data_7GV4
# 
_entry.id   7GV4 
# 
_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   7GV4         pdb_00007gv4 10.2210/pdb7gv4/pdb 
WWPDB D_1001406675 ?            ?                   
# 
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                        7GV4 
_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   301 178 HOH   HOH A . 
F 6 HOH   2   302 7   HOH   HOH A . 
F 6 HOH   3   303 173 HOH   HOH A . 
F 6 HOH   4   304 166 HOH   HOH A . 
F 6 HOH   5   305 45  HOH   HOH A . 
F 6 HOH   6   306 140 HOH   HOH A . 
F 6 HOH   7   307 19  HOH   HOH A . 
F 6 HOH   8   308 90  HOH   HOH A . 
F 6 HOH   9   309 139 HOH   HOH A . 
F 6 HOH   10  310 247 HOH   HOH A . 
F 6 HOH   11  311 179 HOH   HOH A . 
F 6 HOH   12  312 94  HOH   HOH A . 
F 6 HOH   13  313 29  HOH   HOH A . 
F 6 HOH   14  314 84  HOH   HOH A . 
F 6 HOH   15  315 106 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 87  HOH   HOH A . 
F 6 HOH   19  319 42  HOH   HOH A . 
F 6 HOH   20  320 202 HOH   HOH A . 
F 6 HOH   21  321 47  HOH   HOH A . 
F 6 HOH   22  322 132 HOH   HOH A . 
F 6 HOH   23  323 99  HOH   HOH A . 
F 6 HOH   24  324 75  HOH   HOH A . 
F 6 HOH   25  325 101 HOH   HOH A . 
F 6 HOH   26  326 37  HOH   HOH A . 
F 6 HOH   27  327 119 HOH   HOH A . 
F 6 HOH   28  328 83  HOH   HOH A . 
F 6 HOH   29  329 17  HOH   HOH A . 
F 6 HOH   30  330 27  HOH   HOH A . 
F 6 HOH   31  331 237 HOH   HOH A . 
F 6 HOH   32  332 91  HOH   HOH A . 
F 6 HOH   33  333 40  HOH   HOH A . 
F 6 HOH   34  334 5   HOH   HOH A . 
F 6 HOH   35  335 6   HOH   HOH A . 
F 6 HOH   36  336 193 HOH   HOH A . 
F 6 HOH   37  337 117 HOH   HOH A . 
F 6 HOH   38  338 243 HOH   HOH A . 
F 6 HOH   39  339 34  HOH   HOH A . 
F 6 HOH   40  340 242 HOH   HOH A . 
F 6 HOH   41  341 244 HOH   HOH A . 
F 6 HOH   42  342 20  HOH   HOH A . 
F 6 HOH   43  343 30  HOH   HOH A . 
F 6 HOH   44  344 239 HOH   HOH A . 
F 6 HOH   45  345 85  HOH   HOH A . 
F 6 HOH   46  346 12  HOH   HOH A . 
F 6 HOH   47  347 50  HOH   HOH A . 
F 6 HOH   48  348 44  HOH   HOH A . 
F 6 HOH   49  349 14  HOH   HOH A . 
F 6 HOH   50  350 145 HOH   HOH A . 
F 6 HOH   51  351 122 HOH   HOH A . 
F 6 HOH   52  352 151 HOH   HOH A . 
F 6 HOH   53  353 24  HOH   HOH A . 
F 6 HOH   54  354 96  HOH   HOH A . 
F 6 HOH   55  355 175 HOH   HOH A . 
F 6 HOH   56  356 4   HOH   HOH A . 
F 6 HOH   57  357 124 HOH   HOH A . 
F 6 HOH   58  358 51  HOH   HOH A . 
F 6 HOH   59  359 89  HOH   HOH A . 
F 6 HOH   60  360 86  HOH   HOH A . 
F 6 HOH   61  361 93  HOH   HOH A . 
F 6 HOH   62  362 141 HOH   HOH A . 
F 6 HOH   63  363 207 HOH   HOH A . 
F 6 HOH   64  364 97  HOH   HOH A . 
F 6 HOH   65  365 196 HOH   HOH A . 
F 6 HOH   66  366 170 HOH   HOH A . 
F 6 HOH   67  367 76  HOH   HOH A . 
F 6 HOH   68  368 25  HOH   HOH A . 
F 6 HOH   69  369 103 HOH   HOH A . 
F 6 HOH   70  370 144 HOH   HOH A . 
F 6 HOH   71  371 167 HOH   HOH A . 
F 6 HOH   72  372 21  HOH   HOH A . 
F 6 HOH   73  373 177 HOH   HOH A . 
F 6 HOH   74  374 131 HOH   HOH A . 
F 6 HOH   75  375 15  HOH   HOH A . 
F 6 HOH   76  376 169 HOH   HOH A . 
F 6 HOH   77  377 180 HOH   HOH A . 
F 6 HOH   78  378 105 HOH   HOH A . 
F 6 HOH   79  379 192 HOH   HOH A . 
F 6 HOH   80  380 157 HOH   HOH A . 
F 6 HOH   81  381 23  HOH   HOH A . 
F 6 HOH   82  382 186 HOH   HOH A . 
F 6 HOH   83  383 28  HOH   HOH A . 
F 6 HOH   84  384 70  HOH   HOH A . 
F 6 HOH   85  385 32  HOH   HOH A . 
F 6 HOH   86  386 74  HOH   HOH A . 
F 6 HOH   87  387 55  HOH   HOH A . 
F 6 HOH   88  388 229 HOH   HOH A . 
F 6 HOH   89  389 133 HOH   HOH A . 
F 6 HOH   90  390 191 HOH   HOH A . 
F 6 HOH   91  391 194 HOH   HOH A . 
F 6 HOH   92  392 245 HOH   HOH A . 
F 6 HOH   93  393 108 HOH   HOH A . 
F 6 HOH   94  394 241 HOH   HOH A . 
F 6 HOH   95  395 165 HOH   HOH A . 
F 6 HOH   96  396 129 HOH   HOH A . 
F 6 HOH   97  397 205 HOH   HOH A . 
F 6 HOH   98  398 39  HOH   HOH A . 
F 6 HOH   99  399 16  HOH   HOH A . 
F 6 HOH   100 400 92  HOH   HOH A . 
F 6 HOH   101 401 22  HOH   HOH A . 
F 6 HOH   102 402 176 HOH   HOH A . 
F 6 HOH   103 403 67  HOH   HOH A . 
F 6 HOH   104 404 212 HOH   HOH A . 
F 6 HOH   105 405 35  HOH   HOH A . 
F 6 HOH   106 406 185 HOH   HOH A . 
F 6 HOH   107 407 174 HOH   HOH A . 
F 6 HOH   108 408 190 HOH   HOH A . 
F 6 HOH   109 409 69  HOH   HOH A . 
F 6 HOH   110 410 26  HOH   HOH A . 
F 6 HOH   111 411 46  HOH   HOH A . 
F 6 HOH   112 412 120 HOH   HOH A . 
F 6 HOH   113 413 43  HOH   HOH A . 
F 6 HOH   114 414 36  HOH   HOH A . 
F 6 HOH   115 415 236 HOH   HOH A . 
F 6 HOH   116 416 64  HOH   HOH A . 
F 6 HOH   117 417 82  HOH   HOH A . 
F 6 HOH   118 418 223 HOH   HOH A . 
F 6 HOH   119 419 60  HOH   HOH A . 
F 6 HOH   120 420 56  HOH   HOH A . 
F 6 HOH   121 421 88  HOH   HOH A . 
F 6 HOH   122 422 204 HOH   HOH A . 
F 6 HOH   123 423 215 HOH   HOH A . 
F 6 HOH   124 424 57  HOH   HOH A . 
F 6 HOH   125 425 110 HOH   HOH A . 
F 6 HOH   126 426 214 HOH   HOH A . 
F 6 HOH   127 427 65  HOH   HOH A . 
F 6 HOH   128 428 95  HOH   HOH A . 
F 6 HOH   129 429 68  HOH   HOH A . 
F 6 HOH   130 430 147 HOH   HOH A . 
F 6 HOH   131 431 135 HOH   HOH A . 
F 6 HOH   132 432 61  HOH   HOH A . 
F 6 HOH   133 433 41  HOH   HOH A . 
F 6 HOH   134 434 116 HOH   HOH A . 
F 6 HOH   135 435 168 HOH   HOH A . 
F 6 HOH   136 436 200 HOH   HOH A . 
F 6 HOH   137 437 187 HOH   HOH A . 
F 6 HOH   138 438 123 HOH   HOH A . 
F 6 HOH   139 439 227 HOH   HOH A . 
F 6 HOH   140 440 248 HOH   HOH A . 
F 6 HOH   141 441 228 HOH   HOH A . 
F 6 HOH   142 442 63  HOH   HOH A . 
F 6 HOH   143 443 121 HOH   HOH A . 
F 6 HOH   144 444 231 HOH   HOH A . 
F 6 HOH   145 445 225 HOH   HOH A . 
F 6 HOH   146 446 171 HOH   HOH A . 
F 6 HOH   147 447 71  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   151 451 158 HOH   HOH A . 
F 6 HOH   152 452 125 HOH   HOH A . 
F 6 HOH   153 453 181 HOH   HOH A . 
F 6 HOH   154 454 217 HOH   HOH A . 
F 6 HOH   155 455 235 HOH   HOH A . 
F 6 HOH   156 456 246 HOH   HOH A . 
F 6 HOH   157 457 81  HOH   HOH A . 
F 6 HOH   158 458 114 HOH   HOH A . 
F 6 HOH   159 459 238 HOH   HOH A . 
F 6 HOH   160 460 79  HOH   HOH A . 
F 6 HOH   161 461 58  HOH   HOH A . 
F 6 HOH   162 462 183 HOH   HOH A . 
F 6 HOH   163 463 221 HOH   HOH A . 
F 6 HOH   164 464 188 HOH   HOH A . 
F 6 HOH   165 465 115 HOH   HOH A . 
F 6 HOH   166 466 107 HOH   HOH A . 
F 6 HOH   167 467 216 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   171 471 213 HOH   HOH A . 
F 6 HOH   172 472 113 HOH   HOH A . 
F 6 HOH   173 473 148 HOH   HOH A . 
F 6 HOH   174 474 48  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 73  HOH   HOH D . 
G 6 HOH   5   205 53  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           7GV4 
_cell.length_a           67.760 
_cell.length_b           67.760 
_cell.length_c           166.730 
_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                         7GV4 
_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          7GV4 
_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   66.28 
_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                     7GV4 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.980 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23773 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.086 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.100 
_reflns.B_iso_Wilson_estimate        33.470 
_reflns.pdbx_redundancy              9.000 
_reflns.pdbx_Rrim_I_all              0.092 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     214806 
_reflns.pdbx_scaling_rejects         782 
_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  ? 11952 1287 ? 1.873 ? ? ? 9.300 ? 1.100  ? ? ? ? ? ? 100.000 1.983 0.643 0.628 ? 
1 2 9.090 33.980 ? 1500  234  ? 0.045 ? ? ? 6.400 ? 32.100 ? ? ? ? ? ? 98.800  0.049 0.019 0.997 ? 
# 
_refine.entry_id                                 7GV4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             33.9800 
_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                     23696 
_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                       0.2040 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1500 
_refine.ls_number_reflns_R_free                  1221 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               39.1900 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.0447 
_refine.aniso_B[2][2]                            -0.0447 
_refine.aniso_B[3][3]                            0.0893 
_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               0.9630 
_refine.correlation_coeff_Fo_to_Fc_free          0.9490 
_refine.overall_SU_R_Cruickshank_DPI             0.0850 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0860 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0970 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0940 
_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                                130.660 
_refine.B_iso_min                                20.650 
_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                        7GV4 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.230 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.7500 
_refine_hist.d_res_low                        33.9800 
_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           33.85 
_refine_hist.pdbx_B_iso_mean_solvent          57.56 
_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      1633 ?      ? 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           ?    3.320  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.760 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.7500 
_refine_ls_shell.d_res_low                        1.8300 
_refine_ls_shell.pdbx_total_number_of_bins_used   12 
_refine_ls_shell.percent_reflns_obs               99.6800 
_refine_ls_shell.number_reflns_R_work             2682 
_refine_ls_shell.R_factor_all                     0.2953 
_refine_ls_shell.R_factor_R_work                  0.2944 
_refine_ls_shell.R_factor_R_free                  0.3135 
_refine_ls_shell.percent_reflns_R_free            4.6900 
_refine_ls_shell.number_reflns_R_free             132 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2814 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GV4 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 16.25 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GV4 
_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 7GV4       7GV4   ? 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 7GV4 A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GV4 D 1 ? 6   ? 7GV4   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 7GV4 GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GV4 PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GV4 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)' 7410  ? 
1 MORE         -65   ? 
1 'SSA (A^2)'  13010 ? 
# 
_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 33.8800000000 0.8660254038 
-0.5000000000 0.0000000000 -58.6818813604 0.0000000000 0.0000000000 -1.0000000000 27.7883333333 
# 
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                   7GV4 
_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 61.83   -121.23 
2 1 SER A 39  ? B 38.12   65.16   
3 1 ARG A 40  ? B 75.80   -22.31  
4 1 SER A 93  ? A 76.57   -5.38   
5 1 MET A 114 ? ? -115.64 79.97   
# 
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 366 ? F HOH . 
2 1 A HOH 376 ? F HOH . 
3 1 A HOH 455 ? F HOH . 
4 1 A HOH 462 ? 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 0.0157  -0.0518 -0.0724 -0.0390 0.0310  -0.0251 1.0428 1.8624  2.0302 
0.4387  -0.2988 1.1848 0.1339 -0.0745 -0.0594 -0.0563 0.1087 0.0961 0.2725  0.0014 -0.0076 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1191 0.1337  -0.0512 -0.0288 -0.0242 -0.0899 0.9787 -0.3550 0.0000 
-0.0249 -0.1186 0.0548 0.0222 -0.0065 -0.0157 0.0019  0.0097 0.0245 -0.0239 0.0032 -0.0153 
# 
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                    7GV4 
_atom_sites.fract_transf_matrix[1][1]   0.014758 
_atom_sites.fract_transf_matrix[1][2]   0.008521 
_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]   0.017041 
_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]   0.005998 
_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   ? 17.298 -21.299 -4.821 1.00 69.11  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.220 -22.172 -5.548 1.00 67.99  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.767 -23.653 -5.505 1.00 67.45  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.701 -23.965 -4.962 1.00 68.16  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.651 -22.018 -4.976 1.00 68.75  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.748 -22.043 -6.029 1.00 83.28  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.887 -23.081 -6.725 1.00 83.72  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.477 -21.031 -6.151 1.00 90.94  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.573 -24.553 -6.093 1.00 58.78  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.326 -25.994 -6.098 1.00 56.16  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.325 -26.717 -5.141 1.00 52.04  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.645 -27.888 -5.341 1.00 51.16  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.423 -26.538 -7.519 1.00 62.18  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.700 -26.289 -8.084 1.00 73.79  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.787 -26.018 -4.090 1.00 43.59  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.733 -26.570 -3.117 1.00 40.43  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.111 -27.722 -2.309 1.00 39.99  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.892 -27.765 -2.137 1.00 40.21  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.213 -25.467 -2.171 1.00 41.55  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.384 -24.282 -2.901 1.00 46.85  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.947 -28.626 -1.789 1.00 30.92  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.569 -29.615 -0.776 1.00 28.30  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.187 -29.088 0.520  1.00 29.73  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.146 -28.312 0.463  1.00 28.59  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.924 -31.091 -1.086 1.00 31.00  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.442 -31.260 -1.337 1.00 30.53  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.097 -31.603 -2.265 1.00 30.51  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.936 -32.704 -1.574 1.00 34.93  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.702 -29.510 1.695  0.66 24.66  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.578 -29.429 1.654  0.34 25.75  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.268 -29.026 2.957  0.66 24.12  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 20.989 -28.941 2.955  0.34 24.98  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.625 -30.171 3.893  0.66 27.28  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.398 -30.070 3.881  0.34 28.89  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.875 -31.140 3.976  0.66 27.06  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.700 -31.077 3.972  0.34 28.98  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.294 -28.032 3.640  0.66 25.69  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.850 -28.123 3.572  0.34 26.26  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.687 -27.645 5.083  0.66 26.45  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.329 -27.106 4.601  0.34 31.70  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.064 -26.375 5.601  0.66 49.29  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.605 -27.245 5.915  0.34 42.71  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.394 -25.635 4.882  0.66 45.51  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.385 -27.440 5.968  0.34 33.11  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.308 -26.078 6.871  0.66 44.45  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.346 -27.129 7.008  0.34 39.47  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.767 -30.069 4.583  0.66 24.21  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.527 -29.895 4.568  0.34 25.40  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.157 -31.082 5.566  0.66 23.80  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.050 -30.872 5.520  0.34 25.23  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.683 -30.588 6.931  0.66 26.47  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.562 -30.435 6.884  0.34 27.62  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.272 -29.649 7.499  0.66 24.94  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.999 -29.392 7.399  0.34 26.67  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.674 -31.374 5.529  0.66 24.74  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.586 -30.960 5.411  0.34 26.66  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 25.051 -32.583 6.354  0.66 25.77  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.044 -31.748 4.202  0.34 29.07  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.680 -33.865 5.953  0.66 29.36  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.772 -31.300 2.911  0.34 32.78  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.805 -32.445 7.513  0.66 26.79  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.737 -32.942 4.352  0.34 32.28  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 25.020 -34.982 6.729  0.66 30.32  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.188 -32.030 1.794  0.34 33.86  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.132 -33.555 8.293  0.66 29.07  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.153 -33.674 3.229  0.34 35.80  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.753 -34.816 7.891  0.66 27.87  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.872 -33.213 1.962  0.34 33.65  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.585 -31.186 7.433  1.00 24.27  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.919 -30.811 8.699  1.00 24.75  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.887 -30.558 9.878  1.00 26.41  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.757 -29.539 10.568 1.00 26.15  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.847 -31.843 9.076  1.00 32.43  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.947 -32.000 7.963  1.00 32.35  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.039 -31.431 10.330 1.00 36.14  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.814 -31.491 10.109 1.00 24.59  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.733 -31.393 11.261 1.00 25.68  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.990 -30.517 11.052 1.00 26.93  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.827 -30.453 11.964 1.00 25.29  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.166 -32.813 11.682 1.00 30.17  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.044 -33.750 12.176 1.00 41.00  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.460 -33.337 13.515 1.00 63.85  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.424 -33.452 14.614 1.00 76.91  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.309 -32.824 15.780 1.00 87.74  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.225 -32.992 16.723 1.00 75.62  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.284 -32.011 16.007 1.00 70.40  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.151 -29.875 9.880  1.00 23.07  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.387 -29.138 9.586  1.00 22.59  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.670 -28.038 10.614 1.00 24.51  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.801 -27.976 11.124 1.00 24.11  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.375 -28.552 8.161  1.00 22.80  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.644 -27.817 7.839  1.00 24.86  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.828 -28.494 7.655  1.00 25.72  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.872 -26.488 7.709  1.00 25.28  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.739 -27.570 7.399  1.00 25.51  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.208 -26.345 7.421  1.00 25.10  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.672 -27.157 10.894 1.00 22.45  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.904 -26.033 11.835 1.00 22.07  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.324 -26.535 13.227 1.00 25.03  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.256 -25.977 13.819 1.00 21.85  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.673 -25.121 11.917 1.00 23.18  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.656 -27.587 13.724 0.42 23.69  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.655 -27.592 13.729 0.30 23.18  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.654 -27.588 13.739 0.28 23.20  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.938 -28.208 15.019 0.42 23.83  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.941 -28.212 15.027 0.30 23.20  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.965 -28.176 15.047 0.28 23.25  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.355 -28.783 15.044 0.42 26.96  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.348 -28.805 15.055 0.30 26.97  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.357 -28.808 15.064 0.28 27.04  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.088 -28.570 16.019 0.42 24.29  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.064 -28.636 16.050 0.30 25.11  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.076 -28.660 16.058 0.28 25.27  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.904 -29.291 15.320 0.42 27.51  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.906 -29.287 15.349 0.30 26.45  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.894 -29.179 15.468 0.28 26.65  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.110 -29.881 16.592 0.42 32.19  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.599 -28.742 15.428 0.30 29.97  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.834 -30.286 14.585 0.28 30.81  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.753 -29.476 13.955 1.00 24.24  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.087 -30.088 13.818 1.00 25.38  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.162 -28.986 13.792 1.00 25.55  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.203 -29.127 14.425 1.00 24.77  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.151 -30.940 12.544 1.00 27.56  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.354 -32.244 12.631 1.00 39.90  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.808 -32.541 13.723 1.00 37.53  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.270 -32.960 11.607 1.00 42.19  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.895 -27.873 13.078 1.00 21.87  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.847 -26.757 13.044 1.00 21.68  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.052 -26.206 14.467 1.00 24.61  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.182 -26.037 14.921 1.00 22.88  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.368 -25.642 12.067 1.00 23.76  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.127 -24.336 12.285 1.00 23.79  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.446 -26.103 10.606 1.00 23.14  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.956 -25.974 15.188 1.00 21.95  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.065 -25.405 16.530 1.00 22.53  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.797 -26.361 17.486 1.00 23.74  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.650 -25.909 18.267 1.00 22.97  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.682 -25.021 17.063 1.00 23.39  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.709 -24.101 18.315 1.00 26.98  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.294 -22.713 17.994 1.00 27.30  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.308 -23.929 18.877 1.00 31.39  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.508 -27.667 17.377 1.00 22.94  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.182 -28.692 18.178 1.00 23.74  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.702 -28.613 17.935 1.00 25.81  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.484 -28.604 18.904 1.00 24.79  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.637 -30.084 17.812 1.00 25.59  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.194 -31.251 18.628 1.00 33.99  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.737 -31.156 20.093 1.00 36.00  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.689 -32.566 18.067 1.00 39.01  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.120 -28.478 16.654 1.00 23.06  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.540 -28.364 16.312 1.00 22.54  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.166 -27.069 16.816 1.00 25.48  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.302 -27.084 17.280 1.00 24.83  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.763 -28.576 14.832 1.00 26.56  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.719 -30.045 14.475 1.00 33.99  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.969 -30.927 15.316 1.00 31.67  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.388 -30.342 13.225 1.00 28.09  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.428 -25.947 16.721 1.00 21.94  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.901 -24.665 17.264 1.00 22.61  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.121 -24.815 18.774 1.00 24.35  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.113 -24.305 19.305 1.00 23.77  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.907 -23.524 16.963 1.00 22.97  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.786 -23.130 15.469 1.00 26.34  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.664 -22.099 15.262 1.00 27.23  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.113 -22.609 14.897 1.00 26.93  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.197 -25.512 19.480 1.00 22.30  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.371 -25.729 20.928 1.00 23.23  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.601 -26.619 21.237 1.00 26.93  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.279 -26.385 22.236 1.00 28.19  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.113 -26.319 21.562 1.00 23.91  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.134 -26.182 23.074 1.00 31.48  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.675 -25.222 23.634 1.00 29.27  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.554 -27.144 23.756 1.00 32.01  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.893 -27.629 20.378 1.00 24.74  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.090 -28.486 20.536 1.00 25.92  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.347 -27.631 20.379 1.00 29.64  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.309 -27.811 21.124 1.00 29.44  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 37.096 -29.608 19.490 1.00 25.42  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 36.071 -30.699 19.806 1.00 28.80  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.878 -31.634 18.614 1.00 32.47  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 35.033 -32.766 18.980 1.00 39.34  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.382 -33.537 18.117 1.00 54.95  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.435 -33.282 16.814 1.00 42.84  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.660 -34.559 18.549 1.00 46.65  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.330 -26.668 19.434 1.00 26.43  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.466 -25.760 19.265 1.00 25.97  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.621 -24.886 20.513 1.00 29.51  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.749 -24.700 20.994 1.00 29.74  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.263 -24.851 18.056 1.00 25.57  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.278 -25.527 16.674 1.00 29.88  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.152 -24.476 15.570 1.00 30.21  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.558 -26.373 16.471 1.00 30.39  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.493 -24.370 21.051 1.00 25.39  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.563 -23.575 22.284 1.00 26.21  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.187 -24.408 23.448 1.00 31.66  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 40.075 -23.897 24.157 1.00 32.55  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.171 -23.062 22.693 1.00 27.35  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.283 -22.163 23.935 1.00 31.33  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.975 -21.557 24.344 1.00 35.50  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.975 -22.561 24.700 1.00 31.87  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.340 -22.615 25.869 1.00 41.37  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.656 -21.768 26.846 1.00 37.66  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.410 -23.531 26.080 1.00 32.96  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.710 -25.650 23.645 0.39 29.53  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.711 -25.659 23.628 0.28 29.29  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.709 -25.650 23.647 0.33 29.64  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.180 -26.550 24.708 0.39 30.86  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.161 -26.612 24.654 0.28 30.54  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.178 -26.553 24.706 0.33 31.06  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.691 -26.809 24.640 0.39 36.73  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.675 -26.810 24.627 0.28 36.48  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.690 -26.809 24.638 0.33 36.76  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.339 -26.907 25.684 0.39 37.65  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.305 -26.886 25.683 0.28 37.33  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.336 -26.910 25.683 0.33 37.64  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.401 -27.861 24.693 0.39 34.34  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.490 -27.967 24.448 0.28 33.83  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.412 -27.871 24.665 0.33 34.93  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.799 -28.723 23.639 0.39 40.08  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.156 -27.993 24.922 0.28 39.23  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.813 -28.736 25.716 0.33 43.87  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.250 -26.892 23.415 1.00 33.22  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.687 -27.124 23.200 1.00 34.82  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.483 -25.828 23.003 1.00 37.16  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.687 -25.876 22.732 1.00 37.86  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.871 -28.100 22.033 1.00 36.58  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.170 -29.436 22.273 1.00 42.95  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.110 -30.282 21.023 1.00 48.43  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.451 -30.623 20.547 1.00 62.70  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.759 -30.802 19.269 1.00 79.09  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 45.004 -31.090 18.915 1.00 69.13  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.833 -30.663 18.333 1.00 64.63  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.810 -24.670 23.168 1.00 30.99  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.384 -23.333 23.020 1.00 31.83  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.991 -23.115 21.608 1.00 36.73  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 45.049 -22.504 21.466 1.00 38.48  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.415 -23.045 24.149 1.00 35.06  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.724 -21.573 24.314 1.00 46.03  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.798 -20.745 24.118 1.00 44.17  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.890 -21.244 24.629 1.00 52.31  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.325 -23.628 20.571 1.00 30.69  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.841 -23.522 19.203 1.00 30.16  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.235 -22.322 18.495 1.00 32.82  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 42.006 -22.197 18.418 1.00 29.29  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.635 -24.835 18.404 1.00 33.05  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.416 -26.011 19.050 1.00 34.99  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.999 -24.643 16.905 1.00 32.30  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.991 -27.405 18.548 1.00 39.29  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.113 -21.439 17.980 1.00 31.11  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.742 -20.242 17.221 1.00 30.95  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.829 -19.261 17.979 1.00 32.56  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.215 -18.398 17.353 1.00 31.11  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.162 -20.582 15.844 1.00 31.73  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.205 -21.113 14.818 1.00 39.63  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.604 -21.209 13.481 1.00 40.44  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.415 -20.212 14.715 1.00 46.38  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.810 -19.337 19.320 1.00 29.02  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.132 -18.335 20.148 1.00 28.52  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.957 -17.047 19.955 1.00 35.02  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.192 -17.102 19.842 1.00 35.21  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 42.037 -18.776 21.608 1.00 33.00  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.350 -19.110 22.048 1.00 34.46  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.067 -19.977 21.800 1.00 29.86  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.283 -15.914 19.802 1.00 31.47  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.962 -14.662 19.468 1.00 31.94  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.628 -13.518 20.383 1.00 33.02  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.991 -12.376 20.103 1.00 33.37  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.670 -14.299 17.998 1.00 33.35  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.194 -14.286 17.608 1.00 42.12  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.333 -14.439 18.508 1.00 36.88  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.903 -14.128 16.409 1.00 52.71  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.942 -13.806 21.491 1.00 27.05  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.636 -12.755 22.457 1.00 26.60  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.476 -13.346 23.850 1.00 29.64  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 41.070 -14.512 23.996 1.00 28.98  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.374 -11.914 22.021 1.00 29.24  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 39.063 -12.691 22.191 1.00 27.29  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.300 -10.558 22.753 1.00 29.82  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.787 -12.533 24.868 0.60 26.93  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.787 -12.546 24.876 0.40 26.46  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.572 -12.852 26.274 0.60 26.81  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.532 -12.921 26.256 0.40 26.11  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.501 -11.869 26.757 0.60 29.92  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.556 -11.894 26.846 0.40 29.91  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.628 -10.661 26.526 0.60 29.64  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.772 -10.685 26.723 0.40 30.10  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.874 -12.732 27.122 0.60 32.22  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.788 -13.218 27.127 0.40 30.96  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.606 -12.961 28.613 0.60 32.53  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.622 -11.970 27.395 0.40 31.63  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.946 -13.688 26.622 0.60 32.72  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.403 -13.904 28.433 0.40 31.03  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.442 -12.385 27.392 1.00 25.90  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.389 -11.559 27.993 1.00 26.13  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.679 -11.582 29.489 1.00 31.37  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.675 -12.664 30.105 1.00 30.63  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.943 -12.051 27.673 1.00 27.59  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.672 -12.203 26.145 1.00 26.54  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.908 -11.138 28.322 1.00 28.92  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.992 -10.943 25.242 1.00 27.60  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.911 -10.398 30.067 1.00 28.09  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.213 -10.270 31.495 1.00 28.78  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.942 -9.855  32.234 1.00 33.24  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.329 -8.834  31.897 1.00 31.92  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.398 -9.300  31.762 1.00 33.61  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.705 -9.190  33.262 1.00 34.38  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.648 -9.735  31.006 1.00 34.32  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.559 -10.644 33.254 1.00 30.39  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.361 -10.418 34.064 1.00 30.67  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.842 -10.467 35.500 1.00 38.02  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 37.018 -11.550 36.062 1.00 35.23  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.243 -11.450 33.750 1.00 34.14  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.931 -11.037 34.404 1.00 34.26  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 35.060 -11.619 32.239 1.00 33.07  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.166 -9.294  36.068 0.54 38.66  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.053 -9.266  36.072 0.46 37.73  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.743 -9.155  37.413 0.54 40.45  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.577 -9.006  37.412 0.46 39.22  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.121 -9.884  37.455 0.54 41.87  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.684 -10.008 37.778 0.46 41.84  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 39.989 -9.572  36.636 0.54 40.74  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.510 -10.890 38.625 0.46 41.44  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.780 -9.659  38.492 0.54 46.76  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.457 -8.916  38.441 0.46 44.25  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.476 -9.115  38.352 0.54 60.96  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.781 -7.678  38.288 0.46 52.99  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.288 -10.880 38.352 0.54 37.51  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.788 -9.902  37.012 0.46 36.64  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.522 -11.655 38.520 0.54 37.76  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 41.041 -10.663 37.055 0.46 36.91  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.633 -12.829 37.545 0.54 40.25  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.922 -12.082 36.458 0.46 38.97  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.670 -13.501 37.521 0.54 39.83  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.945 -12.604 36.006 0.46 38.95  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.648 -12.167 39.972 0.54 38.50  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.696 -10.674 38.449 0.46 38.97  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 41.083 -11.106 40.969 0.54 46.12  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.179 -9.285  38.872 0.46 50.44  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.403 -11.726 42.316 0.54 45.60  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.170 -9.328  40.015 0.46 58.92  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.609 -10.714 43.350 0.54 50.13  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.630 -7.987  40.385 0.46 66.57  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.783 -10.166 43.652 0.54 64.38  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.063 -7.227  41.318 0.46 78.35  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.868 -9.259  44.613 0.54 52.18  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 42.001 -7.661  41.985 0.46 64.23  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.878 -10.513 42.988 0.54 51.31  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.552 -6.024  41.588 0.46 64.32  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.566 -13.097 36.765 0.54 35.61  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.696 -12.674 36.386 0.46 34.82  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.540 -14.220 35.823 0.54 34.77  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.460 -13.998 35.769 0.46 34.12  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.832 -13.813 34.384 0.54 36.96  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.607 -13.866 34.247 0.46 36.39  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.520 -12.697 33.970 0.54 34.82  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 39.004 -12.969 33.655 0.46 33.38  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.201 -14.987 35.903 0.54 35.88  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.073 -14.559 36.140 0.46 35.38  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.903 -15.582 37.273 0.54 52.03  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.982 -15.075 37.568 0.46 49.51  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.212 -17.059 37.415 0.54 88.45  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.193 -16.569 37.704 0.46 84.05  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.513 -17.881 36.778 0.54 88.89  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.216 -16.970 38.306 0.46 85.05  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.148 -17.397 38.177 0.54 89.01  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.339 -17.341 37.209 0.46 85.20  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.398 -14.758 33.613 1.00 33.20  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.726 -14.634 32.199 1.00 32.20  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.090 -15.751 31.399 1.00 34.07  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.128 -16.899 31.838 1.00 34.34  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.251 -14.664 32.023 1.00 34.86  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.956 -13.433 32.575 1.00 49.62  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.425 -13.345 32.231 1.00 70.39  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.998 -14.174 31.504 1.00 62.41  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 45.069 -12.317 32.755 1.00 72.76  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.492 -15.419 30.241 1.00 27.51  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.834 -16.414 29.369 1.00 27.68  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.347 -16.239 27.965 1.00 31.68  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.214 -15.145 27.406 1.00 32.01  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.302 -16.234 29.384 1.00 28.77  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.677 -16.353 30.752 1.00 30.59  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.555 -15.237 31.581 1.00 33.03  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.223 -17.581 31.221 1.00 33.61  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 35.995 -15.349 32.855 1.00 35.32  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.663 -17.691 32.501 1.00 37.25  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.558 -16.574 33.309 1.00 34.89  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.955 -17.292 27.389 1.00 28.37  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.469 -17.228 26.024 1.00 26.90  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.340 -17.630 25.073 1.00 29.59  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.529 -18.509 25.395 1.00 28.35  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.690 -18.153 25.836 1.00 29.74  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.916 -17.731 26.693 1.00 34.91  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.237 -18.100 26.032 1.00 45.88  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.241 -17.685 24.625 1.00 56.56  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.866 -16.619 24.138 1.00 69.27  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.638 -15.877 24.920 1.00 63.18  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.767 -16.318 22.852 1.00 49.73  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.251 -16.968 23.920 1.00 26.49  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.178 -17.282 22.960 1.00 26.40  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.548 -16.846 21.553 1.00 27.66  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.639 -16.322 21.319 1.00 26.13  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.863 -16.621 23.388 1.00 27.07  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.652 -17.141 20.596 1.00 24.70  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.821 -16.725 19.210 1.00 23.49  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.948 -15.482 19.020 1.00 26.43  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.739 -15.522 19.304 1.00 25.04  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.358 -17.850 18.250 1.00 22.64  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.128 -19.128 18.434 1.00 26.18  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.643 -20.162 19.237 1.00 27.82  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.356 -19.471 17.973 1.00 27.57  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.575 -21.111 19.202 1.00 28.01  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.633 -20.732 18.467 1.00 27.79  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.552 -14.382 18.545 1.00 25.29  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.814 -13.129 18.296 1.00 24.74  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.577 -13.380 17.420 1.00 26.94  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.519 -12.855 17.732 1.00 24.30  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.712 -12.099 17.587 1.00 26.79  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.696 -11.454 18.538 1.00 27.29  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.625 -10.530 17.741 1.00 27.17  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.737 -10.086 18.637 1.00 35.55  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.715 -9.273  17.890 1.00 34.44  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.693 -14.210 16.372 1.00 24.01  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.559 -14.427 15.461 1.00 23.37  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.377 -15.073 16.144 1.00 25.14  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.241 -14.704 15.874 1.00 25.66  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.973 -15.190 14.209 1.00 31.65  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.585 -16.405 14.629 1.00 32.12  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.889 -14.368 13.309 1.00 34.01  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.636 -16.032 17.026 1.00 21.79  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.549 -16.715 17.743 1.00 21.90  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.878 -15.739 18.707 1.00 24.66  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.638 -15.705 18.796 1.00 22.81  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 33.053 -17.994 18.460 1.00 23.89  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.944 -18.599 19.340 1.00 24.74  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.527 -19.029 17.424 1.00 23.67  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.684 -14.956 19.448 1.00 22.33  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.110 -13.949 20.351 1.00 21.66  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.205 -12.964 19.589 1.00 24.70  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.096 -12.663 20.046 1.00 24.28  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.231 -13.170 21.068 1.00 21.47  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.192 -13.966 21.980 1.00 25.38  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.228 -13.019 22.615 1.00 25.40  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.423 -14.706 23.078 1.00 27.45  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.672 -12.481 18.433 1.00 22.29  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.903 -11.564 17.590 1.00 23.85  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.613 -12.199 17.088 1.00 28.40  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.572 -11.536 17.074 1.00 28.70  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.723 -11.093 16.392 1.00 25.50  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.912 -10.261 16.776 1.00 27.86  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.940 -10.167 15.309 1.00 32.64  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.128 -8.868  14.479 1.00 28.86  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.666 -13.493 16.714 1.00 24.85  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.500 -14.212 16.203 1.00 24.18  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.397 -14.419 17.277 1.00 26.77  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.239 -14.637 16.925 1.00 28.63  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.931 -15.558 15.602 1.00 24.97  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.769 -14.364 18.576 1.00 23.07  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.856 -14.623 19.688 1.00 23.08  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.409 -13.404 20.473 1.00 27.04  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.449 -13.525 21.241 1.00 25.52  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.502 -15.629 20.640 1.00 23.25  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.871 -17.224 19.889 1.00 26.87  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.163 -12.292 20.392 1.00 23.44  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.958 -11.151 21.286 1.00 22.22  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.972 -9.840  20.546 1.00 27.14  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.940 -9.552  19.823 1.00 25.69  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.077 -11.180 22.329 1.00 23.87  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.403 -9.938  22.936 1.00 26.97  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.932 -9.034  20.760 1.00 25.53  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.850 -7.693  20.176 1.00 25.35  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.970 -6.795  20.673 1.00 28.64  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.508 -5.981  19.904 1.00 28.69  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.382 -6.979  21.949 1.00 26.28  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.492 -6.207  22.517 1.00 27.29  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.830 -6.547  21.825 1.00 29.04  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.510 -5.623  21.357 1.00 27.84  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.594 -6.371  24.050 1.00 27.65  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.653 -5.494  24.731 1.00 31.98  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.226 -4.006  24.769 1.00 33.09  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.962 -6.003  26.124 1.00 30.13  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.174 -7.854  21.705 1.00 24.21  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.433 -8.223  21.028 1.00 23.54  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.409 -7.878  19.554 1.00 27.92  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.441 -7.502  19.008 1.00 27.11  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.823 -9.677  21.275 1.00 24.19  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.232 -9.922  22.711 1.00 25.20  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.311 -9.237  23.277 1.00 28.00  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.554 -10.854 23.495 1.00 26.63  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.674 -9.449  24.622 1.00 28.95  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.958 -11.109 24.814 1.00 29.50  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 32.994 -10.387 25.375 1.00 27.53  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.227 -7.953  18.917 1.00 25.41  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.105 -7.553  17.508 1.00 26.30  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.533 -6.087  17.347 1.00 30.22  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.350 -5.785  16.472 1.00 28.88  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.660 -7.782  17.038 1.00 28.22  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.400 -7.255  15.650 1.00 32.17  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 29.005 -7.836  14.538 1.00 34.24  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.544 -6.179  15.445 1.00 36.18  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.772 -7.345  13.251 1.00 37.51  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.299 -5.686  14.168 1.00 39.33  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.899 -6.286  13.075 1.00 45.72  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.635 -5.797  11.829 1.00 50.58  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.999 -5.188  18.204 0.53 27.50  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.999 -5.193  18.207 0.47 27.51  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.328 -3.757  18.198 0.53 28.85  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.324 -3.763  18.216 0.47 28.83  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.818 -3.520  18.508 0.53 33.83  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.823 -3.553  18.481 0.47 33.62  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.457 -2.713  17.835 0.53 35.74  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.470 -2.800  17.755 0.47 35.19  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.443 -3.016  19.195 0.53 31.64  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.500 -3.051  19.286 0.47 31.72  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 28.098 -3.013  18.745 0.53 36.26  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.782 -1.661  19.297 0.47 38.74  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.371 -4.240  19.500 1.00 29.65  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.788 -4.129  19.898 1.00 28.99  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.734 -4.514  18.764 1.00 32.61  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.617 -3.725  18.407 1.00 33.59  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.110 -4.966  21.195 1.00 30.38  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.362 -4.422  22.436 1.00 30.48  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.634 -5.037  21.458 1.00 29.22  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.449 -5.400  23.667 1.00 31.11  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.551 -5.704  18.186 1.00 27.12  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.522 -6.155  17.200 1.00 28.17  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.293 -5.612  15.787 1.00 32.93  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.152 -5.831  14.928 1.00 33.63  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.685 -7.675  17.235 1.00 28.26  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.114 -8.169  18.606 1.00 28.73  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.315 -7.747  19.175 1.00 31.54  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.314 -9.043  19.328 1.00 29.26  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.708 -8.204  20.440 1.00 32.35  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.718 -9.516  20.581 1.00 31.90  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.901 -9.079  21.138 1.00 30.36  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.218 -4.835  15.556 1.00 30.05  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 34.070 -4.146  14.256 1.00 31.00  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.626 -2.724  14.391 1.00 38.18  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.700 -1.977  13.402 1.00 38.11  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.648 -4.166  13.705 1.00 37.38  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.761 -3.634  14.686 1.00 33.75  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.207 -5.563  13.242 1.00 34.74  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 35.039 -2.340  15.619 1.00 35.18  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.646 -1.028  15.831 1.00 36.50  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 37.073 -1.081  15.276 1.00 41.08  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.825 -1.986  15.622 1.00 38.23  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.643 -0.639  17.319 1.00 38.41  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.395 0.650   17.555 1.00 51.15  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.783 1.724   17.414 1.00 55.81  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.612 0.584   17.824 1.00 53.73  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.447 -0.100  14.435 1.00 42.44  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.755 -0.051  13.773 1.00 43.64  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.962 -0.086  14.728 1.00 47.36  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 41.015 -0.573  14.317 1.00 49.41  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.845 1.143   12.813 1.00 47.18  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 38.012 0.954   11.547 1.00 64.96  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.832 0.417   15.980 1.00 40.10  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.925 0.337   16.951 1.00 39.02  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.839 -0.920  17.808 1.00 43.20  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.859 -1.545  18.079 1.00 44.80  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.920 1.544   17.912 1.00 39.94  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.530 2.829   17.402 1.00 46.59  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.375 3.926   18.434 1.00 47.76  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 43.018 2.661   17.059 1.00 52.50  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.642 -1.240  18.321 1.00 37.21  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.472 -2.363  19.247 1.00 35.35  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.622 -3.723  18.578 1.00 39.56  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 40.007 -4.675  19.254 1.00 37.77  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.138 -2.278  20.010 1.00 35.88  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 38.021 -1.078  20.944 1.00 33.53  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.714 -1.151  21.729 1.00 31.21  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.393 0.149   22.434 1.00 38.49  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.880 1.182   21.504 1.00 39.25  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.348 -3.810  17.258 1.00 38.76  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.475 -5.059  16.486 1.00 39.59  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.874 -5.684  16.625 1.00 44.35  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 41.010 -6.899  16.468 1.00 44.23  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.105 -4.843  15.019 1.00 41.69  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.265 -3.791  14.091 1.00 48.28  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.900 -4.844  16.915 1.00 40.42  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.306 -5.232  17.039 1.00 40.82  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.775 -5.538  18.454 1.00 42.70  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.939 -5.902  18.653 1.00 41.90  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.207 -4.170  16.390 1.00 42.60  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 43.990 -4.086  14.893 1.00 58.96  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.919 -3.002  14.315 1.00 57.25  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.826 -5.231  14.232 1.00 47.12  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.893 -5.383  19.444 1.00 39.22  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.281 -5.656  20.820 1.00 38.35  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.267 -7.153  21.096 1.00 41.07  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.372 -7.861  20.607 1.00 39.70  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.351 -4.929  21.814 1.00 38.35  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.337 -3.395  21.747 1.00 43.57  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.272 -2.839  22.674 1.00 43.71  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.719 -2.792  22.080 1.00 45.65  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.247 -7.637  21.872 0.51 38.06  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.258 -7.624  21.872 0.49 38.07  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.328 -9.053  22.247 0.51 37.06  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.400 -9.028  22.272 0.49 37.17  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.720 -9.267  23.642 0.51 37.73  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.763 -9.259  23.651 0.49 37.80  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.518 -10.409 24.055 0.51 35.68  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.580 -10.406 24.059 0.49 35.77  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.773 -9.541  22.205 0.51 41.84  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.874 -9.422  22.303 0.49 41.94  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.581 -8.822  23.120 0.51 49.14  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.423 -9.463  20.996 0.49 49.00  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.449 -8.162  24.374 1.00 34.32  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.846 -8.195  25.714 1.00 34.07  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.659 -7.221  25.760 1.00 35.72  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.811 -6.046  25.383 1.00 35.72  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.876 -7.849  26.838 1.00 39.74  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.214 -7.822  28.219 1.00 39.81  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 45.065 -8.808  26.839 1.00 40.61  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.501 -7.702  26.253 1.00 28.79  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.299 -6.887  26.464 1.00 27.79  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.902 -7.007  27.925 1.00 30.70  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.687 -8.121  28.414 1.00 30.42  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.127 -7.264  25.498 1.00 30.08  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.526 -7.110  23.988 1.00 31.88  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.828 -6.494  25.835 1.00 31.14  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.882 -5.673  23.481 1.00 38.13  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.787 -5.855  28.624 1.00 29.18  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.384 -5.825  30.014 1.00 29.63  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.907 -5.500  30.131 1.00 32.49  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.472 -4.436  29.688 1.00 30.61  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.208 -4.786  30.796 1.00 33.06  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.688 -4.983  30.703 1.00 52.99  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.217 -6.029  31.057 1.00 41.59  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.394 -3.968  30.243 1.00 50.11  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.141 -6.394  30.744 1.00 27.43  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.716 -6.150  30.931 1.00 27.34  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.488 -5.271  32.152 1.00 30.48  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.368 -5.154  33.020 1.00 31.25  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.900 -7.454  31.061 1.00 27.10  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.985 -8.479  29.899 1.00 30.10  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.867 -9.550  30.026 1.00 30.94  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.949 -7.806  28.517 1.00 29.87  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.288 -4.707  32.240 1.00 27.76  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.853 -3.836  33.342 1.00 30.01  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 33.046 -4.591  34.675 1.00 34.75  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.728 -5.775  34.739 1.00 33.70  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.378 -3.467  33.136 1.00 31.67  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.829 -2.429  34.100 1.00 43.23  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.714 -2.735  35.309 1.00 43.94  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.482 -1.328  33.643 1.00 46.56  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.595 -3.949  35.729 1.00 35.29  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.826 -4.682  36.997 1.00 35.55  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.593 -5.259  37.674 1.00 38.88  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.743 -6.113  38.544 1.00 40.09  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.508 -3.645  37.905 1.00 38.35  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.199 -2.324  37.295 1.00 44.33  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.068 -2.550  35.820 1.00 38.44  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.386 -4.813  37.292 1.00 35.80  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.143 -5.333  37.869 1.00 37.48  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.850 -6.746  37.314 1.00 36.93  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 29.016 -7.462  37.866 1.00 36.10  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.968 -4.397  37.523 1.00 40.46  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.832 -4.407  38.533 1.00 61.09  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 28.042 -3.502  39.732 1.00 91.32  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.139 -2.268  39.537 1.00 91.56  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.102 -4.025  40.869 1.00 87.49  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.516 -7.136  36.215 1.00 31.76  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.277 -8.444  35.591 1.00 31.37  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.876 -9.575  36.414 1.00 35.74  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 32.048 -9.543  36.789 1.00 34.74  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.722 -8.469  34.101 1.00 33.05  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 29.963 -7.386  33.281 1.00 33.80  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.529 -9.873  33.484 1.00 29.97  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.342 -7.433  33.356 1.00 40.22  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 30.046 -10.559 36.688 1.00 35.31  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.372 -11.742 37.473 1.00 35.67  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.113 -12.769 36.598 1.00 35.03  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.568 -13.173 35.574 1.00 33.36  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 29.073 -12.339 38.034 1.00 39.73  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.281 -13.622 38.790 1.00 53.00  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.960 -14.696 38.298 1.00 44.64  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.836 -13.537 39.996 1.00 44.76  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.322 -13.246 37.005 1.00 32.37  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 33.045 -14.234 36.177 1.00 31.69  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.279 -15.539 35.932 1.00 35.16  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.380 -16.087 34.835 1.00 34.12  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.326 -14.494 36.978 1.00 35.22  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.501 -13.283 37.826 1.00 39.92  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 33.113 -12.869 38.197 1.00 35.71  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.513 -16.040 36.936 1.00 32.00  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.753 -17.286 36.726 1.00 32.08  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.666 -17.084 35.656 1.00 33.41  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.537 -17.931 34.779 1.00 31.08  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.154 -17.826 38.039 1.00 34.98  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.594 -19.231 37.848 1.00 45.73  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.747 -19.813 38.966 1.00 71.76  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.746 -21.057 39.105 1.00 71.99  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.076 -19.042 39.690 1.00 63.80  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.929 -15.963 35.732 1.00 31.94  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.908 -15.610 34.747 1.00 31.09  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.506 -15.562 33.352 1.00 31.76  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.939 -16.116 32.393 1.00 29.14  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.699 -14.954 33.241 1.00 27.84  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.400 -14.891 31.954 1.00 26.50  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.788 -16.291 31.480 1.00 28.08  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.578 -16.619 30.315 1.00 27.43  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.650 -13.990 32.008 1.00 27.72  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.263 -13.854 30.630 1.00 27.72  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.693 -13.012 29.677 1.00 31.08  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.323 -14.664 30.240 1.00 28.94  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.209 -12.941 28.381 1.00 31.45  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.833 -14.599 28.945 1.00 30.66  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.261 -13.751 28.015 1.00 29.18  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.368 -17.108 32.374 1.00 28.37  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.766 -18.482 32.047 1.00 30.57  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.573 -19.301 31.483 1.00 30.89  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.709 -19.983 30.460 1.00 28.85  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.378 -19.162 33.267 1.00 34.51  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.053 -20.808 32.913 1.00 40.31  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.402 -19.211 32.145 1.00 27.67  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.185 -19.920 31.729 1.00 26.36  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.775 -19.463 30.329 1.00 27.07  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.426 -20.297 29.480 1.00 25.45  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 27.062 -19.694 32.788 1.00 29.11  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.349 -20.522 34.094 1.00 29.60  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.649 -19.968 32.215 1.00 28.64  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.635 -20.011 35.286 1.00 34.69  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.867 -18.164 30.071 1.00 23.87  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.501 -17.608 28.755 1.00 23.94  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.503 -17.957 27.672 1.00 26.61  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.108 -18.249 26.539 1.00 24.76  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.234 -16.114 28.826 1.00 25.06  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.927 -15.763 29.580 1.00 31.14  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.818 -14.303 29.774 1.00 32.03  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.680 -16.262 28.836 1.00 33.52  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.790 -17.972 28.017 1.00 24.87  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.833 -18.370 27.063 1.00 23.96  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.603 -19.838 26.658 1.00 26.84  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.668 -20.175 25.475 1.00 25.56  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.221 -18.149 27.681 1.00 24.45  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.391 -18.447 26.720 1.00 29.29  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.349 -17.533 25.477 1.00 28.87  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.752 -18.347 27.460 1.00 30.99  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.305 -20.711 27.637 1.00 24.94  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 29.971 -22.113 27.354 1.00 24.47  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.764 -22.204 26.420 1.00 26.27  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.796 -22.985 25.475 1.00 25.81  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.680 -22.852 28.665 1.00 27.70  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.924 -23.222 29.465 1.00 42.32  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.044 -23.168 28.894 1.00 43.84  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.778 -23.582 30.655 1.00 43.48  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.707 -21.419 26.681 1.00 24.68  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.506 -21.361 25.827 1.00 22.86  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.873 -20.976 24.376 1.00 24.08  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.393 -21.583 23.407 1.00 22.20  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.471 -20.375 26.404 1.00 23.11  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.348 -20.113 25.421 1.00 23.33  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.398 -21.097 25.146 1.00 26.11  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.322 -18.940 24.664 1.00 25.88  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.395 -20.882 24.206 1.00 25.64  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.317 -18.733 23.701 1.00 28.43  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.368 -19.710 23.477 1.00 26.67  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.707 -19.955 24.225 1.00 21.47  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.116 -19.509 22.884 1.00 20.65  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.686 -20.647 22.058 1.00 24.53  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.346 -20.778 20.891 1.00 23.81  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.196 -18.412 22.990 1.00 21.53  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.674 -17.138 23.598 1.00 23.48  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 30.018 -15.909 23.480 1.00 27.37  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.336 -14.628 24.574 1.00 27.04  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.549 -21.474 22.675 1.00 21.13  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.234 -22.570 21.986 1.00 21.70  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.484 -23.902 21.976 1.00 25.07  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.958 -24.861 21.342 1.00 24.64  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.624 -22.774 22.625 1.00 22.83  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.671 -21.793 22.133 1.00 23.77  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.833 -20.551 22.743 1.00 25.16  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.528 -22.126 21.079 1.00 24.67  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.805 -19.644 22.291 1.00 25.36  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.542 -21.257 20.665 1.00 25.32  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.656 -20.009 21.255 1.00 27.96  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.678 -19.190 20.851 1.00 26.52  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.332 -24.001 22.676 1.00 22.50  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.635 -25.304 22.733 1.00 23.59  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.111 -25.283 22.505 1.00 26.09  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.544 -26.369 22.294 1.00 25.83  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.832 -25.992 24.126 1.00 27.95  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.162 -25.219 25.136 1.00 27.53  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.309 -26.206 24.515 1.00 29.82  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.461 -24.098 22.592 0.67 21.89  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.454 -24.103 22.622 0.33 22.31  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 23.988 -23.896 22.542 0.67 21.68  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 23.986 -23.902 22.559 0.33 22.32  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.342 -24.294 23.890 0.67 24.19  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.303 -24.424 23.844 0.33 26.05  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.153 -24.057 24.079 0.67 23.28  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.075 -24.522 23.890 0.33 25.84  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.327 -24.688 21.406 0.67 22.40  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.369 -24.551 21.316 0.33 24.41  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.980 -24.528 20.157 0.67 23.71  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.052 -25.921 21.513 0.33 28.56  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.126 -24.851 24.846 0.67 22.19  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.107 -24.758 24.880 0.33 23.41  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.578 -25.264 26.147 0.67 22.99  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.630 -25.292 26.160 0.33 24.13  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.823 -24.217 27.216 0.67 27.59  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.847 -24.262 27.263 0.33 28.10  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.956 -23.761 27.403 0.67 26.89  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.980 -23.826 27.491 0.33 27.34  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.156 -26.612 26.597 0.67 26.12  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.346 -26.617 26.503 0.33 25.89  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.834 -27.762 25.644 0.67 30.93  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.213 -27.702 25.429 0.33 32.93  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.822 -28.909 25.835 0.67 37.77  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.095 -28.679 25.732 0.33 38.16  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.761 -29.448 27.196 0.67 47.92  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.940 -29.696 24.688 0.33 40.79  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 23.978 -30.456 27.563 0.67 61.48  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.254 -30.980 24.836 0.33 54.41  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.205 -31.063 26.672 0.67 50.24  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.065 -31.834 23.839 0.33 46.34  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 23.973 -30.873 28.820 0.67 48.29  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.744 -31.423 25.986 0.33 38.01  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.759 -23.869 27.938 1.00 25.27  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.802 -22.862 28.998 1.00 24.94  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.574 -23.504 30.359 1.00 30.68  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.507 -24.085 30.606 1.00 30.42  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.746 -21.791 28.713 1.00 25.45  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.795 -20.564 29.658 1.00 29.03  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.068 -19.729 29.400 1.00 28.17  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.539 -19.713 29.508 1.00 31.37  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.575 -23.386 31.258 1.00 29.02  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.484 -23.966 32.609 1.00 30.74  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.787 -22.968 33.541 1.00 35.70  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.430 -22.294 34.343 1.00 35.72  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.880 -24.363 33.131 1.00 34.27  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.858 -24.994 34.514 1.00 53.04  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.860 -25.572 34.950 1.00 41.97  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.952 -24.877 35.244 1.00 47.67  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.472 -22.861 33.398 1.00 33.46  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.657 -21.919 34.151 1.00 34.79  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.131 -22.569 35.420 1.00 38.74  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.488 -23.626 35.361 1.00 38.39  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.532 -21.436 33.229 1.00 35.72  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.798 -20.167 33.569 1.00 41.82  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.765 -18.962 33.603 1.00 42.04  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.678 -19.943 32.557 1.00 41.54  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.493 -21.983 36.582 1.00 35.70  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.118 -22.504 37.906 1.00 37.72  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.583 -21.378 38.783 1.00 39.37  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.901 -20.207 38.553 1.00 37.87  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.329 -23.167 38.599 1.00 38.92  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.955 -24.322 37.805 1.00 45.65  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.209 -24.893 38.457 1.00 63.39  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.939 -25.511 39.760 1.00 82.84  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.529 -26.765 39.937 1.00 104.39 ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.303 -27.229 41.159 1.00 92.44  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.327 -27.560 38.891 1.00 95.43  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.761 -21.719 39.787 1.00 37.84  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.221 -20.711 40.709 1.00 38.26  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.343 -19.823 41.295 1.00 43.41  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.177 -18.604 41.378 1.00 43.37  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.417 -21.389 41.845 1.00 41.65  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.732 -20.405 42.778 1.00 52.22  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.032 -21.014 43.979 1.00 85.04  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.598 -21.938 44.610 1.00 81.55  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.913 -20.552 44.300 1.00 86.87  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.479 -20.437 41.631 1.00 40.85  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.623 -19.743 42.219 1.00 41.09  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.416 -18.845 41.282 1.00 42.25  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.191 -18.007 41.743 1.00 43.00  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.238 -18.998 39.965 1.00 36.74  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 23.015 -18.188 39.021 1.00 34.10  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.171 -17.335 38.069 1.00 38.02  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.745 -16.521 37.332 1.00 36.01  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 23.985 -19.101 38.240 1.00 33.20  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.331 -20.028 37.235 1.00 41.21  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.276 -19.727 36.671 1.00 33.18  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 23.965 -21.161 36.948 1.00 35.34  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.825 -17.533 38.049 1.00 35.76  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.953 -16.872 37.060 1.00 35.58  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.089 -15.340 37.045 1.00 36.91  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.106 -14.749 35.958 1.00 34.13  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.473 -17.313 37.128 1.00 39.92  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.678 -16.759 35.909 1.00 39.82  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.811 -16.998 38.485 1.00 39.91  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.489 -17.569 35.504 1.00 43.72  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.196 -14.705 38.214 1.00 35.42  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.339 -13.245 38.258 1.00 36.15  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.642 -12.760 37.617 1.00 38.60  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.605 -11.818 36.822 1.00 36.23  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.159 -12.688 39.682 1.00 40.58  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.774 -12.973 40.273 1.00 47.63  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.374 -12.551 39.189 1.00 53.77  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.267 -10.782 39.467 1.00 51.93  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.779 -13.432 37.921 1.00 36.48  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.093 -13.093 37.346 1.00 35.55  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.103 -13.381 35.839 1.00 35.99  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.637 -12.581 35.067 1.00 34.21  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.196 -13.895 38.029 1.00 36.79  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.513 -14.518 35.421 1.00 31.09  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.449 -14.880 33.994 1.00 28.06  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.633 -13.839 33.220 1.00 29.97  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.107 -13.376 32.181 1.00 28.37  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.944 -16.333 33.771 1.00 31.28  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.665 -16.621 32.292 1.00 29.38  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.944 -17.340 34.322 1.00 31.61  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.437 -13.459 33.723 0.20 28.94  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.435 -13.460 33.720 0.80 29.63  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.592 -12.460 33.059 0.20 29.88  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.616 -12.458 33.024 0.80 31.34  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.303 -11.109 32.924 0.20 34.35  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.327 -11.103 32.911 0.80 34.95  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.280 -10.525 31.839 0.20 33.38  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.308 -10.495 31.837 0.80 33.40  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.243 -12.292 33.770 0.20 33.57  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.249 -12.284 33.691 0.80 34.98  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.276 -11.426 32.991 0.20 37.74  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.321 -11.370 32.898 0.80 39.11  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.745 -11.112 33.875 0.20 43.69  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.635 -11.385 33.530 0.80 44.97  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.240 -9.627  33.078 0.20 40.96  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.808 -10.339 35.060 0.80 43.18  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.939 -10.628 34.015 1.00 31.97  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.683 -9.347  34.026 1.00 32.17  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.834 -9.379  33.011 1.00 32.43  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 24.006 -8.422  32.240 1.00 31.07  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.209 -9.048  35.429 1.00 33.55  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.569 -10.506 32.956 1.00 28.22  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.665 -10.671 31.999 1.00 27.36  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.127 -10.709 30.550 1.00 30.43  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.716 -10.051 29.682 1.00 27.51  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.583 -11.862 32.361 1.00 32.50  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.893 -11.826 33.758 1.00 32.66  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.892 -11.854 31.561 1.00 31.86  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 24.022 -11.464 30.288 1.00 27.33  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.429 -11.545 28.940 1.00 26.73  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.911 -10.181 28.476 1.00 29.09  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.095 -9.826  27.312 1.00 27.46  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.331 -12.604 28.891 1.00 27.63  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.351 -9.360  29.399 1.00 27.58  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.918 -8.000  29.039 1.00 27.75  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.117 -7.126  28.603 1.00 31.23  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.064 -6.455  27.573 1.00 31.21  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.164 -7.366  30.214 1.00 31.01  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.786 -7.959  30.396 1.00 36.41  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 19.020 -7.381  31.934 1.00 44.91  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.778 -5.628  31.526 1.00 42.90  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.201 -7.178  29.370 1.00 28.80  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.444 -6.451  29.085 1.00 27.70  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 26.060 -6.933  27.754 1.00 29.95  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.469 -6.104  26.929 1.00 27.17  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.415 -6.697  30.236 1.00 28.03  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.820 -6.186  29.998 1.00 28.17  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.115 -4.826  30.095 1.00 31.54  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.873 -7.070  29.768 1.00 27.72  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.417 -4.353  29.902 1.00 29.78  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.179 -6.612  29.605 1.00 28.07  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.442 -5.255  29.671 1.00 32.07  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.738 -4.848  29.544 1.00 29.37  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.091 -8.259  27.537 1.00 27.16  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.663 -8.850  26.314 1.00 25.90  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.736 -8.723  25.109 1.00 29.28  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.161 -8.975  23.982 1.00 27.93  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.065 -10.320 26.548 1.00 24.70  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.205 -10.589 27.549 1.00 27.25  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.499 -12.108 27.636 1.00 26.85  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.505 -9.814  27.174 1.00 28.20  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.474 -8.323  25.336 1.00 26.43  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.476 -8.185  24.260 1.00 26.31  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.218 -9.538  23.580 1.00 30.02  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.456 -9.724  22.389 1.00 29.49  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.849 -7.070  23.261 1.00 27.11  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 23.997 -5.685  23.918 1.00 30.38  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.694 -4.733  22.979 1.00 43.41  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.567 -4.828  21.764 1.00 36.02  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.463 -3.807  23.516 1.00 37.89  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.782 -10.499 24.399 1.00 25.77  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.436 -11.867 23.976 1.00 25.15  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.943 -12.032 24.235 1.00 31.85  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.521 -12.534 25.286 1.00 30.15  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.301 -12.856 24.755 1.00 26.03  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.778 -12.708 24.428 1.00 27.86  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.803 -13.750 25.467 1.00 31.59  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.461 -15.405 24.686 1.00 28.56  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.139 -11.495 23.303 1.00 31.92  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.672 -11.386 23.410 1.00 34.23  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.920 -12.671 23.743 1.00 34.49  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 17.005 -12.615 24.558 1.00 34.20  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.069 -10.759 22.142 1.00 37.47  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.586 -9.354  21.874 1.00 50.21  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.278 -13.818 23.135 1.00 30.72  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.540 -15.052 23.431 1.00 32.24  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.783 -15.538 24.852 1.00 33.65  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.848 -16.026 25.493 1.00 34.14  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.815 -16.142 22.398 1.00 34.30  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.380 -15.772 21.017 1.00 39.40  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.048 -15.557 20.714 1.00 43.46  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.111 -15.656 19.883 1.00 41.18  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 16.015 -15.265 19.423 1.00 43.35  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.231 -15.324 18.880 1.00 42.42  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 19.016 -15.354 25.366 1.00 27.31  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.346 -15.716 26.755 1.00 26.94  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.550 -14.815 27.708 1.00 33.40  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.940 -15.319 28.652 1.00 32.51  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.869 -15.687 27.063 1.00 29.92  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.124 -15.955 28.548 1.00 30.09  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.615 -16.713 26.201 1.00 29.06  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.539 -13.490 27.449 1.00 30.66  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.778 -12.527 28.273 1.00 31.66  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.291 -12.947 28.353 1.00 37.23  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.744 -13.025 29.452 1.00 36.22  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.969 -11.053 27.806 1.00 34.56  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.126 -10.081 28.653 1.00 35.35  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.440 -10.651 27.855 1.00 33.45  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.688 -13.287 27.203 0.61 34.87  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.654 -13.189 27.188 0.39 35.17  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.300 -13.738 27.084 0.61 36.42  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.245 -13.587 27.057 0.39 36.83  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 14.001 -14.979 27.940 0.61 38.77  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.883 -14.805 27.909 0.39 40.55  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 13.012 -14.958 28.672 0.61 39.67  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.859 -14.782 28.590 0.39 41.71  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.950 -13.993 25.607 0.61 38.95  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.900 -13.863 25.578 0.39 39.10  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.505 -14.393 25.368 0.61 55.14  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.686 -12.637 24.707 0.39 52.65  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.603 -13.589 25.697 0.61 59.22  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.249 -11.594 25.242 0.39 55.64  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.277 -15.505 24.846 0.61 61.49  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.930 -12.728 23.484 0.39 59.26  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.836 -16.051 27.864 0.61 33.54  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.724 -15.858 27.875 0.39 35.78  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.563 -17.250 28.677 0.61 33.93  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.493 -17.100 28.619 0.39 36.03  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.742 -16.975 30.170 0.61 37.57  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.680 -16.889 30.128 0.39 38.93  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.012 -17.556 30.970 0.61 36.48  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.890 -17.430 30.903 0.39 38.73  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.322 -18.509 28.216 0.61 34.95  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.323 -18.248 28.037 0.39 42.39  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.718 -19.632 28.860 0.61 36.71  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.255 -18.178 26.612 0.39 41.32  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.814 -18.481 28.558 0.61 29.82  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.821 -19.607 28.487 0.39 42.51  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.699 -16.093 30.540 1.00 34.40  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.949 -15.736 31.956 1.00 35.36  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.731 -15.023 32.503 1.00 40.60  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.264 -15.376 33.596 1.00 40.59  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.194 -14.869 32.097 1.00 34.82  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.745 -15.765 31.870 1.00 37.30  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.196 -14.047 31.730 0.48 38.37  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.200 -14.032 31.746 0.52 38.68  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.997 -13.270 32.076 0.48 40.19  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 13.002 -13.275 32.132 0.52 40.64  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.800 -14.196 32.325 0.48 44.83  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.792 -14.201 32.337 0.52 45.01  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.063 -14.000 33.294 0.48 45.43  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.040 -14.012 33.297 0.52 45.57  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.648 -12.275 30.957 0.48 41.56  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.678 -12.192 31.097 0.52 42.78  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.594 -11.090 30.856 0.48 53.50  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.408 -10.874 31.340 0.52 57.15  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.991 -9.947  30.060 0.48 65.96  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.681 -9.698  30.701 0.52 67.51  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.996 -8.940  29.713 0.48 71.01  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.814 -9.692  29.241 0.52 73.02  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.328 -7.905  30.479 0.48 81.52  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.608 -8.871  28.559 0.52 83.03  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.731 -7.717  31.651 0.48 71.68  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.342 -7.964  29.195 0.52 67.69  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.259 -7.050  30.080 0.48 63.51  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.666 -8.944  27.237 0.52 67.42  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.626 -15.212 31.458 1.00 41.21  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.524 -16.190 31.549 1.00 42.44  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.656 -17.102 32.769 1.00 45.86  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.666  -17.308 33.475 1.00 45.54  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.393 -17.004 30.247 1.00 44.64  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.839  -16.163 29.101 1.00 64.50  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.719  -16.920 27.792 1.00 77.42  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.269  -15.989 26.690 1.00 91.82  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.419  -16.682 25.689 1.00 105.16 ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.880 -17.616 33.040 1.00 41.12  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.155 -18.485 34.194 1.00 41.51  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 11.967 -17.713 35.501 1.00 47.22  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.425 -18.266 36.463 1.00 47.08  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.563 -19.097 34.101 1.00 41.69  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.697 -20.378 33.291 1.00 43.08  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.174 -20.470 32.003 1.00 46.17  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.424 -21.459 33.783 1.00 45.86  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.317 -21.649 31.250 1.00 46.77  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.574 -22.634 33.025 1.00 47.44  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 14.020 -22.719 31.767 1.00 44.57  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.369 -16.422 35.523 1.00 42.95  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.178 -15.557 36.700 1.00 44.40  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.677 -15.300 36.952 1.00 51.54  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.224 -15.445 38.096 1.00 52.93  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.034 -14.264 36.612 1.00 46.35  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.520 -14.615 36.820 1.00 45.26  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.582 -13.204 37.662 1.00 48.90  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.508 -13.637 36.223 1.00 50.83  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.904  -14.984 35.883 1.00 49.08  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.453  -14.740 35.970 1.00 51.59  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.701  -15.960 36.526 1.00 56.73  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.744  -15.794 37.277 1.00 57.50  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.878  -14.338 34.605 1.00 54.61  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.152  -17.181 36.173 1.00 51.87  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.543  -18.429 36.647 1.00 53.33  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.722  -18.664 38.156 1.00 59.74  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.863  -19.287 38.768 1.00 60.33  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.106  -19.609 35.867 1.00 52.42  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.836  -18.200 38.743 1.00 58.19  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.139  -18.411 40.162 1.00 61.13  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.537  -17.364 41.116 1.00 69.46  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.513  -17.605 42.327 1.00 71.74  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.645 -18.528 40.379 1.00 65.06  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 11.076 -19.871 40.216 1.00 75.47  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.024  -16.231 40.586 1.00 66.21  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.434  -15.163 41.406 1.00 87.28  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 6.002  -15.474 41.872 1.00 130.66 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.646  -16.631 42.093 1.00 98.00  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.514  -13.797 40.694 1.00 87.78  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.483  -13.582 39.592 1.00 98.12  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.641  -12.347 38.723 1.00 119.47 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.771  -11.814 38.620 1.00 112.62 ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.626  -11.922 38.125 1.00 113.68 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.265 -35.137 5.836  1.00 30.93  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.311 -33.999 6.336  1.00 31.87  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.488 -36.381 6.709  1.00 31.11  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.985 -35.374 4.556  0.66 28.90  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 21.013 -35.366 4.546  0.34 29.65  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.760 -34.329 3.560  0.66 28.24  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.715 -34.290 3.600  0.34 29.35  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.251 -34.175 3.261  0.66 32.43  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.207 -34.138 3.460  0.34 32.28  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.542 -35.184 3.163  0.66 32.03  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.462 -35.114 3.610  0.34 31.37  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.549 -34.674 2.278  0.66 27.23  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.363 -34.518 2.209  0.34 28.61  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.044 -34.655 2.468  0.66 27.48  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.724 -35.591 1.373  0.34 29.76  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.837 -35.683 2.890  0.66 30.07  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.105 -36.897 1.296  0.34 32.89  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.914 -33.538 2.254  0.66 26.85  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.618 -35.441 0.462  0.34 29.89  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.148 -35.264 2.976  0.66 29.10  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.284 -37.582 0.431  0.34 32.58  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.227 -33.959 2.569  0.66 30.13  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.364 -36.713 -0.098 0.34 33.96  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.711 -32.209 1.846  0.66 27.59  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.794 -34.363 0.091  0.34 30.66  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.334 -33.108 2.457  0.66 29.72  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.327 -36.935 -1.014 0.34 33.32  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.814 -31.384 1.688  0.66 28.54  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.764 -34.585 -0.809 0.34 32.43  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.101 -31.825 2.018  0.66 29.26  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.544 -35.856 -1.358 0.34 32.98  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.760 -32.920 3.143  1.00 28.09  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.341 -32.603 2.914  1.00 28.07  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.201 -31.552 1.809  1.00 30.60  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.178 -30.875 1.454  1.00 28.95  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.620 -32.091 4.211  1.00 30.94  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.643 -33.132 5.338  1.00 30.76  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.196 -30.742 4.692  1.00 30.85  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.967 -31.389 1.324  1.00 27.25  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.575 -30.307 0.430  1.00 27.05  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.194 -29.171 1.409  1.00 31.60  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.187 -29.306 2.123  1.00 30.76  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.377 -30.667 -0.483 1.00 29.58  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.656 -31.927 -1.365 1.00 28.61  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.955 -29.421 -1.331 1.00 32.00  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.982 -31.841 -2.310 1.00 32.16  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.983 -28.075 1.484  1.00 31.43  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.660 -27.004 2.447  1.00 32.06  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.410 -26.203 2.088  1.00 35.94  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.122 -26.011 0.908  1.00 35.57  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.921 -26.130 2.441  1.00 34.30  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.489 -26.312 1.055  1.00 37.89  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.204 -27.757 0.709  1.00 33.52  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.763 -25.612 3.102  1.00 34.85  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.523 -10.171 16.484 1.00 28.04  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.931 -8.904  16.523 1.00 28.72  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.910 -8.623  17.422 1.00 29.30  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.474 -9.637  18.270 1.00 30.94  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.309 -10.820 19.839 1.00 34.92  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 24.019 -10.916 18.209 1.00 29.28  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.322 -10.264 11.928 1.00 32.79  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.449 -10.608 13.259 1.00 30.36  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.415 -10.254 14.154 1.00 30.21  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.307 -11.773 19.216 1.00 32.24  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.482 -11.083 20.710 1.00 35.86  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.474 -9.606  19.249 1.00 33.10  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 25.042 -11.189 17.312 1.00 27.87  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.415 -10.584 15.476 1.00 28.35  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.328 -9.632  13.665 1.00 33.15  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.324 -9.378  12.369 1.00 34.50  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.888 -8.600  11.781 0.41 34.58  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 29.000 -11.503 13.839 0.65 28.07  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.241 -9.637  11.453 1.00 33.33  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.344 -15.363 22.687 1.00 41.21  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.557 -35.458 -1.296 0.66 49.90  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.302 -35.214 -0.602 0.66 50.53  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.726 -34.546 -0.320 0.66 49.01  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 17.989 -37.087 -0.791 0.66 49.72  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 35.785 -25.838 25.552 1.00 42.92  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 25.872 -3.572  26.535 1.00 36.58  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 44.407 -0.826  17.921 1.00 53.41  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 22.754 -5.455  19.925 1.00 58.52  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 26.805 -32.143 16.155 1.00 48.48  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 41.148 -21.677 25.209 1.00 46.10  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 38.530 -15.003 15.519 1.00 40.23  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 29.910 -32.348 9.574  1.00 55.67  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 23.440 -5.912  33.010 1.00 39.43  ? 309 HOH   A O   1 
HETATM 1210 O  O   A HOH   F 6 .   ? 18.997 -23.024 4.385  0.67 50.97  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 33.402 -20.960 29.605 1.00 50.28  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 20.803 -5.907  26.224 1.00 45.52  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 37.877 2.354   19.836 1.00 43.33  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 19.923 -9.732  37.091 1.00 43.03  ? 314 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 6 .   ? 16.472 -27.462 -3.283 1.00 54.73  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 45.168 -11.318 18.914 1.00 73.71  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 43.715 -6.589  31.917 1.00 53.20  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 31.751 -0.967  15.897 1.00 46.53  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 28.316 -23.858 31.740 1.00 43.68  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 37.286 -12.589 40.337 1.00 70.11  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 37.757 -20.551 26.993 1.00 39.09  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 30.369 1.361   33.921 1.00 73.46  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 15.445 -10.031 24.997 1.00 54.59  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 20.424 -13.571 20.576 1.00 52.07  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 22.736 -27.750 17.798 1.00 52.01  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 28.333 -8.973  40.010 1.00 50.69  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 21.485 -27.226 14.666 0.50 38.68  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 21.774 -29.566 -5.250 1.00 41.08  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 41.317 -16.967 15.226 1.00 44.89  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 27.238 -10.252 35.946 1.00 42.81  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 28.756 -21.937 41.678 1.00 75.98  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 25.755 -2.985  20.155 1.00 61.37  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 17.926 -29.489 7.713  1.00 39.38  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 29.407 -27.436 20.648 1.00 27.37  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 22.978 -28.307 12.671 1.00 27.89  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 32.694 -24.707 32.235 1.00 66.86  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 23.370 -17.169 44.337 1.00 67.55  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 34.504 -23.829 29.890 1.00 76.28  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 30.368 -0.644  37.040 1.00 55.73  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 21.512 -30.022 14.205 1.00 77.25  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 26.975 -16.721 38.739 1.00 55.34  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 36.919 -5.714  12.297 1.00 41.38  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 37.361 -6.483  34.359 1.00 43.48  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 41.435 -12.794 14.068 1.00 116.51 ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 29.087 -31.214 7.315  1.00 36.88  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 26.154 -22.688 29.984 1.00 29.39  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 26.168 -21.958 38.739 1.00 42.66  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 24.016 -15.880 21.339 1.00 35.71  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 27.337 -28.264 18.686 1.00 30.25  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 29.019 -0.478  16.917 1.00 79.01  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 44.011 -4.427  25.836 1.00 50.66  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 41.227 -1.472  11.706 1.00 71.99  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 18.118 -34.626 8.334  1.00 36.02  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 20.935 -7.394  19.930 1.00 52.52  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 46.082 -14.240 21.551 1.00 62.99  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 21.913 -25.084 18.375 1.00 26.94  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 44.463 -12.741 41.422 1.00 59.75  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 46.885 -21.719 18.078 1.00 50.18  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 10.852 -11.554 34.616 1.00 51.32  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 24.970 -26.894 19.058 1.00 37.32  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 42.497 -10.572 15.544 1.00 54.10  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 28.580 -24.356 34.445 1.00 59.22  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 46.312 -15.954 27.640 1.00 74.97  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 30.721 -29.001 22.725 1.00 46.25  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 26.905 -35.412 11.646 1.00 63.73  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 34.833 -19.011 13.894 0.50 26.66  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 43.866 -10.735 35.156 1.00 74.90  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 34.172 -8.023  35.741 1.00 40.49  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 41.423 -7.815  46.554 1.00 60.62  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 12.278 -18.127 25.883 1.00 62.65  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 26.155 -8.119  9.075  1.00 49.78  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 39.029 -18.905 33.492 1.00 50.87  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 47.232 -25.245 21.670 1.00 57.11  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 27.194 -2.359  16.137 1.00 67.90  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 20.311 -16.032 40.982 1.00 38.34  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 27.647 -23.159 13.894 0.50 29.41  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 14.335 -16.907 23.453 1.00 46.99  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 26.059 -19.183 41.706 1.00 63.85  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 17.984 -24.469 39.791 1.00 45.94  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 29.618 -22.759 36.981 1.00 66.62  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 22.670 -34.062 8.860  1.00 37.77  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 24.160 -28.781 21.614 1.00 61.61  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 38.029 -16.708 13.163 0.50 29.65  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 46.380 -18.947 19.684 1.00 56.17  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 23.719 -15.746 17.803 1.00 45.19  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 44.658 -16.443 29.746 1.00 54.21  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 41.234 -7.042  35.983 1.00 48.70  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 45.537 -10.919 30.260 1.00 58.50  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 12.621 -20.696 42.532 1.00 62.69  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 19.937 -25.565 41.349 1.00 80.90  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 34.759 -29.157 26.065 1.00 69.55  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 11.600 -15.314 40.651 1.00 83.27  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 26.424 -30.829 19.011 1.00 64.93  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 21.315 -31.376 29.904 1.00 74.41  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 16.746 -6.536  27.626 1.00 67.06  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 44.594 -8.811  18.032 1.00 70.63  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 42.223 -5.803  11.849 1.00 73.59  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 45.341 -12.718 23.658 1.00 53.47  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 31.899 -31.974 14.572 1.00 41.61  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 33.134 -29.854 21.536 1.00 45.59  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 40.476 -19.671 29.033 1.00 38.15  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 46.853 -20.232 22.006 1.00 69.14  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 21.160 -23.261 42.157 1.00 52.59  ? 403 HOH   A O   1 
HETATM 1304 O  O   A HOH   F 6 .   ? 12.071 -20.655 27.955 0.66 49.34  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 30.454 -10.699 40.662 1.00 47.76  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 37.051 -2.328  11.586 1.00 61.34  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 47.480 -6.744  20.319 1.00 71.20  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 35.387 1.896   13.571 1.00 59.53  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 4.235  -20.481 37.947 1.00 67.79  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 22.984 -15.021 40.463 1.00 37.48  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 27.117 -1.716  22.123 1.00 57.72  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 45.938 -17.120 17.378 1.00 70.03  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 41.327 -17.134 35.241 1.00 48.88  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 32.172 -15.676 39.879 1.00 40.16  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 33.563 -33.034 12.085 1.00 51.40  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 46.192 -8.950  44.205 1.00 57.82  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 25.583 -4.568  17.975 1.00 53.12  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 10.452 -11.771 40.124 1.00 67.40  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 35.152 -29.803 23.452 1.00 48.76  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 33.569 -0.351  20.118 1.00 46.79  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 32.435 -9.054  39.828 1.00 62.00  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 42.102 -8.128  13.829 1.00 63.47  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 19.639 -27.313 10.077 1.00 59.88  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 25.711 -16.222 41.132 1.00 55.46  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 34.001 -32.826 21.967 1.00 67.56  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 37.256 -31.518 23.421 1.00 87.77  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 34.502 -18.871 36.310 1.00 69.68  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 39.911 -5.560  33.968 1.00 45.83  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 29.589 -0.783  22.394 1.00 65.61  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 23.569 -30.563 19.343 1.00 72.34  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 31.878 -26.168 27.133 1.00 58.91  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 27.471 -25.741 28.317 1.00 60.78  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 45.810 -5.533  23.825 1.00 51.72  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 42.927 -18.311 30.791 1.00 52.26  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 22.317 -10.596 14.648 1.00 48.84  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 44.433 -4.189  28.910 1.00 71.60  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 26.577 -29.574 22.689 1.00 62.82  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 23.184 -3.145  26.834 1.00 64.96  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 31.885 -0.073  13.323 1.00 68.09  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 26.964 -34.564 18.012 1.00 72.01  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 28.826 -2.614  13.161 1.00 86.41  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 48.034 -23.458 19.803 1.00 66.57  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 30.646 -34.372 14.931 1.00 66.01  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 19.445 -31.750 13.827 1.00 72.43  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 19.813 -8.164  24.687 1.00 55.97  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 35.415 -4.244  10.636 1.00 52.37  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 36.926 -24.527 27.643 1.00 63.70  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 47.501 -28.514 17.666 1.00 65.23  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 46.736 -14.658 18.364 1.00 68.84  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 24.573 -21.831 41.112 1.00 64.24  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 12.005 -18.877 22.803 1.00 67.44  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 47.224 -11.938 25.468 1.00 73.24  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 32.241 -1.100  22.363 1.00 59.97  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 47.113 -12.640 28.509 1.00 66.73  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 44.005 -13.715 13.894 0.50 106.35 ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 45.556 -8.529  31.477 1.00 66.42  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 25.366 -5.766  34.945 1.00 66.73  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 35.884 -21.334 30.696 1.00 65.55  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 34.076 -17.618 39.674 1.00 70.14  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 19.458 -7.695  35.376 1.00 59.81  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 20.138 -35.333 10.136 1.00 45.37  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 33.880 -11.148 41.683 0.50 68.24  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 17.132 -7.948  25.044 1.00 71.66  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 28.250 -29.886 24.826 1.00 70.21  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 17.093 -28.216 9.937  1.00 57.33  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 19.971 -14.898 43.422 1.00 57.92  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 43.191 -3.023  34.055 1.00 61.55  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 19.123 -28.304 13.811 0.50 70.72  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 33.880 -14.046 41.683 0.50 46.88  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 32.603 -20.732 36.944 1.00 80.88  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 12.619 -18.285 20.021 1.00 66.25  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 31.935 -23.889 35.002 1.00 81.24  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 16.695 -6.859  34.960 1.00 80.55  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 21.301 -5.741  34.767 1.00 55.51  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 45.187 -12.349 15.943 1.00 77.29  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   F 6 .   ? 39.524 -5.515  11.541 1.00 75.75  ? 476 HOH   A O   1 
HETATM 1377 O  O   . HOH   F 6 .   ? 16.707 -30.272 12.483 1.00 60.52  ? 477 HOH   A O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 12.186 -24.341 0.046  1.00 54.35  ? 201 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 14.888 -25.864 -1.772 1.00 48.03  ? 202 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 17.737 -36.330 6.040  1.00 43.19  ? 203 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 11.550 -23.617 3.047  1.00 60.24  ? 204 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 20.846 -38.366 4.039  1.00 54.30  ? 205 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 20.829 -39.504 -2.104 1.00 63.45  ? 206 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 10.682 -24.712 5.493  1.00 60.74  ? 207 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.701 -36.532 9.946  1.00 54.49  ? 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   ? 0.8553 1.0350 0.7355 0.0301  -0.1361 -0.0215 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8494 1.0229 0.7109 0.0140  -0.1270 -0.0239 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8249 1.0278 0.7102 0.0027  -0.1226 -0.0405 6   ASP A C   
4    O O   . ASP A 5   ? 0.8153 1.0441 0.7303 0.0065  -0.1268 -0.0500 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8715 1.0172 0.7235 0.0056  -0.1094 -0.0173 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0739 1.1994 0.8910 -0.0046 -0.1042 -0.0126 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0765 1.2138 0.8904 -0.0156 -0.1016 -0.0214 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1883 1.2857 0.9812 -0.0027 -0.1016 -0.0010 6   ASP A OD2 
9    N N   . SER A 6   ? 0.7209 0.9194 0.5931 -0.0119 -0.1133 -0.0447 7   SER A N   
10   C CA  . SER A 6   ? 0.6747 0.8943 0.5649 -0.0243 -0.1068 -0.0600 7   SER A CA  
11   C C   . SER A 6   ? 0.6231 0.8298 0.5245 -0.0344 -0.0874 -0.0625 7   SER A C   
12   O O   . SER A 6   ? 0.6093 0.8204 0.5139 -0.0464 -0.0787 -0.0722 7   SER A O   
13   C CB  . SER A 6   ? 0.7569 0.9816 0.6240 -0.0326 -0.1116 -0.0646 7   SER A CB  
14   O OG  . SER A 6   ? 0.9227 1.1209 0.7601 -0.0387 -0.1037 -0.0567 7   SER A OG  
15   N N   . CYS A 7   ? 0.5194 0.7099 0.4268 -0.0286 -0.0815 -0.0542 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4807 0.6581 0.3974 -0.0356 -0.0658 -0.0554 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4613 0.6539 0.4042 -0.0416 -0.0597 -0.0674 8   CYS A C   
18   O O   . CYS A 7   ? 0.4518 0.6649 0.4111 -0.0384 -0.0664 -0.0734 8   CYS A O   
19   C CB  . CYS A 7   ? 0.5008 0.6600 0.4178 -0.0275 -0.0630 -0.0444 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5879 0.7201 0.4720 -0.0257 -0.0627 -0.0312 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3489 0.5305 0.2953 -0.0501 -0.0470 -0.0712 9   ILE A N   
22   C CA  . ILE A 8   ? 0.3080 0.4933 0.2741 -0.0557 -0.0388 -0.0797 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3307 0.4980 0.3011 -0.0509 -0.0326 -0.0718 9   ILE A C   
24   O O   . ILE A 8   ? 0.3253 0.4776 0.2835 -0.0466 -0.0321 -0.0626 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3427 0.5265 0.3086 -0.0677 -0.0302 -0.0903 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3480 0.5118 0.3001 -0.0699 -0.0232 -0.0867 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3301 0.5351 0.2942 -0.0734 -0.0366 -0.1001 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.4053 0.5639 0.3578 -0.0798 -0.0142 -0.0972 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2613 0.4286 0.2470 -0.0527 -0.0269 -0.0756 10  GLN A N   
30   N N   B GLN A 9   ? 0.2742 0.4436 0.2606 -0.0521 -0.0280 -0.0757 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2596 0.4096 0.2472 -0.0486 -0.0215 -0.0685 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2683 0.4223 0.2584 -0.0480 -0.0228 -0.0692 10  GLN A CA  
33   C C   A GLN A 9   ? 0.3028 0.4397 0.2940 -0.0559 -0.0112 -0.0733 10  GLN A C   
34   C C   B GLN A 9   ? 0.3215 0.4618 0.3145 -0.0555 -0.0122 -0.0737 10  GLN A C   
35   O O   A GLN A 9   ? 0.2952 0.4393 0.2937 -0.0636 -0.0076 -0.0827 10  GLN A O   
36   O O   B GLN A 9   ? 0.3181 0.4650 0.3182 -0.0634 -0.0082 -0.0832 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2727 0.4316 0.2719 -0.0410 -0.0258 -0.0659 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2760 0.4422 0.2796 -0.0415 -0.0271 -0.0688 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2867 0.4292 0.2890 -0.0387 -0.0192 -0.0608 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3504 0.5010 0.3530 -0.0344 -0.0249 -0.0595 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5721 0.7189 0.5817 -0.0295 -0.0234 -0.0562 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4844 0.6368 0.5016 -0.0362 -0.0188 -0.0638 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.5191 0.6792 0.5309 -0.0222 -0.0327 -0.0552 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3514 0.5232 0.3836 -0.0378 -0.0200 -0.0724 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.5142 0.6481 0.5264 -0.0288 -0.0171 -0.0533 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.4514 0.5841 0.4642 -0.0366 -0.0120 -0.0588 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2726 0.3894 0.2577 -0.0537 -0.0068 -0.0673 11  PHE A N   
48   N N   B PHE A 10  ? 0.2861 0.4063 0.2727 -0.0530 -0.0080 -0.0671 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2730 0.3731 0.2582 -0.0584 0.0011  -0.0701 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2900 0.3927 0.2759 -0.0574 0.0001  -0.0694 11  PHE A CA  
51   C C   A PHE A 10  ? 0.3071 0.4014 0.2973 -0.0561 0.0035  -0.0667 11  PHE A C   
52   C C   B PHE A 10  ? 0.3205 0.4174 0.3117 -0.0555 0.0027  -0.0665 11  PHE A C   
53   O O   A PHE A 10  ? 0.2913 0.3775 0.2788 -0.0497 0.0021  -0.0588 11  PHE A O   
54   O O   B PHE A 10  ? 0.3109 0.4019 0.3004 -0.0487 0.0008  -0.0587 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2933 0.3768 0.2701 -0.0566 0.0034  -0.0675 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.3162 0.4035 0.2932 -0.0549 0.0016  -0.0657 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.3131 0.3781 0.2879 -0.0600 0.0094  -0.0711 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3471 0.4379 0.3196 -0.0594 0.0023  -0.0719 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3592 0.4227 0.3336 -0.0676 0.0135  -0.0799 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3904 0.4964 0.3588 -0.0601 -0.0026 -0.0726 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3330 0.3803 0.3045 -0.0554 0.0106  -0.0658 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3927 0.4703 0.3636 -0.0627 0.0076  -0.0773 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3806 0.4217 0.3497 -0.0701 0.0190  -0.0824 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.4049 0.5141 0.3676 -0.0655 -0.0011 -0.0793 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3707 0.3972 0.3367 -0.0572 0.0146  -0.0681 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.4372 0.5183 0.4048 -0.0670 0.0093  -0.0844 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3576 0.3796 0.3217 -0.0642 0.0189  -0.0759 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.4058 0.5033 0.3694 -0.0692 0.0055  -0.0857 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2751 0.3746 0.2727 -0.0627 0.0079  -0.0737 12  THR A N   
70   C CA  . THR A 11  ? 0.2804 0.3767 0.2832 -0.0632 0.0120  -0.0732 12  THR A CA  
71   C C   . THR A 11  ? 0.3128 0.3849 0.3057 -0.0597 0.0148  -0.0652 12  THR A C   
72   O O   . THR A 11  ? 0.3086 0.3808 0.3041 -0.0548 0.0141  -0.0605 12  THR A O   
73   C CB  . THR A 11  ? 0.3747 0.4745 0.3830 -0.0746 0.0197  -0.0839 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3611 0.4873 0.3806 -0.0775 0.0158  -0.0925 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.4199 0.5191 0.4343 -0.0770 0.0256  -0.0854 12  THR A CG2 
76   N N   . ARG A 12  ? 0.3002 0.3521 0.2820 -0.0618 0.0176  -0.0646 13  ARG A N   
77   C CA  . ARG A 12  ? 0.3251 0.3542 0.2966 -0.0583 0.0188  -0.0582 13  ARG A CA  
78   C C   . ARG A 12  ? 0.3420 0.3697 0.3117 -0.0493 0.0129  -0.0512 13  ARG A C   
79   O O   . ARG A 12  ? 0.3291 0.3404 0.2916 -0.0460 0.0127  -0.0470 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3936 0.3994 0.3534 -0.0630 0.0231  -0.0608 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.5343 0.5328 0.4906 -0.0742 0.0315  -0.0675 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.8282 0.8178 0.7799 -0.0774 0.0366  -0.0654 13  ARG A CD  
83   N NE  . ARG A 12  ? 1.0088 0.9703 0.9433 -0.0733 0.0356  -0.0582 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.1510 1.1037 1.0790 -0.0732 0.0376  -0.0541 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 1.0118 0.9390 0.9224 -0.0692 0.0351  -0.0478 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.9219 0.8918 0.8610 -0.0765 0.0415  -0.0569 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2860 0.3297 0.2607 -0.0461 0.0085  -0.0505 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2816 0.3232 0.2535 -0.0402 0.0051  -0.0456 14  HIS A CA  
89   C C   . HIS A 13  ? 0.3086 0.3435 0.2792 -0.0358 0.0046  -0.0393 14  HIS A C   
90   O O   . HIS A 13  ? 0.3082 0.3328 0.2750 -0.0330 0.0040  -0.0373 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2788 0.3356 0.2517 -0.0393 0.0016  -0.0454 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.3074 0.3609 0.2761 -0.0359 0.0005  -0.0417 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.3205 0.3686 0.2881 -0.0365 0.0021  -0.0453 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.3134 0.3679 0.2791 -0.0325 -0.0012 -0.0359 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.3184 0.3670 0.2838 -0.0346 0.0019  -0.0426 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.3134 0.3641 0.2760 -0.0328 0.0003  -0.0364 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2785 0.3207 0.2537 -0.0347 0.0046  -0.0373 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2764 0.3119 0.2502 -0.0309 0.0049  -0.0321 15  ALA A CA  
99   C C   . ALA A 14  ? 0.3216 0.3402 0.2890 -0.0326 0.0079  -0.0318 15  ALA A C   
100  O O   . ALA A 14  ? 0.2856 0.2959 0.2486 -0.0297 0.0067  -0.0285 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2846 0.3304 0.2659 -0.0287 0.0047  -0.0316 15  ALA A CB  
102  N N   A SER A 15  ? 0.3076 0.3201 0.2725 -0.0380 0.0116  -0.0357 16  SER A N   
103  N N   B SER A 15  ? 0.3011 0.3135 0.2659 -0.0380 0.0116  -0.0357 16  SER A N   
104  N N   C SER A 15  ? 0.3014 0.3138 0.2663 -0.0380 0.0117  -0.0357 16  SER A N   
105  C CA  A SER A 15  ? 0.3200 0.3121 0.2734 -0.0404 0.0143  -0.0350 16  SER A CA  
106  C CA  B SER A 15  ? 0.3121 0.3041 0.2654 -0.0405 0.0143  -0.0350 16  SER A CA  
107  C CA  C SER A 15  ? 0.3127 0.3046 0.2660 -0.0403 0.0142  -0.0349 16  SER A CA  
108  C C   A SER A 15  ? 0.3661 0.3461 0.3122 -0.0364 0.0098  -0.0336 16  SER A C   
109  C C   B SER A 15  ? 0.3664 0.3461 0.3124 -0.0365 0.0099  -0.0337 16  SER A C   
110  C C   C SER A 15  ? 0.3674 0.3469 0.3132 -0.0365 0.0099  -0.0336 16  SER A C   
111  O O   A SER A 15  ? 0.3392 0.3064 0.2773 -0.0335 0.0077  -0.0306 16  SER A O   
112  O O   B SER A 15  ? 0.3501 0.3165 0.2877 -0.0337 0.0078  -0.0307 16  SER A O   
113  O O   C SER A 15  ? 0.3523 0.3183 0.2897 -0.0337 0.0078  -0.0307 16  SER A O   
114  C CB  A SER A 15  ? 0.3696 0.3560 0.3195 -0.0488 0.0205  -0.0401 16  SER A CB  
115  C CB  B SER A 15  ? 0.3565 0.3425 0.3062 -0.0488 0.0205  -0.0401 16  SER A CB  
116  C CB  C SER A 15  ? 0.3592 0.3448 0.3086 -0.0486 0.0207  -0.0397 16  SER A CB  
117  O OG  A SER A 15  ? 0.4425 0.4046 0.3761 -0.0519 0.0235  -0.0386 16  SER A OG  
118  O OG  B SER A 15  ? 0.3929 0.3932 0.3525 -0.0524 0.0249  -0.0435 16  SER A OG  
119  O OG  C SER A 15  ? 0.4110 0.3982 0.3613 -0.0517 0.0209  -0.0441 16  SER A OG  
120  N N   . ASP A 16  ? 0.3286 0.3141 0.2785 -0.0358 0.0080  -0.0368 17  ASP A N   
121  C CA  . ASP A 16  ? 0.3465 0.3240 0.2938 -0.0311 0.0039  -0.0379 17  ASP A CA  
122  C C   . ASP A 16  ? 0.3445 0.3295 0.2967 -0.0257 0.0001  -0.0356 17  ASP A C   
123  O O   . ASP A 16  ? 0.3384 0.3150 0.2877 -0.0211 -0.0039 -0.0356 17  ASP A O   
124  C CB  . ASP A 16  ? 0.3700 0.3549 0.3223 -0.0327 0.0045  -0.0434 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.5322 0.5054 0.4782 -0.0386 0.0086  -0.0472 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.5109 0.4682 0.4470 -0.0417 0.0114  -0.0453 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.5581 0.5372 0.5078 -0.0412 0.0100  -0.0526 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2907 0.2908 0.2494 -0.0264 0.0010  -0.0340 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2858 0.2909 0.2472 -0.0235 -0.0006 -0.0322 18  VAL A CA  
130  C C   . VAL A 17  ? 0.3280 0.3228 0.2844 -0.0219 -0.0015 -0.0292 18  VAL A C   
131  O O   . VAL A 17  ? 0.3068 0.2993 0.2634 -0.0189 -0.0046 -0.0304 18  VAL A O   
132  C CB  . VAL A 17  ? 0.3071 0.3242 0.2714 -0.0248 0.0010  -0.0298 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.3077 0.3247 0.2716 -0.0236 0.0014  -0.0272 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2954 0.3223 0.2616 -0.0268 0.0012  -0.0332 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2973 0.2871 0.2498 -0.0242 0.0013  -0.0265 19  LEU A N   
136  C CA  . LEU A 18  ? 0.3102 0.2898 0.2561 -0.0238 0.0014  -0.0241 19  LEU A CA  
137  C C   . LEU A 18  ? 0.3341 0.2981 0.2697 -0.0220 -0.0026 -0.0248 19  LEU A C   
138  O O   . LEU A 18  ? 0.3271 0.2866 0.2590 -0.0194 -0.0063 -0.0243 19  LEU A O   
139  C CB  . LEU A 18  ? 0.3219 0.3003 0.2665 -0.0274 0.0067  -0.0229 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3719 0.3423 0.3108 -0.0279 0.0084  -0.0210 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.3717 0.3493 0.3163 -0.0252 0.0077  -0.0194 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.4280 0.3976 0.3669 -0.0321 0.0149  -0.0220 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.3288 0.2838 0.2592 -0.0230 -0.0026 -0.0263 20  LEU A N   
144  C CA  . LEU A 19  ? 0.3494 0.2853 0.2672 -0.0196 -0.0076 -0.0263 20  LEU A CA  
145  C C   . LEU A 19  ? 0.3709 0.3134 0.2962 -0.0120 -0.0153 -0.0291 20  LEU A C   
146  O O   . LEU A 19  ? 0.3635 0.2968 0.2815 -0.0074 -0.0217 -0.0285 20  LEU A O   
147  C CB  . LEU A 19  ? 0.3785 0.3034 0.2905 -0.0222 -0.0052 -0.0282 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4993 0.3980 0.3941 -0.0183 -0.0103 -0.0273 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.5389 0.4163 0.4128 -0.0219 -0.0089 -0.0226 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.5680 0.4558 0.4584 -0.0215 -0.0066 -0.0300 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.3252 0.2854 0.2654 -0.0112 -0.0145 -0.0330 21  ASN A N   
152  C CA  . ASN A 20  ? 0.3116 0.2823 0.2624 -0.0056 -0.0197 -0.0381 21  ASN A CA  
153  C C   . ASN A 20  ? 0.3448 0.3239 0.2994 -0.0057 -0.0209 -0.0379 21  ASN A C   
154  O O   . ASN A 20  ? 0.3346 0.3161 0.2929 -0.0005 -0.0273 -0.0419 21  ASN A O   
155  C CB  . ASN A 20  ? 0.3534 0.3391 0.3165 -0.0069 -0.0165 -0.0431 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.4511 0.4279 0.4124 -0.0044 -0.0178 -0.0464 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.4305 0.3896 0.3831 0.0010  -0.0230 -0.0461 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3713 0.3577 0.3385 -0.0083 -0.0130 -0.0497 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2987 0.2823 0.2527 -0.0112 -0.0149 -0.0340 22  LEU A N   
160  C CA  . LEU A 21  ? 0.3053 0.2932 0.2606 -0.0125 -0.0145 -0.0338 22  LEU A CA  
161  C C   . LEU A 21  ? 0.3354 0.3100 0.2796 -0.0100 -0.0199 -0.0325 22  LEU A C   
162  O O   . LEU A 21  ? 0.3256 0.3049 0.2727 -0.0083 -0.0242 -0.0359 22  LEU A O   
163  C CB  . LEU A 21  ? 0.3094 0.2995 0.2639 -0.0175 -0.0074 -0.0292 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.3459 0.3475 0.3073 -0.0198 -0.0033 -0.0296 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.3585 0.3589 0.3171 -0.0219 0.0014  -0.0243 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.3476 0.3593 0.3162 -0.0210 -0.0028 -0.0349 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.3196 0.2775 0.2500 -0.0108 -0.0195 -0.0283 23  ASN A N   
168  C CA  . ASN A 22  ? 0.3424 0.2836 0.2567 -0.0092 -0.0246 -0.0264 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3912 0.3281 0.3039 -0.0006 -0.0360 -0.0298 23  ASN A C   
170  O O   . ASN A 22  ? 0.4111 0.3435 0.3165 0.0025  -0.0431 -0.0305 23  ASN A O   
171  C CB  . ASN A 22  ? 0.3629 0.2852 0.2605 -0.0138 -0.0198 -0.0219 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4712 0.3759 0.3489 -0.0151 -0.0224 -0.0194 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.4412 0.3513 0.3198 -0.0150 -0.0245 -0.0206 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4923 0.3742 0.3498 -0.0172 -0.0217 -0.0164 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.3604 0.2993 0.2804 0.0039  -0.0382 -0.0326 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3752 0.3121 0.2977 0.0142  -0.0495 -0.0373 24  ARG A CA  
177  C C   . ARG A 23  ? 0.4083 0.3686 0.3493 0.0169  -0.0537 -0.0449 24  ARG A C   
178  O O   . ARG A 23  ? 0.4060 0.3660 0.3464 0.0246  -0.0647 -0.0486 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3665 0.3032 0.2963 0.0174  -0.0486 -0.0404 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.4249 0.3348 0.3346 0.0154  -0.0461 -0.0346 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.4678 0.3799 0.3860 0.0155  -0.0421 -0.0383 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.5709 0.4551 0.4689 0.0133  -0.0399 -0.0342 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.7688 0.6504 0.6685 0.0088  -0.0331 -0.0362 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.6009 0.5064 0.5203 0.0064  -0.0286 -0.0415 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.6797 0.5335 0.5594 0.0056  -0.0303 -0.0331 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.3560 0.3360 0.3121 0.0102  -0.0450 -0.0476 25  LEU A N   
187  C CA  . LEU A 24  ? 0.3376 0.3390 0.3101 0.0096  -0.0461 -0.0557 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3866 0.3843 0.3502 0.0078  -0.0493 -0.0543 25  LEU A C   
189  O O   . LEU A 24  ? 0.3833 0.3919 0.3549 0.0118  -0.0572 -0.0617 25  LEU A O   
190  C CB  . LEU A 24  ? 0.3242 0.3401 0.3072 0.0009  -0.0346 -0.0569 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.3729 0.3967 0.3656 0.0008  -0.0305 -0.0603 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.3715 0.4069 0.3695 -0.0084 -0.0199 -0.0609 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.3704 0.4058 0.3784 0.0087  -0.0376 -0.0712 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.3444 0.3280 0.2925 0.0017  -0.0433 -0.0461 26  ARG A N   
195  C CA  . ARG A 25  ? 0.3601 0.3381 0.2977 -0.0008 -0.0454 -0.0451 26  ARG A CA  
196  C C   . ARG A 25  ? 0.4371 0.4036 0.3621 0.0076  -0.0594 -0.0459 26  ARG A C   
197  O O   . ARG A 25  ? 0.4451 0.4196 0.3720 0.0090  -0.0664 -0.0513 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3841 0.3477 0.3074 -0.0079 -0.0363 -0.0372 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.4398 0.3982 0.3525 -0.0115 -0.0370 -0.0375 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.5001 0.4467 0.4020 -0.0184 -0.0270 -0.0320 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.4652 0.3939 0.3517 -0.0183 -0.0259 -0.0265 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.5982 0.5092 0.4645 -0.0222 -0.0241 -0.0236 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.5546 0.4634 0.4130 -0.0253 -0.0248 -0.0256 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.5016 0.3964 0.3544 -0.0241 -0.0209 -0.0196 26  ARG A NH2 
205  N N   A SER A 26  ? 0.4216 0.3683 0.3321 0.0126  -0.0634 -0.0407 27  SER A N   
206  N N   B SER A 26  ? 0.4184 0.3652 0.3291 0.0127  -0.0633 -0.0407 27  SER A N   
207  N N   C SER A 26  ? 0.4230 0.3697 0.3335 0.0126  -0.0634 -0.0406 27  SER A N   
208  C CA  A SER A 26  ? 0.4505 0.3791 0.3430 0.0215  -0.0771 -0.0393 27  SER A CA  
209  C CA  B SER A 26  ? 0.4464 0.3748 0.3393 0.0217  -0.0770 -0.0392 27  SER A CA  
210  C CA  C SER A 26  ? 0.4530 0.3816 0.3456 0.0215  -0.0771 -0.0393 27  SER A CA  
211  C C   A SER A 26  ? 0.5134 0.4593 0.4227 0.0326  -0.0908 -0.0489 27  SER A C   
212  C C   B SER A 26  ? 0.5103 0.4562 0.4196 0.0325  -0.0906 -0.0488 27  SER A C   
213  C C   C SER A 26  ? 0.5138 0.4597 0.4231 0.0326  -0.0908 -0.0489 27  SER A C   
214  O O   A SER A 26  ? 0.5306 0.4709 0.4292 0.0391  -0.1037 -0.0503 27  SER A O   
215  O O   B SER A 26  ? 0.5266 0.4667 0.4249 0.0387  -0.1033 -0.0501 27  SER A O   
216  O O   C SER A 26  ? 0.5305 0.4707 0.4290 0.0391  -0.1037 -0.0503 27  SER A O   
217  C CB  A SER A 26  ? 0.5092 0.4117 0.3839 0.0239  -0.0767 -0.0325 27  SER A CB  
218  C CB  B SER A 26  ? 0.5004 0.4058 0.3794 0.0250  -0.0768 -0.0335 27  SER A CB  
219  C CB  C SER A 26  ? 0.5164 0.4192 0.3915 0.0241  -0.0767 -0.0326 27  SER A CB  
220  O OG  A SER A 26  ? 0.5743 0.4838 0.4645 0.0306  -0.0786 -0.0365 27  SER A OG  
221  O OG  B SER A 26  ? 0.5827 0.4672 0.4405 0.0159  -0.0673 -0.0256 27  SER A OG  
222  O OG  C SER A 26  ? 0.6452 0.5244 0.4974 0.0327  -0.0900 -0.0298 27  SER A OG  
223  N N   . ARG A 27  ? 0.4528 0.4209 0.3885 0.0345  -0.0880 -0.0565 28  ARG A N   
224  C CA  . ARG A 27  ? 0.4585 0.4484 0.4162 0.0444  -0.0990 -0.0685 28  ARG A CA  
225  C C   . ARG A 27  ? 0.4710 0.4908 0.4500 0.0376  -0.0952 -0.0786 28  ARG A C   
226  O O   . ARG A 27  ? 0.4643 0.5079 0.4662 0.0434  -0.1019 -0.0912 28  ARG A O   
227  C CB  . ARG A 27  ? 0.4740 0.4689 0.4468 0.0501  -0.0975 -0.0726 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.5727 0.5357 0.5236 0.0567  -0.1014 -0.0638 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.6363 0.6030 0.6007 0.0589  -0.0960 -0.0674 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.8008 0.7900 0.7915 0.0695  -0.1042 -0.0809 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.9945 1.0026 1.0078 0.0679  -0.0967 -0.0895 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.8525 0.8827 0.8913 0.0774  -0.1035 -0.1036 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.8127 0.8192 0.8236 0.0566  -0.0822 -0.0850 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.3959 0.4140 0.3676 0.0251  -0.0841 -0.0740 29  ASP A N   
235  C CA  . ASP A 28  ? 0.3943 0.4342 0.3808 0.0160  -0.0777 -0.0820 29  ASP A CA  
236  C C   . ASP A 28  ? 0.4398 0.5036 0.4522 0.0121  -0.0692 -0.0914 29  ASP A C   
237  O O   . ASP A 28  ? 0.4477 0.5352 0.4790 0.0090  -0.0691 -0.1038 29  ASP A O   
238  C CB  . ASP A 28  ? 0.4313 0.4813 0.4195 0.0202  -0.0908 -0.0903 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.5631 0.6275 0.5582 0.0079  -0.0826 -0.0964 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.5464 0.5999 0.5319 -0.0026 -0.0689 -0.0891 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.6301 0.7168 0.6408 0.0090  -0.0899 -0.1094 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.3652 0.4230 0.3777 0.0112  -0.0615 -0.0864 30  ILE A N   
243  C CA  . ILE A 29  ? 0.3452 0.4226 0.3780 0.0069  -0.0531 -0.0947 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3806 0.4572 0.4093 -0.0066 -0.0377 -0.0905 30  ILE A C   
245  O O   . ILE A 29  ? 0.3471 0.4059 0.3598 -0.0094 -0.0324 -0.0787 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3823 0.4553 0.4181 0.0142  -0.0546 -0.0940 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.4050 0.4781 0.4463 0.0295  -0.0707 -0.0998 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.3613 0.4523 0.4139 0.0072  -0.0432 -0.1018 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.4657 0.5244 0.5027 0.0376  -0.0730 -0.0964 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.3477 0.4434 0.3910 -0.0149 -0.0307 -0.1009 31  LEU A N   
251  C CA  . LEU A 30  ? 0.3482 0.4413 0.3864 -0.0280 -0.0160 -0.0980 31  LEU A CA  
252  C C   . LEU A 30  ? 0.3808 0.4555 0.4008 -0.0325 -0.0126 -0.0876 31  LEU A C   
253  O O   . LEU A 30  ? 0.3683 0.4340 0.3798 -0.0403 -0.0018 -0.0818 31  LEU A O   
254  C CB  . LEU A 30  ? 0.3602 0.4496 0.3959 -0.0305 -0.0079 -0.0936 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.4470 0.5571 0.5017 -0.0316 -0.0051 -0.1069 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.4614 0.5661 0.5091 -0.0368 0.0043  -0.1022 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.5212 0.6507 0.5902 -0.0411 0.0012  -0.1208 31  LEU A CD2 
258  N N   . THR A 31  ? 0.3399 0.4090 0.3536 -0.0277 -0.0217 -0.0863 32  THR A N   
259  C CA  . THR A 31  ? 0.3434 0.3979 0.3423 -0.0329 -0.0178 -0.0798 32  THR A CA  
260  C C   . THR A 31  ? 0.4194 0.4849 0.4262 -0.0440 -0.0092 -0.0890 32  THR A C   
261  O O   . THR A 31  ? 0.4093 0.4958 0.4329 -0.0456 -0.0117 -0.1022 32  THR A O   
262  C CB  . THR A 31  ? 0.4063 0.4526 0.3949 -0.0263 -0.0292 -0.0779 32  THR A CB  
263  O OG1 . THR A 31  ? 0.4144 0.4788 0.4161 -0.0221 -0.0397 -0.0898 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3764 0.4058 0.3522 -0.0180 -0.0346 -0.0678 32  THR A CG2 
265  N N   . ASP A 32  ? 0.3829 0.4344 0.3786 -0.0520 0.0016  -0.0829 33  ASP A N   
266  C CA  . ASP A 32  ? 0.3860 0.4420 0.3853 -0.0642 0.0123  -0.0904 33  ASP A CA  
267  C C   . ASP A 32  ? 0.4080 0.4507 0.3960 -0.0699 0.0167  -0.0886 33  ASP A C   
268  O O   . ASP A 32  ? 0.4139 0.4536 0.4005 -0.0809 0.0275  -0.0930 33  ASP A O   
269  C CB  . ASP A 32  ? 0.4071 0.4571 0.4030 -0.0699 0.0238  -0.0864 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.5304 0.5593 0.5108 -0.0653 0.0260  -0.0712 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.4700 0.4885 0.4429 -0.0592 0.0210  -0.0643 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.6678 0.6915 0.6434 -0.0681 0.0327  -0.0671 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.3389 0.3715 0.3172 -0.0636 0.0096  -0.0827 34  VAL A N   
274  C CA  . VAL A 33  ? 0.3409 0.3613 0.3086 -0.0692 0.0139  -0.0823 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3825 0.4008 0.3429 -0.0631 0.0027  -0.0818 34  VAL A C   
276  O O   . VAL A 33  ? 0.3759 0.3923 0.3331 -0.0538 -0.0061 -0.0762 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3862 0.3837 0.3412 -0.0710 0.0249  -0.0714 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.3676 0.3543 0.3150 -0.0616 0.0207  -0.0602 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.4004 0.3854 0.3472 -0.0792 0.0331  -0.0740 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3505 0.3672 0.3057 -0.0694 0.0036  -0.0876 35  VAL A N   
281  N N   B VAL A 34  ? 0.3444 0.3612 0.2996 -0.0693 0.0034  -0.0876 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3552 0.3658 0.2978 -0.0661 -0.0052 -0.0870 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.3465 0.3567 0.2889 -0.0655 -0.0056 -0.0864 35  VAL A CA  
284  C C   A VAL A 34  ? 0.4063 0.3958 0.3347 -0.0714 0.0057  -0.0814 35  VAL A C   
285  C C   B VAL A 34  ? 0.4061 0.3962 0.3342 -0.0714 0.0049  -0.0819 35  VAL A C   
286  O O   A VAL A 34  ? 0.4034 0.3892 0.3336 -0.0801 0.0166  -0.0851 35  VAL A O   
287  O O   B VAL A 34  ? 0.4087 0.3963 0.3386 -0.0805 0.0151  -0.0867 35  VAL A O   
288  C CB  A VAL A 34  ? 0.4158 0.4441 0.3642 -0.0690 -0.0145 -0.1004 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.4002 0.4283 0.3477 -0.0647 -0.0186 -0.0982 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.4293 0.4476 0.3591 -0.0666 -0.0234 -0.0991 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.4032 0.4413 0.3572 -0.0768 -0.0123 -0.1106 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.4085 0.4600 0.3748 -0.0621 -0.0256 -0.1078 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.4112 0.4279 0.3398 -0.0585 -0.0300 -0.0938 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.3649 0.3398 0.2795 -0.0665 0.0037  -0.0731 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3778 0.3345 0.2803 -0.0705 0.0135  -0.0696 36  ILE A CA  
296  C C   . ILE A 35  ? 0.4499 0.4037 0.3384 -0.0736 0.0074  -0.0747 36  ILE A C   
297  O O   . ILE A 35  ? 0.4442 0.3967 0.3227 -0.0681 -0.0034 -0.0722 36  ILE A O   
298  C CB  . ILE A 35  ? 0.4021 0.3463 0.3001 -0.0647 0.0175  -0.0590 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3832 0.3316 0.2934 -0.0606 0.0207  -0.0537 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.4270 0.3554 0.3162 -0.0686 0.0281  -0.0580 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3946 0.3421 0.3119 -0.0659 0.0304  -0.0558 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.4105 0.3610 0.2958 -0.0825 0.0145  -0.0817 37  VAL A N   
303  C CA  . VAL A 36  ? 0.4252 0.3730 0.2955 -0.0871 0.0094  -0.0878 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4937 0.4208 0.3484 -0.0900 0.0193  -0.0837 37  VAL A C   
305  O O   . VAL A 36  ? 0.4786 0.3966 0.3377 -0.0937 0.0328  -0.0835 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4800 0.4402 0.3570 -0.0965 0.0101  -0.1009 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4961 0.4544 0.3559 -0.1013 0.0036  -0.1078 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4747 0.4588 0.3704 -0.0941 0.0014  -0.1072 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.4667 0.3853 0.3025 -0.0883 0.0128  -0.0811 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4818 0.3820 0.3016 -0.0921 0.0223  -0.0787 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5839 0.4794 0.3813 -0.0979 0.0155  -0.0847 38  VAL A C   
312  O O   . VAL A 37  ? 0.5552 0.4472 0.3362 -0.0941 0.0034  -0.0812 38  VAL A O   
313  C CB  . VAL A 37  ? 0.5296 0.4215 0.3459 -0.0857 0.0234  -0.0690 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.5396 0.4162 0.3460 -0.0906 0.0368  -0.0690 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.5057 0.4067 0.3440 -0.0786 0.0251  -0.0636 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5928 0.4879 0.3883 -0.1071 0.0221  -0.0939 39  SER A N   
317  N N   B SER A 38  ? 0.5815 0.4753 0.3767 -0.1073 0.0233  -0.0936 39  SER A N   
318  C CA  A SER A 38  ? 0.6231 0.5161 0.3978 -0.1142 0.0155  -0.1016 39  SER A CA  
319  C CA  B SER A 38  ? 0.6081 0.4990 0.3830 -0.1151 0.0184  -0.1017 39  SER A CA  
320  C C   A SER A 38  ? 0.6345 0.5453 0.4109 -0.1091 -0.0047 -0.1048 39  SER A C   
321  C C   B SER A 38  ? 0.6403 0.5424 0.4071 -0.1098 -0.0026 -0.1025 39  SER A C   
322  O O   A SER A 38  ? 0.6065 0.5359 0.4056 -0.1080 -0.0070 -0.1098 39  SER A O   
323  O O   B SER A 38  ? 0.6473 0.5381 0.3892 -0.1077 -0.0118 -0.0984 39  SER A O   
324  C CB  A SER A 38  ? 0.7191 0.5919 0.4656 -0.1169 0.0180  -0.0977 39  SER A CB  
325  C CB  B SER A 38  ? 0.6864 0.5566 0.4383 -0.1210 0.0282  -0.1008 39  SER A CB  
326  O OG  A SER A 38  ? 0.9020 0.7624 0.6520 -0.1197 0.0361  -0.0959 39  SER A OG  
327  O OG  B SER A 38  ? 0.7960 0.6597 0.5579 -0.1267 0.0462  -0.1051 39  SER A OG  
328  N N   A ARG A 39  ? 0.5895 0.4937 0.3419 -0.1054 -0.0191 -0.1020 40  ARG A N   
329  N N   B ARG A 39  ? 0.5598 0.4836 0.3488 -0.1069 -0.0098 -0.1076 40  ARG A N   
330  C CA  A ARG A 39  ? 0.5879 0.5070 0.3399 -0.0980 -0.0406 -0.1049 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.5556 0.4979 0.3488 -0.1003 -0.0296 -0.1116 40  ARG A CA  
332  C C   A ARG A 39  ? 0.6133 0.5380 0.3780 -0.0848 -0.0495 -0.0966 40  ARG A C   
333  C C   B ARG A 39  ? 0.5814 0.5231 0.3763 -0.0869 -0.0403 -0.1012 40  ARG A C   
334  O O   A ARG A 39  ? 0.6016 0.5405 0.3712 -0.0764 -0.0673 -0.0997 40  ARG A O   
335  O O   B ARG A 39  ? 0.5697 0.5307 0.3797 -0.0796 -0.0535 -0.1051 40  ARG A O   
336  C CB  A ARG A 39  ? 0.6140 0.5191 0.3297 -0.0990 -0.0533 -0.1050 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.5890 0.5319 0.3599 -0.1041 -0.0425 -0.1193 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.7128 0.6213 0.4182 -0.1110 -0.0516 -0.1172 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.7298 0.6811 0.5056 -0.1175 -0.0341 -0.1331 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.7225 0.6193 0.3909 -0.1103 -0.0683 -0.1173 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.8385 0.8004 0.6000 -0.1201 -0.0507 -0.1436 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.7849 0.6813 0.4386 -0.1236 -0.0644 -0.1287 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.9305 0.9010 0.6977 -0.1345 -0.0415 -0.1582 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.9547 0.8738 0.6175 -0.1266 -0.0750 -0.1422 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 1.0925 1.0459 0.8386 -0.1458 -0.0310 -0.1616 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.8063 0.7228 0.4536 -0.1399 -0.0701 -0.1526 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.9314 0.8592 0.6498 -0.1449 -0.0275 -0.1519 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.7716 0.7178 0.4604 -0.1172 -0.0899 -0.1468 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.9099 0.8714 0.6627 -0.1590 -0.0225 -0.1758 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.5562 0.4703 0.3266 -0.0826 -0.0377 -0.0871 41  GLU A N   
351  N N   B GLU A 40  ? 0.5398 0.4610 0.3222 -0.0841 -0.0336 -0.0897 41  GLU A N   
352  C CA  A GLU A 40  ? 0.5410 0.4581 0.3221 -0.0713 -0.0442 -0.0793 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.5319 0.4495 0.3151 -0.0730 -0.0411 -0.0800 41  GLU A CA  
354  C C   A GLU A 40  ? 0.5513 0.4875 0.3656 -0.0695 -0.0377 -0.0814 41  GLU A C   
355  C C   B GLU A 40  ? 0.5447 0.4786 0.3594 -0.0692 -0.0356 -0.0795 41  GLU A C   
356  O O   A GLU A 40  ? 0.5196 0.4578 0.3455 -0.0769 -0.0233 -0.0843 41  GLU A O   
357  O O   B GLU A 40  ? 0.5032 0.4360 0.3293 -0.0746 -0.0201 -0.0793 41  GLU A O   
358  C CB  A GLU A 40  ? 0.5687 0.4623 0.3323 -0.0701 -0.0372 -0.0680 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.5636 0.4556 0.3250 -0.0741 -0.0330 -0.0700 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.7934 0.6640 0.5194 -0.0725 -0.0432 -0.0649 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.7615 0.6336 0.4862 -0.0766 -0.0408 -0.0685 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.2640 1.1236 0.9731 -0.0621 -0.0596 -0.0578 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.2086 1.0691 0.9159 -0.0665 -0.0563 -0.0608 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.2720 1.1226 0.9828 -0.0580 -0.0556 -0.0498 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.2242 1.0874 0.9198 -0.0609 -0.0747 -0.0636 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.2763 1.1357 0.9698 -0.0577 -0.0770 -0.0605 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.2278 1.0763 0.9332 -0.0639 -0.0506 -0.0524 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4956 0.4431 0.3229 -0.0595 -0.0481 -0.0795 42  GLN A N   
369  C CA  . GLN A 41  ? 0.4678 0.4323 0.3235 -0.0571 -0.0435 -0.0810 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4932 0.4508 0.3507 -0.0486 -0.0443 -0.0712 42  GLN A C   
371  O O   . GLN A 41  ? 0.5041 0.4529 0.3477 -0.0409 -0.0561 -0.0668 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4867 0.4773 0.3605 -0.0543 -0.0555 -0.0926 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.6684 0.6706 0.5463 -0.0649 -0.0525 -0.1049 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.9134 0.9460 0.8151 -0.0642 -0.0612 -0.1188 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.8020 0.8493 0.7202 -0.0552 -0.0695 -0.1203 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.9385 0.9822 0.8437 -0.0746 -0.0587 -0.1309 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.4044 0.3641 0.2768 -0.0501 -0.0320 -0.0676 43  PHE A N   
378  C CA  . PHE A 42  ? 0.4069 0.3620 0.2827 -0.0434 -0.0314 -0.0593 43  PHE A CA  
379  C C   . PHE A 42  ? 0.4437 0.4163 0.3436 -0.0422 -0.0282 -0.0622 43  PHE A C   
380  O O   . PHE A 42  ? 0.4438 0.4197 0.3526 -0.0487 -0.0169 -0.0639 43  PHE A O   
381  C CB  . PHE A 42  ? 0.4297 0.3674 0.2959 -0.0469 -0.0189 -0.0514 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.4673 0.3864 0.3084 -0.0505 -0.0186 -0.0494 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.5022 0.4169 0.3359 -0.0586 -0.0118 -0.0539 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.5168 0.4206 0.3394 -0.0469 -0.0242 -0.0434 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.5454 0.4425 0.3541 -0.0633 -0.0105 -0.0530 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.5785 0.4627 0.3741 -0.0521 -0.0227 -0.0418 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.5515 0.4334 0.3406 -0.0603 -0.0159 -0.0469 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3955 0.3778 0.3046 -0.0341 -0.0376 -0.0630 44  ARG A N   
389  C CA  . ARG A 43  ? 0.3640 0.3631 0.2949 -0.0337 -0.0340 -0.0667 44  ARG A CA  
390  C C   . ARG A 43  ? 0.4013 0.3912 0.3317 -0.0322 -0.0263 -0.0574 44  ARG A C   
391  O O   . ARG A 43  ? 0.3944 0.3704 0.3125 -0.0279 -0.0289 -0.0504 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3901 0.4062 0.3338 -0.0256 -0.0472 -0.0742 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.4488 0.4800 0.3975 -0.0266 -0.0564 -0.0860 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.5704 0.6285 0.5442 -0.0222 -0.0633 -0.0981 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.6971 0.7647 0.6871 -0.0284 -0.0499 -0.1000 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.8488 0.9311 0.8522 -0.0392 -0.0401 -0.1093 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.7665 0.8603 0.7737 -0.0449 -0.0426 -0.1197 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.5973 0.6827 0.6094 -0.0449 -0.0278 -0.1090 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.3560 0.3525 0.2980 -0.0364 -0.0165 -0.0577 45  ALA A N   
400  C CA  . ALA A 44  ? 0.3571 0.3469 0.2989 -0.0347 -0.0104 -0.0496 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3654 0.3657 0.3199 -0.0377 -0.0039 -0.0518 45  ALA A C   
402  O O   . ALA A 44  ? 0.3387 0.3513 0.3026 -0.0421 -0.0028 -0.0600 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3745 0.3488 0.3053 -0.0376 -0.0023 -0.0429 45  ALA A CB  
404  N N   . HIS A 45  ? 0.3294 0.3256 0.2835 -0.0359 0.0002  -0.0451 46  HIS A N   
405  C CA  . HIS A 45  ? 0.3101 0.3120 0.2706 -0.0391 0.0066  -0.0454 46  HIS A CA  
406  C C   . HIS A 45  ? 0.3540 0.3432 0.3068 -0.0428 0.0155  -0.0396 46  HIS A C   
407  O O   . HIS A 45  ? 0.3417 0.3212 0.2885 -0.0394 0.0161  -0.0331 46  HIS A O   
408  C CB  . HIS A 45  ? 0.2974 0.3023 0.2607 -0.0343 0.0043  -0.0421 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.3368 0.3508 0.3070 -0.0290 -0.0045 -0.0475 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.3627 0.3682 0.3262 -0.0230 -0.0115 -0.0442 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.3451 0.3743 0.3279 -0.0288 -0.0070 -0.0565 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.3598 0.3735 0.3308 -0.0179 -0.0192 -0.0503 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.3470 0.3771 0.3319 -0.0207 -0.0170 -0.0585 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.3399 0.3284 0.2928 -0.0497 0.0226  -0.0427 47  LYS A N   
415  C CA  . LYS A 46  ? 0.3413 0.3139 0.2850 -0.0522 0.0308  -0.0371 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3724 0.3388 0.3123 -0.0462 0.0306  -0.0280 47  LYS A C   
417  O O   . LYS A 46  ? 0.3443 0.2997 0.2794 -0.0427 0.0324  -0.0228 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3688 0.3389 0.3103 -0.0615 0.0392  -0.0413 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.3731 0.3466 0.3174 -0.0689 0.0415  -0.0506 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.3727 0.3444 0.3152 -0.0802 0.0515  -0.0563 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.4732 0.4548 0.4227 -0.0885 0.0529  -0.0685 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.4591 0.4412 0.4082 -0.1017 0.0639  -0.0764 47  LYS A NZ  
423  N N   . THR A 47  ? 0.3314 0.3065 0.2745 -0.0446 0.0281  -0.0274 48  THR A N   
424  C CA  . THR A 47  ? 0.3258 0.2971 0.2650 -0.0395 0.0271  -0.0200 48  THR A CA  
425  C C   . THR A 47  ? 0.3473 0.3188 0.2892 -0.0329 0.0228  -0.0168 48  THR A C   
426  O O   . THR A 47  ? 0.3565 0.3224 0.2961 -0.0287 0.0233  -0.0116 48  THR A O   
427  C CB  . THR A 47  ? 0.4269 0.4077 0.3680 -0.0406 0.0260  -0.0212 48  THR A CB  
428  O OG1 . THR A 47  ? 0.4252 0.4190 0.3763 -0.0394 0.0208  -0.0273 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.4601 0.4374 0.3949 -0.0487 0.0330  -0.0235 48  THR A CG2 
430  N N   . VAL A 48  ? 0.3015 0.2789 0.2476 -0.0321 0.0184  -0.0204 49  VAL A N   
431  C CA  . VAL A 48  ? 0.3035 0.2790 0.2496 -0.0283 0.0160  -0.0183 49  VAL A CA  
432  C C   . VAL A 48  ? 0.3430 0.3086 0.2855 -0.0286 0.0203  -0.0172 49  VAL A C   
433  O O   . VAL A 48  ? 0.3198 0.2834 0.2635 -0.0254 0.0218  -0.0147 49  VAL A O   
434  C CB  . VAL A 48  ? 0.3275 0.3062 0.2739 -0.0277 0.0104  -0.0217 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.3420 0.3141 0.2838 -0.0264 0.0103  -0.0198 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.3200 0.3079 0.2716 -0.0262 0.0068  -0.0234 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.3161 0.2770 0.2553 -0.0326 0.0225  -0.0204 50  LEU A N   
438  C CA  . LEU A 49  ? 0.3124 0.2628 0.2477 -0.0335 0.0277  -0.0205 50  LEU A CA  
439  C C   . LEU A 49  ? 0.3530 0.2966 0.2890 -0.0299 0.0322  -0.0160 50  LEU A C   
440  O O   . LEU A 49  ? 0.3485 0.2880 0.2862 -0.0265 0.0347  -0.0153 50  LEU A O   
441  C CB  . LEU A 49  ? 0.3124 0.2595 0.2441 -0.0396 0.0298  -0.0256 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.3601 0.3137 0.2904 -0.0419 0.0235  -0.0309 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.3614 0.3141 0.2897 -0.0484 0.0257  -0.0374 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3903 0.3388 0.3138 -0.0402 0.0211  -0.0298 50  LEU A CD2 
445  N N   . MET A 50  ? 0.3237 0.2655 0.2577 -0.0304 0.0330  -0.0136 51  MET A N   
446  C CA  . MET A 50  ? 0.3478 0.2798 0.2785 -0.0256 0.0353  -0.0082 51  MET A CA  
447  C C   . MET A 50  ? 0.4009 0.3404 0.3378 -0.0177 0.0307  -0.0050 51  MET A C   
448  O O   . MET A 50  ? 0.4058 0.3398 0.3447 -0.0112 0.0315  -0.0028 51  MET A O   
449  C CB  . MET A 50  ? 0.3733 0.2998 0.2959 -0.0292 0.0370  -0.0060 51  MET A CB  
450  C CG  . MET A 50  ? 0.4076 0.3263 0.3248 -0.0381 0.0433  -0.0104 51  MET A CG  
451  S SD  . MET A 50  ? 0.4712 0.3889 0.3802 -0.0449 0.0461  -0.0100 51  MET A SD  
452  C CE  . MET A 50  ? 0.4373 0.3293 0.3299 -0.0406 0.0496  -0.0009 51  MET A CE  
453  N N   . ALA A 51  ? 0.3500 0.3029 0.2913 -0.0181 0.0259  -0.0058 52  ALA A N   
454  C CA  . ALA A 51  ? 0.3360 0.2986 0.2839 -0.0125 0.0219  -0.0044 52  ALA A CA  
455  C C   . ALA A 51  ? 0.3653 0.3309 0.3210 -0.0105 0.0237  -0.0076 52  ALA A C   
456  O O   . ALA A 51  ? 0.3835 0.3571 0.3471 -0.0055 0.0218  -0.0079 52  ALA A O   
457  C CB  . ALA A 51  ? 0.3417 0.3156 0.2913 -0.0150 0.0178  -0.0057 52  ALA A CB  
458  N N   . CYS A 52  ? 0.3211 0.2812 0.2742 -0.0152 0.0275  -0.0111 53  CYS A N   
459  C CA  . CYS A 52  ? 0.3197 0.2807 0.2766 -0.0161 0.0311  -0.0151 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3726 0.3247 0.3303 -0.0148 0.0371  -0.0172 53  CYS A C   
461  O O   . CYS A 52  ? 0.3506 0.3052 0.3136 -0.0151 0.0413  -0.0215 53  CYS A O   
462  C CB  . CYS A 52  ? 0.3249 0.2842 0.2744 -0.0226 0.0306  -0.0176 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.3679 0.3356 0.3173 -0.0233 0.0242  -0.0166 53  CYS A SG  
464  N N   . SER A 53  ? 0.3328 0.2736 0.2844 -0.0151 0.0390  -0.0154 54  SER A N   
465  C CA  . SER A 53  ? 0.3216 0.2510 0.2717 -0.0156 0.0457  -0.0184 54  SER A CA  
466  C C   . SER A 53  ? 0.3886 0.3058 0.3367 -0.0103 0.0471  -0.0148 54  SER A C   
467  O O   . SER A 53  ? 0.3750 0.2862 0.3149 -0.0128 0.0457  -0.0112 54  SER A O   
468  C CB  . SER A 53  ? 0.3477 0.2715 0.2879 -0.0246 0.0478  -0.0217 54  SER A CB  
469  O OG  . SER A 53  ? 0.3929 0.3036 0.3281 -0.0274 0.0539  -0.0244 54  SER A OG  
470  N N   . GLY A 54  ? 0.3677 0.2799 0.3225 -0.0033 0.0504  -0.0164 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3725 0.2677 0.3230 0.0033  0.0518  -0.0128 55  GLY A CA  
472  C C   . GLY A 54  ? 0.4244 0.3018 0.3621 -0.0050 0.0583  -0.0138 55  GLY A C   
473  O O   . GLY A 54  ? 0.4337 0.2953 0.3609 -0.0047 0.0590  -0.0091 55  GLY A O   
474  N N   . LEU A 55  ? 0.3940 0.2737 0.3308 -0.0138 0.0631  -0.0204 56  LEU A N   
475  C CA  . LEU A 55  ? 0.4148 0.2815 0.3408 -0.0232 0.0689  -0.0235 56  LEU A CA  
476  C C   . LEU A 55  ? 0.4384 0.3081 0.3570 -0.0302 0.0655  -0.0212 56  LEU A C   
477  O O   . LEU A 55  ? 0.4309 0.2861 0.3408 -0.0340 0.0697  -0.0201 56  LEU A O   
478  C CB  . LEU A 55  ? 0.4187 0.2881 0.3436 -0.0308 0.0733  -0.0315 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4809 0.3383 0.3957 -0.0408 0.0792  -0.0366 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.5028 0.3388 0.4155 -0.0379 0.0879  -0.0379 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.4566 0.3207 0.3673 -0.0490 0.0798  -0.0436 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3700 0.2575 0.2923 -0.0321 0.0588  -0.0210 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3608 0.2541 0.2795 -0.0380 0.0559  -0.0206 57  PHE A CA  
484  C C   . PHE A 56  ? 0.4198 0.3066 0.3345 -0.0345 0.0554  -0.0141 57  PHE A C   
485  O O   . PHE A 56  ? 0.4133 0.2955 0.3212 -0.0414 0.0582  -0.0149 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3615 0.2729 0.2848 -0.0394 0.0488  -0.0225 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3742 0.2881 0.2952 -0.0448 0.0486  -0.0288 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.4122 0.3229 0.3287 -0.0528 0.0514  -0.0348 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3906 0.3093 0.3119 -0.0427 0.0455  -0.0292 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.4250 0.3379 0.3371 -0.0574 0.0498  -0.0407 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.4296 0.3476 0.3438 -0.0479 0.0445  -0.0342 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.4070 0.3224 0.3166 -0.0546 0.0459  -0.0397 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3872 0.2732 0.3050 -0.0243 0.0521  -0.0085 58  TYR A N   
494  C CA  . TYR A 57  ? 0.4042 0.2809 0.3141 -0.0200 0.0503  -0.0014 58  TYR A CA  
495  C C   . TYR A 57  ? 0.4671 0.3179 0.3630 -0.0232 0.0579  0.0001  58  TYR A C   
496  O O   . TYR A 57  ? 0.4573 0.2990 0.3410 -0.0292 0.0604  0.0025  58  TYR A O   
497  C CB  . TYR A 57  ? 0.4246 0.3058 0.3416 -0.0073 0.0443  0.0029  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4827 0.3513 0.3884 -0.0009 0.0408  0.0108  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.5098 0.3832 0.4078 -0.0048 0.0376  0.0141  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.5408 0.3915 0.4423 0.0095  0.0404  0.0149  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.5609 0.4203 0.4440 0.0002  0.0343  0.0219  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5905 0.4263 0.4775 0.0163  0.0357  0.0232  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6736 0.5135 0.5501 0.0112  0.0325  0.0270  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.7467 0.5698 0.6051 0.0174  0.0276  0.0356  58  TYR A OH  
505  N N   A SER A 58  ? 0.4368 0.2745 0.3335 -0.0202 0.0627  -0.0021 59  SER A N   
506  N N   B SER A 58  ? 0.4369 0.2747 0.3337 -0.0202 0.0627  -0.0021 59  SER A N   
507  C CA  A SER A 58  ? 0.4679 0.2775 0.3508 -0.0232 0.0710  -0.0014 59  SER A CA  
508  C CA  B SER A 58  ? 0.4674 0.2773 0.3506 -0.0232 0.0710  -0.0015 59  SER A CA  
509  C C   A SER A 58  ? 0.5339 0.3416 0.4098 -0.0394 0.0783  -0.0076 59  SER A C   
510  C C   B SER A 58  ? 0.5310 0.3392 0.4070 -0.0393 0.0781  -0.0075 59  SER A C   
511  O O   A SER A 58  ? 0.5698 0.3577 0.4305 -0.0456 0.0843  -0.0056 59  SER A O   
512  O O   B SER A 58  ? 0.5623 0.3516 0.4231 -0.0455 0.0837  -0.0052 59  SER A O   
513  C CB  A SER A 58  ? 0.5045 0.3043 0.3932 -0.0169 0.0749  -0.0048 59  SER A CB  
514  C CB  B SER A 58  ? 0.5050 0.3060 0.3942 -0.0178 0.0752  -0.0055 59  SER A CB  
515  O OG  A SER A 58  ? 0.5606 0.3607 0.4564 -0.0013 0.0687  -0.0001 59  SER A OG  
516  O OG  B SER A 58  ? 0.6085 0.3796 0.4838 -0.0204 0.0837  -0.0052 59  SER A OG  
517  N N   . ILE A 59  ? 0.4707 0.2988 0.3570 -0.0462 0.0774  -0.0156 60  ILE A N   
518  C CA  . ILE A 59  ? 0.4615 0.2944 0.3457 -0.0606 0.0821  -0.0238 60  ILE A CA  
519  C C   . ILE A 59  ? 0.5063 0.3457 0.3869 -0.0669 0.0816  -0.0230 60  ILE A C   
520  O O   . ILE A 59  ? 0.5261 0.3533 0.3969 -0.0776 0.0899  -0.0262 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4682 0.3228 0.3633 -0.0639 0.0779  -0.0318 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4722 0.3182 0.3677 -0.0618 0.0816  -0.0350 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.4493 0.3153 0.3456 -0.0768 0.0794  -0.0411 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4720 0.3365 0.3735 -0.0636 0.0761  -0.0407 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.4283 0.2861 0.3162 -0.0614 0.0732  -0.0198 61  PHE A N   
526  C CA  . PHE A 60  ? 0.4390 0.3059 0.3255 -0.0683 0.0734  -0.0214 61  PHE A CA  
527  C C   . PHE A 60  ? 0.5112 0.3587 0.3814 -0.0674 0.0766  -0.0130 61  PHE A C   
528  O O   . PHE A 60  ? 0.5200 0.3719 0.3860 -0.0756 0.0795  -0.0152 61  PHE A O   
529  C CB  . PHE A 60  ? 0.4263 0.3206 0.3270 -0.0649 0.0641  -0.0237 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.4236 0.3330 0.3351 -0.0669 0.0605  -0.0318 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.4569 0.3712 0.3704 -0.0775 0.0646  -0.0419 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.4254 0.3431 0.3432 -0.0587 0.0532  -0.0299 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.4601 0.3877 0.3812 -0.0783 0.0593  -0.0490 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.4539 0.3816 0.3765 -0.0606 0.0492  -0.0363 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.4326 0.3649 0.3562 -0.0696 0.0514  -0.0454 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4857 0.3106 0.3455 -0.0583 0.0767  -0.0045 62  THR A N   
537  C CA  . THR A 61  ? 0.5131 0.3133 0.3515 -0.0576 0.0795  0.0041  62  THR A CA  
538  C C   . THR A 61  ? 0.6198 0.3898 0.4409 -0.0672 0.0916  0.0027  62  THR A C   
539  O O   . THR A 61  ? 0.6359 0.3784 0.4337 -0.0698 0.0965  0.0093  62  THR A O   
540  C CB  . THR A 61  ? 0.5976 0.3900 0.4326 -0.0410 0.0706  0.0145  62  THR A CB  
541  O OG1 . THR A 61  ? 0.5512 0.3372 0.3941 -0.0321 0.0699  0.0141  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.5507 0.3705 0.3986 -0.0347 0.0601  0.0158  62  THR A CG2 
543  N N   . ASP A 62  ? 0.5779 0.3509 0.4078 -0.0736 0.0970  -0.0062 63  ASP A N   
544  C CA  . ASP A 62  ? 0.6087 0.3545 0.4235 -0.0849 0.1098  -0.0098 63  ASP A CA  
545  C C   . ASP A 62  ? 0.6665 0.4182 0.4762 -0.1031 0.1182  -0.0174 63  ASP A C   
546  O O   . ASP A 62  ? 0.6135 0.3975 0.4415 -0.1086 0.1152  -0.0266 63  ASP A O   
547  C CB  . ASP A 62  ? 0.6279 0.3773 0.4540 -0.0869 0.1129  -0.0184 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.8027 0.5264 0.6143 -0.1012 0.1271  -0.0243 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.8788 0.5677 0.6741 -0.0965 0.1323  -0.0182 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.8290 0.5669 0.6455 -0.1170 0.1330  -0.0356 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.7028 0.4225 0.4873 -0.1123 0.1290  -0.0141 64  GLN A N   
552  C CA  . GLN A 63  ? 0.7195 0.4419 0.4967 -0.1314 0.1396  -0.0220 64  GLN A CA  
553  C C   . GLN A 63  ? 0.7522 0.4990 0.5481 -0.1468 0.1461  -0.0396 64  GLN A C   
554  O O   . GLN A 63  ? 0.7686 0.5366 0.5723 -0.1590 0.1499  -0.0492 64  GLN A O   
555  C CB  . GLN A 63  ? 0.7914 0.4679 0.5332 -0.1397 0.1518  -0.0150 64  GLN A CB  
556  C CG  . GLN A 63  ? 1.0296 0.6880 0.7508 -0.1278 0.1445  0.0006  64  GLN A CG  
557  N N   . LEU A 64  ? 0.6581 0.4036 0.4620 -0.1463 0.1471  -0.0450 65  LEU A N   
558  C CA  . LEU A 64  ? 0.6298 0.4011 0.4518 -0.1595 0.1506  -0.0620 65  LEU A CA  
559  C C   . LEU A 64  ? 0.6608 0.4714 0.5094 -0.1494 0.1357  -0.0662 65  LEU A C   
560  O O   . LEU A 64  ? 0.6648 0.5065 0.5307 -0.1570 0.1335  -0.0786 65  LEU A O   
561  C CB  . LEU A 64  ? 0.6511 0.4004 0.4658 -0.1663 0.1598  -0.0673 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.7545 0.4697 0.5461 -0.1839 0.1779  -0.0707 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.7784 0.4720 0.5643 -0.1883 0.1858  -0.0757 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.8193 0.5568 0.6187 -0.2049 0.1868  -0.0863 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.5847 0.3929 0.4361 -0.1329 0.1260  -0.0570 66  LYS A N   
566  C CA  . LYS A 65  ? 0.5442 0.3831 0.4157 -0.1242 0.1131  -0.0602 66  LYS A CA  
567  C C   . LYS A 65  ? 0.5853 0.4496 0.4682 -0.1182 0.1033  -0.0582 66  LYS A C   
568  O O   . LYS A 65  ? 0.5482 0.4396 0.4473 -0.1160 0.0944  -0.0647 66  LYS A O   
569  C CB  . LYS A 65  ? 0.5548 0.3830 0.4254 -0.1106 0.1081  -0.0526 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.5344 0.3422 0.3976 -0.1159 0.1170  -0.0573 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.5058 0.3084 0.3717 -0.1025 0.1121  -0.0519 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.6097 0.3862 0.4664 -0.1057 0.1222  -0.0551 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.6364 0.3779 0.4769 -0.1019 0.1296  -0.0464 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.5820 0.4358 0.4548 -0.1159 0.1048  -0.0497 67  CYS A N   
575  C CA  . CYS A 66  ? 0.5823 0.4578 0.4642 -0.1112 0.0969  -0.0482 67  CYS A CA  
576  C C   . CYS A 66  ? 0.6270 0.5323 0.5259 -0.1210 0.0968  -0.0627 67  CYS A C   
577  O O   . CYS A 66  ? 0.6131 0.5417 0.5256 -0.1148 0.0876  -0.0642 67  CYS A O   
578  C CB  . CYS A 66  ? 0.6210 0.4777 0.4853 -0.1104 0.1006  -0.0383 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.7168 0.5549 0.5628 -0.1307 0.1178  -0.0442 67  CYS A SG  
580  N N   . ASN A 67  ? 0.5775 0.4820 0.4762 -0.1361 0.1070  -0.0744 68  ASN A N   
581  C CA  . ASN A 67  ? 0.5667 0.5007 0.4834 -0.1469 0.1081  -0.0911 68  ASN A CA  
582  C C   . ASN A 67  ? 0.5773 0.5339 0.5113 -0.1454 0.0996  -0.1017 68  ASN A C   
583  O O   . ASN A 67  ? 0.5519 0.5364 0.5038 -0.1521 0.0980  -0.1167 68  ASN A O   
584  C CB  . ASN A 67  ? 0.5966 0.5186 0.5033 -0.1664 0.1253  -0.0996 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.8159 0.7195 0.7047 -0.1692 0.1327  -0.0910 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.8128 0.6845 0.6779 -0.1790 0.1457  -0.0868 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.6577 0.5780 0.5545 -0.1604 0.1244  -0.0875 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.5386 0.4840 0.4674 -0.1369 0.0942  -0.0949 69  LEU A N   
589  C CA  . LEU A 68  ? 0.5178 0.4813 0.4579 -0.1358 0.0857  -0.1040 69  LEU A CA  
590  C C   . LEU A 68  ? 0.5399 0.5270 0.4934 -0.1229 0.0697  -0.1031 69  LEU A C   
591  O O   . LEU A 68  ? 0.5258 0.5069 0.4757 -0.1118 0.0647  -0.0912 69  LEU A O   
592  C CB  . LEU A 68  ? 0.5294 0.4708 0.4569 -0.1328 0.0872  -0.0982 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.6094 0.5236 0.5224 -0.1446 0.1028  -0.0997 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.6215 0.5150 0.5243 -0.1387 0.1034  -0.0936 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.6289 0.5565 0.5491 -0.1621 0.1100  -0.1176 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4882 0.5013 0.4566 -0.1242 0.0611  -0.1160 70  SER A N   
597  N N   B SER A 69  ? 0.4884 0.5014 0.4568 -0.1244 0.0612  -0.1161 70  SER A N   
598  C CA  A SER A 69  ? 0.4656 0.4980 0.4446 -0.1113 0.0448  -0.1157 70  SER A CA  
599  C CA  B SER A 69  ? 0.4664 0.4998 0.4460 -0.1119 0.0448  -0.1166 70  SER A CA  
600  C C   A SER A 69  ? 0.4792 0.5049 0.4494 -0.1042 0.0354  -0.1116 70  SER A C   
601  C C   B SER A 69  ? 0.4798 0.5061 0.4504 -0.1045 0.0353  -0.1121 70  SER A C   
602  O O   A SER A 69  ? 0.4505 0.4830 0.4223 -0.0929 0.0224  -0.1080 70  SER A O   
603  O O   B SER A 69  ? 0.4511 0.4845 0.4235 -0.0931 0.0222  -0.1086 70  SER A O   
604  C CB  A SER A 69  ? 0.5081 0.5729 0.5086 -0.1145 0.0391  -0.1324 70  SER A CB  
605  C CB  B SER A 69  ? 0.5089 0.5746 0.5099 -0.1160 0.0395  -0.1341 70  SER A CB  
606  O OG  A SER A 69  ? 0.5954 0.6708 0.6008 -0.1240 0.0395  -0.1460 70  SER A OG  
607  O OG  B SER A 69  ? 0.5924 0.6668 0.6026 -0.1221 0.0480  -0.1387 70  SER A OG  
608  N N   . VAL A 70  ? 0.4448 0.4553 0.4040 -0.1117 0.0427  -0.1127 71  VAL A N   
609  C CA  . VAL A 70  ? 0.4482 0.4499 0.3962 -0.1077 0.0367  -0.1099 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4837 0.4566 0.4167 -0.1095 0.0487  -0.1009 71  VAL A C   
611  O O   . VAL A 70  ? 0.4887 0.4498 0.4186 -0.1193 0.0615  -0.1039 71  VAL A O   
612  C CB  . VAL A 70  ? 0.5138 0.5308 0.4654 -0.1152 0.0318  -0.1248 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.5241 0.5289 0.4597 -0.1126 0.0269  -0.1217 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.5087 0.5565 0.4777 -0.1112 0.0180  -0.1352 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.4030 0.3641 0.3268 -0.1003 0.0448  -0.0909 72  ILE A N   
616  C CA  . ILE A 71  ? 0.4022 0.3391 0.3147 -0.0998 0.0544  -0.0839 72  ILE A CA  
617  C C   . ILE A 71  ? 0.4435 0.3766 0.3462 -0.0994 0.0505  -0.0860 72  ILE A C   
618  O O   . ILE A 71  ? 0.4388 0.3782 0.3388 -0.0926 0.0401  -0.0829 72  ILE A O   
619  C CB  . ILE A 71  ? 0.4347 0.3615 0.3467 -0.0899 0.0559  -0.0710 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.4552 0.3834 0.3726 -0.0912 0.0600  -0.0687 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.4581 0.3633 0.3617 -0.0871 0.0641  -0.0655 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.5415 0.4538 0.4533 -0.1012 0.0733  -0.0716 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.4312 0.3512 0.3264 -0.1073 0.0598  -0.0913 73  ASN A N   
624  C CA  . ASN A 72  ? 0.4427 0.3570 0.3263 -0.1090 0.0584  -0.0942 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4874 0.3821 0.3649 -0.1041 0.0669  -0.0869 73  ASN A C   
626  O O   . ASN A 72  ? 0.4685 0.3479 0.3468 -0.1056 0.0783  -0.0860 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4873 0.4015 0.3671 -0.1217 0.0634  -0.1070 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.7291 0.6661 0.6183 -0.1275 0.0558  -0.1173 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.5781 0.5326 0.4695 -0.1226 0.0413  -0.1189 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.6907 0.6276 0.5858 -0.1381 0.0655  -0.1254 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.4256 0.3198 0.2966 -0.0984 0.0617  -0.0824 74  LEU A N   
632  C CA  . LEU A 73  ? 0.4303 0.3100 0.2984 -0.0944 0.0701  -0.0779 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4776 0.3455 0.3349 -0.1023 0.0785  -0.0859 74  LEU A C   
634  O O   . LEU A 73  ? 0.4888 0.3610 0.3374 -0.1105 0.0749  -0.0938 74  LEU A O   
635  C CB  . LEU A 73  ? 0.4270 0.3101 0.2924 -0.0872 0.0638  -0.0711 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.4581 0.3523 0.3334 -0.0791 0.0556  -0.0634 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.4700 0.3630 0.3426 -0.0734 0.0538  -0.0575 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.4513 0.3445 0.3390 -0.0758 0.0605  -0.0598 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.4474 0.3018 0.3057 -0.0994 0.0889  -0.0847 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4830 0.3245 0.3327 -0.1060 0.0994  -0.0928 75  ASP A CA  
641  C C   . ASP A 74  ? 0.5474 0.3930 0.3800 -0.1124 0.0937  -0.0971 75  ASP A C   
642  O O   . ASP A 74  ? 0.5334 0.3848 0.3621 -0.1081 0.0862  -0.0914 75  ASP A O   
643  C CB  . ASP A 74  ? 0.5049 0.3360 0.3623 -0.0985 0.1092  -0.0903 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.6579 0.4745 0.5101 -0.1039 0.1223  -0.0996 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.6713 0.4879 0.5104 -0.1113 0.1237  -0.1056 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.7019 0.5053 0.5617 -0.1006 0.1312  -0.1008 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.5598 0.4009 0.3800 -0.1231 0.0967  -0.1069 76  PRO A N   
648  C CA  . PRO A 75  ? 0.5695 0.4125 0.3690 -0.1291 0.0897  -0.1104 76  PRO A CA  
649  C C   . PRO A 75  ? 0.6183 0.4524 0.4067 -0.1284 0.0949  -0.1082 76  PRO A C   
650  O O   . PRO A 75  ? 0.6407 0.4739 0.4089 -0.1319 0.0875  -0.1080 76  PRO A O   
651  C CB  . PRO A 75  ? 0.6097 0.4482 0.3992 -0.1412 0.0945  -0.1226 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.6843 0.5124 0.4877 -0.1417 0.1088  -0.1257 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.6020 0.4346 0.4239 -0.1308 0.1064  -0.1157 76  PRO A CD  
654  N N   . GLU A 76  ? 0.5774 0.4045 0.3782 -0.1239 0.1074  -0.1073 77  GLU A N   
655  C CA  . GLU A 76  ? 0.6027 0.4243 0.3971 -0.1242 0.1146  -0.1075 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5927 0.4220 0.3885 -0.1172 0.1052  -0.0975 77  GLU A C   
657  O O   . GLU A 76  ? 0.5870 0.4121 0.3726 -0.1197 0.1091  -0.0973 77  GLU A O   
658  C CB  . GLU A 76  ? 0.6362 0.4521 0.4490 -0.1197 0.1297  -0.1112 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.9023 0.7113 0.7076 -0.1253 0.1425  -0.1188 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.2942 1.0916 1.0840 -0.1371 0.1521  -0.1306 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.2958 1.0869 1.0963 -0.1362 0.1597  -0.1361 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.2556 1.0483 1.0204 -0.1476 0.1523  -0.1344 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.5197 0.3594 0.3277 -0.1095 0.0944  -0.0901 78  ILE A N   
664  C CA  . ILE A 77  ? 0.5115 0.3581 0.3221 -0.1027 0.0859  -0.0812 78  ILE A CA  
665  C C   . ILE A 77  ? 0.5759 0.4196 0.3623 -0.1067 0.0748  -0.0792 78  ILE A C   
666  O O   . ILE A 77  ? 0.5657 0.4119 0.3425 -0.1093 0.0650  -0.0812 78  ILE A O   
667  C CB  . ILE A 77  ? 0.5222 0.3800 0.3535 -0.0934 0.0794  -0.0747 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.5258 0.3816 0.3767 -0.0880 0.0898  -0.0752 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4803 0.3451 0.3134 -0.0871 0.0706  -0.0665 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.6050 0.4588 0.4644 -0.0845 0.1000  -0.0764 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.5758 0.4138 0.3522 -0.1072 0.0764  -0.0757 79  ASN A N   
672  C CA  . ASN A 78  ? 0.5926 0.4213 0.3414 -0.1104 0.0671  -0.0723 79  ASN A CA  
673  C C   . ASN A 78  ? 0.5799 0.4167 0.3344 -0.1012 0.0518  -0.0641 79  ASN A C   
674  O O   . ASN A 78  ? 0.5504 0.3943 0.3229 -0.0949 0.0535  -0.0595 79  ASN A O   
675  C CB  . ASN A 78  ? 0.6523 0.4691 0.3882 -0.1163 0.0783  -0.0726 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.8365 0.6377 0.5395 -0.1201 0.0701  -0.0677 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.7315 0.5307 0.4341 -0.1163 0.0668  -0.0612 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.7466 0.5346 0.4196 -0.1276 0.0662  -0.0706 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.5512 0.3877 0.2909 -0.0999 0.0365  -0.0631 80  PRO A N   
680  C CA  . PRO A 79  ? 0.5373 0.3822 0.2845 -0.0901 0.0222  -0.0568 80  PRO A CA  
681  C C   . PRO A 79  ? 0.5873 0.4222 0.3264 -0.0872 0.0219  -0.0493 80  PRO A C   
682  O O   . PRO A 79  ? 0.5650 0.4096 0.3216 -0.0793 0.0175  -0.0449 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5884 0.4324 0.3174 -0.0897 0.0062  -0.0591 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.6502 0.4935 0.3730 -0.0989 0.0125  -0.0678 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.6029 0.4335 0.3204 -0.1064 0.0307  -0.0688 80  PRO A CD  
686  N N   . GLU A 80  ? 0.5632 0.3779 0.2748 -0.0947 0.0276  -0.0484 81  GLU A N   
687  C CA  . GLU A 80  ? 0.5712 0.3743 0.2734 -0.0941 0.0294  -0.0422 81  GLU A CA  
688  C C   . GLU A 80  ? 0.5740 0.3901 0.3055 -0.0926 0.0418  -0.0428 81  GLU A C   
689  O O   . GLU A 80  ? 0.5398 0.3600 0.2810 -0.0868 0.0381  -0.0379 81  GLU A O   
690  C CB  . GLU A 80  ? 0.6296 0.4061 0.2933 -0.1048 0.0350  -0.0420 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.7758 0.5365 0.4253 -0.1048 0.0350  -0.0354 81  GLU A CG  
692  C CD  . GLU A 80  ? 1.1273 0.8598 0.7395 -0.1178 0.0453  -0.0354 81  GLU A CD  
693  O OE1 . GLU A 80  ? 1.1456 0.8567 0.7331 -0.1177 0.0400  -0.0286 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 1.0290 0.7591 0.6358 -0.1286 0.0595  -0.0425 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.5485 0.3712 0.2940 -0.0971 0.0555  -0.0492 82  GLY A N   
696  C CA  . GLY A 81  ? 0.5233 0.3600 0.2979 -0.0939 0.0656  -0.0507 82  GLY A CA  
697  C C   . GLY A 81  ? 0.5180 0.3714 0.3174 -0.0831 0.0567  -0.0463 82  GLY A C   
698  O O   . GLY A 81  ? 0.4772 0.3386 0.2915 -0.0785 0.0573  -0.0434 82  GLY A O   
699  N N   . PHE A 82  ? 0.4656 0.3243 0.2680 -0.0799 0.0484  -0.0467 83  PHE A N   
700  C CA  . PHE A 82  ? 0.4366 0.3103 0.2599 -0.0715 0.0408  -0.0435 83  PHE A CA  
701  C C   . PHE A 82  ? 0.4579 0.3319 0.2772 -0.0664 0.0301  -0.0379 83  PHE A C   
702  O O   . PHE A 82  ? 0.4407 0.3247 0.2770 -0.0609 0.0293  -0.0348 83  PHE A O   
703  C CB  . PHE A 82  ? 0.4489 0.3287 0.2757 -0.0716 0.0356  -0.0471 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.4371 0.3313 0.2850 -0.0650 0.0311  -0.0450 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.4721 0.3713 0.3377 -0.0626 0.0392  -0.0443 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.4495 0.3514 0.2985 -0.0605 0.0187  -0.0435 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.4682 0.3779 0.3489 -0.0577 0.0357  -0.0418 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.4608 0.3759 0.3284 -0.0558 0.0163  -0.0424 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.4363 0.3545 0.3181 -0.0552 0.0252  -0.0412 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.4735 0.3352 0.2691 -0.0678 0.0214  -0.0365 84  CYS A N   
711  C CA  . CYS A 83  ? 0.5051 0.3627 0.2939 -0.0621 0.0107  -0.0313 84  CYS A CA  
712  C C   . CYS A 83  ? 0.5092 0.3630 0.3014 -0.0629 0.0183  -0.0281 84  CYS A C   
713  O O   . CYS A 83  ? 0.4767 0.3381 0.2814 -0.0568 0.0137  -0.0251 84  CYS A O   
714  C CB  . CYS A 83  ? 0.5716 0.4107 0.3290 -0.0634 0.0008  -0.0301 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.6511 0.4817 0.3990 -0.0538 -0.0147 -0.0240 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4752 0.3189 0.2574 -0.0713 0.0307  -0.0300 85  ILE A N   
717  C CA  . ILE A 84  ? 0.4576 0.2999 0.2440 -0.0744 0.0396  -0.0295 85  ILE A CA  
718  C C   . ILE A 84  ? 0.4480 0.3129 0.2674 -0.0683 0.0422  -0.0303 85  ILE A C   
719  O O   . ILE A 84  ? 0.4232 0.2928 0.2509 -0.0657 0.0411  -0.0282 85  ILE A O   
720  C CB  . ILE A 84  ? 0.5011 0.3317 0.2733 -0.0859 0.0541  -0.0344 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.5305 0.3324 0.2619 -0.0932 0.0513  -0.0319 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4866 0.3261 0.2754 -0.0894 0.0663  -0.0380 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.6047 0.3949 0.3186 -0.1052 0.0643  -0.0377 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3981 0.2749 0.2340 -0.0659 0.0450  -0.0331 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3839 0.2787 0.2471 -0.0595 0.0466  -0.0330 86  LEU A CA  
726  C C   . LEU A 85  ? 0.4119 0.3154 0.2837 -0.0523 0.0358  -0.0288 86  LEU A C   
727  O O   . LEU A 85  ? 0.3801 0.2943 0.2666 -0.0481 0.0353  -0.0271 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3926 0.2922 0.2674 -0.0590 0.0535  -0.0369 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.4705 0.3671 0.3457 -0.0646 0.0663  -0.0430 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.4784 0.3761 0.3625 -0.0634 0.0723  -0.0472 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.4912 0.3994 0.3830 -0.0626 0.0709  -0.0446 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3940 0.2942 0.2569 -0.0512 0.0272  -0.0281 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3763 0.2861 0.2481 -0.0451 0.0176  -0.0262 87  LEU A CA  
734  C C   . LEU A 86  ? 0.4151 0.3215 0.2831 -0.0427 0.0135  -0.0231 87  LEU A C   
735  O O   . LEU A 86  ? 0.3908 0.3079 0.2726 -0.0385 0.0115  -0.0218 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3852 0.2942 0.2495 -0.0446 0.0091  -0.0285 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.4379 0.3601 0.3149 -0.0388 0.0003  -0.0292 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.4218 0.3570 0.3181 -0.0383 0.0060  -0.0296 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.4607 0.3850 0.3319 -0.0381 -0.0094 -0.0336 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.4037 0.2930 0.2507 -0.0464 0.0132  -0.0220 88  ASP A N   
741  C CA  . ASP A 87  ? 0.4029 0.2839 0.2429 -0.0457 0.0113  -0.0193 88  ASP A CA  
742  C C   . ASP A 87  ? 0.4168 0.3084 0.2730 -0.0475 0.0199  -0.0202 88  ASP A C   
743  O O   . ASP A 87  ? 0.4066 0.3035 0.2705 -0.0442 0.0169  -0.0191 88  ASP A O   
744  C CB  . ASP A 87  ? 0.4621 0.3180 0.2723 -0.0517 0.0124  -0.0179 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.6583 0.5010 0.4487 -0.0474 -0.0006 -0.0159 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.6691 0.5243 0.4723 -0.0391 -0.0110 -0.0165 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.6901 0.5102 0.4519 -0.0524 -0.0005 -0.0144 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3933 0.2891 0.2555 -0.0523 0.0303  -0.0233 89  PHE A N   
749  C CA  . PHE A 88  ? 0.3594 0.2691 0.2400 -0.0527 0.0374  -0.0257 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3621 0.2897 0.2632 -0.0449 0.0320  -0.0240 89  PHE A C   
751  O O   . PHE A 88  ? 0.3319 0.2687 0.2429 -0.0434 0.0316  -0.0242 89  PHE A O   
752  C CB  . PHE A 88  ? 0.3593 0.2726 0.2460 -0.0569 0.0481  -0.0307 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.3480 0.2801 0.2583 -0.0542 0.0525  -0.0340 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3806 0.3170 0.2944 -0.0586 0.0568  -0.0373 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3700 0.3152 0.2981 -0.0466 0.0509  -0.0337 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.3601 0.3171 0.2971 -0.0553 0.0588  -0.0414 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3898 0.3521 0.3383 -0.0421 0.0521  -0.0362 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3631 0.3331 0.3171 -0.0462 0.0554  -0.0405 89  PHE A CZ  
759  N N   . MET A 89  ? 0.3262 0.2578 0.2319 -0.0410 0.0286  -0.0229 90  MET A N   
760  C CA  . MET A 89  ? 0.3063 0.2513 0.2269 -0.0351 0.0248  -0.0212 90  MET A CA  
761  C C   . MET A 89  ? 0.3541 0.3024 0.2754 -0.0328 0.0183  -0.0197 90  MET A C   
762  O O   . MET A 89  ? 0.3378 0.2970 0.2700 -0.0303 0.0177  -0.0192 90  MET A O   
763  C CB  . MET A 89  ? 0.3177 0.2623 0.2382 -0.0338 0.0227  -0.0210 90  MET A CB  
764  C CG  . MET A 89  ? 0.3432 0.2843 0.2648 -0.0354 0.0297  -0.0228 90  MET A CG  
765  S SD  . MET A 89  ? 0.3926 0.3330 0.3144 -0.0354 0.0280  -0.0234 90  MET A SD  
766  C CE  . MET A 89  ? 0.3926 0.3235 0.3112 -0.0385 0.0371  -0.0267 90  MET A CE  
767  N N   . TYR A 90  ? 0.3184 0.2568 0.2274 -0.0330 0.0128  -0.0195 91  TYR A N   
768  C CA  . TYR A 90  ? 0.3249 0.2648 0.2348 -0.0297 0.0061  -0.0191 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3726 0.3041 0.2756 -0.0320 0.0077  -0.0189 91  TYR A C   
770  O O   . TYR A 90  ? 0.3668 0.2983 0.2709 -0.0291 0.0030  -0.0192 91  TYR A O   
771  C CB  . TYR A 90  ? 0.3438 0.2778 0.2458 -0.0266 -0.0023 -0.0199 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.3474 0.2948 0.2611 -0.0244 -0.0046 -0.0223 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3651 0.3127 0.2780 -0.0272 -0.0017 -0.0233 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.3510 0.3100 0.2761 -0.0209 -0.0087 -0.0246 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.3609 0.3192 0.2833 -0.0273 -0.0023 -0.0264 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.3521 0.3229 0.2869 -0.0210 -0.0093 -0.0282 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.3864 0.3564 0.3195 -0.0246 -0.0058 -0.0290 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.3620 0.3422 0.3036 -0.0266 -0.0052 -0.0335 91  TYR A OH  
779  N N   . THR A 91  ? 0.3451 0.2689 0.2409 -0.0381 0.0151  -0.0196 92  THR A N   
780  C CA  . THR A 91  ? 0.3653 0.2786 0.2523 -0.0426 0.0182  -0.0203 92  THR A CA  
781  C C   . THR A 91  ? 0.3912 0.3131 0.2870 -0.0490 0.0281  -0.0242 92  THR A C   
782  O O   . THR A 91  ? 0.3908 0.3077 0.2828 -0.0538 0.0313  -0.0263 92  THR A O   
783  C CB  . THR A 91  ? 0.4385 0.3250 0.2985 -0.0466 0.0179  -0.0185 92  THR A CB  
784  O OG1 . THR A 91  ? 0.4368 0.3191 0.2900 -0.0529 0.0255  -0.0200 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.4689 0.3457 0.3184 -0.0393 0.0061  -0.0157 92  THR A CG2 
786  N N   A SER A 92  ? 0.3300 0.2641 0.2376 -0.0492 0.0330  -0.0263 93  SER A N   
787  N N   B SER A 92  ? 0.3356 0.2693 0.2428 -0.0494 0.0331  -0.0263 93  SER A N   
788  C CA  A SER A 92  ? 0.3196 0.2651 0.2389 -0.0541 0.0420  -0.0320 93  SER A CA  
789  C CA  B SER A 92  ? 0.3279 0.2731 0.2470 -0.0542 0.0421  -0.0320 93  SER A CA  
790  C C   A SER A 92  ? 0.3623 0.2914 0.2652 -0.0644 0.0515  -0.0354 93  SER A C   
791  C C   B SER A 92  ? 0.3861 0.3149 0.2887 -0.0649 0.0517  -0.0356 93  SER A C   
792  O O   A SER A 92  ? 0.3444 0.2830 0.2572 -0.0697 0.0607  -0.0421 93  SER A O   
793  O O   B SER A 92  ? 0.3775 0.3152 0.2891 -0.0712 0.0607  -0.0424 93  SER A O   
794  C CB  A SER A 92  ? 0.3202 0.2792 0.2519 -0.0549 0.0420  -0.0352 93  SER A CB  
795  C CB  B SER A 92  ? 0.3443 0.3052 0.2778 -0.0538 0.0413  -0.0349 93  SER A CB  
796  O OG  A SER A 92  ? 0.3296 0.3001 0.2712 -0.0471 0.0336  -0.0320 93  SER A OG  
797  O OG  B SER A 92  ? 0.4045 0.3538 0.3267 -0.0616 0.0451  -0.0373 93  SER A OG  
798  N N   A ARG A 93  ? 0.3539 0.2584 0.2311 -0.0672 0.0493  -0.0314 94  ARG A N   
799  N N   B ARG A 93  ? 0.3688 0.2739 0.2466 -0.0671 0.0496  -0.0316 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3782 0.2622 0.2333 -0.0781 0.0585  -0.0337 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3932 0.2763 0.2474 -0.0780 0.0581  -0.0334 94  ARG A CA  
802  C C   A ARG A 93  ? 0.4413 0.3192 0.2878 -0.0790 0.0605  -0.0337 94  ARG A C   
803  C C   B ARG A 93  ? 0.4487 0.3253 0.2937 -0.0792 0.0604  -0.0335 94  ARG A C   
804  O O   A ARG A 93  ? 0.4358 0.3095 0.2765 -0.0724 0.0513  -0.0289 94  ARG A O   
805  O O   B ARG A 93  ? 0.4430 0.3146 0.2813 -0.0729 0.0513  -0.0287 94  ARG A O   
806  C CB  A ARG A 93  ? 0.4368 0.2923 0.2633 -0.0812 0.0548  -0.0292 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.4335 0.2895 0.2606 -0.0794 0.0527  -0.0283 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4953 0.3526 0.3272 -0.0825 0.0551  -0.0305 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.5191 0.3785 0.3534 -0.0785 0.0509  -0.0288 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.5990 0.4293 0.4067 -0.0792 0.0466  -0.0243 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5931 0.4403 0.4164 -0.0918 0.0631  -0.0338 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.7506 0.5472 0.5230 -0.0874 0.0508  -0.0219 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.6227 0.4737 0.4534 -0.0920 0.0620  -0.0355 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.9359 0.7110 0.6889 -0.0994 0.0609  -0.0241 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.8119 0.6356 0.6199 -0.0950 0.0611  -0.0328 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.7847 0.5712 0.5529 -0.1045 0.0675  -0.0296 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.7050 0.5338 0.5219 -0.0957 0.0612  -0.0357 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.7924 0.5336 0.5089 -0.1072 0.0647  -0.0210 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.6267 0.4162 0.4012 -0.0972 0.0600  -0.0274 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.4119 0.2902 0.2581 -0.0881 0.0731  -0.0403 95  LEU A N   
821  C CA  . LEU A 94  ? 0.4122 0.2850 0.2506 -0.0907 0.0777  -0.0423 95  LEU A CA  
822  C C   . LEU A 94  ? 0.5052 0.3503 0.3101 -0.1036 0.0858  -0.0434 95  LEU A C   
823  O O   . LEU A 94  ? 0.5042 0.3461 0.3057 -0.1148 0.0982  -0.0496 95  LEU A O   
824  C CB  . LEU A 94  ? 0.4011 0.2977 0.2681 -0.0899 0.0865  -0.0505 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.4484 0.3419 0.3125 -0.0911 0.0916  -0.0537 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.4371 0.3309 0.3022 -0.0809 0.0798  -0.0470 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.4622 0.3763 0.3533 -0.0910 0.1022  -0.0638 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4997 0.3246 0.2785 -0.1029 0.0790  -0.0380 96  ASN A N   
829  C CA  . ASN A 95  ? 0.5448 0.3386 0.2847 -0.1147 0.0848  -0.0374 96  ASN A CA  
830  C C   . ASN A 95  ? 0.6070 0.4032 0.3461 -0.1236 0.0981  -0.0455 96  ASN A C   
831  O O   . ASN A 95  ? 0.6150 0.4026 0.3396 -0.1232 0.0946  -0.0442 96  ASN A O   
832  C CB  . ASN A 95  ? 0.6065 0.3778 0.3177 -0.1086 0.0692  -0.0283 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.8717 0.6066 0.5371 -0.1196 0.0727  -0.0261 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.7416 0.4619 0.3914 -0.1331 0.0869  -0.0297 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.8168 0.5362 0.4584 -0.1148 0.0601  -0.0208 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.5681 0.3781 0.3251 -0.1315 0.1133  -0.0551 97  LEU A N   
837  C CA  . LEU A 96  ? 0.5808 0.3975 0.3438 -0.1394 0.1278  -0.0653 97  LEU A CA  
838  C C   . LEU A 96  ? 0.6521 0.4412 0.3785 -0.1576 0.1416  -0.0692 97  LEU A C   
839  O O   . LEU A 96  ? 0.6540 0.4338 0.3708 -0.1674 0.1495  -0.0712 97  LEU A O   
840  C CB  . LEU A 96  ? 0.5670 0.4171 0.3731 -0.1361 0.1355  -0.0750 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.6312 0.4985 0.4592 -0.1364 0.1462  -0.0859 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.6323 0.5008 0.4640 -0.1252 0.1365  -0.0808 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.6028 0.5027 0.4726 -0.1312 0.1508  -0.0949 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.6274 0.4000 0.3291 -0.1630 0.1441  -0.0697 98  ARG A N   
845  C CA  . ARG A 97  ? 0.6773 0.4191 0.3369 -0.1812 0.1568  -0.0725 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6950 0.4429 0.3579 -0.1893 0.1710  -0.0838 98  ARG A C   
847  O O   . ARG A 97  ? 0.6613 0.4287 0.3488 -0.1790 0.1662  -0.0858 98  ARG A O   
848  C CB  . ARG A 97  ? 0.7201 0.4260 0.3326 -0.1801 0.1423  -0.0596 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.8104 0.5067 0.4173 -0.1710 0.1276  -0.0487 98  ARG A CG  
850  C CD  . ARG A 97  ? 1.0601 0.7238 0.6246 -0.1661 0.1105  -0.0367 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.3376 0.9608 0.8494 -0.1822 0.1191  -0.0356 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.6308 1.2235 1.1121 -0.1920 0.1251  -0.0322 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.5100 1.0630 0.9394 -0.2075 0.1336  -0.0309 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.5085 1.1084 1.0089 -0.1873 0.1235  -0.0304 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.6901 0.4202 0.3274 -0.2087 0.1897  -0.0920 99  GLU A N   
856  C CA  . GLU A 98  ? 0.6940 0.4280 0.3317 -0.2183 0.2053  -0.1044 99  GLU A CA  
857  C C   . GLU A 98  ? 0.7673 0.4926 0.3894 -0.2112 0.1932  -0.0987 99  GLU A C   
858  O O   . GLU A 98  ? 0.7525 0.4964 0.3989 -0.2076 0.1981  -0.1071 99  GLU A O   
859  C CB  . GLU A 98  ? 0.7587 0.4658 0.3580 -0.2425 0.2261  -0.1121 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.8897 0.6028 0.4916 -0.2543 0.2452  -0.1275 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.3294 1.0134 0.8884 -0.2802 0.2668  -0.1355 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.3168 0.9602 0.8215 -0.2886 0.2617  -0.1240 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.3403 1.0412 0.9192 -0.2922 0.2892  -0.1537 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.7565 0.4549 0.3408 -0.2082 0.1767  -0.0852 100 GLY A N   
865  C CA  . GLY A 99  ? 0.7683 0.4582 0.3349 -0.2024 0.1635  -0.0802 100 GLY A CA  
866  C C   . GLY A 99  ? 0.7610 0.4785 0.3657 -0.1836 0.1485  -0.0772 100 GLY A C   
867  O O   . GLY A 99  ? 0.7726 0.4898 0.3714 -0.1806 0.1417  -0.0773 100 GLY A O   
868  N N   . ASN A 100 ? 0.6709 0.4116 0.3133 -0.1719 0.1438  -0.0750 101 ASN A N   
869  C CA  . ASN A 100 ? 0.6192 0.3827 0.2939 -0.1552 0.1302  -0.0715 101 ASN A CA  
870  C C   . ASN A 100 ? 0.6426 0.4368 0.3651 -0.1484 0.1385  -0.0792 101 ASN A C   
871  O O   . ASN A 100 ? 0.6038 0.4139 0.3505 -0.1360 0.1295  -0.0769 101 ASN A O   
872  C CB  . ASN A 100 ? 0.6097 0.3704 0.2812 -0.1440 0.1110  -0.0592 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.7028 0.4717 0.3914 -0.1417 0.1129  -0.0574 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5846 0.3733 0.3029 -0.1426 0.1244  -0.0649 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.6388 0.3937 0.3105 -0.1375 0.1006  -0.0480 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.6069 0.4092 0.3426 -0.1562 0.1549  -0.0886 102 ILE A N   
877  C CA  . ILE A 101 ? 0.5790 0.4116 0.3611 -0.1476 0.1603  -0.0959 102 ILE A CA  
878  C C   . ILE A 101 ? 0.5848 0.4292 0.3883 -0.1397 0.1614  -0.1010 102 ILE A C   
879  O O   . ILE A 101 ? 0.5327 0.3961 0.3678 -0.1258 0.1547  -0.0992 102 ILE A O   
880  C CB  . ILE A 101 ? 0.6264 0.4690 0.4215 -0.1578 0.1780  -0.1080 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5972 0.4737 0.4419 -0.1450 0.1780  -0.1140 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.6362 0.4672 0.4132 -0.1744 0.1972  -0.1203 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.6360 0.5275 0.4975 -0.1512 0.1877  -0.1225 102 ILE A CD1 
884  N N   . MET A 102 ? 0.5768 0.4080 0.3611 -0.1487 0.1697  -0.1070 103 MET A N   
885  C CA  . MET A 102 ? 0.5773 0.4163 0.3797 -0.1422 0.1719  -0.1125 103 MET A CA  
886  C C   . MET A 102 ? 0.6073 0.4468 0.4125 -0.1302 0.1546  -0.1021 103 MET A C   
887  O O   . MET A 102 ? 0.5633 0.4163 0.3971 -0.1187 0.1526  -0.1030 103 MET A O   
888  C CB  . MET A 102 ? 0.6458 0.4702 0.4258 -0.1560 0.1858  -0.1227 103 MET A CB  
889  C CG  . MET A 102 ? 0.7333 0.5605 0.5160 -0.1687 0.2063  -0.1363 103 MET A CG  
890  S SD  . MET A 102 ? 0.7810 0.6423 0.6199 -0.1576 0.2147  -0.1473 103 MET A SD  
891  C CE  . MET A 102 ? 0.7486 0.6155 0.6091 -0.1504 0.2218  -0.1579 103 MET A CE  
892  N N   . ALA A 103 ? 0.5951 0.4198 0.3710 -0.1324 0.1418  -0.0926 104 ALA A N   
893  C CA  . ALA A 103 ? 0.5816 0.4087 0.3602 -0.1226 0.1256  -0.0843 104 ALA A CA  
894  C C   . ALA A 103 ? 0.5725 0.4163 0.3787 -0.1097 0.1169  -0.0775 104 ALA A C   
895  O O   . ALA A 103 ? 0.5409 0.3939 0.3652 -0.1005 0.1109  -0.0752 104 ALA A O   
896  C CB  . ALA A 103 ? 0.6150 0.4249 0.3580 -0.1271 0.1134  -0.0773 104 ALA A CB  
897  N N   . VAL A 104 ? 0.5091 0.3556 0.3165 -0.1103 0.1168  -0.0747 105 VAL A N   
898  C CA  . VAL A 104 ? 0.4573 0.3198 0.2891 -0.0992 0.1090  -0.0691 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4641 0.3446 0.3298 -0.0910 0.1150  -0.0745 105 VAL A C   
900  O O   . VAL A 104 ? 0.4356 0.3250 0.3175 -0.0802 0.1064  -0.0694 105 VAL A O   
901  C CB  . VAL A 104 ? 0.5012 0.3615 0.3258 -0.1031 0.1089  -0.0665 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.4615 0.3410 0.3138 -0.0928 0.1030  -0.0632 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.5232 0.3632 0.3144 -0.1070 0.0989  -0.0587 105 VAL A CG2 
904  N N   A MET A 105 ? 0.4464 0.3313 0.3219 -0.0957 0.1294  -0.0852 106 MET A N   
905  N N   B MET A 105 ? 0.4551 0.3401 0.3307 -0.0956 0.1294  -0.0852 106 MET A N   
906  C CA  A MET A 105 ? 0.4419 0.3434 0.3502 -0.0859 0.1342  -0.0914 106 MET A CA  
907  C CA  B MET A 105 ? 0.4602 0.3618 0.3688 -0.0856 0.1338  -0.0911 106 MET A CA  
908  C C   A MET A 105 ? 0.4986 0.3952 0.4115 -0.0785 0.1309  -0.0898 106 MET A C   
909  C C   B MET A 105 ? 0.5062 0.4027 0.4190 -0.0784 0.1307  -0.0896 106 MET A C   
910  O O   A MET A 105 ? 0.4765 0.3819 0.4098 -0.0661 0.1251  -0.0863 106 MET A O   
911  O O   B MET A 105 ? 0.4770 0.3821 0.4101 -0.0660 0.1250  -0.0862 106 MET A O   
912  C CB  A MET A 105 ? 0.4830 0.3909 0.4017 -0.0928 0.1509  -0.1055 106 MET A CB  
913  C CB  B MET A 105 ? 0.5001 0.4088 0.4201 -0.0919 0.1503  -0.1052 106 MET A CB  
914  C CG  A MET A 105 ? 0.5168 0.4445 0.4726 -0.0801 0.1537  -0.1125 106 MET A CG  
915  C CG  B MET A 105 ? 0.5336 0.4617 0.4906 -0.0788 0.1526  -0.1118 106 MET A CG  
916  S SD  A MET A 105 ? 0.5828 0.5216 0.5556 -0.0873 0.1740  -0.1323 106 MET A SD  
917  S SD  B MET A 105 ? 0.5958 0.5396 0.5733 -0.0854 0.1713  -0.1308 106 MET A SD  
918  C CE  A MET A 105 ? 0.5318 0.4837 0.5410 -0.0674 0.1716  -0.1368 106 MET A CE  
919  C CE  B MET A 105 ? 0.5850 0.5103 0.5454 -0.0953 0.1857  -0.1403 106 MET A CE  
920  N N   . ALA A 106 ? 0.4805 0.3617 0.3723 -0.0869 0.1348  -0.0923 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4851 0.3592 0.3780 -0.0829 0.1334  -0.0922 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4878 0.3630 0.3812 -0.0755 0.1189  -0.0812 107 ALA A C   
923  O O   . ALA A 106 ? 0.4656 0.3417 0.3731 -0.0668 0.1171  -0.0795 107 ALA A O   
924  C CB  . ALA A 106 ? 0.5164 0.3749 0.3833 -0.0955 0.1392  -0.0976 107 ALA A CB  
925  N N   . THR A 107 ? 0.4399 0.3143 0.3179 -0.0786 0.1090  -0.0742 108 THR A N   
926  C CA  . THR A 107 ? 0.4273 0.3052 0.3071 -0.0725 0.0961  -0.0654 108 THR A CA  
927  C C   . THR A 107 ? 0.4542 0.3448 0.3573 -0.0613 0.0927  -0.0610 108 THR A C   
928  O O   . THR A 107 ? 0.4144 0.3059 0.3251 -0.0550 0.0879  -0.0569 108 THR A O   
929  C CB  . THR A 107 ? 0.5007 0.3745 0.3595 -0.0772 0.0860  -0.0604 108 THR A CB  
930  O OG1 . THR A 107 ? 0.5149 0.3759 0.3500 -0.0872 0.0890  -0.0649 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4902 0.3686 0.3516 -0.0722 0.0739  -0.0546 108 THR A CG2 
932  N N   . ALA A 108 ? 0.4085 0.3085 0.3214 -0.0598 0.0954  -0.0623 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3891 0.3029 0.3235 -0.0493 0.0912  -0.0591 109 ALA A CA  
934  C C   . ALA A 108 ? 0.4129 0.3277 0.3647 -0.0401 0.0948  -0.0617 109 ALA A C   
935  O O   . ALA A 108 ? 0.3883 0.3062 0.3490 -0.0307 0.0880  -0.0558 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3945 0.3193 0.3361 -0.0515 0.0944  -0.0625 109 ALA A CB  
937  N N   . MET A 109 ? 0.3950 0.3042 0.3489 -0.0426 0.1056  -0.0705 110 MET A N   
938  C CA  . MET A 109 ? 0.3932 0.2993 0.3620 -0.0327 0.1090  -0.0733 110 MET A CA  
939  C C   . MET A 109 ? 0.4454 0.3369 0.4043 -0.0307 0.1042  -0.0665 110 MET A C   
940  O O   . MET A 109 ? 0.4431 0.3320 0.4106 -0.0201 0.1000  -0.0617 110 MET A O   
941  C CB  . MET A 109 ? 0.4347 0.3368 0.4067 -0.0372 0.1226  -0.0855 110 MET A CB  
942  C CG  . MET A 109 ? 0.4918 0.4109 0.4808 -0.0371 0.1290  -0.0943 110 MET A CG  
943  S SD  . MET A 109 ? 0.6009 0.5155 0.5900 -0.0464 0.1473  -0.1105 110 MET A SD  
944  C CE  . MET A 109 ? 0.5718 0.4788 0.5793 -0.0311 0.1492  -0.1137 110 MET A CE  
945  N N   . TYR A 110 ? 0.4241 0.3062 0.3639 -0.0413 0.1046  -0.0664 111 TYR A N   
946  C CA  . TYR A 110 ? 0.4172 0.2879 0.3474 -0.0429 0.1013  -0.0623 111 TYR A CA  
947  C C   . TYR A 110 ? 0.4430 0.3198 0.3751 -0.0377 0.0905  -0.0527 111 TYR A C   
948  O O   . TYR A 110 ? 0.4102 0.2787 0.3433 -0.0332 0.0893  -0.0487 111 TYR A O   
949  C CB  . TYR A 110 ? 0.4295 0.2951 0.3404 -0.0556 0.1019  -0.0658 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.4362 0.2956 0.3384 -0.0596 0.0976  -0.0636 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4839 0.3295 0.3850 -0.0611 0.1046  -0.0674 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.4304 0.2976 0.3255 -0.0628 0.0876  -0.0594 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.4657 0.3067 0.3592 -0.0670 0.1023  -0.0672 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.4371 0.3023 0.3270 -0.0675 0.0845  -0.0600 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4922 0.3449 0.3813 -0.0705 0.0923  -0.0642 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4598 0.3121 0.3441 -0.0773 0.0904  -0.0665 111 TYR A OH  
957  N N   . LEU A 111 ? 0.4038 0.2929 0.3351 -0.0388 0.0837  -0.0493 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3848 0.2811 0.3180 -0.0349 0.0742  -0.0415 112 LEU A CA  
959  C C   . LEU A 111 ? 0.4209 0.3232 0.3685 -0.0237 0.0717  -0.0376 112 LEU A C   
960  O O   . LEU A 111 ? 0.4025 0.3082 0.3505 -0.0201 0.0649  -0.0313 112 LEU A O   
961  C CB  . LEU A 111 ? 0.3691 0.2741 0.2954 -0.0397 0.0679  -0.0400 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.4085 0.3083 0.3186 -0.0487 0.0657  -0.0423 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.4038 0.3095 0.3068 -0.0504 0.0579  -0.0396 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.4224 0.3191 0.3300 -0.0505 0.0632  -0.0418 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3801 0.2845 0.3397 -0.0180 0.0770  -0.0423 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3707 0.2832 0.3458 -0.0057 0.0730  -0.0401 113 GLN A CA  
967  C C   . GLN A 112 ? 0.4102 0.3401 0.3903 -0.0053 0.0658  -0.0373 113 GLN A C   
968  O O   . GLN A 112 ? 0.4023 0.3355 0.3826 -0.0001 0.0580  -0.0306 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3866 0.2851 0.3585 0.0024  0.0698  -0.0336 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.4362 0.3148 0.4033 0.0022  0.0781  -0.0372 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.6112 0.4707 0.5676 0.0059  0.0759  -0.0297 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.5173 0.3777 0.4736 0.0136  0.0683  -0.0224 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.5513 0.3922 0.4963 -0.0009 0.0829  -0.0318 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3532 0.2919 0.3342 -0.0125 0.0696  -0.0428 114 MET A N   
975  C CA  . MET A 113 ? 0.3393 0.2924 0.3240 -0.0144 0.0652  -0.0421 114 MET A CA  
976  C C   . MET A 113 ? 0.4135 0.3806 0.4159 -0.0124 0.0708  -0.0510 114 MET A C   
977  O O   . MET A 113 ? 0.3926 0.3605 0.3923 -0.0215 0.0791  -0.0580 114 MET A O   
978  C CB  . MET A 113 ? 0.3583 0.3053 0.3253 -0.0256 0.0653  -0.0412 114 MET A CB  
979  C CG  . MET A 113 ? 0.3886 0.3269 0.3431 -0.0267 0.0591  -0.0346 114 MET A CG  
980  S SD  . MET A 113 ? 0.4449 0.3758 0.3796 -0.0369 0.0571  -0.0346 114 MET A SD  
981  C CE  . MET A 113 ? 0.4021 0.3435 0.3397 -0.0363 0.0513  -0.0319 114 MET A CE  
982  N N   . GLU A 114 ? 0.4051 0.3826 0.4252 -0.0003 0.0666  -0.0515 115 GLU A N   
983  C CA  . GLU A 114 ? 0.4209 0.4156 0.4640 0.0049  0.0707  -0.0618 115 GLU A CA  
984  C C   . GLU A 114 ? 0.4163 0.4277 0.4663 -0.0042 0.0753  -0.0695 115 GLU A C   
985  O O   . GLU A 114 ? 0.4061 0.4255 0.4677 -0.0081 0.0853  -0.0810 115 GLU A O   
986  C CB  . GLU A 114 ? 0.4536 0.4575 0.5126 0.0213  0.0610  -0.0594 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.6241 0.6077 0.6759 0.0307  0.0586  -0.0530 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3694 0.3854 0.4124 -0.0087 0.0694  -0.0645 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3827 0.4117 0.4305 -0.0185 0.0748  -0.0723 116 HIS A CA  
990  C C   . HIS A 115 ? 0.4115 0.4258 0.4411 -0.0334 0.0861  -0.0758 116 HIS A C   
991  O O   . HIS A 115 ? 0.4129 0.4353 0.4490 -0.0419 0.0964  -0.0864 116 HIS A O   
992  C CB  . HIS A 115 ? 0.4075 0.4433 0.4522 -0.0193 0.0662  -0.0668 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.4612 0.5132 0.5227 -0.0061 0.0555  -0.0650 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4962 0.5715 0.5836 0.0004  0.0555  -0.0751 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4873 0.5356 0.5417 0.0010  0.0445  -0.0549 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4901 0.5734 0.5835 0.0124  0.0430  -0.0697 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4908 0.5573 0.5635 0.0123  0.0368  -0.0574 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.3461 0.3389 0.3525 -0.0367 0.0845  -0.0678 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3544 0.3302 0.3390 -0.0497 0.0931  -0.0701 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.4331 0.4098 0.4259 -0.0520 0.1052  -0.0807 117 VAL A C   
1001 O O   . VAL A 116 ? 0.4246 0.3994 0.4113 -0.0637 0.1166  -0.0889 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.4069 0.3628 0.3670 -0.0514 0.0866  -0.0604 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.4230 0.3610 0.3591 -0.0637 0.0943  -0.0632 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3984 0.3543 0.3516 -0.0500 0.0761  -0.0522 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3937 0.3719 0.3992 -0.0412 0.1037  -0.0809 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.4024 0.3817 0.4188 -0.0412 0.1151  -0.0919 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.4579 0.4592 0.4973 -0.0435 0.1238  -0.1056 118 VAL A C   
1008 O O   . VAL A 117 ? 0.4468 0.4463 0.4832 -0.0546 0.1376  -0.1162 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.4369 0.4122 0.4640 -0.0272 0.1109  -0.0895 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.4422 0.4186 0.4825 -0.0263 0.1232  -0.1023 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.4375 0.3919 0.4416 -0.0286 0.1052  -0.0788 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.4141 0.4361 0.4747 -0.0347 0.1160  -0.1058 119 ASP A N   
1013 N N   B ASP A 118 ? 0.4172 0.4396 0.4793 -0.0337 0.1160  -0.1061 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.4165 0.4645 0.5030 -0.0361 0.1222  -0.1197 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.4203 0.4694 0.5095 -0.0344 0.1220  -0.1202 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.4516 0.4973 0.5242 -0.0560 0.1345  -0.1264 119 ASP A C   
1017 C C   B ASP A 118 ? 0.4717 0.5200 0.5489 -0.0541 0.1346  -0.1277 119 ASP A C   
1018 O O   A ASP A 118 ? 0.4553 0.5117 0.5404 -0.0638 0.1486  -0.1415 119 ASP A O   
1019 O O   B ASP A 118 ? 0.4777 0.5382 0.5690 -0.0612 0.1483  -0.1432 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.4351 0.5038 0.5411 -0.0237 0.1086  -0.1165 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.4359 0.5055 0.5442 -0.0221 0.1083  -0.1169 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.6191 0.7196 0.7562 -0.0237 0.1130  -0.1324 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.5989 0.6752 0.7262 -0.0015 0.0978  -0.1146 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.6580 0.7727 0.8195 -0.0174 0.1190  -0.1451 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.6330 0.7085 0.7724 0.0046  0.1037  -0.1221 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.6953 0.8074 0.8337 -0.0300 0.1107  -0.1332 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.6806 0.7615 0.8095 0.0084  0.0838  -0.1057 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.3992 0.4295 0.4455 -0.0644 0.1300  -0.1159 120 THR A N   
1029 N N   B THR A 119 ? 0.4255 0.4580 0.4758 -0.0629 0.1306  -0.1174 120 THR A N   
1030 C CA  A THR A 119 ? 0.4129 0.4349 0.4411 -0.0833 0.1416  -0.1211 120 THR A CA  
1031 C CA  B THR A 119 ? 0.4375 0.4620 0.4696 -0.0816 0.1413  -0.1219 120 THR A CA  
1032 C C   A THR A 119 ? 0.4740 0.4747 0.4790 -0.0957 0.1546  -0.1249 120 THR A C   
1033 C C   B THR A 119 ? 0.4895 0.4922 0.4975 -0.0946 0.1546  -0.1256 120 THR A C   
1034 O O   A THR A 119 ? 0.4625 0.4620 0.4615 -0.1110 0.1695  -0.1356 120 THR A O   
1035 O O   B THR A 119 ? 0.4880 0.4914 0.4922 -0.1095 0.1696  -0.1370 120 THR A O   
1036 C CB  A THR A 119 ? 0.4374 0.4468 0.4438 -0.0881 0.1335  -0.1100 120 THR A CB  
1037 C CB  B THR A 119 ? 0.5286 0.5416 0.5405 -0.0842 0.1314  -0.1096 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.4655 0.4696 0.4597 -0.1056 0.1462  -0.1177 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.5013 0.5337 0.5348 -0.0706 0.1184  -0.1058 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.3922 0.3736 0.3673 -0.0872 0.1252  -0.0955 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.5362 0.5441 0.5349 -0.1015 0.1418  -0.1155 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.4441 0.4279 0.4352 -0.0902 0.1497  -0.1170 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.4711 0.4342 0.4383 -0.1014 0.1607  -0.1205 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.5246 0.5031 0.5148 -0.1041 0.1762  -0.1378 121 CYS A C   
1045 O O   . CYS A 120 ? 0.5323 0.5024 0.5076 -0.1204 0.1918  -0.1473 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.4747 0.4212 0.4272 -0.0942 0.1515  -0.1101 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.5235 0.4495 0.4442 -0.0948 0.1360  -0.0929 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4773 0.4775 0.5029 -0.0879 0.1721  -0.1426 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4814 0.4813 0.5068 -0.0879 0.1722  -0.1426 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4842 0.5034 0.5395 -0.0858 0.1846  -0.1604 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4905 0.5089 0.5447 -0.0865 0.1852  -0.1606 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.5325 0.5704 0.6004 -0.0990 0.1982  -0.1757 122 ARG A C   
1053 C C   B ARG A 121 ? 0.5348 0.5727 0.6026 -0.0992 0.1984  -0.1758 122 ARG A C   
1054 O O   A ARG A 121 ? 0.5378 0.5789 0.6096 -0.1101 0.2159  -0.1912 122 ARG A O   
1055 O O   B ARG A 121 ? 0.5393 0.5808 0.6115 -0.1103 0.2161  -0.1915 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4833 0.5221 0.5737 -0.0631 0.1734  -0.1605 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.5000 0.5367 0.5887 -0.0639 0.1747  -0.1610 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.6437 0.6638 0.7253 -0.0513 0.1652  -0.1501 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6905 0.7089 0.7721 -0.0547 0.1718  -0.1555 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7856 0.8205 0.9002 -0.0304 0.1590  -0.1542 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.8046 0.8390 0.9215 -0.0348 0.1682  -0.1623 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.8606 0.8744 0.9632 -0.0195 0.1495  -0.1415 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.8672 0.9110 0.9964 -0.0181 0.1501  -0.1515 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 1.0022 0.9983 1.0969 -0.0199 0.1567  -0.1442 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 1.0013 1.0300 1.1236 -0.0049 0.1380  -0.1386 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.8762 0.8734 0.9737 -0.0300 0.1733  -0.1591 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.8206 0.8252 0.9263 -0.0062 0.1421  -0.1355 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.7845 0.7611 0.8677 -0.0115 0.1484  -0.1329 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.7981 0.8347 0.9287 0.0085  0.1226  -0.1294 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4809 0.5307 0.5543 -0.0993 0.1910  -0.1722 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4862 0.5545 0.5719 -0.1131 0.2033  -0.1868 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.5510 0.5933 0.5984 -0.1378 0.2192  -0.1886 123 LYS A C   
1073 O O   . LYS A 122 ? 0.5411 0.5930 0.5961 -0.1525 0.2382  -0.2063 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.5036 0.5894 0.6032 -0.1068 0.1905  -0.1819 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.7307 0.8479 0.8722 -0.0845 0.1780  -0.1857 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.8844 1.0193 1.0381 -0.0784 0.1645  -0.1813 123 LYS A CD  
1077 C CE  . LYS A 122 ? 1.0462 1.2072 1.2352 -0.0549 0.1500  -0.1829 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.1954 1.3891 1.4109 -0.0526 0.1440  -0.1914 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.5159 0.5248 0.5215 -0.1422 0.2116  -0.1711 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.5460 0.5235 0.5078 -0.1637 0.2234  -0.1696 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.6260 0.5923 0.5760 -0.1732 0.2388  -0.1791 124 PHE A C   
1082 O O   . PHE A 123 ? 0.6346 0.5894 0.5648 -0.1937 0.2570  -0.1890 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.5712 0.5179 0.4950 -0.1615 0.2080  -0.1487 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.5914 0.5361 0.5093 -0.1631 0.2005  -0.1414 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.6081 0.5836 0.5626 -0.1524 0.1932  -0.1445 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.6526 0.5631 0.5269 -0.1736 0.1988  -0.1307 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.6185 0.5917 0.5669 -0.1545 0.1868  -0.1386 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.6756 0.5822 0.5445 -0.1744 0.1921  -0.1244 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.6162 0.5546 0.5225 -0.1655 0.1869  -0.1288 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.5671 0.5362 0.5288 -0.1592 0.2327  -0.1773 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5907 0.5513 0.5449 -0.1668 0.2472  -0.1877 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.6603 0.6489 0.6489 -0.1732 0.2668  -0.2116 125 ILE A C   
1093 O O   . ILE A 124 ? 0.6874 0.6655 0.6582 -0.1925 0.2866  -0.2236 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.6164 0.5710 0.5737 -0.1508 0.2359  -0.1798 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.6267 0.5506 0.5423 -0.1519 0.2222  -0.1605 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.6477 0.6010 0.6091 -0.1561 0.2524  -0.1948 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.6954 0.6177 0.6181 -0.1342 0.2060  -0.1494 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.6013 0.6255 0.6378 -0.1577 0.2613  -0.2192 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.6084 0.6662 0.6856 -0.1605 0.2772  -0.2436 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.6773 0.7358 0.7423 -0.1860 0.2961  -0.2559 126 LYS A C   
1101 O O   . LYS A 125 ? 0.6784 0.7496 0.7566 -0.1989 0.3173  -0.2771 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.6177 0.7124 0.7448 -0.1377 0.2630  -0.2469 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.6296 0.6729 0.6684 -0.1939 0.2895  -0.2431 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.6562 0.6932 0.6769 -0.2191 0.3069  -0.2523 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.7654 0.7662 0.7382 -0.2431 0.3260  -0.2547 127 ALA A C   
1106 O O   . ALA A 126 ? 0.7745 0.7762 0.7414 -0.2656 0.3479  -0.2707 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.6552 0.6796 0.6568 -0.2193 0.2933  -0.2362 127 ALA A CB  
1108 N N   . SER A 127 ? 0.7684 0.7370 0.7055 -0.2394 0.3177  -0.2393 128 SER A N   
1109 C CA  . SER A 127 ? 0.8354 0.7663 0.7212 -0.2607 0.3324  -0.2391 128 SER A CA  
1110 C C   . SER A 127 ? 0.9344 0.8735 0.8313 -0.2673 0.3513  -0.2579 128 SER A C   
1111 O O   . SER A 127 ? 0.9860 0.8975 0.8424 -0.2891 0.3682  -0.2625 128 SER A O   
1112 C CB  . SER A 127 ? 0.9131 0.8059 0.7529 -0.2548 0.3138  -0.2147 128 SER A CB  
1113 O OG  . SER A 127 ? 1.0648 0.9327 0.8702 -0.2629 0.3078  -0.2015 128 SER A OG  
1114 N N   . GLU A 128 ? 0.8637 0.8387 0.8134 -0.2490 0.3490  -0.2692 129 GLU A N   
1115 C CA  . GLU A 128 ? 1.1217 1.1067 1.0877 -0.2524 0.3663  -0.2884 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.6559 1.6644 1.6441 -0.2717 0.3938  -0.3162 129 GLU A C   
1117 O O   . GLU A 128 ? 1.2525 1.2520 1.2192 -0.2925 0.4053  -0.3192 129 GLU A O   
1118 C CB  . GLU A 128 ? 1.1054 1.1141 1.1157 -0.2241 0.3525  -0.2888 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.2004 1.2554 1.2725 -0.2077 0.3488  -0.3019 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.4522 1.5249 1.5624 -0.1775 0.3311  -0.2981 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.3808 1.4293 1.4690 -0.1666 0.3161  -0.2794 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.3491 1.4595 1.5108 -0.1646 0.3321  -0.3143 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.2573 0.5139 0.3270 -0.0304 -0.0233 -0.0883 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2668 0.5234 0.3364 -0.0304 -0.0232 -0.0883 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.2504 0.5046 0.3182 -0.0299 -0.0235 -0.0895 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2643 0.5187 0.3322 -0.0299 -0.0235 -0.0895 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.3029 0.5572 0.3720 -0.0299 -0.0245 -0.0895 1   TRP D C   
1131 C C   B TRP B 2   ? 0.3007 0.5555 0.3701 -0.0299 -0.0244 -0.0895 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2974 0.5517 0.3679 -0.0301 -0.0254 -0.0891 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2886 0.5438 0.3595 -0.0303 -0.0252 -0.0889 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.2391 0.4907 0.3048 -0.0294 -0.0242 -0.0901 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.2566 0.5082 0.3224 -0.0294 -0.0242 -0.0901 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.2432 0.4943 0.3066 -0.0294 -0.0234 -0.0903 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2707 0.5220 0.3379 -0.0294 -0.0256 -0.0905 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2758 0.5272 0.3393 -0.0297 -0.0232 -0.0898 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.3100 0.5608 0.3790 -0.0297 -0.0261 -0.0908 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.2362 0.4868 0.2973 -0.0290 -0.0225 -0.0909 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2719 0.5238 0.3397 -0.0290 -0.0264 -0.0911 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2648 0.5157 0.3250 -0.0296 -0.0222 -0.0903 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.3050 0.5564 0.3764 -0.0297 -0.0271 -0.0920 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2786 0.5290 0.3373 -0.0291 -0.0219 -0.0911 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.3226 0.5750 0.3928 -0.0293 -0.0272 -0.0922 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.2455 0.4958 0.3070 -0.0285 -0.0220 -0.0911 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2816 0.5343 0.3489 -0.0286 -0.0262 -0.0907 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2746 0.5243 0.3305 -0.0288 -0.0209 -0.0919 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.3134 0.5677 0.3848 -0.0290 -0.0278 -0.0934 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.2583 0.5080 0.3182 -0.0281 -0.0211 -0.0916 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.3032 0.5577 0.3712 -0.0282 -0.0268 -0.0912 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2685 0.5178 0.3253 -0.0283 -0.0205 -0.0921 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.3092 0.5648 0.3790 -0.0285 -0.0275 -0.0928 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.2478 0.5023 0.3170 -0.0296 -0.0241 -0.0899 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.2472 0.5020 0.3172 -0.0295 -0.0247 -0.0898 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2797 0.5336 0.3494 -0.0287 -0.0244 -0.0896 2   VAL D C   
1157 O O   . VAL B 3   ? 0.2591 0.5123 0.3287 -0.0282 -0.0236 -0.0895 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2818 0.5397 0.3540 -0.0301 -0.0245 -0.0902 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2782 0.5391 0.3515 -0.0308 -0.0249 -0.0895 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2797 0.5389 0.3538 -0.0301 -0.0231 -0.0914 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.2370 0.4914 0.3069 -0.0284 -0.0248 -0.0892 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.2340 0.4889 0.3048 -0.0275 -0.0242 -0.0881 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2906 0.5456 0.3643 -0.0279 -0.0234 -0.0885 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2796 0.5355 0.3535 -0.0284 -0.0241 -0.0892 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.2658 0.5223 0.3356 -0.0271 -0.0248 -0.0876 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.2537 0.5115 0.3220 -0.0270 -0.0256 -0.0885 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2953 0.5536 0.3668 -0.0260 -0.0238 -0.0856 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.2982 0.5573 0.3664 -0.0263 -0.0255 -0.0882 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2876 0.5423 0.3642 -0.0276 -0.0221 -0.0884 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2938 0.5495 0.3750 -0.0280 -0.0212 -0.0898 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.3419 0.5980 0.4257 -0.0276 -0.0211 -0.0888 4   PRO D C   
1172 O O   . PRO B 5   ? 0.3374 0.5933 0.4208 -0.0266 -0.0209 -0.0863 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.3213 0.5765 0.4056 -0.0277 -0.0196 -0.0902 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.3680 0.6218 0.4500 -0.0267 -0.0197 -0.0876 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.3144 0.5682 0.3910 -0.0269 -0.0214 -0.0875 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.3263 0.5841 0.4137 -0.0283 -0.0210 -0.0907 5   ALA D N   
# 
