data_7GV1
# 
_entry.id   7GV1 
# 
_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   7GV1         pdb_00007gv1 10.2210/pdb7gv1/pdb 
WWPDB D_1001406672 ?            ?                   
# 
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                        7GV1 
_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 19  HOH   HOH A . 
F 6 HOH   4   304 166 HOH   HOH A . 
F 6 HOH   5   305 29  HOH   HOH A . 
F 6 HOH   6   306 45  HOH   HOH A . 
F 6 HOH   7   307 94  HOH   HOH A . 
F 6 HOH   8   308 140 HOH   HOH A . 
F 6 HOH   9   309 173 HOH   HOH A . 
F 6 HOH   10  310 179 HOH   HOH A . 
F 6 HOH   11  311 142 HOH   HOH A . 
F 6 HOH   12  312 90  HOH   HOH A . 
F 6 HOH   13  313 47  HOH   HOH A . 
F 6 HOH   14  314 247 HOH   HOH A . 
F 6 HOH   15  315 139 HOH   HOH A . 
F 6 HOH   16  316 106 HOH   HOH A . 
F 6 HOH   17  317 83  HOH   HOH A . 
F 6 HOH   18  318 100 HOH   HOH A . 
F 6 HOH   19  319 101 HOH   HOH A . 
F 6 HOH   20  320 99  HOH   HOH A . 
F 6 HOH   21  321 202 HOH   HOH A . 
F 6 HOH   22  322 75  HOH   HOH A . 
F 6 HOH   23  323 132 HOH   HOH A . 
F 6 HOH   24  324 40  HOH   HOH A . 
F 6 HOH   25  325 119 HOH   HOH A . 
F 6 HOH   26  326 87  HOH   HOH A . 
F 6 HOH   27  327 37  HOH   HOH A . 
F 6 HOH   28  328 27  HOH   HOH A . 
F 6 HOH   29  329 193 HOH   HOH A . 
F 6 HOH   30  330 6   HOH   HOH A . 
F 6 HOH   31  331 91  HOH   HOH A . 
F 6 HOH   32  332 237 HOH   HOH A . 
F 6 HOH   33  333 84  HOH   HOH A . 
F 6 HOH   34  334 117 HOH   HOH A . 
F 6 HOH   35  335 242 HOH   HOH A . 
F 6 HOH   36  336 42  HOH   HOH A . 
F 6 HOH   37  337 14  HOH   HOH A . 
F 6 HOH   38  338 243 HOH   HOH A . 
F 6 HOH   39  339 239 HOH   HOH A . 
F 6 HOH   40  340 20  HOH   HOH A . 
F 6 HOH   41  341 17  HOH   HOH A . 
F 6 HOH   42  342 34  HOH   HOH A . 
F 6 HOH   43  343 5   HOH   HOH A . 
F 6 HOH   44  344 86  HOH   HOH A . 
F 6 HOH   45  345 196 HOH   HOH A . 
F 6 HOH   46  346 4   HOH   HOH A . 
F 6 HOH   47  347 30  HOH   HOH A . 
F 6 HOH   48  348 85  HOH   HOH A . 
F 6 HOH   49  349 44  HOH   HOH A . 
F 6 HOH   50  350 12  HOH   HOH A . 
F 6 HOH   51  351 24  HOH   HOH A . 
F 6 HOH   52  352 97  HOH   HOH A . 
F 6 HOH   53  353 151 HOH   HOH A . 
F 6 HOH   54  354 244 HOH   HOH A . 
F 6 HOH   55  355 96  HOH   HOH A . 
F 6 HOH   56  356 124 HOH   HOH A . 
F 6 HOH   57  357 93  HOH   HOH A . 
F 6 HOH   58  358 51  HOH   HOH A . 
F 6 HOH   59  359 141 HOH   HOH A . 
F 6 HOH   60  360 175 HOH   HOH A . 
F 6 HOH   61  361 89  HOH   HOH A . 
F 6 HOH   62  362 122 HOH   HOH A . 
F 6 HOH   63  363 15  HOH   HOH A . 
F 6 HOH   64  364 145 HOH   HOH A . 
F 6 HOH   65  365 207 HOH   HOH A . 
F 6 HOH   66  366 103 HOH   HOH A . 
F 6 HOH   67  367 28  HOH   HOH A . 
F 6 HOH   68  368 133 HOH   HOH A . 
F 6 HOH   69  369 39  HOH   HOH A . 
F 6 HOH   70  370 186 HOH   HOH A . 
F 6 HOH   71  371 50  HOH   HOH A . 
F 6 HOH   72  372 180 HOH   HOH A . 
F 6 HOH   73  373 144 HOH   HOH A . 
F 6 HOH   74  374 25  HOH   HOH A . 
F 6 HOH   75  375 170 HOH   HOH A . 
F 6 HOH   76  376 21  HOH   HOH A . 
F 6 HOH   77  377 131 HOH   HOH A . 
F 6 HOH   78  378 70  HOH   HOH A . 
F 6 HOH   79  379 167 HOH   HOH A . 
F 6 HOH   80  380 105 HOH   HOH A . 
F 6 HOH   81  381 192 HOH   HOH A . 
F 6 HOH   82  382 55  HOH   HOH A . 
F 6 HOH   83  383 177 HOH   HOH A . 
F 6 HOH   84  384 16  HOH   HOH A . 
F 6 HOH   85  385 241 HOH   HOH A . 
F 6 HOH   86  386 69  HOH   HOH A . 
F 6 HOH   87  387 76  HOH   HOH A . 
F 6 HOH   88  388 157 HOH   HOH A . 
F 6 HOH   89  389 169 HOH   HOH A . 
F 6 HOH   90  390 108 HOH   HOH A . 
F 6 HOH   91  391 245 HOH   HOH A . 
F 6 HOH   92  392 229 HOH   HOH A . 
F 6 HOH   93  393 194 HOH   HOH A . 
F 6 HOH   94  394 32  HOH   HOH A . 
F 6 HOH   95  395 92  HOH   HOH A . 
F 6 HOH   96  396 74  HOH   HOH A . 
F 6 HOH   97  397 191 HOH   HOH A . 
F 6 HOH   98  398 165 HOH   HOH A . 
F 6 HOH   99  399 205 HOH   HOH A . 
F 6 HOH   100 400 22  HOH   HOH A . 
F 6 HOH   101 401 212 HOH   HOH A . 
F 6 HOH   102 402 35  HOH   HOH A . 
F 6 HOH   103 403 185 HOH   HOH A . 
F 6 HOH   104 404 174 HOH   HOH A . 
F 6 HOH   105 405 64  HOH   HOH A . 
F 6 HOH   106 406 129 HOH   HOH A . 
F 6 HOH   107 407 120 HOH   HOH A . 
F 6 HOH   108 408 223 HOH   HOH A . 
F 6 HOH   109 409 60  HOH   HOH A . 
F 6 HOH   110 410 82  HOH   HOH A . 
F 6 HOH   111 411 43  HOH   HOH A . 
F 6 HOH   112 412 46  HOH   HOH A . 
F 6 HOH   113 413 26  HOH   HOH A . 
F 6 HOH   114 414 176 HOH   HOH A . 
F 6 HOH   115 415 190 HOH   HOH A . 
F 6 HOH   116 416 67  HOH   HOH A . 
F 6 HOH   117 417 236 HOH   HOH A . 
F 6 HOH   118 418 215 HOH   HOH A . 
F 6 HOH   119 419 36  HOH   HOH A . 
F 6 HOH   120 420 204 HOH   HOH A . 
F 6 HOH   121 421 110 HOH   HOH A . 
F 6 HOH   122 422 56  HOH   HOH A . 
F 6 HOH   123 423 88  HOH   HOH A . 
F 6 HOH   124 424 61  HOH   HOH A . 
F 6 HOH   125 425 68  HOH   HOH A . 
F 6 HOH   126 426 57  HOH   HOH A . 
F 6 HOH   127 427 95  HOH   HOH A . 
F 6 HOH   128 428 65  HOH   HOH A . 
F 6 HOH   129 429 41  HOH   HOH A . 
F 6 HOH   130 430 116 HOH   HOH A . 
F 6 HOH   131 431 135 HOH   HOH A . 
F 6 HOH   132 432 147 HOH   HOH A . 
F 6 HOH   133 433 200 HOH   HOH A . 
F 6 HOH   134 434 168 HOH   HOH A . 
F 6 HOH   135 435 187 HOH   HOH A . 
F 6 HOH   136 436 214 HOH   HOH A . 
F 6 HOH   137 437 227 HOH   HOH A . 
F 6 HOH   138 438 248 HOH   HOH A . 
F 6 HOH   139 439 123 HOH   HOH A . 
F 6 HOH   140 440 228 HOH   HOH A . 
F 6 HOH   141 441 231 HOH   HOH A . 
F 6 HOH   142 442 63  HOH   HOH A . 
F 6 HOH   143 443 71  HOH   HOH A . 
F 6 HOH   144 444 225 HOH   HOH A . 
F 6 HOH   145 445 171 HOH   HOH A . 
F 6 HOH   146 446 121 HOH   HOH A . 
F 6 HOH   147 447 234 HOH   HOH A . 
F 6 HOH   148 448 220 HOH   HOH A . 
F 6 HOH   149 449 203 HOH   HOH A . 
F 6 HOH   150 450 125 HOH   HOH A . 
F 6 HOH   151 451 181 HOH   HOH A . 
F 6 HOH   152 452 158 HOH   HOH A . 
F 6 HOH   153 453 217 HOH   HOH A . 
F 6 HOH   154 454 235 HOH   HOH A . 
F 6 HOH   155 455 238 HOH   HOH A . 
F 6 HOH   156 456 114 HOH   HOH A . 
F 6 HOH   157 457 79  HOH   HOH A . 
F 6 HOH   158 458 246 HOH   HOH A . 
F 6 HOH   159 459 81  HOH   HOH A . 
F 6 HOH   160 460 221 HOH   HOH A . 
F 6 HOH   161 461 216 HOH   HOH A . 
F 6 HOH   162 462 107 HOH   HOH A . 
F 6 HOH   163 463 115 HOH   HOH A . 
F 6 HOH   164 464 230 HOH   HOH A . 
F 6 HOH   165 465 182 HOH   HOH A . 
F 6 HOH   166 466 183 HOH   HOH A . 
F 6 HOH   167 467 188 HOH   HOH A . 
F 6 HOH   168 468 201 HOH   HOH A . 
F 6 HOH   169 469 213 HOH   HOH A . 
F 6 HOH   170 470 48  HOH   HOH A . 
F 6 HOH   171 471 148 HOH   HOH A . 
F 6 HOH   172 472 113 HOH   HOH A . 
F 6 HOH   173 473 206 HOH   HOH A . 
F 6 HOH   174 474 172 HOH   HOH A . 
F 6 HOH   175 475 211 HOH   HOH A . 
G 6 HOH   1   201 62  HOH   HOH D . 
G 6 HOH   2   202 38  HOH   HOH D . 
G 6 HOH   3   203 23  HOH   HOH D . 
G 6 HOH   4   204 78  HOH   HOH D . 
G 6 HOH   5   205 73  HOH   HOH D . 
G 6 HOH   6   206 53  HOH   HOH D . 
G 6 HOH   7   207 240 HOH   HOH D . 
G 6 HOH   8   208 49  HOH   HOH D . 
G 6 HOH   9   209 58  HOH   HOH D . 
G 6 HOH   10  210 195 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 A LYS 126 ? CG  ? A LYS 125 CG  
8  1 Y 1 A LYS 126 ? CD  ? A LYS 125 CD  
9  1 Y 1 A LYS 126 ? CE  ? A LYS 125 CE  
10 1 Y 1 A LYS 126 ? NZ  ? A LYS 125 NZ  
11 1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
12 1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
13 1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
14 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com phasing           
http://www.globalphasing.com/buster/                ?   ? 
5 PDB_EXTRACT 3.24   'Sep. 1, 2017' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.entry_id           7GV1 
_cell.length_a           67.640 
_cell.length_b           67.640 
_cell.length_c           166.630 
_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                         7GV1 
_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          7GV1 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.63 
_exptl_crystal.density_percent_sol   66.14 
_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                     7GV1 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.950 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23675 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.074 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.500 
_reflns.B_iso_Wilson_estimate        33.320 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.078 
_reflns.pdbx_Rpim_I_all              0.026 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     214723 
_reflns.pdbx_scaling_rejects         976 
_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  ? 11920 1279 ? 2.214 ? ? ? 9.300 ? 1.200  ? ? ? ? ? ? 100.000 2.341 0.753 0.571 ? 
1 2 9.090 33.950 ? 1492  228  ? 0.030 ? ? ? 6.500 ? 41.300 ? ? ? ? ? ? 98.800  0.032 0.012 0.999 ? 
# 
_refine.entry_id                                 7GV1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             33.9500 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.9000 
_refine.ls_number_reflns_obs                     23607 
_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                       0.1780 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2030 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1500 
_refine.ls_number_reflns_R_free                  1215 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               37.8900 
_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]                            -0.0894 
_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          0.9460 
_refine.overall_SU_R_Cruickshank_DPI             0.0860 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0860 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0980 
_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                                128.630 
_refine.B_iso_min                                19.200 
_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                        7GV1 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.230 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.7500 
_refine_hist.d_res_low                        33.9500 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             185 
_refine_hist.number_atoms_total               1231 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           32.94 
_refine_hist.pdbx_B_iso_mean_solvent          55.53 
_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      1652 ?      ? 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           ?    14.660 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.7500 
_refine_ls_shell.d_res_low                        1.8300 
_refine_ls_shell.pdbx_total_number_of_bins_used   12 
_refine_ls_shell.percent_reflns_obs               99.7200 
_refine_ls_shell.number_reflns_R_work             2690 
_refine_ls_shell.R_factor_all                     0.3405 
_refine_ls_shell.R_factor_R_work                  0.3396 
_refine_ls_shell.R_factor_R_free                  0.3585 
_refine_ls_shell.percent_reflns_R_free            4.6100 
_refine_ls_shell.number_reflns_R_free             130 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2820 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GV1 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 12.50 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GV1 
_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 7GV1       7GV1   ? 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 7GV1 A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GV1 D 1 ? 6   ? 7GV1   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 7GV1 GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GV1 PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GV1 GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7390  ? 
1 MORE         -64   ? 
1 'SSA (A^2)'  12970 ? 
# 
_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 33.8200000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5779583120 0.0000000000 0.0000000000 -1.0000000000 27.7716666667 
# 
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 ? ? ? ? ? ? ? 1.330 ? ? 
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                   7GV1 
_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 61.41 -118.87 
2 1 SER A 39  ? B 38.51 65.93   
3 1 ARG A 40  ? B 74.82 -22.59  
4 1 SER A 93  ? A 76.08 -3.23   
5 1 GLN A 113 ? ? 62.28 60.30   
# 
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 375 ? F HOH . 
2 1 A HOH 389 ? F HOH . 
3 1 A HOH 454 ? F HOH . 
4 1 A HOH 464 ? F HOH . 
5 1 A HOH 466 ? F HOH . 
6 1 A HOH 468 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.2144 -16.5503 24.6837 0.0155  -0.0485 -0.0708 -0.0418 0.0282  -0.0218 1.0106 1.8047  1.9421 
0.4762 -0.3030 1.1738 0.1386 -0.0732 -0.0653 -0.0560 0.1022  0.0906 0.2472  -0.0119 -0.0090 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1160 0.1272  -0.0391 -0.0277 -0.0178 -0.0893 0.9740 -0.2793 0.0000 
0.0393 0.0092  0.4636 0.0288 -0.0125 -0.0163 -0.0145 -0.0023 0.0309 -0.0324 0.0049  -0.0092 
# 
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                    7GV1 
_atom_sites.fract_transf_matrix[1][1]   0.014784 
_atom_sites.fract_transf_matrix[1][2]   0.008536 
_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]   0.017071 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006001 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
BR 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP   A 1 5   ? 17.294 -21.239 -4.798 1.00 68.81  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.209 -22.114 -5.532 1.00 67.72  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.760 -23.595 -5.467 1.00 67.02  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.723 -23.909 -4.870 1.00 67.71  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.647 -21.953 -4.980 1.00 68.64  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.732 -21.998 -6.046 1.00 82.81  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.868 -23.052 -6.717 1.00 83.13  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.452 -20.985 -6.202 1.00 89.94  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.536 -24.493 -6.093 1.00 58.14  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.286 -25.932 -6.087 1.00 55.23  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.282 -26.649 -5.121 1.00 50.44  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.591 -27.823 -5.310 1.00 49.06  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.381 -26.489 -7.504 1.00 61.00  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.650 -26.239 -8.085 1.00 72.72  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.753 -25.946 -4.071 1.00 41.55  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.698 -26.509 -3.101 1.00 38.43  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.097 -27.669 -2.295 1.00 38.27  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.877 -27.743 -2.128 1.00 38.56  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.194 -25.414 -2.154 1.00 39.30  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.348 -24.226 -2.898 1.00 44.79  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.950 -28.559 -1.786 1.00 29.94  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.575 -29.556 -0.777 1.00 27.20  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.183 -29.026 0.515  1.00 28.87  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.144 -28.245 0.462  1.00 27.13  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.926 -31.034 -1.087 1.00 30.45  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.440 -31.209 -1.369 1.00 30.73  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.069 -31.548 -2.257 1.00 30.68  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.957 -32.660 -1.527 1.00 34.86  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.697 -29.459 1.680  0.66 23.92  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.582 -29.380 1.649  0.34 24.77  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.237 -28.966 2.953  0.66 23.34  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 20.998 -28.882 2.947  0.34 23.81  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.582 -30.115 3.888  0.66 26.23  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.377 -30.014 3.882  0.34 27.38  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.822 -31.082 3.964  0.66 27.25  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.657 -31.007 3.976  0.34 27.83  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.237 -27.989 3.623  0.66 25.43  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.874 -28.031 3.551  0.34 25.30  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.508 -27.716 5.122  0.66 30.51  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.351 -27.079 4.646  0.34 26.06  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.060 -26.365 5.613  0.66 50.23  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.548 -27.210 5.919  0.34 39.51  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.467 -25.569 4.884  0.66 44.77  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.324 -27.383 5.906  0.34 31.32  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.362 -26.065 6.873  0.66 42.82  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.225 -27.107 7.055  0.34 37.94  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.719 -30.013 4.587  0.66 23.98  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.509 -29.857 4.566  0.34 24.31  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.096 -31.027 5.565  0.66 22.85  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.011 -30.832 5.527  0.34 23.50  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.640 -30.530 6.929  0.66 25.35  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.524 -30.381 6.884  0.34 26.27  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.231 -29.592 7.486  0.66 24.07  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.954 -29.332 7.384  0.34 25.51  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.607 -31.343 5.505  0.66 24.05  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.544 -30.934 5.427  0.34 24.83  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 24.982 -32.543 6.341  0.66 24.72  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.008 -31.705 4.210  0.34 26.68  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.610 -33.828 5.952  0.66 27.23  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.720 -31.255 2.924  0.34 30.19  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.770 -32.401 7.479  0.66 25.35  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.754 -32.868 4.348  0.34 29.71  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 24.954 -34.940 6.734  0.66 28.09  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.149 -31.966 1.801  0.34 31.33  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.085 -33.505 8.275  0.66 27.24  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.192 -33.576 3.219  0.34 33.11  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.689 -34.766 7.893  0.66 25.70  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.883 -33.120 1.956  0.34 31.04  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.549 -31.126 7.438  1.00 23.12  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.887 -30.751 8.704  1.00 23.79  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.846 -30.517 9.888  1.00 26.00  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.730 -29.491 10.572 1.00 25.55  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.806 -31.781 9.064  1.00 30.04  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.907 -31.915 7.939  1.00 30.96  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.006 -31.381 10.326 1.00 34.14  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.783 -31.452 10.107 1.00 23.09  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.692 -31.377 11.258 1.00 23.85  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.936 -30.486 11.048 1.00 24.37  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.760 -30.394 11.969 1.00 23.69  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.139 -32.796 11.671 1.00 28.97  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.029 -33.741 12.180 1.00 40.24  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.453 -33.323 13.523 1.00 61.13  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.427 -33.414 14.616 1.00 73.44  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.309 -32.782 15.780 1.00 84.14  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.235 -32.929 16.717 1.00 73.01  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.271 -31.985 16.011 1.00 65.87  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.082 -29.841 9.874  1.00 20.73  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.311 -29.095 9.585  1.00 21.20  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.607 -27.991 10.603 1.00 24.01  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.744 -27.923 11.106 1.00 23.00  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.296 -28.527 8.152  1.00 21.25  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.555 -27.777 7.851  1.00 22.96  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.732 -28.450 7.635  1.00 23.56  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.774 -26.445 7.719  1.00 23.46  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.646 -27.523 7.388  1.00 22.99  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.120 -26.298 7.418  1.00 22.38  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.616 -27.104 10.876 1.00 21.15  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.845 -25.977 11.821 1.00 21.29  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.269 -26.482 13.219 1.00 22.57  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.190 -25.927 13.816 1.00 20.95  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.603 -25.097 11.912 1.00 22.59  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.608 -27.536 13.714 0.42 22.03  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.610 -27.545 13.714 0.30 21.42  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.605 -27.534 13.732 0.28 21.11  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.907 -28.125 15.016 0.42 21.96  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.904 -28.150 15.015 0.30 21.34  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.933 -28.094 15.046 0.28 20.88  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.316 -28.718 15.038 0.42 25.64  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.307 -28.740 15.044 0.30 25.59  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.319 -28.740 15.057 0.28 25.41  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.045 -28.524 16.018 0.42 23.34  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.021 -28.575 16.040 0.30 23.90  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.038 -28.603 16.051 0.28 23.77  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.868 -29.187 15.367 0.42 26.00  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.877 -29.229 15.344 0.30 24.84  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.861 -29.077 15.505 0.28 24.01  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.115 -29.733 16.651 0.42 29.45  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.576 -28.676 15.414 0.30 27.46  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.782 -30.188 14.629 0.28 25.25  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.708 -29.411 13.946 1.00 23.23  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.035 -30.038 13.816 1.00 23.80  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.109 -28.943 13.782 1.00 23.98  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.150 -29.097 14.418 1.00 23.74  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.101 -30.898 12.547 1.00 25.34  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.311 -32.206 12.622 1.00 35.63  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.775 -32.524 13.715 1.00 33.85  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.222 -32.907 11.586 1.00 38.46  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.840 -27.828 13.069 1.00 19.56  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.794 -26.704 13.025 1.00 19.20  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.016 -26.168 14.453 1.00 23.00  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.152 -25.997 14.894 1.00 21.37  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.329 -25.582 12.053 1.00 21.43  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.100 -24.281 12.285 1.00 21.97  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.413 -26.033 10.585 1.00 21.22  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.924 -25.912 15.167 1.00 20.40  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.018 -25.360 16.521 1.00 21.89  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.745 -26.312 17.484 1.00 22.61  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.605 -25.861 18.264 1.00 20.90  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.632 -24.967 17.031 1.00 22.65  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.642 -24.094 18.306 1.00 26.25  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.228 -22.716 18.029 1.00 26.18  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.232 -23.939 18.854 1.00 28.74  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.454 -27.615 17.377 1.00 21.46  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.133 -28.642 18.166 1.00 22.67  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.644 -28.556 17.911 1.00 24.84  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.429 -28.547 18.872 1.00 24.55  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.604 -30.022 17.773 1.00 24.65  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.177 -31.216 18.536 1.00 33.21  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.804 -31.141 20.024 1.00 36.15  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.609 -32.510 17.974 1.00 37.63  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.051 -28.435 16.629 1.00 21.62  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.476 -28.315 16.308 1.00 20.23  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.099 -27.015 16.811 1.00 23.27  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.238 -27.022 17.274 1.00 22.88  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.710 -28.525 14.827 1.00 22.77  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.679 -29.992 14.469 1.00 32.13  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.897 -30.872 15.318 1.00 30.11  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.400 -30.294 13.205 1.00 26.99  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.361 -25.907 16.734 1.00 21.35  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.859 -24.631 17.262 1.00 21.43  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.076 -24.771 18.773 1.00 23.90  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.061 -24.236 19.311 1.00 23.46  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.878 -23.498 16.953 1.00 21.82  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.771 -23.146 15.460 1.00 23.81  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.665 -22.119 15.230 1.00 25.23  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.139 -22.714 14.862 1.00 26.91  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.158 -25.490 19.463 1.00 21.37  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.317 -25.696 20.921 1.00 21.98  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.553 -26.564 21.218 1.00 26.44  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.258 -26.312 22.200 1.00 26.87  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.067 -26.312 21.544 1.00 23.25  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.071 -26.190 23.059 1.00 30.14  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.577 -25.219 23.628 1.00 28.70  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.511 -27.174 23.724 1.00 32.72  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.831 -27.566 20.354 1.00 23.98  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.023 -28.420 20.493 1.00 25.01  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.286 -27.567 20.339 1.00 28.22  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.242 -27.758 21.085 1.00 28.03  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 37.011 -29.549 19.455 1.00 25.45  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 36.005 -30.646 19.797 1.00 27.83  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.788 -31.572 18.607 1.00 30.68  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 34.946 -32.710 18.968 1.00 39.21  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.304 -33.480 18.097 1.00 53.86  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.354 -33.212 16.796 1.00 40.89  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.587 -34.510 18.521 1.00 47.84  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.279 -26.597 19.394 1.00 24.42  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.432 -25.705 19.237 1.00 25.04  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.575 -24.858 20.492 1.00 28.63  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.697 -24.676 20.992 1.00 29.26  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.259 -24.786 18.032 1.00 24.54  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.237 -25.486 16.655 1.00 28.94  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.138 -24.451 15.534 1.00 28.78  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.484 -26.363 16.459 1.00 29.36  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.433 -24.354 21.024 1.00 24.66  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.490 -23.566 22.253 1.00 25.09  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.114 -24.372 23.424 1.00 30.22  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 39.999 -23.849 24.119 1.00 30.86  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.101 -23.053 22.654 1.00 26.11  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.224 -22.172 23.896 1.00 29.36  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.939 -21.530 24.295 1.00 33.78  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.924 -22.511 24.664 1.00 31.17  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.300 -22.558 25.837 1.00 42.09  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.645 -21.727 26.817 1.00 35.95  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.348 -23.452 26.050 1.00 31.90  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.649 -25.613 23.635 0.39 28.17  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.651 -25.624 23.615 0.28 27.86  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.648 -25.613 23.636 0.33 28.13  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.116 -26.499 24.707 0.39 29.57  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.096 -26.569 24.650 0.28 29.12  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.116 -26.507 24.703 0.33 29.53  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.626 -26.780 24.640 0.39 35.24  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.610 -26.782 24.626 0.28 34.92  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.627 -26.772 24.638 0.33 35.14  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.270 -26.906 25.685 0.39 36.31  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.235 -26.886 25.684 0.28 35.85  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.271 -26.888 25.684 0.33 36.12  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.322 -27.801 24.716 0.39 33.20  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.415 -27.921 24.456 0.28 32.57  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.344 -27.821 24.673 0.33 33.28  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.630 -28.632 23.608 0.39 39.51  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.047 -27.906 24.822 0.28 38.31  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.776 -28.705 25.696 0.33 41.64  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.188 -26.848 23.417 1.00 31.50  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.617 -27.095 23.195 1.00 33.15  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.405 -25.804 22.989 1.00 35.88  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.611 -25.856 22.726 1.00 37.27  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.782 -28.057 22.015 1.00 34.21  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.072 -29.392 22.236 1.00 41.66  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.039 -30.232 20.984 1.00 47.17  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.390 -30.594 20.554 1.00 61.88  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.734 -30.793 19.289 1.00 76.98  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 44.986 -31.099 18.976 1.00 65.34  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.838 -30.660 18.324 1.00 61.98  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.731 -24.649 23.139 1.00 30.28  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.297 -23.310 22.991 1.00 30.95  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.912 -23.081 21.582 1.00 34.96  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 44.965 -22.450 21.441 1.00 36.90  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.312 -23.015 24.127 1.00 34.53  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.626 -21.543 24.288 1.00 44.86  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.704 -20.715 24.096 1.00 44.41  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.793 -21.216 24.599 1.00 50.43  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.259 -23.612 20.553 1.00 28.30  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.749 -23.508 19.179 1.00 28.31  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.154 -22.299 18.472 1.00 30.52  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 41.923 -22.164 18.382 1.00 26.83  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.539 -24.821 18.385 1.00 31.56  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.350 -25.999 19.010 1.00 33.64  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.855 -24.627 16.875 1.00 30.77  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.869 -27.381 18.516 1.00 36.95  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.047 -21.411 17.977 1.00 29.77  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.690 -20.209 17.219 1.00 30.27  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.775 -19.229 17.980 1.00 31.09  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.166 -18.363 17.357 1.00 28.67  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.122 -20.534 15.833 1.00 30.91  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.160 -21.075 14.801 1.00 38.05  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.534 -21.187 13.455 1.00 38.81  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.372 -20.188 14.687 1.00 44.89  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.758 -19.309 19.317 1.00 28.16  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.081 -18.308 20.147 1.00 27.52  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.902 -17.023 19.953 1.00 33.34  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.135 -17.085 19.837 1.00 33.37  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 42.014 -18.752 21.604 1.00 31.57  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.338 -19.073 22.032 1.00 34.15  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.058 -19.957 21.806 1.00 30.39  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.226 -15.889 19.795 1.00 29.93  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.898 -14.638 19.450 1.00 30.01  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.563 -13.483 20.362 1.00 31.32  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.935 -12.342 20.074 1.00 31.89  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.607 -14.280 17.979 1.00 31.41  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.129 -14.270 17.585 1.00 41.99  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.268 -14.416 18.482 1.00 37.49  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.840 -14.114 16.385 1.00 52.30  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.881 -13.764 21.472 1.00 25.52  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.565 -12.720 22.450 1.00 25.13  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.402 -13.322 23.838 1.00 29.20  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 40.991 -14.489 23.979 1.00 28.51  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.290 -11.901 22.015 1.00 27.89  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 38.997 -12.710 22.179 1.00 25.53  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.180 -10.555 22.753 1.00 28.37  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.710 -12.512 24.856 0.60 26.53  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.705 -12.525 24.869 0.40 26.08  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.495 -12.821 26.262 0.60 26.47  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.456 -12.898 26.253 0.40 25.80  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.410 -11.840 26.720 0.60 29.07  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.488 -11.866 26.849 0.40 29.28  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.520 -10.635 26.462 0.60 28.72  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.726 -10.656 26.762 0.40 29.54  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.792 -12.670 27.123 0.60 32.02  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.717 -13.201 27.117 0.40 30.74  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.522 -12.936 28.606 0.60 32.56  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.584 -11.969 27.343 0.40 31.32  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.903 -13.579 26.619 0.60 32.60  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.340 -13.853 28.444 0.40 30.82  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.363 -12.355 27.375 1.00 24.76  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.306 -11.539 27.978 1.00 25.39  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.595 -11.560 29.470 1.00 30.55  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.624 -12.641 30.082 1.00 29.53  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.864 -12.035 27.662 1.00 27.08  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.626 -12.210 26.127 1.00 26.54  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.827 -11.101 28.295 1.00 28.96  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.904 -10.954 25.228 1.00 26.30  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.826 -10.377 30.041 1.00 27.16  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.140 -10.248 31.469 1.00 27.73  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.882 -9.824  32.211 1.00 32.71  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.283 -8.792  31.889 1.00 31.01  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.341 -9.296  31.727 1.00 32.57  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.642 -9.175  33.227 1.00 33.16  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.589 -9.779  30.987 1.00 33.33  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.496 -10.618 33.217 1.00 29.78  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.304 -10.386 34.030 1.00 29.89  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.803 -10.430 35.459 1.00 37.73  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 36.967 -11.513 36.029 1.00 34.32  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.187 -11.425 33.736 1.00 32.79  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.872 -10.991 34.375 1.00 32.67  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 35.011 -11.636 32.229 1.00 31.84  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.165 -9.251  35.998 0.54 38.62  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.036 -9.231  36.026 0.46 37.54  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.760 -9.075  37.329 0.54 40.11  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.569 -8.987  37.367 0.46 38.65  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.114 -9.834  37.394 0.54 41.82  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.663 -10.005 37.725 0.46 41.01  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 40.002 -9.541  36.592 0.54 41.43  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.471 -10.905 38.551 0.46 40.63  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.792 -9.508  38.436 0.54 45.91  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.452 -8.897  38.400 0.46 43.15  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.525 -8.880  38.315 0.54 60.64  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.758 -7.670  38.242 0.46 51.57  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.243 -10.826 38.298 0.54 37.52  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.769 -9.899  36.970 0.46 36.01  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.458 -11.623 38.488 0.54 37.49  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 41.016 -10.669 37.011 0.46 36.28  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.569 -12.807 37.520 0.54 38.81  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.887 -12.085 36.420 0.46 38.31  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.604 -13.481 37.509 0.54 38.32  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.905 -12.606 35.955 0.46 38.67  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.561 -12.123 39.945 0.54 38.12  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.677 -10.681 38.404 0.46 37.28  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 40.984 -11.056 40.945 0.54 45.50  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.193 -9.299  38.805 0.46 48.72  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.337 -11.688 42.276 0.54 46.28  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.174 -9.343  39.956 0.46 55.96  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.557 -10.693 43.323 0.54 47.98  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.617 -8.001  40.342 0.46 63.36  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.733 -10.147 43.619 0.54 61.46  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.029 -7.251  41.270 0.46 75.81  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.831 -9.260  44.599 0.54 50.14  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 41.958 -7.698  41.916 0.46 60.21  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.820 -10.475 42.931 0.54 45.91  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.504 -6.046  41.556 0.46 63.32  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.504 -13.083 36.733 0.54 33.22  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.657 -12.675 36.357 0.46 33.62  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.492 -14.212 35.799 0.54 32.18  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.414 -13.996 35.742 0.46 32.72  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.766 -13.799 34.358 0.54 34.36  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.552 -13.850 34.222 0.46 34.68  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.454 -12.679 33.953 0.54 32.05  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 38.960 -12.940 33.640 0.46 32.36  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.166 -14.999 35.890 0.54 33.29  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.023 -14.547 36.117 0.46 33.97  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.870 -15.563 37.274 0.54 49.26  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.932 -15.069 37.542 0.46 47.15  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.180 -17.038 37.438 0.54 85.88  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.161 -16.561 37.672 0.46 82.63  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.440 -17.872 36.865 0.54 86.35  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.212 -16.953 38.227 0.46 84.66  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.159 -17.362 38.150 0.54 86.47  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.291 -17.340 37.216 0.46 83.16  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.338 -14.735 33.583 1.00 30.95  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.659 -14.604 32.169 1.00 30.41  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.019 -15.730 31.385 1.00 33.00  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.080 -16.880 31.825 1.00 32.92  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.187 -14.635 31.994 1.00 33.20  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.893 -13.411 32.568 1.00 51.70  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.364 -13.322 32.234 1.00 70.25  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.947 -14.166 31.537 1.00 62.75  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 44.997 -12.275 32.734 1.00 72.68  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.413 -15.409 30.220 1.00 27.18  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.754 -16.405 29.358 1.00 27.32  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.271 -16.219 27.953 1.00 31.20  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.134 -15.124 27.399 1.00 31.64  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.230 -16.196 29.363 1.00 28.32  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.611 -16.318 30.732 1.00 30.03  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.510 -15.210 31.573 1.00 32.54  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.122 -17.539 31.183 1.00 32.68  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 35.948 -15.327 32.846 1.00 34.54  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.566 -17.655 32.461 1.00 36.17  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.489 -16.550 33.286 1.00 34.23  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.900 -17.257 27.389 1.00 27.68  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.411 -17.201 26.019 1.00 26.38  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.274 -17.592 25.061 1.00 29.81  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.471 -18.482 25.369 1.00 28.67  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.629 -18.135 25.843 1.00 27.52  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.852 -17.710 26.700 1.00 35.93  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.173 -18.127 26.064 1.00 43.14  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.190 -17.765 24.642 1.00 55.14  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.739 -16.668 24.134 1.00 68.63  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.429 -15.842 24.908 1.00 62.14  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.651 -16.417 22.837 1.00 51.00  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.193 -16.941 23.898 1.00 26.50  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.116 -17.252 22.939 1.00 26.12  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.496 -16.836 21.534 1.00 27.34  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.591 -16.304 21.317 1.00 25.87  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.812 -16.553 23.356 1.00 26.97  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.595 -17.108 20.579 1.00 23.72  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.757 -16.702 19.193 1.00 23.14  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.883 -15.451 19.012 1.00 25.22  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.669 -15.495 19.298 1.00 23.58  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.277 -17.817 18.247 1.00 23.02  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.052 -19.091 18.412 1.00 26.19  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.586 -20.124 19.225 1.00 27.75  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.297 -19.409 17.970 1.00 27.49  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.526 -21.064 19.185 1.00 27.89  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.584 -20.669 18.461 1.00 27.75  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.486 -14.357 18.545 1.00 24.37  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.752 -13.097 18.285 1.00 24.12  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.502 -13.357 17.423 1.00 26.58  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.433 -12.845 17.742 1.00 23.47  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.657 -12.077 17.566 1.00 26.70  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.658 -11.453 18.523 1.00 28.55  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.595 -10.546 17.742 1.00 28.11  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.684 -10.053 18.644 1.00 33.00  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.644 -9.242  17.870 1.00 33.46  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.629 -14.160 16.361 1.00 23.79  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.492 -14.398 15.459 1.00 23.72  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.310 -15.052 16.152 1.00 24.43  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.177 -14.663 15.883 1.00 24.78  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.917 -15.150 14.207 1.00 30.17  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.548 -16.358 14.618 1.00 31.24  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.816 -14.296 13.303 1.00 30.84  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.553 -16.029 17.031 1.00 21.22  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.469 -16.713 17.749 1.00 21.04  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.805 -15.719 18.705 1.00 23.92  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.574 -15.667 18.770 1.00 22.44  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 32.990 -17.964 18.496 1.00 22.83  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.871 -18.590 19.344 1.00 23.13  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.532 -18.991 17.488 1.00 22.79  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.616 -14.928 19.439 1.00 22.62  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.046 -13.913 20.338 1.00 22.01  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.150 -12.916 19.579 1.00 24.30  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.031 -12.631 20.023 1.00 24.37  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.157 -13.152 21.079 1.00 21.30  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.117 -13.961 21.978 1.00 24.48  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.205 -13.030 22.569 1.00 24.29  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.350 -14.691 23.081 1.00 26.21  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.605 -12.446 18.412 1.00 21.16  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.826 -11.516 17.579 1.00 22.85  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.539 -12.159 17.081 1.00 26.54  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.486 -11.513 17.075 1.00 26.66  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.639 -11.068 16.374 1.00 24.93  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.838 -10.247 16.760 1.00 27.47  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.891 -10.149 15.313 1.00 31.60  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.099 -8.830  14.485 1.00 27.92  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.609 -13.450 16.699 1.00 23.21  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.445 -14.185 16.184 1.00 22.83  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.364 -14.384 17.270 1.00 26.44  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.205 -14.599 16.927 1.00 26.75  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.885 -15.547 15.618 1.00 23.09  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.748 -14.333 18.564 1.00 22.72  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.834 -14.582 19.677 1.00 23.15  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.366 -13.359 20.463 1.00 26.40  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.419 -13.500 21.237 1.00 25.71  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.481 -15.578 20.633 1.00 23.04  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.836 -17.183 19.891 1.00 25.59  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.123 -12.247 20.411 1.00 22.84  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.911 -11.112 21.304 1.00 22.66  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.916 -9.808  20.554 1.00 25.92  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.892 -9.514  19.845 1.00 23.81  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.031 -11.135 22.344 1.00 23.87  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.343 -9.890  22.944 1.00 27.09  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.868 -9.000  20.758 1.00 24.68  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.800 -7.665  20.169 1.00 24.55  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.923 -6.778  20.673 1.00 27.73  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.487 -5.980  19.906 1.00 26.89  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.322 -6.969  21.952 1.00 25.41  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.437 -6.189  22.514 1.00 25.56  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.777 -6.529  21.813 1.00 27.88  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.465 -5.611  21.345 1.00 25.72  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.543 -6.401  24.041 1.00 25.57  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.616 -5.520  24.717 1.00 30.87  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.204 -4.033  24.717 1.00 32.11  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.899 -5.995  26.126 1.00 30.14  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.117 -7.828  21.698 1.00 23.84  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.373 -8.216  21.023 1.00 23.23  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.347 -7.866  19.556 1.00 26.61  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.375 -7.464  19.028 1.00 25.26  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.734 -9.686  21.258 1.00 24.31  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.165 -9.905  22.696 1.00 25.19  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.240 -9.197  23.238 1.00 27.24  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.529 -10.854 23.491 1.00 26.56  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.623 -9.381  24.583 1.00 27.70  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.941 -11.071 24.819 1.00 28.67  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 32.975 -10.327 25.358 1.00 26.66  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.166 -7.939  18.912 1.00 24.35  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.044 -7.543  17.496 1.00 24.72  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.464 -6.069  17.331 1.00 29.20  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.241 -5.746  16.426 1.00 27.20  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.595 -7.758  17.036 1.00 26.68  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.334 -7.241  15.646 1.00 30.27  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 28.960 -7.809  14.541 1.00 31.72  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.465 -6.175  15.434 1.00 34.42  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.715 -7.335  13.249 1.00 33.98  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.212 -5.696  14.153 1.00 37.80  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.830 -6.287  13.065 1.00 44.04  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.563 -5.808  11.817 1.00 49.43  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.948 -5.189  18.205 0.53 26.87  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.946 -5.191  18.207 0.47 26.93  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.263 -3.759  18.205 0.53 28.03  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.265 -3.764  18.210 0.47 28.11  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.750 -3.512  18.517 0.53 33.11  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.761 -3.548  18.483 0.47 32.93  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.377 -2.686  17.860 0.53 34.72  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.400 -2.779  17.768 0.47 34.27  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.365 -3.025  19.197 0.53 30.63  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.427 -3.039  19.260 0.47 31.08  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 28.027 -3.001  18.726 0.53 35.13  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.760 -1.661  19.296 0.47 37.93  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.314 -4.247  19.494 1.00 28.99  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.729 -4.126  19.894 1.00 28.48  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.674 -4.517  18.753 1.00 31.00  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.564 -3.740  18.403 1.00 32.54  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.061 -4.953  21.192 1.00 30.10  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.320 -4.407  22.441 1.00 29.67  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.584 -5.015  21.449 1.00 29.39  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.391 -5.396  23.658 1.00 31.98  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.487 -5.712  18.178 1.00 26.53  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.461 -6.150  17.199 1.00 26.46  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.238 -5.603  15.786 1.00 30.87  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.081 -5.856  14.919 1.00 31.46  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.604 -7.677  17.229 1.00 27.02  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.030 -8.162  18.603 1.00 27.84  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.241 -7.755  19.161 1.00 31.53  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.234 -9.044  19.324 1.00 28.79  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.631 -8.203  20.430 1.00 32.25  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.640 -9.518  20.575 1.00 31.16  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.828 -9.089  21.125 1.00 29.93  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.170 -4.810  15.556 1.00 28.75  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 34.010 -4.123  14.260 1.00 29.15  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.561 -2.701  14.384 1.00 35.92  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.669 -1.987  13.381 1.00 35.64  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.586 -4.158  13.701 1.00 37.25  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.678 -3.658  14.677 1.00 34.60  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.169 -5.545  13.205 1.00 33.07  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 34.951 -2.294  15.612 1.00 32.36  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.567 -0.982  15.811 1.00 34.07  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 37.003 -1.060  15.273 1.00 39.52  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.740 -1.969  15.649 1.00 36.78  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.547 -0.581  17.297 1.00 35.83  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.309 0.700   17.532 1.00 48.46  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.717 1.779   17.346 1.00 53.11  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.520 0.623   17.833 1.00 49.73  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.400 -0.090  14.423 1.00 41.15  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.710 -0.045  13.762 1.00 42.55  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.912 -0.070  14.718 1.00 46.32  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 40.979 -0.527  14.306 1.00 48.83  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.808 1.139   12.787 1.00 46.27  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.962 0.951   11.529 1.00 62.18  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.763 0.419   15.968 1.00 38.67  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.848 0.345   16.944 1.00 37.91  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.755 -0.914  17.791 1.00 41.76  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.776 -1.544  18.054 1.00 43.66  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.848 1.560   17.900 1.00 38.88  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.447 2.853   17.385 1.00 45.90  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.298 3.948   18.418 1.00 47.06  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 42.929 2.696   17.024 1.00 50.64  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.550 -1.242  18.292 1.00 34.76  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.390 -2.362  19.222 1.00 33.45  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.528 -3.724  18.554 1.00 38.40  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.914 -4.676  19.228 1.00 37.69  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.076 -2.262  20.026 1.00 33.92  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 37.977 -1.011  20.908 1.00 35.07  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.696 -1.047  21.734 1.00 34.55  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.399 0.284   22.388 1.00 39.14  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.800 1.265   21.454 1.00 42.06  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.279 -3.806  17.227 1.00 37.58  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.404 -5.059  16.458 1.00 38.12  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.798 -5.684  16.611 1.00 42.51  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 40.935 -6.899  16.450 1.00 43.00  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.049 -4.845  14.985 1.00 40.15  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.180 -3.741  14.080 1.00 46.64  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.823 -4.842  16.903 1.00 38.37  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.228 -5.226  17.028 1.00 39.31  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.703 -5.525  18.449 1.00 42.00  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.865 -5.906  18.640 1.00 41.46  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.125 -4.166  16.369 1.00 42.00  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 43.902 -4.087  14.868 1.00 57.80  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.812 -3.004  14.292 1.00 56.01  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.756 -5.232  14.204 1.00 47.26  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.827 -5.354  19.444 1.00 37.97  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.210 -5.624  20.821 1.00 37.29  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.212 -7.125  21.093 1.00 39.66  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.328 -7.842  20.598 1.00 38.13  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.260 -4.913  21.806 1.00 37.45  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.223 -3.378  21.724 1.00 42.65  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.151 -2.832  22.645 1.00 42.56  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.586 -2.753  22.069 1.00 45.13  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.198 -7.600  21.870 0.51 36.87  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.200 -7.589  21.875 0.49 36.70  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.300 -9.015  22.243 0.51 36.40  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.349 -8.994  22.268 0.49 36.20  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.680 -9.251  23.632 0.51 37.24  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.700 -9.243  23.637 0.49 37.18  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.487 -10.398 24.035 0.51 34.96  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.510 -10.393 24.031 0.49 34.90  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.753 -9.483  22.205 0.51 41.54  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.825 -9.378  22.311 0.49 41.04  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.553 -8.779  23.139 0.51 50.73  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.380 -9.395  21.006 0.49 48.79  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.392 -8.155  24.369 1.00 33.97  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.782 -8.187  25.704 1.00 33.57  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.595 -7.213  25.739 1.00 34.47  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.735 -6.045  25.342 1.00 33.76  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.803 -7.851  26.836 1.00 39.28  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.147 -7.927  28.220 1.00 39.50  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 45.041 -8.754  26.778 1.00 39.99  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.447 -7.692  26.247 1.00 27.38  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.240 -6.889  26.441 1.00 27.28  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.847 -7.010  27.906 1.00 30.95  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.598 -8.127  28.388 1.00 30.87  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.075 -7.276  25.478 1.00 28.89  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.456 -7.099  23.963 1.00 29.73  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.756 -6.549  25.825 1.00 29.96  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.801 -5.632  23.478 1.00 33.41  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.735 -5.864  28.599 1.00 28.59  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.333 -5.825  29.995 1.00 28.41  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.856 -5.501  30.109 1.00 30.65  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.426 -4.435  29.665 1.00 29.37  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.148 -4.780  30.778 1.00 32.52  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.627 -4.978  30.709 1.00 50.79  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.151 -6.014  31.098 1.00 42.49  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.333 -3.974  30.234 1.00 45.56  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.084 -6.395  30.726 1.00 26.44  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.658 -6.159  30.912 1.00 26.35  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.417 -5.268  32.129 1.00 30.33  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.290 -5.134  33.002 1.00 30.27  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.858 -7.476  31.056 1.00 25.69  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.907 -8.495  29.884 1.00 29.13  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.777 -9.529  30.034 1.00 29.70  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.845 -7.808  28.510 1.00 27.54  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.220 -4.681  32.197 1.00 27.19  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.792 -3.812  33.301 1.00 28.01  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 32.991 -4.561  34.639 1.00 32.76  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.674 -5.751  34.700 1.00 31.73  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.318 -3.434  33.094 1.00 29.50  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.764 -2.425  34.085 1.00 40.86  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.615 -2.777  35.277 1.00 43.08  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.441 -1.302  33.663 1.00 42.98  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.547 -3.917  35.689 1.00 33.79  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.786 -4.647  36.959 1.00 34.56  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.554 -5.236  37.632 1.00 37.73  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.704 -6.103  38.488 1.00 38.54  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.477 -3.616  37.864 1.00 37.72  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.203 -2.285  37.243 1.00 42.45  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.022 -2.515  35.769 1.00 36.28  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.346 -4.788  37.259 1.00 34.83  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.102 -5.313  37.828 1.00 36.37  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.814 -6.728  37.277 1.00 36.32  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 28.978 -7.435  37.832 1.00 35.19  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.922 -4.379  37.485 1.00 39.05  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.776 -4.405  38.484 1.00 59.88  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 27.980 -3.539  39.713 1.00 89.58  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.059 -2.298  39.561 1.00 89.69  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.054 -4.101  40.830 1.00 83.62  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.473 -7.123  36.174 1.00 30.34  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.220 -8.433  35.561 1.00 29.35  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.801 -9.563  36.383 1.00 33.41  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 31.974 -9.551  36.755 1.00 31.91  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.677 -8.461  34.079 1.00 31.54  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 29.956 -7.349  33.265 1.00 32.65  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.463 -9.848  33.461 1.00 28.27  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.359 -7.360  33.321 1.00 38.90  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 29.957 -10.538 36.653 1.00 34.16  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.280 -11.723 37.426 1.00 34.49  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.032 -12.758 36.561 1.00 34.18  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.506 -13.166 35.524 1.00 31.54  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 28.982 -12.301 37.995 1.00 35.79  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.207 -13.557 38.774 1.00 51.75  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.936 -14.642 38.283 1.00 41.09  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.740 -13.438 39.988 1.00 42.94  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.243 -13.217 36.976 1.00 32.01  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 32.982 -14.208 36.163 1.00 31.08  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.231 -15.520 35.905 1.00 33.95  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.343 -16.069 34.808 1.00 31.90  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.265 -14.441 36.967 1.00 34.78  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.407 -13.223 37.839 1.00 39.63  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 33.005 -12.841 38.186 1.00 35.48  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.456 -16.013 36.898 1.00 31.39  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.690 -17.246 36.701 1.00 31.54  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.594 -17.051 35.633 1.00 32.72  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.444 -17.908 34.773 1.00 30.41  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.107 -17.783 38.016 1.00 34.35  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.542 -19.184 37.813 1.00 43.04  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.710 -19.791 38.929 1.00 69.17  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.729 -21.036 39.054 1.00 70.47  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.027 -19.039 39.661 1.00 60.53  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.867 -15.925 35.696 1.00 30.01  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.851 -15.589 34.706 1.00 28.96  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.476 -15.532 33.321 1.00 29.88  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.930 -16.079 32.350 1.00 28.30  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.664 -14.906 33.228 1.00 26.20  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.355 -14.842 31.934 1.00 24.53  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.743 -16.259 31.462 1.00 27.01  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.538 -16.603 30.294 1.00 25.39  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.600 -13.915 31.993 1.00 26.30  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.225 -13.802 30.616 1.00 26.73  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.650 -12.991 29.636 1.00 29.98  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.284 -14.625 30.246 1.00 27.36  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.165 -12.960 28.336 1.00 30.68  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.806 -14.584 28.950 1.00 28.76  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.227 -13.771 27.995 1.00 27.92  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.314 -17.065 32.360 1.00 27.63  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.711 -18.436 32.030 1.00 29.61  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.528 -19.264 31.456 1.00 29.98  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.682 -19.955 30.434 1.00 27.88  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.330 -19.115 33.247 1.00 33.57  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.020 -20.748 32.880 1.00 39.37  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.345 -19.168 32.108 1.00 27.23  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.123 -19.873 31.701 1.00 25.39  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.726 -19.422 30.295 1.00 25.82  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.378 -20.249 29.439 1.00 24.81  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 26.994 -19.636 32.749 1.00 28.43  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.285 -20.445 34.059 1.00 30.06  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.596 -19.966 32.172 1.00 28.23  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.566 -19.929 35.276 1.00 35.41  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.799 -18.120 30.056 1.00 22.42  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.450 -17.584 28.731 1.00 22.32  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.466 -17.936 27.662 1.00 25.91  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.079 -18.196 26.523 1.00 24.32  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.178 -16.092 28.799 1.00 23.13  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.886 -15.735 29.573 1.00 28.53  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.802 -14.268 29.756 1.00 29.43  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.618 -16.228 28.839 1.00 29.81  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.768 -17.939 28.008 1.00 22.90  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.804 -18.345 27.051 1.00 22.52  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.568 -19.815 26.637 1.00 25.28  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.594 -20.157 25.451 1.00 23.37  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.192 -18.136 27.668 1.00 22.58  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.355 -18.435 26.694 1.00 26.98  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.297 -17.520 25.454 1.00 26.87  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.727 -18.309 27.416 1.00 28.33  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.295 -20.681 27.620 1.00 23.95  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 29.949 -22.069 27.332 1.00 23.91  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.734 -22.158 26.409 1.00 26.08  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.757 -22.942 25.470 1.00 25.40  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.662 -22.808 28.639 1.00 26.94  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.909 -23.166 29.430 1.00 42.04  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.027 -23.093 28.854 1.00 43.21  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.770 -23.528 30.621 1.00 42.32  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.666 -21.386 26.686 1.00 23.69  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.478 -21.338 25.819 1.00 21.70  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.860 -20.946 24.374 1.00 22.30  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.391 -21.570 23.403 1.00 20.88  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.415 -20.371 26.384 1.00 22.32  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.315 -20.084 25.386 1.00 22.80  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.344 -21.043 25.101 1.00 25.27  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.312 -18.899 24.648 1.00 25.40  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.362 -20.801 24.138 1.00 25.25  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.324 -18.662 23.677 1.00 28.11  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.357 -19.609 23.433 1.00 25.86  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.682 -19.903 24.219 1.00 20.16  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.080 -19.481 22.857 1.00 19.58  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.644 -20.625 22.039 1.00 22.99  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.324 -20.733 20.854 1.00 22.55  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.167 -18.395 22.951 1.00 20.47  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.658 -17.110 23.555 1.00 22.33  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 29.998 -15.865 23.469 1.00 26.41  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.293 -14.581 24.545 1.00 27.26  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.498 -21.459 22.664 1.00 19.94  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.193 -22.554 21.979 1.00 20.06  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.449 -23.867 21.962 1.00 24.91  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.923 -24.825 21.344 1.00 24.03  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.571 -22.778 22.618 1.00 21.98  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.623 -21.800 22.139 1.00 23.49  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.764 -20.545 22.736 1.00 25.21  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.468 -22.118 21.072 1.00 24.48  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.736 -19.637 22.295 1.00 25.77  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.482 -21.245 20.664 1.00 25.58  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.582 -19.991 21.247 1.00 28.00  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.611 -19.169 20.858 1.00 25.80  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.305 -23.946 22.659 1.00 21.40  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.613 -25.242 22.733 1.00 22.19  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.101 -25.234 22.502 1.00 24.82  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.544 -26.320 22.295 1.00 24.37  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.810 -25.916 24.128 1.00 25.56  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.127 -25.168 25.141 1.00 25.79  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.274 -26.152 24.519 1.00 26.62  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.442 -24.060 22.588 0.67 21.02  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.447 -24.057 22.618 0.33 21.07  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 23.968 -23.866 22.541 0.67 21.12  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 23.986 -23.840 22.554 0.33 21.16  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.309 -24.273 23.881 0.67 23.94  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.285 -24.338 23.843 0.33 25.25  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.116 -24.064 24.044 0.67 23.37  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.059 -24.306 23.922 0.33 25.43  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.299 -24.642 21.398 0.67 22.41  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.365 -24.466 21.301 0.33 23.18  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.953 -24.511 20.150 0.67 20.83  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.046 -25.837 21.476 0.33 26.87  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.095 -24.793 24.856 0.67 22.20  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.078 -24.755 24.860 0.33 22.71  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.555 -25.229 26.148 0.67 22.62  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.593 -25.278 26.140 0.33 23.31  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.787 -24.190 27.207 0.67 26.93  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.807 -24.242 27.237 0.33 27.24  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.914 -23.715 27.387 0.67 24.44  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.939 -23.793 27.447 0.33 25.66  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.148 -26.574 26.594 0.67 24.87  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.297 -26.608 26.498 0.33 24.90  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.836 -27.731 25.639 0.67 29.42  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.182 -27.698 25.421 0.33 31.78  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.833 -28.868 25.838 0.67 39.71  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.081 -28.696 25.717 0.33 35.91  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.774 -29.400 27.202 0.67 50.64  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.940 -29.711 24.667 0.33 37.99  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 23.977 -30.392 27.581 0.67 61.29  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.236 -30.999 24.817 0.33 50.05  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.183 -30.987 26.700 0.67 48.93  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.060 -31.847 23.812 0.33 39.93  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 23.974 -30.804 28.840 0.67 45.99  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.688 -31.454 25.977 0.33 33.54  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.721 -23.858 27.927 1.00 24.27  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.768 -22.851 28.986 1.00 23.73  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.553 -23.490 30.341 1.00 28.85  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.486 -24.079 30.581 1.00 27.95  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.705 -21.776 28.714 1.00 24.56  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.739 -20.554 29.660 1.00 27.88  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 22.995 -19.699 29.398 1.00 26.29  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.488 -19.706 29.490 1.00 30.01  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.551 -23.369 31.235 1.00 28.54  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.462 -23.933 32.594 1.00 30.07  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.761 -22.928 33.530 1.00 34.81  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.406 -22.242 34.327 1.00 34.51  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.855 -24.347 33.113 1.00 34.22  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.831 -24.969 34.500 1.00 52.12  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.829 -25.530 34.937 1.00 41.78  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.932 -24.868 35.229 1.00 45.85  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.452 -22.796 33.362 1.00 32.11  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.632 -21.851 34.120 1.00 33.31  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.102 -22.514 35.386 1.00 37.41  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.444 -23.564 35.320 1.00 36.65  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.504 -21.359 33.204 1.00 34.19  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.776 -20.088 33.550 1.00 40.39  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.758 -18.892 33.643 1.00 40.82  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.682 -19.823 32.513 1.00 40.24  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.460 -21.934 36.555 1.00 34.86  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.095 -22.455 37.878 1.00 37.11  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.566 -21.328 38.761 1.00 38.23  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.912 -20.158 38.542 1.00 35.46  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.310 -23.126 38.556 1.00 39.63  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.943 -24.274 37.756 1.00 45.26  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.190 -24.852 38.416 1.00 62.16  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.911 -25.468 39.719 1.00 81.39  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.496 -26.721 39.897 1.00 102.61 ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.261 -27.181 41.120 1.00 90.56  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.301 -27.519 38.853 1.00 93.20  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.730 -21.660 39.757 1.00 37.09  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.184 -20.651 40.679 1.00 37.59  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.299 -19.757 41.262 1.00 42.11  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.129 -18.538 41.353 1.00 42.39  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.380 -21.327 41.817 1.00 40.91  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.720 -20.352 42.777 1.00 53.23  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.009 -20.987 43.960 1.00 84.94  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.576 -21.915 44.584 1.00 78.48  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.882 -20.541 44.273 1.00 86.55  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.431 -20.369 41.607 1.00 39.76  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.569 -19.669 42.195 1.00 40.52  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.365 -18.779 41.255 1.00 41.30  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.119 -17.919 41.716 1.00 41.49  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.208 -18.954 39.932 1.00 36.07  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 22.987 -18.144 38.992 1.00 33.59  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.140 -17.292 38.035 1.00 36.17  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.716 -16.511 37.268 1.00 34.19  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 23.972 -19.045 38.213 1.00 33.05  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.326 -19.984 37.213 1.00 41.85  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.255 -19.707 36.669 1.00 31.93  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 23.979 -21.103 36.923 1.00 35.41  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.798 -17.487 38.018 1.00 33.73  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.922 -16.828 37.027 1.00 33.27  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.049 -15.298 37.009 1.00 34.35  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.078 -14.711 35.918 1.00 31.60  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.442 -17.272 37.107 1.00 37.60  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.632 -16.714 35.900 1.00 38.00  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.798 -16.957 38.469 1.00 37.56  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.446 -17.527 35.482 1.00 41.88  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.147 -14.661 38.180 1.00 33.24  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.283 -13.202 38.218 1.00 34.36  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.586 -12.723 37.569 1.00 36.01  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.553 -11.778 36.772 1.00 34.38  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.118 -12.649 39.649 1.00 38.74  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.745 -12.941 40.268 1.00 45.71  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.317 -12.580 39.201 1.00 51.83  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.267 -10.789 39.307 1.00 49.80  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.727 -13.387 37.886 1.00 33.55  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.038 -13.037 37.307 1.00 32.73  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.050 -13.322 35.808 1.00 33.65  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.562 -12.512 35.033 1.00 31.64  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.158 -13.817 37.990 1.00 34.05  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.485 -14.474 35.394 1.00 28.50  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.419 -14.837 33.969 1.00 26.42  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.606 -13.802 33.190 1.00 29.59  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.082 -13.345 32.144 1.00 28.10  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.895 -16.290 33.772 1.00 29.54  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.591 -16.589 32.296 1.00 27.46  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.903 -17.294 34.317 1.00 29.91  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.403 -13.432 33.684 0.20 28.29  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.405 -13.427 33.686 0.80 28.65  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.546 -12.446 33.018 0.20 29.07  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.576 -12.443 32.982 0.80 29.91  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.250 -11.098 32.884 0.20 32.86  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.278 -11.093 32.873 0.80 32.67  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.231 -10.513 31.800 0.20 31.84  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.268 -10.491 31.800 0.80 30.88  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.209 -12.275 33.747 0.20 32.86  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.208 -12.268 33.640 0.80 33.71  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.239 -11.399 32.989 0.20 37.25  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.291 -11.349 32.843 0.80 38.15  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.738 -11.074 33.915 0.20 43.28  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.599 -11.356 33.462 0.80 44.03  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.178 -9.641  33.079 0.20 40.69  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.771 -10.338 35.017 0.80 42.23  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.877 -10.619 33.977 1.00 30.22  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.612 -9.336  33.991 1.00 30.85  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.780 -9.370  32.984 1.00 31.90  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 23.978 -8.408  32.222 1.00 30.19  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.122 -9.039  35.392 1.00 32.35  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.509 -10.508 32.934 1.00 27.32  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.622 -10.659 31.990 1.00 26.73  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.091 -10.691 30.540 1.00 28.91  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.667 -10.030 29.675 1.00 26.45  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.542 -11.846 32.356 1.00 30.68  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.840 -11.826 33.759 1.00 29.91  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.857 -11.836 31.558 1.00 30.77  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 23.991 -11.449 30.276 1.00 26.00  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.403 -11.531 28.926 1.00 24.83  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.870 -10.158 28.466 1.00 28.82  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.018 -9.806  27.295 1.00 28.09  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.304 -12.596 28.883 1.00 25.88  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.331 -9.342  29.396 1.00 26.39  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.873 -8.000  29.003 1.00 26.35  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.071 -7.128  28.569 1.00 28.56  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.037 -6.475  27.525 1.00 28.47  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.102 -7.343  30.164 1.00 29.60  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.717 -7.945  30.371 1.00 34.65  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 18.979 -7.371  31.928 1.00 42.74  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.726 -5.622  31.525 1.00 40.84  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.142 -7.161  29.354 1.00 27.09  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.381 -6.423  29.080 1.00 26.27  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 25.996 -6.885  27.736 1.00 29.12  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.401 -6.053  26.919 1.00 28.24  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.353 -6.700  30.221 1.00 27.05  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.760 -6.191  29.999 1.00 27.47  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.055 -4.829  30.084 1.00 30.86  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.809 -7.076  29.743 1.00 27.15  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.361 -4.359  29.892 1.00 29.55  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.115 -6.623  29.586 1.00 27.47  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.383 -5.264  29.658 1.00 30.60  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.680 -4.860  29.546 1.00 28.83  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.053 -8.206  27.518 1.00 25.34  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.613 -8.802  26.302 1.00 23.97  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.699 -8.674  25.086 1.00 27.52  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.126 -8.955  23.958 1.00 26.83  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.018 -10.271 26.539 1.00 22.69  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.166 -10.548 27.541 1.00 25.57  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.438 -12.080 27.635 1.00 26.19  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.471 -9.816  27.131 1.00 28.70  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.427 -8.294  25.310 1.00 25.17  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.422 -8.160  24.248 1.00 25.78  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.177 -9.517  23.571 1.00 28.92  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.438 -9.702  22.382 1.00 27.64  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.786 -7.056  23.241 1.00 27.06  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 23.965 -5.683  23.897 1.00 28.26  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.651 -4.718  22.959 1.00 39.31  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.544 -4.826  21.744 1.00 33.54  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.389 -3.772  23.499 1.00 37.66  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.729 -10.476 24.380 1.00 26.33  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.398 -11.845 23.960 1.00 26.17  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.898 -12.005 24.223 1.00 31.67  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.463 -12.495 25.280 1.00 29.28  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.263 -12.834 24.748 1.00 27.32  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.749 -12.682 24.425 1.00 28.41  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.766 -13.743 25.455 1.00 30.71  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.428 -15.398 24.642 1.00 27.49  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.104 -11.473 23.281 1.00 31.21  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.638 -11.351 23.393 1.00 33.37  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.883 -12.633 23.735 1.00 34.09  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 16.986 -12.573 24.566 1.00 32.74  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.031 -10.722 22.127 1.00 36.33  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.579 -9.331  21.841 1.00 48.57  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.222 -13.773 23.111 1.00 30.74  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.495 -15.021 23.397 1.00 32.29  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.722 -15.503 24.827 1.00 33.48  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.774 -15.970 25.476 1.00 34.13  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.834 -16.102 22.366 1.00 34.08  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.390 -15.745 20.985 1.00 39.10  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.060 -15.489 20.703 1.00 42.79  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.110 -15.634 19.845 1.00 40.91  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 16.015 -15.207 19.410 1.00 42.71  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.221 -15.295 18.850 1.00 41.89  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 18.961 -15.329 25.336 1.00 27.22  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.298 -15.689 26.718 1.00 27.16  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.516 -14.787 27.688 1.00 33.01  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.912 -15.292 28.644 1.00 30.90  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.822 -15.694 27.011 1.00 29.96  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.088 -15.943 28.499 1.00 30.09  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.547 -16.726 26.147 1.00 29.29  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.516 -13.457 27.436 1.00 29.88  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.760 -12.498 28.265 1.00 30.50  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.275 -12.925 28.334 1.00 36.32  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.732 -13.014 29.430 1.00 35.45  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.941 -11.027 27.790 1.00 33.09  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.106 -10.056 28.647 1.00 33.81  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.410 -10.621 27.828 1.00 31.78  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.676 -13.268 27.178 0.61 34.93  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.642 -13.175 27.167 0.39 34.64  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.290 -13.726 27.060 0.61 36.45  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.236 -13.585 27.038 0.39 36.16  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 13.982 -14.957 27.927 0.61 38.99  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.876 -14.797 27.901 0.39 39.76  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 12.996 -14.924 28.664 0.61 39.71  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.861 -14.763 28.596 0.39 40.87  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.925 -13.984 25.586 0.61 38.90  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.884 -13.868 25.563 0.39 38.34  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.478 -14.383 25.363 0.61 54.34  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.660 -12.648 24.685 0.39 51.03  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.580 -13.588 25.721 0.61 58.06  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.261 -11.592 25.223 0.39 54.02  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.244 -15.483 24.824 0.61 60.13  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.857 -12.758 23.455 0.39 57.00  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.811 -16.031 27.858 0.61 33.64  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.709 -15.855 27.864 0.39 34.68  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.536 -17.228 28.676 0.61 33.82  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.463 -17.088 28.621 0.39 34.79  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.723 -16.950 30.171 0.61 36.91  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.657 -16.865 30.128 0.39 37.67  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.007 -17.533 30.982 0.61 37.06  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.868 -17.393 30.912 0.39 38.14  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.294 -18.482 28.206 0.61 34.82  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.272 -18.256 28.051 0.39 39.38  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.684 -19.616 28.827 0.61 35.44  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.249 -18.175 26.624 0.39 38.11  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.789 -18.455 28.545 0.61 29.89  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.710 -19.601 28.469 0.39 38.83  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.679 -16.070 30.528 1.00 33.25  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.922 -15.705 31.944 1.00 33.88  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.704 -15.002 32.493 1.00 39.72  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.240 -15.367 33.583 1.00 37.97  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.161 -14.828 32.076 1.00 33.46  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.714 -15.726 31.883 1.00 35.93  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.165 -14.020 31.728 0.48 37.58  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.170 -14.007 31.745 0.52 37.99  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.961 -13.254 32.076 0.48 39.09  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 12.970 -13.261 32.132 0.52 39.68  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.772 -14.187 32.341 0.48 43.36  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.766 -14.192 32.353 0.52 43.57  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.062 -14.013 33.333 0.48 43.34  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.042 -14.026 33.337 0.52 43.46  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.602 -12.262 30.957 0.48 39.70  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.638 -12.177 31.100 0.52 41.27  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.557 -11.087 30.836 0.48 51.50  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.406 -10.877 31.318 0.52 56.01  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.955 -9.940  30.044 0.48 63.62  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.692 -9.689  30.691 0.52 67.39  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.964 -8.936  29.700 0.48 66.99  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.825 -9.674  29.231 0.52 72.40  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.305 -7.907  30.470 0.48 75.71  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.607 -8.839  28.554 0.52 81.97  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.712 -7.722  31.644 0.48 66.44  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.329 -7.926  29.194 0.52 66.15  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.239 -7.056  30.073 0.48 55.18  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.667 -8.904  27.231 0.52 66.47  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.586 -15.190 31.463 1.00 39.83  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.499 -16.178 31.552 1.00 41.97  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.654 -17.091 32.761 1.00 45.18  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.670  -17.313 33.468 1.00 45.15  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.368 -16.980 30.252 1.00 44.33  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.815  -16.135 29.111 1.00 64.92  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.699  -16.892 27.806 1.00 76.70  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.270  -15.961 26.698 1.00 89.78  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.441  -16.656 25.681 1.00 102.55 ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.891 -17.572 33.031 1.00 39.91  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.172 -18.433 34.189 1.00 40.26  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 11.977 -17.668 35.493 1.00 45.14  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.435 -18.233 36.448 1.00 44.63  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.577 -19.043 34.107 1.00 40.30  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.708 -20.327 33.308 1.00 41.80  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.175 -20.431 32.025 1.00 44.94  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.423 -21.409 33.813 1.00 44.70  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.313 -21.612 31.283 1.00 45.79  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.570 -22.587 33.063 1.00 46.45  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 14.008 -22.681 31.809 1.00 43.96  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.372 -16.374 35.525 1.00 41.11  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.164 -15.522 36.712 1.00 42.38  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.663 -15.273 36.951 1.00 50.16  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.203 -15.416 38.090 1.00 50.69  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.013 -14.223 36.648 1.00 44.55  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.508 -14.578 36.781 1.00 43.17  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.589 -13.199 37.746 1.00 47.15  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.470 -13.574 36.204 1.00 48.81  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.900  -14.958 35.875 1.00 48.24  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.456  -14.709 35.956 1.00 50.92  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.700  -15.943 36.484 1.00 55.50  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.746  -15.785 37.238 1.00 55.99  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.892  -14.259 34.601 1.00 54.26  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.161  -17.161 36.133 1.00 50.52  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.538  -18.404 36.603 1.00 51.98  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.705  -18.634 38.119 1.00 58.49  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.819  -19.210 38.738 1.00 59.30  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.094  -19.593 35.829 1.00 51.06  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.834  -18.200 38.704 1.00 57.14  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.143  -18.404 40.123 1.00 60.00  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.541  -17.359 41.081 1.00 68.57  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.529  -17.603 42.293 1.00 71.09  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.652 -18.509 40.330 1.00 63.67  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 11.096 -19.847 40.161 1.00 74.16  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.022  -16.223 40.559 1.00 65.22  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.431  -15.162 41.390 1.00 85.58  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 6.000  -15.476 41.857 1.00 128.63 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.627  -16.636 42.024 1.00 95.55  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.508  -13.790 40.691 1.00 86.15  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.489  -13.573 39.580 1.00 96.31  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.651  -12.329 38.724 1.00 117.51 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.784  -11.801 38.624 1.00 110.26 ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.637  -11.892 38.133 1.00 111.17 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.217 -35.072 5.834  1.00 30.01  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.294 -33.934 6.323  1.00 31.56  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.411 -36.308 6.710  1.00 29.94  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.943 -35.304 4.553  0.66 28.34  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.962 -35.302 4.545  0.34 29.10  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.735 -34.246 3.569  0.66 27.23  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.692 -34.223 3.594  0.34 28.55  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.223 -34.094 3.289  0.66 31.56  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.183 -34.070 3.428  0.34 31.14  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.508 -35.102 3.229  0.66 31.82  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.440 -35.053 3.533  0.34 30.56  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.516 -34.586 2.279  0.66 26.31  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.363 -34.461 2.217  0.34 27.92  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.015 -34.569 2.465  0.66 26.52  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.742 -35.543 1.382  0.34 29.16  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.804 -35.595 2.902  0.66 29.11  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.104 -36.855 1.348  0.34 32.39  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.890 -33.451 2.260  0.66 26.00  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.664 -35.399 0.440  0.34 29.12  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.114 -35.177 2.997  0.66 28.15  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.295 -37.550 0.482  0.34 32.06  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.198 -33.874 2.585  0.66 29.24  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.404 -36.680 -0.095 0.34 33.30  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.691 -32.117 1.860  0.66 26.69  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.852 -34.322 0.041  0.34 30.01  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.310 -33.027 2.469  0.66 28.63  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.387 -36.910 -1.030 0.34 32.60  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.794 -31.292 1.713  0.66 27.59  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.845 -34.551 -0.884 0.34 31.60  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.081 -31.741 2.035  0.66 28.10  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.624 -35.830 -1.413 0.34 32.20  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.733 -32.849 3.137  1.00 26.43  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.298 -32.560 2.897  1.00 26.62  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.156 -31.502 1.797  1.00 28.68  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.146 -30.834 1.451  1.00 27.73  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.586 -32.062 4.202  1.00 30.21  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.631 -33.114 5.317  1.00 30.25  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.156 -30.713 4.692  1.00 29.56  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.920 -31.316 1.316  1.00 26.96  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.549 -30.233 0.426  1.00 26.54  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.181 -29.085 1.415  1.00 31.32  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.152 -29.190 2.101  1.00 31.49  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.328 -30.601 -0.464 1.00 28.40  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.619 -31.865 -1.354 1.00 26.97  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.888 -29.362 -1.308 1.00 30.91  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.925 -31.774 -2.301 1.00 32.00  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.974 -27.991 1.492  1.00 30.95  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.647 -26.919 2.455  1.00 31.52  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.401 -26.115 2.074  1.00 35.11  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.081 -26.004 0.894  1.00 33.39  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.912 -26.048 2.459  1.00 33.50  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.495 -26.247 1.082  1.00 37.42  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.227 -27.694 0.758  1.00 33.12  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.668 -25.611 3.078  1.00 34.69  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.479 -10.140 16.486 1.00 27.03  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.883 -8.875  16.514 1.00 27.16  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.857 -8.591  17.407 1.00 29.93  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.416 -9.603  18.256 1.00 30.40  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.243 -10.780 19.824 1.00 34.89  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.959 -10.882 18.201 1.00 29.15  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.247 -10.252 11.923 1.00 31.14  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.392 -10.578 13.258 1.00 29.28  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.365 -10.221 14.157 1.00 29.11  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.240 -11.737 19.205 1.00 32.74  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.421 -11.037 20.701 1.00 35.31  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.412 -9.568  19.231 1.00 32.85  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 24.989 -11.159 17.309 1.00 26.89  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.380 -10.544 15.477 1.00 26.23  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.275 -9.600  13.676 1.00 31.82  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.255 -9.360  12.376 1.00 33.64  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.813 -8.586  11.796 0.47 34.33  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 28.940 -11.481 13.834 0.67 27.08  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.159 -9.632  11.453 1.00 32.97  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.329 -15.344 22.686 1.00 40.30  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.505 -35.351 -1.260 0.66 47.77  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.203 -35.108 -0.650 0.66 48.97  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.618 -34.430 -0.232 0.66 46.41  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 17.914 -36.978 -0.734 0.66 47.01  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 35.661 -25.803 25.568 1.00 41.08  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 25.822 -3.515  26.498 1.00 36.78  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 38.484 -15.005 15.523 1.00 37.62  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 22.723 -5.489  19.914 1.00 56.17  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 37.815 2.368   19.827 1.00 41.00  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 26.808 -32.078 16.161 1.00 46.69  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 20.774 -5.890  26.234 1.00 41.55  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 41.081 -21.658 25.198 1.00 45.99  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 10.842 -20.600 37.604 1.00 53.20  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 33.291 -20.850 29.623 1.00 46.73  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 43.599 -6.654  32.004 1.00 51.48  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 29.830 -32.236 9.537  1.00 52.55  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 37.666 -20.482 26.979 1.00 36.86  ? 313 HOH   A O   1 
HETATM 1214 O  O   A HOH   F 6 .   ? 19.046 -22.965 4.345  0.67 49.37  ? 314 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 6 .   ? 23.400 -5.878  32.941 1.00 38.75  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 16.441 -27.566 -3.263 1.00 53.77  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 21.663 -29.544 -5.250 1.00 39.03  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 45.091 -11.299 18.839 1.00 70.02  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 22.679 -27.705 17.764 1.00 51.45  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 15.451 -10.034 24.992 1.00 49.88  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 37.200 -12.496 40.321 1.00 63.06  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 20.428 -13.547 20.558 1.00 49.78  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 30.286 1.387   33.900 1.00 68.13  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 17.905 -29.415 7.682  1.00 36.62  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 21.492 -27.129 14.642 0.50 41.18  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 31.644 -0.933  15.927 1.00 45.04  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 28.236 -8.900  39.990 1.00 49.31  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 27.196 -10.239 35.935 1.00 40.49  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 32.674 -24.632 32.220 1.00 64.55  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 22.956 -28.253 12.662 1.00 25.28  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 25.662 -2.976  20.090 1.00 60.40  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 28.732 -21.795 41.669 1.00 76.73  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 19.847 -9.678  37.093 1.00 40.29  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 23.211 -17.050 44.299 1.00 62.38  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 21.528 -29.999 14.191 1.00 74.72  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 28.275 -23.778 31.704 1.00 42.00  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 27.305 -28.234 18.659 1.00 28.77  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 34.442 -23.914 29.839 1.00 78.37  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 41.342 -12.747 14.069 1.00 109.66 ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 36.824 -5.750  12.287 1.00 40.67  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 41.236 -16.899 15.232 1.00 41.06  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 30.374 -0.708  37.062 1.00 55.49  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 29.382 -27.426 20.653 1.00 25.75  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 24.887 -26.854 19.058 1.00 36.04  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 26.955 -35.349 11.640 1.00 59.88  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 21.916 -24.999 18.355 1.00 24.38  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 37.326 -6.434  34.339 1.00 42.13  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 29.051 -31.170 7.234  1.00 37.47  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 23.947 -15.846 21.301 1.00 33.08  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 26.120 -22.669 29.943 1.00 29.46  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 17.986 -34.505 8.322  1.00 35.72  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 30.676 -28.970 22.666 1.00 43.04  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 41.096 -1.460  11.692 1.00 67.19  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 26.922 -16.662 38.734 1.00 53.66  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 20.847 -7.373  19.912 1.00 52.24  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 44.345 -12.697 41.343 1.00 55.51  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 42.442 -10.509 15.522 1.00 55.96  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 46.824 -21.597 18.084 1.00 50.91  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 28.519 -24.265 34.387 1.00 57.22  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 45.935 -14.250 21.645 1.00 59.38  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 10.840 -11.530 34.595 1.00 52.52  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 43.981 -4.426  25.796 1.00 48.24  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 20.199 -15.978 40.927 1.00 37.46  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 28.845 -0.394  16.963 1.00 72.85  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 46.226 -15.890 27.603 1.00 73.08  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 41.285 -7.813  46.453 1.00 56.29  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 37.937 -16.684 13.165 0.50 29.07  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 12.762 -20.573 42.418 1.00 58.89  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 45.228 -12.595 23.661 1.00 52.45  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 21.017 -23.412 6.183  1.00 55.37  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 26.076 -21.921 38.693 1.00 41.58  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 14.357 -16.851 23.545 1.00 45.68  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 12.223 -18.093 25.903 1.00 60.56  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 34.145 -7.958  35.698 1.00 38.20  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 34.757 -18.985 13.886 0.50 26.15  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 39.025 -18.891 33.533 1.00 48.62  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 27.076 -2.338  16.131 1.00 65.19  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 46.298 -18.919 19.641 1.00 56.37  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 26.149 -8.077  9.073  1.00 47.47  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 26.065 -19.271 41.709 1.00 65.90  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 17.926 -24.392 39.744 1.00 45.26  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 41.187 -7.026  35.968 1.00 47.05  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 47.155 -25.255 21.577 1.00 56.37  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 31.860 -31.860 14.560 1.00 40.15  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 17.369 -24.557 -2.160 1.00 65.28  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 4.328  -20.396 37.980 1.00 60.62  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 43.840 -10.675 35.097 1.00 73.34  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 29.619 -22.700 36.896 1.00 69.09  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 27.637 -23.096 13.886 0.50 29.28  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 26.399 -30.796 18.997 1.00 65.16  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 11.642 -15.294 40.583 1.00 81.58  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 45.514 -10.881 30.253 1.00 55.42  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 34.761 -29.199 26.055 1.00 71.70  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 23.675 -15.729 17.795 1.00 45.32  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 33.077 -29.780 21.483 1.00 43.53  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 44.608 -16.419 29.726 1.00 55.55  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 19.860 -25.542 41.287 1.00 77.64  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 16.727 -6.512  27.622 1.00 66.75  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 42.115 -5.993  11.909 1.00 72.92  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 40.399 -19.623 29.033 1.00 38.74  ? 400 HOH   A O   1 
HETATM 1301 O  O   A HOH   F 6 .   ? 12.181 -20.822 27.904 0.66 45.64  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 30.398 -10.656 40.641 1.00 45.96  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 37.007 -2.308  11.597 1.00 62.56  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 47.363 -6.695  20.251 1.00 67.37  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 46.071 -8.985  44.178 1.00 55.20  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 44.639 -8.793  17.894 1.00 73.05  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 45.856 -17.127 17.386 1.00 69.92  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 10.422 -11.660 40.036 1.00 68.31  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 35.134 -29.736 23.415 1.00 46.55  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 25.622 -4.637  17.966 1.00 52.34  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 41.258 -17.106 35.209 1.00 48.10  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 27.039 -1.679  22.044 1.00 54.97  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 22.979 -14.999 40.456 1.00 35.16  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 46.904 -20.155 21.960 1.00 67.50  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 35.253 1.877   13.509 1.00 58.43  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 21.150 -23.294 42.142 1.00 49.76  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 33.535 -33.025 12.128 1.00 49.39  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 19.636 -27.299 10.060 1.00 55.68  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 32.162 -15.716 39.870 1.00 38.16  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 42.054 -8.123  13.856 1.00 61.22  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 34.038 -32.904 21.916 1.00 66.06  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 33.535 -0.350  20.106 1.00 45.58  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 32.381 -9.003  39.795 1.00 60.34  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 27.360 -25.533 28.369 1.00 59.90  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 29.542 -0.877  22.320 1.00 59.89  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 25.608 -16.071 41.100 1.00 51.69  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 39.881 -5.556  33.963 1.00 43.61  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 34.496 -18.906 36.290 1.00 67.19  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 45.754 -5.544  23.756 1.00 48.02  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 42.812 -18.212 30.756 1.00 51.65  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 31.748 -26.077 27.145 1.00 59.59  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 23.401 -30.550 19.316 1.00 68.24  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 44.359 -4.189  28.975 1.00 67.89  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 22.256 -10.511 14.633 1.00 48.24  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 26.421 -29.489 22.685 1.00 60.70  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 37.093 -31.608 23.421 1.00 81.57  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 31.924 -0.033  13.361 1.00 66.77  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 26.959 -34.483 18.009 1.00 68.59  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 23.101 -3.126  26.811 1.00 66.10  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 28.769 -2.640  13.100 1.00 80.09  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 19.462 -31.736 13.898 1.00 70.52  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 47.949 -23.395 19.777 1.00 65.34  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 36.775 -24.448 27.650 1.00 63.49  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 19.805 -8.156  24.623 1.00 58.01  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 35.370 -4.230  10.663 1.00 49.35  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 30.664 -34.329 14.885 1.00 61.68  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 46.689 -14.680 18.300 1.00 68.42  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 47.462 -28.430 17.700 1.00 61.26  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 24.538 -21.803 41.114 1.00 59.33  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 47.169 -11.893 25.448 1.00 71.90  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 32.203 -1.132  22.326 1.00 61.65  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 11.949 -18.818 22.749 1.00 69.75  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 47.030 -12.624 28.543 1.00 59.89  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 43.899 -13.707 13.886 0.50 93.28  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 34.108 -17.711 39.578 1.00 67.90  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 35.804 -21.283 30.614 1.00 63.81  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 19.453 -7.689  35.311 1.00 55.44  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 45.531 -8.464  31.410 1.00 67.59  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 25.348 -5.723  34.976 1.00 61.62  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 17.142 -7.976  25.080 1.00 67.19  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 43.119 -3.046  33.933 1.00 60.91  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 19.919 -14.933 43.408 1.00 54.93  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 17.074 -28.119 9.906  1.00 53.33  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 19.126 -28.234 13.808 0.50 70.29  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 32.535 -20.687 36.972 1.00 79.60  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 33.820 -11.155 41.658 0.50 64.33  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 28.336 -29.845 24.598 1.00 71.25  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 33.820 -14.003 41.658 0.50 45.13  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 12.539 -18.251 19.951 1.00 63.23  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 21.228 -5.715  34.709 1.00 53.63  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 16.818 -6.883  34.937 1.00 75.49  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 32.104 -23.977 35.019 1.00 71.08  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 45.120 -12.306 15.886 1.00 73.64  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 39.441 -5.547  11.595 1.00 74.82  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 16.677 -30.170 12.467 1.00 60.37  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   G 6 .   ? 12.227 -24.220 0.032  1.00 54.39  ? 201 HOH   D O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 17.724 -36.228 6.024  1.00 44.10  ? 202 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 22.632 -34.027 8.844  1.00 36.34  ? 203 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 14.969 -25.807 -1.824 1.00 47.24  ? 204 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 11.470 -23.575 3.020  1.00 58.01  ? 205 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 20.831 -38.315 4.024  1.00 49.88  ? 206 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 20.846 -39.561 -2.090 1.00 60.97  ? 207 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 10.652 -24.692 5.470  1.00 59.24  ? 208 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 20.123 -35.313 10.111 1.00 39.66  ? 209 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.653 -36.498 9.973  1.00 52.66  ? 210 HOH   D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP A 5   ? 0.8612 1.0242 0.7289 0.0227  -0.1348 -0.0139 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8552 1.0126 0.7052 0.0061  -0.1256 -0.0165 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8281 1.0157 0.7027 -0.0048 -0.1207 -0.0324 6   ASP A C   
4    O O   . ASP A 5   ? 0.8186 1.0313 0.7227 -0.0002 -0.1243 -0.0413 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8790 1.0092 0.7198 -0.0025 -0.1082 -0.0106 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0764 1.1868 0.8833 -0.0138 -0.1029 -0.0066 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0768 1.1997 0.8819 -0.0253 -0.0996 -0.0154 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1845 1.2663 0.9663 -0.0124 -0.1007 0.0044  6   ASP A OD2 
9    N N   . SER A 6   ? 0.7208 0.9052 0.5830 -0.0197 -0.1117 -0.0368 7   SER A N   
10   C CA  . SER A 6   ? 0.6703 0.8769 0.5513 -0.0316 -0.1049 -0.0515 7   SER A CA  
11   C C   . SER A 6   ? 0.6093 0.8045 0.5028 -0.0412 -0.0858 -0.0544 7   SER A C   
12   O O   . SER A 6   ? 0.5884 0.7892 0.4863 -0.0533 -0.0770 -0.0640 7   SER A O   
13   C CB  . SER A 6   ? 0.7491 0.9609 0.6079 -0.0409 -0.1090 -0.0560 7   SER A CB  
14   O OG  . SER A 6   ? 0.9160 1.1014 0.7456 -0.0480 -0.1013 -0.0488 7   SER A OG  
15   N N   . CYS A 7   ? 0.5003 0.6791 0.3993 -0.0351 -0.0804 -0.0466 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4611 0.6283 0.3706 -0.0419 -0.0649 -0.0483 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4450 0.6284 0.3809 -0.0471 -0.0588 -0.0598 8   CYS A C   
18   O O   . CYS A 7   ? 0.4367 0.6404 0.3882 -0.0435 -0.0654 -0.0655 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4785 0.6269 0.3877 -0.0338 -0.0624 -0.0380 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5684 0.6890 0.4446 -0.0330 -0.0622 -0.0255 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3413 0.5147 0.2816 -0.0555 -0.0461 -0.0637 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2981 0.4767 0.2586 -0.0603 -0.0382 -0.0720 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3236 0.4847 0.2886 -0.0551 -0.0325 -0.0646 9   ILE A C   
24   O O   . ILE A 8   ? 0.3108 0.4564 0.2637 -0.0515 -0.0321 -0.0560 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3388 0.5176 0.3007 -0.0725 -0.0293 -0.0824 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3530 0.5125 0.3021 -0.0757 -0.0222 -0.0795 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3351 0.5352 0.2952 -0.0782 -0.0354 -0.0916 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.4058 0.5610 0.3576 -0.0858 -0.0125 -0.0898 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2554 0.4177 0.2359 -0.0561 -0.0273 -0.0684 10  GLN A N   
30   N N   B GLN A 9   ? 0.2653 0.4294 0.2464 -0.0555 -0.0283 -0.0684 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2526 0.3984 0.2357 -0.0517 -0.0225 -0.0618 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2570 0.4059 0.2418 -0.0510 -0.0236 -0.0622 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2911 0.4259 0.2794 -0.0587 -0.0124 -0.0667 10  GLN A C   
34   C C   B GLN A 9   ? 0.3044 0.4420 0.2940 -0.0581 -0.0133 -0.0669 10  GLN A C   
35   O O   A GLN A 9   ? 0.2987 0.4419 0.2947 -0.0657 -0.0089 -0.0757 10  GLN A O   
36   O O   B GLN A 9   ? 0.3048 0.4504 0.3021 -0.0654 -0.0095 -0.0760 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2728 0.4271 0.2664 -0.0436 -0.0273 -0.0594 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2681 0.4283 0.2649 -0.0435 -0.0286 -0.0613 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.3401 0.4802 0.3389 -0.0417 -0.0206 -0.0559 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2833 0.4275 0.2795 -0.0369 -0.0262 -0.0529 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5882 0.7291 0.5911 -0.0317 -0.0252 -0.0501 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4474 0.5953 0.4586 -0.0377 -0.0211 -0.0574 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.5156 0.6671 0.5184 -0.0243 -0.0344 -0.0481 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3323 0.5001 0.3576 -0.0384 -0.0230 -0.0654 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.4979 0.6259 0.5031 -0.0307 -0.0193 -0.0471 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.4344 0.5642 0.4428 -0.0381 -0.0144 -0.0532 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2709 0.3862 0.2540 -0.0568 -0.0080 -0.0612 11  PHE A N   
48   N N   B PHE A 10  ? 0.2738 0.3919 0.2578 -0.0561 -0.0091 -0.0610 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2609 0.3616 0.2457 -0.0612 -0.0003 -0.0642 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2684 0.3710 0.2535 -0.0603 -0.0013 -0.0635 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2929 0.3880 0.2824 -0.0582 0.0015  -0.0608 11  PHE A C   
52   C C   B PHE A 10  ? 0.3035 0.4008 0.2937 -0.0576 0.0007  -0.0605 11  PHE A C   
53   O O   A PHE A 10  ? 0.2806 0.3670 0.2671 -0.0520 0.0000  -0.0533 11  PHE A O   
54   O O   B PHE A 10  ? 0.2967 0.3876 0.2848 -0.0509 -0.0014 -0.0531 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2838 0.3687 0.2614 -0.0605 0.0022  -0.0622 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2930 0.3803 0.2703 -0.0588 0.0006  -0.0603 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2978 0.3662 0.2752 -0.0638 0.0082  -0.0657 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3163 0.4075 0.2897 -0.0639 0.0017  -0.0663 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3296 0.3976 0.3075 -0.0713 0.0125  -0.0742 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3579 0.4628 0.3263 -0.0650 -0.0029 -0.0669 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3124 0.3637 0.2872 -0.0592 0.0091  -0.0607 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3587 0.4380 0.3320 -0.0673 0.0071  -0.0715 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3484 0.3961 0.3228 -0.0736 0.0178  -0.0767 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3730 0.4812 0.3363 -0.0711 -0.0009 -0.0733 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3437 0.3763 0.3149 -0.0609 0.0130  -0.0630 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.4014 0.4844 0.3722 -0.0723 0.0092  -0.0785 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3257 0.3549 0.2958 -0.0678 0.0174  -0.0705 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3720 0.4700 0.3376 -0.0749 0.0058  -0.0796 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2603 0.3611 0.2570 -0.0639 0.0055  -0.0674 12  THR A N   
70   C CA  . THR A 11  ? 0.2682 0.3661 0.2698 -0.0636 0.0090  -0.0669 12  THR A CA  
71   C C   . THR A 11  ? 0.3068 0.3814 0.2996 -0.0605 0.0117  -0.0595 12  THR A C   
72   O O   . THR A 11  ? 0.3008 0.3746 0.2954 -0.0553 0.0106  -0.0549 12  THR A O   
73   C CB  . THR A 11  ? 0.3437 0.4465 0.3512 -0.0741 0.0163  -0.0772 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3434 0.4719 0.3611 -0.0766 0.0124  -0.0852 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3940 0.4961 0.4070 -0.0756 0.0215  -0.0787 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2794 0.3352 0.2627 -0.0629 0.0146  -0.0590 13  ARG A N   
77   C CA  . ARG A 12  ? 0.2994 0.3333 0.2736 -0.0598 0.0157  -0.0531 13  ARG A CA  
78   C C   . ARG A 12  ? 0.3073 0.3390 0.2796 -0.0516 0.0102  -0.0465 13  ARG A C   
79   O O   . ARG A 12  ? 0.3060 0.3221 0.2720 -0.0485 0.0099  -0.0426 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3746 0.3872 0.3389 -0.0644 0.0199  -0.0557 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.5204 0.5269 0.4815 -0.0747 0.0279  -0.0620 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.7895 0.7873 0.7458 -0.0772 0.0322  -0.0599 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.9595 0.9307 0.9003 -0.0733 0.0310  -0.0530 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.1000 1.0626 1.0344 -0.0729 0.0325  -0.0491 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.9721 0.9108 0.8909 -0.0692 0.0298  -0.0431 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8600 0.8387 0.8041 -0.0758 0.0361  -0.0518 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2550 0.3012 0.2312 -0.0488 0.0062  -0.0459 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2630 0.3061 0.2362 -0.0437 0.0031  -0.0413 14  HIS A CA  
89   C C   . HIS A 13  ? 0.3016 0.3376 0.2731 -0.0391 0.0024  -0.0353 14  HIS A C   
90   O O   . HIS A 13  ? 0.2932 0.3192 0.2615 -0.0368 0.0020  -0.0336 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2592 0.3159 0.2322 -0.0433 0.0000  -0.0413 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.2839 0.3362 0.2524 -0.0405 -0.0009 -0.0379 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.2931 0.3405 0.2615 -0.0418 0.0010  -0.0417 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2916 0.3436 0.2561 -0.0372 -0.0026 -0.0323 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2871 0.3337 0.2527 -0.0404 0.0010  -0.0393 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2805 0.3280 0.2420 -0.0382 -0.0008 -0.0332 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2620 0.3047 0.2369 -0.0374 0.0020  -0.0332 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2667 0.3023 0.2399 -0.0335 0.0022  -0.0282 15  ALA A CA  
99   C C   . ALA A 14  ? 0.2898 0.3099 0.2579 -0.0351 0.0050  -0.0280 15  ALA A C   
100  O O   . ALA A 14  ? 0.2734 0.2852 0.2375 -0.0325 0.0040  -0.0249 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2779 0.3229 0.2574 -0.0309 0.0018  -0.0276 15  ALA A CB  
102  N N   A SER A 15  ? 0.2850 0.3005 0.2516 -0.0401 0.0084  -0.0317 16  SER A N   
103  N N   B SER A 15  ? 0.2772 0.2927 0.2438 -0.0401 0.0084  -0.0317 16  SER A N   
104  N N   C SER A 15  ? 0.2734 0.2887 0.2399 -0.0401 0.0084  -0.0317 16  SER A N   
105  C CA  A SER A 15  ? 0.2936 0.2904 0.2502 -0.0423 0.0107  -0.0310 16  SER A CA  
106  C CA  B SER A 15  ? 0.2858 0.2826 0.2424 -0.0423 0.0107  -0.0310 16  SER A CA  
107  C CA  C SER A 15  ? 0.2801 0.2766 0.2365 -0.0421 0.0106  -0.0308 16  SER A CA  
108  C C   A SER A 15  ? 0.3461 0.3314 0.2968 -0.0391 0.0067  -0.0299 16  SER A C   
109  C C   B SER A 15  ? 0.3456 0.3307 0.2961 -0.0391 0.0068  -0.0299 16  SER A C   
110  C C   C SER A 15  ? 0.3434 0.3284 0.2939 -0.0391 0.0067  -0.0299 16  SER A C   
111  O O   A SER A 15  ? 0.3235 0.2965 0.2668 -0.0365 0.0047  -0.0271 16  SER A O   
112  O O   B SER A 15  ? 0.3309 0.3034 0.2739 -0.0367 0.0048  -0.0271 16  SER A O   
113  O O   C SER A 15  ? 0.3294 0.3015 0.2722 -0.0367 0.0047  -0.0272 16  SER A O   
114  C CB  A SER A 15  ? 0.3474 0.3395 0.3010 -0.0499 0.0164  -0.0356 16  SER A CB  
115  C CB  B SER A 15  ? 0.3328 0.3248 0.2863 -0.0500 0.0164  -0.0357 16  SER A CB  
116  C CB  C SER A 15  ? 0.3226 0.3140 0.2758 -0.0497 0.0166  -0.0352 16  SER A CB  
117  O OG  A SER A 15  ? 0.4035 0.3732 0.3424 -0.0526 0.0189  -0.0340 16  SER A OG  
118  O OG  B SER A 15  ? 0.3584 0.3641 0.3208 -0.0528 0.0203  -0.0389 16  SER A OG  
119  O OG  C SER A 15  ? 0.3371 0.3307 0.2916 -0.0530 0.0171  -0.0395 16  SER A OG  
120  N N   . ASP A 16  ? 0.3124 0.3032 0.2670 -0.0389 0.0053  -0.0331 17  ASP A N   
121  C CA  . ASP A 16  ? 0.3227 0.3058 0.2758 -0.0351 0.0016  -0.0343 17  ASP A CA  
122  C C   . ASP A 16  ? 0.3215 0.3108 0.2788 -0.0302 -0.0018 -0.0324 17  ASP A C   
123  O O   . ASP A 16  ? 0.3219 0.3030 0.2771 -0.0261 -0.0056 -0.0326 17  ASP A O   
124  C CB  . ASP A 16  ? 0.3380 0.3284 0.2963 -0.0371 0.0025  -0.0397 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.4734 0.4540 0.4265 -0.0425 0.0064  -0.0433 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.4590 0.4246 0.4027 -0.0450 0.0087  -0.0413 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.5058 0.4926 0.4629 -0.0453 0.0080  -0.0485 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2595 0.2621 0.2216 -0.0308 -0.0008 -0.0309 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2531 0.2594 0.2170 -0.0283 -0.0021 -0.0294 18  VAL A CA  
130  C C   . VAL A 17  ? 0.3060 0.3025 0.2653 -0.0264 -0.0032 -0.0264 18  VAL A C   
131  O O   . VAL A 17  ? 0.2859 0.2801 0.2459 -0.0240 -0.0060 -0.0279 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2776 0.2940 0.2426 -0.0295 -0.0005 -0.0270 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2854 0.3005 0.2490 -0.0284 0.0000  -0.0247 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2713 0.2969 0.2379 -0.0319 -0.0001 -0.0303 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2759 0.2681 0.2312 -0.0281 -0.0009 -0.0236 19  LEU A N   
136  C CA  . LEU A 18  ? 0.3001 0.2825 0.2491 -0.0276 -0.0008 -0.0212 19  LEU A CA  
137  C C   . LEU A 18  ? 0.3167 0.2850 0.2573 -0.0261 -0.0048 -0.0219 19  LEU A C   
138  O O   . LEU A 18  ? 0.2976 0.2616 0.2349 -0.0238 -0.0082 -0.0215 19  LEU A O   
139  C CB  . LEU A 18  ? 0.3105 0.2922 0.2581 -0.0304 0.0039  -0.0198 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3607 0.3343 0.3023 -0.0308 0.0055  -0.0179 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.3566 0.3357 0.3025 -0.0283 0.0052  -0.0166 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.3925 0.3657 0.3340 -0.0344 0.0114  -0.0188 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.3061 0.2667 0.2426 -0.0271 -0.0050 -0.0233 20  LEU A N   
144  C CA  . LEU A 19  ? 0.3307 0.2740 0.2567 -0.0242 -0.0099 -0.0233 20  LEU A CA  
145  C C   . LEU A 19  ? 0.3535 0.3030 0.2874 -0.0174 -0.0169 -0.0263 20  LEU A C   
146  O O   . LEU A 19  ? 0.3548 0.2957 0.2823 -0.0132 -0.0231 -0.0258 20  LEU A O   
147  C CB  . LEU A 19  ? 0.3602 0.2944 0.2819 -0.0265 -0.0078 -0.0251 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4814 0.3918 0.3887 -0.0229 -0.0129 -0.0244 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.5321 0.4222 0.4193 -0.0255 -0.0127 -0.0198 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.5415 0.4427 0.4454 -0.0264 -0.0090 -0.0270 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.3027 0.2683 0.2504 -0.0170 -0.0158 -0.0303 21  ASN A N   
152  C CA  . ASN A 20  ? 0.2785 0.2534 0.2365 -0.0122 -0.0204 -0.0356 21  ASN A CA  
153  C C   . ASN A 20  ? 0.3138 0.2959 0.2745 -0.0123 -0.0214 -0.0355 21  ASN A C   
154  O O   . ASN A 20  ? 0.3067 0.2911 0.2717 -0.0077 -0.0274 -0.0397 21  ASN A O   
155  C CB  . ASN A 20  ? 0.3022 0.2910 0.2718 -0.0138 -0.0171 -0.0407 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.4233 0.4047 0.3928 -0.0116 -0.0183 -0.0440 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.4055 0.3707 0.3678 -0.0066 -0.0235 -0.0434 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3532 0.3439 0.3284 -0.0154 -0.0137 -0.0474 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2890 0.2745 0.2476 -0.0171 -0.0157 -0.0316 22  LEU A N   
160  C CA  . LEU A 21  ? 0.2887 0.2778 0.2479 -0.0183 -0.0152 -0.0316 22  LEU A CA  
161  C C   . LEU A 21  ? 0.3272 0.3044 0.2767 -0.0159 -0.0206 -0.0303 22  LEU A C   
162  O O   . LEU A 21  ? 0.3192 0.3006 0.2713 -0.0146 -0.0243 -0.0337 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2938 0.2844 0.2508 -0.0226 -0.0084 -0.0272 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.3139 0.3144 0.2765 -0.0249 -0.0043 -0.0278 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.3336 0.3326 0.2922 -0.0265 0.0001  -0.0225 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.3477 0.3574 0.3173 -0.0265 -0.0035 -0.0337 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.3042 0.2664 0.2412 -0.0162 -0.0206 -0.0259 23  ASN A N   
168  C CA  . ASN A 22  ? 0.3220 0.2688 0.2442 -0.0148 -0.0257 -0.0238 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3796 0.3231 0.3018 -0.0071 -0.0366 -0.0273 23  ASN A C   
170  O O   . ASN A 22  ? 0.3883 0.3282 0.3045 -0.0043 -0.0435 -0.0283 23  ASN A O   
171  C CB  . ASN A 22  ? 0.3491 0.2786 0.2555 -0.0188 -0.0217 -0.0192 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4483 0.3612 0.3358 -0.0202 -0.0243 -0.0166 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.4284 0.3459 0.3162 -0.0204 -0.0258 -0.0177 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4940 0.3860 0.3631 -0.0221 -0.0242 -0.0135 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.3451 0.2908 0.2751 -0.0031 -0.0386 -0.0302 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3573 0.3017 0.2914 0.0062  -0.0492 -0.0350 24  ARG A CA  
177  C C   . ARG A 23  ? 0.3849 0.3508 0.3363 0.0085  -0.0529 -0.0427 24  ARG A C   
178  O O   . ARG A 23  ? 0.3826 0.3482 0.3342 0.0157  -0.0635 -0.0463 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3603 0.3046 0.3020 0.0090  -0.0483 -0.0379 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.4051 0.3245 0.3280 0.0076  -0.0466 -0.0321 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.4376 0.3592 0.3689 0.0073  -0.0425 -0.0356 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.5603 0.4563 0.4731 0.0055  -0.0407 -0.0314 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.7459 0.6400 0.6607 0.0012  -0.0341 -0.0333 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.5679 0.4847 0.5013 -0.0013 -0.0294 -0.0386 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.6841 0.5528 0.5806 -0.0017 -0.0317 -0.0302 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.3265 0.3104 0.2911 0.0021  -0.0442 -0.0456 25  LEU A N   
187  C CA  . LEU A 24  ? 0.3229 0.3261 0.3025 0.0013  -0.0449 -0.0538 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3726 0.3721 0.3432 -0.0001 -0.0481 -0.0523 25  LEU A C   
189  O O   . LEU A 24  ? 0.3746 0.3842 0.3530 0.0035  -0.0557 -0.0596 25  LEU A O   
190  C CB  . LEU A 24  ? 0.3092 0.3255 0.2976 -0.0070 -0.0336 -0.0555 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.3596 0.3827 0.3572 -0.0073 -0.0295 -0.0588 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.3531 0.3863 0.3543 -0.0161 -0.0191 -0.0598 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.3562 0.3900 0.3695 -0.0002 -0.0363 -0.0695 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.3321 0.3181 0.2870 -0.0055 -0.0425 -0.0438 26  ARG A N   
195  C CA  . ARG A 25  ? 0.3428 0.3234 0.2872 -0.0078 -0.0445 -0.0426 26  ARG A CA  
196  C C   . ARG A 25  ? 0.4146 0.3853 0.3484 -0.0002 -0.0581 -0.0433 26  ARG A C   
197  O O   . ARG A 25  ? 0.4194 0.3978 0.3552 0.0009  -0.0644 -0.0486 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3649 0.3320 0.2950 -0.0141 -0.0359 -0.0347 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.4112 0.3734 0.3309 -0.0175 -0.0367 -0.0349 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.4743 0.4258 0.3833 -0.0238 -0.0271 -0.0294 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.4514 0.3865 0.3463 -0.0237 -0.0264 -0.0237 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.6015 0.5204 0.4774 -0.0274 -0.0251 -0.0207 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.5269 0.4439 0.3951 -0.0304 -0.0258 -0.0227 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4814 0.3856 0.3449 -0.0293 -0.0223 -0.0167 26  ARG A NH2 
205  N N   A SER A 26  ? 0.3989 0.3515 0.3200 0.0047  -0.0625 -0.0381 27  SER A N   
206  N N   B SER A 26  ? 0.3948 0.3475 0.3161 0.0048  -0.0625 -0.0381 27  SER A N   
207  N N   C SER A 26  ? 0.3984 0.3510 0.3194 0.0047  -0.0625 -0.0381 27  SER A N   
208  C CA  A SER A 26  ? 0.4274 0.3636 0.3325 0.0129  -0.0761 -0.0366 27  SER A CA  
209  C CA  B SER A 26  ? 0.4217 0.3576 0.3271 0.0131  -0.0760 -0.0365 27  SER A CA  
210  C CA  C SER A 26  ? 0.4269 0.3630 0.3320 0.0129  -0.0761 -0.0366 27  SER A CA  
211  C C   A SER A 26  ? 0.4883 0.4406 0.4102 0.0232  -0.0892 -0.0462 27  SER A C   
212  C C   B SER A 26  ? 0.4842 0.4364 0.4060 0.0231  -0.0890 -0.0461 27  SER A C   
213  C C   C SER A 26  ? 0.4869 0.4394 0.4089 0.0232  -0.0892 -0.0462 27  SER A C   
214  O O   A SER A 26  ? 0.5069 0.4539 0.4190 0.0293  -0.1019 -0.0473 27  SER A O   
215  O O   B SER A 26  ? 0.5013 0.4479 0.4129 0.0290  -0.1015 -0.0471 27  SER A O   
216  O O   C SER A 26  ? 0.5043 0.4515 0.4165 0.0292  -0.1018 -0.0474 27  SER A O   
217  C CB  A SER A 26  ? 0.4871 0.3987 0.3755 0.0152  -0.0762 -0.0297 27  SER A CB  
218  C CB  B SER A 26  ? 0.4768 0.3912 0.3696 0.0162  -0.0762 -0.0307 27  SER A CB  
219  C CB  C SER A 26  ? 0.4877 0.3998 0.3769 0.0154  -0.0762 -0.0299 27  SER A CB  
220  O OG  A SER A 26  ? 0.5596 0.4780 0.4637 0.0207  -0.0769 -0.0335 27  SER A OG  
221  O OG  B SER A 26  ? 0.5617 0.4582 0.4355 0.0074  -0.0665 -0.0230 27  SER A OG  
222  O OG  C SER A 26  ? 0.6073 0.4981 0.4766 0.0238  -0.0897 -0.0272 27  SER A OG  
223  N N   . ARG A 27  ? 0.4255 0.3987 0.3728 0.0249  -0.0861 -0.0539 28  ARG A N   
224  C CA  . ARG A 27  ? 0.4323 0.4259 0.4014 0.0340  -0.0965 -0.0659 28  ARG A CA  
225  C C   . ARG A 27  ? 0.4512 0.4724 0.4396 0.0273  -0.0922 -0.0760 28  ARG A C   
226  O O   . ARG A 27  ? 0.4538 0.4974 0.4647 0.0326  -0.0985 -0.0886 28  ARG A O   
227  C CB  . ARG A 27  ? 0.4389 0.4373 0.4234 0.0390  -0.0947 -0.0701 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.5497 0.5188 0.5146 0.0452  -0.0988 -0.0613 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.6135 0.5865 0.5923 0.0472  -0.0937 -0.0652 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.7843 0.7779 0.7889 0.0574  -0.1018 -0.0786 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.9622 0.9737 0.9890 0.0559  -0.0947 -0.0876 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.7995 0.8314 0.8515 0.0650  -0.1017 -0.1016 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.7734 0.7838 0.7977 0.0453  -0.0806 -0.0836 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.3837 0.4029 0.3637 0.0156  -0.0812 -0.0714 29  ASP A N   
235  C CA  . ASP A 28  ? 0.3814 0.4205 0.3742 0.0068  -0.0743 -0.0794 29  ASP A CA  
236  C C   . ASP A 28  ? 0.4167 0.4779 0.4339 0.0028  -0.0657 -0.0891 29  ASP A C   
237  O O   . ASP A 28  ? 0.4281 0.5112 0.4628 -0.0005 -0.0650 -0.1016 29  ASP A O   
238  C CB  . ASP A 28  ? 0.4229 0.4717 0.4175 0.0105  -0.0867 -0.0873 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.5476 0.6094 0.5474 -0.0012 -0.0782 -0.0934 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.5490 0.6001 0.5384 -0.0109 -0.0650 -0.0862 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.6061 0.6891 0.6210 -0.0004 -0.0848 -0.1063 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.3343 0.3896 0.3515 0.0022  -0.0588 -0.0844 30  ILE A N   
243  C CA  . ILE A 29  ? 0.3224 0.3950 0.3581 -0.0022 -0.0501 -0.0928 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3529 0.4239 0.3830 -0.0150 -0.0350 -0.0888 30  ILE A C   
245  O O   . ILE A 29  ? 0.3171 0.3712 0.3312 -0.0174 -0.0300 -0.0770 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3635 0.4323 0.4034 0.0045  -0.0519 -0.0921 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3866 0.4570 0.4344 0.0189  -0.0676 -0.0981 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.3434 0.4277 0.3980 -0.0028 -0.0403 -0.0997 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.4344 0.4910 0.4786 0.0262  -0.0699 -0.0940 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.3332 0.4215 0.3763 -0.0233 -0.0279 -0.0995 31  LEU A N   
251  C CA  . LEU A 30  ? 0.3429 0.4278 0.3794 -0.0357 -0.0134 -0.0971 31  LEU A CA  
252  C C   . LEU A 30  ? 0.3653 0.4326 0.3833 -0.0394 -0.0101 -0.0865 31  LEU A C   
253  O O   . LEU A 30  ? 0.3410 0.3989 0.3494 -0.0467 0.0003  -0.0809 31  LEU A O   
254  C CB  . LEU A 30  ? 0.3533 0.4342 0.3869 -0.0384 -0.0055 -0.0930 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.4311 0.5313 0.4834 -0.0401 -0.0026 -0.1065 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.4454 0.5393 0.4898 -0.0453 0.0064  -0.1018 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.5075 0.6252 0.5728 -0.0495 0.0039  -0.1208 31  LEU A CD2 
258  N N   . THR A 31  ? 0.3314 0.3943 0.3442 -0.0346 -0.0191 -0.0849 32  THR A N   
259  C CA  . THR A 31  ? 0.3330 0.3819 0.3307 -0.0392 -0.0153 -0.0783 32  THR A CA  
260  C C   . THR A 31  ? 0.4015 0.4599 0.4054 -0.0500 -0.0064 -0.0875 32  THR A C   
261  O O   . THR A 31  ? 0.3899 0.4680 0.4101 -0.0518 -0.0085 -0.1007 32  THR A O   
262  C CB  . THR A 31  ? 0.3891 0.4319 0.3785 -0.0328 -0.0267 -0.0762 32  THR A CB  
263  O OG1 . THR A 31  ? 0.4113 0.4719 0.4143 -0.0293 -0.0365 -0.0882 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3829 0.4105 0.3612 -0.0245 -0.0328 -0.0661 32  THR A CG2 
265  N N   . ASP A 32  ? 0.3671 0.4114 0.3589 -0.0573 0.0043  -0.0815 33  ASP A N   
266  C CA  . ASP A 32  ? 0.3664 0.4138 0.3601 -0.0691 0.0153  -0.0891 33  ASP A CA  
267  C C   . ASP A 32  ? 0.3911 0.4256 0.3732 -0.0744 0.0200  -0.0871 33  ASP A C   
268  O O   . ASP A 32  ? 0.4005 0.4313 0.3799 -0.0850 0.0310  -0.0917 33  ASP A O   
269  C CB  . ASP A 32  ? 0.3881 0.4283 0.3771 -0.0746 0.0264  -0.0855 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.5339 0.5540 0.5077 -0.0698 0.0281  -0.0703 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.4819 0.4930 0.4493 -0.0637 0.0230  -0.0631 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.6682 0.6824 0.6365 -0.0725 0.0344  -0.0665 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.3232 0.3493 0.2970 -0.0682 0.0128  -0.0808 34  VAL A N   
274  C CA  . VAL A 33  ? 0.3257 0.3402 0.2888 -0.0733 0.0172  -0.0802 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3793 0.3933 0.3368 -0.0675 0.0061  -0.0792 34  VAL A C   
276  O O   . VAL A 33  ? 0.3716 0.3845 0.3273 -0.0586 -0.0029 -0.0735 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3725 0.3646 0.3225 -0.0744 0.0276  -0.0692 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.3478 0.3307 0.2914 -0.0650 0.0226  -0.0580 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3857 0.3654 0.3268 -0.0819 0.0360  -0.0713 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3476 0.3604 0.3000 -0.0735 0.0074  -0.0847 35  VAL A N   
281  N N   B VAL A 34  ? 0.3420 0.3547 0.2943 -0.0734 0.0073  -0.0847 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3520 0.3602 0.2935 -0.0706 -0.0011 -0.0837 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.3437 0.3516 0.2850 -0.0700 -0.0016 -0.0832 35  VAL A CA  
284  C C   A VAL A 34  ? 0.3963 0.3843 0.3238 -0.0754 0.0097  -0.0778 35  VAL A C   
285  C C   B VAL A 34  ? 0.3989 0.3877 0.3260 -0.0755 0.0086  -0.0786 35  VAL A C   
286  O O   A VAL A 34  ? 0.3933 0.3767 0.3212 -0.0835 0.0209  -0.0814 35  VAL A O   
287  O O   B VAL A 34  ? 0.4029 0.3889 0.3305 -0.0843 0.0189  -0.0836 35  VAL A O   
288  C CB  A VAL A 34  ? 0.4148 0.4401 0.3619 -0.0741 -0.0093 -0.0970 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.3984 0.4241 0.3454 -0.0697 -0.0139 -0.0947 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.4298 0.4470 0.3604 -0.0718 -0.0183 -0.0951 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.4005 0.4360 0.3534 -0.0813 -0.0070 -0.1071 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.4084 0.4564 0.3738 -0.0682 -0.0199 -0.1050 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.4082 0.4244 0.3383 -0.0642 -0.0252 -0.0902 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.3503 0.3252 0.2652 -0.0707 0.0071  -0.0696 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3679 0.3257 0.2711 -0.0744 0.0166  -0.0658 36  ILE A CA  
296  C C   . ILE A 35  ? 0.4380 0.3941 0.3286 -0.0778 0.0109  -0.0706 36  ILE A C   
297  O O   . ILE A 35  ? 0.4279 0.3840 0.3103 -0.0728 -0.0002 -0.0682 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3945 0.3406 0.2937 -0.0685 0.0197  -0.0554 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3828 0.3323 0.2931 -0.0641 0.0223  -0.0506 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.4261 0.3572 0.3169 -0.0721 0.0301  -0.0542 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3789 0.3258 0.2944 -0.0688 0.0322  -0.0526 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.3972 0.3502 0.2844 -0.0865 0.0184  -0.0773 37  VAL A N   
303  C CA  . VAL A 36  ? 0.4094 0.3611 0.2831 -0.0915 0.0138  -0.0831 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4838 0.4162 0.3429 -0.0944 0.0232  -0.0790 37  VAL A C   
305  O O   . VAL A 36  ? 0.4642 0.3874 0.3266 -0.0978 0.0365  -0.0790 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4648 0.4284 0.3444 -0.1006 0.0152  -0.0960 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4777 0.4405 0.3416 -0.1060 0.0094  -0.1024 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4611 0.4471 0.3582 -0.0980 0.0064  -0.1023 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.4547 0.3800 0.2969 -0.0931 0.0164  -0.0761 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4666 0.3750 0.2940 -0.0970 0.0254  -0.0737 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5739 0.4791 0.3808 -0.1034 0.0190  -0.0793 38  VAL A C   
312  O O   . VAL A 37  ? 0.5367 0.4389 0.3284 -0.1001 0.0069  -0.0758 38  VAL A O   
313  C CB  . VAL A 37  ? 0.5070 0.4075 0.3313 -0.0906 0.0254  -0.0642 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.5133 0.3995 0.3287 -0.0955 0.0383  -0.0641 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4858 0.3939 0.3301 -0.0830 0.0264  -0.0590 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5854 0.4910 0.3909 -0.1124 0.0259  -0.0884 39  SER A N   
317  N N   B SER A 38  ? 0.5726 0.4765 0.3772 -0.1126 0.0272  -0.0880 39  SER A N   
318  C CA  A SER A 38  ? 0.6108 0.5157 0.3974 -0.1202 0.0202  -0.0960 39  SER A CA  
319  C CA  B SER A 38  ? 0.5935 0.4957 0.3791 -0.1209 0.0227  -0.0956 39  SER A CA  
320  C C   A SER A 38  ? 0.6264 0.5482 0.4144 -0.1154 0.0006  -0.0989 39  SER A C   
321  C C   B SER A 38  ? 0.6221 0.5354 0.4005 -0.1160 0.0021  -0.0962 39  SER A C   
322  O O   A SER A 38  ? 0.6087 0.5479 0.4175 -0.1139 -0.0016 -0.1041 39  SER A O   
323  O O   B SER A 38  ? 0.6283 0.5315 0.3840 -0.1142 -0.0073 -0.0918 39  SER A O   
324  C CB  A SER A 38  ? 0.6991 0.5854 0.4597 -0.1238 0.0228  -0.0924 39  SER A CB  
325  C CB  B SER A 38  ? 0.6640 0.5472 0.4283 -0.1270 0.0318  -0.0945 39  SER A CB  
326  O OG  A SER A 38  ? 0.8885 0.7629 0.6527 -0.1268 0.0405  -0.0913 39  SER A OG  
327  O OG  B SER A 38  ? 0.7699 0.6463 0.5432 -0.1323 0.0498  -0.0986 39  SER A OG  
328  N N   A ARG A 39  ? 0.5813 0.4971 0.3470 -0.1125 -0.0134 -0.0958 40  ARG A N   
329  N N   B ARG A 39  ? 0.5452 0.4787 0.3442 -0.1130 -0.0044 -0.1014 40  ARG A N   
330  C CA  A ARG A 39  ? 0.5766 0.5065 0.3415 -0.1055 -0.0344 -0.0984 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.5412 0.4926 0.3447 -0.1067 -0.0237 -0.1054 40  ARG A CA  
332  C C   A ARG A 39  ? 0.5877 0.5222 0.3648 -0.0923 -0.0439 -0.0904 40  ARG A C   
333  C C   B ARG A 39  ? 0.5666 0.5170 0.3721 -0.0936 -0.0349 -0.0953 40  ARG A C   
334  O O   A ARG A 39  ? 0.5754 0.5235 0.3572 -0.0844 -0.0613 -0.0934 40  ARG A O   
335  O O   B ARG A 39  ? 0.5601 0.5288 0.3804 -0.0865 -0.0475 -0.0992 40  ARG A O   
336  C CB  A ARG A 39  ? 0.6001 0.5173 0.3310 -0.1077 -0.0464 -0.0981 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.5601 0.5133 0.3430 -0.1111 -0.0359 -0.1126 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.6957 0.6165 0.4165 -0.1199 -0.0437 -0.1098 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.7004 0.6625 0.4881 -0.1241 -0.0270 -0.1262 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.7201 0.6315 0.4070 -0.1199 -0.0606 -0.1096 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.7930 0.7659 0.5672 -0.1273 -0.0427 -0.1361 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.7464 0.6579 0.4187 -0.1333 -0.0564 -0.1204 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.8827 0.8636 0.6612 -0.1415 -0.0325 -0.1502 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.9068 0.8406 0.5878 -0.1365 -0.0658 -0.1335 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 1.0524 1.0173 0.8108 -0.1527 -0.0217 -0.1529 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7692 0.7011 0.4348 -0.1498 -0.0607 -0.1434 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.8714 0.8122 0.6041 -0.1521 -0.0191 -0.1430 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.6928 0.6522 0.3993 -0.1270 -0.0796 -0.1382 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.8900 0.8624 0.6536 -0.1657 -0.0123 -0.1667 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.5185 0.4426 0.3012 -0.0896 -0.0330 -0.0813 41  GLU A N   
351  N N   B GLU A 40  ? 0.5177 0.4485 0.3113 -0.0908 -0.0292 -0.0840 41  GLU A N   
352  C CA  A GLU A 40  ? 0.5011 0.4278 0.2940 -0.0783 -0.0402 -0.0739 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.5071 0.4342 0.3019 -0.0798 -0.0372 -0.0746 41  GLU A CA  
354  C C   A GLU A 40  ? 0.5127 0.4563 0.3364 -0.0760 -0.0334 -0.0762 41  GLU A C   
355  C C   B GLU A 40  ? 0.5173 0.4588 0.3415 -0.0756 -0.0315 -0.0745 41  GLU A C   
356  O O   A GLU A 40  ? 0.4797 0.4246 0.3136 -0.0828 -0.0189 -0.0791 41  GLU A O   
357  O O   B GLU A 40  ? 0.4851 0.4251 0.3194 -0.0806 -0.0164 -0.0745 41  GLU A O   
358  C CB  A GLU A 40  ? 0.5281 0.4324 0.3044 -0.0770 -0.0346 -0.0628 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.5377 0.4407 0.3122 -0.0811 -0.0299 -0.0648 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.7491 0.6324 0.4901 -0.0802 -0.0407 -0.0597 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.7222 0.6070 0.4622 -0.0842 -0.0379 -0.0630 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.2217 1.0946 0.9468 -0.0705 -0.0573 -0.0527 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.1801 1.0546 0.9048 -0.0745 -0.0538 -0.0554 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.2313 1.0937 0.9560 -0.0666 -0.0538 -0.0448 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.2076 1.0861 0.9231 -0.0692 -0.0716 -0.0582 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.2329 1.1073 0.9453 -0.0664 -0.0743 -0.0555 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.1920 1.0540 0.9138 -0.0718 -0.0489 -0.0473 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4617 0.4159 0.2984 -0.0662 -0.0438 -0.0747 42  GLN A N   
369  C CA  . GLN A 41  ? 0.4409 0.4105 0.3040 -0.0635 -0.0391 -0.0765 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4754 0.4380 0.3404 -0.0550 -0.0407 -0.0668 42  GLN A C   
371  O O   . GLN A 41  ? 0.4810 0.4361 0.3339 -0.0478 -0.0528 -0.0627 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4622 0.4566 0.3428 -0.0610 -0.0503 -0.0880 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.6919 0.6971 0.5753 -0.0714 -0.0466 -0.0999 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.9097 0.9436 0.8157 -0.0709 -0.0546 -0.1139 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.8049 0.8525 0.7266 -0.0619 -0.0634 -0.1156 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.9360 0.9805 0.8451 -0.0812 -0.0509 -0.1257 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.3969 0.3605 0.2752 -0.0559 -0.0288 -0.0634 43  PHE A N   
378  C CA  . PHE A 42  ? 0.3991 0.3581 0.2808 -0.0491 -0.0289 -0.0554 43  PHE A CA  
379  C C   . PHE A 42  ? 0.4354 0.4103 0.3396 -0.0478 -0.0255 -0.0586 43  PHE A C   
380  O O   . PHE A 42  ? 0.4378 0.4149 0.3493 -0.0538 -0.0142 -0.0605 43  PHE A O   
381  C CB  . PHE A 42  ? 0.4202 0.3630 0.2929 -0.0523 -0.0171 -0.0477 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.4552 0.3812 0.3045 -0.0561 -0.0171 -0.0455 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4908 0.4128 0.3327 -0.0641 -0.0102 -0.0499 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.4990 0.4109 0.3317 -0.0528 -0.0228 -0.0394 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.5293 0.4353 0.3478 -0.0690 -0.0092 -0.0487 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.5577 0.4517 0.3651 -0.0582 -0.0216 -0.0377 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.5360 0.4279 0.3366 -0.0663 -0.0149 -0.0426 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3845 0.3688 0.2983 -0.0402 -0.0349 -0.0598 44  ARG A N   
389  C CA  . ARG A 43  ? 0.3563 0.3558 0.2904 -0.0397 -0.0312 -0.0637 44  ARG A CA  
390  C C   . ARG A 43  ? 0.4030 0.3933 0.3364 -0.0378 -0.0241 -0.0546 44  ARG A C   
391  O O   . ARG A 43  ? 0.3963 0.3742 0.3188 -0.0336 -0.0273 -0.0476 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3609 0.3766 0.3080 -0.0321 -0.0441 -0.0713 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.4609 0.4912 0.4129 -0.0334 -0.0526 -0.0827 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.5359 0.5913 0.5119 -0.0290 -0.0596 -0.0949 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.6802 0.7439 0.6712 -0.0344 -0.0468 -0.0971 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.8433 0.9191 0.8452 -0.0450 -0.0360 -0.1059 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.7573 0.8424 0.7612 -0.0514 -0.0367 -0.1153 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.6167 0.6947 0.6262 -0.0500 -0.0245 -0.1060 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.3559 0.3515 0.2993 -0.0416 -0.0145 -0.0551 45  ALA A N   
400  C CA  . ALA A 44  ? 0.3536 0.3425 0.2964 -0.0397 -0.0089 -0.0472 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3623 0.3602 0.3162 -0.0425 -0.0026 -0.0497 45  ALA A C   
402  O O   . ALA A 44  ? 0.3372 0.3461 0.2995 -0.0470 -0.0010 -0.0582 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3729 0.3472 0.3048 -0.0423 -0.0011 -0.0405 45  ALA A CB  
404  N N   . HIS A 45  ? 0.3182 0.3117 0.2713 -0.0406 0.0012  -0.0432 46  HIS A N   
405  C CA  . HIS A 45  ? 0.3078 0.3056 0.2659 -0.0437 0.0076  -0.0437 46  HIS A CA  
406  C C   . HIS A 45  ? 0.3414 0.3261 0.2906 -0.0468 0.0162  -0.0379 46  HIS A C   
407  O O   . HIS A 45  ? 0.3255 0.3014 0.2692 -0.0432 0.0164  -0.0312 46  HIS A O   
408  C CB  . HIS A 45  ? 0.3043 0.3049 0.2653 -0.0391 0.0049  -0.0403 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.3386 0.3487 0.3078 -0.0345 -0.0035 -0.0457 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.3623 0.3657 0.3265 -0.0286 -0.0108 -0.0424 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.3461 0.3705 0.3277 -0.0349 -0.0056 -0.0551 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.3584 0.3702 0.3311 -0.0242 -0.0181 -0.0485 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.3475 0.3740 0.3328 -0.0273 -0.0155 -0.0570 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.3317 0.3146 0.2797 -0.0535 0.0235  -0.0412 47  LYS A N   
415  C CA  . LYS A 46  ? 0.3372 0.3040 0.2751 -0.0557 0.0316  -0.0357 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3718 0.3325 0.3058 -0.0494 0.0308  -0.0266 47  LYS A C   
417  O O   . LYS A 46  ? 0.3373 0.2877 0.2667 -0.0456 0.0323  -0.0212 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3723 0.3354 0.3067 -0.0647 0.0402  -0.0402 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.3935 0.3605 0.3309 -0.0720 0.0429  -0.0496 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.3898 0.3540 0.3242 -0.0831 0.0530  -0.0558 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.4468 0.4199 0.3874 -0.0914 0.0553  -0.0677 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.4536 0.4254 0.3921 -0.1042 0.0666  -0.0757 47  LYS A NZ  
423  N N   . THR A 47  ? 0.3328 0.3014 0.2698 -0.0483 0.0284  -0.0262 48  THR A N   
424  C CA  . THR A 47  ? 0.3344 0.2993 0.2675 -0.0431 0.0269  -0.0187 48  THR A CA  
425  C C   . THR A 47  ? 0.3417 0.3080 0.2784 -0.0363 0.0222  -0.0152 48  THR A C   
426  O O   . THR A 47  ? 0.3490 0.3096 0.2829 -0.0319 0.0225  -0.0099 48  THR A O   
427  C CB  . THR A 47  ? 0.4127 0.3862 0.3473 -0.0447 0.0258  -0.0202 48  THR A CB  
428  O OG1 . THR A 47  ? 0.4180 0.4051 0.3637 -0.0439 0.0209  -0.0263 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.4256 0.3937 0.3523 -0.0528 0.0331  -0.0228 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2969 0.2702 0.2391 -0.0356 0.0178  -0.0186 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2946 0.2671 0.2377 -0.0317 0.0150  -0.0162 49  VAL A CA  
432  C C   . VAL A 48  ? 0.3354 0.2986 0.2748 -0.0316 0.0192  -0.0149 49  VAL A C   
433  O O   . VAL A 48  ? 0.3168 0.2783 0.2575 -0.0282 0.0203  -0.0123 49  VAL A O   
434  C CB  . VAL A 48  ? 0.3154 0.2920 0.2601 -0.0314 0.0095  -0.0196 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.3220 0.2936 0.2633 -0.0299 0.0089  -0.0174 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.3101 0.2955 0.2602 -0.0304 0.0059  -0.0216 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.3217 0.2801 0.2578 -0.0357 0.0218  -0.0182 50  LEU A N   
438  C CA  . LEU A 49  ? 0.3185 0.2671 0.2508 -0.0364 0.0269  -0.0181 50  LEU A CA  
439  C C   . LEU A 49  ? 0.3502 0.2910 0.2819 -0.0325 0.0312  -0.0137 50  LEU A C   
440  O O   . LEU A 49  ? 0.3515 0.2890 0.2853 -0.0288 0.0333  -0.0127 50  LEU A O   
441  C CB  . LEU A 49  ? 0.3119 0.2571 0.2404 -0.0425 0.0295  -0.0233 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.3498 0.3022 0.2781 -0.0450 0.0234  -0.0284 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.3482 0.3000 0.2746 -0.0516 0.0261  -0.0350 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3748 0.3235 0.2977 -0.0434 0.0207  -0.0271 50  LEU A CD2 
445  N N   . MET A 50  ? 0.3125 0.2505 0.2411 -0.0329 0.0322  -0.0115 51  MET A N   
446  C CA  . MET A 50  ? 0.3388 0.2663 0.2632 -0.0279 0.0343  -0.0062 51  MET A CA  
447  C C   . MET A 50  ? 0.3809 0.3160 0.3115 -0.0200 0.0292  -0.0028 51  MET A C   
448  O O   . MET A 50  ? 0.3836 0.3134 0.3160 -0.0134 0.0297  -0.0005 51  MET A O   
449  C CB  . MET A 50  ? 0.3703 0.2913 0.2856 -0.0315 0.0361  -0.0042 51  MET A CB  
450  C CG  . MET A 50  ? 0.4070 0.3201 0.3165 -0.0405 0.0429  -0.0090 51  MET A CG  
451  S SD  . MET A 50  ? 0.4631 0.3739 0.3636 -0.0477 0.0459  -0.0092 51  MET A SD  
452  C CE  . MET A 50  ? 0.4311 0.3156 0.3141 -0.0433 0.0494  -0.0003 51  MET A CE  
453  N N   . ALA A 51  ? 0.3327 0.2812 0.2680 -0.0207 0.0244  -0.0036 52  ALA A N   
454  C CA  . ALA A 51  ? 0.3223 0.2806 0.2644 -0.0150 0.0199  -0.0020 52  ALA A CA  
455  C C   . ALA A 51  ? 0.3640 0.3261 0.3143 -0.0129 0.0213  -0.0049 52  ALA A C   
456  O O   . ALA A 51  ? 0.3629 0.3328 0.3209 -0.0077 0.0191  -0.0050 52  ALA A O   
457  C CB  . ALA A 51  ? 0.3211 0.2909 0.2654 -0.0178 0.0159  -0.0035 52  ALA A CB  
458  N N   . CYS A 52  ? 0.3191 0.2767 0.2676 -0.0176 0.0251  -0.0083 53  CYS A N   
459  C CA  . CYS A 52  ? 0.3223 0.2817 0.2754 -0.0182 0.0283  -0.0120 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3661 0.3168 0.3200 -0.0168 0.0343  -0.0140 53  CYS A C   
461  O O   . CYS A 52  ? 0.3545 0.3084 0.3141 -0.0170 0.0380  -0.0181 53  CYS A O   
462  C CB  . CYS A 52  ? 0.3231 0.2820 0.2703 -0.0248 0.0278  -0.0145 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.3524 0.3198 0.3001 -0.0256 0.0215  -0.0136 53  CYS A SG  
464  N N   . SER A 53  ? 0.3272 0.2662 0.2745 -0.0173 0.0367  -0.0125 54  SER A N   
465  C CA  . SER A 53  ? 0.3290 0.2571 0.2750 -0.0177 0.0435  -0.0154 54  SER A CA  
466  C C   . SER A 53  ? 0.3754 0.2908 0.3185 -0.0123 0.0450  -0.0119 54  SER A C   
467  O O   . SER A 53  ? 0.3540 0.2626 0.2882 -0.0150 0.0441  -0.0086 54  SER A O   
468  C CB  . SER A 53  ? 0.3489 0.2721 0.2858 -0.0269 0.0460  -0.0187 54  SER A CB  
469  O OG  . SER A 53  ? 0.3957 0.3062 0.3276 -0.0295 0.0524  -0.0213 54  SER A OG  
470  N N   . GLY A 54  ? 0.3593 0.2697 0.3088 -0.0052 0.0480  -0.0133 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3653 0.2581 0.3096 0.0013  0.0496  -0.0097 55  GLY A CA  
472  C C   . GLY A 54  ? 0.4154 0.2911 0.3471 -0.0071 0.0566  -0.0109 55  GLY A C   
473  O O   . GLY A 54  ? 0.4140 0.2735 0.3342 -0.0070 0.0577  -0.0065 55  GLY A O   
474  N N   . LEU A 55  ? 0.3849 0.2639 0.3167 -0.0158 0.0615  -0.0174 56  LEU A N   
475  C CA  . LEU A 55  ? 0.3946 0.2609 0.3157 -0.0252 0.0679  -0.0205 56  LEU A CA  
476  C C   . LEU A 55  ? 0.4258 0.2944 0.3390 -0.0322 0.0649  -0.0184 56  LEU A C   
477  O O   . LEU A 55  ? 0.4066 0.2604 0.3102 -0.0358 0.0694  -0.0176 56  LEU A O   
478  C CB  . LEU A 55  ? 0.3931 0.2639 0.3146 -0.0329 0.0721  -0.0282 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4673 0.3267 0.3788 -0.0429 0.0787  -0.0332 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4911 0.3292 0.3998 -0.0400 0.0874  -0.0343 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.4566 0.3233 0.3652 -0.0512 0.0796  -0.0400 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3675 0.2536 0.2846 -0.0341 0.0582  -0.0183 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3594 0.2507 0.2725 -0.0400 0.0556  -0.0182 57  PHE A CA  
484  C C   . PHE A 56  ? 0.4065 0.2902 0.3144 -0.0365 0.0550  -0.0121 57  PHE A C   
485  O O   . PHE A 56  ? 0.3936 0.2718 0.2941 -0.0434 0.0582  -0.0132 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3650 0.2748 0.2837 -0.0414 0.0483  -0.0200 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3755 0.2886 0.2929 -0.0471 0.0484  -0.0261 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.4041 0.3138 0.3169 -0.0550 0.0520  -0.0320 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3904 0.3095 0.3093 -0.0453 0.0449  -0.0264 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.4100 0.3228 0.3196 -0.0600 0.0508  -0.0378 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.4191 0.3382 0.3320 -0.0507 0.0442  -0.0312 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3960 0.3125 0.3044 -0.0574 0.0464  -0.0367 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3772 0.2599 0.2880 -0.0263 0.0512  -0.0064 58  TYR A N   
494  C CA  . TYR A 57  ? 0.3883 0.2607 0.2902 -0.0220 0.0494  0.0004  58  TYR A CA  
495  C C   . TYR A 57  ? 0.4587 0.3050 0.3459 -0.0250 0.0572  0.0018  58  TYR A C   
496  O O   . TYR A 57  ? 0.4411 0.2771 0.3152 -0.0306 0.0597  0.0042  58  TYR A O   
497  C CB  . TYR A 57  ? 0.4094 0.2860 0.3183 -0.0094 0.0429  0.0049  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4633 0.3267 0.3602 -0.0031 0.0393  0.0126  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.4832 0.3503 0.3718 -0.0073 0.0364  0.0156  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.5233 0.3689 0.4157 0.0074  0.0387  0.0168  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.5218 0.3743 0.3949 -0.0024 0.0328  0.0231  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5761 0.4064 0.4536 0.0141  0.0338  0.0249  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6578 0.4912 0.5242 0.0087  0.0309  0.0283  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.7381 0.5542 0.5859 0.0148  0.0258  0.0367  58  TYR A OH  
505  N N   A SER A 58  ? 0.4326 0.2672 0.3212 -0.0221 0.0621  -0.0003 59  SER A N   
506  N N   B SER A 58  ? 0.4333 0.2679 0.3219 -0.0221 0.0621  -0.0003 59  SER A N   
507  C CA  A SER A 58  ? 0.4612 0.2680 0.3358 -0.0248 0.0706  0.0003  59  SER A CA  
508  C CA  B SER A 58  ? 0.4622 0.2691 0.3368 -0.0249 0.0706  0.0002  59  SER A CA  
509  C C   A SER A 58  ? 0.5288 0.3333 0.3960 -0.0407 0.0784  -0.0061 59  SER A C   
510  C C   B SER A 58  ? 0.5263 0.3314 0.3936 -0.0407 0.0781  -0.0060 59  SER A C   
511  O O   A SER A 58  ? 0.5613 0.3453 0.4125 -0.0467 0.0847  -0.0044 59  SER A O   
512  O O   B SER A 58  ? 0.5551 0.3405 0.4064 -0.0467 0.0841  -0.0041 59  SER A O   
513  C CB  A SER A 58  ? 0.4949 0.2930 0.3759 -0.0184 0.0743  -0.0027 59  SER A CB  
514  C CB  B SER A 58  ? 0.5003 0.2991 0.3815 -0.0192 0.0747  -0.0032 59  SER A CB  
515  O OG  A SER A 58  ? 0.5498 0.3476 0.4375 -0.0030 0.0677  0.0023  59  SER A OG  
516  O OG  B SER A 58  ? 0.6016 0.3712 0.4685 -0.0223 0.0837  -0.0033 59  SER A OG  
517  N N   . ILE A 59  ? 0.4660 0.2914 0.3442 -0.0476 0.0776  -0.0138 60  ILE A N   
518  C CA  . ILE A 59  ? 0.4588 0.2887 0.3346 -0.0618 0.0830  -0.0221 60  ILE A CA  
519  C C   . ILE A 59  ? 0.4904 0.3256 0.3617 -0.0680 0.0824  -0.0217 60  ILE A C   
520  O O   . ILE A 59  ? 0.5175 0.3403 0.3784 -0.0785 0.0910  -0.0252 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4679 0.3201 0.3557 -0.0654 0.0790  -0.0299 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4644 0.3093 0.3535 -0.0634 0.0827  -0.0327 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.4550 0.3180 0.3436 -0.0782 0.0812  -0.0393 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4847 0.3490 0.3812 -0.0652 0.0771  -0.0379 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.4253 0.2785 0.3043 -0.0628 0.0737  -0.0186 61  PHE A N   
526  C CA  . PHE A 60  ? 0.4226 0.2835 0.2994 -0.0698 0.0741  -0.0206 61  PHE A CA  
527  C C   . PHE A 60  ? 0.4909 0.3317 0.3505 -0.0691 0.0771  -0.0127 61  PHE A C   
528  O O   . PHE A 60  ? 0.4986 0.3432 0.3536 -0.0770 0.0797  -0.0151 61  PHE A O   
529  C CB  . PHE A 60  ? 0.4157 0.3038 0.3073 -0.0667 0.0646  -0.0227 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.4170 0.3206 0.3202 -0.0687 0.0614  -0.0304 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.4614 0.3701 0.3666 -0.0792 0.0659  -0.0405 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.4234 0.3365 0.3342 -0.0607 0.0537  -0.0282 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.4631 0.3857 0.3766 -0.0802 0.0609  -0.0473 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.4478 0.3718 0.3644 -0.0627 0.0501  -0.0344 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.4303 0.3589 0.3478 -0.0717 0.0528  -0.0434 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4752 0.2934 0.3240 -0.0600 0.0770  -0.0041 62  THR A N   
537  C CA  . THR A 61  ? 0.4959 0.2888 0.3227 -0.0592 0.0795  0.0042  62  THR A CA  
538  C C   . THR A 61  ? 0.5977 0.3605 0.4064 -0.0683 0.0919  0.0026  62  THR A C   
539  O O   . THR A 61  ? 0.6112 0.3469 0.3962 -0.0712 0.0966  0.0086  62  THR A O   
540  C CB  . THR A 61  ? 0.6020 0.3876 0.4257 -0.0428 0.0702  0.0147  62  THR A CB  
541  O OG1 . THR A 61  ? 0.5671 0.3479 0.3996 -0.0335 0.0692  0.0148  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.5361 0.3482 0.3724 -0.0370 0.0596  0.0161  62  THR A CG2 
543  N N   . ASP A 62  ? 0.5487 0.3146 0.3663 -0.0742 0.0977  -0.0058 63  ASP A N   
544  C CA  . ASP A 62  ? 0.5846 0.3235 0.3865 -0.0852 0.1109  -0.0096 63  ASP A CA  
545  C C   . ASP A 62  ? 0.6535 0.3982 0.4500 -0.1031 0.1193  -0.0177 63  ASP A C   
546  O O   . ASP A 62  ? 0.6019 0.3785 0.4170 -0.1086 0.1164  -0.0269 63  ASP A O   
547  C CB  . ASP A 62  ? 0.6015 0.3447 0.4152 -0.0868 0.1143  -0.0175 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.7749 0.4929 0.5735 -0.1006 0.1289  -0.0236 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.8509 0.5343 0.6326 -0.0960 0.1341  -0.0174 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.7846 0.5168 0.5881 -0.1161 0.1351  -0.0351 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.6935 0.4062 0.4640 -0.1124 0.1301  -0.0151 64  GLN A N   
552  C CA  . GLN A 63  ? 0.7134 0.4277 0.4757 -0.1312 0.1408  -0.0235 64  GLN A CA  
553  C C   . GLN A 63  ? 0.7472 0.4853 0.5276 -0.1462 0.1479  -0.0408 64  GLN A C   
554  O O   . GLN A 63  ? 0.7703 0.5276 0.5572 -0.1588 0.1522  -0.0508 64  GLN A O   
555  C CB  . GLN A 63  ? 0.7878 0.4563 0.5138 -0.1393 0.1528  -0.0169 64  GLN A CB  
556  C CG  . GLN A 63  ? 1.0024 0.6522 0.7079 -0.1277 0.1448  -0.0016 64  GLN A CG  
557  N N   . LEU A 64  ? 0.6474 0.3856 0.4364 -0.1452 0.1490  -0.0455 65  LEU A N   
558  C CA  . LEU A 64  ? 0.6234 0.3868 0.4302 -0.1580 0.1531  -0.0623 65  LEU A CA  
559  C C   . LEU A 64  ? 0.6499 0.4526 0.4841 -0.1484 0.1384  -0.0659 65  LEU A C   
560  O O   . LEU A 64  ? 0.6582 0.4912 0.5095 -0.1560 0.1365  -0.0782 65  LEU A O   
561  C CB  . LEU A 64  ? 0.6450 0.3875 0.4446 -0.1645 0.1629  -0.0673 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.7537 0.4615 0.5288 -0.1812 0.1811  -0.0708 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.7768 0.4646 0.5466 -0.1853 0.1895  -0.0755 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.8052 0.5327 0.5861 -0.2019 0.1904  -0.0865 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.5603 0.3618 0.3986 -0.1320 0.1283  -0.0563 66  LYS A N   
566  C CA  . LYS A 65  ? 0.5263 0.3588 0.3857 -0.1239 0.1157  -0.0591 66  LYS A CA  
567  C C   . LYS A 65  ? 0.5771 0.4340 0.4480 -0.1183 0.1055  -0.0572 66  LYS A C   
568  O O   . LYS A 65  ? 0.5534 0.4375 0.4411 -0.1163 0.0968  -0.0634 66  LYS A O   
569  C CB  . LYS A 65  ? 0.5351 0.3586 0.3949 -0.1108 0.1106  -0.0515 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.5593 0.3622 0.4111 -0.1162 0.1204  -0.0558 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.5527 0.3515 0.4084 -0.1036 0.1157  -0.0505 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.6228 0.3956 0.4689 -0.1068 0.1264  -0.0533 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.6768 0.4150 0.5065 -0.1016 0.1327  -0.0443 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.5740 0.4198 0.4342 -0.1163 0.1067  -0.0493 67  CYS A N   
575  C CA  . CYS A 66  ? 0.5707 0.4374 0.4402 -0.1120 0.0986  -0.0480 67  CYS A CA  
576  C C   . CYS A 66  ? 0.6112 0.5066 0.4973 -0.1219 0.0987  -0.0626 67  CYS A C   
577  O O   . CYS A 66  ? 0.6051 0.5235 0.5054 -0.1162 0.0896  -0.0641 67  CYS A O   
578  C CB  . CYS A 66  ? 0.6090 0.4563 0.4601 -0.1115 0.1019  -0.0387 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.7051 0.5313 0.5358 -0.1313 0.1193  -0.0449 67  CYS A SG  
580  N N   . ASN A 67  ? 0.5596 0.4537 0.4447 -0.1366 0.1094  -0.0743 68  ASN A N   
581  C CA  . ASN A 67  ? 0.5563 0.4785 0.4587 -0.1473 0.1109  -0.0910 68  ASN A CA  
582  C C   . ASN A 67  ? 0.5767 0.5221 0.4971 -0.1461 0.1031  -0.1012 68  ASN A C   
583  O O   . ASN A 67  ? 0.5550 0.5275 0.4930 -0.1527 0.1017  -0.1161 68  ASN A O   
584  C CB  . ASN A 67  ? 0.5987 0.5078 0.4895 -0.1663 0.1282  -0.0999 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.8114 0.7013 0.6836 -0.1691 0.1350  -0.0918 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.8077 0.6654 0.6552 -0.1782 0.1477  -0.0876 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.6695 0.5760 0.5503 -0.1612 0.1265  -0.0887 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.5303 0.4660 0.4465 -0.1377 0.0978  -0.0941 69  LEU A N   
589  C CA  . LEU A 68  ? 0.5114 0.4657 0.4397 -0.1367 0.0899  -0.1027 69  LEU A CA  
590  C C   . LEU A 68  ? 0.5285 0.5068 0.4715 -0.1247 0.0738  -0.1018 69  LEU A C   
591  O O   . LEU A 68  ? 0.5119 0.4848 0.4520 -0.1139 0.0683  -0.0901 69  LEU A O   
592  C CB  . LEU A 68  ? 0.5242 0.4582 0.4408 -0.1334 0.0914  -0.0963 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.6043 0.5109 0.5053 -0.1443 0.1071  -0.0976 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.6125 0.5001 0.5044 -0.1382 0.1076  -0.0910 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.6299 0.5482 0.5366 -0.1614 0.1151  -0.1152 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4796 0.4836 0.4378 -0.1263 0.0659  -0.1145 70  SER A N   
597  N N   B SER A 69  ? 0.4775 0.4813 0.4356 -0.1264 0.0660  -0.1146 70  SER A N   
598  C CA  A SER A 69  ? 0.4629 0.4869 0.4333 -0.1143 0.0496  -0.1143 70  SER A CA  
599  C CA  B SER A 69  ? 0.4600 0.4847 0.4308 -0.1147 0.0496  -0.1149 70  SER A CA  
600  C C   A SER A 69  ? 0.4776 0.4967 0.4408 -0.1071 0.0401  -0.1095 70  SER A C   
601  C C   B SER A 69  ? 0.4766 0.4959 0.4400 -0.1073 0.0401  -0.1097 70  SER A C   
602  O O   A SER A 69  ? 0.4452 0.4718 0.4114 -0.0963 0.0270  -0.1058 70  SER A O   
603  O O   B SER A 69  ? 0.4443 0.4713 0.4107 -0.0965 0.0270  -0.1060 70  SER A O   
604  C CB  A SER A 69  ? 0.5107 0.5657 0.5021 -0.1180 0.0445  -0.1312 70  SER A CB  
605  C CB  B SER A 69  ? 0.5041 0.5597 0.4956 -0.1191 0.0449  -0.1324 70  SER A CB  
606  O OG  A SER A 69  ? 0.6220 0.6876 0.6179 -0.1270 0.0454  -0.1444 70  SER A OG  
607  O OG  B SER A 69  ? 0.5975 0.6598 0.5967 -0.1254 0.0534  -0.1376 70  SER A OG  
608  N N   . VAL A 70  ? 0.4447 0.4493 0.3968 -0.1140 0.0476  -0.1102 71  VAL A N   
609  C CA  . VAL A 70  ? 0.4453 0.4426 0.3876 -0.1102 0.0417  -0.1069 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4711 0.4405 0.3983 -0.1116 0.0533  -0.0977 71  VAL A C   
611  O O   . VAL A 70  ? 0.4675 0.4246 0.3905 -0.1208 0.0663  -0.1007 71  VAL A O   
612  C CB  . VAL A 70  ? 0.5113 0.5239 0.4573 -0.1176 0.0375  -0.1212 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.5219 0.5250 0.4539 -0.1145 0.0316  -0.1174 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.5042 0.5470 0.4683 -0.1149 0.0248  -0.1322 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3873 0.3464 0.3067 -0.1027 0.0490  -0.0877 72  ILE A N   
616  C CA  . ILE A 71  ? 0.3974 0.3333 0.3058 -0.1019 0.0582  -0.0806 72  ILE A CA  
617  C C   . ILE A 71  ? 0.4473 0.3810 0.3476 -0.1018 0.0544  -0.0822 72  ILE A C   
618  O O   . ILE A 71  ? 0.4447 0.3849 0.3434 -0.0953 0.0438  -0.0787 72  ILE A O   
619  C CB  . ILE A 71  ? 0.4212 0.3472 0.3291 -0.0920 0.0588  -0.0680 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.4309 0.3562 0.3424 -0.0931 0.0630  -0.0660 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.4443 0.3500 0.3442 -0.0887 0.0662  -0.0621 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.4855 0.3939 0.3898 -0.1026 0.0767  -0.0692 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.4240 0.3455 0.3169 -0.1095 0.0639  -0.0872 73  ASN A N   
624  C CA  . ASN A 72  ? 0.4266 0.3437 0.3093 -0.1115 0.0627  -0.0898 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4629 0.3614 0.3401 -0.1066 0.0705  -0.0824 73  ASN A C   
626  O O   . ASN A 72  ? 0.4519 0.3350 0.3291 -0.1078 0.0819  -0.0816 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4799 0.3970 0.3585 -0.1240 0.0686  -0.1022 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.7012 0.6401 0.5885 -0.1298 0.0616  -0.1126 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.5894 0.5456 0.4793 -0.1255 0.0473  -0.1142 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.6337 0.5718 0.5254 -0.1399 0.0718  -0.1207 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.4112 0.3101 0.2833 -0.1013 0.0648  -0.0778 74  LEU A N   
632  C CA  . LEU A 73  ? 0.4154 0.3006 0.2851 -0.0972 0.0725  -0.0732 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4727 0.3472 0.3326 -0.1053 0.0813  -0.0807 74  LEU A C   
634  O O   . LEU A 73  ? 0.4731 0.3522 0.3249 -0.1137 0.0786  -0.0885 74  LEU A O   
635  C CB  . LEU A 73  ? 0.4063 0.2956 0.2743 -0.0904 0.0654  -0.0665 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.4435 0.3425 0.3207 -0.0821 0.0570  -0.0590 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.4518 0.3498 0.3270 -0.0768 0.0548  -0.0534 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.4207 0.3171 0.3085 -0.0783 0.0620  -0.0557 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.4368 0.2982 0.2982 -0.1023 0.0915  -0.0795 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4537 0.3035 0.3073 -0.1092 0.1020  -0.0873 75  ASP A CA  
641  C C   . ASP A 74  ? 0.5171 0.3722 0.3555 -0.1162 0.0965  -0.0914 75  ASP A C   
642  O O   . ASP A 74  ? 0.5031 0.3642 0.3383 -0.1121 0.0884  -0.0858 75  ASP A O   
643  C CB  . ASP A 74  ? 0.4733 0.3130 0.3347 -0.1017 0.1111  -0.0849 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.6230 0.4496 0.4800 -0.1074 0.1242  -0.0938 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.6545 0.4824 0.5000 -0.1149 0.1254  -0.0992 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.6522 0.4653 0.5156 -0.1043 0.1333  -0.0954 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.5352 0.3867 0.3620 -0.1271 0.1002  -0.1009 76  PRO A N   
648  C CA  . PRO A 75  ? 0.5501 0.4047 0.3581 -0.1337 0.0932  -0.1041 76  PRO A CA  
649  C C   . PRO A 75  ? 0.5960 0.4429 0.3945 -0.1333 0.0974  -0.1018 76  PRO A C   
650  O O   . PRO A 75  ? 0.6125 0.4595 0.3925 -0.1372 0.0897  -0.1013 76  PRO A O   
651  C CB  . PRO A 75  ? 0.5946 0.4456 0.3931 -0.1460 0.0988  -0.1159 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.6538 0.4942 0.4650 -0.1461 0.1132  -0.1190 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5691 0.4122 0.3971 -0.1346 0.1106  -0.1093 76  PRO A CD  
654  N N   . GLU A 76  ? 0.5577 0.3975 0.3681 -0.1287 0.1093  -0.1011 77  GLU A N   
655  C CA  . GLU A 76  ? 0.5805 0.4156 0.3858 -0.1292 0.1154  -0.1011 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5771 0.4193 0.3836 -0.1221 0.1053  -0.0915 77  GLU A C   
657  O O   . GLU A 76  ? 0.5669 0.4056 0.3644 -0.1249 0.1085  -0.0914 77  GLU A O   
658  C CB  . GLU A 76  ? 0.6105 0.4396 0.4335 -0.1245 0.1301  -0.1048 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.8782 0.7016 0.6952 -0.1304 0.1421  -0.1121 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.2628 1.0760 1.0648 -0.1430 0.1521  -0.1235 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.2632 1.0698 1.0749 -0.1424 0.1606  -0.1292 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.1963 1.0061 0.9749 -0.1538 0.1516  -0.1267 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.4947 0.3462 0.3121 -0.1140 0.0947  -0.0843 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4791 0.3370 0.2990 -0.1071 0.0858  -0.0757 78  ILE A CA  
665  C C   . ILE A 77  ? 0.5388 0.3946 0.3361 -0.1116 0.0749  -0.0737 78  ILE A C   
666  O O   . ILE A 77  ? 0.5221 0.3805 0.3099 -0.1143 0.0657  -0.0755 78  ILE A O   
667  C CB  . ILE A 77  ? 0.4975 0.3650 0.3360 -0.0974 0.0793  -0.0695 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.5064 0.3712 0.3630 -0.0919 0.0895  -0.0702 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4532 0.3272 0.2937 -0.0911 0.0702  -0.0617 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.5833 0.4459 0.4486 -0.0882 0.0988  -0.0714 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.5530 0.4037 0.3414 -0.1121 0.0758  -0.0704 79  ASN A N   
672  C CA  . ASN A 78  ? 0.5683 0.4110 0.3312 -0.1158 0.0664  -0.0670 79  ASN A CA  
673  C C   . ASN A 78  ? 0.5602 0.4103 0.3281 -0.1064 0.0511  -0.0590 79  ASN A C   
674  O O   . ASN A 78  ? 0.5190 0.3755 0.3039 -0.0996 0.0521  -0.0546 79  ASN A O   
675  C CB  . ASN A 78  ? 0.5923 0.4241 0.3435 -0.1217 0.0766  -0.0675 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.8095 0.6270 0.5296 -0.1261 0.0682  -0.0629 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.6755 0.4909 0.3947 -0.1220 0.0638  -0.0565 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.7112 0.5169 0.4033 -0.1344 0.0652  -0.0658 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.5375 0.3876 0.2913 -0.1057 0.0366  -0.0580 80  PRO A N   
680  C CA  . PRO A 79  ? 0.5209 0.3786 0.2814 -0.0960 0.0222  -0.0520 80  PRO A CA  
681  C C   . PRO A 79  ? 0.5627 0.4112 0.3162 -0.0928 0.0209  -0.0446 80  PRO A C   
682  O O   . PRO A 79  ? 0.5282 0.3857 0.2982 -0.0847 0.0163  -0.0405 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5735 0.4309 0.3170 -0.0963 0.0072  -0.0542 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.6374 0.4940 0.3745 -0.1059 0.0145  -0.0626 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5904 0.4351 0.3228 -0.1130 0.0319  -0.0634 80  PRO A CD  
686  N N   . GLU A 80  ? 0.5449 0.3749 0.2729 -0.1005 0.0261  -0.0438 81  GLU A N   
687  C CA  . GLU A 80  ? 0.5535 0.3724 0.2726 -0.0999 0.0271  -0.0379 81  GLU A CA  
688  C C   . GLU A 80  ? 0.5552 0.3860 0.3019 -0.0977 0.0390  -0.0386 81  GLU A C   
689  O O   . GLU A 80  ? 0.5220 0.3561 0.2775 -0.0918 0.0352  -0.0339 81  GLU A O   
690  C CB  . GLU A 80  ? 0.6093 0.4036 0.2922 -0.1108 0.0319  -0.0377 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.7287 0.5083 0.3985 -0.1105 0.0311  -0.0313 81  GLU A CG  
692  C CD  . GLU A 80  ? 1.0803 0.8333 0.7146 -0.1235 0.0402  -0.0312 81  GLU A CD  
693  O OE1 . GLU A 80  ? 1.1111 0.8441 0.7224 -0.1233 0.0342  -0.0246 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 0.9736 0.7240 0.6021 -0.1345 0.0541  -0.0381 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.5144 0.3515 0.2745 -0.1018 0.0524  -0.0448 82  GLY A N   
696  C CA  . GLY A 81  ? 0.4877 0.3375 0.2751 -0.0980 0.0619  -0.0463 82  GLY A CA  
697  C C   . GLY A 81  ? 0.4868 0.3517 0.2970 -0.0869 0.0533  -0.0421 82  GLY A C   
698  O O   . GLY A 81  ? 0.4595 0.3319 0.2839 -0.0818 0.0533  -0.0392 82  GLY A O   
699  N N   . PHE A 82  ? 0.4376 0.3073 0.2504 -0.0841 0.0461  -0.0425 83  PHE A N   
700  C CA  . PHE A 82  ? 0.4056 0.2888 0.2378 -0.0755 0.0391  -0.0395 83  PHE A CA  
701  C C   . PHE A 82  ? 0.4379 0.3216 0.2665 -0.0705 0.0282  -0.0340 83  PHE A C   
702  O O   . PHE A 82  ? 0.4093 0.3020 0.2537 -0.0646 0.0271  -0.0310 83  PHE A O   
703  C CB  . PHE A 82  ? 0.4252 0.3139 0.2603 -0.0759 0.0349  -0.0431 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.4198 0.3215 0.2742 -0.0690 0.0306  -0.0411 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.4542 0.3598 0.3249 -0.0660 0.0384  -0.0404 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.4252 0.3339 0.2805 -0.0649 0.0185  -0.0397 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.4556 0.3704 0.3398 -0.0609 0.0350  -0.0380 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.4332 0.3539 0.3057 -0.0599 0.0162  -0.0388 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.4176 0.3404 0.3028 -0.0587 0.0248  -0.0376 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.4568 0.3295 0.2635 -0.0725 0.0197  -0.0326 84  CYS A N   
711  C CA  . CYS A 83  ? 0.4851 0.3540 0.2858 -0.0670 0.0089  -0.0276 84  CYS A CA  
712  C C   . CYS A 83  ? 0.4898 0.3554 0.2939 -0.0672 0.0155  -0.0244 84  CYS A C   
713  O O   . CYS A 83  ? 0.4569 0.3295 0.2728 -0.0609 0.0107  -0.0216 84  CYS A O   
714  C CB  . CYS A 83  ? 0.5506 0.4028 0.3222 -0.0688 -0.0009 -0.0263 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.6290 0.4739 0.3928 -0.0595 -0.0164 -0.0204 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4610 0.3174 0.2560 -0.0753 0.0273  -0.0263 85  ILE A N   
717  C CA  . ILE A 84  ? 0.4369 0.2919 0.2358 -0.0779 0.0354  -0.0259 85  ILE A CA  
718  C C   . ILE A 84  ? 0.4251 0.3011 0.2549 -0.0713 0.0379  -0.0267 85  ILE A C   
719  O O   . ILE A 84  ? 0.4081 0.2887 0.2459 -0.0683 0.0364  -0.0246 85  ILE A O   
720  C CB  . ILE A 84  ? 0.4832 0.3278 0.2692 -0.0892 0.0492  -0.0309 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.5253 0.3436 0.2732 -0.0969 0.0463  -0.0284 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4730 0.3256 0.2740 -0.0920 0.0602  -0.0342 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.6025 0.4096 0.3334 -0.1092 0.0589  -0.0342 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3735 0.2600 0.2182 -0.0690 0.0412  -0.0295 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3584 0.2612 0.2283 -0.0621 0.0426  -0.0293 86  LEU A CA  
726  C C   . LEU A 85  ? 0.3987 0.3093 0.2764 -0.0552 0.0324  -0.0252 86  LEU A C   
727  O O   . LEU A 85  ? 0.3706 0.2911 0.2622 -0.0506 0.0318  -0.0237 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3638 0.2708 0.2444 -0.0616 0.0497  -0.0331 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.4330 0.3372 0.3139 -0.0671 0.0619  -0.0391 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.4414 0.3463 0.3306 -0.0658 0.0680  -0.0431 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.4402 0.3554 0.3370 -0.0648 0.0660  -0.0408 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3644 0.2720 0.2338 -0.0545 0.0244  -0.0247 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3538 0.2702 0.2316 -0.0485 0.0153  -0.0229 87  LEU A CA  
734  C C   . LEU A 86  ? 0.3907 0.3043 0.2656 -0.0462 0.0109  -0.0198 87  LEU A C   
735  O O   . LEU A 86  ? 0.3589 0.2823 0.2467 -0.0420 0.0091  -0.0187 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3572 0.2728 0.2280 -0.0486 0.0074  -0.0252 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.4047 0.3326 0.2877 -0.0430 -0.0008 -0.0260 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.3939 0.3330 0.2941 -0.0422 0.0051  -0.0266 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.4227 0.3530 0.3008 -0.0428 -0.0097 -0.0305 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3854 0.2836 0.2410 -0.0499 0.0100  -0.0187 88  ASP A N   
741  C CA  . ASP A 87  ? 0.3894 0.2802 0.2390 -0.0492 0.0078  -0.0161 88  ASP A CA  
742  C C   . ASP A 87  ? 0.4086 0.3092 0.2731 -0.0504 0.0160  -0.0169 88  ASP A C   
743  O O   . ASP A 87  ? 0.3958 0.3015 0.2678 -0.0471 0.0130  -0.0159 88  ASP A O   
744  C CB  . ASP A 87  ? 0.4447 0.3125 0.2666 -0.0552 0.0083  -0.0146 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.6458 0.5016 0.4498 -0.0516 -0.0041 -0.0127 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.6525 0.5202 0.4691 -0.0437 -0.0136 -0.0135 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.6653 0.5002 0.4424 -0.0567 -0.0045 -0.0111 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3755 0.2797 0.2449 -0.0548 0.0260  -0.0199 89  PHE A N   
749  C CA  . PHE A 88  ? 0.3402 0.2576 0.2269 -0.0547 0.0325  -0.0222 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3361 0.2696 0.2416 -0.0468 0.0275  -0.0205 89  PHE A C   
751  O O   . PHE A 88  ? 0.3122 0.2544 0.2269 -0.0451 0.0268  -0.0206 89  PHE A O   
752  C CB  . PHE A 88  ? 0.3450 0.2658 0.2374 -0.0586 0.0428  -0.0271 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.3378 0.2763 0.2523 -0.0552 0.0467  -0.0302 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3661 0.3095 0.2846 -0.0591 0.0506  -0.0335 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3617 0.3114 0.2921 -0.0477 0.0455  -0.0298 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.3521 0.3149 0.2924 -0.0552 0.0521  -0.0373 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3844 0.3500 0.3338 -0.0428 0.0464  -0.0321 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3511 0.3250 0.3066 -0.0462 0.0491  -0.0362 89  PHE A CZ  
759  N N   . MET A 89  ? 0.3064 0.2433 0.2161 -0.0432 0.0249  -0.0196 90  MET A N   
760  C CA  . MET A 89  ? 0.2906 0.2395 0.2138 -0.0374 0.0214  -0.0180 90  MET A CA  
761  C C   . MET A 89  ? 0.3324 0.2846 0.2566 -0.0353 0.0151  -0.0166 90  MET A C   
762  O O   . MET A 89  ? 0.3201 0.2823 0.2543 -0.0327 0.0145  -0.0161 90  MET A O   
763  C CB  . MET A 89  ? 0.3024 0.2503 0.2250 -0.0364 0.0199  -0.0179 90  MET A CB  
764  C CG  . MET A 89  ? 0.3270 0.2711 0.2501 -0.0378 0.0267  -0.0196 90  MET A CG  
765  S SD  . MET A 89  ? 0.3796 0.3220 0.3021 -0.0381 0.0260  -0.0204 90  MET A SD  
766  C CE  . MET A 89  ? 0.3942 0.3277 0.3137 -0.0410 0.0350  -0.0234 90  MET A CE  
767  N N   . TYR A 90  ? 0.3003 0.2435 0.2136 -0.0360 0.0098  -0.0164 91  TYR A N   
768  C CA  . TYR A 90  ? 0.3010 0.2458 0.2156 -0.0330 0.0034  -0.0162 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3667 0.3044 0.2755 -0.0350 0.0044  -0.0159 91  TYR A C   
770  O O   . TYR A 90  ? 0.3550 0.2929 0.2653 -0.0324 0.0000  -0.0162 91  TYR A O   
771  C CB  . TYR A 90  ? 0.3294 0.2686 0.2370 -0.0305 -0.0045 -0.0170 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.3411 0.2921 0.2592 -0.0286 -0.0063 -0.0195 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3634 0.3143 0.2800 -0.0313 -0.0031 -0.0206 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.3465 0.3082 0.2755 -0.0254 -0.0099 -0.0220 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.3647 0.3248 0.2897 -0.0315 -0.0031 -0.0238 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.3540 0.3261 0.2917 -0.0258 -0.0100 -0.0258 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.3859 0.3567 0.3212 -0.0292 -0.0062 -0.0265 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.3526 0.3324 0.2954 -0.0313 -0.0052 -0.0313 91  TYR A OH  
779  N N   . THR A 91  ? 0.3267 0.2577 0.2289 -0.0406 0.0112  -0.0164 92  THR A N   
780  C CA  . THR A 91  ? 0.3424 0.2641 0.2366 -0.0448 0.0138  -0.0170 92  THR A CA  
781  C C   . THR A 91  ? 0.3704 0.3002 0.2724 -0.0504 0.0229  -0.0207 92  THR A C   
782  O O   . THR A 91  ? 0.3673 0.2928 0.2659 -0.0548 0.0257  -0.0226 92  THR A O   
783  C CB  . THR A 91  ? 0.4015 0.2986 0.2709 -0.0489 0.0132  -0.0153 92  THR A CB  
784  O OG1 . THR A 91  ? 0.4083 0.3010 0.2707 -0.0550 0.0205  -0.0166 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.4213 0.3090 0.2812 -0.0425 0.0021  -0.0126 92  THR A CG2 
786  N N   A SER A 92  ? 0.3151 0.2561 0.2276 -0.0504 0.0277  -0.0227 93  SER A N   
787  N N   B SER A 92  ? 0.3160 0.2565 0.2281 -0.0505 0.0278  -0.0226 93  SER A N   
788  C CA  A SER A 92  ? 0.3092 0.2609 0.2324 -0.0547 0.0362  -0.0282 93  SER A CA  
789  C CA  B SER A 92  ? 0.3097 0.2614 0.2329 -0.0546 0.0361  -0.0281 93  SER A CA  
790  C C   A SER A 92  ? 0.3549 0.2918 0.2630 -0.0647 0.0450  -0.0315 93  SER A C   
791  C C   B SER A 92  ? 0.3713 0.3084 0.2795 -0.0649 0.0451  -0.0316 93  SER A C   
792  O O   A SER A 92  ? 0.3415 0.2877 0.2589 -0.0695 0.0536  -0.0381 93  SER A O   
793  O O   B SER A 92  ? 0.3675 0.3139 0.2849 -0.0702 0.0535  -0.0383 93  SER A O   
794  C CB  A SER A 92  ? 0.3171 0.2822 0.2522 -0.0551 0.0361  -0.0312 93  SER A CB  
795  C CB  B SER A 92  ? 0.3256 0.2925 0.2625 -0.0538 0.0353  -0.0307 93  SER A CB  
796  O OG  A SER A 92  ? 0.2907 0.2660 0.2346 -0.0477 0.0283  -0.0281 93  SER A OG  
797  O OG  B SER A 92  ? 0.3789 0.3360 0.3060 -0.0611 0.0386  -0.0331 93  SER A OG  
798  N N   A ARG A 93  ? 0.3484 0.2624 0.2327 -0.0678 0.0429  -0.0277 94  ARG A N   
799  N N   B ARG A 93  ? 0.3545 0.2690 0.2393 -0.0677 0.0430  -0.0278 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3671 0.2619 0.2305 -0.0785 0.0512  -0.0300 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3763 0.2704 0.2389 -0.0784 0.0509  -0.0297 94  ARG A CA  
802  C C   A ARG A 93  ? 0.4263 0.3153 0.2816 -0.0797 0.0533  -0.0300 94  ARG A C   
803  C C   B ARG A 93  ? 0.4310 0.3189 0.2851 -0.0800 0.0533  -0.0298 94  ARG A C   
804  O O   A ARG A 93  ? 0.3977 0.2828 0.2479 -0.0736 0.0449  -0.0254 94  ARG A O   
805  O O   B ARG A 93  ? 0.4144 0.2978 0.2627 -0.0740 0.0448  -0.0252 94  ARG A O   
806  C CB  A ARG A 93  ? 0.4132 0.2816 0.2501 -0.0816 0.0474  -0.0255 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.4134 0.2820 0.2507 -0.0802 0.0457  -0.0248 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4684 0.3388 0.3107 -0.0825 0.0474  -0.0267 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.4970 0.3690 0.3413 -0.0790 0.0438  -0.0252 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.6147 0.4597 0.4345 -0.0797 0.0391  -0.0207 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5567 0.4175 0.3904 -0.0915 0.0550  -0.0300 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.7747 0.5880 0.5612 -0.0879 0.0428  -0.0184 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.5793 0.4439 0.4203 -0.0913 0.0539  -0.0315 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.9224 0.7158 0.6905 -0.0994 0.0523  -0.0205 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.7476 0.5867 0.5676 -0.0945 0.0531  -0.0290 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.7574 0.5620 0.5398 -0.1040 0.0588  -0.0260 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.6146 0.4591 0.4434 -0.0947 0.0531  -0.0317 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.7508 0.5122 0.4843 -0.1073 0.0555  -0.0176 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5599 0.3664 0.3482 -0.0975 0.0522  -0.0240 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.3927 0.2821 0.2475 -0.0885 0.0654  -0.0366 95  LEU A N   
821  C CA  . LEU A 94  ? 0.3901 0.2741 0.2375 -0.0915 0.0699  -0.0385 95  LEU A CA  
822  C C   . LEU A 94  ? 0.4740 0.3322 0.2898 -0.1043 0.0772  -0.0396 95  LEU A C   
823  O O   . LEU A 94  ? 0.4647 0.3201 0.2772 -0.1148 0.0887  -0.0457 95  LEU A O   
824  C CB  . LEU A 94  ? 0.3843 0.2906 0.2584 -0.0904 0.0785  -0.0466 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.4283 0.3315 0.2997 -0.0920 0.0838  -0.0498 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.4077 0.3110 0.2803 -0.0823 0.0732  -0.0433 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.4400 0.3630 0.3374 -0.0915 0.0939  -0.0597 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4846 0.3238 0.2759 -0.1041 0.0708  -0.0343 96  ASN A N   
829  C CA  . ASN A 95  ? 0.5259 0.3360 0.2805 -0.1161 0.0760  -0.0339 96  ASN A CA  
830  C C   . ASN A 95  ? 0.5854 0.3978 0.3392 -0.1250 0.0890  -0.0419 96  ASN A C   
831  O O   . ASN A 95  ? 0.5888 0.3933 0.3291 -0.1251 0.0859  -0.0406 96  ASN A O   
832  C CB  . ASN A 95  ? 0.5947 0.3833 0.3222 -0.1108 0.0611  -0.0249 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.8473 0.6017 0.5313 -0.1220 0.0641  -0.0228 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.7258 0.4667 0.3951 -0.1351 0.0774  -0.0265 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.7803 0.5199 0.4418 -0.1179 0.0519  -0.0173 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.5407 0.3670 0.3123 -0.1319 0.1033  -0.0514 97  LEU A N   
837  C CA  . LEU A 96  ? 0.5518 0.3845 0.3292 -0.1399 0.1174  -0.0615 97  LEU A CA  
838  C C   . LEU A 96  ? 0.6241 0.4307 0.3666 -0.1581 0.1303  -0.0655 97  LEU A C   
839  O O   . LEU A 96  ? 0.6201 0.4185 0.3538 -0.1674 0.1375  -0.0678 97  LEU A O   
840  C CB  . LEU A 96  ? 0.5389 0.4031 0.3572 -0.1360 0.1249  -0.0711 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.6051 0.4852 0.4442 -0.1364 0.1354  -0.0817 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.6101 0.4898 0.4511 -0.1264 0.1268  -0.0766 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5794 0.4906 0.4588 -0.1300 0.1392  -0.0905 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.6048 0.3958 0.3239 -0.1642 0.1329  -0.0661 98  ARG A N   
845  C CA  . ARG A 97  ? 0.6565 0.4183 0.3354 -0.1825 0.1447  -0.0690 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6676 0.4352 0.3497 -0.1909 0.1586  -0.0801 98  ARG A C   
847  O O   . ARG A 97  ? 0.6189 0.4043 0.3239 -0.1808 0.1542  -0.0816 98  ARG A O   
848  C CB  . ARG A 97  ? 0.7145 0.4425 0.3488 -0.1819 0.1304  -0.0562 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.7905 0.5096 0.4198 -0.1725 0.1160  -0.0454 98  ARG A CG  
850  C CD  . ARG A 97  ? 1.0284 0.7163 0.6171 -0.1687 0.0996  -0.0335 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.3013 0.9510 0.8399 -0.1851 0.1077  -0.0327 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.5895 1.2103 1.0989 -0.1945 0.1129  -0.0296 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.4659 1.0491 0.9259 -0.2105 0.1208  -0.0286 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.4621 1.0896 0.9896 -0.1891 0.1110  -0.0278 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.6665 0.4178 0.3249 -0.2101 0.1764  -0.0886 99  GLU A N   
856  C CA  . GLU A 98  ? 0.6712 0.4264 0.3305 -0.2201 0.1917  -0.1010 99  GLU A CA  
857  C C   . GLU A 98  ? 0.7359 0.4831 0.3808 -0.2140 0.1808  -0.0952 99  GLU A C   
858  O O   . GLU A 98  ? 0.7258 0.4906 0.3941 -0.2108 0.1862  -0.1034 99  GLU A O   
859  C CB  . GLU A 98  ? 0.7340 0.4639 0.3567 -0.2443 0.2113  -0.1089 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.8882 0.6225 0.5119 -0.2567 0.2298  -0.1238 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.3126 1.0194 0.8955 -0.2827 0.2501  -0.1320 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.2609 0.9291 0.7917 -0.2912 0.2447  -0.1207 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.3211 1.0441 0.9235 -0.2945 0.2717  -0.1502 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.7270 0.4485 0.3353 -0.2117 0.1650  -0.0819 100 GLY A N   
865  C CA  . GLY A 99  ? 0.7447 0.4584 0.3365 -0.2068 0.1529  -0.0768 100 GLY A CA  
866  C C   . GLY A 99  ? 0.7339 0.4734 0.3619 -0.1880 0.1390  -0.0734 100 GLY A C   
867  O O   . GLY A 99  ? 0.7378 0.4776 0.3610 -0.1857 0.1335  -0.0737 100 GLY A O   
868  N N   . ASN A 100 ? 0.6488 0.4097 0.3119 -0.1756 0.1340  -0.0710 101 ASN A N   
869  C CA  . ASN A 100 ? 0.6001 0.3824 0.2939 -0.1590 0.1215  -0.0673 101 ASN A CA  
870  C C   . ASN A 100 ? 0.6080 0.4190 0.3473 -0.1516 0.1296  -0.0749 101 ASN A C   
871  O O   . ASN A 100 ? 0.5703 0.3962 0.3327 -0.1390 0.1212  -0.0723 101 ASN A O   
872  C CB  . ASN A 100 ? 0.5953 0.3747 0.2858 -0.1476 0.1027  -0.0552 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.6990 0.4858 0.4052 -0.1446 0.1039  -0.0534 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5581 0.3632 0.2919 -0.1453 0.1151  -0.0609 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.6270 0.4009 0.3173 -0.1403 0.0915  -0.0441 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5702 0.3890 0.3223 -0.1589 0.1451  -0.0843 102 ILE A N   
877  C CA  . ILE A 101 ? 0.5402 0.3874 0.3364 -0.1498 0.1503  -0.0915 102 ILE A CA  
878  C C   . ILE A 101 ? 0.5433 0.4016 0.3602 -0.1423 0.1521  -0.0964 102 ILE A C   
879  O O   . ILE A 101 ? 0.4927 0.3685 0.3394 -0.1281 0.1457  -0.0945 102 ILE A O   
880  C CB  . ILE A 101 ? 0.5878 0.4445 0.3963 -0.1596 0.1669  -0.1036 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5664 0.4550 0.4223 -0.1465 0.1672  -0.1097 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.5966 0.4424 0.3881 -0.1765 0.1852  -0.1157 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.6053 0.5084 0.4774 -0.1518 0.1757  -0.1181 102 ILE A CD1 
884  N N   . MET A 102 ? 0.5392 0.3853 0.3383 -0.1519 0.1606  -0.1024 103 MET A N   
885  C CA  . MET A 102 ? 0.5452 0.3986 0.3619 -0.1457 0.1634  -0.1077 103 MET A CA  
886  C C   . MET A 102 ? 0.5653 0.4188 0.3843 -0.1337 0.1472  -0.0972 103 MET A C   
887  O O   . MET A 102 ? 0.5314 0.3972 0.3775 -0.1221 0.1457  -0.0979 103 MET A O   
888  C CB  . MET A 102 ? 0.6122 0.4520 0.4079 -0.1602 0.1770  -0.1176 103 MET A CB  
889  C CG  . MET A 102 ? 0.6988 0.5412 0.4969 -0.1730 0.1964  -0.1313 103 MET A CG  
890  S SD  . MET A 102 ? 0.7481 0.6221 0.5992 -0.1620 0.2045  -0.1423 103 MET A SD  
891  C CE  . MET A 102 ? 0.7120 0.5929 0.5873 -0.1530 0.2102  -0.1512 103 MET A CE  
892  N N   . ALA A 103 ? 0.5482 0.3877 0.3389 -0.1363 0.1351  -0.0878 104 ALA A N   
893  C CA  . ALA A 103 ? 0.5364 0.3780 0.3293 -0.1266 0.1200  -0.0795 104 ALA A CA  
894  C C   . ALA A 103 ? 0.5345 0.3913 0.3529 -0.1132 0.1114  -0.0729 104 ALA A C   
895  O O   . ALA A 103 ? 0.5005 0.3654 0.3361 -0.1039 0.1064  -0.0707 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5696 0.3955 0.3288 -0.1315 0.1082  -0.0727 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4682 0.3274 0.2873 -0.1134 0.1104  -0.0701 105 VAL A N   
898  C CA  . VAL A 104 ? 0.4294 0.3032 0.2711 -0.1020 0.1026  -0.0647 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4534 0.3437 0.3273 -0.0934 0.1085  -0.0699 105 VAL A C   
900  O O   . VAL A 104 ? 0.4269 0.3250 0.3157 -0.0826 0.1004  -0.0647 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4719 0.3437 0.3066 -0.1058 0.1021  -0.0623 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.4310 0.3207 0.2918 -0.0951 0.0965  -0.0592 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.4934 0.3465 0.2965 -0.1098 0.0922  -0.0546 105 VAL A CG2 
904  N N   A MET A 105 ? 0.4320 0.3269 0.3160 -0.0980 0.1222  -0.0804 106 MET A N   
905  N N   B MET A 105 ? 0.4365 0.3314 0.3205 -0.0980 0.1222  -0.0804 106 MET A N   
906  C CA  A MET A 105 ? 0.4264 0.3366 0.3416 -0.0881 0.1269  -0.0865 106 MET A CA  
907  C CA  B MET A 105 ? 0.4369 0.3472 0.3524 -0.0877 0.1264  -0.0861 106 MET A CA  
908  C C   A MET A 105 ? 0.4746 0.3797 0.3941 -0.0811 0.1246  -0.0848 106 MET A C   
909  C C   B MET A 105 ? 0.4724 0.3773 0.3916 -0.0810 0.1243  -0.0845 106 MET A C   
910  O O   A MET A 105 ? 0.4531 0.3657 0.3912 -0.0686 0.1190  -0.0813 106 MET A O   
911  O O   B MET A 105 ? 0.4411 0.3534 0.3789 -0.0685 0.1188  -0.0811 106 MET A O   
912  C CB  A MET A 105 ? 0.4688 0.3852 0.3943 -0.0951 0.1428  -0.1005 106 MET A CB  
913  C CB  B MET A 105 ? 0.4787 0.3962 0.4059 -0.0939 0.1420  -0.1000 106 MET A CB  
914  C CG  A MET A 105 ? 0.5067 0.4412 0.4675 -0.0825 0.1456  -0.1075 106 MET A CG  
915  C CG  B MET A 105 ? 0.5173 0.4525 0.4797 -0.0806 0.1441  -0.1064 106 MET A CG  
916  S SD  A MET A 105 ? 0.5743 0.5189 0.5513 -0.0902 0.1652  -0.1270 106 MET A SD  
917  S SD  B MET A 105 ? 0.5796 0.5305 0.5629 -0.0870 0.1615  -0.1252 106 MET A SD  
918  C CE  A MET A 105 ? 0.5250 0.4828 0.5382 -0.0704 0.1632  -0.1316 106 MET A CE  
919  C CE  B MET A 105 ? 0.5679 0.5014 0.5353 -0.0980 0.1762  -0.1346 106 MET A CE  
920  N N   . ALA A 106 ? 0.4525 0.3434 0.3522 -0.0899 0.1289  -0.0873 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4627 0.3464 0.3632 -0.0862 0.1284  -0.0872 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4762 0.3601 0.3758 -0.0787 0.1146  -0.0762 107 ALA A C   
923  O O   . ALA A 106 ? 0.4504 0.3342 0.3625 -0.0701 0.1132  -0.0744 107 ALA A O   
924  C CB  . ALA A 106 ? 0.4944 0.3640 0.3708 -0.0992 0.1345  -0.0924 107 ALA A CB  
925  N N   . THR A 107 ? 0.4234 0.3067 0.3081 -0.0819 0.1048  -0.0694 108 THR A N   
926  C CA  . THR A 107 ? 0.4147 0.3007 0.3001 -0.0757 0.0925  -0.0608 108 THR A CA  
927  C C   . THR A 107 ? 0.4314 0.3287 0.3383 -0.0641 0.0889  -0.0565 108 THR A C   
928  O O   . THR A 107 ? 0.3981 0.2954 0.3116 -0.0577 0.0847  -0.0525 108 THR A O   
929  C CB  . THR A 107 ? 0.4726 0.3551 0.3380 -0.0806 0.0827  -0.0559 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4742 0.3452 0.3172 -0.0911 0.0857  -0.0603 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4719 0.3584 0.3391 -0.0756 0.0713  -0.0503 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3884 0.2947 0.3049 -0.0624 0.0908  -0.0578 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3628 0.2815 0.2992 -0.0516 0.0864  -0.0546 109 ALA A CA  
934  C C   . ALA A 108 ? 0.4076 0.3267 0.3605 -0.0423 0.0903  -0.0573 109 ALA A C   
935  O O   . ALA A 108 ? 0.3949 0.3164 0.3560 -0.0328 0.0838  -0.0515 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3700 0.2997 0.3137 -0.0535 0.0888  -0.0580 109 ALA A CB  
937  N N   . MET A 109 ? 0.3779 0.2917 0.3331 -0.0452 0.1008  -0.0657 110 MET A N   
938  C CA  . MET A 109 ? 0.3736 0.2842 0.3434 -0.0352 0.1042  -0.0683 110 MET A CA  
939  C C   . MET A 109 ? 0.4098 0.3058 0.3693 -0.0332 0.1003  -0.0617 110 MET A C   
940  O O   . MET A 109 ? 0.4074 0.3000 0.3742 -0.0227 0.0961  -0.0568 110 MET A O   
941  C CB  . MET A 109 ? 0.4143 0.3217 0.3887 -0.0396 0.1175  -0.0803 110 MET A CB  
942  C CG  . MET A 109 ? 0.4671 0.3912 0.4584 -0.0396 0.1232  -0.0893 110 MET A CG  
943  S SD  . MET A 109 ? 0.5706 0.4909 0.5626 -0.0497 0.1411  -0.1051 110 MET A SD  
944  C CE  . MET A 109 ? 0.5432 0.4556 0.5530 -0.0348 0.1436  -0.1084 110 MET A CE  
945  N N   . TYR A 110 ? 0.4002 0.2875 0.3416 -0.0440 0.1014  -0.0618 111 TYR A N   
946  C CA  . TYR A 110 ? 0.3970 0.2727 0.3282 -0.0456 0.0991  -0.0579 111 TYR A CA  
947  C C   . TYR A 110 ? 0.4312 0.3117 0.3634 -0.0401 0.0885  -0.0485 111 TYR A C   
948  O O   . TYR A 110 ? 0.4232 0.2947 0.3552 -0.0355 0.0877  -0.0447 111 TYR A O   
949  C CB  . TYR A 110 ? 0.4142 0.2861 0.3274 -0.0586 0.0999  -0.0612 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.4247 0.2902 0.3287 -0.0625 0.0965  -0.0591 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4727 0.3247 0.3753 -0.0639 0.1039  -0.0627 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.4204 0.2935 0.3175 -0.0655 0.0867  -0.0549 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.4604 0.3076 0.3549 -0.0697 0.1024  -0.0626 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.4272 0.2980 0.3185 -0.0702 0.0843  -0.0556 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4715 0.3299 0.3614 -0.0731 0.0926  -0.0597 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4511 0.3088 0.3357 -0.0799 0.0915  -0.0622 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3796 0.2722 0.3110 -0.0412 0.0814  -0.0452 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3599 0.2587 0.2923 -0.0371 0.0720  -0.0377 112 LEU A CA  
959  C C   . LEU A 111 ? 0.3988 0.3025 0.3444 -0.0257 0.0691  -0.0338 112 LEU A C   
960  O O   . LEU A 111 ? 0.3893 0.2958 0.3344 -0.0222 0.0624  -0.0276 112 LEU A O   
961  C CB  . LEU A 111 ? 0.3426 0.2505 0.2689 -0.0420 0.0656  -0.0362 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3855 0.2893 0.2967 -0.0513 0.0638  -0.0385 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.3933 0.3034 0.2983 -0.0531 0.0559  -0.0359 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.4273 0.3277 0.3354 -0.0530 0.0618  -0.0379 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3642 0.2703 0.3218 -0.0200 0.0738  -0.0383 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3648 0.2780 0.3368 -0.0077 0.0696  -0.0361 113 GLN A CA  
967  C C   . GLN A 112 ? 0.3974 0.3273 0.3740 -0.0072 0.0621  -0.0333 113 GLN A C   
968  O O   . GLN A 112 ? 0.3808 0.3130 0.3565 -0.0022 0.0545  -0.0267 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3872 0.2858 0.3551 0.0004  0.0668  -0.0297 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.4105 0.2897 0.3736 -0.0001 0.0753  -0.0331 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.5608 0.4204 0.5123 0.0037  0.0736  -0.0260 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.4881 0.3477 0.4384 0.0112  0.0660  -0.0188 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.5496 0.3911 0.4901 -0.0029 0.0812  -0.0281 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3608 0.3003 0.3395 -0.0142 0.0653  -0.0387 114 MET A N   
975  C CA  . MET A 113 ? 0.3528 0.3065 0.3350 -0.0160 0.0606  -0.0380 114 MET A CA  
976  C C   . MET A 113 ? 0.4120 0.3796 0.4117 -0.0138 0.0655  -0.0466 114 MET A C   
977  O O   . MET A 113 ? 0.3817 0.3509 0.3799 -0.0227 0.0734  -0.0537 114 MET A O   
978  C CB  . MET A 113 ? 0.3746 0.3233 0.3404 -0.0273 0.0608  -0.0371 114 MET A CB  
979  C CG  . MET A 113 ? 0.3954 0.3353 0.3486 -0.0286 0.0553  -0.0308 114 MET A CG  
980  S SD  . MET A 113 ? 0.4326 0.3666 0.3677 -0.0390 0.0533  -0.0308 114 MET A SD  
981  C CE  . MET A 113 ? 0.3872 0.3318 0.3255 -0.0380 0.0470  -0.0281 114 MET A CE  
982  N N   . GLU A 114 ? 0.3976 0.3743 0.4137 -0.0016 0.0612  -0.0469 115 GLU A N   
983  C CA  . GLU A 114 ? 0.4120 0.4052 0.4506 0.0038  0.0647  -0.0569 115 GLU A CA  
984  C C   . GLU A 114 ? 0.4130 0.4232 0.4590 -0.0050 0.0686  -0.0646 115 GLU A C   
985  O O   . GLU A 114 ? 0.3895 0.4075 0.4469 -0.0088 0.0781  -0.0758 115 GLU A O   
986  C CB  . GLU A 114 ? 0.4421 0.4431 0.4952 0.0201  0.0551  -0.0545 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.6066 0.5870 0.6518 0.0290  0.0531  -0.0480 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3711 0.3863 0.4105 -0.0089 0.0627  -0.0598 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3847 0.4131 0.4291 -0.0184 0.0674  -0.0673 116 HIS A CA  
990  C C   . HIS A 115 ? 0.4096 0.4250 0.4375 -0.0332 0.0785  -0.0711 116 HIS A C   
991  O O   . HIS A 115 ? 0.4126 0.4367 0.4477 -0.0414 0.0881  -0.0817 116 HIS A O   
992  C CB  . HIS A 115 ? 0.4069 0.4411 0.4470 -0.0189 0.0588  -0.0614 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.4604 0.5094 0.5158 -0.0059 0.0484  -0.0595 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4916 0.5624 0.5718 0.0010  0.0481  -0.0693 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4872 0.5322 0.5351 0.0009  0.0379  -0.0496 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4865 0.5644 0.5718 0.0128  0.0361  -0.0639 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4883 0.5501 0.5533 0.0122  0.0304  -0.0519 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.3446 0.3395 0.3502 -0.0370 0.0773  -0.0632 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3558 0.3351 0.3412 -0.0501 0.0857  -0.0655 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.4270 0.4070 0.4204 -0.0526 0.0974  -0.0758 117 VAL A C   
1001 O O   . VAL A 116 ? 0.4025 0.3812 0.3905 -0.0642 0.1081  -0.0841 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.4054 0.3658 0.3672 -0.0522 0.0797  -0.0559 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.4199 0.3639 0.3595 -0.0646 0.0871  -0.0587 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3990 0.3597 0.3543 -0.0507 0.0696  -0.0480 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3832 0.3637 0.3884 -0.0421 0.0962  -0.0760 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3871 0.3687 0.4031 -0.0424 0.1073  -0.0868 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.4461 0.4491 0.4847 -0.0443 0.1151  -0.1001 118 VAL A C   
1008 O O   . VAL A 117 ? 0.4361 0.4381 0.4726 -0.0554 0.1282  -0.1107 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.4180 0.3951 0.4441 -0.0287 0.1037  -0.0844 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.4223 0.4005 0.4619 -0.0281 0.1157  -0.0969 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.4156 0.3725 0.4194 -0.0302 0.0987  -0.0738 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.4155 0.4379 0.4739 -0.0351 0.1071  -0.1002 119 ASP A N   
1013 N N   B ASP A 118 ? 0.4112 0.4340 0.4709 -0.0342 0.1071  -0.1005 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.4179 0.4655 0.5014 -0.0361 0.1125  -0.1139 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.4133 0.4617 0.4990 -0.0347 0.1125  -0.1144 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.4548 0.5011 0.5256 -0.0556 0.1242  -0.1208 119 ASP A C   
1017 C C   B ASP A 118 ? 0.4626 0.5110 0.5372 -0.0540 0.1243  -0.1219 119 ASP A C   
1018 O O   A ASP A 118 ? 0.4563 0.5131 0.5395 -0.0632 0.1375  -0.1357 119 ASP A O   
1019 O O   B ASP A 118 ? 0.4682 0.5282 0.5566 -0.0610 0.1374  -0.1372 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.4365 0.5035 0.5381 -0.0235 0.0992  -0.1107 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.4285 0.4962 0.5320 -0.0222 0.0990  -0.1111 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.6119 0.7095 0.7435 -0.0233 0.1031  -0.1264 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.5814 0.6548 0.7029 -0.0020 0.0889  -0.1087 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.6467 0.7575 0.8019 -0.0175 0.1091  -0.1390 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.6160 0.6876 0.7488 0.0038  0.0946  -0.1156 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.6809 0.7901 0.8136 -0.0289 0.1005  -0.1271 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.6548 0.7330 0.7779 0.0079  0.0755  -0.1003 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.4003 0.4323 0.4457 -0.0639 0.1199  -0.1106 120 THR A N   
1029 N N   B THR A 119 ? 0.4117 0.4455 0.4605 -0.0626 0.1205  -0.1119 120 THR A N   
1030 C CA  A THR A 119 ? 0.4106 0.4354 0.4389 -0.0824 0.1308  -0.1159 120 THR A CA  
1031 C CA  B THR A 119 ? 0.4210 0.4481 0.4529 -0.0809 0.1307  -0.1167 120 THR A CA  
1032 C C   A THR A 119 ? 0.4637 0.4685 0.4703 -0.0951 0.1435  -0.1197 120 THR A C   
1033 C C   B THR A 119 ? 0.4718 0.4784 0.4812 -0.0941 0.1435  -0.1204 120 THR A C   
1034 O O   A THR A 119 ? 0.4679 0.4717 0.4687 -0.1103 0.1575  -0.1303 120 THR A O   
1035 O O   B THR A 119 ? 0.4785 0.4861 0.4846 -0.1087 0.1578  -0.1319 120 THR A O   
1036 C CB  A THR A 119 ? 0.4342 0.4474 0.4415 -0.0867 0.1228  -0.1049 120 THR A CB  
1037 C CB  B THR A 119 ? 0.4892 0.5056 0.5014 -0.0836 0.1214  -0.1049 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.4471 0.4563 0.4433 -0.1037 0.1345  -0.1126 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4609 0.4946 0.4925 -0.0697 0.1085  -0.1004 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.3906 0.3771 0.3679 -0.0863 0.1152  -0.0906 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.4866 0.5004 0.4881 -0.1000 0.1311  -0.1114 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.4271 0.4156 0.4205 -0.0901 0.1392  -0.1118 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.4489 0.4181 0.4202 -0.1018 0.1500  -0.1155 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.5105 0.4944 0.5043 -0.1046 0.1649  -0.1326 121 CYS A C   
1045 O O   . CYS A 120 ? 0.4954 0.4718 0.4754 -0.1210 0.1797  -0.1420 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.4534 0.4068 0.4110 -0.0950 0.1417  -0.1052 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.5018 0.4353 0.4279 -0.0961 0.1272  -0.0883 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4654 0.4694 0.4931 -0.0885 0.1612  -0.1373 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4707 0.4745 0.4982 -0.0886 0.1613  -0.1373 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4687 0.4910 0.5254 -0.0867 0.1732  -0.1549 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4768 0.4983 0.5324 -0.0874 0.1738  -0.1551 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.5130 0.5531 0.5815 -0.0996 0.1858  -0.1701 122 ARG A C   
1053 C C   B ARG A 121 ? 0.5157 0.5558 0.5841 -0.0998 0.1860  -0.1702 122 ARG A C   
1054 O O   A ARG A 121 ? 0.5109 0.5535 0.5825 -0.1114 0.2029  -0.1853 122 ARG A O   
1055 O O   B ARG A 121 ? 0.5122 0.5551 0.5841 -0.1116 0.2031  -0.1856 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4591 0.4996 0.5496 -0.0642 0.1625  -0.1550 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.4804 0.5186 0.5690 -0.0651 0.1639  -0.1554 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.6176 0.6397 0.6994 -0.0528 0.1550  -0.1444 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6756 0.6956 0.7568 -0.0565 0.1612  -0.1493 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7560 0.7916 0.8695 -0.0322 0.1491  -0.1483 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.8038 0.8380 0.9187 -0.0370 0.1578  -0.1558 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.8098 0.8245 0.9112 -0.0217 0.1404  -0.1357 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.8608 0.9032 0.9867 -0.0200 0.1402  -0.1450 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 0.9283 0.9259 1.0223 -0.0228 0.1479  -0.1381 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 0.9894 1.0166 1.1083 -0.0070 0.1292  -0.1324 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.8093 0.8084 0.9066 -0.0333 0.1640  -0.1528 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.8019 0.8063 0.9054 -0.0087 0.1338  -0.1294 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.6786 0.6571 0.7609 -0.0146 0.1404  -0.1269 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.7885 0.8225 0.9145 0.0066  0.1141  -0.1232 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4625 0.5144 0.5364 -0.0990 0.1785  -0.1668 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4800 0.5496 0.5652 -0.1122 0.1897  -0.1811 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.5409 0.5862 0.5894 -0.1365 0.2046  -0.1828 123 LYS A C   
1073 O O   . LYS A 122 ? 0.5352 0.5895 0.5908 -0.1511 0.2225  -0.2003 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.5001 0.5864 0.5980 -0.1051 0.1771  -0.1761 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.7378 0.8533 0.8755 -0.0830 0.1650  -0.1796 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.8779 1.0100 1.0263 -0.0764 0.1519  -0.1750 123 LYS A CD  
1077 C CE  . LYS A 122 ? 1.0246 1.1804 1.2061 -0.0531 0.1376  -0.1759 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.1677 1.3546 1.3740 -0.0501 0.1314  -0.1839 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.4982 0.5117 0.5066 -0.1407 0.1972  -0.1654 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.5264 0.5103 0.4930 -0.1620 0.2084  -0.1641 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.5951 0.5687 0.5512 -0.1722 0.2234  -0.1738 124 PHE A C   
1082 O O   . PHE A 123 ? 0.5984 0.5614 0.5358 -0.1926 0.2407  -0.1837 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.5489 0.5036 0.4788 -0.1602 0.1939  -0.1436 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.5706 0.5234 0.4941 -0.1612 0.1864  -0.1364 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.5893 0.5710 0.5472 -0.1503 0.1794  -0.1393 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.6321 0.5525 0.5137 -0.1720 0.1849  -0.1262 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.6028 0.5825 0.5545 -0.1520 0.1732  -0.1336 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.6575 0.5741 0.5333 -0.1724 0.1783  -0.1200 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.6040 0.5508 0.5153 -0.1631 0.1733  -0.1242 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.5395 0.5155 0.5071 -0.1591 0.2183  -0.1719 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5604 0.5285 0.5215 -0.1676 0.2328  -0.1825 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.6389 0.6337 0.6335 -0.1737 0.2512  -0.2061 125 ILE A C   
1093 O O   . ILE A 124 ? 0.6541 0.6394 0.6323 -0.1931 0.2702  -0.2183 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.5890 0.5508 0.5529 -0.1526 0.2229  -0.1747 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.5940 0.5275 0.5188 -0.1530 0.2090  -0.1551 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.6219 0.5813 0.5883 -0.1595 0.2393  -0.1893 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.6637 0.5955 0.5955 -0.1359 0.1945  -0.1444 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.5881 0.6165 0.6285 -0.1577 0.2455  -0.2134 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.5982 0.6585 0.6781 -0.1602 0.2604  -0.2374 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.6594 0.7213 0.7280 -0.1846 0.2778  -0.2497 126 LYS A C   
1101 O O   . LYS A 125 ? 0.6574 0.7313 0.7388 -0.1978 0.2981  -0.2708 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.6131 0.7079 0.7407 -0.1367 0.2466  -0.2404 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.6100 0.6573 0.6524 -0.1919 0.2711  -0.2370 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.6359 0.6779 0.6612 -0.2162 0.2874  -0.2466 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.7448 0.7528 0.7249 -0.2407 0.3060  -0.2495 127 ALA A C   
1106 O O   . ALA A 126 ? 0.7554 0.7659 0.7317 -0.2623 0.3271  -0.2664 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.6346 0.6647 0.6408 -0.2160 0.2744  -0.2307 127 ALA A CB  
1108 N N   . SER A 127 ? 0.7498 0.7264 0.6948 -0.2380 0.2984  -0.2339 128 SER A N   
1109 C CA  . SER A 127 ? 0.8142 0.7551 0.7104 -0.2597 0.3125  -0.2339 128 SER A CA  
1110 C C   . SER A 127 ? 0.9163 0.8650 0.8239 -0.2671 0.3309  -0.2525 128 SER A C   
1111 O O   . SER A 127 ? 0.9700 0.8923 0.8387 -0.2891 0.3469  -0.2571 128 SER A O   
1112 C CB  . SER A 127 ? 0.8874 0.7923 0.7396 -0.2543 0.2947  -0.2096 128 SER A CB  
1113 O OG  . SER A 127 ? 1.0393 0.9205 0.8581 -0.2615 0.2883  -0.1965 128 SER A OG  
1114 N N   . GLU A 128 ? 0.8455 0.8283 0.8043 -0.2492 0.3292  -0.2637 129 GLU A N   
1115 C CA  . GLU A 128 ? 1.0949 1.0870 1.0698 -0.2536 0.3463  -0.2827 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.6255 1.6400 1.6219 -0.2726 0.3724  -0.3106 129 GLU A C   
1117 O O   . GLU A 128 ? 1.2147 1.2228 1.1928 -0.2916 0.3823  -0.3139 129 GLU A O   
1118 C CB  . GLU A 128 ? 1.0803 1.0948 1.0981 -0.2260 0.3337  -0.2829 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.1747 1.2329 1.2517 -0.2090 0.3295  -0.2955 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.4255 1.5000 1.5392 -0.1793 0.3131  -0.2915 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.3486 1.3999 1.4409 -0.1690 0.2990  -0.2727 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.3168 1.4270 1.4803 -0.1663 0.3139  -0.3075 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.2506 0.4976 0.3288 -0.0293 -0.0179 -0.0869 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2601 0.5071 0.3383 -0.0293 -0.0179 -0.0869 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.2375 0.4828 0.3143 -0.0287 -0.0175 -0.0885 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2541 0.4996 0.3311 -0.0287 -0.0175 -0.0884 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2918 0.5371 0.3702 -0.0290 -0.0182 -0.0882 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2863 0.5319 0.3648 -0.0291 -0.0182 -0.0881 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2948 0.5396 0.3746 -0.0293 -0.0194 -0.0875 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2786 0.5240 0.3586 -0.0296 -0.0192 -0.0873 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.2274 0.4699 0.3024 -0.0280 -0.0185 -0.0896 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.2478 0.4903 0.3229 -0.0280 -0.0185 -0.0896 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.2309 0.4731 0.3036 -0.0278 -0.0179 -0.0910 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2629 0.5047 0.3402 -0.0279 -0.0204 -0.0896 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2636 0.5059 0.3366 -0.0279 -0.0188 -0.0912 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.3030 0.5447 0.3829 -0.0280 -0.0218 -0.0898 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.2253 0.4673 0.2954 -0.0275 -0.0161 -0.0928 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2621 0.5041 0.3403 -0.0273 -0.0209 -0.0900 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2525 0.4947 0.3223 -0.0275 -0.0177 -0.0935 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.2975 0.5398 0.3808 -0.0277 -0.0230 -0.0906 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2670 0.5090 0.3351 -0.0273 -0.0159 -0.0946 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.3136 0.5564 0.3954 -0.0271 -0.0223 -0.0909 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.2342 0.4759 0.3040 -0.0273 -0.0146 -0.0930 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2737 0.5158 0.3507 -0.0268 -0.0203 -0.0900 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2604 0.5021 0.3254 -0.0270 -0.0140 -0.0973 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.3033 0.5480 0.3874 -0.0263 -0.0226 -0.0921 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.2464 0.4877 0.3142 -0.0271 -0.0128 -0.0949 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.2931 0.5362 0.3713 -0.0259 -0.0209 -0.0907 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2537 0.4951 0.3188 -0.0269 -0.0123 -0.0973 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.2991 0.5439 0.3806 -0.0256 -0.0219 -0.0920 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.2266 0.4724 0.3052 -0.0288 -0.0176 -0.0890 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.2287 0.4745 0.3083 -0.0289 -0.0184 -0.0895 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2557 0.4995 0.3345 -0.0277 -0.0183 -0.0899 2   VAL D C   
1157 O O   . VAL B 3   ? 0.2443 0.4872 0.3222 -0.0272 -0.0174 -0.0896 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2717 0.5220 0.3542 -0.0304 -0.0181 -0.0903 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2709 0.5244 0.3541 -0.0318 -0.0183 -0.0890 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2617 0.5149 0.3466 -0.0304 -0.0167 -0.0915 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.2339 0.4773 0.3130 -0.0272 -0.0193 -0.0905 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.2291 0.4713 0.3082 -0.0260 -0.0194 -0.0904 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2878 0.5317 0.3706 -0.0270 -0.0192 -0.0915 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2887 0.5347 0.3731 -0.0280 -0.0201 -0.0933 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.2531 0.4950 0.3311 -0.0248 -0.0206 -0.0912 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.2350 0.4777 0.3119 -0.0239 -0.0207 -0.0912 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2851 0.5262 0.3632 -0.0233 -0.0209 -0.0905 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.2991 0.5423 0.3747 -0.0234 -0.0205 -0.0898 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2823 0.5262 0.3674 -0.0269 -0.0180 -0.0911 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2864 0.5337 0.3775 -0.0278 -0.0177 -0.0931 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.3312 0.5777 0.4250 -0.0274 -0.0195 -0.0940 4   PRO D C   
1172 O O   . PRO B 5   ? 0.3116 0.5545 0.4026 -0.0258 -0.0202 -0.0922 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.3107 0.5579 0.4042 -0.0275 -0.0156 -0.0926 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.3638 0.6061 0.4520 -0.0262 -0.0155 -0.0897 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.3112 0.5529 0.3943 -0.0261 -0.0167 -0.0893 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.3225 0.5736 0.4219 -0.0289 -0.0204 -0.0972 5   ALA D N   
# 
