.85 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.770  -11.814 38.624 1.00 115.04 ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.621  -11.912 38.145 1.00 114.53 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.251 -35.157 5.835  1.00 32.08  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.344 -34.025 6.324  1.00 33.21  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.447 -36.396 6.709  1.00 32.12  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.972 -35.384 4.552  0.66 29.27  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.985 -35.387 4.548  0.34 30.67  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.763 -34.320 3.567  0.66 28.35  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.720 -34.311 3.594  0.34 30.49  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.258 -34.170 3.282  0.66 33.14  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.216 -34.149 3.427  0.34 33.33  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.550 -35.177 3.211  0.66 33.33  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.471 -35.126 3.547  0.34 32.83  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.548 -34.638 2.271  0.66 27.08  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.401 -34.553 2.221  0.34 29.87  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.050 -34.618 2.453  0.66 27.07  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.778 -35.621 1.369  0.34 31.23  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.842 -35.649 2.872  0.66 29.44  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.147 -36.931 1.303  0.34 34.39  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.927 -33.500 2.241  0.66 26.72  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.697 -35.460 0.435  0.34 31.24  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.149 -35.223 2.993  0.66 28.36  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.341 -37.607 0.418  0.34 34.14  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.237 -33.926 2.562  0.66 29.48  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.444 -36.728 -0.134 0.34 35.38  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.730 -32.169 1.838  0.66 27.35  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.889 -34.374 0.054  0.34 32.22  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.350 -33.086 2.434  0.66 29.06  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.426 -36.938 -1.073 0.34 34.75  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.837 -31.352 1.675  0.66 28.32  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.879 -34.584 -0.872 0.34 33.85  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.122 -31.799 2.003  0.66 29.02  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.660 -35.851 -1.431 0.34 34.50  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.768 -32.926 3.128  1.00 28.90  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.338 -32.629 2.895  1.00 28.28  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.190 -31.572 1.788  1.00 30.96  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.161 -30.885 1.447  1.00 30.03  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.632 -32.125 4.208  1.00 31.43  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.664 -33.181 5.320  1.00 31.29  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.226 -30.789 4.707  1.00 30.85  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.950 -31.380 1.330  1.00 28.83  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.567 -30.299 0.435  1.00 28.85  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.191 -29.158 1.421  1.00 33.00  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.176 -29.281 2.129  1.00 33.07  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.349 -30.673 -0.463 1.00 31.24  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.629 -31.954 -1.336 1.00 29.64  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.931 -29.442 -1.314 1.00 32.68  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.919 -31.867 -2.329 1.00 34.46  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.984 -28.064 1.501  1.00 32.05  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.664 -27.002 2.473  1.00 32.62  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.403 -26.217 2.109  1.00 36.76  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.091 -26.077 0.930  1.00 35.17  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.920 -26.120 2.459  1.00 34.35  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.476 -26.298 1.053  1.00 38.21  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.230 -27.761 0.755  1.00 33.90  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.724 -25.648 3.116  1.00 35.77  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.519 -10.161 16.502 1.00 30.36  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.931 -8.891  16.540 1.00 29.42  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.907 -8.606  17.437 1.00 32.18  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.461 -9.619  18.281 1.00 32.68  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.283 -10.799 19.844 1.00 36.53  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.997 -10.902 18.218 1.00 31.50  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.312 -10.266 11.940 1.00 32.51  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.454 -10.592 13.277 1.00 29.93  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.422 -10.247 14.174 1.00 31.19  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.274 -11.758 19.217 1.00 34.21  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.452 -11.059 20.712 1.00 36.19  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.459 -9.584  19.258 1.00 33.36  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 25.024 -11.180 17.322 1.00 29.07  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.422 -10.566 15.496 1.00 28.62  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.329 -9.633  13.686 1.00 33.57  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.315 -9.383  12.389 1.00 35.19  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.870 -8.611  11.809 0.40 35.24  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 29.001 -11.503 13.847 0.62 27.45  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.225 -9.644  11.468 1.00 35.80  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.399 -15.393 22.714 1.00 42.92  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.537 -35.441 -1.266 0.66 50.31  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.257 -35.222 -0.611 0.66 51.82  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.674 -34.533 -0.253 0.66 49.23  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 17.974 -37.073 -0.775 0.66 49.80  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 25.923 -3.540  26.526 1.00 38.36  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 35.797 -25.866 25.568 1.00 42.08  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 37.730 -20.495 26.995 1.00 38.36  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 38.534 -15.017 15.562 1.00 41.06  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 20.790 -5.948  26.317 1.00 44.92  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 29.875 -32.317 9.582  1.00 54.03  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 37.864 2.418   19.785 1.00 43.28  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 26.804 -32.153 16.178 1.00 49.43  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 41.200 -21.717 25.199 1.00 48.19  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 44.459 -0.898  17.990 1.00 58.77  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 22.687 -5.488  20.047 1.00 58.54  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 17.915 -29.515 7.704  1.00 38.50  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 33.436 -20.931 29.623 1.00 51.24  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 22.706 -27.765 17.822 1.00 54.19  ? 314 HOH   A O   1 
HETATM 1215 O  O   A HOH   F 6 .   ? 19.085 -23.024 4.320  0.67 51.70  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 45.083 -11.213 18.864 1.00 69.48  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 43.708 -6.612  32.017 1.00 54.59  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 16.478 -27.551 -3.294 1.00 53.39  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 37.304 -12.554 40.386 1.00 67.99  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 15.450 -10.099 25.007 1.00 53.15  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 23.454 -5.888  33.012 1.00 40.15  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 21.471 -27.245 14.684 0.50 45.33  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 31.763 -0.981  15.908 1.00 49.11  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 30.370 1.348   33.915 1.00 75.05  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 21.698 -29.628 -5.249 1.00 42.19  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 28.360 -8.931  40.075 1.00 50.45  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 20.462 -13.586 20.589 1.00 56.87  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 27.289 -10.287 35.968 1.00 41.50  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 32.788 -24.580 32.293 1.00 70.66  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 19.896 -9.713  37.143 1.00 45.48  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 41.344 -16.926 15.270 1.00 42.38  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 25.698 -2.925  20.140 1.00 60.56  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 28.945 -21.846 41.752 1.00 82.76  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 36.904 -5.746  12.306 1.00 42.40  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 27.348 -28.275 18.677 1.00 31.74  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 28.324 -23.869 31.765 1.00 44.65  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 22.960 -28.304 12.692 1.00 26.81  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 41.420 -12.844 14.155 1.00 111.23 ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 26.189 -21.888 38.753 1.00 45.33  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 26.979 -35.402 11.619 1.00 61.40  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 30.405 -0.697  37.081 1.00 61.29  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 34.517 -24.001 29.825 1.00 81.97  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 21.513 -29.995 14.237 1.00 78.85  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 24.936 -26.902 19.086 1.00 38.46  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 26.912 -16.715 38.775 1.00 58.01  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 43.969 -4.387  25.874 1.00 51.96  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 23.448 -17.263 44.419 1.00 68.06  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 23.992 -15.863 21.345 1.00 36.69  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 29.456 -27.501 20.707 1.00 28.15  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 29.012 -0.429  16.958 1.00 81.32  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 12.696 -20.763 42.561 1.00 63.10  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 20.858 -7.411  19.923 1.00 57.47  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 41.126 -1.416  11.688 1.00 71.17  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 10.748 -11.534 34.523 1.00 53.87  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 21.957 -25.060 18.384 1.00 26.76  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 44.379 -12.779 41.418 1.00 57.31  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 46.895 -21.592 18.174 1.00 52.82  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 29.143 -31.225 7.271  1.00 39.27  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 37.394 -6.491  34.419 1.00 44.43  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 42.533 -10.557 15.582 1.00 57.93  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 46.075 -14.246 21.606 1.00 61.16  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 30.741 -29.043 22.698 1.00 45.29  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 39.101 -18.970 33.437 1.00 52.58  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 26.169 -22.731 30.004 1.00 32.17  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 20.292 -16.047 41.010 1.00 39.84  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 28.559 -24.406 34.445 1.00 59.94  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 18.073 -34.615 8.329  1.00 37.36  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 34.187 -8.027  35.786 1.00 39.85  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 12.229 -18.101 25.880 1.00 62.25  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 34.830 -19.029 13.905 0.50 28.20  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 37.660 3.277   15.878 1.00 47.98  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 46.304 -15.949 27.638 1.00 79.70  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 22.647 -34.064 8.875  1.00 38.28  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 21.058 -23.486 6.168  1.00 59.39  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 31.913 -31.920 14.588 1.00 41.71  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 46.409 -18.947 19.688 1.00 57.65  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 41.264 -7.036  36.025 1.00 46.64  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 27.150 -2.408  16.184 1.00 67.46  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 43.909 -10.726 35.156 1.00 74.48  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 45.364 -12.672 23.677 1.00 53.25  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 26.234 -8.093  9.060  1.00 49.06  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 26.398 -30.857 19.032 1.00 67.47  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 41.396 -7.807  46.569 1.00 62.92  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 11.638 -15.315 40.649 1.00 83.71  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 26.035 -19.259 41.718 1.00 69.46  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 14.356 -16.902 23.520 1.00 49.14  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 47.246 -25.217 21.576 1.00 58.11  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 45.582 -10.900 30.335 1.00 61.66  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 16.713 -6.562  27.581 1.00 65.86  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 27.743 -23.121 13.905 0.50 31.86  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 23.715 -15.750 17.834 1.00 47.62  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 38.063 -16.708 13.150 0.50 31.33  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 34.783 -29.187 26.093 1.00 68.48  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 19.841 -25.562 41.300 1.00 79.66  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 44.672 -8.718  17.883 1.00 70.58  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 4.263  -20.370 37.908 1.00 64.79  ? 396 HOH   A O   1 
HETATM 1297 O  O   A HOH   F 6 .   ? 12.084 -20.683 27.939 0.66 49.89  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 33.154 -29.849 21.553 1.00 45.13  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 17.388 -24.602 -2.129 1.00 74.69  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 44.673 -16.467 29.762 1.00 57.59  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 29.679 -22.708 36.905 1.00 68.37  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 25.689 -4.598  18.029 1.00 53.63  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 40.513 -19.697 29.103 1.00 40.33  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 42.131 -5.935  11.905 1.00 77.43  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 46.976 -20.247 21.978 1.00 72.63  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 47.482 -6.743  20.377 1.00 71.48  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 45.932 -17.167 17.402 1.00 72.04  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 21.133 -23.309 42.163 1.00 52.64  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 22.929 -15.006 40.495 1.00 38.07  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 30.409 -10.642 40.684 1.00 48.08  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 41.356 -17.120 35.271 1.00 49.48  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 46.182 -8.986  44.263 1.00 55.00  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 35.277 1.861   13.571 1.00 58.38  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 42.108 -8.161  13.893 1.00 63.74  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 35.195 -29.925 23.513 1.00 49.49  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 32.170 -15.719 39.934 1.00 41.55  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 32.441 -9.070  39.836 1.00 63.46  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 27.367 -25.571 28.431 1.00 60.47  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 27.145 -1.676  22.071 1.00 56.16  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 19.659 -27.362 10.096 1.00 56.90  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 33.548 -33.072 12.127 1.00 53.69  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 33.620 -0.344  20.146 1.00 49.28  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 37.215 -2.348  11.562 1.00 68.83  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 10.525 -11.732 40.142 1.00 67.83  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 34.034 -32.950 21.977 1.00 71.73  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 34.476 -18.812 36.397 1.00 69.75  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 25.742 -16.191 41.195 1.00 55.36  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 29.637 -0.801  22.364 1.00 63.33  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 31.815 -26.038 27.137 1.00 60.10  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 37.347 -31.573 23.415 1.00 92.73  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 39.938 -5.571  34.031 1.00 46.83  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 23.534 -30.570 19.367 1.00 71.51  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 42.880 -18.305 30.743 1.00 56.91  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 26.448 -29.524 22.744 1.00 61.70  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 45.929 -5.583  23.874 1.00 55.70  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 22.323 -10.597 14.674 1.00 52.39  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 44.457 -4.237  28.997 1.00 67.73  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 31.973 -0.013  13.360 1.00 68.79  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 26.941 -34.572 17.991 1.00 68.84  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 30.540 -34.337 14.904 1.00 68.68  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 23.236 -3.101  26.779 1.00 69.71  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 19.516 -31.802 13.853 1.00 72.63  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 35.421 -4.191  10.712 1.00 53.45  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 28.755 -2.651  13.080 1.00 83.51  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 19.795 -8.164  24.689 1.00 56.43  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 36.892 -24.555 27.687 1.00 65.95  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 48.110 -23.440 19.736 1.00 68.55  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 47.456 -28.523 17.654 1.00 63.54  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 46.780 -14.729 18.316 1.00 70.53  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 24.564 -21.866 41.168 1.00 66.64  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 47.087 -12.562 28.572 1.00 67.74  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 32.288 -1.151  22.376 1.00 66.15  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 43.994 -13.739 13.905 0.50 86.35  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 11.960 -18.864 22.804 1.00 69.13  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 34.123 -17.705 39.688 1.00 70.59  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 25.357 -5.736  34.965 1.00 65.61  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 19.473 -7.727  35.355 1.00 58.26  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 47.286 -11.963 25.472 1.00 74.96  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 35.873 -21.349 30.779 1.00 66.46  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 45.633 -8.425  31.400 1.00 70.36  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 20.090 -35.331 10.165 1.00 45.08  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 17.111 -8.010  25.000 1.00 68.35  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 43.276 -3.048  33.976 1.00 61.95  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 17.123 -28.223 9.940  1.00 55.17  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 33.895 -11.215 41.715 0.50 65.98  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 19.901 -14.880 43.426 1.00 55.44  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 28.366 -29.874 24.658 1.00 74.45  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 19.107 -28.340 13.844 0.50 71.26  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 33.895 -14.062 41.715 0.50 46.41  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 32.668 -20.783 36.942 1.00 80.01  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 32.006 -23.922 35.063 1.00 78.48  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 21.293 -5.775  34.774 1.00 57.33  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 16.761 -6.910  35.031 1.00 87.06  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 12.483 -18.338 20.047 1.00 68.59  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 45.222 -12.395 15.940 1.00 77.92  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   F 6 .   ? 39.465 -5.504  11.459 1.00 71.35  ? 476 HOH   A O   1 
HETATM 1377 O  O   . HOH   F 6 .   ? 16.705 -30.321 12.485 1.00 61.81  ? 477 HOH   A O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 12.209 -24.336 0.076  1.00 58.85  ? 201 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 14.972 -25.862 -1.807 1.00 49.19  ? 202 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 17.740 -36.371 6.055  1.00 47.94  ? 203 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 20.860 -38.353 4.028  1.00 51.47  ? 204 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 11.505 -23.599 3.110  1.00 60.86  ? 205 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 20.876 -39.515 -2.035 1.00 64.69  ? 206 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 10.725 -24.754 5.503  1.00 59.88  ? 207 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.664 -36.544 9.959  1.00 52.42  ? 208 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   ? 0.8621 1.0388 0.7615 0.0333  -0.1399 -0.0204 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8581 1.0288 0.7387 0.0166  -0.1307 -0.0230 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8333 1.0348 0.7388 0.0049  -0.1260 -0.0402 6   ASP A C   
4    O O   . ASP A 5   ? 0.8244 1.0524 0.7597 0.0091  -0.1305 -0.0500 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8808 1.0223 0.7519 0.0077  -0.1128 -0.0163 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0800 1.2011 0.9156 -0.0029 -0.1076 -0.0114 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0810 1.2147 0.9141 -0.0146 -0.1045 -0.0208 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1910 1.2828 1.0012 -0.0007 -0.1054 0.0007  6   ASP A OD2 
9    N N   . SER A 6   ? 0.7279 0.9252 0.6209 -0.0104 -0.1163 -0.0448 7   SER A N   
10   C CA  . SER A 6   ? 0.6785 0.8983 0.5907 -0.0231 -0.1095 -0.0607 7   SER A CA  
11   C C   . SER A 6   ? 0.6220 0.8286 0.5468 -0.0336 -0.0898 -0.0635 7   SER A C   
12   O O   . SER A 6   ? 0.6080 0.8200 0.5371 -0.0462 -0.0808 -0.0738 7   SER A O   
13   C CB  . SER A 6   ? 0.7502 0.9765 0.6396 -0.0319 -0.1141 -0.0657 7   SER A CB  
14   O OG  . SER A 6   ? 0.9080 1.1071 0.7673 -0.0387 -0.1060 -0.0578 7   SER A OG  
15   N N   . CYS A 7   ? 0.5155 0.7043 0.4459 -0.0278 -0.0839 -0.0547 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4792 0.6546 0.4201 -0.0351 -0.0680 -0.0561 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4609 0.6522 0.4291 -0.0412 -0.0617 -0.0685 8   CYS A C   
18   O O   . CYS A 7   ? 0.4521 0.6650 0.4365 -0.0379 -0.0685 -0.0750 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4965 0.6522 0.4370 -0.0269 -0.0653 -0.0446 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5849 0.7126 0.4913 -0.0252 -0.0652 -0.0310 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3521 0.5320 0.3247 -0.0500 -0.0486 -0.0723 9   ILE A N   
22   C CA  . ILE A 8   ? 0.3100 0.4937 0.3032 -0.0558 -0.0401 -0.0811 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3363 0.5012 0.3341 -0.0507 -0.0342 -0.0727 9   ILE A C   
24   O O   . ILE A 8   ? 0.3344 0.4835 0.3198 -0.0465 -0.0338 -0.0631 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3505 0.5339 0.3449 -0.0684 -0.0310 -0.0923 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3639 0.5268 0.3451 -0.0712 -0.0235 -0.0888 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3571 0.5634 0.3500 -0.0742 -0.0373 -0.1028 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.4353 0.5936 0.4192 -0.0817 -0.0137 -0.0998 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2732 0.4384 0.2870 -0.0526 -0.0286 -0.0769 10  GLN A N   
30   N N   B GLN A 9   ? 0.2825 0.4499 0.2970 -0.0517 -0.0298 -0.0768 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2683 0.4159 0.2848 -0.0483 -0.0235 -0.0694 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2731 0.4245 0.2916 -0.0474 -0.0249 -0.0698 10  GLN A CA  
33   C C   A GLN A 9   ? 0.3034 0.4383 0.3252 -0.0558 -0.0130 -0.0743 10  GLN A C   
34   C C   B GLN A 9   ? 0.3188 0.4570 0.3419 -0.0552 -0.0141 -0.0745 10  GLN A C   
35   O O   A GLN A 9   ? 0.3022 0.4454 0.3323 -0.0633 -0.0093 -0.0840 10  GLN A O   
36   O O   B GLN A 9   ? 0.3152 0.4609 0.3460 -0.0631 -0.0100 -0.0845 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2859 0.4427 0.3131 -0.0401 -0.0287 -0.0667 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2826 0.4462 0.3140 -0.0404 -0.0298 -0.0694 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.3551 0.4962 0.3872 -0.0382 -0.0219 -0.0621 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3259 0.4730 0.3565 -0.0334 -0.0276 -0.0597 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.6182 0.7616 0.6553 -0.0281 -0.0268 -0.0563 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4758 0.6256 0.5217 -0.0348 -0.0221 -0.0642 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.5438 0.6992 0.5809 -0.0203 -0.0364 -0.0546 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3413 0.5115 0.4020 -0.0361 -0.0237 -0.0732 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.5712 0.7015 0.6115 -0.0276 -0.0205 -0.0532 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.4355 0.5655 0.4780 -0.0351 -0.0154 -0.0590 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2900 0.4042 0.3060 -0.0538 -0.0084 -0.0679 11  PHE A N   
48   N N   B PHE A 10  ? 0.2908 0.4083 0.3080 -0.0528 -0.0098 -0.0676 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2735 0.3713 0.2912 -0.0586 -0.0003 -0.0707 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2839 0.3843 0.3020 -0.0576 -0.0015 -0.0699 11  PHE A CA  
51   C C   A PHE A 10  ? 0.3001 0.3919 0.3228 -0.0561 0.0016  -0.0670 11  PHE A C   
52   C C   B PHE A 10  ? 0.3123 0.4069 0.3358 -0.0553 0.0007  -0.0667 11  PHE A C   
53   O O   A PHE A 10  ? 0.2722 0.3548 0.2916 -0.0496 0.0002  -0.0587 11  PHE A O   
54   O O   B PHE A 10  ? 0.3012 0.3895 0.3225 -0.0484 -0.0016 -0.0585 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2930 0.3738 0.3029 -0.0574 0.0024  -0.0679 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.3094 0.3938 0.3190 -0.0556 0.0004  -0.0660 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.3124 0.3753 0.3219 -0.0611 0.0088  -0.0716 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3395 0.4276 0.3450 -0.0605 0.0017  -0.0725 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3520 0.4145 0.3621 -0.0690 0.0133  -0.0809 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3825 0.4859 0.3831 -0.0613 -0.0032 -0.0736 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3248 0.3693 0.3314 -0.0566 0.0099  -0.0659 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3855 0.4603 0.3907 -0.0639 0.0074  -0.0777 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3702 0.4107 0.3765 -0.0718 0.0191  -0.0835 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3997 0.5064 0.3949 -0.0671 -0.0011 -0.0805 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3574 0.3818 0.3601 -0.0586 0.0143  -0.0682 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.4290 0.5074 0.4314 -0.0686 0.0096  -0.0852 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3441 0.3648 0.3458 -0.0659 0.0190  -0.0765 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3997 0.4947 0.3972 -0.0710 0.0059  -0.0869 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2622 0.3599 0.2925 -0.0624 0.0058  -0.0743 12  THR A N   
70   C CA  . THR A 11  ? 0.2694 0.3637 0.3050 -0.0626 0.0095  -0.0735 12  THR A CA  
71   C C   . THR A 11  ? 0.3195 0.3890 0.3457 -0.0595 0.0125  -0.0652 12  THR A C   
72   O O   . THR A 11  ? 0.3136 0.3828 0.3418 -0.0543 0.0112  -0.0601 12  THR A O   
73   C CB  . THR A 11  ? 0.3799 0.4789 0.4218 -0.0738 0.0172  -0.0848 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3935 0.5195 0.4461 -0.0763 0.0131  -0.0937 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.4209 0.5193 0.4689 -0.0758 0.0225  -0.0862 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2991 0.3484 0.3153 -0.0620 0.0157  -0.0645 13  ARG A N   
77   C CA  . ARG A 12  ? 0.3170 0.3431 0.3235 -0.0587 0.0169  -0.0577 13  ARG A CA  
78   C C   . ARG A 12  ? 0.3331 0.3575 0.3375 -0.0499 0.0111  -0.0502 13  ARG A C   
79   O O   . ARG A 12  ? 0.3269 0.3351 0.3247 -0.0467 0.0108  -0.0455 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3871 0.3906 0.3834 -0.0635 0.0214  -0.0603 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.5341 0.5302 0.5271 -0.0746 0.0299  -0.0672 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.8163 0.8041 0.8050 -0.0776 0.0344  -0.0650 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.9977 0.9577 0.9703 -0.0737 0.0334  -0.0571 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.1387 1.0906 1.1052 -0.0736 0.0350  -0.0528 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 1.0083 0.9352 0.9585 -0.0698 0.0326  -0.0461 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8805 0.8500 0.8576 -0.0767 0.0384  -0.0560 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2775 0.3176 0.2859 -0.0466 0.0067  -0.0497 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2773 0.3146 0.2824 -0.0409 0.0034  -0.0443 14  HIS A CA  
89   C C   . HIS A 13  ? 0.3077 0.3379 0.3111 -0.0363 0.0026  -0.0375 14  HIS A C   
90   O O   . HIS A 13  ? 0.2951 0.3149 0.2950 -0.0338 0.0022  -0.0352 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2758 0.3279 0.2807 -0.0399 -0.0001 -0.0443 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.3012 0.3491 0.3013 -0.0366 -0.0011 -0.0402 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.3031 0.3457 0.3028 -0.0376 0.0009  -0.0437 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.3037 0.3522 0.2997 -0.0331 -0.0030 -0.0341 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.3004 0.3428 0.2970 -0.0358 0.0008  -0.0407 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2959 0.3398 0.2886 -0.0336 -0.0012 -0.0344 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2588 0.2961 0.2658 -0.0349 0.0022  -0.0355 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2694 0.2996 0.2748 -0.0310 0.0023  -0.0299 15  ALA A CA  
99   C C   . ALA A 14  ? 0.3047 0.3183 0.3047 -0.0330 0.0054  -0.0294 15  ALA A C   
100  O O   . ALA A 14  ? 0.2874 0.2923 0.2831 -0.0304 0.0044  -0.0257 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2803 0.3208 0.2924 -0.0286 0.0018  -0.0297 15  ALA A CB  
102  N N   A SER A 15  ? 0.2990 0.3073 0.2975 -0.0384 0.0090  -0.0335 16  SER A N   
103  N N   B SER A 15  ? 0.2901 0.2984 0.2886 -0.0384 0.0090  -0.0335 16  SER A N   
104  N N   C SER A 15  ? 0.2919 0.3001 0.2904 -0.0384 0.0091  -0.0335 16  SER A N   
105  C CA  A SER A 15  ? 0.3063 0.2948 0.2946 -0.0410 0.0117  -0.0325 16  SER A CA  
106  C CA  B SER A 15  ? 0.2971 0.2856 0.2853 -0.0411 0.0117  -0.0326 16  SER A CA  
107  C CA  C SER A 15  ? 0.3004 0.2888 0.2886 -0.0409 0.0116  -0.0324 16  SER A CA  
108  C C   A SER A 15  ? 0.3519 0.3284 0.3337 -0.0374 0.0077  -0.0309 16  SER A C   
109  C C   B SER A 15  ? 0.3527 0.3289 0.3343 -0.0375 0.0077  -0.0309 16  SER A C   
110  C C   C SER A 15  ? 0.3549 0.3309 0.3364 -0.0375 0.0077  -0.0309 16  SER A C   
111  O O   A SER A 15  ? 0.3240 0.2877 0.2981 -0.0348 0.0056  -0.0275 16  SER A O   
112  O O   B SER A 15  ? 0.3347 0.2977 0.3084 -0.0351 0.0058  -0.0276 16  SER A O   
113  O O   C SER A 15  ? 0.3382 0.3009 0.3118 -0.0350 0.0057  -0.0276 16  SER A O   
114  C CB  A SER A 15  ? 0.3670 0.3501 0.3523 -0.0492 0.0177  -0.0379 16  SER A CB  
115  C CB  B SER A 15  ? 0.3471 0.3304 0.3325 -0.0493 0.0178  -0.0380 16  SER A CB  
116  C CB  C SER A 15  ? 0.3571 0.3397 0.3421 -0.0491 0.0179  -0.0374 16  SER A CB  
117  O OG  A SER A 15  ? 0.4516 0.4106 0.4216 -0.0523 0.0204  -0.0359 16  SER A OG  
118  O OG  B SER A 15  ? 0.3847 0.3820 0.3793 -0.0525 0.0217  -0.0415 16  SER A OG  
119  O OG  C SER A 15  ? 0.4227 0.4079 0.4094 -0.0522 0.0184  -0.0423 16  SER A OG  
120  N N   . ASP A 16  ? 0.3216 0.3036 0.3073 -0.0369 0.0062  -0.0343 17  ASP A N   
121  C CA  . ASP A 16  ? 0.3312 0.3053 0.3151 -0.0325 0.0025  -0.0352 17  ASP A CA  
122  C C   . ASP A 16  ? 0.3338 0.3146 0.3217 -0.0273 -0.0013 -0.0326 17  ASP A C   
123  O O   . ASP A 16  ? 0.3332 0.3055 0.3189 -0.0230 -0.0050 -0.0323 17  ASP A O   
124  C CB  . ASP A 16  ? 0.3582 0.3392 0.3471 -0.0342 0.0034  -0.0411 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.5150 0.4851 0.4987 -0.0400 0.0076  -0.0452 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.5060 0.4602 0.4802 -0.0430 0.0102  -0.0432 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.5325 0.5088 0.5202 -0.0427 0.0093  -0.0510 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2738 0.2690 0.2669 -0.0278 -0.0004 -0.0311 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2611 0.2606 0.2561 -0.0250 -0.0019 -0.0291 18  VAL A CA  
130  C C   . VAL A 17  ? 0.3295 0.3188 0.3197 -0.0234 -0.0030 -0.0257 18  VAL A C   
131  O O   . VAL A 17  ? 0.3051 0.2923 0.2958 -0.0208 -0.0058 -0.0267 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2833 0.2939 0.2795 -0.0260 -0.0005 -0.0268 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2823 0.2919 0.2770 -0.0249 0.0000  -0.0240 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2874 0.3076 0.2851 -0.0280 -0.0001 -0.0304 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2940 0.2787 0.2803 -0.0255 -0.0006 -0.0230 19  LEU A N   
136  C CA  . LEU A 18  ? 0.3115 0.2863 0.2914 -0.0254 -0.0005 -0.0203 19  LEU A CA  
137  C C   . LEU A 18  ? 0.3328 0.2926 0.3037 -0.0240 -0.0043 -0.0206 19  LEU A C   
138  O O   . LEU A 18  ? 0.3197 0.2752 0.2871 -0.0217 -0.0078 -0.0198 19  LEU A O   
139  C CB  . LEU A 18  ? 0.3226 0.2966 0.3012 -0.0287 0.0043  -0.0191 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3740 0.3399 0.3466 -0.0295 0.0061  -0.0170 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.3648 0.3367 0.3417 -0.0268 0.0056  -0.0154 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.4114 0.3767 0.3841 -0.0335 0.0122  -0.0183 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.3108 0.2624 0.2776 -0.0249 -0.0043 -0.0223 20  LEU A N   
144  C CA  . LEU A 19  ? 0.3428 0.2760 0.2985 -0.0219 -0.0091 -0.0220 20  LEU A CA  
145  C C   . LEU A 19  ? 0.3718 0.3115 0.3352 -0.0146 -0.0164 -0.0245 20  LEU A C   
146  O O   . LEU A 19  ? 0.3700 0.3008 0.3267 -0.0103 -0.0226 -0.0236 20  LEU A O   
147  C CB  . LEU A 19  ? 0.3799 0.3030 0.3311 -0.0244 -0.0067 -0.0242 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.5010 0.3990 0.4371 -0.0206 -0.0115 -0.0231 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.5495 0.4262 0.4648 -0.0242 -0.0106 -0.0182 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.5642 0.4523 0.4972 -0.0239 -0.0075 -0.0263 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.3130 0.2697 0.2906 -0.0137 -0.0154 -0.0287 21  ASN A N   
152  C CA  . ASN A 20  ? 0.2886 0.2551 0.2765 -0.0083 -0.0203 -0.0336 21  ASN A CA  
153  C C   . ASN A 20  ? 0.3287 0.3032 0.3194 -0.0086 -0.0214 -0.0331 21  ASN A C   
154  O O   . ASN A 20  ? 0.3227 0.3001 0.3177 -0.0038 -0.0275 -0.0369 21  ASN A O   
155  C CB  . ASN A 20  ? 0.3068 0.2877 0.3066 -0.0094 -0.0171 -0.0391 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.4643 0.4371 0.4638 -0.0070 -0.0180 -0.0426 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.4103 0.3657 0.4020 -0.0021 -0.0229 -0.0417 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3705 0.3534 0.3764 -0.0106 -0.0134 -0.0467 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.3087 0.2871 0.2976 -0.0138 -0.0157 -0.0294 22  LEU A N   
160  C CA  . LEU A 21  ? 0.3012 0.2839 0.2909 -0.0152 -0.0153 -0.0292 22  LEU A CA  
161  C C   . LEU A 21  ? 0.3330 0.3034 0.3125 -0.0131 -0.0207 -0.0275 22  LEU A C   
162  O O   . LEU A 21  ? 0.3303 0.3054 0.3124 -0.0118 -0.0245 -0.0306 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2998 0.2843 0.2875 -0.0199 -0.0084 -0.0250 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.3303 0.3251 0.3236 -0.0219 -0.0042 -0.0256 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.3446 0.3376 0.3340 -0.0238 0.0003  -0.0205 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.3528 0.3575 0.3532 -0.0232 -0.0035 -0.0312 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.3123 0.2667 0.2789 -0.0137 -0.0206 -0.0232 23  ASN A N   
168  C CA  . ASN A 22  ? 0.3315 0.2701 0.2829 -0.0126 -0.0256 -0.0209 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3923 0.3274 0.3433 -0.0043 -0.0367 -0.0239 23  ASN A C   
170  O O   . ASN A 22  ? 0.3972 0.3288 0.3417 -0.0015 -0.0437 -0.0244 23  ASN A O   
171  C CB  . ASN A 22  ? 0.3710 0.2914 0.3065 -0.0170 -0.0212 -0.0164 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4801 0.3835 0.3963 -0.0187 -0.0238 -0.0136 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.4385 0.3471 0.3548 -0.0191 -0.0256 -0.0144 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.5097 0.3910 0.4068 -0.0206 -0.0236 -0.0105 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.3614 0.2984 0.3202 0.0003  -0.0387 -0.0269 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3691 0.3047 0.3317 0.0102  -0.0496 -0.0313 24  ARG A CA  
177  C C   . ARG A 23  ? 0.4054 0.3639 0.3857 0.0129  -0.0536 -0.0388 24  ARG A C   
178  O O   . ARG A 23  ? 0.4088 0.3673 0.3891 0.0204  -0.0644 -0.0420 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3660 0.3010 0.3362 0.0136  -0.0485 -0.0345 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.4178 0.3265 0.3689 0.0119  -0.0464 -0.0288 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.4461 0.3570 0.4060 0.0118  -0.0419 -0.0327 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.5403 0.4238 0.4814 0.0100  -0.0400 -0.0288 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.7532 0.6340 0.6963 0.0059  -0.0334 -0.0312 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.5930 0.4973 0.5551 0.0034  -0.0286 -0.0369 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.6642 0.5178 0.5886 0.0031  -0.0308 -0.0284 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.3396 0.3168 0.3336 0.0063  -0.0449 -0.0420 25  LEU A N   
187  C CA  . LEU A 24  ? 0.3314 0.3296 0.3410 0.0055  -0.0456 -0.0500 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3866 0.3814 0.3870 0.0035  -0.0488 -0.0483 25  LEU A C   
189  O O   . LEU A 24  ? 0.3851 0.3915 0.3938 0.0070  -0.0562 -0.0555 25  LEU A O   
190  C CB  . LEU A 24  ? 0.3177 0.3291 0.3362 -0.0029 -0.0341 -0.0517 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.3729 0.3916 0.4011 -0.0029 -0.0300 -0.0555 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.3608 0.3899 0.3926 -0.0118 -0.0194 -0.0565 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.3777 0.4077 0.4217 0.0049  -0.0369 -0.0661 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.3460 0.3266 0.3305 -0.0023 -0.0432 -0.0400 26  ARG A N   
195  C CA  . ARG A 25  ? 0.3635 0.3390 0.3373 -0.0052 -0.0452 -0.0387 26  ARG A CA  
196  C C   . ARG A 25  ? 0.4296 0.3951 0.3922 0.0027  -0.0591 -0.0390 26  ARG A C   
197  O O   . ARG A 25  ? 0.4307 0.4049 0.3955 0.0037  -0.0657 -0.0442 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3812 0.3424 0.3405 -0.0122 -0.0363 -0.0309 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.4278 0.3844 0.3764 -0.0160 -0.0373 -0.0311 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.4873 0.4328 0.4254 -0.0230 -0.0273 -0.0259 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.4893 0.4174 0.4129 -0.0230 -0.0265 -0.0203 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.6439 0.5555 0.5482 -0.0271 -0.0250 -0.0174 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.5415 0.4518 0.4383 -0.0305 -0.0257 -0.0193 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.5143 0.4100 0.4057 -0.0290 -0.0220 -0.0134 26  ARG A NH2 
205  N N   A SER A 26  ? 0.4145 0.3606 0.3637 0.0079  -0.0635 -0.0337 27  SER A N   
206  N N   B SER A 26  ? 0.4124 0.3587 0.3620 0.0080  -0.0635 -0.0337 27  SER A N   
207  N N   C SER A 26  ? 0.4178 0.3640 0.3672 0.0080  -0.0635 -0.0337 27  SER A N   
208  C CA  A SER A 26  ? 0.4419 0.3714 0.3746 0.0165  -0.0773 -0.0319 27  SER A CA  
209  C CA  B SER A 26  ? 0.4398 0.3689 0.3729 0.0168  -0.0771 -0.0318 27  SER A CA  
210  C CA  C SER A 26  ? 0.4475 0.3769 0.3803 0.0165  -0.0772 -0.0318 27  SER A CA  
211  C C   A SER A 26  ? 0.5073 0.4541 0.4571 0.0275  -0.0907 -0.0411 27  SER A C   
212  C C   B SER A 26  ? 0.5041 0.4509 0.4539 0.0274  -0.0904 -0.0411 27  SER A C   
213  C C   C SER A 26  ? 0.5086 0.4553 0.4583 0.0275  -0.0906 -0.0411 27  SER A C   
214  O O   A SER A 26  ? 0.5240 0.4656 0.4635 0.0340  -0.1037 -0.0419 27  SER A O   
215  O O   B SER A 26  ? 0.5198 0.4614 0.4591 0.0335  -0.1032 -0.0418 27  SER A O   
216  O O   C SER A 26  ? 0.5249 0.4661 0.4641 0.0339  -0.1036 -0.0418 27  SER A O   
217  C CB  A SER A 26  ? 0.4975 0.4005 0.4126 0.0190  -0.0772 -0.0248 27  SER A CB  
218  C CB  B SER A 26  ? 0.4936 0.4000 0.4140 0.0203  -0.0772 -0.0261 27  SER A CB  
219  C CB  C SER A 26  ? 0.5114 0.4154 0.4281 0.0193  -0.0770 -0.0251 27  SER A CB  
220  O OG  A SER A 26  ? 0.5562 0.4660 0.4875 0.0248  -0.0775 -0.0286 27  SER A OG  
221  O OG  B SER A 26  ? 0.5884 0.4749 0.4886 0.0112  -0.0676 -0.0184 27  SER A OG  
222  O OG  C SER A 26  ? 0.6526 0.5339 0.5476 0.0276  -0.0903 -0.0217 27  SER A OG  
223  N N   . ARG A 27  ? 0.4441 0.4126 0.4200 0.0294  -0.0875 -0.0491 28  ARG A N   
224  C CA  . ARG A 27  ? 0.4497 0.4397 0.4477 0.0392  -0.0981 -0.0609 28  ARG A CA  
225  C C   . ARG A 27  ? 0.4729 0.4922 0.4908 0.0321  -0.0938 -0.0710 28  ARG A C   
226  O O   . ARG A 27  ? 0.4800 0.5229 0.5207 0.0376  -0.1001 -0.0836 28  ARG A O   
227  C CB  . ARG A 27  ? 0.4607 0.4551 0.4743 0.0448  -0.0962 -0.0650 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.5592 0.5225 0.5524 0.0514  -0.1002 -0.0561 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.6033 0.5696 0.6103 0.0539  -0.0948 -0.0601 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.7702 0.7593 0.8041 0.0642  -0.1024 -0.0736 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.9572 0.9641 1.0131 0.0626  -0.0947 -0.0825 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.7931 0.8225 0.8751 0.0716  -0.1011 -0.0966 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.7796 0.7837 0.8322 0.0518  -0.0806 -0.0784 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.4020 0.4193 0.4117 0.0196  -0.0826 -0.0666 29  ASP A N   
235  C CA  . ASP A 28  ? 0.4001 0.4383 0.4229 0.0102  -0.0756 -0.0747 29  ASP A CA  
236  C C   . ASP A 28  ? 0.4364 0.4975 0.4843 0.0064  -0.0669 -0.0847 29  ASP A C   
237  O O   . ASP A 28  ? 0.4420 0.5261 0.5075 0.0025  -0.0659 -0.0970 29  ASP A O   
238  C CB  . ASP A 28  ? 0.4386 0.4873 0.4627 0.0136  -0.0882 -0.0823 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.5721 0.6352 0.6022 0.0012  -0.0796 -0.0888 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.5667 0.6183 0.5863 -0.0091 -0.0661 -0.0818 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.6293 0.7152 0.6751 0.0020  -0.0864 -0.1017 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.3454 0.4000 0.3936 0.0062  -0.0600 -0.0802 30  ILE A N   
243  C CA  . ILE A 29  ? 0.3287 0.4013 0.3959 0.0020  -0.0511 -0.0887 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3635 0.4343 0.4252 -0.0114 -0.0357 -0.0849 30  ILE A C   
245  O O   . ILE A 29  ? 0.3302 0.3831 0.3757 -0.0140 -0.0306 -0.0732 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3672 0.4352 0.4383 0.0095  -0.0529 -0.0880 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3921 0.4623 0.4713 0.0244  -0.0688 -0.0939 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.3480 0.4316 0.4339 0.0023  -0.0411 -0.0956 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.4484 0.5037 0.5239 0.0326  -0.0713 -0.0902 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.3360 0.4250 0.4109 -0.0198 -0.0284 -0.0955 31  LEU A N   
251  C CA  . LEU A 30  ? 0.3496 0.4352 0.4181 -0.0327 -0.0136 -0.0932 31  LEU A CA  
252  C C   . LEU A 30  ? 0.3770 0.4446 0.4269 -0.0372 -0.0103 -0.0828 31  LEU A C   
253  O O   . LEU A 30  ? 0.3606 0.4182 0.4008 -0.0448 0.0005  -0.0773 31  LEU A O   
254  C CB  . LEU A 30  ? 0.3619 0.4428 0.4273 -0.0351 -0.0056 -0.0891 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.4487 0.5495 0.5327 -0.0365 -0.0024 -0.1024 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.4673 0.5611 0.5432 -0.0410 0.0064  -0.0976 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.5242 0.6429 0.6207 -0.0466 0.0049  -0.1162 31  LEU A CD2 
258  N N   . THR A 31  ? 0.3407 0.4039 0.3854 -0.0326 -0.0194 -0.0812 32  THR A N   
259  C CA  . THR A 31  ? 0.3434 0.3920 0.3726 -0.0377 -0.0155 -0.0745 32  THR A CA  
260  C C   . THR A 31  ? 0.4113 0.4703 0.4471 -0.0490 -0.0065 -0.0839 32  THR A C   
261  O O   . THR A 31  ? 0.4042 0.4840 0.4566 -0.0507 -0.0087 -0.0971 32  THR A O   
262  C CB  . THR A 31  ? 0.4016 0.4440 0.4222 -0.0315 -0.0272 -0.0724 32  THR A CB  
263  O OG1 . THR A 31  ? 0.4205 0.4821 0.4550 -0.0279 -0.0372 -0.0844 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.4007 0.4270 0.4099 -0.0228 -0.0335 -0.0624 32  THR A CG2 
265  N N   . ASP A 32  ? 0.3719 0.4163 0.3957 -0.0569 0.0045  -0.0781 33  ASP A N   
266  C CA  . ASP A 32  ? 0.3684 0.4166 0.3944 -0.0692 0.0157  -0.0860 33  ASP A CA  
267  C C   . ASP A 32  ? 0.4095 0.4444 0.4238 -0.0752 0.0206  -0.0840 33  ASP A C   
268  O O   . ASP A 32  ? 0.4122 0.4432 0.4238 -0.0861 0.0320  -0.0883 33  ASP A O   
269  C CB  . ASP A 32  ? 0.3905 0.4310 0.4118 -0.0746 0.0273  -0.0823 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.5321 0.5516 0.5382 -0.0692 0.0287  -0.0670 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.4709 0.4803 0.4699 -0.0636 0.0238  -0.0598 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.6748 0.6888 0.6759 -0.0711 0.0345  -0.0632 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.3501 0.3762 0.3558 -0.0692 0.0132  -0.0779 34  VAL A N   
274  C CA  . VAL A 33  ? 0.3444 0.3584 0.3391 -0.0750 0.0180  -0.0774 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3924 0.4061 0.3813 -0.0693 0.0065  -0.0764 34  VAL A C   
276  O O   . VAL A 33  ? 0.3843 0.3967 0.3712 -0.0599 -0.0028 -0.0706 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3814 0.3717 0.3628 -0.0764 0.0289  -0.0665 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.3616 0.3417 0.3364 -0.0666 0.0238  -0.0552 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3989 0.3765 0.3714 -0.0848 0.0376  -0.0690 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3628 0.3754 0.3464 -0.0760 0.0080  -0.0821 35  VAL A N   
281  N N   B VAL A 34  ? 0.3550 0.3677 0.3386 -0.0759 0.0077  -0.0821 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3681 0.3762 0.3404 -0.0734 -0.0009 -0.0813 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.3565 0.3644 0.3287 -0.0726 -0.0015 -0.0806 35  VAL A CA  
284  C C   A VAL A 34  ? 0.4071 0.3940 0.3651 -0.0787 0.0102  -0.0757 35  VAL A C   
285  C C   B VAL A 34  ? 0.4087 0.3967 0.3664 -0.0788 0.0091  -0.0764 35  VAL A C   
286  O O   A VAL A 34  ? 0.4083 0.3907 0.3670 -0.0874 0.0218  -0.0796 35  VAL A O   
287  O O   B VAL A 34  ? 0.4147 0.4000 0.3733 -0.0881 0.0197  -0.0818 35  VAL A O   
288  C CB  A VAL A 34  ? 0.4301 0.4573 0.4087 -0.0772 -0.0092 -0.0947 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.4103 0.4376 0.3883 -0.0723 -0.0142 -0.0921 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.4398 0.4590 0.4013 -0.0753 -0.0184 -0.0932 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.4100 0.4491 0.3956 -0.0845 -0.0071 -0.1053 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.4256 0.4763 0.4224 -0.0705 -0.0202 -0.1023 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.4206 0.4380 0.3808 -0.0675 -0.0253 -0.0879 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.3675 0.3406 0.3127 -0.0739 0.0077  -0.0673 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3720 0.3271 0.3053 -0.0781 0.0175  -0.0639 36  ILE A CA  
296  C C   . ILE A 35  ? 0.4426 0.3964 0.3629 -0.0820 0.0118  -0.0688 36  ILE A C   
297  O O   . ILE A 35  ? 0.4399 0.3937 0.3515 -0.0768 0.0004  -0.0661 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3946 0.3367 0.3237 -0.0718 0.0208  -0.0534 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3892 0.3344 0.3298 -0.0669 0.0235  -0.0485 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.4197 0.3461 0.3406 -0.0762 0.0319  -0.0527 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.4138 0.3561 0.3596 -0.0720 0.0340  -0.0506 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.4051 0.3561 0.3221 -0.0914 0.0196  -0.0760 37  VAL A N   
303  C CA  . VAL A 36  ? 0.4109 0.3609 0.3139 -0.0970 0.0149  -0.0820 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4924 0.4221 0.3804 -0.1003 0.0246  -0.0782 37  VAL A C   
305  O O   . VAL A 36  ? 0.4689 0.3886 0.3602 -0.1042 0.0384  -0.0787 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4662 0.4293 0.3755 -0.1068 0.0165  -0.0953 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4804 0.4433 0.3736 -0.1127 0.0106  -0.1020 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4571 0.4438 0.3841 -0.1037 0.0072  -0.1013 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.4775 0.4001 0.3480 -0.0988 0.0176  -0.0750 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4865 0.3912 0.3416 -0.1029 0.0267  -0.0728 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5854 0.4876 0.4192 -0.1097 0.0201  -0.0786 38  VAL A C   
312  O O   . VAL A 37  ? 0.5581 0.4580 0.3766 -0.1061 0.0074  -0.0749 38  VAL A O   
313  C CB  . VAL A 37  ? 0.5275 0.4237 0.3797 -0.0959 0.0266  -0.0630 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.5383 0.4194 0.3815 -0.1009 0.0399  -0.0631 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4993 0.4029 0.3722 -0.0878 0.0277  -0.0577 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5959 0.4983 0.4279 -0.1196 0.0275  -0.0881 39  SER A N   
317  N N   B SER A 38  ? 0.5788 0.4798 0.4105 -0.1197 0.0287  -0.0877 39  SER A N   
318  C CA  A SER A 38  ? 0.6236 0.5260 0.4359 -0.1278 0.0216  -0.0958 39  SER A CA  
319  C CA  B SER A 38  ? 0.5998 0.5000 0.4122 -0.1287 0.0244  -0.0958 39  SER A CA  
320  C C   A SER A 38  ? 0.6410 0.5621 0.4550 -0.1229 0.0016  -0.0987 39  SER A C   
321  C C   B SER A 38  ? 0.6307 0.5431 0.4352 -0.1236 0.0033  -0.0961 39  SER A C   
322  O O   A SER A 38  ? 0.6167 0.5557 0.4522 -0.1218 -0.0003 -0.1041 39  SER A O   
323  O O   B SER A 38  ? 0.6384 0.5406 0.4192 -0.1219 -0.0061 -0.0916 39  SER A O   
324  C CB  A SER A 38  ? 0.7134 0.5969 0.4988 -0.1311 0.0236  -0.0920 39  SER A CB  
325  C CB  B SER A 38  ? 0.6706 0.5510 0.4614 -0.1353 0.0341  -0.0952 39  SER A CB  
326  O OG  A SER A 38  ? 0.8999 0.7700 0.6886 -0.1339 0.0414  -0.0905 39  SER A OG  
327  O OG  B SER A 38  ? 0.7516 0.6249 0.5520 -0.1411 0.0525  -0.1001 39  SER A OG  
328  N N   A ARG A 39  ? 0.5976 0.5136 0.3890 -0.1195 -0.0131 -0.0953 40  ARG A N   
329  N N   B ARG A 39  ? 0.5506 0.4840 0.3763 -0.1202 -0.0036 -0.1011 40  ARG A N   
330  C CA  A ARG A 39  ? 0.5939 0.5257 0.3848 -0.1122 -0.0346 -0.0978 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.5457 0.4985 0.3757 -0.1136 -0.0234 -0.1048 40  ARG A CA  
332  C C   A ARG A 39  ? 0.6159 0.5520 0.4191 -0.0981 -0.0443 -0.0891 40  ARG A C   
333  C C   B ARG A 39  ? 0.5722 0.5238 0.4042 -0.0996 -0.0350 -0.0941 40  ARG A C   
334  O O   A ARG A 39  ? 0.6107 0.5613 0.4184 -0.0897 -0.0622 -0.0917 40  ARG A O   
335  O O   B ARG A 39  ? 0.5631 0.5341 0.4102 -0.0921 -0.0480 -0.0978 40  ARG A O   
336  C CB  A ARG A 39  ? 0.6185 0.5383 0.3745 -0.1143 -0.0471 -0.0975 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.5702 0.5257 0.3787 -0.1185 -0.0358 -0.1121 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.7006 0.6251 0.4464 -0.1274 -0.0443 -0.1098 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.6984 0.6625 0.5113 -0.1326 -0.0261 -0.1262 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.7302 0.6452 0.4402 -0.1278 -0.0609 -0.1094 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.7938 0.7713 0.5938 -0.1362 -0.0422 -0.1367 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.7755 0.6920 0.4714 -0.1420 -0.0566 -0.1211 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.8759 0.8621 0.6807 -0.1513 -0.0316 -0.1515 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.9342 0.8749 0.6390 -0.1453 -0.0667 -0.1345 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 1.0436 1.0135 0.8277 -0.1633 -0.0208 -0.1550 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7591 0.6990 0.4488 -0.1595 -0.0615 -0.1453 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.8822 0.8272 0.6395 -0.1625 -0.0184 -0.1451 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.7644 0.7314 0.4948 -0.1351 -0.0813 -0.1387 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.8770 0.8548 0.6668 -0.1772 -0.0109 -0.1695 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.5469 0.4710 0.3557 -0.0951 -0.0331 -0.0798 41  GLU A N   
351  N N   B GLU A 40  ? 0.5288 0.4594 0.3484 -0.0964 -0.0293 -0.0825 41  GLU A N   
352  C CA  A GLU A 40  ? 0.5280 0.4541 0.3470 -0.0831 -0.0404 -0.0719 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.5202 0.4469 0.3411 -0.0845 -0.0378 -0.0727 41  GLU A CA  
354  C C   A GLU A 40  ? 0.5410 0.4840 0.3918 -0.0805 -0.0335 -0.0741 41  GLU A C   
355  C C   B GLU A 40  ? 0.5366 0.4775 0.3878 -0.0801 -0.0318 -0.0725 41  GLU A C   
356  O O   A GLU A 40  ? 0.5170 0.4605 0.3782 -0.0877 -0.0185 -0.0771 41  GLU A O   
357  O O   B GLU A 40  ? 0.5067 0.4451 0.3681 -0.0854 -0.0161 -0.0727 41  GLU A O   
358  C CB  A GLU A 40  ? 0.5527 0.4550 0.3547 -0.0816 -0.0344 -0.0606 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.5507 0.4519 0.3507 -0.0854 -0.0306 -0.0626 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.7841 0.6653 0.5498 -0.0847 -0.0408 -0.0572 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.7469 0.6300 0.5114 -0.0886 -0.0387 -0.0607 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.2516 1.1221 1.0012 -0.0742 -0.0574 -0.0495 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.2010 1.0727 0.9490 -0.0784 -0.0544 -0.0523 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.2441 1.1037 0.9943 -0.0701 -0.0534 -0.0414 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.2237 1.0996 0.9612 -0.0727 -0.0728 -0.0545 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.2651 1.1376 1.0009 -0.0699 -0.0749 -0.0518 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.2075 1.0658 0.9531 -0.0756 -0.0488 -0.0440 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4857 0.4401 0.3498 -0.0701 -0.0444 -0.0724 42  GLN A N   
369  C CA  . GLN A 41  ? 0.4646 0.4343 0.3559 -0.0671 -0.0395 -0.0741 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4956 0.4576 0.3889 -0.0578 -0.0412 -0.0642 42  GLN A C   
371  O O   . GLN A 41  ? 0.5034 0.4573 0.3836 -0.0503 -0.0534 -0.0595 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4856 0.4818 0.3947 -0.0647 -0.0508 -0.0857 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.6774 0.6853 0.5900 -0.0761 -0.0465 -0.0981 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.9113 0.9495 0.8466 -0.0754 -0.0550 -0.1121 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.8079 0.8603 0.7594 -0.0659 -0.0638 -0.1134 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.9311 0.9810 0.8693 -0.0863 -0.0518 -0.1244 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.4118 0.3742 0.3190 -0.0586 -0.0291 -0.0608 43  PHE A N   
378  C CA  . PHE A 42  ? 0.4054 0.3624 0.3163 -0.0512 -0.0291 -0.0526 43  PHE A CA  
379  C C   . PHE A 42  ? 0.4408 0.4139 0.3747 -0.0495 -0.0257 -0.0557 43  PHE A C   
380  O O   . PHE A 42  ? 0.4449 0.4200 0.3865 -0.0557 -0.0140 -0.0575 43  PHE A O   
381  C CB  . PHE A 42  ? 0.4292 0.3687 0.3308 -0.0545 -0.0171 -0.0450 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.4682 0.3905 0.3457 -0.0586 -0.0171 -0.0428 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4961 0.4143 0.3662 -0.0673 -0.0098 -0.0474 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.5122 0.4200 0.3726 -0.0549 -0.0232 -0.0366 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.5320 0.4340 0.3780 -0.0725 -0.0089 -0.0464 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.5669 0.4563 0.4013 -0.0606 -0.0220 -0.0348 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.5414 0.4289 0.3690 -0.0695 -0.0147 -0.0399 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3933 0.3760 0.3366 -0.0412 -0.0354 -0.0565 44  ARG A N   
389  C CA  . ARG A 43  ? 0.3651 0.3632 0.3291 -0.0403 -0.0317 -0.0603 44  ARG A CA  
390  C C   . ARG A 43  ? 0.4131 0.4011 0.3765 -0.0382 -0.0244 -0.0513 44  ARG A C   
391  O O   . ARG A 43  ? 0.4045 0.3792 0.3567 -0.0337 -0.0276 -0.0441 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3857 0.4011 0.3629 -0.0322 -0.0449 -0.0677 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.4691 0.5013 0.4522 -0.0343 -0.0528 -0.0796 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.5697 0.6279 0.5771 -0.0293 -0.0601 -0.0914 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.6855 0.7520 0.7083 -0.0347 -0.0470 -0.0938 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.8510 0.9307 0.8855 -0.0457 -0.0363 -0.1031 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.7599 0.8501 0.7967 -0.0525 -0.0372 -0.1128 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.6206 0.7025 0.6631 -0.0506 -0.0244 -0.1034 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.3680 0.3612 0.3418 -0.0420 -0.0146 -0.0519 45  ALA A N   
400  C CA  . ALA A 44  ? 0.3649 0.3506 0.3381 -0.0398 -0.0088 -0.0440 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3633 0.3582 0.3480 -0.0423 -0.0023 -0.0465 45  ALA A C   
402  O O   . ALA A 44  ? 0.3396 0.3462 0.3329 -0.0471 -0.0005 -0.0548 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3821 0.3523 0.3443 -0.0428 -0.0009 -0.0376 45  ALA A CB  
404  N N   . HIS A 45  ? 0.3287 0.3187 0.3127 -0.0400 0.0013  -0.0400 46  HIS A N   
405  C CA  . HIS A 45  ? 0.3134 0.3077 0.3025 -0.0428 0.0079  -0.0404 46  HIS A CA  
406  C C   . HIS A 45  ? 0.3573 0.3381 0.3376 -0.0462 0.0167  -0.0347 46  HIS A C   
407  O O   . HIS A 45  ? 0.3448 0.3162 0.3195 -0.0426 0.0170  -0.0281 46  HIS A O   
408  C CB  . HIS A 45  ? 0.3114 0.3082 0.3034 -0.0376 0.0052  -0.0370 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.3472 0.3537 0.3473 -0.0326 -0.0035 -0.0422 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.3713 0.3704 0.3660 -0.0268 -0.0108 -0.0387 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.3630 0.3845 0.3755 -0.0327 -0.0058 -0.0513 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.3653 0.3730 0.3682 -0.0219 -0.0183 -0.0447 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.3571 0.3803 0.3730 -0.0247 -0.0159 -0.0531 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.3369 0.3161 0.3161 -0.0531 0.0243  -0.0379 47  LYS A N   
415  C CA  . LYS A 46  ? 0.3494 0.3120 0.3185 -0.0554 0.0327  -0.0324 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3791 0.3351 0.3441 -0.0488 0.0319  -0.0234 47  LYS A C   
417  O O   . LYS A 46  ? 0.3546 0.2995 0.3149 -0.0451 0.0336  -0.0181 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3790 0.3383 0.3447 -0.0646 0.0415  -0.0369 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.4133 0.3773 0.3823 -0.0728 0.0445  -0.0465 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.4159 0.3767 0.3815 -0.0841 0.0552  -0.0524 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.4357 0.4059 0.4076 -0.0931 0.0577  -0.0644 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.4629 0.4319 0.4328 -0.1064 0.0695  -0.0725 47  LYS A NZ  
423  N N   . THR A 47  ? 0.3407 0.3048 0.3087 -0.0472 0.0294  -0.0230 48  THR A N   
424  C CA  . THR A 47  ? 0.3438 0.3039 0.3078 -0.0414 0.0278  -0.0156 48  THR A CA  
425  C C   . THR A 47  ? 0.3554 0.3166 0.3231 -0.0348 0.0229  -0.0124 48  THR A C   
426  O O   . THR A 47  ? 0.3623 0.3173 0.3272 -0.0302 0.0234  -0.0072 48  THR A O   
427  C CB  . THR A 47  ? 0.4076 0.3769 0.3732 -0.0424 0.0265  -0.0171 48  THR A CB  
428  O OG1 . THR A 47  ? 0.4148 0.3978 0.3915 -0.0415 0.0213  -0.0230 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.4373 0.4020 0.3953 -0.0506 0.0340  -0.0196 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2998 0.2679 0.2730 -0.0343 0.0184  -0.0159 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2935 0.2603 0.2675 -0.0304 0.0157  -0.0137 49  VAL A CA  
432  C C   . VAL A 48  ? 0.3406 0.2977 0.3110 -0.0308 0.0200  -0.0126 49  VAL A C   
433  O O   . VAL A 48  ? 0.3182 0.2735 0.2900 -0.0274 0.0212  -0.0102 49  VAL A O   
434  C CB  . VAL A 48  ? 0.3294 0.3002 0.3049 -0.0302 0.0100  -0.0170 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.3350 0.3003 0.3072 -0.0289 0.0095  -0.0150 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.3323 0.3122 0.3132 -0.0286 0.0063  -0.0189 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.3251 0.2775 0.2921 -0.0353 0.0228  -0.0156 50  LEU A N   
438  C CA  . LEU A 49  ? 0.3243 0.2665 0.2874 -0.0365 0.0281  -0.0157 50  LEU A CA  
439  C C   . LEU A 49  ? 0.3676 0.3018 0.3304 -0.0323 0.0325  -0.0114 50  LEU A C   
440  O O   . LEU A 49  ? 0.3732 0.3037 0.3380 -0.0288 0.0347  -0.0107 50  LEU A O   
441  C CB  . LEU A 49  ? 0.3250 0.2641 0.2843 -0.0431 0.0308  -0.0208 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.3597 0.3064 0.3187 -0.0458 0.0246  -0.0259 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.3609 0.3073 0.3178 -0.0529 0.0274  -0.0324 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3917 0.3342 0.3451 -0.0444 0.0219  -0.0247 50  LEU A CD2 
445  N N   . MET A 50  ? 0.3327 0.2642 0.2923 -0.0323 0.0335  -0.0089 51  MET A N   
446  C CA  . MET A 50  ? 0.3586 0.2792 0.3139 -0.0269 0.0358  -0.0035 51  MET A CA  
447  C C   . MET A 50  ? 0.3961 0.3244 0.3578 -0.0186 0.0305  -0.0004 51  MET A C   
448  O O   . MET A 50  ? 0.4069 0.3296 0.3705 -0.0118 0.0311  0.0017  51  MET A O   
449  C CB  . MET A 50  ? 0.3896 0.3035 0.3355 -0.0302 0.0378  -0.0012 51  MET A CB  
450  C CG  . MET A 50  ? 0.4330 0.3393 0.3732 -0.0397 0.0447  -0.0058 51  MET A CG  
451  S SD  . MET A 50  ? 0.4867 0.3909 0.4174 -0.0466 0.0479  -0.0057 51  MET A SD  
452  C CE  . MET A 50  ? 0.4554 0.3328 0.3683 -0.0420 0.0516  0.0034  51  MET A CE  
453  N N   . ALA A 51  ? 0.3393 0.2815 0.3059 -0.0190 0.0254  -0.0013 52  ALA A N   
454  C CA  . ALA A 51  ? 0.3320 0.2841 0.3054 -0.0130 0.0207  0.0000  52  ALA A CA  
455  C C   . ALA A 51  ? 0.3820 0.3379 0.3641 -0.0111 0.0222  -0.0033 52  ALA A C   
456  O O   . ALA A 51  ? 0.3756 0.3397 0.3657 -0.0057 0.0198  -0.0038 52  ALA A O   
457  C CB  . ALA A 51  ? 0.3310 0.2949 0.3065 -0.0156 0.0165  -0.0015 52  ALA A CB  
458  N N   . CYS A 52  ? 0.3310 0.2821 0.3113 -0.0163 0.0262  -0.0067 53  CYS A N   
459  C CA  . CYS A 52  ? 0.3408 0.2936 0.3259 -0.0175 0.0294  -0.0108 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3823 0.3261 0.3682 -0.0164 0.0357  -0.0129 53  CYS A C   
461  O O   . CYS A 52  ? 0.3587 0.3055 0.3504 -0.0170 0.0396  -0.0174 53  CYS A O   
462  C CB  . CYS A 52  ? 0.3437 0.2956 0.3224 -0.0245 0.0289  -0.0132 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.3713 0.3320 0.3505 -0.0250 0.0224  -0.0123 53  CYS A SG  
464  N N   . SER A 53  ? 0.3471 0.2790 0.3261 -0.0170 0.0382  -0.0111 54  SER A N   
465  C CA  . SER A 53  ? 0.3479 0.2684 0.3255 -0.0177 0.0453  -0.0141 54  SER A CA  
466  C C   . SER A 53  ? 0.4042 0.3116 0.3788 -0.0120 0.0470  -0.0103 54  SER A C   
467  O O   . SER A 53  ? 0.3955 0.2961 0.3610 -0.0145 0.0461  -0.0067 54  SER A O   
468  C CB  . SER A 53  ? 0.3634 0.2788 0.3317 -0.0275 0.0479  -0.0173 54  SER A CB  
469  O OG  . SER A 53  ? 0.4196 0.3219 0.3829 -0.0305 0.0547  -0.0199 54  SER A OG  
470  N N   . GLY A 54  ? 0.3681 0.2703 0.3494 -0.0048 0.0502  -0.0120 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3761 0.2603 0.3520 0.0020  0.0520  -0.0081 55  GLY A CA  
472  C C   . GLY A 54  ? 0.4264 0.2928 0.3894 -0.0068 0.0594  -0.0092 55  GLY A C   
473  O O   . GLY A 54  ? 0.4286 0.2781 0.3800 -0.0062 0.0607  -0.0045 55  GLY A O   
474  N N   . LEU A 55  ? 0.3950 0.2645 0.3580 -0.0163 0.0644  -0.0158 56  LEU A N   
475  C CA  . LEU A 55  ? 0.3961 0.2522 0.3480 -0.0261 0.0711  -0.0188 56  LEU A CA  
476  C C   . LEU A 55  ? 0.4345 0.2936 0.3784 -0.0332 0.0680  -0.0165 56  LEU A C   
477  O O   . LEU A 55  ? 0.4056 0.2498 0.3399 -0.0371 0.0727  -0.0155 56  LEU A O   
478  C CB  . LEU A 55  ? 0.3920 0.2524 0.3443 -0.0345 0.0756  -0.0268 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4668 0.3157 0.4089 -0.0453 0.0824  -0.0319 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4961 0.3227 0.4352 -0.0426 0.0917  -0.0332 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.4630 0.3199 0.4023 -0.0541 0.0832  -0.0389 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3734 0.2508 0.3215 -0.0350 0.0609  -0.0163 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3614 0.2442 0.3052 -0.0410 0.0582  -0.0160 57  PHE A CA  
484  C C   . PHE A 56  ? 0.4181 0.2933 0.3567 -0.0369 0.0576  -0.0095 57  PHE A C   
485  O O   . PHE A 56  ? 0.4147 0.2846 0.3457 -0.0438 0.0609  -0.0103 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3645 0.2664 0.3139 -0.0425 0.0505  -0.0177 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3719 0.2775 0.3200 -0.0486 0.0505  -0.0240 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.4090 0.3115 0.3524 -0.0571 0.0543  -0.0299 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3861 0.2978 0.3358 -0.0468 0.0468  -0.0243 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.4164 0.3223 0.3566 -0.0625 0.0529  -0.0357 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.4173 0.3295 0.3610 -0.0527 0.0460  -0.0292 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3858 0.2955 0.3247 -0.0599 0.0483  -0.0347 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3910 0.2650 0.3325 -0.0262 0.0538  -0.0039 58  TYR A N   
494  C CA  . TYR A 57  ? 0.4122 0.2761 0.3448 -0.0212 0.0519  0.0032  58  TYR A CA  
495  C C   . TYR A 57  ? 0.4687 0.3056 0.3863 -0.0243 0.0602  0.0048  58  TYR A C   
496  O O   . TYR A 57  ? 0.4559 0.2825 0.3601 -0.0299 0.0630  0.0074  58  TYR A O   
497  C CB  . TYR A 57  ? 0.4314 0.2996 0.3711 -0.0080 0.0453  0.0075  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4910 0.3457 0.4184 -0.0010 0.0418  0.0155  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.5127 0.3715 0.4315 -0.0050 0.0387  0.0187  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.5513 0.3877 0.4741 0.0099  0.0413  0.0197  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.5525 0.3966 0.4554 0.0006  0.0352  0.0265  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.6030 0.4239 0.5104 0.0173  0.0364  0.0282  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6986 0.5231 0.5947 0.0121  0.0334  0.0319  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.7836 0.5907 0.6606 0.0188  0.0284  0.0406  58  TYR A OH  
505  N N   A SER A 58  ? 0.4526 0.2769 0.3715 -0.0217 0.0654  0.0026  59  SER A N   
506  N N   B SER A 58  ? 0.4556 0.2800 0.3746 -0.0217 0.0654  0.0025  59  SER A N   
507  C CA  A SER A 58  ? 0.4807 0.2762 0.3852 -0.0247 0.0745  0.0032  59  SER A CA  
508  C CA  B SER A 58  ? 0.4861 0.2817 0.3906 -0.0247 0.0745  0.0032  59  SER A CA  
509  C C   A SER A 58  ? 0.5542 0.3477 0.4513 -0.0413 0.0825  -0.0030 59  SER A C   
510  C C   B SER A 58  ? 0.5532 0.3472 0.4503 -0.0413 0.0823  -0.0029 59  SER A C   
511  O O   A SER A 58  ? 0.5878 0.3604 0.4685 -0.0473 0.0890  -0.0009 59  SER A O   
512  O O   B SER A 58  ? 0.5820 0.3559 0.4628 -0.0473 0.0885  -0.0007 59  SER A O   
513  C CB  A SER A 58  ? 0.5145 0.3007 0.4255 -0.0187 0.0787  -0.0002 59  SER A CB  
514  C CB  B SER A 58  ? 0.5307 0.3173 0.4418 -0.0194 0.0789  -0.0005 59  SER A CB  
515  O OG  A SER A 58  ? 0.5361 0.3223 0.4543 -0.0026 0.0720  0.0045  59  SER A OG  
516  O OG  B SER A 58  ? 0.6271 0.3833 0.5234 -0.0225 0.0884  -0.0003 59  SER A OG  
517  N N   . ILE A 59  ? 0.4946 0.3097 0.4029 -0.0488 0.0816  -0.0110 60  ILE A N   
518  C CA  . ILE A 59  ? 0.4812 0.3013 0.3872 -0.0637 0.0870  -0.0193 60  ILE A CA  
519  C C   . ILE A 59  ? 0.5214 0.3472 0.4228 -0.0697 0.0865  -0.0186 60  ILE A C   
520  O O   . ILE A 59  ? 0.5559 0.3690 0.4468 -0.0805 0.0954  -0.0220 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4959 0.3390 0.4141 -0.0678 0.0827  -0.0274 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4988 0.3338 0.4179 -0.0665 0.0868  -0.0307 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.4848 0.3400 0.4040 -0.0812 0.0847  -0.0368 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.5065 0.3617 0.4334 -0.0683 0.0807  -0.0360 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.4431 0.2874 0.3521 -0.0641 0.0773  -0.0154 61  PHE A N   
526  C CA  . PHE A 60  ? 0.4415 0.2945 0.3485 -0.0709 0.0775  -0.0171 61  PHE A CA  
527  C C   . PHE A 60  ? 0.5199 0.3522 0.4093 -0.0695 0.0808  -0.0089 61  PHE A C   
528  O O   . PHE A 60  ? 0.5342 0.3707 0.4188 -0.0773 0.0835  -0.0111 61  PHE A O   
529  C CB  . PHE A 60  ? 0.4300 0.3111 0.3521 -0.0674 0.0675  -0.0194 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.4271 0.3243 0.3610 -0.0699 0.0640  -0.0274 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.4672 0.3698 0.4032 -0.0810 0.0687  -0.0375 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.4320 0.3390 0.3737 -0.0618 0.0560  -0.0253 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.4677 0.3846 0.4121 -0.0824 0.0636  -0.0445 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.4619 0.3798 0.4093 -0.0642 0.0522  -0.0316 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.4430 0.3658 0.3913 -0.0737 0.0551  -0.0407 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4990 0.3076 0.3773 -0.0602 0.0811  -0.0003 62  THR A N   
537  C CA  . THR A 61  ? 0.5225 0.3052 0.3782 -0.0589 0.0838  0.0084  62  THR A CA  
538  C C   . THR A 61  ? 0.6263 0.3778 0.4637 -0.0684 0.0969  0.0071  62  THR A C   
539  O O   . THR A 61  ? 0.6536 0.3767 0.4666 -0.0705 0.1018  0.0138  62  THR A O   
540  C CB  . THR A 61  ? 0.6127 0.3878 0.4653 -0.0416 0.0742  0.0191  62  THR A CB  
541  O OG1 . THR A 61  ? 0.5748 0.3437 0.4356 -0.0324 0.0735  0.0190  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.5592 0.3623 0.4250 -0.0352 0.0630  0.0202  62  THR A CG2 
543  N N   . ASP A 62  ? 0.5727 0.3274 0.4193 -0.0752 0.1029  -0.0018 63  ASP A N   
544  C CA  . ASP A 62  ? 0.6028 0.3292 0.4332 -0.0867 0.1168  -0.0053 63  ASP A CA  
545  C C   . ASP A 62  ? 0.6791 0.4114 0.5038 -0.1051 0.1255  -0.0133 63  ASP A C   
546  O O   . ASP A 62  ? 0.6398 0.4051 0.4836 -0.1111 0.1224  -0.0228 63  ASP A O   
547  C CB  . ASP A 62  ? 0.6125 0.3433 0.4551 -0.0893 0.1204  -0.0139 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.8155 0.5203 0.6430 -0.1040 0.1357  -0.0202 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.8904 0.5594 0.7008 -0.0993 0.1415  -0.0139 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.8326 0.5526 0.6653 -0.1201 0.1419  -0.0318 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.7161 0.4151 0.5141 -0.1143 0.1369  -0.0102 64  GLN A N   
552  C CA  . GLN A 63  ? 0.7349 0.4358 0.5246 -0.1336 0.1481  -0.0184 64  GLN A CA  
553  C C   . GLN A 63  ? 0.7654 0.4914 0.5741 -0.1497 0.1552  -0.0363 64  GLN A C   
554  O O   . GLN A 63  ? 0.7889 0.5351 0.6042 -0.1624 0.1595  -0.0462 64  GLN A O   
555  C CB  . GLN A 63  ? 0.8113 0.4645 0.5639 -0.1416 0.1609  -0.0115 64  GLN A CB  
556  C CG  . GLN A 63  ? 1.0513 0.6848 0.7826 -0.1288 0.1529  0.0046  64  GLN A CG  
557  N N   . LEU A 64  ? 0.6677 0.3944 0.4859 -0.1492 0.1561  -0.0416 65  LEU A N   
558  C CA  . LEU A 64  ? 0.6471 0.4005 0.4838 -0.1630 0.1602  -0.0589 65  LEU A CA  
559  C C   . LEU A 64  ? 0.6674 0.4616 0.5321 -0.1533 0.1447  -0.0629 65  LEU A C   
560  O O   . LEU A 64  ? 0.6714 0.4973 0.5535 -0.1612 0.1426  -0.0754 65  LEU A O   
561  C CB  . LEU A 64  ? 0.6720 0.4032 0.5011 -0.1706 0.1708  -0.0645 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.7821 0.4775 0.5864 -0.1879 0.1899  -0.0678 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.8034 0.4770 0.6020 -0.1925 0.1988  -0.0726 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.8388 0.5556 0.6496 -0.2092 0.1994  -0.0837 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.5765 0.3691 0.4452 -0.1366 0.1344  -0.0535 66  LYS A N   
566  C CA  . LYS A 65  ? 0.5413 0.3659 0.4314 -0.1283 0.1210  -0.0565 66  LYS A CA  
567  C C   . LYS A 65  ? 0.5925 0.4420 0.4939 -0.1220 0.1103  -0.0542 66  LYS A C   
568  O O   . LYS A 65  ? 0.5726 0.4504 0.4912 -0.1198 0.1010  -0.0604 66  LYS A O   
569  C CB  . LYS A 65  ? 0.5464 0.3609 0.4366 -0.1152 0.1159  -0.0491 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.5644 0.3570 0.4463 -0.1213 0.1264  -0.0536 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.5488 0.3379 0.4351 -0.1083 0.1210  -0.0487 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.6481 0.4105 0.5250 -0.1116 0.1320  -0.0517 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.6667 0.3927 0.5265 -0.1068 0.1394  -0.0428 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.5906 0.4284 0.4809 -0.1194 0.1117  -0.0458 67  CYS A N   
575  C CA  . CYS A 66  ? 0.5871 0.4465 0.4866 -0.1144 0.1031  -0.0443 67  CYS A CA  
576  C C   . CYS A 66  ? 0.6272 0.5169 0.5438 -0.1246 0.1031  -0.0590 67  CYS A C   
577  O O   . CYS A 66  ? 0.6216 0.5351 0.5526 -0.1184 0.0934  -0.0604 67  CYS A O   
578  C CB  . CYS A 66  ? 0.6314 0.4708 0.5122 -0.1131 0.1066  -0.0345 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.7291 0.5483 0.5897 -0.1334 0.1246  -0.0407 67  CYS A SG  
580  N N   . ASN A 67  ? 0.5713 0.4600 0.4871 -0.1401 0.1142  -0.0709 68  ASN A N   
581  C CA  . ASN A 67  ? 0.5661 0.4845 0.4998 -0.1513 0.1157  -0.0879 68  ASN A CA  
582  C C   . ASN A 67  ? 0.5906 0.5334 0.5428 -0.1505 0.1074  -0.0984 68  ASN A C   
583  O O   . ASN A 67  ? 0.5682 0.5393 0.5383 -0.1576 0.1060  -0.1136 68  ASN A O   
584  C CB  . ASN A 67  ? 0.6127 0.5180 0.5349 -0.1708 0.1336  -0.0967 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.8472 0.7333 0.7507 -0.1733 0.1408  -0.0885 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.8527 0.7061 0.7314 -0.1832 0.1544  -0.0848 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.7089 0.6118 0.6209 -0.1643 0.1316  -0.0850 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.5473 0.4798 0.4952 -0.1420 0.1018  -0.0914 69  LEU A N   
589  C CA  . LEU A 68  ? 0.5300 0.4819 0.4902 -0.1414 0.0935  -0.1002 69  LEU A CA  
590  C C   . LEU A 68  ? 0.5424 0.5193 0.5175 -0.1287 0.0767  -0.0992 69  LEU A C   
591  O O   . LEU A 68  ? 0.5228 0.4934 0.4946 -0.1171 0.0709  -0.0871 69  LEU A O   
592  C CB  . LEU A 68  ? 0.5422 0.4726 0.4904 -0.1386 0.0953  -0.0941 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.6228 0.5256 0.5557 -0.1507 0.1117  -0.0963 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.6329 0.5159 0.5565 -0.1452 0.1125  -0.0903 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.6412 0.5584 0.5811 -0.1684 0.1195  -0.1145 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4922 0.4964 0.4829 -0.1307 0.0686  -0.1122 70  SER A N   
597  N N   B SER A 69  ? 0.4910 0.4952 0.4817 -0.1308 0.0687  -0.1123 70  SER A N   
598  C CA  A SER A 69  ? 0.4759 0.5009 0.4789 -0.1180 0.0516  -0.1119 70  SER A CA  
599  C CA  B SER A 69  ? 0.4743 0.5001 0.4777 -0.1185 0.0517  -0.1126 70  SER A CA  
600  C C   A SER A 69  ? 0.4942 0.5141 0.4897 -0.1111 0.0419  -0.1073 70  SER A C   
601  C C   B SER A 69  ? 0.4937 0.5141 0.4895 -0.1114 0.0419  -0.1077 70  SER A C   
602  O O   A SER A 69  ? 0.4638 0.4918 0.4623 -0.0999 0.0282  -0.1036 70  SER A O   
603  O O   B SER A 69  ? 0.4629 0.4918 0.4619 -0.1002 0.0281  -0.1042 70  SER A O   
604  C CB  A SER A 69  ? 0.5247 0.5824 0.5491 -0.1217 0.0463  -0.1288 70  SER A CB  
605  C CB  B SER A 69  ? 0.5208 0.5792 0.5455 -0.1230 0.0468  -0.1301 70  SER A CB  
606  O OG  A SER A 69  ? 0.6350 0.7036 0.6639 -0.1324 0.0485  -0.1426 70  SER A OG  
607  O OG  B SER A 69  ? 0.6156 0.6809 0.6482 -0.1285 0.0552  -0.1346 70  SER A OG  
608  N N   . VAL A 70  ? 0.4574 0.4622 0.4416 -0.1188 0.0498  -0.1083 71  VAL A N   
609  C CA  . VAL A 70  ? 0.4510 0.4485 0.4252 -0.1153 0.0437  -0.1054 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4800 0.4481 0.4389 -0.1170 0.0557  -0.0965 71  VAL A C   
611  O O   . VAL A 70  ? 0.4844 0.4397 0.4390 -0.1268 0.0692  -0.0997 71  VAL A O   
612  C CB  . VAL A 70  ? 0.5128 0.5273 0.4911 -0.1235 0.0392  -0.1202 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.5250 0.5294 0.4887 -0.1212 0.0338  -0.1169 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.5051 0.5512 0.5016 -0.1198 0.0257  -0.1307 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3988 0.3558 0.3495 -0.1078 0.0511  -0.0863 72  ILE A N   
616  C CA  . ILE A 71  ? 0.4089 0.3415 0.3483 -0.1072 0.0607  -0.0794 72  ILE A CA  
617  C C   . ILE A 71  ? 0.4621 0.3923 0.3930 -0.1075 0.0568  -0.0813 72  ILE A C   
618  O O   . ILE A 71  ? 0.4434 0.3806 0.3726 -0.1007 0.0458  -0.0777 72  ILE A O   
619  C CB  . ILE A 71  ? 0.4337 0.3551 0.3724 -0.0966 0.0614  -0.0665 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.4492 0.3701 0.3919 -0.0973 0.0657  -0.0642 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.4576 0.3573 0.3881 -0.0936 0.0693  -0.0609 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.4958 0.4000 0.4316 -0.1076 0.0799  -0.0678 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.4453 0.3629 0.3687 -0.1159 0.0667  -0.0866 73  ASN A N   
624  C CA  . ASN A 72  ? 0.4458 0.3589 0.3587 -0.1183 0.0656  -0.0895 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4834 0.3764 0.3905 -0.1132 0.0737  -0.0821 73  ASN A C   
626  O O   . ASN A 72  ? 0.4690 0.3457 0.3763 -0.1145 0.0855  -0.0814 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4967 0.4104 0.4055 -0.1318 0.0717  -0.1024 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.7247 0.6616 0.6425 -0.1378 0.0645  -0.1128 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.5938 0.5493 0.5146 -0.1331 0.0497  -0.1142 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.6677 0.6036 0.5901 -0.1485 0.0752  -0.1213 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.4215 0.3150 0.3234 -0.1076 0.0677  -0.0774 74  LEU A N   
632  C CA  . LEU A 73  ? 0.4256 0.3042 0.3248 -0.1035 0.0757  -0.0731 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4869 0.3546 0.3760 -0.1123 0.0848  -0.0812 74  LEU A C   
634  O O   . LEU A 73  ? 0.4922 0.3652 0.3730 -0.1214 0.0820  -0.0893 74  LEU A O   
635  C CB  . LEU A 73  ? 0.4161 0.2988 0.3136 -0.0962 0.0682  -0.0662 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.4638 0.3564 0.3708 -0.0872 0.0596  -0.0583 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.4688 0.3602 0.3737 -0.0814 0.0571  -0.0526 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.4404 0.3296 0.3582 -0.0831 0.0651  -0.0548 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.4562 0.3098 0.3468 -0.1093 0.0953  -0.0802 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4845 0.3261 0.3671 -0.1168 0.1062  -0.0885 75  ASP A CA  
641  C C   . ASP A 74  ? 0.5488 0.3965 0.4157 -0.1242 0.1003  -0.0927 75  ASP A C   
642  O O   . ASP A 74  ? 0.5310 0.3849 0.3946 -0.1196 0.0920  -0.0868 75  ASP A O   
643  C CB  . ASP A 74  ? 0.5064 0.3370 0.3967 -0.1089 0.1155  -0.0861 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.6469 0.4637 0.5327 -0.1152 0.1291  -0.0957 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.6621 0.4805 0.5359 -0.1233 0.1303  -0.1016 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.6706 0.4731 0.5633 -0.1118 0.1386  -0.0972 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.5521 0.3967 0.4071 -0.1358 0.1041  -0.1027 76  PRO A N   
648  C CA  . PRO A 75  ? 0.5696 0.4180 0.4052 -0.1427 0.0969  -0.1060 76  PRO A CA  
649  C C   . PRO A 75  ? 0.6196 0.4598 0.4453 -0.1421 0.1012  -0.1038 76  PRO A C   
650  O O   . PRO A 75  ? 0.6359 0.4769 0.4426 -0.1460 0.0931  -0.1030 76  PRO A O   
651  C CB  . PRO A 75  ? 0.6157 0.4609 0.4417 -0.1559 0.1029  -0.1184 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.6751 0.5085 0.5142 -0.1561 0.1179  -0.1218 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5883 0.4245 0.4446 -0.1441 0.1148  -0.1117 76  PRO A CD  
654  N N   . GLU A 76  ? 0.5766 0.4087 0.4144 -0.1373 0.1134  -0.1031 77  GLU A N   
655  C CA  . GLU A 76  ? 0.6034 0.4303 0.4360 -0.1376 0.1198  -0.1033 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5965 0.4307 0.4302 -0.1300 0.1093  -0.0931 77  GLU A C   
657  O O   . GLU A 76  ? 0.5896 0.4201 0.4136 -0.1328 0.1123  -0.0930 77  GLU A O   
658  C CB  . GLU A 76  ? 0.6348 0.4549 0.4858 -0.1326 0.1349  -0.1071 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.9115 0.7257 0.7568 -0.1385 0.1472  -0.1147 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.2937 1.0976 1.1242 -0.1516 0.1578  -0.1268 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.2941 1.0909 1.1348 -0.1510 0.1667  -0.1327 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.2242 1.0250 1.0307 -0.1629 0.1576  -0.1303 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.5115 0.3552 0.3564 -0.1215 0.0984  -0.0855 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4944 0.3444 0.3416 -0.1140 0.0891  -0.0765 78  ILE A CA  
665  C C   . ILE A 77  ? 0.5598 0.4085 0.3838 -0.1186 0.0778  -0.0742 78  ILE A C   
666  O O   . ILE A 77  ? 0.5510 0.4032 0.3656 -0.1215 0.0683  -0.0760 78  ILE A O   
667  C CB  . ILE A 77  ? 0.5125 0.3723 0.3791 -0.1037 0.0824  -0.0699 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.5234 0.3799 0.4088 -0.0979 0.0929  -0.0706 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4771 0.3436 0.3458 -0.0967 0.0728  -0.0615 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.5876 0.4413 0.4819 -0.0940 0.1026  -0.0721 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.5644 0.4078 0.3794 -0.1187 0.0784  -0.0706 79  ASN A N   
672  C CA  . ASN A 78  ? 0.5841 0.4196 0.3725 -0.1224 0.0687  -0.0668 79  ASN A CA  
673  C C   . ASN A 78  ? 0.5738 0.4171 0.3677 -0.1124 0.0531  -0.0584 79  ASN A C   
674  O O   . ASN A 78  ? 0.5395 0.3888 0.3510 -0.1051 0.0542  -0.0539 79  ASN A O   
675  C CB  . ASN A 78  ? 0.6236 0.4475 0.4000 -0.1284 0.0792  -0.0674 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.8262 0.6357 0.5708 -0.1326 0.0707  -0.0623 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.7163 0.5236 0.4605 -0.1281 0.0664  -0.0556 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.7382 0.5359 0.4535 -0.1415 0.0679  -0.0652 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.5461 0.3902 0.3256 -0.1115 0.0381  -0.0571 80  PRO A N   
680  C CA  . PRO A 79  ? 0.5295 0.3816 0.3162 -0.1011 0.0235  -0.0505 80  PRO A CA  
681  C C   . PRO A 79  ? 0.5857 0.4277 0.3647 -0.0975 0.0221  -0.0428 80  PRO A C   
682  O O   . PRO A 79  ? 0.5521 0.4028 0.3480 -0.0889 0.0174  -0.0384 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5770 0.4299 0.3462 -0.1014 0.0080  -0.0525 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.6475 0.5001 0.4101 -0.1117 0.0153  -0.0615 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5980 0.4376 0.3556 -0.1192 0.0331  -0.0626 80  PRO A CD  
686  N N   . GLU A 80  ? 0.5642 0.3872 0.3173 -0.1055 0.0277  -0.0421 81  GLU A N   
687  C CA  . GLU A 80  ? 0.5660 0.3768 0.3095 -0.1046 0.0287  -0.0359 81  GLU A CA  
688  C C   . GLU A 80  ? 0.5767 0.3986 0.3484 -0.1025 0.0409  -0.0368 81  GLU A C   
689  O O   . GLU A 80  ? 0.5496 0.3746 0.3304 -0.0961 0.0369  -0.0319 81  GLU A O   
690  C CB  . GLU A 80  ? 0.6208 0.4065 0.3270 -0.1160 0.0337  -0.0357 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.7552 0.5247 0.4470 -0.1155 0.0328  -0.0289 81  GLU A CG  
692  C CD  . GLU A 80  ? 1.1143 0.8568 0.7703 -0.1291 0.0429  -0.0291 81  GLU A CD  
693  O OE1 . GLU A 80  ? 1.1262 0.8479 0.7585 -0.1291 0.0377  -0.0222 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 1.0308 0.7715 0.6818 -0.1404 0.0570  -0.0366 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.5318 0.3600 0.3173 -0.1069 0.0547  -0.0436 82  GLY A N   
696  C CA  . GLY A 81  ? 0.5088 0.3495 0.3227 -0.1029 0.0643  -0.0453 82  GLY A CA  
697  C C   . GLY A 81  ? 0.5034 0.3597 0.3409 -0.0912 0.0555  -0.0409 82  GLY A C   
698  O O   . GLY A 81  ? 0.4650 0.3286 0.3173 -0.0858 0.0557  -0.0381 82  GLY A O   
699  N N   . PHE A 82  ? 0.4484 0.3103 0.2887 -0.0884 0.0479  -0.0412 83  PHE A N   
700  C CA  . PHE A 82  ? 0.4169 0.2925 0.2771 -0.0793 0.0407  -0.0380 83  PHE A CA  
701  C C   . PHE A 82  ? 0.4575 0.3336 0.3141 -0.0738 0.0297  -0.0321 83  PHE A C   
702  O O   . PHE A 82  ? 0.4294 0.3142 0.3022 -0.0677 0.0288  -0.0292 83  PHE A O   
703  C CB  . PHE A 82  ? 0.4298 0.3116 0.2926 -0.0798 0.0361  -0.0415 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.4278 0.3228 0.3106 -0.0726 0.0319  -0.0394 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.4515 0.3500 0.3510 -0.0697 0.0401  -0.0391 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.4389 0.3417 0.3230 -0.0680 0.0196  -0.0376 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.4487 0.3566 0.3623 -0.0642 0.0369  -0.0366 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.4459 0.3608 0.3477 -0.0626 0.0174  -0.0366 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.4252 0.3417 0.3400 -0.0616 0.0264  -0.0357 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.4841 0.3494 0.3182 -0.0757 0.0208  -0.0304 84  CYS A N   
711  C CA  . CYS A 83  ? 0.5053 0.3665 0.3330 -0.0697 0.0099  -0.0250 84  CYS A CA  
712  C C   . CYS A 83  ? 0.5127 0.3696 0.3439 -0.0698 0.0167  -0.0219 84  CYS A C   
713  O O   . CYS A 83  ? 0.4784 0.3423 0.3218 -0.0631 0.0118  -0.0190 84  CYS A O   
714  C CB  . CYS A 83  ? 0.5713 0.4158 0.3690 -0.0716 -0.0001 -0.0233 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.6550 0.4918 0.4443 -0.0615 -0.0160 -0.0170 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4752 0.3225 0.2972 -0.0784 0.0288  -0.0242 85  ILE A N   
717  C CA  . ILE A 84  ? 0.4595 0.3048 0.2855 -0.0811 0.0373  -0.0240 85  ILE A CA  
718  C C   . ILE A 84  ? 0.4404 0.3068 0.2982 -0.0742 0.0398  -0.0251 85  ILE A C   
719  O O   . ILE A 84  ? 0.4260 0.2968 0.2921 -0.0710 0.0385  -0.0231 85  ILE A O   
720  C CB  . ILE A 84  ? 0.5076 0.3418 0.3201 -0.0930 0.0514  -0.0292 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.5431 0.3505 0.3164 -0.1007 0.0483  -0.0264 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4957 0.3375 0.3238 -0.0960 0.0630  -0.0331 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.6576 0.4536 0.4136 -0.1135 0.0611  -0.0322 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3858 0.2633 0.2590 -0.0720 0.0432  -0.0281 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3775 0.2716 0.2767 -0.0648 0.0446  -0.0281 86  LEU A CA  
726  C C   . LEU A 85  ? 0.4217 0.3239 0.3289 -0.0573 0.0341  -0.0237 86  LEU A C   
727  O O   . LEU A 85  ? 0.3845 0.2967 0.3061 -0.0525 0.0335  -0.0223 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3777 0.2760 0.2876 -0.0645 0.0518  -0.0321 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.4568 0.3523 0.3675 -0.0703 0.0643  -0.0386 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.4730 0.3696 0.3928 -0.0690 0.0706  -0.0428 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.4775 0.3837 0.4041 -0.0678 0.0683  -0.0405 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3902 0.2896 0.2885 -0.0565 0.0257  -0.0227 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3741 0.2825 0.2809 -0.0501 0.0164  -0.0206 87  LEU A CA  
734  C C   . LEU A 86  ? 0.4038 0.3090 0.3074 -0.0474 0.0118  -0.0175 87  LEU A C   
735  O O   . LEU A 86  ? 0.3707 0.2859 0.2878 -0.0428 0.0101  -0.0164 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3757 0.2842 0.2755 -0.0502 0.0083  -0.0227 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.4289 0.3503 0.3411 -0.0442 -0.0001 -0.0234 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.4054 0.3384 0.3354 -0.0433 0.0059  -0.0241 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.4562 0.3806 0.3630 -0.0441 -0.0092 -0.0276 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3970 0.2861 0.2808 -0.0514 0.0112  -0.0163 88  ASP A N   
741  C CA  . ASP A 87  ? 0.4044 0.2853 0.2817 -0.0506 0.0091  -0.0137 88  ASP A CA  
742  C C   . ASP A 87  ? 0.4266 0.3174 0.3196 -0.0517 0.0174  -0.0150 88  ASP A C   
743  O O   . ASP A 87  ? 0.4174 0.3133 0.3183 -0.0480 0.0143  -0.0140 88  ASP A O   
744  C CB  . ASP A 87  ? 0.4671 0.3242 0.3158 -0.0570 0.0099  -0.0121 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.6647 0.5098 0.4947 -0.0531 -0.0029 -0.0096 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.6696 0.5273 0.5124 -0.0448 -0.0128 -0.0101 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.6888 0.5123 0.4910 -0.0584 -0.0032 -0.0078 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3789 0.2736 0.2776 -0.0565 0.0276  -0.0183 89  PHE A N   
749  C CA  . PHE A 88  ? 0.3517 0.2596 0.2682 -0.0563 0.0342  -0.0211 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3527 0.2775 0.2885 -0.0479 0.0289  -0.0195 89  PHE A C   
751  O O   . PHE A 88  ? 0.3334 0.2669 0.2788 -0.0460 0.0284  -0.0199 89  PHE A O   
752  C CB  . PHE A 88  ? 0.3637 0.2754 0.2863 -0.0605 0.0447  -0.0264 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.3549 0.2847 0.3003 -0.0571 0.0487  -0.0300 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3777 0.3122 0.3273 -0.0612 0.0528  -0.0338 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3768 0.3184 0.3386 -0.0493 0.0474  -0.0297 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.3686 0.3230 0.3407 -0.0571 0.0544  -0.0381 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3920 0.3500 0.3735 -0.0441 0.0483  -0.0325 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3678 0.3340 0.3555 -0.0478 0.0513  -0.0372 89  PHE A CZ  
759  N N   . MET A 89  ? 0.3096 0.2381 0.2495 -0.0441 0.0260  -0.0183 90  MET A N   
760  C CA  . MET A 89  ? 0.2999 0.2408 0.2535 -0.0379 0.0224  -0.0166 90  MET A CA  
761  C C   . MET A 89  ? 0.3445 0.2887 0.2991 -0.0354 0.0159  -0.0151 90  MET A C   
762  O O   . MET A 89  ? 0.3297 0.2842 0.2946 -0.0324 0.0153  -0.0148 90  MET A O   
763  C CB  . MET A 89  ? 0.3141 0.2543 0.2671 -0.0369 0.0208  -0.0163 90  MET A CB  
764  C CG  . MET A 89  ? 0.3438 0.2805 0.2977 -0.0385 0.0279  -0.0181 90  MET A CG  
765  S SD  . MET A 89  ? 0.3988 0.3343 0.3521 -0.0388 0.0271  -0.0185 90  MET A SD  
766  C CE  . MET A 89  ? 0.4060 0.3320 0.3561 -0.0424 0.0366  -0.0219 90  MET A CE  
767  N N   . TYR A 90  ? 0.3218 0.2568 0.2651 -0.0360 0.0106  -0.0146 91  TYR A N   
768  C CA  . TYR A 90  ? 0.3243 0.2606 0.2687 -0.0325 0.0041  -0.0142 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3838 0.3124 0.3224 -0.0347 0.0053  -0.0142 91  TYR A C   
770  O O   . TYR A 90  ? 0.3642 0.2929 0.3044 -0.0317 0.0008  -0.0144 91  TYR A O   
771  C CB  . TYR A 90  ? 0.3495 0.2806 0.2868 -0.0298 -0.0040 -0.0146 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.3558 0.2996 0.3039 -0.0278 -0.0059 -0.0169 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3807 0.3246 0.3273 -0.0309 -0.0026 -0.0179 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.3563 0.3113 0.3155 -0.0242 -0.0096 -0.0193 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.3962 0.3501 0.3513 -0.0310 -0.0028 -0.0210 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.3642 0.3303 0.3321 -0.0244 -0.0098 -0.0229 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.4113 0.3764 0.3769 -0.0283 -0.0061 -0.0236 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.3593 0.3340 0.3325 -0.0304 -0.0049 -0.0281 91  TYR A OH  
779  N N   . THR A 91  ? 0.3437 0.2652 0.2757 -0.0407 0.0124  -0.0150 92  THR A N   
780  C CA  . THR A 91  ? 0.3569 0.2684 0.2808 -0.0451 0.0152  -0.0159 92  THR A CA  
781  C C   . THR A 91  ? 0.3862 0.3059 0.3184 -0.0511 0.0246  -0.0202 92  THR A C   
782  O O   . THR A 91  ? 0.3871 0.3020 0.3160 -0.0556 0.0276  -0.0224 92  THR A O   
783  C CB  . THR A 91  ? 0.4296 0.3155 0.3279 -0.0495 0.0148  -0.0138 92  THR A CB  
784  O OG1 . THR A 91  ? 0.4174 0.2991 0.3088 -0.0562 0.0224  -0.0154 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.4333 0.3099 0.3217 -0.0427 0.0035  -0.0105 92  THR A CG2 
786  N N   A SER A 92  ? 0.3309 0.2623 0.2740 -0.0513 0.0293  -0.0224 93  SER A N   
787  N N   B SER A 92  ? 0.3308 0.2618 0.2735 -0.0514 0.0294  -0.0224 93  SER A N   
788  C CA  A SER A 92  ? 0.3234 0.2657 0.2776 -0.0560 0.0380  -0.0285 93  SER A CA  
789  C CA  B SER A 92  ? 0.3228 0.2650 0.2769 -0.0559 0.0380  -0.0285 93  SER A CA  
790  C C   A SER A 92  ? 0.3702 0.2968 0.3088 -0.0666 0.0472  -0.0320 93  SER A C   
791  C C   B SER A 92  ? 0.3854 0.3121 0.3241 -0.0668 0.0473  -0.0321 93  SER A C   
792  O O   A SER A 92  ? 0.3538 0.2901 0.3023 -0.0718 0.0560  -0.0390 93  SER A O   
793  O O   B SER A 92  ? 0.3802 0.3162 0.3283 -0.0726 0.0561  -0.0393 93  SER A O   
794  C CB  A SER A 92  ? 0.3363 0.2922 0.3029 -0.0562 0.0379  -0.0321 93  SER A CB  
795  C CB  B SER A 92  ? 0.3379 0.2954 0.3060 -0.0551 0.0372  -0.0317 93  SER A CB  
796  O OG  A SER A 92  ? 0.2986 0.2651 0.2740 -0.0482 0.0299  -0.0289 93  SER A OG  
797  O OG  B SER A 92  ? 0.3716 0.3180 0.3292 -0.0628 0.0408  -0.0341 93  SER A OG  
798  N N   A ARG A 93  ? 0.3592 0.2622 0.2733 -0.0698 0.0451  -0.0276 94  ARG A N   
799  N N   B ARG A 93  ? 0.3667 0.2700 0.2811 -0.0697 0.0453  -0.0277 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3844 0.2674 0.2771 -0.0811 0.0540  -0.0300 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3919 0.2741 0.2837 -0.0810 0.0536  -0.0296 94  ARG A CA  
802  C C   A ARG A 93  ? 0.4451 0.3225 0.3294 -0.0825 0.0561  -0.0297 94  ARG A C   
803  C C   B ARG A 93  ? 0.4472 0.3236 0.3304 -0.0827 0.0560  -0.0295 94  ARG A C   
804  O O   A ARG A 93  ? 0.4276 0.3013 0.3065 -0.0761 0.0473  -0.0246 94  ARG A O   
805  O O   B ARG A 93  ? 0.4359 0.3080 0.3130 -0.0765 0.0472  -0.0244 94  ARG A O   
806  C CB  A ARG A 93  ? 0.4411 0.2964 0.3063 -0.0843 0.0504  -0.0251 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.4348 0.2901 0.3001 -0.0827 0.0485  -0.0242 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.5188 0.3754 0.3893 -0.0849 0.0503  -0.0265 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.5234 0.3811 0.3954 -0.0813 0.0465  -0.0247 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.6420 0.4722 0.4893 -0.0817 0.0419  -0.0199 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5938 0.4416 0.4571 -0.0944 0.0586  -0.0305 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.7922 0.5894 0.6052 -0.0903 0.0460  -0.0173 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.6202 0.4715 0.4910 -0.0939 0.0575  -0.0323 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.9627 0.7391 0.7572 -0.1022 0.0559  -0.0196 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.7900 0.6145 0.6391 -0.0972 0.0570  -0.0296 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.7941 0.5816 0.6037 -0.1067 0.0625  -0.0256 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.6617 0.4913 0.5198 -0.0972 0.0570  -0.0326 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.7988 0.5419 0.5577 -0.1105 0.0596  -0.0164 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5941 0.3849 0.4106 -0.1004 0.0565  -0.0240 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.4078 0.2858 0.2919 -0.0917 0.0684  -0.0366 95  LEU A N   
821  C CA  . LEU A 94  ? 0.4136 0.2865 0.2902 -0.0949 0.0730  -0.0384 95  LEU A CA  
822  C C   . LEU A 94  ? 0.5021 0.3482 0.3462 -0.1083 0.0808  -0.0394 95  LEU A C   
823  O O   . LEU A 94  ? 0.4907 0.3337 0.3317 -0.1193 0.0926  -0.0459 95  LEU A O   
824  C CB  . LEU A 94  ? 0.4052 0.3012 0.3096 -0.0938 0.0815  -0.0470 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.4484 0.3418 0.3502 -0.0958 0.0871  -0.0504 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.4158 0.3088 0.3175 -0.0861 0.0762  -0.0434 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.4622 0.3762 0.3910 -0.0952 0.0972  -0.0608 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.5047 0.3315 0.3234 -0.1082 0.0742  -0.0336 96  ASN A N   
829  C CA  . ASN A 95  ? 0.5452 0.3422 0.3264 -0.1206 0.0799  -0.0330 96  ASN A CA  
830  C C   . ASN A 95  ? 0.6063 0.4059 0.3866 -0.1301 0.0931  -0.0412 96  ASN A C   
831  O O   . ASN A 95  ? 0.6094 0.4014 0.3758 -0.1302 0.0898  -0.0397 96  ASN A O   
832  C CB  . ASN A 95  ? 0.6103 0.3854 0.3632 -0.1150 0.0647  -0.0232 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.8549 0.5949 0.5631 -0.1268 0.0683  -0.0209 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.7539 0.4795 0.4472 -0.1403 0.0820  -0.0248 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.7921 0.5175 0.4771 -0.1228 0.0562  -0.0151 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.5479 0.3611 0.3461 -0.1376 0.1079  -0.0514 97  LEU A N   
837  C CA  . LEU A 96  ? 0.5660 0.3860 0.3703 -0.1460 0.1223  -0.0620 97  LEU A CA  
838  C C   . LEU A 96  ? 0.6408 0.4340 0.4094 -0.1647 0.1355  -0.0658 97  LEU A C   
839  O O   . LEU A 96  ? 0.6342 0.4181 0.3933 -0.1743 0.1430  -0.0681 97  LEU A O   
840  C CB  . LEU A 96  ? 0.5509 0.4033 0.3975 -0.1421 0.1299  -0.0723 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.6181 0.4870 0.4858 -0.1424 0.1402  -0.0832 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.6208 0.4899 0.4906 -0.1317 0.1307  -0.0774 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5933 0.4938 0.5022 -0.1364 0.1446  -0.0928 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.6160 0.3939 0.3608 -0.1710 0.1383  -0.0663 98  ARG A N   
845  C CA  . ARG A 97  ? 0.6684 0.4163 0.3719 -0.1898 0.1505  -0.0691 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6872 0.4414 0.3938 -0.1988 0.1648  -0.0806 98  ARG A C   
847  O O   . ARG A 97  ? 0.6406 0.4132 0.3704 -0.1885 0.1601  -0.0822 98  ARG A O   
848  C CB  . ARG A 97  ? 0.7221 0.4358 0.3799 -0.1889 0.1360  -0.0555 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.8013 0.5053 0.4536 -0.1791 0.1213  -0.0442 98  ARG A CG  
850  C CD  . ARG A 97  ? 1.0599 0.7318 0.6699 -0.1752 0.1049  -0.0316 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.3339 0.9667 0.8927 -0.1922 0.1137  -0.0306 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.6279 1.2313 1.1579 -0.2019 0.1197  -0.0276 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.5103 1.0753 0.9898 -0.2184 0.1284  -0.0264 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.4947 1.1052 1.0442 -0.1962 0.1180  -0.0260 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.6879 0.4249 0.3698 -0.2187 0.1831  -0.0892 99  GLU A N   
856  C CA  . GLU A 98  ? 0.6856 0.4270 0.3683 -0.2292 0.1987  -0.1020 99  GLU A CA  
857  C C   . GLU A 98  ? 0.7545 0.4883 0.4224 -0.2228 0.1874  -0.0960 99  GLU A C   
858  O O   . GLU A 98  ? 0.7465 0.4989 0.4387 -0.2195 0.1927  -0.1046 99  GLU A O   
859  C CB  . GLU A 98  ? 0.7529 0.4683 0.3981 -0.2541 0.2191  -0.1100 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.9057 0.6286 0.5558 -0.2667 0.2387  -0.1264 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.3242 1.0191 0.9327 -0.2934 0.2599  -0.1348 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.2954 0.9507 0.8501 -0.3022 0.2549  -0.1230 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.3236 1.0356 0.9527 -0.3054 0.2819  -0.1537 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.7432 0.4508 0.3732 -0.2205 0.1715  -0.0820 100 GLY A N   
865  C CA  . GLY A 99  ? 0.7609 0.4613 0.3739 -0.2153 0.1588  -0.0766 100 GLY A CA  
866  C C   . GLY A 99  ? 0.7553 0.4822 0.4054 -0.1960 0.1444  -0.0732 100 GLY A C   
867  O O   . GLY A 99  ? 0.7681 0.4955 0.4128 -0.1935 0.1382  -0.0732 100 GLY A O   
868  N N   . ASN A 100 ? 0.6619 0.4104 0.3484 -0.1832 0.1393  -0.0709 101 ASN A N   
869  C CA  . ASN A 100 ? 0.6186 0.3891 0.3364 -0.1660 0.1262  -0.0672 101 ASN A CA  
870  C C   . ASN A 100 ? 0.6309 0.4308 0.3957 -0.1585 0.1344  -0.0754 101 ASN A C   
871  O O   . ASN A 100 ? 0.5917 0.4068 0.3800 -0.1459 0.1260  -0.0730 101 ASN A O   
872  C CB  . ASN A 100 ? 0.6133 0.3807 0.3274 -0.1543 0.1070  -0.0544 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.7259 0.5006 0.4568 -0.1507 0.1081  -0.0526 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5794 0.3729 0.3393 -0.1513 0.1193  -0.0606 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.6470 0.4079 0.3612 -0.1462 0.0957  -0.0429 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5942 0.4017 0.3723 -0.1661 0.1503  -0.0853 102 ILE A N   
877  C CA  . ILE A 101 ? 0.5675 0.4038 0.3909 -0.1569 0.1557  -0.0930 102 ILE A CA  
878  C C   . ILE A 101 ? 0.5786 0.4265 0.4230 -0.1493 0.1574  -0.0982 102 ILE A C   
879  O O   . ILE A 101 ? 0.5293 0.3949 0.4041 -0.1346 0.1506  -0.0962 102 ILE A O   
880  C CB  . ILE A 101 ? 0.6166 0.4624 0.4527 -0.1669 0.1726  -0.1055 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5968 0.4750 0.4815 -0.1534 0.1728  -0.1121 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.6215 0.4562 0.4399 -0.1846 0.1916  -0.1180 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.6066 0.4995 0.5081 -0.1585 0.1811  -0.1204 102 ILE A CD1 
884  N N   . MET A 102 ? 0.5667 0.4023 0.3928 -0.1593 0.1661  -0.1043 103 MET A N   
885  C CA  . MET A 102 ? 0.5718 0.4152 0.4163 -0.1529 0.1690  -0.1099 103 MET A CA  
886  C C   . MET A 102 ? 0.5921 0.4359 0.4390 -0.1406 0.1523  -0.0990 103 MET A C   
887  O O   . MET A 102 ? 0.5544 0.4105 0.4288 -0.1288 0.1508  -0.0999 103 MET A O   
888  C CB  . MET A 102 ? 0.6427 0.4727 0.4661 -0.1678 0.1830  -0.1202 103 MET A CB  
889  C CG  . MET A 102 ? 0.7347 0.5670 0.5603 -0.1811 0.2030  -0.1344 103 MET A CG  
890  S SD  . MET A 102 ? 0.7858 0.6501 0.6652 -0.1703 0.2115  -0.1460 103 MET A SD  
891  C CE  . MET A 102 ? 0.7446 0.6175 0.6515 -0.1589 0.2154  -0.1541 103 MET A CE  
892  N N   . ALA A 103 ? 0.5711 0.4010 0.3890 -0.1431 0.1397  -0.0890 104 ALA A N   
893  C CA  . ALA A 103 ? 0.5567 0.3887 0.3765 -0.1333 0.1243  -0.0805 104 ALA A CA  
894  C C   . ALA A 103 ? 0.5527 0.3998 0.3984 -0.1193 0.1152  -0.0735 104 ALA A C   
895  O O   . ALA A 103 ? 0.5284 0.3837 0.3913 -0.1097 0.1096  -0.0711 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5905 0.4066 0.3753 -0.1385 0.1125  -0.0733 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4880 0.3374 0.3348 -0.1194 0.1145  -0.0708 105 VAL A N   
898  C CA  . VAL A 104 ? 0.4494 0.3134 0.3193 -0.1073 0.1063  -0.0651 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4713 0.3523 0.3746 -0.0984 0.1123  -0.0708 105 VAL A C   
900  O O   . VAL A 104 ? 0.4440 0.3330 0.3627 -0.0871 0.1041  -0.0656 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4990 0.3607 0.3617 -0.1111 0.1059  -0.0628 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.4566 0.3363 0.3462 -0.1001 0.1004  -0.0599 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.5269 0.3695 0.3572 -0.1151 0.0958  -0.0545 105 VAL A CG2 
904  N N   A MET A 105 ? 0.4487 0.3340 0.3621 -0.1034 0.1265  -0.0819 106 MET A N   
905  N N   B MET A 105 ? 0.4481 0.3335 0.3616 -0.1033 0.1265  -0.0819 106 MET A N   
906  C CA  A MET A 105 ? 0.4444 0.3452 0.3898 -0.0933 0.1314  -0.0884 106 MET A CA  
907  C CA  B MET A 105 ? 0.4532 0.3542 0.3989 -0.0929 0.1310  -0.0880 106 MET A CA  
908  C C   A MET A 105 ? 0.4939 0.3897 0.4437 -0.0861 0.1291  -0.0866 106 MET A C   
909  C C   B MET A 105 ? 0.4913 0.3870 0.4409 -0.0859 0.1288  -0.0864 106 MET A C   
910  O O   A MET A 105 ? 0.4723 0.3757 0.4415 -0.0730 0.1234  -0.0832 106 MET A O   
911  O O   B MET A 105 ? 0.4622 0.3654 0.4311 -0.0729 0.1232  -0.0830 106 MET A O   
912  C CB  A MET A 105 ? 0.4880 0.3953 0.4441 -0.1005 0.1478  -0.1029 106 MET A CB  
913  C CB  B MET A 105 ? 0.4987 0.4069 0.4564 -0.0995 0.1470  -0.1025 106 MET A CB  
914  C CG  A MET A 105 ? 0.5264 0.4522 0.5188 -0.0874 0.1506  -0.1103 106 MET A CG  
915  C CG  B MET A 105 ? 0.5394 0.4659 0.5334 -0.0857 0.1493  -0.1093 106 MET A CG  
916  S SD  A MET A 105 ? 0.5954 0.5327 0.6059 -0.0949 0.1705  -0.1306 106 MET A SD  
917  S SD  B MET A 105 ? 0.6068 0.5492 0.6220 -0.0925 0.1674  -0.1290 106 MET A SD  
918  C CE  A MET A 105 ? 0.5456 0.4953 0.5922 -0.0744 0.1684  -0.1352 106 MET A CE  
919  C CE  B MET A 105 ? 0.5946 0.5193 0.5937 -0.1035 0.1821  -0.1384 106 MET A CE  
920  N N   . ALA A 106 ? 0.4728 0.3540 0.4021 -0.0953 0.1334  -0.0891 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4782 0.3523 0.4086 -0.0915 0.1329  -0.0889 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4895 0.3640 0.4193 -0.0836 0.1188  -0.0775 107 ALA A C   
923  O O   . ALA A 106 ? 0.4605 0.3347 0.4032 -0.0746 0.1175  -0.0757 107 ALA A O   
924  C CB  . ALA A 106 ? 0.5105 0.3704 0.4163 -0.1051 0.1393  -0.0943 107 ALA A CB  
925  N N   . THR A 107 ? 0.4360 0.3101 0.3504 -0.0867 0.1087  -0.0703 108 THR A N   
926  C CA  . THR A 107 ? 0.4262 0.3032 0.3413 -0.0802 0.0960  -0.0613 108 THR A CA  
927  C C   . THR A 107 ? 0.4442 0.3325 0.3815 -0.0680 0.0922  -0.0569 108 THR A C   
928  O O   . THR A 107 ? 0.4197 0.3081 0.3638 -0.0613 0.0880  -0.0528 108 THR A O   
929  C CB  . THR A 107 ? 0.5041 0.3780 0.3989 -0.0851 0.0858  -0.0560 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4969 0.3595 0.3689 -0.0961 0.0888  -0.0603 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4889 0.3670 0.3854 -0.0799 0.0741  -0.0499 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3942 0.2917 0.3414 -0.0661 0.0942  -0.0584 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3727 0.2827 0.3405 -0.0546 0.0897  -0.0552 109 ALA A CA  
934  C C   . ALA A 108 ? 0.4033 0.3135 0.3880 -0.0451 0.0937  -0.0580 109 ALA A C   
935  O O   . ALA A 108 ? 0.3846 0.2972 0.3777 -0.0349 0.0871  -0.0522 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3832 0.3045 0.3586 -0.0563 0.0917  -0.0586 109 ALA A CB  
937  N N   . MET A 109 ? 0.3883 0.2930 0.3752 -0.0483 0.1046  -0.0668 110 MET A N   
938  C CA  . MET A 109 ? 0.3997 0.3006 0.4014 -0.0380 0.1083  -0.0696 110 MET A CA  
939  C C   . MET A 109 ? 0.4430 0.3290 0.4341 -0.0360 0.1044  -0.0627 110 MET A C   
940  O O   . MET A 109 ? 0.4442 0.3267 0.4430 -0.0248 0.1003  -0.0577 110 MET A O   
941  C CB  . MET A 109 ? 0.4450 0.3426 0.4513 -0.0428 0.1220  -0.0821 110 MET A CB  
942  C CG  . MET A 109 ? 0.4963 0.4110 0.5199 -0.0428 0.1278  -0.0915 110 MET A CG  
943  S SD  . MET A 109 ? 0.5951 0.5061 0.6196 -0.0534 0.1462  -0.1079 110 MET A SD  
944  C CE  . MET A 109 ? 0.5650 0.4668 0.6067 -0.0385 0.1493  -0.1114 110 MET A CE  
945  N N   . TYR A 110 ? 0.4240 0.3014 0.3964 -0.0474 0.1053  -0.0625 111 TYR A N   
946  C CA  . TYR A 110 ? 0.4245 0.2901 0.3866 -0.0491 0.1030  -0.0584 111 TYR A CA  
947  C C   . TYR A 110 ? 0.4472 0.3178 0.4103 -0.0431 0.0922  -0.0486 111 TYR A C   
948  O O   . TYR A 110 ? 0.4318 0.2932 0.3950 -0.0381 0.0915  -0.0446 111 TYR A O   
949  C CB  . TYR A 110 ? 0.4402 0.3019 0.3838 -0.0628 0.1040  -0.0618 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.4429 0.2985 0.3772 -0.0669 0.1005  -0.0594 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4817 0.3232 0.4144 -0.0687 0.1082  -0.0632 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.4342 0.2980 0.3614 -0.0699 0.0902  -0.0549 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.4650 0.3019 0.3895 -0.0747 0.1066  -0.0629 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.4425 0.3043 0.3637 -0.0749 0.0878  -0.0554 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4709 0.3199 0.3909 -0.0781 0.0964  -0.0597 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4755 0.3242 0.3902 -0.0851 0.0953  -0.0620 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3905 0.2738 0.3529 -0.0440 0.0847  -0.0451 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3693 0.2590 0.3329 -0.0394 0.0751  -0.0372 112 LEU A CA  
959  C C   . LEU A 111 ? 0.4151 0.3097 0.3922 -0.0273 0.0721  -0.0333 112 LEU A C   
960  O O   . LEU A 111 ? 0.4119 0.3097 0.3886 -0.0233 0.0650  -0.0269 112 LEU A O   
961  C CB  . LEU A 111 ? 0.3518 0.2510 0.3090 -0.0444 0.0683  -0.0356 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3940 0.2893 0.3357 -0.0542 0.0665  -0.0377 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.4027 0.3046 0.3381 -0.0558 0.0582  -0.0349 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.4178 0.3097 0.3562 -0.0561 0.0645  -0.0370 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3800 0.2769 0.3695 -0.0214 0.0770  -0.0381 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3835 0.2877 0.3878 -0.0083 0.0726  -0.0359 113 GLN A CA  
967  C C   . GLN A 112 ? 0.4114 0.3330 0.4204 -0.0076 0.0647  -0.0332 113 GLN A C   
968  O O   . GLN A 112 ? 0.3956 0.3196 0.4036 -0.0021 0.0568  -0.0263 113 GLN A O   
969  C CB  . GLN A 112 ? 0.4068 0.2959 0.4065 0.0001  0.0698  -0.0292 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.4367 0.3057 0.4319 -0.0003 0.0787  -0.0327 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.5613 0.4099 0.5442 0.0035  0.0773  -0.0251 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.5164 0.3649 0.4976 0.0114  0.0695  -0.0176 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.5650 0.3949 0.5370 -0.0035 0.0855  -0.0275 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3635 0.2950 0.3748 -0.0149 0.0680  -0.0389 114 MET A N   
975  C CA  . MET A 113 ? 0.3586 0.3048 0.3736 -0.0167 0.0631  -0.0384 114 MET A CA  
976  C C   . MET A 113 ? 0.4196 0.3799 0.4527 -0.0144 0.0681  -0.0475 114 MET A C   
977  O O   . MET A 113 ? 0.3953 0.3571 0.4269 -0.0238 0.0762  -0.0549 114 MET A O   
978  C CB  . MET A 113 ? 0.3798 0.3210 0.3781 -0.0285 0.0633  -0.0375 114 MET A CB  
979  C CG  . MET A 113 ? 0.4077 0.3399 0.3929 -0.0298 0.0575  -0.0306 114 MET A CG  
980  S SD  . MET A 113 ? 0.4455 0.3713 0.4117 -0.0407 0.0555  -0.0303 114 MET A SD  
981  C CE  . MET A 113 ? 0.3994 0.3357 0.3684 -0.0398 0.0490  -0.0277 114 MET A CE  
982  N N   . GLU A 114 ? 0.4158 0.3858 0.4657 -0.0017 0.0635  -0.0479 115 GLU A N   
983  C CA  . GLU A 114 ? 0.4276 0.4147 0.5007 0.0039  0.0670  -0.0584 115 GLU A CA  
984  C C   . GLU A 114 ? 0.4388 0.4433 0.5195 -0.0053 0.0711  -0.0667 115 GLU A C   
985  O O   . GLU A 114 ? 0.4193 0.4319 0.5120 -0.0094 0.0809  -0.0783 115 GLU A O   
986  C CB  . GLU A 114 ? 0.4584 0.4537 0.5461 0.0210  0.0572  -0.0558 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.6541 0.6285 0.7344 0.0306  0.0556  -0.0495 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3966 0.4062 0.4706 -0.0093 0.0650  -0.0618 116 HIS A N   
989  C CA  . HIS A 115 ? 0.4064 0.4294 0.4855 -0.0193 0.0698  -0.0697 116 HIS A CA  
990  C C   . HIS A 115 ? 0.4237 0.4331 0.4860 -0.0349 0.0813  -0.0735 116 HIS A C   
991  O O   . HIS A 115 ? 0.4229 0.4411 0.4924 -0.0435 0.0911  -0.0845 116 HIS A O   
992  C CB  . HIS A 115 ? 0.4294 0.4586 0.5044 -0.0196 0.0609  -0.0639 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.4795 0.5246 0.5704 -0.0058 0.0503  -0.0623 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.5110 0.5785 0.6275 0.0015  0.0501  -0.0726 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.5038 0.5455 0.5873 0.0013  0.0395  -0.0522 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.5050 0.5806 0.6270 0.0139  0.0377  -0.0674 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.5045 0.5640 0.6057 0.0133  0.0317  -0.0549 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.3583 0.3464 0.3976 -0.0389 0.0802  -0.0653 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3761 0.3483 0.3948 -0.0527 0.0890  -0.0676 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.4389 0.4118 0.4659 -0.0554 0.1011  -0.0783 117 VAL A C   
1001 O O   . VAL A 116 ? 0.4106 0.3827 0.4328 -0.0675 0.1121  -0.0870 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.4261 0.3786 0.4203 -0.0549 0.0830  -0.0574 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.4368 0.3725 0.4081 -0.0680 0.0907  -0.0601 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.4187 0.3713 0.4061 -0.0531 0.0725  -0.0491 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3915 0.3647 0.4300 -0.0447 0.0999  -0.0783 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3953 0.3696 0.4450 -0.0451 0.1112  -0.0894 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.4574 0.4536 0.5303 -0.0471 0.1192  -0.1033 118 VAL A C   
1008 O O   . VAL A 117 ? 0.4584 0.4535 0.5289 -0.0588 0.1326  -0.1141 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.4365 0.4064 0.4967 -0.0308 0.1075  -0.0868 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.4450 0.4165 0.5196 -0.0299 0.1197  -0.0999 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.4352 0.3843 0.4725 -0.0324 0.1026  -0.0759 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.4226 0.4389 0.5159 -0.0373 0.1110  -0.1036 119 ASP A N   
1013 N N   B ASP A 118 ? 0.4185 0.4352 0.5133 -0.0363 0.1109  -0.1039 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.4210 0.4634 0.5403 -0.0384 0.1165  -0.1179 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.4171 0.4604 0.5389 -0.0366 0.1162  -0.1183 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.4617 0.5029 0.5684 -0.0585 0.1283  -0.1251 119 ASP A C   
1017 C C   B ASP A 118 ? 0.4684 0.5119 0.5792 -0.0566 0.1283  -0.1262 119 ASP A C   
1018 O O   A ASP A 118 ? 0.4628 0.5153 0.5828 -0.0664 0.1420  -0.1407 119 ASP A O   
1019 O O   B ASP A 118 ? 0.4715 0.5273 0.5969 -0.0639 0.1417  -0.1420 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.4381 0.5007 0.5765 -0.0247 0.1028  -0.1150 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.4310 0.4938 0.5703 -0.0234 0.1021  -0.1147 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.6065 0.7008 0.7759 -0.0245 0.1069  -0.1315 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.5860 0.6557 0.7446 -0.0024 0.0921  -0.1128 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.6413 0.7492 0.8347 -0.0185 0.1130  -0.1444 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.6175 0.6868 0.7889 0.0034  0.0983  -0.1206 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.6809 0.7872 0.8515 -0.0304 0.1043  -0.1326 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.6607 0.7346 0.8202 0.0083  0.0782  -0.1037 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.4132 0.4394 0.4937 -0.0672 0.1240  -0.1145 120 THR A N   
1029 N N   B THR A 119 ? 0.4220 0.4503 0.5063 -0.0656 0.1244  -0.1158 120 THR A N   
1030 C CA  A THR A 119 ? 0.4248 0.4439 0.4885 -0.0864 0.1353  -0.1202 120 THR A CA  
1031 C CA  B THR A 119 ? 0.4336 0.4551 0.5010 -0.0846 0.1349  -0.1208 120 THR A CA  
1032 C C   A THR A 119 ? 0.4796 0.4781 0.5210 -0.0997 0.1484  -0.1239 120 THR A C   
1033 C C   B THR A 119 ? 0.4860 0.4865 0.5303 -0.0986 0.1483  -0.1246 120 THR A C   
1034 O O   A THR A 119 ? 0.4839 0.4818 0.5200 -0.1154 0.1629  -0.1351 120 THR A O   
1035 O O   B THR A 119 ? 0.4919 0.4937 0.5334 -0.1137 0.1630  -0.1366 120 THR A O   
1036 C CB  A THR A 119 ? 0.4257 0.4326 0.4677 -0.0910 0.1273  -0.1089 120 THR A CB  
1037 C CB  B THR A 119 ? 0.5020 0.5123 0.5491 -0.0873 0.1254  -0.1086 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.4679 0.4712 0.4995 -0.1085 0.1395  -0.1172 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4720 0.5007 0.5393 -0.0730 0.1123  -0.1045 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.3751 0.3538 0.3854 -0.0910 0.1199  -0.0940 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.5086 0.5148 0.5437 -0.1047 0.1356  -0.1151 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.4402 0.4217 0.4675 -0.0947 0.1440  -0.1156 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.4628 0.4246 0.4673 -0.1070 0.1553  -0.1191 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.5284 0.5052 0.5559 -0.1100 0.1706  -0.1369 121 CYS A C   
1045 O O   . CYS A 120 ? 0.5220 0.4911 0.5354 -0.1270 0.1858  -0.1465 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.4674 0.4125 0.4570 -0.1003 0.1469  -0.1084 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.5154 0.4405 0.4733 -0.1009 0.1317  -0.0906 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4840 0.4816 0.5462 -0.0933 0.1666  -0.1418 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4885 0.4859 0.5505 -0.0934 0.1667  -0.1418 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4887 0.5052 0.5809 -0.0911 0.1788  -0.1599 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4956 0.5113 0.5867 -0.0919 0.1794  -0.1601 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.5299 0.5651 0.6348 -0.1044 0.1917  -0.1757 122 ARG A C   
1053 C C   B ARG A 121 ? 0.5324 0.5675 0.6371 -0.1046 0.1919  -0.1759 122 ARG A C   
1054 O O   A ARG A 121 ? 0.5324 0.5709 0.6415 -0.1162 0.2091  -0.1916 122 ARG A O   
1055 O O   B ARG A 121 ? 0.5341 0.5728 0.6433 -0.1165 0.2094  -0.1918 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4902 0.5254 0.6166 -0.0677 0.1676  -0.1599 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.5082 0.5411 0.6328 -0.0687 0.1690  -0.1603 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.6464 0.6627 0.7640 -0.0561 0.1602  -0.1492 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6967 0.7110 0.8139 -0.0597 0.1664  -0.1540 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7971 0.8276 0.9472 -0.0345 0.1539  -0.1531 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.8337 0.8631 0.9856 -0.0395 0.1631  -0.1610 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.8671 0.8762 1.0049 -0.0234 0.1450  -0.1399 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.8954 0.9332 1.0585 -0.0217 0.1450  -0.1499 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 1.0091 1.0005 1.1394 -0.0243 0.1526  -0.1422 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 1.0314 1.0535 1.1873 -0.0082 0.1338  -0.1368 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.8878 0.8804 1.0215 -0.0353 0.1691  -0.1573 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.8485 0.8469 0.9884 -0.0101 0.1387  -0.1337 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.7926 0.7643 0.9112 -0.0156 0.1449  -0.1305 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.8315 0.8607 0.9947 0.0062  0.1183  -0.1274 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4724 0.5193 0.5822 -0.1040 0.1842  -0.1723 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4832 0.5485 0.6051 -0.1177 0.1959  -0.1874 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.5534 0.5934 0.6376 -0.1429 0.2113  -0.1890 123 LYS A C   
1073 O O   . LYS A 122 ? 0.5431 0.5928 0.6350 -0.1582 0.2296  -0.2070 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.4952 0.5779 0.6305 -0.1104 0.1830  -0.1827 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.7300 0.8431 0.9061 -0.0874 0.1705  -0.1864 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.8718 1.0027 1.0597 -0.0805 0.1571  -0.1824 123 LYS A CD  
1077 C CE  . LYS A 122 ? 1.0316 1.1875 1.2536 -0.0562 0.1425  -0.1836 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.1837 1.3720 1.4314 -0.0528 0.1358  -0.1921 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.5224 0.5295 0.5654 -0.1474 0.2038  -0.1710 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.5535 0.5304 0.5541 -0.1696 0.2156  -0.1697 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.6168 0.5831 0.6062 -0.1803 0.2312  -0.1795 124 PHE A C   
1082 O O   . PHE A 123 ? 0.6223 0.5779 0.5929 -0.2013 0.2490  -0.1897 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.5813 0.5278 0.5439 -0.1677 0.2008  -0.1483 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.6085 0.5535 0.5655 -0.1684 0.1930  -0.1411 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.6252 0.6006 0.6184 -0.1571 0.1861  -0.1449 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.6697 0.5814 0.5842 -0.1789 0.1910  -0.1299 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.6347 0.6083 0.6223 -0.1585 0.1795  -0.1391 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.6956 0.6039 0.6051 -0.1790 0.1843  -0.1238 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.6428 0.5824 0.5891 -0.1696 0.1794  -0.1289 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.5553 0.5243 0.5565 -0.1668 0.2259  -0.1776 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5755 0.5363 0.5696 -0.1756 0.2407  -0.1882 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.6586 0.6468 0.6869 -0.1820 0.2597  -0.2128 125 ILE A C   
1093 O O   . ILE A 124 ? 0.6826 0.6609 0.6937 -0.2022 0.2791  -0.2249 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.6013 0.5561 0.5985 -0.1598 0.2302  -0.1800 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.6045 0.5302 0.5615 -0.1602 0.2160  -0.1596 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.6407 0.5932 0.6406 -0.1667 0.2468  -0.1948 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.6659 0.5891 0.6290 -0.1431 0.2016  -0.1489 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.6131 0.6360 0.6885 -0.1656 0.2540  -0.2205 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.6180 0.6740 0.7342 -0.1680 0.2692  -0.2454 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.6802 0.7382 0.7856 -0.1933 0.2873  -0.2584 126 LYS A C   
1101 O O   . LYS A 125 ? 0.6750 0.7461 0.7946 -0.2065 0.3080  -0.2802 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.6313 0.7228 0.7963 -0.1437 0.2548  -0.2486 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.6372 0.6798 0.7156 -0.2011 0.2807  -0.2454 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.6651 0.7024 0.7264 -0.2263 0.2976  -0.2553 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.7754 0.7776 0.7903 -0.2514 0.3167  -0.2580 127 ALA A C   
1106 O O   . ALA A 126 ? 0.7836 0.7876 0.7937 -0.2741 0.3383  -0.2749 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.6664 0.6908 0.7078 -0.2260 0.2841  -0.2388 127 ALA A CB  
1108 N N   . SER A 127 ? 0.7865 0.7568 0.7657 -0.2485 0.3089  -0.2418 128 SER A N   
1109 C CA  . SER A 127 ? 0.8535 0.7873 0.7827 -0.2709 0.3236  -0.2417 128 SER A CA  
1110 C C   . SER A 127 ? 0.9555 0.8981 0.8969 -0.2784 0.3426  -0.2611 128 SER A C   
1111 O O   . SER A 127 ? 1.0078 0.9246 0.9106 -0.3015 0.3599  -0.2664 128 SER A O   
1112 C CB  . SER A 127 ? 0.9234 0.8199 0.8070 -0.2654 0.3056  -0.2165 128 SER A CB  
1113 O OG  . SER A 127 ? 1.0639 0.9368 0.9147 -0.2718 0.2983  -0.2026 128 SER A OG  
1114 N N   . GLU A 128 ? 0.8865 0.8636 0.8798 -0.2594 0.3399  -0.2720 129 GLU A N   
1115 C CA  . GLU A 128 ? 1.1172 1.1047 1.1278 -0.2635 0.3573  -0.2917 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.6728 1.6838 1.7060 -0.2829 0.3841  -0.3204 129 GLU A C   
1117 O O   . GLU A 128 ? 1.2707 1.2757 1.2862 -0.3023 0.3942  -0.3239 129 GLU A O   
1118 C CB  . GLU A 128 ? 1.1021 1.1127 1.1567 -0.2348 0.3440  -0.2919 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.1973 1.2530 1.3127 -0.2174 0.3399  -0.3053 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.4555 1.5279 1.6083 -0.1866 0.3228  -0.3011 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.3972 1.4457 1.5281 -0.1758 0.3082  -0.2817 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.3460 1.4554 1.5500 -0.1732 0.3236  -0.3178 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.2474 0.5083 0.3563 -0.0449 -0.0089 -0.0785 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2652 0.5261 0.3741 -0.0449 -0.0089 -0.0785 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.2367 0.4961 0.3442 -0.0442 -0.0086 -0.0796 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2639 0.5233 0.3714 -0.0442 -0.0086 -0.0795 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2969 0.5565 0.4060 -0.0442 -0.0095 -0.0792 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2990 0.5589 0.4084 -0.0443 -0.0094 -0.0791 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2987 0.5583 0.4095 -0.0445 -0.0107 -0.0787 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2920 0.5522 0.4031 -0.0448 -0.0105 -0.0785 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.2223 0.4791 0.3276 -0.0437 -0.0096 -0.0807 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.2576 0.5143 0.3629 -0.0436 -0.0096 -0.0806 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.2232 0.4794 0.3261 -0.0437 -0.0087 -0.0821 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2743 0.5308 0.3815 -0.0435 -0.0116 -0.0806 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2530 0.5093 0.3563 -0.0440 -0.0095 -0.0825 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.3136 0.5701 0.4230 -0.0439 -0.0129 -0.0809 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.2199 0.4753 0.3201 -0.0434 -0.0068 -0.0836 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2741 0.5308 0.3820 -0.0428 -0.0123 -0.0807 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2404 0.4963 0.3408 -0.0438 -0.0083 -0.0846 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.3092 0.5666 0.4214 -0.0436 -0.0142 -0.0815 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2555 0.5108 0.3539 -0.0435 -0.0065 -0.0855 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.3252 0.5829 0.4362 -0.0429 -0.0138 -0.0815 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.2283 0.4831 0.3277 -0.0430 -0.0053 -0.0837 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2869 0.5434 0.3938 -0.0421 -0.0119 -0.0805 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2515 0.5060 0.3469 -0.0432 -0.0045 -0.0880 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.3161 0.5753 0.4288 -0.0420 -0.0145 -0.0823 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.2419 0.4956 0.3387 -0.0428 -0.0033 -0.0856 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.3070 0.5644 0.4149 -0.0412 -0.0130 -0.0810 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2514 0.5051 0.3462 -0.0430 -0.0027 -0.0879 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.3137 0.5728 0.4243 -0.0411 -0.0141 -0.0820 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.2430 0.5028 0.3522 -0.0438 -0.0088 -0.0796 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.2346 0.4947 0.3453 -0.0437 -0.0097 -0.0799 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2697 0.5277 0.3790 -0.0424 -0.0098 -0.0800 2   VAL D C   
1157 O O   . VAL B 3   ? 0.2589 0.5157 0.3666 -0.0420 -0.0086 -0.0798 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2722 0.5360 0.3859 -0.0450 -0.0092 -0.0804 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2691 0.5357 0.3841 -0.0465 -0.0092 -0.0796 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2637 0.5296 0.3790 -0.0451 -0.0074 -0.0811 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.2425 0.5005 0.3525 -0.0417 -0.0109 -0.0804 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.2435 0.5000 0.3528 -0.0403 -0.0112 -0.0802 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2944 0.5524 0.4071 -0.0411 -0.0105 -0.0809 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2938 0.5540 0.4089 -0.0420 -0.0113 -0.0823 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.2738 0.5304 0.3827 -0.0390 -0.0129 -0.0809 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.2537 0.5109 0.3614 -0.0385 -0.0134 -0.0811 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2928 0.5481 0.4010 -0.0374 -0.0133 -0.0801 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.3159 0.5725 0.4211 -0.0381 -0.0132 -0.0800 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2822 0.5397 0.3957 -0.0410 -0.0089 -0.0804 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2867 0.5471 0.4055 -0.0419 -0.0081 -0.0817 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.3386 0.5984 0.4598 -0.0412 -0.0097 -0.0823 4   PRO D C   
1172 O O   . PRO B 5   ? 0.3205 0.5770 0.4389 -0.0395 -0.0108 -0.0810 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.3087 0.5684 0.4281 -0.0416 -0.0056 -0.0813 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.3609 0.6160 0.4749 -0.0402 -0.0059 -0.0793 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.3075 0.5625 0.4181 -0.0403 -0.0076 -0.0792 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.3228 0.5866 0.4497 -0.0425 -0.0100 -0.0846 5   ALA D N   
# 
