data_7GUV
# 
_entry.id   7GUV 
# 
_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   7GUV         pdb_00007guv 10.2210/pdb7guv/pdb 
WWPDB D_1001406666 ?            ?                   
# 
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                        7GUV 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              Rob.vanMontfort@icr.ac.uk 
_pdbx_contact_author.name_first         Rob 
_pdbx_contact_author.name_last          'van Montfort' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodrigues, M.J.'      1 0000-0003-1243-903X 
'Le Bihan, Y.V.'       2 0000-0002-6850-9706 
'van Montfort, R.L.M.' 3 0000-0002-5688-3450 
# 
_citation.id                        primary 
_citation.title                     
'Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.' 
_citation.journal_abbrev            J.Appl.Crystallogr. 
_citation.journal_volume            57 
_citation.page_first                1951 
_citation.page_last                 1965 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39628887 
_citation.pdbx_database_id_DOI      10.1107/S1600576724010549 
_citation.journal_id_ASTM           JACGAR 
_citation.country                   DK 
_citation.journal_id_ISSN           0021-8898 
_citation.journal_id_CSD            0228 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodrigues, M.J.'      1 0000-0003-1243-903X 
primary 'Cabry, M.'            2 0000-0002-9070-5498 
primary 'Collie, G.'           3 0000-0002-0406-922X 
primary 'Carter, M.'           4 ?                   
primary 'McAndrew, C.'         5 0000-0002-1366-088X 
primary 'Owen, R.L.'           6 0000-0002-2104-7057 
primary 'Bellenie, B.R.'       7 0000-0001-9987-3079 
primary 'Le Bihan, Y.V.'       8 0000-0002-6850-9706 
primary 'van Montfort, R.L.M.' 9 0000-0002-5688-3450 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'B-cell lymphoma 6 protein'                                            14536.915 1   ? ? ? ? 
2 polymer     syn 'WVIP tetrapeptide'                                                    610.744   1   ? ? ? ? 
3 non-polymer syn '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' 339.575   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                         35.453    1   ? ? ? ? 
5 non-polymer nat 'DIMETHYL SULFOXIDE'                                                   78.133    1   ? ? ? ? 
6 water       nat water                                                                  18.015    185 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'BCL-6,B-cell lymphoma 5 protein,BCL-5,Protein LAZ-3,Zinc finger and BTB domain-containing protein 27,Zinc finger protein 51' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
A ? 
2 'polypeptide(L)' no yes '(ACE)WVIPA' XWVIPA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' A1ACA 
4 'CHLORIDE ION'                                                         CL    
5 'DIMETHYL SULFOXIDE'                                                   DMS   
6 water                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   ALA n 
1 5   ASP n 
1 6   SER n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  PHE n 
1 11  THR n 
1 12  ARG n 
1 13  HIS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  LEU n 
1 19  LEU n 
1 20  ASN n 
1 21  LEU n 
1 22  ASN n 
1 23  ARG n 
1 24  LEU n 
1 25  ARG n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  THR n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  ILE n 
1 36  VAL n 
1 37  VAL n 
1 38  SER n 
1 39  ARG n 
1 40  GLU n 
1 41  GLN n 
1 42  PHE n 
1 43  ARG n 
1 44  ALA n 
1 45  HIS n 
1 46  LYS n 
1 47  THR n 
1 48  VAL n 
1 49  LEU n 
1 50  MET n 
1 51  ALA n 
1 52  CYS n 
1 53  SER n 
1 54  GLY n 
1 55  LEU n 
1 56  PHE n 
1 57  TYR n 
1 58  SER n 
1 59  ILE n 
1 60  PHE n 
1 61  THR n 
1 62  ASP n 
1 63  GLN n 
1 64  LEU n 
1 65  LYS n 
1 66  CYS n 
1 67  ASN n 
1 68  LEU n 
1 69  SER n 
1 70  VAL n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ASP n 
1 75  PRO n 
1 76  GLU n 
1 77  ILE n 
1 78  ASN n 
1 79  PRO n 
1 80  GLU n 
1 81  GLY n 
1 82  PHE n 
1 83  CYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  ASP n 
1 88  PHE n 
1 89  MET n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ARG n 
1 94  LEU n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLU n 
1 99  GLY n 
1 100 ASN n 
1 101 ILE n 
1 102 MET n 
1 103 ALA n 
1 104 VAL n 
1 105 MET n 
1 106 ALA n 
1 107 THR n 
1 108 ALA n 
1 109 MET n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 MET n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 VAL n 
1 118 ASP n 
1 119 THR n 
1 120 CYS n 
1 121 ARG n 
1 122 LYS n 
1 123 PHE n 
1 124 ILE n 
1 125 LYS n 
1 126 ALA n 
1 127 SER n 
1 128 GLU n 
2 1   ACE n 
2 2   TRP n 
2 3   VAL n 
2 4   ILE n 
2 5   PRO n 
2 6   ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCL6, BCL5, LAZ3, ZBTB27, ZNF51' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21-AI 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET48b 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 6 'synthetic construct' ? 32630 ? 
3 2 sample ? ? 'synthetic construct' ? 32630 ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ACA non-polymer         . '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' ? 'C12 H8 Br Cl N4 O' 339.575 
ACE   non-polymer         . 'ACETYL GROUP'                                                         ? 'C2 H4 O'           44.053  
ALA   'L-peptide linking' y ALANINE                                                                ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE                                                               ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                             ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                        ? 'C4 H7 N O4'        133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                         ? 'Cl -1'             35.453  
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'      121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                   ? 'C2 H6 O S'         78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                  ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                                             ? 'C5 H11 N O2 S'     149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                                                                ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE                                                                 ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE                                                              ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                             ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE                                                               ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE                                                                 ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLY 3   4   ?   ?   ?   A . n 
A 1 4   ALA 4   5   ?   ?   ?   A . n 
A 1 5   ASP 5   6   6   ASP ASP A . n 
A 1 6   SER 6   7   7   SER SER A . n 
A 1 7   CYS 7   8   8   CYS CYS A . n 
A 1 8   ILE 8   9   9   ILE ILE A . n 
A 1 9   GLN 9   10  10  GLN GLN A . n 
A 1 10  PHE 10  11  11  PHE PHE A . n 
A 1 11  THR 11  12  12  THR THR A . n 
A 1 12  ARG 12  13  13  ARG ARG A . n 
A 1 13  HIS 13  14  14  HIS HIS A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ASP 16  17  17  ASP ASP A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  ASN 20  21  21  ASN ASN A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  ARG 23  24  24  ARG ARG A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  ARG 25  26  26  ARG ARG A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  THR 31  32  32  THR THR A . n 
A 1 32  ASP 32  33  33  ASP ASP A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  VAL 36  37  37  VAL VAL A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  SER 38  39  39  SER SER A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLN 41  42  42  GLN GLN A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  ALA 44  45  45  ALA ALA A . n 
A 1 45  HIS 45  46  46  HIS HIS A . n 
A 1 46  LYS 46  47  47  LYS LYS A . n 
A 1 47  THR 47  48  48  THR THR A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  MET 50  51  51  MET MET A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  CYS 52  53  53  CYS CYS A . n 
A 1 53  SER 53  54  54  SER SER A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  PHE 60  61  61  PHE PHE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  ASN 67  68  68  ASN ASN A . n 
A 1 68  LEU 68  69  69  LEU LEU A . n 
A 1 69  SER 69  70  70  SER SER A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ILE 71  72  72  ILE ILE A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  ASP 74  75  75  ASP ASP A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLU 76  77  77  GLU GLU A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  PRO 79  80  80  PRO PRO A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  CYS 83  84  84  CYS CYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  LEU 85  86  86  LEU LEU A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  PHE 88  89  89  PHE PHE A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  ASN 95  96  96  ASN ASN A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ARG 97  98  98  ARG ARG A . n 
A 1 98  GLU 98  99  99  GLU GLU A . n 
A 1 99  GLY 99  100 100 GLY GLY A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 MET 102 103 103 MET MET A . n 
A 1 103 ALA 103 104 104 ALA ALA A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 MET 105 106 106 MET MET A . n 
A 1 106 ALA 106 107 107 ALA ALA A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 MET 109 110 110 MET MET A . n 
A 1 110 TYR 110 111 111 TYR TYR A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLN 112 113 113 GLN GLN A . n 
A 1 113 MET 113 114 114 MET MET A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 HIS 115 116 116 HIS HIS A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 VAL 117 118 118 VAL VAL A . n 
A 1 118 ASP 118 119 119 ASP ASP A . n 
A 1 119 THR 119 120 120 THR THR A . n 
A 1 120 CYS 120 121 121 CYS CYS A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 PHE 123 124 124 PHE PHE A . n 
A 1 124 ILE 124 125 125 ILE ILE A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 SER 127 128 128 SER SER A . n 
A 1 128 GLU 128 129 129 GLU GLU A . n 
B 2 1   ACE 1   0   0   ACE ACE D . n 
B 2 2   TRP 2   1   1   TRP TRP D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ILE 4   3   3   ILE ILE D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   ALA 6   5   5   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1ACA 1   201 1   A1ACA 763 A . 
D 4 CL    1   202 1   CL    CL  A . 
E 5 DMS   1   101 1   DMS   DMS D . 
F 6 HOH   1   301 7   HOH   HOH A . 
F 6 HOH   2   302 178 HOH   HOH A . 
F 6 HOH   3   303 45  HOH   HOH A . 
F 6 HOH   4   304 166 HOH   HOH A . 
F 6 HOH   5   305 140 HOH   HOH A . 
F 6 HOH   6   306 29  HOH   HOH A . 
F 6 HOH   7   307 94  HOH   HOH A . 
F 6 HOH   8   308 19  HOH   HOH A . 
F 6 HOH   9   309 173 HOH   HOH A . 
F 6 HOH   10  310 202 HOH   HOH A . 
F 6 HOH   11  311 179 HOH   HOH A . 
F 6 HOH   12  312 90  HOH   HOH A . 
F 6 HOH   13  313 100 HOH   HOH A . 
F 6 HOH   14  314 106 HOH   HOH A . 
F 6 HOH   15  315 247 HOH   HOH A . 
F 6 HOH   16  316 84  HOH   HOH A . 
F 6 HOH   17  317 99  HOH   HOH A . 
F 6 HOH   18  318 37  HOH   HOH A . 
F 6 HOH   19  319 75  HOH   HOH A . 
F 6 HOH   20  320 27  HOH   HOH A . 
F 6 HOH   21  321 119 HOH   HOH A . 
F 6 HOH   22  322 101 HOH   HOH A . 
F 6 HOH   23  323 193 HOH   HOH A . 
F 6 HOH   24  324 47  HOH   HOH A . 
F 6 HOH   25  325 40  HOH   HOH A . 
F 6 HOH   26  326 87  HOH   HOH A . 
F 6 HOH   27  327 6   HOH   HOH A . 
F 6 HOH   28  328 132 HOH   HOH A . 
F 6 HOH   29  329 91  HOH   HOH A . 
F 6 HOH   30  330 142 HOH   HOH A . 
F 6 HOH   31  331 139 HOH   HOH A . 
F 6 HOH   32  332 83  HOH   HOH A . 
F 6 HOH   33  333 4   HOH   HOH A . 
F 6 HOH   34  334 237 HOH   HOH A . 
F 6 HOH   35  335 117 HOH   HOH A . 
F 6 HOH   36  336 243 HOH   HOH A . 
F 6 HOH   37  337 44  HOH   HOH A . 
F 6 HOH   38  338 17  HOH   HOH A . 
F 6 HOH   39  339 14  HOH   HOH A . 
F 6 HOH   40  340 239 HOH   HOH A . 
F 6 HOH   41  341 5   HOH   HOH A . 
F 6 HOH   42  342 86  HOH   HOH A . 
F 6 HOH   43  343 242 HOH   HOH A . 
F 6 HOH   44  344 34  HOH   HOH A . 
F 6 HOH   45  345 196 HOH   HOH A . 
F 6 HOH   46  346 42  HOH   HOH A . 
F 6 HOH   47  347 151 HOH   HOH A . 
F 6 HOH   48  348 20  HOH   HOH A . 
F 6 HOH   49  349 12  HOH   HOH A . 
F 6 HOH   50  350 24  HOH   HOH A . 
F 6 HOH   51  351 30  HOH   HOH A . 
F 6 HOH   52  352 93  HOH   HOH A . 
F 6 HOH   53  353 145 HOH   HOH A . 
F 6 HOH   54  354 96  HOH   HOH A . 
F 6 HOH   55  355 144 HOH   HOH A . 
F 6 HOH   56  356 89  HOH   HOH A . 
F 6 HOH   57  357 124 HOH   HOH A . 
F 6 HOH   58  358 85  HOH   HOH A . 
F 6 HOH   59  359 51  HOH   HOH A . 
F 6 HOH   60  360 97  HOH   HOH A . 
F 6 HOH   61  361 175 HOH   HOH A . 
F 6 HOH   62  362 141 HOH   HOH A . 
F 6 HOH   63  363 74  HOH   HOH A . 
F 6 HOH   64  364 103 HOH   HOH A . 
F 6 HOH   65  365 50  HOH   HOH A . 
F 6 HOH   66  366 122 HOH   HOH A . 
F 6 HOH   67  367 28  HOH   HOH A . 
F 6 HOH   68  368 180 HOH   HOH A . 
F 6 HOH   69  369 133 HOH   HOH A . 
F 6 HOH   70  370 207 HOH   HOH A . 
F 6 HOH   71  371 170 HOH   HOH A . 
F 6 HOH   72  372 169 HOH   HOH A . 
F 6 HOH   73  373 244 HOH   HOH A . 
F 6 HOH   74  374 105 HOH   HOH A . 
F 6 HOH   75  375 186 HOH   HOH A . 
F 6 HOH   76  376 177 HOH   HOH A . 
F 6 HOH   77  377 21  HOH   HOH A . 
F 6 HOH   78  378 15  HOH   HOH A . 
F 6 HOH   79  379 167 HOH   HOH A . 
F 6 HOH   80  380 191 HOH   HOH A . 
F 6 HOH   81  381 25  HOH   HOH A . 
F 6 HOH   82  382 229 HOH   HOH A . 
F 6 HOH   83  383 131 HOH   HOH A . 
F 6 HOH   84  384 194 HOH   HOH A . 
F 6 HOH   85  385 205 HOH   HOH A . 
F 6 HOH   86  386 245 HOH   HOH A . 
F 6 HOH   87  387 174 HOH   HOH A . 
F 6 HOH   88  388 192 HOH   HOH A . 
F 6 HOH   89  389 76  HOH   HOH A . 
F 6 HOH   90  390 39  HOH   HOH A . 
F 6 HOH   91  391 157 HOH   HOH A . 
F 6 HOH   92  392 32  HOH   HOH A . 
F 6 HOH   93  393 70  HOH   HOH A . 
F 6 HOH   94  394 55  HOH   HOH A . 
F 6 HOH   95  395 64  HOH   HOH A . 
F 6 HOH   96  396 22  HOH   HOH A . 
F 6 HOH   97  397 185 HOH   HOH A . 
F 6 HOH   98  398 16  HOH   HOH A . 
F 6 HOH   99  399 60  HOH   HOH A . 
F 6 HOH   100 400 35  HOH   HOH A . 
F 6 HOH   101 401 92  HOH   HOH A . 
F 6 HOH   102 402 241 HOH   HOH A . 
F 6 HOH   103 403 165 HOH   HOH A . 
F 6 HOH   104 404 82  HOH   HOH A . 
F 6 HOH   105 405 212 HOH   HOH A . 
F 6 HOH   106 406 26  HOH   HOH A . 
F 6 HOH   107 407 108 HOH   HOH A . 
F 6 HOH   108 408 223 HOH   HOH A . 
F 6 HOH   109 409 120 HOH   HOH A . 
F 6 HOH   110 410 176 HOH   HOH A . 
F 6 HOH   111 411 61  HOH   HOH A . 
F 6 HOH   112 412 190 HOH   HOH A . 
F 6 HOH   113 413 69  HOH   HOH A . 
F 6 HOH   114 414 43  HOH   HOH A . 
F 6 HOH   115 415 215 HOH   HOH A . 
F 6 HOH   116 416 46  HOH   HOH A . 
F 6 HOH   117 417 129 HOH   HOH A . 
F 6 HOH   118 418 56  HOH   HOH A . 
F 6 HOH   119 419 88  HOH   HOH A . 
F 6 HOH   120 420 67  HOH   HOH A . 
F 6 HOH   121 421 236 HOH   HOH A . 
F 6 HOH   122 422 36  HOH   HOH A . 
F 6 HOH   123 423 204 HOH   HOH A . 
F 6 HOH   124 424 68  HOH   HOH A . 
F 6 HOH   125 425 57  HOH   HOH A . 
F 6 HOH   126 426 110 HOH   HOH A . 
F 6 HOH   127 427 65  HOH   HOH A . 
F 6 HOH   128 428 95  HOH   HOH A . 
F 6 HOH   129 429 41  HOH   HOH A . 
F 6 HOH   130 430 116 HOH   HOH A . 
F 6 HOH   131 431 168 HOH   HOH A . 
F 6 HOH   132 432 147 HOH   HOH A . 
F 6 HOH   133 433 227 HOH   HOH A . 
F 6 HOH   134 434 135 HOH   HOH A . 
F 6 HOH   135 435 187 HOH   HOH A . 
F 6 HOH   136 436 123 HOH   HOH A . 
F 6 HOH   137 437 200 HOH   HOH A . 
F 6 HOH   138 438 248 HOH   HOH A . 
F 6 HOH   139 439 214 HOH   HOH A . 
F 6 HOH   140 440 228 HOH   HOH A . 
F 6 HOH   141 441 231 HOH   HOH A . 
F 6 HOH   142 442 121 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 63  HOH   HOH A . 
F 6 HOH   146 446 171 HOH   HOH A . 
F 6 HOH   147 447 203 HOH   HOH A . 
F 6 HOH   148 448 234 HOH   HOH A . 
F 6 HOH   149 449 220 HOH   HOH A . 
F 6 HOH   150 450 238 HOH   HOH A . 
F 6 HOH   151 451 125 HOH   HOH A . 
F 6 HOH   152 452 158 HOH   HOH A . 
F 6 HOH   153 453 114 HOH   HOH A . 
F 6 HOH   154 454 181 HOH   HOH A . 
F 6 HOH   155 455 79  HOH   HOH A . 
F 6 HOH   156 456 217 HOH   HOH A . 
F 6 HOH   157 457 235 HOH   HOH A . 
F 6 HOH   158 458 81  HOH   HOH A . 
F 6 HOH   159 459 58  HOH   HOH A . 
F 6 HOH   160 460 246 HOH   HOH A . 
F 6 HOH   161 461 115 HOH   HOH A . 
F 6 HOH   162 462 107 HOH   HOH A . 
F 6 HOH   163 463 221 HOH   HOH A . 
F 6 HOH   164 464 216 HOH   HOH A . 
F 6 HOH   165 465 230 HOH   HOH A . 
F 6 HOH   166 466 182 HOH   HOH A . 
F 6 HOH   167 467 188 HOH   HOH A . 
F 6 HOH   168 468 183 HOH   HOH A . 
F 6 HOH   169 469 201 HOH   HOH A . 
F 6 HOH   170 470 148 HOH   HOH A . 
F 6 HOH   171 471 113 HOH   HOH A . 
F 6 HOH   172 472 48  HOH   HOH A . 
F 6 HOH   173 473 213 HOH   HOH A . 
F 6 HOH   174 474 206 HOH   HOH A . 
F 6 HOH   175 475 172 HOH   HOH A . 
F 6 HOH   176 476 211 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 78  HOH   HOH D . 
G 6 HOH   4   204 23  HOH   HOH D . 
G 6 HOH   5   205 53  HOH   HOH D . 
G 6 HOH   6   206 73  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   209 195 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           7GUV 
_cell.length_a           67.600 
_cell.length_b           67.600 
_cell.length_c           166.530 
_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                         7GUV 
_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          7GUV 
_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   66.08 
_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                     7GUV 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.930 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23647 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.065 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.700 
_reflns.B_iso_Wilson_estimate        29.520 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.069 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     215282 
_reflns.pdbx_scaling_rejects         1295 
_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  ? 12088 1292 ? 1.056 ? ? ? 9.400 ? 2.200  ? ? ? ? ? ? 100.000 1.116 0.358 0.856 ? 
1 2 9.090 33.930 ? 1509  228  ? 0.031 ? ? ? 6.600 ? 40.600 ? ? ? ? ? ? 98.700  0.035 0.014 0.993 ? 
# 
_refine.entry_id                                 7GUV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             33.9300 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    100.0000 
_refine.ls_number_reflns_obs                     23579 
_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                          0.1830 
_refine.ls_R_factor_R_work                       0.1810 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2090 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1400 
_refine.ls_number_reflns_R_free                  1211 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               33.5100 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.6230 
_refine.aniso_B[2][2]                            0.6230 
_refine.aniso_B[3][3]                            -1.2459 
_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               0.9610 
_refine.correlation_coeff_Fo_to_Fc_free          0.9410 
_refine.overall_SU_R_Cruickshank_DPI             0.0870 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0880 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1000 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0970 
_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                                119.720 
_refine.B_iso_min                                16.830 
_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                        7GUV 
_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                        33.9300 
_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           28.53 
_refine_hist.pdbx_B_iso_mean_solvent          49.60 
_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      1669 ?      ? 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           ?    3.400  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.620 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.7500 
_refine_ls_shell.d_res_low                        1.8300 
_refine_ls_shell.pdbx_total_number_of_bins_used   12 
_refine_ls_shell.percent_reflns_obs               99.9600 
_refine_ls_shell.number_reflns_R_work             2702 
_refine_ls_shell.R_factor_all                     0.3463 
_refine_ls_shell.R_factor_R_work                  0.3472 
_refine_ls_shell.R_factor_R_free                  0.3289 
_refine_ls_shell.percent_reflns_R_free            4.4600 
_refine_ls_shell.number_reflns_R_free             126 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2828 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUV 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 5.00 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUV 
_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 7GUV       7GUV   ? 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 7GUV A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUV D 1 ? 6   ? 7GUV   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 7GUV GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUV PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUV 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)' 7380  ? 
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 33.8000000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5433172958 0.0000000000 0.0000000000 -1.0000000000 27.7550000000 
# 
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 ? ? ? ? ? ? ? 1.331 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
# 
_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                   7GUV 
_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 61.55 -119.79 
2 1 SER A 39  ? B 39.86 66.39   
3 1 ARG A 40  ? B 73.79 -22.07  
4 1 SER A 93  ? A 76.64 -4.02   
5 1 GLN A 113 ? ? 62.00 60.77   
# 
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 371 ? F HOH . 
2 1 A HOH 372 ? F HOH . 
3 1 A HOH 457 ? F HOH . 
4 1 A HOH 465 ? F HOH . 
5 1 A HOH 468 ? F HOH . 
6 1 A HOH 469 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.2144 -16.5503 24.6837 0.0217  -0.0426 -0.0894 -0.0428 0.0316  -0.0251 0.9356 1.7503  1.9194 
0.3939  -0.3013 1.1165 0.1296 -0.0645 -0.0651 -0.0491 0.1003 0.0859 0.2456  -0.0136 -0.0033 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.0962 0.1257  -0.0486 -0.0251 -0.0187 -0.0980 0.8199 -0.2791 0.0000 
-0.0051 -0.0583 0.2758 0.0200 -0.0113 -0.0087 -0.0117 0.0018 0.0234 -0.0134 0.0066  -0.0122 
# 
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                    7GUV 
_atom_sites.fract_transf_matrix[1][1]   0.014793 
_atom_sites.fract_transf_matrix[1][2]   0.008541 
_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]   0.017081 
_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]   0.006005 
_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   ? 17.274 -21.209 -4.840 1.00 63.08  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.196 -22.103 -5.542 1.00 61.96  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.732 -23.576 -5.469 1.00 61.32  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.678 -23.876 -4.893 1.00 61.94  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.627 -21.948 -4.966 1.00 62.89  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.730 -22.017 -6.015 1.00 76.82  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.882 -23.089 -6.656 1.00 76.89  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.449 -21.005 -6.187 1.00 83.83  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.517 -24.484 -6.067 1.00 52.32  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.266 -25.921 -6.063 1.00 49.56  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.252 -26.636 -5.092 1.00 45.15  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.546 -27.817 -5.270 1.00 43.90  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.389 -26.475 -7.479 1.00 55.28  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.672 -26.218 -8.028 1.00 66.90  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.730 -25.925 -4.052 1.00 36.75  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.670 -26.488 -3.084 1.00 33.56  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.048 -27.637 -2.277 1.00 34.42  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.830 -27.672 -2.086 1.00 34.10  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.171 -25.395 -2.136 1.00 34.32  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.346 -24.221 -2.874 1.00 39.32  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.884 -28.547 -1.777 1.00 26.59  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.500 -29.538 -0.771 1.00 24.20  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.121 -29.007 0.519  1.00 25.69  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.076 -28.219 0.459  1.00 24.11  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.852 -31.015 -1.079 1.00 27.49  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.371 -31.196 -1.334 1.00 27.23  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.032 -31.523 -2.259 1.00 26.74  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.883 -32.653 -1.478 1.00 31.80  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.648 -29.438 1.689  0.66 20.68  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.537 -29.373 1.657  0.34 21.49  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.211 -28.948 2.951  0.66 20.13  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 20.968 -28.888 2.955  0.34 20.67  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.572 -30.091 3.889  0.66 22.76  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.368 -30.022 3.880  0.34 24.54  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.816 -31.056 3.980  0.66 23.76  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.663 -31.026 3.963  0.34 25.04  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.222 -27.972 3.634  0.66 22.11  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.847 -28.055 3.583  0.34 21.99  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.528 -27.692 5.127  0.66 25.79  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.354 -27.069 4.632  0.34 23.23  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.063 -26.355 5.635  0.66 45.12  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.619 -27.189 5.944  0.34 36.32  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.508 -25.533 4.901  0.66 39.16  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.398 -27.376 5.993  0.34 30.92  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.316 -26.094 6.915  0.66 37.98  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.353 -27.053 7.043  0.34 32.65  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.713 -29.983 4.588  0.66 20.11  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.494 -29.853 4.576  0.34 21.58  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.089 -31.004 5.562  0.66 19.49  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.012 -30.831 5.528  0.34 21.24  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.613 -30.513 6.925  0.66 22.45  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.521 -30.391 6.893  0.34 23.64  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.189 -29.563 7.479  0.66 21.77  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.969 -29.355 7.409  0.34 23.08  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.605 -31.300 5.530  0.66 20.52  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.548 -30.910 5.426  0.34 22.77  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 24.970 -32.511 6.354  0.66 21.12  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.017 -31.687 4.215  0.34 25.00  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.588 -33.789 5.953  0.66 23.54  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.769 -31.222 2.925  0.34 28.79  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.750 -32.383 7.500  0.66 22.47  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.702 -32.886 4.362  0.34 28.12  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 24.912 -34.908 6.729  0.66 24.55  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.200 -31.940 1.808  0.34 29.88  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.061 -33.497 8.282  0.66 24.39  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.128 -33.608 3.237  0.34 31.66  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.653 -34.753 7.888  0.66 22.57  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.875 -33.128 1.971  0.34 29.56  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.532 -31.131 7.438  1.00 19.98  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.863 -30.755 8.704  1.00 20.33  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.823 -30.501 9.882  1.00 21.75  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.699 -29.479 10.578 1.00 21.88  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.798 -31.794 9.074  1.00 25.40  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.900 -31.944 7.954  1.00 26.02  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 18.991 -31.396 10.327 1.00 30.22  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.755 -31.434 10.094 1.00 19.60  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.668 -31.344 11.241 1.00 20.10  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.903 -30.442 11.029 1.00 21.45  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.745 -30.370 11.937 1.00 20.60  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.136 -32.764 11.641 1.00 26.03  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.050 -33.710 12.186 1.00 36.95  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.481 -33.276 13.522 1.00 57.87  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.450 -33.374 14.618 1.00 69.71  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.306 -32.779 15.799 1.00 80.62  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.227 -32.929 16.740 1.00 69.19  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.245 -32.018 16.043 1.00 63.26  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.044 -29.790 9.857  1.00 17.85  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.280 -29.062 9.568  1.00 18.24  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.585 -27.968 10.585 1.00 20.60  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.724 -27.911 11.092 1.00 20.17  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.281 -28.503 8.131  1.00 18.30  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.539 -27.747 7.828  1.00 20.39  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.730 -28.410 7.619  1.00 21.42  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.748 -26.414 7.696  1.00 21.12  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.628 -27.473 7.362  1.00 20.98  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.082 -26.255 7.384  1.00 20.42  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.594 -27.085 10.866 1.00 17.85  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.843 -25.963 11.795 1.00 18.25  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.258 -26.465 13.189 1.00 20.01  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.177 -25.901 13.793 1.00 17.31  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.624 -25.043 11.873 1.00 19.76  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.602 -27.523 13.678 0.42 19.10  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.599 -27.529 13.680 0.30 18.68  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.599 -27.523 13.693 0.28 17.97  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.897 -28.116 14.982 0.42 19.28  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.890 -28.134 14.984 0.30 18.85  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.921 -28.088 15.008 0.28 17.74  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.305 -28.708 15.009 0.42 22.37  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.295 -28.727 15.017 0.30 22.55  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.305 -28.736 15.030 0.28 22.10  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.036 -28.503 15.985 0.42 19.88  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.009 -28.554 16.010 0.30 20.76  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.020 -28.598 16.026 0.28 20.36  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.850 -29.170 15.335 0.42 22.98  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.857 -29.206 15.322 0.30 22.40  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.838 -29.057 15.474 0.28 19.86  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.062 -29.717 16.626 0.42 25.84  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.548 -28.666 15.398 0.30 25.79  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.728 -30.180 14.616 0.28 18.28  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.697 -29.408 13.923 1.00 20.17  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.021 -30.027 13.801 1.00 20.40  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.094 -28.928 13.765 1.00 20.88  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.151 -29.086 14.369 1.00 21.23  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.096 -30.894 12.542 1.00 22.02  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.304 -32.198 12.633 1.00 29.64  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.773 -32.504 13.731 1.00 28.07  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.205 -32.901 11.609 1.00 32.28  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.811 -27.811 13.063 1.00 17.15  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.763 -26.696 13.026 1.00 16.88  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 30.984 -26.154 14.448 1.00 20.26  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.122 -25.986 14.886 1.00 18.32  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.273 -25.582 12.054 1.00 18.62  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.046 -24.280 12.267 1.00 18.57  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.349 -26.037 10.595 1.00 18.39  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.894 -25.915 15.173 1.00 17.74  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 29.993 -25.343 16.511 1.00 18.74  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.725 -26.307 17.459 1.00 19.85  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.581 -25.856 18.247 1.00 18.39  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.612 -24.985 17.051 1.00 18.84  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.633 -24.048 18.294 1.00 21.71  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.247 -22.668 17.960 1.00 21.71  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.238 -23.878 18.855 1.00 26.36  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.433 -27.609 17.333 1.00 18.67  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.107 -28.637 18.141 1.00 19.48  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.630 -28.560 17.890 1.00 21.62  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.417 -28.539 18.852 1.00 20.10  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.564 -30.025 17.780 1.00 21.47  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.169 -31.205 18.536 1.00 28.97  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.786 -31.147 20.026 1.00 31.45  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.641 -32.522 17.952 1.00 33.45  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.036 -28.432 16.610 1.00 18.82  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.458 -28.305 16.264 1.00 18.40  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.086 -27.003 16.779 1.00 21.13  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.217 -27.014 17.254 1.00 20.40  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.660 -28.494 14.782 1.00 21.16  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.643 -29.963 14.410 1.00 30.44  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.900 -30.849 15.243 1.00 25.83  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.331 -30.260 13.156 1.00 23.61  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.345 -25.892 16.704 1.00 18.42  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.815 -24.610 17.247 1.00 18.39  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.042 -24.772 18.755 1.00 20.60  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.026 -24.247 19.284 1.00 20.38  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.813 -23.464 16.966 1.00 18.65  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.710 -23.085 15.468 1.00 20.95  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.572 -22.077 15.227 1.00 21.27  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.053 -22.575 14.897 1.00 23.04  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.116 -25.474 19.454 1.00 18.82  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.278 -25.695 20.900 1.00 19.51  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.509 -26.567 21.207 1.00 22.79  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.201 -26.319 22.194 1.00 23.61  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.027 -26.310 21.519 1.00 19.48  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.050 -26.182 23.030 1.00 27.67  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.576 -25.213 23.593 1.00 23.95  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.488 -27.155 23.710 1.00 27.85  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.791 -27.582 20.350 1.00 20.83  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 36.981 -28.435 20.480 1.00 22.18  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.238 -27.575 20.340 1.00 25.62  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.188 -27.754 21.105 1.00 24.96  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 36.978 -29.526 19.412 1.00 21.34  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 35.996 -30.644 19.745 1.00 23.83  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.800 -31.569 18.551 1.00 27.26  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 34.954 -32.700 18.920 1.00 34.68  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.272 -33.450 18.063 1.00 47.42  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.281 -33.167 16.764 1.00 35.95  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.554 -34.474 18.497 1.00 40.40  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.235 -26.612 19.385 1.00 22.13  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.373 -25.706 19.233 1.00 22.03  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.528 -24.848 20.486 1.00 25.03  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.657 -24.685 20.974 1.00 24.79  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.207 -24.790 18.030 1.00 21.53  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.204 -25.470 16.662 1.00 24.93  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.054 -24.422 15.562 1.00 25.24  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.482 -26.342 16.467 1.00 24.48  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.396 -24.338 21.032 1.00 21.07  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.454 -23.554 22.272 1.00 21.92  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.080 -24.389 23.432 1.00 26.52  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 39.970 -23.875 24.139 1.00 26.64  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.061 -23.063 22.684 1.00 22.35  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.194 -22.144 23.908 1.00 25.72  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.898 -21.520 24.309 1.00 31.05  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.890 -22.511 24.667 1.00 26.44  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.250 -22.556 25.834 1.00 35.85  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.583 -21.723 26.816 1.00 31.19  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.304 -23.455 26.040 1.00 27.46  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.607 -25.633 23.630 0.39 24.76  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.611 -25.645 23.608 0.28 24.56  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.607 -25.635 23.628 0.33 24.99  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.088 -26.531 24.692 0.39 26.08  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.067 -26.600 24.631 0.28 25.86  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.081 -26.548 24.679 0.33 26.48  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.600 -26.793 24.615 0.39 31.75  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.582 -26.798 24.600 0.28 31.55  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.595 -26.798 24.610 0.33 31.88  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.251 -26.909 25.656 0.39 32.64  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.212 -26.894 25.655 0.28 32.36  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.240 -26.916 25.654 0.33 32.72  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.308 -27.843 24.692 0.39 29.29  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.396 -27.956 24.431 0.28 29.30  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.320 -27.870 24.624 0.33 30.47  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.688 -28.695 23.624 0.39 34.11  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.025 -27.950 24.785 0.28 34.70  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.792 -28.792 25.594 0.33 39.83  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.156 -26.861 23.386 1.00 28.11  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.590 -27.095 23.165 1.00 29.50  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.381 -25.800 22.969 1.00 31.57  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.590 -25.845 22.698 1.00 32.56  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.766 -28.066 21.988 1.00 30.82  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.009 -29.379 22.183 1.00 36.37  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 41.979 -30.199 20.916 1.00 40.54  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.332 -30.589 20.519 1.00 52.84  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.703 -30.810 19.264 1.00 67.19  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 44.956 -31.144 18.985 1.00 56.98  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.833 -30.674 18.277 1.00 49.64  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.700 -24.644 23.132 1.00 25.44  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.251 -23.299 22.988 1.00 25.74  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.866 -23.078 21.586 1.00 29.99  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 44.919 -22.457 21.443 1.00 31.51  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.262 -22.990 24.126 1.00 28.90  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.562 -21.515 24.277 1.00 37.80  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.633 -20.696 24.077 1.00 36.83  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.721 -21.176 24.595 1.00 42.10  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.211 -23.613 20.554 1.00 24.75  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.727 -23.516 19.188 1.00 24.65  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.127 -22.320 18.467 1.00 27.41  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 41.898 -22.187 18.376 1.00 24.25  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.513 -24.833 18.396 1.00 27.20  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.319 -26.013 19.028 1.00 28.98  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.849 -24.634 16.890 1.00 25.85  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.868 -27.386 18.530 1.00 32.77  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.015 -21.429 17.979 1.00 26.28  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.643 -20.236 17.214 1.00 25.98  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.729 -19.250 17.966 1.00 26.52  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.146 -18.371 17.338 1.00 24.26  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.062 -20.583 15.837 1.00 26.51  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.097 -21.123 14.804 1.00 33.82  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.505 -21.142 13.449 1.00 34.38  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.346 -20.282 14.753 1.00 39.99  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.702 -19.326 19.305 1.00 23.71  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.039 -18.317 20.130 1.00 23.35  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.859 -17.022 19.929 1.00 29.03  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.088 -17.072 19.781 1.00 28.97  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 41.976 -18.754 21.586 1.00 27.98  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.304 -19.064 22.013 1.00 30.44  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.022 -19.962 21.793 1.00 26.29  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.182 -15.890 19.808 1.00 26.52  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.845 -14.639 19.455 1.00 27.01  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.517 -13.484 20.357 1.00 27.76  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.867 -12.342 20.056 1.00 27.96  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.521 -14.296 17.986 1.00 28.20  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.039 -14.266 17.629 1.00 34.74  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.194 -14.421 18.545 1.00 28.63  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.726 -14.105 16.439 1.00 43.57  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.852 -13.766 21.475 1.00 22.14  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.529 -12.721 22.437 1.00 21.69  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.369 -13.323 23.823 1.00 25.91  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 40.972 -14.496 23.960 1.00 25.18  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.245 -11.923 21.992 1.00 24.29  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 38.954 -12.731 22.179 1.00 22.31  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.132 -10.563 22.701 1.00 24.68  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.661 -12.511 24.840 0.60 22.94  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.662 -12.526 24.855 0.40 22.24  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.435 -12.831 26.242 0.60 22.83  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.407 -12.905 26.237 0.40 21.77  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.365 -11.842 26.709 0.60 25.76  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.445 -11.869 26.837 0.40 25.74  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.485 -10.638 26.445 0.60 25.32  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.691 -10.662 26.742 0.40 26.01  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.727 -12.715 27.105 0.60 27.99  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.661 -13.223 27.104 0.40 26.14  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.452 -13.025 28.579 0.60 28.44  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.540 -12.000 27.333 0.40 26.55  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.826 -13.619 26.570 0.60 28.49  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.271 -13.873 28.430 0.40 26.17  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.318 -12.350 27.367 1.00 21.34  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.259 -11.538 27.976 1.00 22.20  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.548 -11.574 29.460 1.00 26.59  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.546 -12.664 30.067 1.00 25.43  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.822 -12.060 27.661 1.00 24.26  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.571 -12.231 26.135 1.00 23.59  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.761 -11.167 28.308 1.00 25.20  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.905 -10.968 25.236 1.00 22.90  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.786 -10.389 30.038 1.00 23.74  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.097 -10.249 31.460 1.00 24.49  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.839 -9.830  32.202 1.00 29.33  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.224 -8.816  31.867 1.00 28.17  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.288 -9.281  31.712 1.00 29.02  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.587 -9.140  33.214 1.00 29.76  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.544 -9.739  30.969 1.00 30.02  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.458 -10.622 33.214 1.00 26.50  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.260 -10.390 34.018 1.00 26.59  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.759 -10.425 35.444 1.00 33.36  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 36.913 -11.504 36.026 1.00 29.81  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.140 -11.429 33.730 1.00 29.76  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.825 -10.999 34.371 1.00 29.77  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 34.953 -11.643 32.223 1.00 28.69  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.149 -9.247  35.965 0.54 33.73  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.004 -9.223  35.994 0.46 32.92  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.750 -9.077  37.292 0.54 35.27  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.536 -8.976  37.331 0.46 34.21  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.086 -9.863  37.370 0.54 37.04  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.636 -9.984  37.684 0.46 36.58  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 39.977 -9.600  36.564 0.54 36.31  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.450 -10.885 38.508 0.46 36.21  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.772 -9.470  38.403 0.54 40.67  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.419 -8.900  38.364 0.46 38.67  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.538 -8.778  38.291 0.54 55.07  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.716 -7.677  38.206 0.46 47.33  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.203 -10.840 38.298 0.54 33.04  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.746 -9.868  36.937 0.46 31.21  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.409 -11.653 38.495 0.54 32.95  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 40.990 -10.641 36.995 0.46 31.35  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.517 -12.833 37.526 0.54 34.53  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.861 -12.065 36.424 0.46 33.64  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.549 -13.512 37.514 0.54 33.83  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.884 -12.600 35.990 0.46 33.97  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.510 -12.146 39.954 0.54 33.38  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.642 -10.642 38.391 0.46 31.53  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 40.959 -11.074 40.936 0.54 39.57  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.157 -9.261  38.796 0.46 43.53  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.291 -11.677 42.288 0.54 41.25  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.167 -9.321  39.920 0.46 51.12  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.509 -10.654 43.310 0.54 43.16  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.599 -7.985  40.338 0.46 58.20  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.691 -10.133 43.627 0.54 57.90  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.001 -7.260  41.280 0.46 69.05  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.783 -9.217  44.578 0.54 46.77  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 41.930 -7.728  41.909 0.46 53.28  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.789 -10.516 42.986 0.54 44.23  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.466 -6.059  41.595 0.46 55.82  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.458 -13.088 36.726 0.54 29.28  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.629 -12.652 36.352 0.46 29.37  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.432 -14.215 35.791 0.54 28.64  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.399 -13.978 35.746 0.46 28.82  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.700 -13.805 34.347 0.54 31.41  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.545 -13.825 34.228 0.46 31.61  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.356 -12.697 33.933 0.54 29.75  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 38.994 -12.884 33.657 0.46 29.90  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.101 -14.989 35.898 0.54 29.68  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.010 -14.537 36.113 0.46 29.92  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.833 -15.568 37.282 0.54 44.31  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.921 -15.083 37.530 0.46 42.89  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.164 -17.039 37.435 0.54 81.08  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.158 -16.575 37.641 0.46 77.65  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.426 -17.880 36.869 0.54 82.25  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.220 -16.968 38.175 0.46 80.21  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.158 -17.354 38.130 0.54 82.25  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.282 -17.353 37.195 0.46 78.38  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.298 -14.731 33.579 1.00 27.67  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.619 -14.604 32.164 1.00 26.92  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 39.979 -15.722 31.378 1.00 28.85  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.029 -16.872 31.819 1.00 28.56  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.140 -14.652 31.981 1.00 29.57  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.856 -13.415 32.521 1.00 45.63  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.324 -13.348 32.171 1.00 64.45  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.879 -14.191 31.450 1.00 57.36  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 44.987 -12.328 32.684 1.00 66.30  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.398 -15.399 30.205 1.00 23.26  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.749 -16.402 29.341 1.00 23.46  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.265 -16.218 27.937 1.00 27.29  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.099 -15.132 27.371 1.00 28.09  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.212 -16.227 29.346 1.00 24.19  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.589 -16.328 30.719 1.00 26.01  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.489 -15.206 31.544 1.00 28.22  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.135 -17.550 31.203 1.00 29.47  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 35.930 -15.304 32.819 1.00 30.37  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.576 -17.645 32.482 1.00 32.50  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.491 -16.525 33.285 1.00 30.17  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.878 -17.267 27.368 1.00 24.41  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.389 -17.212 26.003 1.00 22.71  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.258 -17.605 25.050 1.00 24.52  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.450 -18.492 25.362 1.00 23.61  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.607 -18.137 25.815 1.00 24.88  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.834 -17.711 26.679 1.00 30.88  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.159 -18.118 26.042 1.00 37.87  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.183 -17.763 24.618 1.00 49.39  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.721 -16.659 24.110 1.00 62.71  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.380 -15.813 24.890 1.00 53.62  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.647 -16.418 22.810 1.00 46.48  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.183 -16.948 23.891 1.00 21.44  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.098 -17.252 22.932 1.00 20.92  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.477 -16.836 21.527 1.00 22.77  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.574 -16.332 21.304 1.00 21.62  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.805 -16.535 23.346 1.00 22.09  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.578 -17.112 20.569 1.00 20.19  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.732 -16.695 19.184 1.00 19.44  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.845 -15.451 19.004 1.00 22.26  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.632 -15.499 19.293 1.00 20.90  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.268 -17.815 18.237 1.00 18.87  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.042 -19.087 18.425 1.00 21.78  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.581 -20.105 19.264 1.00 23.24  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.263 -19.435 17.947 1.00 23.06  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.508 -21.058 19.216 1.00 23.40  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.553 -20.685 18.458 1.00 23.23  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.441 -14.349 18.542 1.00 21.81  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.703 -13.091 18.295 1.00 20.41  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.465 -13.350 17.421 1.00 22.63  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.399 -12.839 17.742 1.00 19.77  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.609 -12.067 17.580 1.00 22.06  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.589 -11.434 18.540 1.00 22.54  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.543 -10.552 17.722 1.00 21.15  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.584 -9.991  18.638 1.00 28.04  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.596 -9.282  17.842 1.00 27.56  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.592 -14.160 16.363 1.00 19.95  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.467 -14.401 15.452 1.00 19.36  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.293 -15.054 16.147 1.00 20.42  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.146 -14.699 15.873 1.00 20.72  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.905 -15.166 14.204 1.00 25.78  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.536 -16.371 14.633 1.00 26.95  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.814 -14.320 13.307 1.00 27.69  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.566 -16.015 17.028 1.00 17.36  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.486 -16.706 17.740 1.00 17.43  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.809 -15.728 18.704 1.00 19.98  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.565 -15.700 18.795 1.00 17.85  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 32.996 -17.976 18.462 1.00 18.72  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.885 -18.592 19.335 1.00 19.24  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.479 -19.014 17.428 1.00 18.66  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.613 -14.937 19.438 1.00 18.45  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.033 -13.930 20.342 1.00 17.89  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.116 -12.949 19.583 1.00 20.45  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.003 -12.664 20.038 1.00 20.19  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.143 -13.136 21.072 1.00 17.43  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.142 -13.933 21.960 1.00 20.37  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.153 -12.992 22.609 1.00 20.33  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.403 -14.728 23.045 1.00 22.43  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.573 -12.461 18.416 1.00 17.77  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.780 -11.544 17.600 1.00 18.91  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.497 -12.195 17.113 1.00 23.18  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.446 -11.553 17.117 1.00 23.30  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.579 -11.055 16.397 1.00 20.55  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.814 -10.271 16.777 1.00 22.29  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.878 -10.182 15.327 1.00 26.57  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.099 -8.863  14.469 1.00 23.34  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.575 -13.486 16.730 1.00 20.09  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.424 -14.227 16.211 1.00 19.64  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.323 -14.422 17.285 1.00 21.32  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.163 -14.646 16.932 1.00 23.32  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.878 -15.581 15.650 1.00 20.17  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.698 -14.353 18.589 1.00 17.81  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.781 -14.609 19.699 1.00 17.97  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.325 -13.396 20.486 1.00 22.24  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.374 -13.535 21.258 1.00 20.57  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.424 -15.615 20.653 1.00 17.88  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.811 -17.206 19.899 1.00 21.21  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.067 -12.285 20.403 1.00 19.37  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.872 -11.139 21.295 1.00 18.28  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.878 -9.831  20.543 1.00 22.69  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.849 -9.544  19.829 1.00 20.23  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.000 -11.171 22.324 1.00 20.23  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.335 -9.924  22.918 1.00 22.66  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.838 -9.015  20.751 1.00 20.94  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.777 -7.680  20.152 1.00 20.60  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.902 -6.789  20.650 1.00 23.72  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.466 -6.000  19.877 1.00 23.58  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.297 -6.964  21.935 1.00 21.29  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.412 -6.189  22.494 1.00 22.68  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.750 -6.532  21.797 1.00 24.88  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.437 -5.616  21.334 1.00 23.25  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.513 -6.384  24.024 1.00 22.88  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.572 -5.501  24.716 1.00 27.86  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.160 -4.008  24.719 1.00 29.22  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.851 -5.993  26.116 1.00 25.72  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.082 -7.841  21.667 1.00 20.47  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.339 -8.239  21.002 1.00 19.67  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.329 -7.893  19.535 1.00 23.64  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.372 -7.520  19.001 1.00 22.43  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.701 -9.708  21.253 1.00 20.48  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.104 -9.939  22.692 1.00 21.37  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.167 -9.234  23.260 1.00 23.20  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.457 -10.899 23.466 1.00 21.72  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.525 -9.428  24.611 1.00 23.87  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.862 -11.146 24.786 1.00 24.44  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 32.877 -10.400 25.356 1.00 22.17  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.150 -7.955  18.890 1.00 20.96  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.033 -7.562  17.472 1.00 21.65  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.450 -6.094  17.311 1.00 26.09  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.256 -5.789  16.436 1.00 23.89  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.592 -7.810  16.995 1.00 23.42  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.306 -7.269  15.618 1.00 27.00  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 28.922 -7.811  14.493 1.00 28.47  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.440 -6.196  15.439 1.00 31.08  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.660 -7.311  13.215 1.00 30.74  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.170 -5.690  14.172 1.00 34.01  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.771 -6.261  13.065 1.00 40.07  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.479 -5.759  11.829 1.00 45.61  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.912 -5.205  18.167 0.53 23.45  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.912 -5.204  18.169 0.47 23.37  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.222 -3.773  18.168 0.53 24.68  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.228 -3.774  18.175 0.47 24.54  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.713 -3.532  18.484 0.53 29.01  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.725 -3.558  18.461 0.47 28.79  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.356 -2.737  17.803 0.53 30.83  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.375 -2.795  17.749 0.47 30.36  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.318 -3.048  19.160 0.53 27.32  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.379 -3.053  19.218 0.47 27.25  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 27.975 -3.077  18.703 0.53 31.58  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.707 -1.674  19.259 0.47 32.57  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.266 -4.247  19.486 1.00 24.91  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.682 -4.128  19.886 1.00 24.37  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.631 -4.518  18.756 1.00 26.84  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.505 -3.730  18.383 1.00 27.68  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.006 -4.954  21.188 1.00 25.97  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.270 -4.386  22.428 1.00 26.15  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.539 -5.002  21.449 1.00 24.64  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.330 -5.381  23.643 1.00 28.86  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.450 -5.711  18.187 1.00 21.62  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.429 -6.158  17.215 1.00 22.55  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.208 -5.624  15.799 1.00 26.73  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.053 -5.886  14.938 1.00 28.28  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.613 -7.680  17.247 1.00 23.08  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.018 -8.176  18.626 1.00 23.77  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.218 -7.770  19.209 1.00 27.62  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.194 -9.035  19.342 1.00 24.08  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.585 -8.226  20.486 1.00 28.13  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.577 -9.517  20.601 1.00 26.46  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.763 -9.102  21.169 1.00 25.80  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.134 -4.845  15.558 1.00 24.86  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 33.976 -4.145  14.263 1.00 25.20  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.517 -2.720  14.397 1.00 32.48  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.613 -1.989  13.403 1.00 31.38  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.557 -4.187  13.691 1.00 30.78  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.643 -3.673  14.655 1.00 28.43  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.144 -5.589  13.217 1.00 27.80  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 34.924 -2.332  15.622 1.00 29.37  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.532 -1.023  15.831 1.00 31.24  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 36.952 -1.071  15.265 1.00 35.57  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.715 -1.970  15.613 1.00 32.89  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.540 -0.638  17.318 1.00 32.76  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.251 0.676   17.539 1.00 42.91  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.601 1.728   17.403 1.00 47.99  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.475 0.652   17.784 1.00 41.19  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.302 -0.095  14.405 1.00 37.01  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.596 -0.018  13.724 1.00 38.48  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.810 -0.047  14.660 1.00 41.64  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 40.878 -0.475  14.217 1.00 43.62  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.659 1.186   12.771 1.00 42.07  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.848 0.986   11.492 1.00 57.47  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.669 0.402   15.932 1.00 34.52  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.768 0.325   16.892 1.00 33.41  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.677 -0.925  17.752 1.00 36.97  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.695 -1.561  18.009 1.00 38.50  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.789 1.539   17.843 1.00 33.98  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.407 2.813   17.303 1.00 40.19  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.344 3.913   18.345 1.00 41.28  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 42.857 2.606   16.858 1.00 45.02  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.480 -1.233  18.281 1.00 30.93  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.324 -2.352  19.207 1.00 28.90  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.472 -3.715  18.540 1.00 34.14  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.888 -4.656  19.205 1.00 33.68  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.012 -2.269  20.007 1.00 28.62  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 37.904 -1.039  20.899 1.00 28.96  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.615 -1.097  21.706 1.00 26.33  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.301 0.221   22.386 1.00 31.15  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.753 1.229   21.450 1.00 33.32  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.199 -3.800  17.223 1.00 33.23  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.337 -5.042  16.445 1.00 33.42  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.733 -5.666  16.595 1.00 37.98  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 40.870 -6.880  16.420 1.00 38.00  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 38.985 -4.811  14.976 1.00 35.32  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.144 -3.733  14.080 1.00 41.60  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.762 -4.826  16.882 1.00 34.06  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.163 -5.235  16.991 1.00 34.93  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.643 -5.521  18.411 1.00 37.52  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.813 -5.870  18.612 1.00 36.51  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.076 -4.203  16.300 1.00 35.96  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 43.821 -4.124  14.803 1.00 48.41  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.739 -3.039  14.223 1.00 49.47  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.636 -5.267  14.145 1.00 39.55  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.757 -5.367  19.403 1.00 33.83  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.148 -5.629  20.780 1.00 32.65  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.145 -7.125  21.053 1.00 35.25  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.273 -7.841  20.544 1.00 33.65  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.202 -4.918  21.766 1.00 32.61  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.167 -3.385  21.680 1.00 37.31  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.075 -2.835  22.580 1.00 36.98  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.527 -2.764  22.046 1.00 39.12  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.110 -7.597  21.854 0.51 32.61  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.118 -7.583  21.856 0.49 32.44  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.200 -9.014  22.223 0.51 31.89  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.271 -8.986  22.252 0.49 31.71  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.596 -9.241  23.616 0.51 32.36  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.631 -9.231  23.623 0.49 32.33  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.400 -10.387 24.022 0.51 30.21  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.443 -10.382 24.019 0.49 30.22  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.648 -9.495  22.172 0.51 37.01  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.750 -9.361  22.292 0.49 36.37  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.456 -8.780  23.090 0.51 44.92  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.305 -9.363  20.987 0.49 42.55  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.323 -8.141  24.355 1.00 29.16  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.718 -8.182  25.692 1.00 28.95  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.537 -7.203  25.730 1.00 30.30  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.681 -6.035  25.323 1.00 29.39  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.750 -7.846  26.819 1.00 33.98  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.091 -7.839  28.205 1.00 33.90  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 44.948 -8.800  26.798 1.00 34.54  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.382 -7.685  26.219 1.00 24.35  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.183 -6.869  26.418 1.00 23.33  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.791 -6.983  27.882 1.00 26.99  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.563 -8.096  28.366 1.00 26.96  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.019 -7.259  25.461 1.00 25.34  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.414 -7.092  23.952 1.00 26.16  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.717 -6.518  25.813 1.00 26.44  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.762 -5.637  23.478 1.00 29.47  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.691 -5.829  28.585 1.00 25.18  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.298 -5.819  29.980 1.00 25.74  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.819 -5.496  30.094 1.00 28.13  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.391 -4.417  29.667 1.00 26.02  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.117 -4.791  30.782 1.00 29.74  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.596 -4.989  30.695 1.00 48.64  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.131 -6.024  31.082 1.00 38.15  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.291 -3.986  30.207 1.00 44.86  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.048 -6.402  30.703 1.00 23.70  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.624 -6.163  30.896 1.00 23.37  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.388 -5.267  32.105 1.00 27.01  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.264 -5.122  32.977 1.00 27.07  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.808 -7.469  31.043 1.00 22.56  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.858 -8.512  29.882 1.00 24.70  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.699 -9.532  30.028 1.00 25.71  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.828 -7.844  28.497 1.00 24.65  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.186 -4.701  32.178 1.00 24.24  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.760 -3.829  33.282 1.00 25.30  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 32.952 -4.587  34.617 1.00 29.78  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.627 -5.776  34.684 1.00 28.46  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.293 -3.433  33.077 1.00 26.98  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.736 -2.423  34.067 1.00 35.51  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.631 -2.758  35.269 1.00 36.39  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.359 -1.325  33.635 1.00 35.82  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.517 -3.938  35.655 1.00 30.16  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.757 -4.658  36.931 1.00 30.35  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.531 -5.241  37.615 1.00 33.41  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.696 -6.077  38.497 1.00 33.94  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.443 -3.614  37.828 1.00 33.30  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.183 -2.298  37.192 1.00 38.55  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 33.991 -2.538  35.725 1.00 32.84  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.317 -4.820  37.227 1.00 30.55  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.075 -5.329  37.822 1.00 31.79  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.770 -6.745  37.266 1.00 30.98  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 28.940 -7.462  37.825 1.00 30.59  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.904 -4.376  37.492 1.00 34.40  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.757 -4.408  38.486 1.00 54.64  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 27.974 -3.546  39.715 1.00 83.40  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.036 -2.303  39.568 1.00 85.02  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.080 -4.113  40.827 1.00 77.75  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.428 -7.137  36.169 1.00 26.51  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.183 -8.437  35.543 1.00 26.18  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.762 -9.572  36.362 1.00 29.87  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 31.927 -9.545  36.760 1.00 29.26  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.649 -8.461  34.063 1.00 28.28  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 29.942 -7.344  33.249 1.00 28.33  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.411 -9.848  33.442 1.00 25.91  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.331 -7.380  33.251 1.00 32.41  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 29.927 -10.554 36.612 1.00 29.61  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.254 -11.732 37.398 1.00 30.22  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.007 -12.762 36.541 1.00 30.26  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.475 -13.170 35.510 1.00 28.47  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 28.959 -12.318 37.966 1.00 32.50  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.164 -13.585 38.741 1.00 45.33  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.852 -14.664 38.255 1.00 34.91  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.702 -13.479 39.956 1.00 37.55  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.222 -13.216 36.958 1.00 27.35  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 32.968 -14.208 36.150 1.00 26.85  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.214 -15.520 35.896 1.00 29.95  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.318 -16.063 34.789 1.00 28.51  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.241 -14.447 36.970 1.00 30.36  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.386 -13.228 37.819 1.00 34.79  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 32.993 -12.817 38.155 1.00 30.55  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.447 -16.028 36.897 1.00 27.23  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.696 -17.271 36.687 1.00 26.89  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.604 -17.075 35.618 1.00 28.22  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.473 -17.924 34.744 1.00 25.61  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.102 -17.817 37.997 1.00 29.23  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.482 -19.190 37.772 1.00 35.51  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.694 -19.807 38.912 1.00 59.19  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.725 -21.053 39.028 1.00 58.37  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.033 -19.064 39.674 1.00 51.38  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.874 -15.950 35.683 1.00 26.56  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.848 -15.610 34.697 1.00 26.19  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.448 -15.551 33.301 1.00 26.57  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.889 -16.097 32.330 1.00 23.96  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.631 -14.930 33.202 1.00 23.07  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.321 -14.860 31.910 1.00 21.35  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.717 -16.266 31.445 1.00 23.06  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.530 -16.601 30.275 1.00 22.99  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.574 -13.958 31.978 1.00 22.98  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.182 -13.833 30.599 1.00 23.16  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.608 -12.998 29.641 1.00 26.52  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.233 -14.659 30.207 1.00 24.12  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.112 -12.948 28.340 1.00 26.89  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.740 -14.605 28.906 1.00 25.80  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.157 -13.770 27.973 1.00 24.30  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.294 -17.070 32.345 1.00 22.84  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.697 -18.440 32.015 1.00 25.22  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.518 -19.263 31.449 1.00 25.63  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.665 -19.943 30.424 1.00 23.79  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.312 -19.123 33.231 1.00 29.08  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.008 -20.752 32.860 1.00 34.76  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.342 -19.183 32.118 1.00 23.58  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.130 -19.897 31.710 1.00 21.91  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.725 -19.450 30.308 1.00 22.82  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.382 -20.289 29.455 1.00 20.96  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 27.006 -19.661 32.755 1.00 24.51  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.302 -20.474 34.063 1.00 25.34  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.596 -19.960 32.171 1.00 24.39  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.573 -20.004 35.260 1.00 30.19  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.806 -18.148 30.059 1.00 20.39  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.447 -17.609 28.739 1.00 20.39  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.449 -17.960 27.665 1.00 21.87  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.045 -18.241 26.536 1.00 20.68  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.185 -16.111 28.803 1.00 21.22  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.894 -15.739 29.565 1.00 26.14  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.798 -14.267 29.728 1.00 27.13  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.630 -16.251 28.854 1.00 26.94  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.756 -17.938 27.990 1.00 20.16  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.783 -18.342 27.020 1.00 19.10  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.552 -19.822 26.620 1.00 22.05  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.598 -20.162 25.434 1.00 20.84  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.174 -18.131 27.626 1.00 19.18  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.339 -18.439 26.661 1.00 22.93  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.294 -17.532 25.409 1.00 22.42  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.703 -18.307 27.395 1.00 25.48  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.272 -20.696 27.602 1.00 19.66  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 29.948 -22.093 27.312 1.00 19.65  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.739 -22.184 26.391 1.00 21.56  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.767 -22.966 25.446 1.00 21.60  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.653 -22.834 28.617 1.00 22.48  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.893 -23.177 29.422 1.00 35.37  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.013 -23.096 28.860 1.00 35.45  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.745 -23.532 30.609 1.00 35.75  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.677 -21.411 26.675 1.00 19.90  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.482 -21.350 25.819 1.00 18.10  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.857 -20.961 24.381 1.00 19.24  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.403 -21.591 23.408 1.00 17.55  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.430 -20.382 26.394 1.00 18.90  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.316 -20.108 25.404 1.00 19.35  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.364 -21.080 25.120 1.00 21.75  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.296 -18.924 24.662 1.00 22.22  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.377 -20.861 24.155 1.00 21.03  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.295 -18.703 23.696 1.00 24.77  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.347 -19.674 23.452 1.00 23.24  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.665 -19.914 24.235 1.00 16.83  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.058 -19.485 22.880 1.00 16.92  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.619 -20.628 22.054 1.00 20.42  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.285 -20.761 20.879 1.00 19.74  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.139 -18.395 22.970 1.00 17.65  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.634 -17.120 23.583 1.00 19.50  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 29.973 -15.886 23.485 1.00 22.47  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.308 -14.645 24.653 1.00 22.80  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.490 -21.446 22.670 1.00 17.31  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.171 -22.545 21.977 1.00 17.37  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.427 -23.874 21.948 1.00 21.51  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.909 -24.830 21.327 1.00 21.05  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.557 -22.762 22.601 1.00 18.75  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.593 -21.772 22.109 1.00 19.44  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.751 -20.530 22.729 1.00 20.83  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.457 -22.099 21.058 1.00 20.90  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.724 -19.619 22.288 1.00 20.70  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.459 -21.217 20.642 1.00 21.30  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.565 -19.970 21.236 1.00 22.79  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.590 -19.155 20.833 1.00 20.88  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.282 -23.977 22.644 1.00 18.93  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.586 -25.283 22.706 1.00 19.82  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.069 -25.270 22.476 1.00 22.00  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.506 -26.363 22.282 1.00 20.75  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.763 -25.942 24.114 1.00 22.33  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.076 -25.164 25.112 1.00 22.25  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.231 -26.165 24.514 1.00 22.64  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.414 -24.085 22.554 0.67 18.37  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.420 -24.086 22.593 0.33 18.45  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 23.939 -23.888 22.503 0.67 17.97  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 23.959 -23.858 22.541 0.33 18.30  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.281 -24.270 23.843 0.67 20.83  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.272 -24.359 23.832 0.33 22.19  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.086 -24.058 24.004 0.67 20.88  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.044 -24.375 23.908 0.33 22.41  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.278 -24.695 21.382 0.67 18.85  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.323 -24.482 21.295 0.33 20.29  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.898 -24.495 20.126 0.67 17.21  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.021 -25.857 21.468 0.33 22.91  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.066 -24.790 24.816 0.67 19.23  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.075 -24.742 24.851 0.33 19.65  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.528 -25.216 26.115 0.67 19.20  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.595 -25.266 26.133 0.33 20.03  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.771 -24.172 27.177 0.67 23.36  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.802 -24.228 27.229 0.33 23.91  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.902 -23.711 27.359 0.67 21.31  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.932 -23.780 27.449 0.33 22.58  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.129 -26.561 26.560 0.67 21.96  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.314 -26.590 26.492 0.33 21.54  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.853 -27.721 25.589 0.67 26.79  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.205 -27.689 25.422 0.33 28.62  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.848 -28.858 25.814 0.67 33.26  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.037 -28.622 25.671 0.33 32.51  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.767 -29.388 27.178 0.67 43.41  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.910 -29.662 24.645 0.33 35.63  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 23.962 -30.379 27.545 0.67 55.65  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.213 -30.943 24.831 0.33 48.58  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.175 -30.967 26.653 0.67 43.87  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.047 -31.820 23.850 0.33 37.18  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 23.942 -30.793 28.803 0.67 42.42  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.669 -31.361 26.005 0.33 35.03  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.712 -23.846 27.912 1.00 21.04  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.760 -22.839 28.971 1.00 20.52  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.538 -23.481 30.320 1.00 25.84  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.477 -24.073 30.556 1.00 25.29  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.695 -21.777 28.688 1.00 20.96  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.743 -20.559 29.624 1.00 23.86  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.025 -19.728 29.371 1.00 22.27  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.481 -19.707 29.475 1.00 26.80  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.530 -23.353 31.220 1.00 24.49  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.432 -23.927 32.573 1.00 25.89  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.727 -22.921 33.504 1.00 30.80  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.365 -22.231 34.299 1.00 30.72  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.827 -24.334 33.092 1.00 30.51  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.806 -24.954 34.482 1.00 46.47  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.807 -25.524 34.915 1.00 36.93  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.903 -24.837 35.217 1.00 40.79  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.416 -22.806 33.343 1.00 28.40  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.589 -21.866 34.089 1.00 29.78  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.066 -22.532 35.359 1.00 33.52  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.428 -23.596 35.298 1.00 33.09  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.463 -21.395 33.153 1.00 30.77  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.709 -20.133 33.488 1.00 37.03  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.672 -18.921 33.589 1.00 37.76  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.623 -19.887 32.436 1.00 36.58  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.437 -21.953 36.523 1.00 30.70  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.080 -22.472 37.851 1.00 32.39  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.553 -21.341 38.732 1.00 33.63  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.870 -20.168 38.502 1.00 31.95  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.304 -23.129 38.530 1.00 34.49  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.927 -24.288 37.741 1.00 40.75  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.165 -24.874 38.407 1.00 58.11  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.878 -25.483 39.712 1.00 75.80  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.486 -26.742 39.895 1.00 96.37  ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.240 -27.196 41.118 1.00 83.20  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.320 -27.553 38.854 1.00 86.94  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.730 -21.682 39.732 1.00 32.30  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.189 -20.672 40.645 1.00 32.38  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.301 -19.774 41.225 1.00 37.33  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.124 -18.557 41.301 1.00 37.35  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.392 -21.356 41.782 1.00 35.31  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.760 -20.383 42.761 1.00 46.02  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.029 -21.027 43.924 1.00 75.11  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.601 -21.934 44.574 1.00 69.36  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.879 -20.613 44.193 1.00 74.75  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.436 -20.381 41.577 1.00 35.53  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.570 -19.678 42.178 1.00 36.09  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.358 -18.775 41.243 1.00 36.61  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.085 -17.891 41.704 1.00 37.04  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.219 -18.969 39.926 1.00 32.25  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 22.984 -18.167 38.973 1.00 29.76  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.136 -17.313 38.021 1.00 33.30  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.716 -16.512 37.276 1.00 32.07  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 23.949 -19.078 38.185 1.00 28.27  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.292 -20.007 37.178 1.00 35.80  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.239 -19.707 36.614 1.00 28.46  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 23.928 -21.138 36.889 1.00 29.90  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.790 -17.506 37.996 1.00 30.42  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.918 -16.844 37.004 1.00 30.16  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.040 -15.314 36.989 1.00 31.05  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.053 -14.717 35.902 1.00 28.70  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.435 -17.287 37.067 1.00 34.23  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.631 -16.720 35.857 1.00 34.08  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.780 -16.979 38.423 1.00 34.02  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.453 -17.552 35.423 1.00 37.60  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.136 -14.684 38.161 1.00 29.55  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.265 -13.230 38.200 1.00 29.95  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.567 -12.752 37.558 1.00 31.78  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.529 -11.822 36.749 1.00 30.27  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.092 -12.683 39.628 1.00 34.01  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.717 -12.990 40.228 1.00 40.92  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.308 -12.529 39.181 1.00 46.95  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.244 -10.772 39.470 1.00 45.61  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.709 -13.418 37.872 1.00 29.41  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.020 -13.064 37.292 1.00 29.00  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.043 -13.363 35.797 1.00 29.49  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.578 -12.569 35.019 1.00 27.54  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.142 -13.821 37.991 1.00 30.58  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.463 -14.501 35.386 1.00 25.26  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.407 -14.860 33.960 1.00 23.01  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.603 -13.821 33.177 1.00 26.39  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.093 -13.346 32.143 1.00 24.58  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.904 -16.314 33.745 1.00 25.97  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.615 -16.609 32.261 1.00 23.85  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.927 -17.303 34.287 1.00 26.38  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.399 -13.453 33.666 0.20 24.95  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.395 -13.457 33.663 0.80 25.51  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.548 -12.460 33.006 0.20 25.70  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.574 -12.461 32.964 0.80 26.85  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.249 -11.108 32.870 0.20 29.70  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.273 -11.101 32.856 0.80 29.75  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.230 -10.526 31.784 0.20 28.87  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.254 -10.488 31.785 0.80 28.57  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.208 -12.296 33.732 0.20 29.20  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.200 -12.303 33.615 0.80 29.95  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.237 -11.427 32.972 0.20 33.23  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.285 -11.374 32.828 0.80 33.35  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.735 -11.116 33.900 0.20 38.78  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.605 -11.374 33.483 0.80 38.06  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.167 -9.682  33.069 0.20 36.20  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.815 -10.385 35.044 0.80 36.53  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.872 -10.619 33.964 1.00 27.12  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.600 -9.334  33.973 1.00 27.86  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.767 -9.373  32.968 1.00 28.23  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 23.927 -8.432  32.176 1.00 26.31  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.104 -9.028  35.377 1.00 29.14  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.504 -10.509 32.919 1.00 24.98  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.613 -10.665 31.975 1.00 24.03  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.079 -10.703 30.524 1.00 25.62  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.656 -10.040 29.653 1.00 22.99  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.540 -11.848 32.352 1.00 26.68  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.847 -11.813 33.755 1.00 26.21  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.853 -11.843 31.549 1.00 25.70  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 23.973 -11.455 30.267 1.00 23.12  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.382 -11.545 28.921 1.00 21.92  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.854 -10.183 28.449 1.00 24.94  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.019 -9.845  27.275 1.00 23.95  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.293 -12.619 28.875 1.00 22.60  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.302 -9.353  29.372 1.00 23.20  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.856 -8.005  28.981 1.00 23.00  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.056 -7.128  28.548 1.00 25.83  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.021 -6.480  27.503 1.00 25.49  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.081 -7.353  30.139 1.00 26.11  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.715 -7.980  30.361 1.00 31.10  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 18.988 -7.403  31.919 1.00 39.07  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.658 -5.689  31.475 1.00 37.11  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.134 -7.179  29.320 1.00 23.21  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.369 -6.435  29.042 1.00 22.77  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 25.979 -6.907  27.710 1.00 25.72  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.366 -6.082  26.869 1.00 24.02  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.347 -6.699  30.188 1.00 23.47  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.754 -6.191  29.957 1.00 23.78  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.051 -4.831  30.045 1.00 27.00  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.804 -7.078  29.711 1.00 23.07  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.353 -4.361  29.845 1.00 24.48  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.111 -6.624  29.551 1.00 22.96  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.380 -5.265  29.631 1.00 26.12  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.673 -4.858  29.518 1.00 25.05  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.031 -8.234  27.507 1.00 22.73  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.609 -8.818  26.284 1.00 20.84  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.673 -8.712  25.079 1.00 24.16  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.093 -8.969  23.950 1.00 23.51  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.022 -10.280 26.520 1.00 20.00  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.157 -10.543 27.528 1.00 22.11  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.433 -12.070 27.614 1.00 21.86  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.457 -9.801  27.126 1.00 24.66  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.408 -8.329  25.311 1.00 21.57  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.406 -8.201  24.240 1.00 21.64  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.167 -9.558  23.566 1.00 25.24  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.418 -9.747  22.376 1.00 24.45  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.783 -7.102  23.228 1.00 22.15  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 23.913 -5.703  23.863 1.00 25.07  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.612 -4.747  22.934 1.00 35.27  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.506 -4.844  21.723 1.00 29.70  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.354 -3.803  23.482 1.00 32.23  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.706 -10.512 24.377 1.00 22.47  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.377 -11.884 23.958 1.00 22.10  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.881 -12.053 24.219 1.00 27.74  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.454 -12.536 25.277 1.00 25.40  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.247 -12.858 24.753 1.00 22.99  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.730 -12.707 24.430 1.00 24.05  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.749 -13.769 25.450 1.00 26.80  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.389 -15.414 24.658 1.00 23.94  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.081 -11.529 23.276 1.00 27.45  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.617 -11.399 23.385 1.00 29.10  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.864 -12.676 23.733 1.00 29.45  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 16.963 -12.617 24.562 1.00 28.62  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.011 -10.770 22.119 1.00 31.94  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.542 -9.372  21.842 1.00 45.70  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.206 -13.816 23.110 1.00 26.23  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.471 -15.050 23.409 1.00 27.86  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.712 -15.524 24.838 1.00 29.18  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.768 -15.992 25.494 1.00 29.77  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.780 -16.141 22.384 1.00 29.59  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.354 -15.781 20.995 1.00 34.76  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.025 -15.543 20.688 1.00 38.71  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.088 -15.685 19.863 1.00 36.78  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 15.998 -15.263 19.395 1.00 38.47  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.212 -15.345 18.854 1.00 37.74  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 18.958 -15.358 25.339 1.00 23.24  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.296 -15.717 26.722 1.00 23.05  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.510 -14.812 27.683 1.00 29.11  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.901 -15.310 28.637 1.00 27.93  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.817 -15.711 27.021 1.00 25.98  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.070 -15.956 28.510 1.00 26.13  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.539 -16.760 26.176 1.00 25.35  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.502 -13.489 27.417 1.00 25.64  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.750 -12.535 28.258 1.00 26.12  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.260 -12.958 28.338 1.00 31.61  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.715 -13.038 29.433 1.00 30.40  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.930 -11.058 27.794 1.00 28.56  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.090 -10.101 28.655 1.00 29.35  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.400 -10.643 27.830 1.00 27.42  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.662 -13.316 27.189 0.61 30.13  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.628 -13.215 27.176 0.39 30.02  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.279 -13.775 27.065 0.61 31.53  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.225 -13.622 27.038 0.39 31.50  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 13.971 -15.007 27.933 0.61 33.90  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.858 -14.832 27.900 0.39 35.08  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 12.984 -14.974 28.673 0.61 34.47  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.841 -14.794 28.594 0.39 35.96  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.940 -14.046 25.587 0.61 33.65  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.893 -13.910 25.558 0.39 33.50  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.493 -14.441 25.345 0.61 46.36  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.684 -12.690 24.677 0.39 44.77  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.596 -13.633 25.666 0.61 49.20  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.273 -11.636 25.206 0.39 47.42  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.262 -15.553 24.827 0.61 51.36  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.902 -12.799 23.451 0.39 51.68  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.801 -16.082 27.862 0.61 28.84  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.687 -15.894 27.866 0.39 30.31  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.530 -17.280 28.682 0.61 29.18  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.437 -17.123 28.630 0.39 30.60  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.729 -17.001 30.175 0.61 32.39  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.641 -16.894 30.134 0.39 33.49  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.043 -17.612 30.994 0.61 32.15  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.859 -17.422 30.926 0.39 33.76  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.280 -18.541 28.212 0.61 29.35  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.231 -18.304 28.063 0.39 35.75  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.694 -19.670 28.867 0.61 30.75  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.218 -18.226 26.637 0.39 34.21  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.781 -18.507 28.510 0.61 23.59  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.648 -19.640 28.482 0.39 35.65  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.664 -16.095 30.523 1.00 29.37  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.923 -15.722 31.933 1.00 30.03  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.702 -15.019 32.488 1.00 35.46  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.239 -15.378 33.585 1.00 34.42  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.160 -14.840 32.050 1.00 29.71  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.718 -15.730 31.858 1.00 31.95  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.152 -14.049 31.716 0.48 33.28  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.157 -14.038 31.733 0.52 33.54  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.951 -13.280 32.075 0.48 34.96  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 12.961 -13.289 32.133 0.52 35.29  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.763 -14.213 32.330 0.48 39.19  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.755 -14.218 32.341 0.52 39.26  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.027 -14.032 33.304 0.48 39.52  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.005 -14.043 33.305 0.52 39.48  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.588 -12.281 30.960 0.48 35.95  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.634 -12.191 31.114 0.52 36.82  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.536 -11.102 30.844 0.48 48.48  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.414 -10.901 31.342 0.52 50.85  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.933 -9.959  30.047 0.48 61.19  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.714 -9.704  30.718 0.52 62.15  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.938 -8.953  29.698 0.48 66.23  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.848 -9.687  29.258 0.52 66.48  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.283 -7.926  30.469 0.48 77.29  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.624 -8.845  28.584 0.52 75.61  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.701 -7.745  31.649 0.48 68.26  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.339 -7.927  29.226 0.52 59.47  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.213 -7.070  30.067 0.48 58.82  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.687 -8.907  27.261 0.52 60.05  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.598 -15.221 31.458 1.00 35.52  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.512 -16.211 31.538 1.00 37.07  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.664 -17.125 32.752 1.00 40.61  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.681  -17.345 33.464 1.00 40.34  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.396 -17.013 30.234 1.00 39.11  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.824  -16.170 29.100 1.00 57.38  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.711  -16.917 27.789 1.00 69.71  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.288  -15.973 26.689 1.00 83.65  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.458  -16.652 25.663 1.00 96.39  ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.899 -17.613 33.018 1.00 35.62  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.178 -18.482 34.172 1.00 35.92  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 11.991 -17.722 35.481 1.00 40.48  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.478 -18.295 36.450 1.00 39.32  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.584 -19.085 34.081 1.00 35.97  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.699 -20.367 33.276 1.00 36.59  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.135 -20.469 32.006 1.00 39.17  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.444 -21.442 33.754 1.00 38.84  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.250 -21.655 31.261 1.00 39.88  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.573 -22.620 32.999 1.00 40.10  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 13.982 -22.714 31.758 1.00 37.54  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.354 -16.423 35.497 1.00 36.52  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.156 -15.577 36.687 1.00 37.79  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.656 -15.335 36.945 1.00 44.97  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.203 -15.496 38.086 1.00 45.59  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.000 -14.272 36.620 1.00 39.82  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.496 -14.610 36.775 1.00 38.73  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.563 -13.258 37.714 1.00 42.00  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.437 -13.596 36.226 1.00 42.87  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.883  -15.008 35.878 1.00 43.29  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.437  -14.762 35.961 1.00 45.84  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.675  -15.988 36.493 1.00 50.20  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.695  -15.826 37.217 1.00 50.47  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.871  -14.322 34.604 1.00 49.20  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.147  -17.205 36.161 1.00 45.15  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.525  -18.450 36.625 1.00 46.43  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.694  -18.686 38.137 1.00 52.36  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.826  -19.298 38.748 1.00 53.15  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.088  -19.633 35.846 1.00 45.50  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.809  -18.228 38.730 1.00 50.37  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.109  -18.439 40.150 1.00 53.00  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.541  -17.368 41.097 1.00 61.62  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.566  -17.573 42.316 1.00 64.00  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.613 -18.598 40.361 1.00 56.78  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 11.009 -19.952 40.198 1.00 67.48  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.003  -16.253 40.555 1.00 58.20  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.434  -15.171 41.375 1.00 76.08  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 6.005  -15.465 41.860 1.00 119.72 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.586  -16.619 41.927 1.00 87.78  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.520  -13.810 40.656 1.00 76.57  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.492  -13.592 39.555 1.00 86.38  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.657  -12.353 38.692 1.00 106.91 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.794  -11.836 38.581 1.00 98.19  ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.642  -11.910 38.108 1.00 100.59 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.208 -35.062 5.839  1.00 26.47  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.277 -33.918 6.321  1.00 27.52  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.424 -36.285 6.709  1.00 27.04  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.934 -35.302 4.559  0.66 24.81  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.949 -35.302 4.552  0.34 25.96  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.715 -34.249 3.574  0.66 23.54  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.662 -34.232 3.601  0.34 25.54  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.201 -34.104 3.276  0.66 28.14  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.154 -34.080 3.439  0.34 28.33  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.494 -35.114 3.172  0.66 27.96  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.407 -35.060 3.549  0.34 27.63  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.505 -34.573 2.288  0.66 22.61  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.331 -34.457 2.221  0.34 24.96  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.002 -34.563 2.478  0.66 22.80  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.719 -35.539 1.377  0.34 26.25  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.792 -35.603 2.878  0.66 25.38  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.130 -36.834 1.291  0.34 29.40  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.881 -33.449 2.274  0.66 22.21  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.626 -35.402 0.450  0.34 26.35  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.105 -35.200 2.955  0.66 24.69  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.327 -37.531 0.420  0.34 29.06  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.191 -33.885 2.578  0.66 25.33  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.400 -36.675 -0.117 0.34 30.42  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.688 -32.110 1.889  0.66 22.73  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.780 -34.339 0.085  0.34 27.27  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.307 -33.044 2.463  0.66 24.82  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.377 -36.911 -1.044 0.34 29.74  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.794 -31.283 1.769  0.66 23.73  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.770 -34.574 -0.834 0.34 28.96  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.082 -31.749 2.056  0.66 24.25  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.578 -35.845 -1.391 0.34 29.49  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.713 -32.857 3.148  1.00 24.02  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.292 -32.542 2.907  1.00 23.95  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.148 -31.487 1.806  1.00 26.15  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.122 -30.813 1.447  1.00 24.70  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.580 -32.035 4.205  1.00 26.90  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.608 -33.085 5.321  1.00 26.54  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.165 -30.693 4.690  1.00 26.30  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.908 -31.314 1.335  1.00 23.37  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.522 -30.230 0.448  1.00 22.62  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.143 -29.097 1.432  1.00 26.91  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.132 -29.233 2.136  1.00 26.60  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.323 -30.606 -0.454 1.00 24.19  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.625 -31.861 -1.353 1.00 22.36  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.867 -29.363 -1.282 1.00 26.09  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.961 -31.729 -2.294 1.00 27.50  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.938 -28.000 1.524  1.00 26.64  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.609 -26.936 2.495  1.00 27.31  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.383 -26.106 2.114  1.00 30.30  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.080 -25.958 0.930  1.00 28.82  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.881 -26.079 2.531  1.00 29.01  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.476 -26.250 1.144  1.00 33.21  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.173 -27.687 0.770  1.00 29.11  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.656 -25.605 3.123  1.00 29.74  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.444 -10.163 16.486 1.00 22.92  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.847 -8.898  16.523 1.00 23.57  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.829 -8.619  17.425 1.00 24.48  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.396 -9.634  18.274 1.00 25.77  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.228 -10.823 19.837 1.00 29.56  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.942 -10.913 18.212 1.00 24.82  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.227 -10.266 11.931 1.00 28.31  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.368 -10.599 13.266 1.00 27.26  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.330 -10.249 14.159 1.00 25.13  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.227 -11.774 19.212 1.00 27.19  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.398 -11.090 20.703 1.00 29.82  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.397 -9.605  19.253 1.00 27.57  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 24.969 -11.184 17.316 1.00 24.04  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.339 -10.572 15.481 1.00 23.06  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.237 -9.638  13.674 1.00 27.80  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.225 -9.388  12.377 1.00 31.04  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.776 -8.628  11.792 0.61 31.28  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 28.924 -11.497 13.846 0.79 25.35  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.138 -9.646  11.458 1.00 29.49  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.317 -15.380 22.682 1.00 35.16  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.543 -35.334 -1.307 0.66 39.86  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.222 -35.141 -0.715 0.66 41.65  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.591 -34.374 -0.242 0.66 38.69  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 17.989 -36.941 -0.757 0.66 39.10  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 25.746 -3.539  26.505 1.00 31.78  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 35.624 -25.835 25.526 1.00 37.20  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 26.792 -32.068 16.157 1.00 40.77  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 22.695 -5.449  19.860 1.00 49.70  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 41.039 -21.656 25.166 1.00 37.95  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 37.805 2.323   19.839 1.00 36.63  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 20.758 -5.908  26.205 1.00 37.32  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 38.376 -14.981 15.518 1.00 33.76  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 44.283 -0.907  17.894 1.00 46.88  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 37.149 -12.427 40.264 1.00 54.72  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 33.261 -20.835 29.573 1.00 42.08  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 29.752 -32.227 9.527  1.00 45.63  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 45.029 -11.394 18.783 1.00 60.95  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 16.414 -27.403 -3.222 1.00 47.74  ? 314 HOH   A O   1 
HETATM 1215 O  O   A HOH   F 6 .   ? 19.047 -22.938 4.396  0.67 42.31  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 19.932 -9.684  37.091 1.00 35.18  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 15.423 -10.028 25.031 1.00 48.26  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 28.321 -8.954  39.978 1.00 43.70  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 20.286 -13.541 20.653 1.00 42.08  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 27.204 -10.216 35.903 1.00 36.38  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 21.441 -27.131 14.676 0.50 30.58  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 22.635 -27.679 17.749 1.00 48.55  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 32.709 -24.607 32.133 1.00 56.66  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 37.638 -20.494 26.996 1.00 33.56  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 17.869 -29.453 7.681  1.00 30.20  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 31.602 -0.956  15.905 1.00 39.91  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 22.946 -28.246 12.645 1.00 21.94  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 30.322 1.374   33.904 1.00 63.32  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 25.616 -2.993  20.079 1.00 55.07  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 43.582 -6.662  32.057 1.00 45.82  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 23.347 -5.887  32.924 1.00 35.79  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 21.681 -29.501 -5.227 1.00 34.76  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 21.914 -25.001 18.336 1.00 21.39  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 28.744 -21.886 41.621 1.00 69.02  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 23.253 -17.020 44.280 1.00 61.91  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 34.409 -23.829 29.935 1.00 70.19  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 23.972 -15.875 21.299 1.00 28.32  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 41.242 -16.903 15.223 1.00 34.55  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 27.291 -28.223 18.632 1.00 24.53  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 41.373 -12.780 14.138 1.00 91.98  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 29.309 -27.406 20.635 1.00 21.84  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 24.853 -26.806 19.020 1.00 31.51  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 21.491 -30.032 14.223 1.00 69.43  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 30.432 -0.724  37.086 1.00 44.23  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 26.892 -35.303 11.590 1.00 51.94  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 28.235 -23.771 31.684 1.00 36.33  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 41.183 -1.482  11.683 1.00 56.86  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 36.802 -5.728  12.300 1.00 35.09  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 26.096 -22.668 29.946 1.00 26.01  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 17.988 -34.520 8.326  1.00 31.60  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 37.259 -6.453  34.346 1.00 38.24  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 42.404 -10.487 15.492 1.00 48.26  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 28.830 -0.518  16.906 1.00 69.69  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 20.860 -7.379  19.844 1.00 44.74  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 12.249 -18.098 25.919 1.00 55.12  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 10.791 -11.596 34.604 1.00 44.17  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 44.322 -12.716 41.385 1.00 48.55  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 28.955 -31.149 7.229  1.00 32.93  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 46.778 -21.566 18.217 1.00 44.04  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 30.626 -28.922 22.639 1.00 38.48  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 45.890 -14.259 21.570 1.00 53.12  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 28.499 -24.311 34.346 1.00 52.12  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 44.592 -16.384 29.739 1.00 50.57  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 26.353 -7.783  36.813 1.00 52.65  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 26.090 -21.918 38.661 1.00 34.49  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 43.869 -4.357  25.797 1.00 43.02  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 37.888 -16.645 13.138 0.50 24.95  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 14.301 -16.929 23.488 1.00 41.11  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 12.716 -20.610 42.403 1.00 52.87  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 46.139 -15.765 27.596 1.00 59.95  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 34.754 -18.963 13.877 0.50 19.28  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 27.564 -23.115 13.878 0.50 24.51  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 26.904 -16.653 38.665 1.00 49.80  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 26.052 -19.231 41.670 1.00 56.81  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 24.042 -28.650 21.514 1.00 51.76  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 47.126 -25.254 21.599 1.00 47.14  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 38.935 -18.907 33.457 1.00 42.29  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 20.255 -15.991 40.898 1.00 34.05  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 26.108 -8.116  9.072  1.00 40.48  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 19.902 -25.601 41.280 1.00 73.67  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 34.085 -7.991  35.712 1.00 33.77  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 45.398 -10.868 30.277 1.00 53.37  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 27.061 -2.443  16.081 1.00 61.90  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 34.745 -29.134 26.023 1.00 59.09  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 42.050 -6.064  11.894 1.00 62.74  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 11.668 -15.396 40.548 1.00 70.58  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 47.288 -6.740  20.350 1.00 66.26  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 18.002 -24.461 39.698 1.00 37.58  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 43.818 -10.637 35.150 1.00 73.08  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 45.161 -12.660 23.611 1.00 43.86  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 29.619 -22.704 36.820 1.00 59.30  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 23.600 -15.681 17.842 1.00 38.50  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 46.258 -19.015 19.707 1.00 48.21  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 41.182 -7.014  35.960 1.00 42.12  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 46.013 -8.987  44.100 1.00 46.71  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 40.342 -19.642 29.007 1.00 32.90  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 36.881 -2.258  11.573 1.00 55.76  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 31.846 -31.943 14.516 1.00 33.54  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 35.111 -29.718 23.404 1.00 42.33  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 30.387 -10.679 40.604 1.00 39.57  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 33.089 -29.836 21.487 1.00 42.21  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 17.323 -24.548 -2.088 1.00 64.33  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 16.769 -6.515  27.614 1.00 63.17  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 25.583 -4.650  17.941 1.00 47.87  ? 404 HOH   A O   1 
HETATM 1305 O  O   A HOH   F 6 .   ? 12.052 -20.620 27.896 0.66 43.25  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 22.895 -14.987 40.391 1.00 31.54  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 26.474 -30.791 19.014 1.00 54.28  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 10.421 -11.691 40.014 1.00 60.03  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 45.718 -17.054 17.267 1.00 64.91  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 46.967 -20.328 21.949 1.00 62.73  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 27.226 -25.464 28.406 1.00 54.63  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 35.195 1.875   13.533 1.00 51.51  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 4.217  -20.507 37.845 1.00 60.31  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 41.232 -17.100 35.206 1.00 42.42  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 19.626 -27.328 10.054 1.00 52.62  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 26.939 -1.641  22.049 1.00 52.58  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 44.612 -8.839  17.967 1.00 64.69  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 33.501 -0.369  20.162 1.00 40.04  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 32.360 -9.024  39.732 1.00 53.45  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 21.141 -23.309 42.066 1.00 45.15  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 33.526 -33.004 12.082 1.00 45.65  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 32.159 -15.732 39.854 1.00 33.18  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 41.966 -8.066  13.756 1.00 56.23  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 29.465 -0.893  22.273 1.00 53.12  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 25.592 -16.129 41.072 1.00 48.32  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 33.990 -32.852 21.905 1.00 60.15  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 34.492 -18.905 36.188 1.00 62.55  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 39.838 -5.611  33.963 1.00 39.83  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 45.751 -5.516  23.706 1.00 46.13  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 42.787 -18.235 30.732 1.00 44.95  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 22.229 -10.503 14.622 1.00 40.80  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 23.436 -30.585 19.337 1.00 59.98  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 31.969 -0.026  13.365 1.00 59.81  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 31.843 -26.245 27.082 1.00 49.23  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 26.340 -29.557 22.680 1.00 56.50  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 23.022 -3.192  26.849 1.00 62.02  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 44.389 -4.323  28.930 1.00 62.65  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 26.965 -34.479 17.966 1.00 61.06  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 37.015 -31.639 23.383 1.00 74.24  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 28.787 -2.658  13.059 1.00 70.65  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 19.465 -31.829 13.988 1.00 61.24  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 30.592 -34.347 14.856 1.00 56.62  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 36.658 -24.514 27.632 1.00 50.59  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 19.838 -8.165  24.551 1.00 50.50  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 47.936 -23.497 19.724 1.00 57.85  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 35.317 -4.252  10.645 1.00 43.36  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 24.485 -21.750 41.100 1.00 54.77  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 46.644 -14.699 18.297 1.00 63.76  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 47.378 -28.461 17.638 1.00 58.12  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 34.114 -17.690 39.427 1.00 58.57  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 47.136 -11.911 25.331 1.00 61.96  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 11.908 -18.762 22.613 1.00 62.56  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 35.867 -21.227 30.497 1.00 57.67  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 32.129 -1.125  22.368 1.00 53.00  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 19.387 -7.756  35.288 1.00 52.65  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 46.985 -12.607 28.392 1.00 57.17  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 43.957 -13.650 13.877 0.50 81.78  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 25.317 -5.694  34.970 1.00 58.28  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 20.145 -35.284 10.096 1.00 36.88  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 45.539 -8.410  31.342 1.00 60.96  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 17.057 -28.142 9.882  1.00 48.36  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 19.822 -14.984 43.366 1.00 47.51  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 17.197 -8.045  25.061 1.00 63.15  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 43.133 -3.021  33.988 1.00 58.20  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 19.098 -28.228 13.798 0.50 64.16  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 32.521 -20.628 36.952 1.00 66.63  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 28.288 -29.854 24.572 1.00 63.87  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 33.800 -11.146 41.632 0.50 61.81  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 33.800 -14.068 41.632 0.50 36.93  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 16.704 -6.892  34.868 1.00 65.77  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 32.047 -23.868 34.917 1.00 68.21  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 21.149 -5.755  34.699 1.00 48.30  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 12.403 -18.327 19.925 1.00 58.37  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 45.092 -12.293 15.957 1.00 68.06  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 39.377 -5.647  11.497 1.00 57.55  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   F 6 .   ? 16.717 -29.902 12.348 1.00 53.85  ? 476 HOH   A O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 12.160 -24.244 0.059  1.00 47.96  ? 201 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 17.720 -36.174 6.034  1.00 38.50  ? 202 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 14.871 -25.706 -1.759 1.00 41.61  ? 203 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 22.577 -34.041 8.868  1.00 33.05  ? 204 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 20.795 -38.260 4.013  1.00 46.77  ? 205 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 11.387 -23.555 3.166  1.00 50.74  ? 206 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 20.798 -39.492 -2.182 1.00 51.11  ? 207 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 10.613 -24.656 5.552  1.00 54.38  ? 208 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.646 -36.480 9.968  1.00 47.65  ? 209 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   ? 0.7979 0.9524 0.6466 0.0299  -0.1279 -0.0198 6   ASP A N   
2    C CA  . ASP A 5   ? 0.7912 0.9397 0.6233 0.0144  -0.1192 -0.0221 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7654 0.9429 0.6215 0.0037  -0.1155 -0.0373 6   ASP A C   
4    O O   . ASP A 5   ? 0.7555 0.9578 0.6400 0.0075  -0.1194 -0.0461 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8145 0.9369 0.6380 0.0059  -0.1022 -0.0160 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0084 1.1110 0.7994 -0.0041 -0.0969 -0.0120 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0059 1.1199 0.7956 -0.0147 -0.0941 -0.0203 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1145 1.1897 0.8812 -0.0023 -0.0943 -0.0013 6   ASP A OD2 
9    N N   . SER A 6   ? 0.6569 0.8303 0.5010 -0.0102 -0.1071 -0.0412 7   SER A N   
10   C CA  . SER A 6   ? 0.6090 0.8033 0.4709 -0.0220 -0.1014 -0.0551 7   SER A CA  
11   C C   . SER A 6   ? 0.5530 0.7361 0.4263 -0.0319 -0.0832 -0.0572 7   SER A C   
12   O O   . SER A 6   ? 0.5342 0.7223 0.4116 -0.0435 -0.0754 -0.0662 7   SER A O   
13   C CB  . SER A 6   ? 0.6877 0.8853 0.5275 -0.0297 -0.1057 -0.0591 7   SER A CB  
14   O OG  . SER A 6   ? 0.8530 1.0243 0.6646 -0.0355 -0.0979 -0.0516 7   SER A OG  
15   N N   . CYS A 7   ? 0.4500 0.6179 0.3285 -0.0268 -0.0774 -0.0495 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4101 0.5669 0.2981 -0.0341 -0.0627 -0.0507 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4074 0.5799 0.3206 -0.0399 -0.0573 -0.0618 8   CYS A C   
18   O O   . CYS A 7   ? 0.3914 0.5837 0.3204 -0.0366 -0.0637 -0.0674 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4255 0.5649 0.3135 -0.0268 -0.0594 -0.0408 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5085 0.6209 0.3647 -0.0252 -0.0586 -0.0287 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3101 0.4730 0.2270 -0.0485 -0.0454 -0.0652 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2718 0.4399 0.2079 -0.0541 -0.0380 -0.0732 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2947 0.4463 0.2349 -0.0499 -0.0319 -0.0659 9   ILE A C   
24   O O   . ILE A 8   ? 0.2836 0.4204 0.2120 -0.0460 -0.0313 -0.0575 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3137 0.4808 0.2499 -0.0657 -0.0302 -0.0828 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3213 0.4690 0.2443 -0.0681 -0.0233 -0.0793 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.2984 0.4849 0.2326 -0.0706 -0.0365 -0.0916 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3805 0.5230 0.3048 -0.0777 -0.0145 -0.0887 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2259 0.3788 0.1811 -0.0518 -0.0267 -0.0697 10  GLN A N   
30   N N   B GLN A 9   ? 0.2354 0.3900 0.1912 -0.0513 -0.0275 -0.0698 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2235 0.3606 0.1809 -0.0483 -0.0214 -0.0632 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2285 0.3689 0.1879 -0.0477 -0.0224 -0.0638 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2591 0.3852 0.2206 -0.0555 -0.0118 -0.0676 10  GLN A C   
34   C C   B GLN A 9   ? 0.2803 0.4091 0.2432 -0.0552 -0.0126 -0.0680 10  GLN A C   
35   O O   A GLN A 9   ? 0.2668 0.4004 0.2355 -0.0626 -0.0087 -0.0763 10  GLN A O   
36   O O   B GLN A 9   ? 0.2819 0.4178 0.2518 -0.0626 -0.0092 -0.0768 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2420 0.3878 0.2103 -0.0409 -0.0254 -0.0612 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2372 0.3890 0.2092 -0.0413 -0.0265 -0.0635 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2916 0.4238 0.2645 -0.0398 -0.0185 -0.0575 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2583 0.3950 0.2292 -0.0350 -0.0238 -0.0550 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5342 0.6681 0.5121 -0.0305 -0.0223 -0.0523 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4184 0.5579 0.4036 -0.0366 -0.0184 -0.0590 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4554 0.5992 0.4332 -0.0229 -0.0310 -0.0504 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3390 0.4973 0.3383 -0.0377 -0.0198 -0.0670 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.4468 0.5690 0.4274 -0.0304 -0.0161 -0.0499 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3791 0.5007 0.3606 -0.0371 -0.0119 -0.0545 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2337 0.3409 0.1895 -0.0538 -0.0073 -0.0620 11  PHE A N   
48   N N   B PHE A 10  ? 0.2509 0.3610 0.2080 -0.0532 -0.0083 -0.0621 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2303 0.3233 0.1869 -0.0586 0.0000  -0.0648 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2517 0.3464 0.2088 -0.0578 -0.0008 -0.0642 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2677 0.3560 0.2295 -0.0565 0.0023  -0.0619 11  PHE A C   
52   C C   B PHE A 10  ? 0.2818 0.3719 0.2444 -0.0560 0.0017  -0.0617 11  PHE A C   
53   O O   A PHE A 10  ? 0.2624 0.3431 0.2217 -0.0505 0.0012  -0.0547 11  PHE A O   
54   O O   B PHE A 10  ? 0.2773 0.3614 0.2380 -0.0497 0.0002  -0.0546 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2512 0.3284 0.1999 -0.0573 0.0024  -0.0623 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2789 0.3587 0.2275 -0.0558 0.0009  -0.0607 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2647 0.3257 0.2120 -0.0609 0.0081  -0.0657 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3077 0.3904 0.2517 -0.0600 0.0015  -0.0661 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.2957 0.3559 0.2427 -0.0681 0.0117  -0.0738 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3530 0.4485 0.2924 -0.0602 -0.0032 -0.0665 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.2883 0.3329 0.2327 -0.0569 0.0094  -0.0610 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3516 0.4225 0.2943 -0.0634 0.0064  -0.0710 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3167 0.3570 0.2591 -0.0708 0.0169  -0.0761 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3679 0.4657 0.3016 -0.0652 -0.0018 -0.0723 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3202 0.3466 0.2599 -0.0589 0.0132  -0.0632 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3967 0.4702 0.3359 -0.0674 0.0079  -0.0773 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.2990 0.3216 0.2369 -0.0656 0.0171  -0.0703 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3670 0.4546 0.3018 -0.0691 0.0043  -0.0782 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2322 0.3258 0.2012 -0.0626 0.0062  -0.0685 12  THR A N   
70   C CA  . THR A 11  ? 0.2356 0.3269 0.2100 -0.0630 0.0101  -0.0682 12  THR A CA  
71   C C   . THR A 11  ? 0.2639 0.3330 0.2293 -0.0600 0.0130  -0.0610 12  THR A C   
72   O O   . THR A 11  ? 0.2649 0.3337 0.2327 -0.0554 0.0125  -0.0567 12  THR A O   
73   C CB  . THR A 11  ? 0.2966 0.3921 0.2765 -0.0736 0.0171  -0.0782 12  THR A CB  
74   O OG1 . THR A 11  ? 0.2929 0.4129 0.2831 -0.0759 0.0131  -0.0860 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3556 0.4510 0.3416 -0.0757 0.0226  -0.0798 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2463 0.2969 0.2016 -0.0623 0.0156  -0.0604 13  ARG A N   
77   C CA  . ARG A 12  ? 0.2626 0.2923 0.2086 -0.0594 0.0170  -0.0546 13  ARG A CA  
78   C C   . ARG A 12  ? 0.2810 0.3090 0.2251 -0.0511 0.0118  -0.0481 13  ARG A C   
79   O O   . ARG A 12  ? 0.2774 0.2905 0.2150 -0.0483 0.0118  -0.0443 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3484 0.3570 0.2836 -0.0638 0.0209  -0.0570 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.4902 0.4918 0.4220 -0.0741 0.0286  -0.0630 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.7590 0.7528 0.6870 -0.0767 0.0332  -0.0612 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.9228 0.8908 0.8351 -0.0730 0.0324  -0.0546 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.0658 1.0254 0.9721 -0.0732 0.0345  -0.0511 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.9340 0.8704 0.8245 -0.0695 0.0323  -0.0454 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8374 0.8125 0.7539 -0.0766 0.0385  -0.0540 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2293 0.2715 0.1775 -0.0480 0.0077  -0.0473 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2363 0.2755 0.1813 -0.0428 0.0049  -0.0428 14  HIS A CA  
89   C C   . HIS A 13  ? 0.2686 0.3015 0.2126 -0.0386 0.0046  -0.0372 14  HIS A C   
90   O O   . HIS A 13  ? 0.2675 0.2908 0.2080 -0.0364 0.0043  -0.0355 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2326 0.2848 0.1778 -0.0417 0.0016  -0.0426 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.2618 0.3101 0.2027 -0.0387 0.0009  -0.0391 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.2769 0.3202 0.2167 -0.0396 0.0025  -0.0424 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2721 0.3205 0.2098 -0.0355 -0.0005 -0.0338 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2723 0.3152 0.2095 -0.0380 0.0026  -0.0399 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2657 0.3100 0.2001 -0.0360 0.0012  -0.0342 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2302 0.2697 0.1783 -0.0373 0.0045  -0.0353 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2379 0.2710 0.1847 -0.0337 0.0050  -0.0306 15  ALA A CA  
99   C C   . ALA A 14  ? 0.2669 0.2851 0.2084 -0.0356 0.0079  -0.0306 15  ALA A C   
100  O O   . ALA A 14  ? 0.2367 0.2470 0.1742 -0.0331 0.0071  -0.0276 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2517 0.2940 0.2052 -0.0313 0.0048  -0.0301 15  ALA A CB  
102  N N   A SER A 15  ? 0.2575 0.2710 0.1973 -0.0406 0.0111  -0.0342 16  SER A N   
103  N N   B SER A 15  ? 0.2522 0.2656 0.1920 -0.0406 0.0111  -0.0342 16  SER A N   
104  N N   C SER A 15  ? 0.2433 0.2566 0.1830 -0.0406 0.0111  -0.0342 16  SER A N   
105  C CA  A SER A 15  ? 0.2692 0.2644 0.1989 -0.0429 0.0136  -0.0336 16  SER A CA  
106  C CA  B SER A 15  ? 0.2638 0.2589 0.1934 -0.0430 0.0136  -0.0337 16  SER A CA  
107  C CA  C SER A 15  ? 0.2498 0.2448 0.1794 -0.0428 0.0135  -0.0335 16  SER A CA  
108  C C   A SER A 15  ? 0.3144 0.2984 0.2373 -0.0396 0.0097  -0.0324 16  SER A C   
109  C C   B SER A 15  ? 0.3167 0.3005 0.2395 -0.0397 0.0097  -0.0325 16  SER A C   
110  C C   C SER A 15  ? 0.3112 0.2947 0.2339 -0.0397 0.0097  -0.0325 16  SER A C   
111  O O   A SER A 15  ? 0.2891 0.2614 0.2048 -0.0371 0.0079  -0.0298 16  SER A O   
112  O O   B SER A 15  ? 0.3006 0.2723 0.2159 -0.0373 0.0080  -0.0299 16  SER A O   
113  O O   C SER A 15  ? 0.2958 0.2670 0.2108 -0.0373 0.0080  -0.0299 16  SER A O   
114  C CB  A SER A 15  ? 0.3186 0.3090 0.2454 -0.0505 0.0191  -0.0382 16  SER A CB  
115  C CB  B SER A 15  ? 0.3114 0.3017 0.2381 -0.0505 0.0191  -0.0383 16  SER A CB  
116  C CB  C SER A 15  ? 0.2795 0.2693 0.2059 -0.0503 0.0193  -0.0378 16  SER A CB  
117  O OG  A SER A 15  ? 0.3671 0.3357 0.2793 -0.0534 0.0219  -0.0368 16  SER A OG  
118  O OG  B SER A 15  ? 0.3468 0.3503 0.2828 -0.0536 0.0230  -0.0414 16  SER A OG  
119  O OG  C SER A 15  ? 0.2587 0.2500 0.1857 -0.0536 0.0196  -0.0419 16  SER A OG  
120  N N   . ASP A 16  ? 0.2838 0.2727 0.2100 -0.0392 0.0080  -0.0353 17  ASP A N   
121  C CA  . ASP A 16  ? 0.2900 0.2714 0.2136 -0.0351 0.0043  -0.0363 17  ASP A CA  
122  C C   . ASP A 16  ? 0.2925 0.2803 0.2204 -0.0303 0.0011  -0.0344 17  ASP A C   
123  O O   . ASP A 16  ? 0.3003 0.2807 0.2258 -0.0263 -0.0025 -0.0347 17  ASP A O   
124  C CB  . ASP A 16  ? 0.3071 0.2948 0.2348 -0.0366 0.0047  -0.0412 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.4089 0.3864 0.3310 -0.0420 0.0083  -0.0446 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.3968 0.3598 0.3098 -0.0448 0.0109  -0.0430 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.4395 0.4224 0.3647 -0.0445 0.0095  -0.0494 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2391 0.2401 0.1725 -0.0309 0.0021  -0.0328 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2335 0.2385 0.1692 -0.0284 0.0009  -0.0313 18  VAL A CA  
130  C C   . VAL A 17  ? 0.2809 0.2766 0.2123 -0.0269 0.0001  -0.0287 18  VAL A C   
131  O O   . VAL A 17  ? 0.2568 0.2506 0.1886 -0.0245 -0.0025 -0.0301 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2516 0.2666 0.1892 -0.0294 0.0025  -0.0289 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2515 0.2658 0.1883 -0.0284 0.0031  -0.0267 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2454 0.2690 0.1844 -0.0311 0.0025  -0.0318 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2516 0.2429 0.1795 -0.0288 0.0026  -0.0262 19  LEU A N   
136  C CA  . LEU A 18  ? 0.2692 0.2514 0.1913 -0.0286 0.0029  -0.0241 19  LEU A CA  
137  C C   . LEU A 18  ? 0.2910 0.2593 0.2041 -0.0271 -0.0009 -0.0250 19  LEU A C   
138  O O   . LEU A 18  ? 0.2748 0.2391 0.1846 -0.0249 -0.0041 -0.0247 19  LEU A O   
139  C CB  . LEU A 18  ? 0.2713 0.2522 0.1923 -0.0316 0.0076  -0.0229 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3119 0.2855 0.2277 -0.0320 0.0094  -0.0212 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.3082 0.2878 0.2288 -0.0296 0.0090  -0.0199 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.3708 0.3438 0.2868 -0.0356 0.0152  -0.0221 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.2800 0.2408 0.1886 -0.0279 -0.0011 -0.0263 20  LEU A N   
144  C CA  . LEU A 19  ? 0.2998 0.2434 0.1971 -0.0250 -0.0057 -0.0265 20  LEU A CA  
145  C C   . LEU A 19  ? 0.3225 0.2723 0.2267 -0.0182 -0.0126 -0.0292 20  LEU A C   
146  O O   . LEU A 19  ? 0.3081 0.2499 0.2059 -0.0141 -0.0184 -0.0289 20  LEU A O   
147  C CB  . LEU A 19  ? 0.3299 0.2639 0.2220 -0.0273 -0.0038 -0.0281 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4376 0.3485 0.3146 -0.0234 -0.0086 -0.0276 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.4823 0.3730 0.3398 -0.0262 -0.0080 -0.0235 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.4989 0.4003 0.3719 -0.0265 -0.0052 -0.0301 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.2773 0.2430 0.1949 -0.0176 -0.0118 -0.0327 21  ASN A N   
152  C CA  . ASN A 20  ? 0.2655 0.2408 0.1928 -0.0128 -0.0164 -0.0376 21  ASN A CA  
153  C C   . ASN A 20  ? 0.2965 0.2792 0.2272 -0.0130 -0.0172 -0.0376 21  ASN A C   
154  O O   . ASN A 20  ? 0.2853 0.2704 0.2196 -0.0085 -0.0230 -0.0416 21  ASN A O   
155  C CB  . ASN A 20  ? 0.2924 0.2812 0.2305 -0.0142 -0.0133 -0.0419 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.4128 0.3941 0.3496 -0.0118 -0.0147 -0.0450 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.3621 0.3279 0.2914 -0.0068 -0.0196 -0.0449 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3218 0.3116 0.2638 -0.0152 -0.0104 -0.0478 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2614 0.2475 0.1912 -0.0179 -0.0117 -0.0339 22  LEU A N   
160  C CA  . LEU A 21  ? 0.2594 0.2491 0.1902 -0.0193 -0.0110 -0.0339 22  LEU A CA  
161  C C   . LEU A 21  ? 0.2945 0.2725 0.2156 -0.0170 -0.0161 -0.0330 22  LEU A C   
162  O O   . LEU A 21  ? 0.2894 0.2718 0.2132 -0.0157 -0.0197 -0.0364 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2628 0.2536 0.1923 -0.0237 -0.0043 -0.0295 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.2867 0.2874 0.2221 -0.0257 -0.0005 -0.0298 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.2922 0.2913 0.2246 -0.0274 0.0039  -0.0247 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.3080 0.3175 0.2498 -0.0272 0.0003  -0.0349 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.2811 0.2441 0.1898 -0.0175 -0.0159 -0.0289 23  ASN A N   
168  C CA  . ASN A 22  ? 0.2998 0.2477 0.1938 -0.0161 -0.0206 -0.0274 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3427 0.2874 0.2356 -0.0083 -0.0311 -0.0308 23  ASN A C   
170  O O   . ASN A 22  ? 0.3564 0.2976 0.2432 -0.0056 -0.0376 -0.0318 23  ASN A O   
171  C CB  . ASN A 22  ? 0.3102 0.2409 0.1891 -0.0200 -0.0165 -0.0231 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4254 0.3399 0.2861 -0.0210 -0.0188 -0.0209 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.3764 0.2957 0.2378 -0.0212 -0.0205 -0.0221 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4408 0.3346 0.2830 -0.0227 -0.0185 -0.0182 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.3151 0.2618 0.2145 -0.0042 -0.0332 -0.0333 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3317 0.2772 0.2339 0.0050  -0.0434 -0.0379 24  ARG A CA  
177  C C   . ARG A 23  ? 0.3625 0.3295 0.2816 0.0073  -0.0471 -0.0451 24  ARG A C   
178  O O   . ARG A 23  ? 0.3544 0.3211 0.2728 0.0143  -0.0573 -0.0486 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3186 0.2646 0.2277 0.0078  -0.0425 -0.0405 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.3645 0.2859 0.2550 0.0067  -0.0409 -0.0352 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.4048 0.3283 0.3029 0.0067  -0.0372 -0.0384 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.5134 0.4114 0.3929 0.0048  -0.0353 -0.0345 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.6751 0.5707 0.5557 0.0005  -0.0290 -0.0359 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.5167 0.4342 0.4152 -0.0022 -0.0246 -0.0404 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.6009 0.4713 0.4630 -0.0023 -0.0266 -0.0331 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.3077 0.2924 0.2406 0.0010  -0.0389 -0.0476 25  LEU A N   
187  C CA  . LEU A 24  ? 0.2951 0.2991 0.2428 0.0001  -0.0397 -0.0553 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3369 0.3375 0.2767 -0.0015 -0.0427 -0.0542 25  LEU A C   
189  O O   . LEU A 24  ? 0.3279 0.3388 0.2752 0.0021  -0.0500 -0.0615 25  LEU A O   
190  C CB  . LEU A 24  ? 0.2812 0.2981 0.2386 -0.0079 -0.0290 -0.0565 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.3193 0.3429 0.2851 -0.0080 -0.0253 -0.0593 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.3187 0.3517 0.2886 -0.0165 -0.0152 -0.0596 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.3052 0.3398 0.2853 -0.0007 -0.0320 -0.0696 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.2961 0.2832 0.2214 -0.0069 -0.0372 -0.0464 26  ARG A N   
195  C CA  . ARG A 25  ? 0.3119 0.2936 0.2273 -0.0092 -0.0391 -0.0456 26  ARG A CA  
196  C C   . ARG A 25  ? 0.3771 0.3490 0.2813 -0.0014 -0.0521 -0.0466 26  ARG A C   
197  O O   . ARG A 25  ? 0.3755 0.3550 0.2817 -0.0003 -0.0585 -0.0520 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3265 0.2943 0.2284 -0.0154 -0.0308 -0.0380 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.3737 0.3371 0.2664 -0.0189 -0.0313 -0.0386 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.4483 0.4007 0.3309 -0.0250 -0.0220 -0.0333 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.4000 0.3361 0.2687 -0.0247 -0.0212 -0.0279 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.5306 0.4505 0.3810 -0.0281 -0.0196 -0.0252 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.4749 0.3925 0.3179 -0.0310 -0.0203 -0.0272 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4333 0.3386 0.2714 -0.0297 -0.0167 -0.0214 26  ARG A NH2 
205  N N   A SER A 26  ? 0.3653 0.3192 0.2563 0.0035  -0.0562 -0.0417 27  SER A N   
206  N N   B SER A 26  ? 0.3626 0.3167 0.2538 0.0036  -0.0561 -0.0417 27  SER A N   
207  N N   C SER A 26  ? 0.3682 0.3222 0.2593 0.0035  -0.0562 -0.0417 27  SER A N   
208  C CA  A SER A 26  ? 0.3928 0.3307 0.2675 0.0119  -0.0691 -0.0408 27  SER A CA  
209  C CA  B SER A 26  ? 0.3900 0.3276 0.2649 0.0121  -0.0690 -0.0407 27  SER A CA  
210  C CA  C SER A 26  ? 0.3979 0.3357 0.2726 0.0119  -0.0691 -0.0407 27  SER A CA  
211  C C   A SER A 26  ? 0.4538 0.4083 0.3443 0.0220  -0.0817 -0.0500 27  SER A C   
212  C C   B SER A 26  ? 0.4513 0.4057 0.3418 0.0219  -0.0815 -0.0499 27  SER A C   
213  C C   C SER A 26  ? 0.4554 0.4099 0.3459 0.0220  -0.0816 -0.0500 27  SER A C   
214  O O   A SER A 26  ? 0.4699 0.4195 0.3506 0.0281  -0.0938 -0.0516 27  SER A O   
215  O O   B SER A 26  ? 0.4667 0.4159 0.3471 0.0278  -0.0934 -0.0514 27  SER A O   
216  O O   C SER A 26  ? 0.4711 0.4205 0.3517 0.0281  -0.0937 -0.0515 27  SER A O   
217  C CB  A SER A 26  ? 0.4471 0.3608 0.3049 0.0144  -0.0690 -0.0342 27  SER A CB  
218  C CB  B SER A 26  ? 0.4449 0.3614 0.3069 0.0154  -0.0690 -0.0352 27  SER A CB  
219  C CB  C SER A 26  ? 0.4615 0.3759 0.3203 0.0146  -0.0689 -0.0344 27  SER A CB  
220  O OG  A SER A 26  ? 0.5011 0.4216 0.3733 0.0204  -0.0706 -0.0378 27  SER A OG  
221  O OG  B SER A 26  ? 0.5252 0.4238 0.3695 0.0068  -0.0594 -0.0278 27  SER A OG  
222  O OG  C SER A 26  ? 0.5934 0.4874 0.4328 0.0236  -0.0818 -0.0326 27  SER A OG  
223  N N   . ARG A 27  ? 0.3927 0.3678 0.3076 0.0235  -0.0789 -0.0570 28  ARG A N   
224  C CA  . ARG A 27  ? 0.3966 0.3923 0.3320 0.0324  -0.0889 -0.0685 28  ARG A CA  
225  C C   . ARG A 27  ? 0.4071 0.4302 0.3623 0.0256  -0.0850 -0.0780 28  ARG A C   
226  O O   . ARG A 27  ? 0.4050 0.4506 0.3816 0.0307  -0.0911 -0.0901 28  ARG A O   
227  C CB  . ARG A 27  ? 0.4070 0.4076 0.3564 0.0376  -0.0874 -0.0720 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.4938 0.4652 0.4228 0.0433  -0.0904 -0.0635 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.5410 0.5166 0.4829 0.0452  -0.0855 -0.0668 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.6824 0.6777 0.6475 0.0556  -0.0938 -0.0793 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.8513 0.8640 0.8375 0.0548  -0.0876 -0.0874 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.7079 0.7402 0.7170 0.0642  -0.0948 -0.1005 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.6297 0.6417 0.6149 0.0444  -0.0741 -0.0836 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.3325 0.3533 0.2806 0.0140  -0.0745 -0.0736 29  ASP A N   
235  C CA  . ASP A 28  ? 0.3255 0.3657 0.2868 0.0051  -0.0681 -0.0810 29  ASP A CA  
236  C C   . ASP A 28  ? 0.3642 0.4262 0.3492 0.0013  -0.0601 -0.0897 29  ASP A C   
237  O O   . ASP A 28  ? 0.3704 0.4542 0.3728 -0.0020 -0.0596 -0.1015 29  ASP A O   
238  C CB  . ASP A 28  ? 0.3617 0.4115 0.3246 0.0086  -0.0799 -0.0889 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.4682 0.5308 0.4373 -0.0031 -0.0718 -0.0948 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.4626 0.5143 0.4225 -0.0127 -0.0590 -0.0876 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.5108 0.5942 0.4944 -0.0026 -0.0782 -0.1071 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.2998 0.3559 0.2847 0.0009  -0.0534 -0.0848 30  ILE A N   
243  C CA  . ILE A 29  ? 0.2866 0.3603 0.2899 -0.0032 -0.0454 -0.0925 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3233 0.3954 0.3226 -0.0158 -0.0308 -0.0885 30  ILE A C   
245  O O   . ILE A 29  ? 0.2940 0.3493 0.2782 -0.0182 -0.0259 -0.0773 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3192 0.3889 0.3253 0.0038  -0.0471 -0.0915 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3393 0.4104 0.3512 0.0180  -0.0622 -0.0972 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.2921 0.3773 0.3129 -0.0030 -0.0362 -0.0983 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.3933 0.4509 0.4007 0.0254  -0.0644 -0.0935 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.2989 0.3882 0.3114 -0.0238 -0.0241 -0.0985 31  LEU A N   
251  C CA  . LEU A 30  ? 0.2980 0.3839 0.3052 -0.0359 -0.0101 -0.0958 31  LEU A CA  
252  C C   . LEU A 30  ? 0.3164 0.3849 0.3064 -0.0400 -0.0068 -0.0860 31  LEU A C   
253  O O   . LEU A 30  ? 0.2934 0.3530 0.2752 -0.0473 0.0035  -0.0808 31  LEU A O   
254  C CB  . LEU A 30  ? 0.3070 0.3887 0.3114 -0.0380 -0.0027 -0.0913 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.3875 0.4882 0.4094 -0.0392 0.0000  -0.1037 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.3991 0.4937 0.4136 -0.0445 0.0093  -0.0991 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.4547 0.5738 0.4908 -0.0477 0.0055  -0.1175 31  LEU A CD2 
258  N N   . THR A 31  ? 0.2841 0.3480 0.2687 -0.0356 -0.0153 -0.0849 32  THR A N   
259  C CA  . THR A 31  ? 0.2887 0.3390 0.2595 -0.0404 -0.0116 -0.0789 32  THR A CA  
260  C C   . THR A 31  ? 0.3553 0.4150 0.3328 -0.0512 -0.0030 -0.0877 32  THR A C   
261  O O   . THR A 31  ? 0.3426 0.4220 0.3360 -0.0531 -0.0048 -0.1002 32  THR A O   
262  C CB  . THR A 31  ? 0.3524 0.3963 0.3146 -0.0342 -0.0225 -0.0775 32  THR A CB  
263  O OG1 . THR A 31  ? 0.3732 0.4351 0.3484 -0.0308 -0.0320 -0.0892 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3398 0.3686 0.2905 -0.0260 -0.0282 -0.0679 32  THR A CG2 
265  N N   . ASP A 32  ? 0.3318 0.3775 0.2982 -0.0584 0.0072  -0.0819 33  ASP A N   
266  C CA  . ASP A 32  ? 0.3361 0.3851 0.3051 -0.0700 0.0178  -0.0890 33  ASP A CA  
267  C C   . ASP A 32  ? 0.3535 0.3897 0.3117 -0.0756 0.0223  -0.0874 33  ASP A C   
268  O O   . ASP A 32  ? 0.3580 0.3904 0.3140 -0.0860 0.0329  -0.0915 33  ASP A O   
269  C CB  . ASP A 32  ? 0.3549 0.3968 0.3197 -0.0750 0.0285  -0.0848 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.4494 0.4711 0.3992 -0.0702 0.0303  -0.0703 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.3773 0.3900 0.3206 -0.0644 0.0253  -0.0638 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.5650 0.5807 0.5096 -0.0725 0.0365  -0.0662 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.2880 0.3157 0.2377 -0.0696 0.0153  -0.0819 34  VAL A N   
274  C CA  . VAL A 33  ? 0.2896 0.3054 0.2290 -0.0747 0.0195  -0.0814 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3453 0.3602 0.2788 -0.0689 0.0087  -0.0808 34  VAL A C   
276  O O   . VAL A 33  ? 0.3371 0.3511 0.2686 -0.0600 0.0000  -0.0756 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3341 0.3277 0.2609 -0.0757 0.0296  -0.0706 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.3144 0.2988 0.2346 -0.0663 0.0249  -0.0600 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3461 0.3271 0.2644 -0.0833 0.0378  -0.0727 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3100 0.3231 0.2385 -0.0749 0.0098  -0.0862 35  VAL A N   
281  N N   B VAL A 34  ? 0.3011 0.3143 0.2296 -0.0747 0.0096  -0.0862 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3140 0.3219 0.2314 -0.0717 0.0014  -0.0855 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.3007 0.3085 0.2180 -0.0711 0.0009  -0.0851 35  VAL A CA  
284  C C   A VAL A 34  ? 0.3625 0.3502 0.2662 -0.0764 0.0118  -0.0799 35  VAL A C   
285  C C   B VAL A 34  ? 0.3621 0.3506 0.2655 -0.0765 0.0107  -0.0807 35  VAL A C   
286  O O   A VAL A 34  ? 0.3580 0.3413 0.2626 -0.0846 0.0225  -0.0833 35  VAL A O   
287  O O   B VAL A 34  ? 0.3661 0.3518 0.2703 -0.0853 0.0205  -0.0855 35  VAL A O   
288  C CB  A VAL A 34  ? 0.3720 0.3967 0.2949 -0.0747 -0.0071 -0.0984 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.3485 0.3737 0.2711 -0.0705 -0.0113 -0.0963 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.3861 0.4021 0.2924 -0.0718 -0.0162 -0.0967 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.3483 0.3833 0.2773 -0.0821 -0.0051 -0.1085 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.3648 0.4122 0.3054 -0.0691 -0.0170 -0.1059 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.3579 0.3729 0.2633 -0.0648 -0.0220 -0.0923 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.3152 0.2895 0.2063 -0.0715 0.0095  -0.0721 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3358 0.2926 0.2152 -0.0750 0.0186  -0.0684 36  ILE A CA  
296  C C   . ILE A 35  ? 0.3963 0.3509 0.2632 -0.0778 0.0128  -0.0732 36  ILE A C   
297  O O   . ILE A 35  ? 0.3845 0.3387 0.2430 -0.0726 0.0023  -0.0709 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3671 0.3125 0.2423 -0.0690 0.0217  -0.0582 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3537 0.3029 0.2399 -0.0650 0.0244  -0.0533 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.3870 0.3170 0.2535 -0.0722 0.0315  -0.0567 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3435 0.2911 0.2354 -0.0702 0.0339  -0.0554 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.3625 0.3135 0.2259 -0.0864 0.0196  -0.0797 37  VAL A N   
303  C CA  . VAL A 36  ? 0.3771 0.3261 0.2272 -0.0908 0.0150  -0.0856 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4499 0.3792 0.2853 -0.0932 0.0240  -0.0814 37  VAL A C   
305  O O   . VAL A 36  ? 0.4373 0.3572 0.2757 -0.0965 0.0368  -0.0808 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4287 0.3891 0.2848 -0.1000 0.0162  -0.0981 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4439 0.4025 0.2845 -0.1048 0.0103  -0.1046 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4278 0.4111 0.3016 -0.0981 0.0079  -0.1044 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.4221 0.3440 0.2407 -0.0913 0.0176  -0.0788 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4340 0.3384 0.2378 -0.0945 0.0264  -0.0762 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5278 0.4283 0.3116 -0.1001 0.0199  -0.0819 38  VAL A C   
312  O O   . VAL A 37  ? 0.4888 0.3862 0.2577 -0.0965 0.0086  -0.0789 38  VAL A O   
313  C CB  . VAL A 37  ? 0.4778 0.3745 0.2783 -0.0882 0.0268  -0.0669 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.4859 0.3679 0.2773 -0.0924 0.0393  -0.0664 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4548 0.3600 0.2752 -0.0814 0.0281  -0.0617 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5329 0.4334 0.3153 -0.1088 0.0260  -0.0907 39  SER A N   
317  N N   B SER A 38  ? 0.5236 0.4222 0.3050 -0.1089 0.0273  -0.0902 39  SER A N   
318  C CA  A SER A 38  ? 0.5590 0.4581 0.3230 -0.1155 0.0200  -0.0983 39  SER A CA  
319  C CA  B SER A 38  ? 0.5469 0.4430 0.3098 -0.1162 0.0227  -0.0979 39  SER A CA  
320  C C   A SER A 38  ? 0.5754 0.4913 0.3408 -0.1109 0.0009  -0.1015 39  SER A C   
321  C C   B SER A 38  ? 0.5752 0.4828 0.3318 -0.1114 0.0029  -0.0991 39  SER A C   
322  O O   A SER A 38  ? 0.5532 0.4870 0.3393 -0.1100 -0.0016 -0.1064 39  SER A O   
323  O O   B SER A 38  ? 0.5812 0.4787 0.3158 -0.1088 -0.0060 -0.0951 39  SER A O   
324  C CB  A SER A 38  ? 0.6424 0.5222 0.3808 -0.1182 0.0230  -0.0949 39  SER A CB  
325  C CB  B SER A 38  ? 0.6171 0.4935 0.3586 -0.1212 0.0313  -0.0964 39  SER A CB  
326  O OG  A SER A 38  ? 0.8278 0.6956 0.5692 -0.1214 0.0403  -0.0936 39  SER A OG  
327  O OG  B SER A 38  ? 0.7266 0.5956 0.4761 -0.1264 0.0485  -0.0998 39  SER A OG  
328  N N   A ARG A 39  ? 0.5341 0.4437 0.2775 -0.1075 -0.0122 -0.0990 40  ARG A N   
329  N N   B ARG A 39  ? 0.4936 0.4217 0.2706 -0.1092 -0.0035 -0.1044 40  ARG A N   
330  C CA  A ARG A 39  ? 0.5286 0.4523 0.2712 -0.1005 -0.0326 -0.1020 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.4878 0.4340 0.2692 -0.1032 -0.0221 -0.1087 40  ARG A CA  
332  C C   A ARG A 39  ? 0.5426 0.4720 0.2972 -0.0882 -0.0411 -0.0944 40  ARG A C   
333  C C   B ARG A 39  ? 0.5164 0.4624 0.2995 -0.0905 -0.0325 -0.0992 40  ARG A C   
334  O O   A ARG A 39  ? 0.5277 0.4708 0.2869 -0.0804 -0.0579 -0.0976 40  ARG A O   
335  O O   B ARG A 39  ? 0.5097 0.4742 0.3068 -0.0839 -0.0450 -0.1032 40  ARG A O   
336  C CB  A ARG A 39  ? 0.5497 0.4600 0.2588 -0.1016 -0.0442 -0.1022 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.4966 0.4437 0.2578 -0.1068 -0.0340 -0.1162 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.6301 0.5435 0.3299 -0.1129 -0.0423 -0.1137 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.6444 0.5994 0.4102 -0.1197 -0.0261 -0.1293 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.6660 0.5691 0.3322 -0.1122 -0.0582 -0.1142 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.7410 0.7068 0.4944 -0.1220 -0.0419 -0.1395 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.6949 0.5973 0.3476 -0.1247 -0.0543 -0.1248 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.8274 0.7998 0.5842 -0.1359 -0.0329 -0.1529 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.8719 0.7956 0.5325 -0.1278 -0.0644 -0.1376 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 0.9774 0.9325 0.7136 -0.1460 -0.0231 -0.1552 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7366 0.6575 0.3828 -0.1403 -0.0595 -0.1473 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.7942 0.7251 0.5052 -0.1443 -0.0204 -0.1453 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.6823 0.6318 0.3666 -0.1190 -0.0787 -0.1423 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.8062 0.7677 0.5468 -0.1589 -0.0148 -0.1683 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.4775 0.3972 0.2379 -0.0859 -0.0301 -0.0853 41  GLU A N   
351  N N   B GLU A 40  ? 0.4726 0.3992 0.2439 -0.0875 -0.0265 -0.0880 41  GLU A N   
352  C CA  A GLU A 40  ? 0.4649 0.3879 0.2352 -0.0753 -0.0365 -0.0782 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.4662 0.3901 0.2386 -0.0769 -0.0339 -0.0791 41  GLU A CA  
354  C C   A GLU A 40  ? 0.4842 0.4245 0.2849 -0.0739 -0.0300 -0.0799 41  GLU A C   
355  C C   B GLU A 40  ? 0.4869 0.4259 0.2883 -0.0737 -0.0284 -0.0787 41  GLU A C   
356  O O   A GLU A 40  ? 0.4597 0.4006 0.2702 -0.0808 -0.0161 -0.0822 41  GLU A O   
357  O O   B GLU A 40  ? 0.4623 0.4001 0.2738 -0.0791 -0.0139 -0.0788 41  GLU A O   
358  C CB  A GLU A 40  ? 0.4911 0.3918 0.2448 -0.0737 -0.0305 -0.0674 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.4948 0.3947 0.2472 -0.0775 -0.0266 -0.0694 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.6950 0.5747 0.4141 -0.0757 -0.0366 -0.0647 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.6766 0.5579 0.3952 -0.0793 -0.0344 -0.0679 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.1687 1.0391 0.8727 -0.0657 -0.0524 -0.0585 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.1248 0.9967 0.8287 -0.0694 -0.0493 -0.0611 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.1870 1.0477 0.8906 -0.0621 -0.0487 -0.0507 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.1586 1.0350 0.8540 -0.0639 -0.0666 -0.0643 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.1869 1.0594 0.8790 -0.0613 -0.0689 -0.0619 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.1392 0.9990 0.8400 -0.0669 -0.0442 -0.0530 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4287 0.3806 0.2421 -0.0647 -0.0399 -0.0788 42  GLN A N   
369  C CA  . GLN A 41  ? 0.4052 0.3729 0.2446 -0.0628 -0.0353 -0.0802 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4312 0.3926 0.2723 -0.0546 -0.0364 -0.0708 42  GLN A C   
371  O O   . GLN A 41  ? 0.4342 0.3881 0.2630 -0.0472 -0.0478 -0.0670 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4249 0.4172 0.2813 -0.0604 -0.0464 -0.0914 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.6235 0.6265 0.4838 -0.0707 -0.0431 -0.1031 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.8449 0.8766 0.7275 -0.0703 -0.0511 -0.1165 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.7454 0.7909 0.6432 -0.0618 -0.0590 -0.1178 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.8636 0.9060 0.7496 -0.0802 -0.0486 -0.1281 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.3554 0.3184 0.2101 -0.0558 -0.0250 -0.0673 43  PHE A N   
378  C CA  . PHE A 42  ? 0.3581 0.3171 0.2160 -0.0492 -0.0249 -0.0594 43  PHE A CA  
379  C C   . PHE A 42  ? 0.3940 0.3691 0.2740 -0.0484 -0.0217 -0.0623 43  PHE A C   
380  O O   . PHE A 42  ? 0.4009 0.3780 0.2883 -0.0546 -0.0107 -0.0636 43  PHE A O   
381  C CB  . PHE A 42  ? 0.3759 0.3184 0.2247 -0.0521 -0.0135 -0.0516 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.4125 0.3376 0.2383 -0.0553 -0.0133 -0.0497 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4442 0.3650 0.2631 -0.0629 -0.0068 -0.0539 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.4665 0.3778 0.2755 -0.0517 -0.0188 -0.0441 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.4845 0.3890 0.2805 -0.0671 -0.0057 -0.0529 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.5192 0.4123 0.3035 -0.0564 -0.0175 -0.0427 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.4926 0.3833 0.2707 -0.0641 -0.0111 -0.0473 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3512 0.3360 0.2401 -0.0410 -0.0306 -0.0633 44  ARG A N   
389  C CA  . ARG A 43  ? 0.3180 0.3181 0.2268 -0.0408 -0.0271 -0.0668 44  ARG A CA  
390  C C   . ARG A 43  ? 0.3441 0.3354 0.2522 -0.0390 -0.0200 -0.0578 44  ARG A C   
391  O O   . ARG A 43  ? 0.3404 0.3192 0.2375 -0.0347 -0.0229 -0.0510 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3358 0.3524 0.2570 -0.0334 -0.0394 -0.0741 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.4054 0.4365 0.3314 -0.0346 -0.0478 -0.0855 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.4777 0.5341 0.4270 -0.0305 -0.0546 -0.0971 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.6158 0.6808 0.5801 -0.0359 -0.0423 -0.0988 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.7768 0.8536 0.7523 -0.0466 -0.0320 -0.1069 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.6583 0.7436 0.6356 -0.0532 -0.0326 -0.1159 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.5676 0.6472 0.5511 -0.0515 -0.0209 -0.1067 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.2998 0.2966 0.2181 -0.0430 -0.0108 -0.0580 45  ALA A N   
400  C CA  . ALA A 44  ? 0.2956 0.2857 0.2134 -0.0412 -0.0052 -0.0500 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3122 0.3116 0.2412 -0.0440 0.0009  -0.0522 45  ALA A C   
402  O O   . ALA A 44  ? 0.2911 0.3017 0.2287 -0.0483 0.0022  -0.0602 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3189 0.2942 0.2262 -0.0438 0.0025  -0.0437 45  ALA A CB  
404  N N   . HIS A 45  ? 0.2813 0.2763 0.2095 -0.0421 0.0047  -0.0457 46  HIS A N   
405  C CA  . HIS A 45  ? 0.2686 0.2680 0.2021 -0.0451 0.0110  -0.0459 46  HIS A CA  
406  C C   . HIS A 45  ? 0.3114 0.2978 0.2366 -0.0483 0.0194  -0.0402 46  HIS A C   
407  O O   . HIS A 45  ? 0.2989 0.2764 0.2186 -0.0447 0.0197  -0.0338 46  HIS A O   
408  C CB  . HIS A 45  ? 0.2595 0.2618 0.1956 -0.0404 0.0084  -0.0425 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.2908 0.3024 0.2342 -0.0357 0.0000  -0.0477 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.3136 0.3182 0.2512 -0.0300 -0.0070 -0.0447 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.2985 0.3243 0.2536 -0.0358 -0.0021 -0.0563 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.3103 0.3232 0.2554 -0.0254 -0.0141 -0.0504 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.2991 0.3268 0.2568 -0.0283 -0.0117 -0.0583 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.3065 0.2913 0.2310 -0.0549 0.0265  -0.0432 47  LYS A N   
415  C CA  . LYS A 46  ? 0.2972 0.2661 0.2122 -0.0570 0.0344  -0.0379 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3286 0.2916 0.2398 -0.0508 0.0339  -0.0292 47  LYS A C   
417  O O   . LYS A 46  ? 0.2973 0.2499 0.2038 -0.0472 0.0354  -0.0241 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3202 0.2858 0.2323 -0.0659 0.0428  -0.0421 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.3241 0.2933 0.2391 -0.0732 0.0452  -0.0511 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.3079 0.2751 0.2207 -0.0840 0.0549  -0.0569 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.3909 0.3654 0.3090 -0.0924 0.0572  -0.0680 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.3845 0.3601 0.3025 -0.1046 0.0676  -0.0759 47  LYS A NZ  
423  N N   . THR A 47  ? 0.2910 0.2619 0.2052 -0.0494 0.0315  -0.0286 48  THR A N   
424  C CA  . THR A 47  ? 0.2860 0.2533 0.1964 -0.0442 0.0303  -0.0214 48  THR A CA  
425  C C   . THR A 47  ? 0.2979 0.2663 0.2115 -0.0377 0.0257  -0.0183 48  THR A C   
426  O O   . THR A 47  ? 0.3044 0.2673 0.2154 -0.0333 0.0260  -0.0132 48  THR A O   
427  C CB  . THR A 47  ? 0.3638 0.3398 0.2760 -0.0453 0.0291  -0.0228 48  THR A CB  
428  O OG1 . THR A 47  ? 0.3707 0.3600 0.2933 -0.0445 0.0240  -0.0286 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.3918 0.3631 0.2971 -0.0530 0.0362  -0.0251 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2553 0.2303 0.1739 -0.0372 0.0213  -0.0217 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2565 0.2303 0.1755 -0.0334 0.0187  -0.0195 49  VAL A CA  
432  C C   . VAL A 48  ? 0.2931 0.2576 0.2084 -0.0335 0.0227  -0.0183 49  VAL A C   
433  O O   . VAL A 48  ? 0.2663 0.2290 0.1828 -0.0302 0.0239  -0.0158 49  VAL A O   
434  C CB  . VAL A 48  ? 0.2710 0.2490 0.1913 -0.0330 0.0131  -0.0228 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.2807 0.2532 0.1973 -0.0315 0.0126  -0.0208 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.2657 0.2524 0.1911 -0.0317 0.0097  -0.0244 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.2763 0.2362 0.1885 -0.0375 0.0252  -0.0215 50  LEU A N   
438  C CA  . LEU A 49  ? 0.2739 0.2238 0.1821 -0.0383 0.0302  -0.0214 50  LEU A CA  
439  C C   . LEU A 49  ? 0.3089 0.2515 0.2168 -0.0345 0.0345  -0.0171 50  LEU A C   
440  O O   . LEU A 49  ? 0.3063 0.2451 0.2157 -0.0310 0.0366  -0.0161 50  LEU A O   
441  C CB  . LEU A 49  ? 0.2704 0.2168 0.1750 -0.0444 0.0326  -0.0264 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.3053 0.2589 0.2097 -0.0469 0.0266  -0.0317 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.3059 0.2584 0.2082 -0.0534 0.0291  -0.0379 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3344 0.2844 0.2334 -0.0450 0.0235  -0.0305 50  LEU A CD2 
445  N N   . MET A 50  ? 0.2766 0.2167 0.1818 -0.0349 0.0356  -0.0149 51  MET A N   
446  C CA  . MET A 50  ? 0.2959 0.2258 0.1970 -0.0300 0.0378  -0.0098 51  MET A CA  
447  C C   . MET A 50  ? 0.3454 0.2829 0.2526 -0.0223 0.0331  -0.0066 51  MET A C   
448  O O   . MET A 50  ? 0.3481 0.2803 0.2568 -0.0159 0.0338  -0.0045 51  MET A O   
449  C CB  . MET A 50  ? 0.3215 0.2451 0.2142 -0.0333 0.0398  -0.0078 51  MET A CB  
450  C CG  . MET A 50  ? 0.3476 0.2642 0.2351 -0.0424 0.0461  -0.0124 51  MET A CG  
451  S SD  . MET A 50  ? 0.4049 0.3200 0.2845 -0.0491 0.0491  -0.0126 51  MET A SD  
452  C CE  . MET A 50  ? 0.3784 0.2678 0.2407 -0.0449 0.0530  -0.0041 51  MET A CE  
453  N N   . ALA A 51  ? 0.3002 0.2508 0.2122 -0.0227 0.0283  -0.0074 52  ALA A N   
454  C CA  . ALA A 51  ? 0.2892 0.2493 0.2076 -0.0172 0.0241  -0.0059 52  ALA A CA  
455  C C   . ALA A 51  ? 0.3069 0.2703 0.2330 -0.0152 0.0255  -0.0087 52  ALA A C   
456  O O   . ALA A 51  ? 0.3272 0.2982 0.2606 -0.0101 0.0235  -0.0088 52  ALA A O   
457  C CB  . ALA A 51  ? 0.2915 0.2626 0.2122 -0.0198 0.0201  -0.0073 52  ALA A CB  
458  N N   . CYS A 52  ? 0.2648 0.2233 0.1888 -0.0198 0.0292  -0.0119 53  CYS A N   
459  C CA  . CYS A 52  ? 0.2649 0.2249 0.1930 -0.0205 0.0322  -0.0154 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3218 0.2731 0.2501 -0.0192 0.0381  -0.0172 53  CYS A C   
461  O O   . CYS A 52  ? 0.2980 0.2520 0.2316 -0.0194 0.0418  -0.0211 53  CYS A O   
462  C CB  . CYS A 52  ? 0.2660 0.2252 0.1882 -0.0269 0.0316  -0.0179 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.3051 0.2727 0.2279 -0.0276 0.0253  -0.0170 53  CYS A SG  
464  N N   . SER A 53  ? 0.2913 0.2314 0.2132 -0.0196 0.0403  -0.0157 54  SER A N   
465  C CA  . SER A 53  ? 0.2820 0.2108 0.2019 -0.0200 0.0468  -0.0183 54  SER A CA  
466  C C   . SER A 53  ? 0.3429 0.2595 0.2597 -0.0149 0.0485  -0.0149 54  SER A C   
467  O O   . SER A 53  ? 0.3165 0.2269 0.2251 -0.0175 0.0476  -0.0119 54  SER A O   
468  C CB  . SER A 53  ? 0.3111 0.2351 0.2223 -0.0289 0.0489  -0.0215 54  SER A CB  
469  O OG  . SER A 53  ? 0.3481 0.2592 0.2538 -0.0316 0.0550  -0.0239 54  SER A OG  
470  N N   . GLY A 54  ? 0.3206 0.2320 0.2429 -0.0080 0.0517  -0.0162 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3239 0.2182 0.2405 -0.0018 0.0534  -0.0127 55  GLY A CA  
472  C C   . GLY A 54  ? 0.3732 0.2505 0.2774 -0.0100 0.0600  -0.0138 55  GLY A C   
473  O O   . GLY A 54  ? 0.3803 0.2422 0.2735 -0.0100 0.0611  -0.0096 55  GLY A O   
474  N N   . LEU A 55  ? 0.3417 0.2215 0.2458 -0.0184 0.0644  -0.0199 56  LEU A N   
475  C CA  . LEU A 55  ? 0.3670 0.2342 0.2606 -0.0276 0.0703  -0.0230 56  LEU A CA  
476  C C   . LEU A 55  ? 0.3961 0.2662 0.2831 -0.0346 0.0674  -0.0212 56  LEU A C   
477  O O   . LEU A 55  ? 0.3832 0.2391 0.2611 -0.0383 0.0718  -0.0204 56  LEU A O   
478  C CB  . LEU A 55  ? 0.3683 0.2391 0.2620 -0.0349 0.0741  -0.0302 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4385 0.2976 0.3223 -0.0447 0.0802  -0.0352 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4641 0.3019 0.3441 -0.0419 0.0887  -0.0360 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.4101 0.2759 0.2912 -0.0525 0.0807  -0.0416 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3328 0.2204 0.2244 -0.0363 0.0607  -0.0211 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3218 0.2152 0.2105 -0.0422 0.0580  -0.0212 57  PHE A CA  
484  C C   . PHE A 56  ? 0.3759 0.2625 0.2599 -0.0389 0.0577  -0.0154 57  PHE A C   
485  O O   . PHE A 56  ? 0.3643 0.2463 0.2417 -0.0457 0.0608  -0.0165 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3241 0.2356 0.2186 -0.0435 0.0508  -0.0230 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3349 0.2492 0.2280 -0.0488 0.0506  -0.0289 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.3607 0.2715 0.2493 -0.0566 0.0538  -0.0346 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3371 0.2569 0.2314 -0.0468 0.0472  -0.0291 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.3695 0.2827 0.2547 -0.0612 0.0524  -0.0402 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.3735 0.2931 0.2619 -0.0518 0.0462  -0.0338 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3474 0.2640 0.2311 -0.0584 0.0481  -0.0391 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3415 0.2269 0.2279 -0.0289 0.0545  -0.0099 58  TYR A N   
494  C CA  . TYR A 57  ? 0.3563 0.2322 0.2343 -0.0247 0.0531  -0.0034 58  TYR A CA  
495  C C   . TYR A 57  ? 0.4257 0.2763 0.2893 -0.0276 0.0608  -0.0020 58  TYR A C   
496  O O   . TYR A 57  ? 0.4049 0.2462 0.2565 -0.0333 0.0634  -0.0001 58  TYR A O   
497  C CB  . TYR A 57  ? 0.3750 0.2554 0.2595 -0.0122 0.0469  0.0009  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4285 0.2961 0.3015 -0.0058 0.0439  0.0083  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.4484 0.3195 0.3138 -0.0095 0.0411  0.0112  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.4875 0.3377 0.3555 0.0044  0.0439  0.0121  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.4870 0.3437 0.3374 -0.0042 0.0381  0.0184  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5344 0.3697 0.3881 0.0114  0.0396  0.0197  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6135 0.4518 0.4572 0.0067  0.0367  0.0232  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.6953 0.5166 0.5210 0.0133  0.0322  0.0311  58  TYR A OH  
505  N N   A SER A 58  ? 0.3962 0.2346 0.2601 -0.0247 0.0654  -0.0038 59  SER A N   
506  N N   B SER A 58  ? 0.3953 0.2336 0.2592 -0.0247 0.0654  -0.0038 59  SER A N   
507  C CA  A SER A 58  ? 0.4256 0.2367 0.2753 -0.0275 0.0738  -0.0033 59  SER A CA  
508  C CA  B SER A 58  ? 0.4239 0.2349 0.2736 -0.0275 0.0738  -0.0033 59  SER A CA  
509  C C   A SER A 58  ? 0.4832 0.2923 0.3266 -0.0431 0.0810  -0.0094 59  SER A C   
510  C C   B SER A 58  ? 0.4804 0.2898 0.3237 -0.0432 0.0808  -0.0094 59  SER A C   
511  O O   A SER A 58  ? 0.5178 0.3076 0.3459 -0.0491 0.0871  -0.0078 59  SER A O   
512  O O   B SER A 58  ? 0.5116 0.3024 0.3398 -0.0492 0.0867  -0.0076 59  SER A O   
513  C CB  A SER A 58  ? 0.4604 0.2625 0.3152 -0.0212 0.0773  -0.0060 59  SER A CB  
514  C CB  B SER A 58  ? 0.4594 0.2619 0.3143 -0.0220 0.0776  -0.0064 59  SER A CB  
515  O OG  A SER A 58  ? 0.5120 0.3149 0.3732 -0.0061 0.0710  -0.0013 59  SER A OG  
516  O OG  B SER A 58  ? 0.5410 0.3149 0.3814 -0.0250 0.0864  -0.0065 59  SER A OG  
517  N N   . ILE A 59  ? 0.4210 0.2500 0.2753 -0.0499 0.0799  -0.0169 60  ILE A N   
518  C CA  . ILE A 59  ? 0.4133 0.2468 0.2658 -0.0639 0.0847  -0.0249 60  ILE A CA  
519  C C   . ILE A 59  ? 0.4437 0.2831 0.2929 -0.0700 0.0843  -0.0246 60  ILE A C   
520  O O   . ILE A 59  ? 0.4618 0.2888 0.3010 -0.0802 0.0927  -0.0277 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4226 0.2773 0.2867 -0.0674 0.0805  -0.0324 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4277 0.2741 0.2918 -0.0655 0.0841  -0.0350 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.4018 0.2672 0.2673 -0.0802 0.0823  -0.0415 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4534 0.3184 0.3248 -0.0670 0.0783  -0.0401 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.3691 0.2263 0.2262 -0.0648 0.0760  -0.0216 61  PHE A N   
526  C CA  . PHE A 60  ? 0.3784 0.2440 0.2343 -0.0715 0.0764  -0.0235 61  PHE A CA  
527  C C   . PHE A 60  ? 0.4431 0.2897 0.2828 -0.0705 0.0797  -0.0160 61  PHE A C   
528  O O   . PHE A 60  ? 0.4624 0.3134 0.2986 -0.0780 0.0822  -0.0182 61  PHE A O   
529  C CB  . PHE A 60  ? 0.3713 0.2637 0.2419 -0.0686 0.0671  -0.0258 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.3713 0.2787 0.2530 -0.0705 0.0635  -0.0332 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.4177 0.3301 0.3016 -0.0808 0.0674  -0.0429 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.3702 0.2860 0.2586 -0.0626 0.0561  -0.0310 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.4172 0.3427 0.3089 -0.0817 0.0622  -0.0495 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.3952 0.3212 0.2889 -0.0644 0.0522  -0.0369 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.3849 0.3155 0.2797 -0.0732 0.0544  -0.0457 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4304 0.2551 0.2592 -0.0615 0.0798  -0.0077 62  THR A N   
537  C CA  . THR A 61  ? 0.4499 0.2500 0.2574 -0.0605 0.0828  0.0002  62  THR A CA  
538  C C   . THR A 61  ? 0.5578 0.3284 0.3477 -0.0695 0.0949  -0.0013 62  THR A C   
539  O O   . THR A 61  ? 0.5604 0.3045 0.3274 -0.0719 0.0999  0.0045  62  THR A O   
540  C CB  . THR A 61  ? 0.5243 0.3172 0.3282 -0.0443 0.0741  0.0102  62  THR A CB  
541  O OG1 . THR A 61  ? 0.4939 0.2812 0.3049 -0.0355 0.0732  0.0104  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.4733 0.2926 0.2902 -0.0385 0.0638  0.0114  62  THR A CG2 
543  N N   . ASP A 62  ? 0.5146 0.2884 0.3130 -0.0757 0.1001  -0.0095 63  ASP A N   
544  C CA  . ASP A 62  ? 0.5521 0.2996 0.3352 -0.0866 0.1128  -0.0131 63  ASP A CA  
545  C C   . ASP A 62  ? 0.6069 0.3593 0.3851 -0.1039 0.1210  -0.0205 63  ASP A C   
546  O O   . ASP A 62  ? 0.5566 0.3401 0.3532 -0.1097 0.1180  -0.0294 63  ASP A O   
547  C CB  . ASP A 62  ? 0.5664 0.3179 0.3603 -0.0889 0.1157  -0.0210 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.7088 0.4343 0.4874 -0.1021 0.1297  -0.0264 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.7895 0.4820 0.5518 -0.0968 0.1346  -0.0203 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.6815 0.4192 0.4643 -0.1177 0.1359  -0.0371 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.6441 0.3650 0.3971 -0.1122 0.1315  -0.0175 64  GLN A N   
552  C CA  . GLN A 63  ? 0.6651 0.3868 0.4104 -0.1304 0.1420  -0.0251 64  GLN A CA  
553  C C   . GLN A 63  ? 0.6914 0.4362 0.4546 -0.1457 0.1484  -0.0417 64  GLN A C   
554  O O   . GLN A 63  ? 0.7083 0.4712 0.4778 -0.1581 0.1529  -0.0509 64  GLN A O   
555  C CB  . GLN A 63  ? 0.7373 0.4138 0.4474 -0.1375 0.1540  -0.0186 64  GLN A CB  
556  C CG  . GLN A 63  ? 0.9447 0.6039 0.6350 -0.1261 0.1471  -0.0041 64  GLN A CG  
557  N N   . LEU A 64  ? 0.5981 0.3437 0.3698 -0.1450 0.1489  -0.0466 65  LEU A N   
558  C CA  . LEU A 64  ? 0.5700 0.3403 0.3593 -0.1580 0.1524  -0.0627 65  LEU A CA  
559  C C   . LEU A 64  ? 0.5935 0.4019 0.4094 -0.1487 0.1378  -0.0663 65  LEU A C   
560  O O   . LEU A 64  ? 0.5971 0.4354 0.4302 -0.1562 0.1356  -0.0780 65  LEU A O   
561  C CB  . LEU A 64  ? 0.5867 0.3361 0.3683 -0.1649 0.1618  -0.0678 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.6842 0.4004 0.4424 -0.1816 0.1796  -0.0712 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.7063 0.4033 0.4589 -0.1872 0.1879  -0.0768 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.7365 0.4727 0.5015 -0.2011 0.1879  -0.0853 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.5165 0.3232 0.3355 -0.1329 0.1283  -0.0573 66  LYS A N   
566  C CA  . LYS A 65  ? 0.4740 0.3107 0.3132 -0.1251 0.1158  -0.0602 66  LYS A CA  
567  C C   . LYS A 65  ? 0.5283 0.3895 0.3793 -0.1194 0.1060  -0.0584 66  LYS A C   
568  O O   . LYS A 65  ? 0.5081 0.3959 0.3755 -0.1178 0.0975  -0.0647 66  LYS A O   
569  C CB  . LYS A 65  ? 0.4737 0.3013 0.3124 -0.1122 0.1107  -0.0530 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.4876 0.2948 0.3181 -0.1175 0.1197  -0.0571 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.4548 0.2576 0.2879 -0.1048 0.1149  -0.0519 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.5277 0.3049 0.3508 -0.1079 0.1250  -0.0545 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.5722 0.3154 0.3785 -0.1035 0.1320  -0.0461 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.5236 0.3743 0.3646 -0.1169 0.1074  -0.0505 67  CYS A N   
575  C CA  . CYS A 66  ? 0.5161 0.3875 0.3664 -0.1126 0.0998  -0.0492 67  CYS A CA  
576  C C   . CYS A 66  ? 0.5587 0.4585 0.4258 -0.1223 0.0997  -0.0631 67  CYS A C   
577  O O   . CYS A 66  ? 0.5469 0.4692 0.4276 -0.1165 0.0908  -0.0644 67  CYS A O   
578  C CB  . CYS A 66  ? 0.5523 0.4048 0.3850 -0.1117 0.1036  -0.0402 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.6444 0.4776 0.4586 -0.1311 0.1206  -0.0463 67  CYS A SG  
580  N N   . ASN A 67  ? 0.5097 0.4083 0.3762 -0.1369 0.1098  -0.0744 68  ASN A N   
581  C CA  . ASN A 67  ? 0.5054 0.4322 0.3894 -0.1473 0.1109  -0.0902 68  ASN A CA  
582  C C   . ASN A 67  ? 0.5252 0.4742 0.4263 -0.1465 0.1030  -0.1003 68  ASN A C   
583  O O   . ASN A 67  ? 0.4978 0.4732 0.4161 -0.1534 0.1017  -0.1147 68  ASN A O   
584  C CB  . ASN A 67  ? 0.5259 0.4408 0.3996 -0.1658 0.1277  -0.0986 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.6958 0.5920 0.5516 -0.1677 0.1345  -0.0902 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.7276 0.5924 0.5597 -0.1766 0.1471  -0.0862 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.5757 0.4875 0.4395 -0.1591 0.1261  -0.0865 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.4833 0.4223 0.3797 -0.1383 0.0976  -0.0936 69  LEU A N   
589  C CA  . LEU A 68  ? 0.4587 0.4154 0.3665 -0.1376 0.0897  -0.1021 69  LEU A CA  
590  C C   . LEU A 68  ? 0.4791 0.4593 0.4009 -0.1257 0.0741  -0.1013 69  LEU A C   
591  O O   . LEU A 68  ? 0.4615 0.4366 0.3804 -0.1150 0.0691  -0.0901 69  LEU A O   
592  C CB  . LEU A 68  ? 0.4691 0.4052 0.3648 -0.1345 0.0910  -0.0962 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.5427 0.4518 0.4233 -0.1453 0.1062  -0.0974 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.5484 0.4377 0.4189 -0.1392 0.1066  -0.0909 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.5596 0.4805 0.4464 -0.1622 0.1134  -0.1144 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4326 0.4376 0.3689 -0.1272 0.0660  -0.1135 70  SER A N   
597  N N   B SER A 69  ? 0.4304 0.4354 0.3667 -0.1273 0.0662  -0.1136 70  SER A N   
598  C CA  A SER A 69  ? 0.4132 0.4376 0.3608 -0.1152 0.0503  -0.1133 70  SER A CA  
599  C CA  B SER A 69  ? 0.4104 0.4358 0.3586 -0.1158 0.0504  -0.1142 70  SER A CA  
600  C C   A SER A 69  ? 0.4233 0.4425 0.3635 -0.1083 0.0410  -0.1093 70  SER A C   
601  C C   B SER A 69  ? 0.4228 0.4424 0.3633 -0.1085 0.0411  -0.1097 70  SER A C   
602  O O   A SER A 69  ? 0.3929 0.4194 0.3355 -0.0976 0.0284  -0.1058 70  SER A O   
603  O O   B SER A 69  ? 0.3927 0.4199 0.3357 -0.0978 0.0284  -0.1063 70  SER A O   
604  C CB  A SER A 69  ? 0.4608 0.5161 0.4292 -0.1187 0.0452  -0.1293 70  SER A CB  
605  C CB  B SER A 69  ? 0.4524 0.5085 0.4210 -0.1203 0.0457  -0.1310 70  SER A CB  
606  O OG  A SER A 69  ? 0.5561 0.6215 0.5290 -0.1279 0.0459  -0.1423 70  SER A OG  
607  O OG  B SER A 69  ? 0.5257 0.5889 0.5022 -0.1264 0.0542  -0.1356 70  SER A OG  
608  N N   . VAL A 70  ? 0.3912 0.3959 0.3207 -0.1153 0.0481  -0.1103 71  VAL A N   
609  C CA  . VAL A 70  ? 0.3945 0.3914 0.3139 -0.1113 0.0422  -0.1074 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4259 0.3950 0.3304 -0.1127 0.0536  -0.0985 71  VAL A C   
611  O O   . VAL A 70  ? 0.4197 0.3767 0.3202 -0.1219 0.0661  -0.1012 71  VAL A O   
612  C CB  . VAL A 70  ? 0.4520 0.4637 0.3752 -0.1187 0.0377  -0.1215 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.4596 0.4604 0.3682 -0.1159 0.0327  -0.1184 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.4434 0.4849 0.3840 -0.1153 0.0248  -0.1317 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3568 0.3152 0.2530 -0.1037 0.0495  -0.0888 72  ILE A N   
616  C CA  . ILE A 71  ? 0.3554 0.2906 0.2404 -0.1029 0.0586  -0.0819 72  ILE A CA  
617  C C   . ILE A 71  ? 0.4056 0.3377 0.2821 -0.1026 0.0547  -0.0837 72  ILE A C   
618  O O   . ILE A 71  ? 0.4035 0.3423 0.2785 -0.0960 0.0446  -0.0806 72  ILE A O   
619  C CB  . ILE A 71  ? 0.3842 0.3100 0.2685 -0.0932 0.0595  -0.0696 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.3930 0.3192 0.2816 -0.0946 0.0637  -0.0676 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.4078 0.3132 0.2837 -0.0901 0.0668  -0.0640 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.4427 0.3526 0.3245 -0.1042 0.0768  -0.0707 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.3894 0.3089 0.2583 -0.1102 0.0636  -0.0886 73  ASN A N   
624  C CA  . ASN A 72  ? 0.4016 0.3163 0.2601 -0.1115 0.0619  -0.0911 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4402 0.3360 0.2925 -0.1065 0.0697  -0.0836 73  ASN A C   
626  O O   . ASN A 72  ? 0.4188 0.2993 0.2705 -0.1080 0.0808  -0.0828 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4538 0.3681 0.3082 -0.1237 0.0669  -0.1032 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.6827 0.6189 0.5464 -0.1296 0.0599  -0.1134 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.5432 0.4966 0.4098 -0.1252 0.0461  -0.1153 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.6336 0.5689 0.5019 -0.1397 0.0696  -0.1210 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.3858 0.2818 0.2330 -0.1008 0.0642  -0.0791 74  LEU A N   
632  C CA  . LEU A 73  ? 0.3873 0.2693 0.2312 -0.0965 0.0718  -0.0744 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4407 0.3111 0.2743 -0.1039 0.0799  -0.0816 74  LEU A C   
634  O O   . LEU A 73  ? 0.4428 0.3172 0.2687 -0.1120 0.0770  -0.0893 74  LEU A O   
635  C CB  . LEU A 73  ? 0.3763 0.2623 0.2186 -0.0895 0.0654  -0.0680 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.3966 0.2933 0.2486 -0.0818 0.0575  -0.0609 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.4104 0.3059 0.2605 -0.0762 0.0559  -0.0554 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.3929 0.2881 0.2555 -0.0786 0.0623  -0.0576 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.4099 0.2672 0.2440 -0.1007 0.0897  -0.0799 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4304 0.2750 0.2558 -0.1070 0.0995  -0.0871 75  ASP A CA  
641  C C   . ASP A 74  ? 0.4906 0.3396 0.3014 -0.1129 0.0939  -0.0911 75  ASP A C   
642  O O   . ASP A 74  ? 0.4726 0.3279 0.2808 -0.1087 0.0864  -0.0859 75  ASP A O   
643  C CB  . ASP A 74  ? 0.4530 0.2872 0.2849 -0.0996 0.1088  -0.0843 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.5677 0.3878 0.3938 -0.1046 0.1210  -0.0925 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.5825 0.4031 0.3971 -0.1114 0.1218  -0.0978 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.5741 0.3810 0.4059 -0.1014 0.1299  -0.0935 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.5006 0.3453 0.2998 -0.1231 0.0969  -0.1002 76  PRO A N   
648  C CA  . PRO A 75  ? 0.5084 0.3554 0.2895 -0.1287 0.0900  -0.1036 76  PRO A CA  
649  C C   . PRO A 75  ? 0.5532 0.3919 0.3243 -0.1276 0.0943  -0.1012 76  PRO A C   
650  O O   . PRO A 75  ? 0.5659 0.4044 0.3192 -0.1310 0.0871  -0.1013 76  PRO A O   
651  C CB  . PRO A 75  ? 0.5505 0.3929 0.3220 -0.1404 0.0949  -0.1150 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.6165 0.4486 0.3996 -0.1409 0.1084  -0.1175 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5373 0.3733 0.3372 -0.1306 0.1065  -0.1082 76  PRO A CD  
654  N N   . GLU A 76  ? 0.5156 0.3475 0.2976 -0.1230 0.1058  -0.0997 77  GLU A N   
655  C CA  . GLU A 76  ? 0.5350 0.3615 0.3113 -0.1229 0.1122  -0.0996 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5213 0.3559 0.2999 -0.1161 0.1031  -0.0905 77  GLU A C   
657  O O   . GLU A 76  ? 0.5206 0.3513 0.2902 -0.1182 0.1063  -0.0902 77  GLU A O   
658  C CB  . GLU A 76  ? 0.5650 0.3851 0.3570 -0.1186 0.1266  -0.1026 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.8258 0.6393 0.6111 -0.1233 0.1381  -0.1090 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.1990 1.0011 0.9686 -0.1347 0.1470  -0.1196 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.2190 1.0142 0.9971 -0.1343 0.1551  -0.1249 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.1364 0.9345 0.8833 -0.1442 0.1461  -0.1226 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.4575 0.3022 0.2475 -0.1092 0.0931  -0.0840 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4498 0.3017 0.2431 -0.1026 0.0849  -0.0760 78  ILE A CA  
665  C C   . ILE A 77  ? 0.5043 0.3542 0.2763 -0.1064 0.0744  -0.0744 78  ILE A C   
666  O O   . ILE A 77  ? 0.4989 0.3511 0.2618 -0.1092 0.0655  -0.0767 78  ILE A O   
667  C CB  . ILE A 77  ? 0.4666 0.3292 0.2787 -0.0942 0.0788  -0.0703 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.4626 0.3224 0.2915 -0.0893 0.0887  -0.0705 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4332 0.3029 0.2482 -0.0881 0.0706  -0.0629 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.5121 0.3699 0.3494 -0.0850 0.0978  -0.0708 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.5054 0.3505 0.2693 -0.1063 0.0756  -0.0711 79  ASN A N   
672  C CA  . ASN A 78  ? 0.5239 0.3610 0.2632 -0.1093 0.0667  -0.0682 79  ASN A CA  
673  C C   . ASN A 78  ? 0.5199 0.3653 0.2646 -0.1009 0.0522  -0.0611 79  ASN A C   
674  O O   . ASN A 78  ? 0.4894 0.3417 0.2508 -0.0949 0.0535  -0.0567 79  ASN A O   
675  C CB  . ASN A 78  ? 0.5604 0.3864 0.2881 -0.1144 0.0768  -0.0684 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.7375 0.5495 0.4355 -0.1179 0.0690  -0.0642 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.6060 0.4166 0.3038 -0.1143 0.0656  -0.0584 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.6524 0.4518 0.3227 -0.1251 0.0658  -0.0672 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.4873 0.3329 0.2187 -0.1001 0.0380  -0.0607 80  PRO A N   
680  C CA  . PRO A 79  ? 0.4759 0.3300 0.2142 -0.0912 0.0244  -0.0553 80  PRO A CA  
681  C C   . PRO A 79  ? 0.5204 0.3658 0.2518 -0.0880 0.0236  -0.0483 80  PRO A C   
682  O O   . PRO A 79  ? 0.4934 0.3484 0.2414 -0.0807 0.0195  -0.0443 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5262 0.3797 0.2478 -0.0912 0.0097  -0.0580 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.5849 0.4368 0.3002 -0.1000 0.0162  -0.0660 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5367 0.3765 0.2475 -0.1065 0.0332  -0.0663 80  PRO A CD  
686  N N   . GLU A 80  ? 0.5007 0.3272 0.2069 -0.0946 0.0287  -0.0473 81  GLU A N   
687  C CA  . GLU A 80  ? 0.5025 0.3186 0.2004 -0.0937 0.0299  -0.0416 81  GLU A CA  
688  C C   . GLU A 80  ? 0.5064 0.3345 0.2312 -0.0922 0.0415  -0.0417 81  GLU A C   
689  O O   . GLU A 80  ? 0.4690 0.3012 0.2029 -0.0868 0.0379  -0.0373 81  GLU A O   
690  C CB  . GLU A 80  ? 0.5524 0.3435 0.2149 -0.1032 0.0348  -0.0413 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.6401 0.4178 0.2913 -0.1031 0.0354  -0.0355 81  GLU A CG  
692  C CD  . GLU A 80  ? 0.9610 0.7115 0.5767 -0.1146 0.0440  -0.0352 81  GLU A CD  
693  O OE1 . GLU A 80  ? 0.9643 0.6957 0.5579 -0.1140 0.0385  -0.0291 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 0.8656 0.6122 0.4746 -0.1247 0.0570  -0.0413 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.4794 0.3130 0.2168 -0.0962 0.0543  -0.0473 82  GLY A N   
696  C CA  . GLY A 81  ? 0.4616 0.3079 0.2256 -0.0932 0.0637  -0.0483 82  GLY A CA  
697  C C   . GLY A 81  ? 0.4535 0.3157 0.2403 -0.0833 0.0555  -0.0444 82  GLY A C   
698  O O   . GLY A 81  ? 0.4131 0.2832 0.2140 -0.0788 0.0559  -0.0416 82  GLY A O   
699  N N   . PHE A 82  ? 0.4067 0.2738 0.1961 -0.0808 0.0483  -0.0451 83  PHE A N   
700  C CA  . PHE A 82  ? 0.3739 0.2550 0.1824 -0.0732 0.0415  -0.0424 83  PHE A CA  
701  C C   . PHE A 82  ? 0.3963 0.2784 0.2016 -0.0685 0.0312  -0.0374 83  PHE A C   
702  O O   . PHE A 82  ? 0.3870 0.2786 0.2079 -0.0633 0.0302  -0.0345 83  PHE A O   
703  C CB  . PHE A 82  ? 0.3920 0.2783 0.2031 -0.0738 0.0369  -0.0459 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.3833 0.2831 0.2136 -0.0678 0.0329  -0.0441 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.4193 0.3231 0.2654 -0.0655 0.0406  -0.0432 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.3924 0.2998 0.2242 -0.0639 0.0214  -0.0430 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.4162 0.3296 0.2758 -0.0610 0.0375  -0.0409 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.4039 0.3237 0.2527 -0.0596 0.0192  -0.0421 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.3801 0.3019 0.2412 -0.0589 0.0277  -0.0407 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.4042 0.2754 0.1881 -0.0699 0.0231  -0.0364 84  CYS A N   
711  C CA  . CYS A 83  ? 0.4373 0.3055 0.2155 -0.0646 0.0128  -0.0319 84  CYS A CA  
712  C C   . CYS A 83  ? 0.4424 0.3073 0.2239 -0.0649 0.0195  -0.0286 84  CYS A C   
713  O O   . CYS A 83  ? 0.4129 0.2852 0.2059 -0.0593 0.0150  -0.0260 84  CYS A O   
714  C CB  . CYS A 83  ? 0.5013 0.3528 0.2510 -0.0657 0.0035  -0.0310 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.5779 0.4230 0.3199 -0.0566 -0.0112 -0.0258 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4230 0.2780 0.1950 -0.0725 0.0309  -0.0302 85  ILE A N   
717  C CA  . ILE A 84  ? 0.4010 0.2547 0.1769 -0.0750 0.0389  -0.0295 85  ILE A CA  
718  C C   . ILE A 84  ? 0.3955 0.2700 0.2015 -0.0693 0.0413  -0.0300 85  ILE A C   
719  O O   . ILE A 84  ? 0.3677 0.2471 0.1816 -0.0668 0.0400  -0.0280 85  ILE A O   
720  C CB  . ILE A 84  ? 0.4418 0.2846 0.2050 -0.0854 0.0523  -0.0339 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.4735 0.2900 0.1995 -0.0920 0.0496  -0.0318 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4324 0.2833 0.2109 -0.0884 0.0634  -0.0369 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.5445 0.3489 0.2536 -0.1031 0.0617  -0.0368 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3563 0.2414 0.1771 -0.0673 0.0442  -0.0325 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3426 0.2440 0.1880 -0.0613 0.0457  -0.0322 86  LEU A CA  
726  C C   . LEU A 85  ? 0.3560 0.2657 0.2092 -0.0549 0.0358  -0.0285 86  LEU A C   
727  O O   . LEU A 85  ? 0.3330 0.2527 0.1999 -0.0509 0.0353  -0.0269 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3486 0.2538 0.2040 -0.0608 0.0523  -0.0355 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.4118 0.3138 0.2675 -0.0657 0.0641  -0.0409 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.4216 0.3241 0.2852 -0.0644 0.0699  -0.0445 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.4134 0.3261 0.2842 -0.0638 0.0684  -0.0423 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3377 0.2449 0.1833 -0.0541 0.0279  -0.0283 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3185 0.2348 0.1725 -0.0486 0.0191  -0.0267 87  LEU A CA  
734  C C   . LEU A 86  ? 0.3578 0.2716 0.2086 -0.0463 0.0150  -0.0238 87  LEU A C   
735  O O   . LEU A 86  ? 0.3348 0.2586 0.1983 -0.0424 0.0131  -0.0227 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3219 0.2378 0.1692 -0.0485 0.0113  -0.0291 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.3612 0.2896 0.2203 -0.0434 0.0033  -0.0301 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.3453 0.2851 0.2215 -0.0429 0.0089  -0.0303 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.3944 0.3251 0.2485 -0.0431 -0.0054 -0.0346 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3389 0.2372 0.1707 -0.0495 0.0143  -0.0229 88  ASP A N   
741  C CA  . ASP A 87  ? 0.3432 0.2345 0.1690 -0.0487 0.0122  -0.0204 88  ASP A CA  
742  C C   . ASP A 87  ? 0.3593 0.2602 0.1998 -0.0501 0.0201  -0.0210 88  ASP A C   
743  O O   . ASP A 87  ? 0.3557 0.2617 0.2034 -0.0471 0.0172  -0.0199 88  ASP A O   
744  C CB  . ASP A 87  ? 0.3958 0.2641 0.1944 -0.0540 0.0130  -0.0192 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.5688 0.4255 0.3497 -0.0502 0.0012  -0.0178 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.5618 0.4304 0.3546 -0.0429 -0.0082 -0.0187 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.5893 0.4252 0.3440 -0.0547 0.0012  -0.0165 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3355 0.2395 0.1810 -0.0545 0.0298  -0.0235 89  PHE A N   
749  C CA  . PHE A 88  ? 0.3028 0.2196 0.1652 -0.0547 0.0362  -0.0255 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3058 0.2389 0.1865 -0.0474 0.0313  -0.0239 89  PHE A C   
751  O O   . PHE A 88  ? 0.2785 0.2200 0.1682 -0.0460 0.0306  -0.0239 89  PHE A O   
752  C CB  . PHE A 88  ? 0.3103 0.2299 0.1780 -0.0584 0.0463  -0.0299 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.3029 0.2400 0.1923 -0.0555 0.0502  -0.0328 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3304 0.2721 0.2237 -0.0594 0.0539  -0.0358 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3302 0.2786 0.2353 -0.0485 0.0490  -0.0323 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.3079 0.2686 0.2224 -0.0559 0.0555  -0.0393 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3510 0.3153 0.2748 -0.0440 0.0500  -0.0345 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3272 0.2992 0.2566 -0.0474 0.0527  -0.0383 89  PHE A CZ  
759  N N   . MET A 89  ? 0.2727 0.2092 0.1575 -0.0441 0.0287  -0.0231 90  MET A N   
760  C CA  . MET A 89  ? 0.2655 0.2140 0.1636 -0.0387 0.0253  -0.0215 90  MET A CA  
761  C C   . MET A 89  ? 0.3082 0.2603 0.2073 -0.0367 0.0191  -0.0202 90  MET A C   
762  O O   . MET A 89  ? 0.2930 0.2550 0.2019 -0.0342 0.0185  -0.0197 90  MET A O   
763  C CB  . MET A 89  ? 0.2751 0.2229 0.1728 -0.0378 0.0237  -0.0215 90  MET A CB  
764  C CG  . MET A 89  ? 0.2997 0.2435 0.1978 -0.0392 0.0303  -0.0230 90  MET A CG  
765  S SD  . MET A 89  ? 0.3379 0.2804 0.2355 -0.0396 0.0294  -0.0237 90  MET A SD  
766  C CE  . MET A 89  ? 0.3466 0.2795 0.2401 -0.0427 0.0380  -0.0267 90  MET A CE  
767  N N   . TYR A 90  ? 0.2754 0.2188 0.1636 -0.0371 0.0139  -0.0202 91  TYR A N   
768  C CA  . TYR A 90  ? 0.2751 0.2204 0.1644 -0.0341 0.0077  -0.0200 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3319 0.2701 0.2154 -0.0360 0.0088  -0.0197 91  TYR A C   
770  O O   . TYR A 90  ? 0.3256 0.2641 0.2101 -0.0334 0.0043  -0.0200 91  TYR A O   
771  C CB  . TYR A 90  ? 0.2966 0.2368 0.1789 -0.0315 0.0000  -0.0210 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.2980 0.2500 0.1907 -0.0299 -0.0018 -0.0233 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3161 0.2678 0.2076 -0.0325 0.0012  -0.0244 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.3093 0.2722 0.2125 -0.0267 -0.0055 -0.0256 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.3085 0.2696 0.2084 -0.0329 0.0010  -0.0274 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.3081 0.2813 0.2199 -0.0272 -0.0056 -0.0291 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.3281 0.3000 0.2379 -0.0307 -0.0021 -0.0298 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.2983 0.2794 0.2158 -0.0328 -0.0011 -0.0343 91  TYR A OH  
779  N N   . THR A 91  ? 0.3037 0.2349 0.1807 -0.0414 0.0155  -0.0202 92  THR A N   
780  C CA  . THR A 91  ? 0.3207 0.2426 0.1898 -0.0455 0.0181  -0.0209 92  THR A CA  
781  C C   . THR A 91  ? 0.3429 0.2727 0.2201 -0.0511 0.0270  -0.0243 92  THR A C   
782  O O   . THR A 91  ? 0.3299 0.2551 0.2035 -0.0555 0.0298  -0.0262 92  THR A O   
783  C CB  . THR A 91  ? 0.3687 0.2663 0.2133 -0.0493 0.0179  -0.0195 92  THR A CB  
784  O OG1 . THR A 91  ? 0.3710 0.2646 0.2097 -0.0550 0.0252  -0.0208 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.3791 0.2675 0.2137 -0.0429 0.0072  -0.0171 92  THR A CG2 
786  N N   A SER A 92  ? 0.2897 0.2305 0.1777 -0.0511 0.0316  -0.0261 93  SER A N   
787  N N   B SER A 92  ? 0.2911 0.2314 0.1786 -0.0513 0.0317  -0.0260 93  SER A N   
788  C CA  A SER A 92  ? 0.2775 0.2289 0.1764 -0.0554 0.0399  -0.0312 93  SER A CA  
789  C CA  B SER A 92  ? 0.2819 0.2328 0.1805 -0.0553 0.0399  -0.0311 93  SER A CA  
790  C C   A SER A 92  ? 0.3235 0.2602 0.2079 -0.0648 0.0487  -0.0344 93  SER A C   
791  C C   B SER A 92  ? 0.3410 0.2772 0.2249 -0.0651 0.0487  -0.0345 93  SER A C   
792  O O   A SER A 92  ? 0.3178 0.2636 0.2118 -0.0694 0.0570  -0.0405 93  SER A O   
793  O O   B SER A 92  ? 0.3380 0.2828 0.2308 -0.0705 0.0570  -0.0407 93  SER A O   
794  C CB  A SER A 92  ? 0.2807 0.2446 0.1908 -0.0561 0.0397  -0.0341 93  SER A CB  
795  C CB  B SER A 92  ? 0.2976 0.2636 0.2098 -0.0548 0.0390  -0.0337 93  SER A CB  
796  O OG  A SER A 92  ? 0.2532 0.2281 0.1726 -0.0488 0.0321  -0.0312 93  SER A OG  
797  O OG  B SER A 92  ? 0.3374 0.2935 0.2397 -0.0619 0.0422  -0.0360 93  SER A OG  
798  N N   A ARG A 93  ? 0.3184 0.2326 0.1795 -0.0674 0.0467  -0.0309 94  ARG A N   
799  N N   B ARG A 93  ? 0.3238 0.2380 0.1848 -0.0674 0.0468  -0.0309 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3311 0.2263 0.1720 -0.0775 0.0551  -0.0331 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3425 0.2365 0.1821 -0.0774 0.0547  -0.0328 94  ARG A CA  
802  C C   A ARG A 93  ? 0.3885 0.2777 0.2214 -0.0783 0.0571  -0.0330 94  ARG A C   
803  C C   B ARG A 93  ? 0.3965 0.2843 0.2278 -0.0786 0.0570  -0.0328 94  ARG A C   
804  O O   A ARG A 93  ? 0.3656 0.2508 0.1931 -0.0723 0.0488  -0.0287 94  ARG A O   
805  O O   B ARG A 93  ? 0.3832 0.2663 0.2083 -0.0728 0.0487  -0.0285 94  ARG A O   
806  C CB  A ARG A 93  ? 0.3835 0.2528 0.1982 -0.0802 0.0515  -0.0291 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.3783 0.2473 0.1927 -0.0789 0.0497  -0.0282 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4423 0.3136 0.2619 -0.0811 0.0511  -0.0301 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.4649 0.3371 0.2856 -0.0780 0.0476  -0.0286 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.5402 0.3864 0.3370 -0.0783 0.0433  -0.0246 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5199 0.3829 0.3325 -0.0901 0.0591  -0.0336 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.6901 0.5051 0.4544 -0.0859 0.0474  -0.0226 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.5564 0.4224 0.3750 -0.0902 0.0578  -0.0350 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.8572 0.6530 0.6041 -0.0970 0.0569  -0.0248 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.7361 0.5766 0.5331 -0.0933 0.0572  -0.0327 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.6995 0.5065 0.4608 -0.1017 0.0630  -0.0299 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.5878 0.4326 0.3922 -0.0940 0.0571  -0.0351 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.7114 0.4757 0.4247 -0.1043 0.0606  -0.0223 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5853 0.3942 0.3513 -0.0958 0.0566  -0.0280 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.3594 0.2483 0.1916 -0.0866 0.0689  -0.0390 95  LEU A N   
821  C CA  . LEU A 94  ? 0.3572 0.2404 0.1821 -0.0891 0.0732  -0.0407 95  LEU A CA  
822  C C   . LEU A 94  ? 0.4433 0.3010 0.2376 -0.1008 0.0806  -0.0418 95  LEU A C   
823  O O   . LEU A 94  ? 0.4383 0.2930 0.2297 -0.1109 0.0919  -0.0475 95  LEU A O   
824  C CB  . LEU A 94  ? 0.3469 0.2518 0.1979 -0.0881 0.0814  -0.0481 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.3857 0.2872 0.2338 -0.0892 0.0863  -0.0508 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.3654 0.2668 0.2140 -0.0800 0.0756  -0.0446 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.4082 0.3287 0.2812 -0.0889 0.0962  -0.0599 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4404 0.2793 0.2107 -0.1003 0.0745  -0.0370 96  ASN A N   
829  C CA  . ASN A 95  ? 0.4796 0.2897 0.2144 -0.1112 0.0799  -0.0368 96  ASN A CA  
830  C C   . ASN A 95  ? 0.5414 0.3533 0.2755 -0.1193 0.0925  -0.0440 96  ASN A C   
831  O O   . ASN A 95  ? 0.5475 0.3513 0.2684 -0.1190 0.0894  -0.0429 96  ASN A O   
832  C CB  . ASN A 95  ? 0.5540 0.3432 0.2620 -0.1057 0.0655  -0.0286 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.7816 0.5368 0.4473 -0.1158 0.0688  -0.0268 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.6698 0.4116 0.3216 -0.1280 0.0819  -0.0302 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.7219 0.4626 0.3655 -0.1114 0.0572  -0.0220 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.5009 0.3259 0.2522 -0.1262 0.1064  -0.0527 97  LEU A N   
837  C CA  . LEU A 96  ? 0.5145 0.3454 0.2716 -0.1334 0.1200  -0.0620 97  LEU A CA  
838  C C   . LEU A 96  ? 0.5819 0.3866 0.3052 -0.1502 0.1327  -0.0656 97  LEU A C   
839  O O   . LEU A 96  ? 0.5821 0.3785 0.2967 -0.1592 0.1399  -0.0676 97  LEU A O   
840  C CB  . LEU A 96  ? 0.5033 0.3653 0.3003 -0.1300 0.1269  -0.0706 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.5708 0.4484 0.3880 -0.1302 0.1371  -0.0805 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.5796 0.4568 0.3984 -0.1206 0.1287  -0.0758 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5416 0.4501 0.3981 -0.1245 0.1405  -0.0884 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.5592 0.3479 0.2592 -0.1552 0.1351  -0.0659 98  ARG A N   
845  C CA  . ARG A 97  ? 0.6034 0.3628 0.2644 -0.1718 0.1467  -0.0686 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6166 0.3808 0.2803 -0.1791 0.1599  -0.0786 98  ARG A C   
847  O O   . ARG A 97  ? 0.5820 0.3640 0.2682 -0.1696 0.1555  -0.0802 98  ARG A O   
848  C CB  . ARG A 97  ? 0.6554 0.3818 0.2731 -0.1706 0.1330  -0.0569 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.7392 0.4574 0.3518 -0.1623 0.1194  -0.0472 98  ARG A CG  
850  C CD  . ARG A 97  ? 0.9827 0.6700 0.5554 -0.1582 0.1038  -0.0364 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.2355 0.8850 0.7596 -0.1730 0.1122  -0.0358 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.5151 1.1361 1.0106 -0.1818 0.1174  -0.0328 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.3765 0.9604 0.8243 -0.1962 0.1257  -0.0320 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.3877 1.0154 0.9002 -0.1772 0.1153  -0.0309 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.6132 0.3605 0.2535 -0.1968 0.1772  -0.0862 99  GLU A N   
856  C CA  . GLU A 98  ? 0.6130 0.3633 0.2539 -0.2055 0.1917  -0.0973 99  GLU A CA  
857  C C   . GLU A 98  ? 0.6832 0.4253 0.3098 -0.1991 0.1807  -0.0921 99  GLU A C   
858  O O   . GLU A 98  ? 0.6704 0.4294 0.3194 -0.1958 0.1856  -0.0995 99  GLU A O   
859  C CB  . GLU A 98  ? 0.6705 0.3952 0.2759 -0.2277 0.2109  -0.1044 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.8053 0.5328 0.4104 -0.2387 0.2283  -0.1178 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.1957 0.8960 0.7622 -0.2624 0.2485  -0.1253 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.1524 0.8146 0.6683 -0.2702 0.2438  -0.1151 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.1793 0.8955 0.7654 -0.2733 0.2693  -0.1419 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.6806 0.3976 0.2718 -0.1966 0.1656  -0.0800 100 GLY A N   
865  C CA  . GLY A 99  ? 0.6960 0.4048 0.2705 -0.1916 0.1537  -0.0756 100 GLY A CA  
866  C C   . GLY A 99  ? 0.6823 0.4169 0.2917 -0.1745 0.1400  -0.0727 100 GLY A C   
867  O O   . GLY A 99  ? 0.6893 0.4239 0.2941 -0.1721 0.1346  -0.0733 100 GLY A O   
868  N N   . ASN A 100 ? 0.6087 0.3647 0.2519 -0.1636 0.1349  -0.0702 101 ASN A N   
869  C CA  . ASN A 100 ? 0.5600 0.3376 0.2331 -0.1484 0.1226  -0.0669 101 ASN A CA  
870  C C   . ASN A 100 ? 0.5807 0.3867 0.2977 -0.1420 0.1303  -0.0737 101 ASN A C   
871  O O   . ASN A 100 ? 0.5530 0.3737 0.2919 -0.1307 0.1220  -0.0715 101 ASN A O   
872  C CB  . ASN A 100 ? 0.5425 0.3184 0.2131 -0.1381 0.1047  -0.0560 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.6299 0.4140 0.3165 -0.1358 0.1062  -0.0544 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5216 0.3241 0.2357 -0.1366 0.1169  -0.0611 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.5642 0.3361 0.2357 -0.1320 0.0948  -0.0460 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5375 0.3511 0.2672 -0.1489 0.1454  -0.0823 102 ILE A N   
877  C CA  . ILE A 101 ? 0.5107 0.3524 0.2830 -0.1408 0.1504  -0.0887 102 ILE A CA  
878  C C   . ILE A 101 ? 0.5121 0.3642 0.3035 -0.1336 0.1518  -0.0931 102 ILE A C   
879  O O   . ILE A 101 ? 0.4668 0.3367 0.2872 -0.1207 0.1457  -0.0915 102 ILE A O   
880  C CB  . ILE A 101 ? 0.5548 0.4060 0.3396 -0.1499 0.1666  -0.0997 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5271 0.4100 0.3577 -0.1379 0.1668  -0.1053 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.5617 0.4013 0.3296 -0.1651 0.1844  -0.1108 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.5615 0.4590 0.4082 -0.1432 0.1752  -0.1129 102 ILE A CD1 
884  N N   . MET A 102 ? 0.5034 0.3425 0.2768 -0.1420 0.1598  -0.0986 103 MET A N   
885  C CA  . MET A 102 ? 0.5009 0.3467 0.2904 -0.1361 0.1622  -0.1034 103 MET A CA  
886  C C   . MET A 102 ? 0.5232 0.3695 0.3149 -0.1253 0.1463  -0.0938 103 MET A C   
887  O O   . MET A 102 ? 0.4914 0.3501 0.3089 -0.1146 0.1446  -0.0944 103 MET A O   
888  C CB  . MET A 102 ? 0.5642 0.3954 0.3326 -0.1489 0.1752  -0.1124 103 MET A CB  
889  C CG  . MET A 102 ? 0.6503 0.4836 0.4209 -0.1605 0.1940  -0.1247 103 MET A CG  
890  S SD  . MET A 102 ? 0.6989 0.5639 0.5212 -0.1502 0.2022  -0.1350 103 MET A SD  
891  C CE  . MET A 102 ? 0.6748 0.5433 0.5148 -0.1436 0.2088  -0.1438 103 MET A CE  
892  N N   . ALA A 103 ? 0.5066 0.3393 0.2713 -0.1277 0.1345  -0.0854 104 ALA A N   
893  C CA  . ALA A 103 ? 0.4998 0.3351 0.2670 -0.1189 0.1197  -0.0781 104 ALA A CA  
894  C C   . ALA A 103 ? 0.4924 0.3435 0.2846 -0.1070 0.1114  -0.0719 104 ALA A C   
895  O O   . ALA A 103 ? 0.4595 0.3189 0.2679 -0.0986 0.1061  -0.0697 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5357 0.3554 0.2706 -0.1233 0.1084  -0.0722 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4374 0.2915 0.2311 -0.1074 0.1110  -0.0694 105 VAL A N   
898  C CA  . VAL A 104 ? 0.3963 0.2657 0.2125 -0.0971 0.1036  -0.0643 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4234 0.3091 0.2703 -0.0892 0.1092  -0.0688 105 VAL A C   
900  O O   . VAL A 104 ? 0.3930 0.2867 0.2542 -0.0794 0.1013  -0.0641 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4363 0.3043 0.2463 -0.1006 0.1032  -0.0620 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.3948 0.2810 0.2305 -0.0910 0.0977  -0.0590 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.4576 0.3073 0.2375 -0.1041 0.0936  -0.0551 105 VAL A CG2 
904  N N   A MET A 105 ? 0.4007 0.2903 0.2568 -0.0932 0.1224  -0.0783 106 MET A N   
905  N N   B MET A 105 ? 0.4078 0.2975 0.2640 -0.0932 0.1224  -0.0783 106 MET A N   
906  C CA  A MET A 105 ? 0.3954 0.2999 0.2811 -0.0840 0.1271  -0.0838 106 MET A CA  
907  C CA  B MET A 105 ? 0.4098 0.3145 0.2958 -0.0836 0.1266  -0.0834 106 MET A CA  
908  C C   A MET A 105 ? 0.4467 0.3461 0.3357 -0.0773 0.1245  -0.0822 106 MET A C   
909  C C   B MET A 105 ? 0.4474 0.3466 0.3363 -0.0772 0.1243  -0.0820 106 MET A C   
910  O O   A MET A 105 ? 0.4275 0.3348 0.3345 -0.0658 0.1192  -0.0789 106 MET A O   
911  O O   B MET A 105 ? 0.4238 0.3308 0.3308 -0.0656 0.1192  -0.0788 106 MET A O   
912  C CB  A MET A 105 ? 0.4349 0.3449 0.3298 -0.0901 0.1425  -0.0965 106 MET A CB  
913  C CB  B MET A 105 ? 0.4433 0.3546 0.3401 -0.0890 0.1417  -0.0961 106 MET A CB  
914  C CG  A MET A 105 ? 0.4688 0.3967 0.3972 -0.0782 0.1453  -0.1028 106 MET A CG  
915  C CG  B MET A 105 ? 0.4694 0.3981 0.3995 -0.0765 0.1439  -0.1019 106 MET A CG  
916  S SD  A MET A 105 ? 0.5311 0.4681 0.4741 -0.0850 0.1643  -0.1206 106 MET A SD  
917  S SD  B MET A 105 ? 0.5180 0.4611 0.4671 -0.0824 0.1613  -0.1192 106 MET A SD  
918  C CE  A MET A 105 ? 0.4828 0.4329 0.4596 -0.0663 0.1625  -0.1248 106 MET A CE  
919  C CE  B MET A 105 ? 0.5110 0.4350 0.4421 -0.0923 0.1748  -0.1273 106 MET A CE  
920  N N   . ALA A 106 ? 0.4255 0.3100 0.2949 -0.0853 0.1284  -0.0846 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4371 0.3145 0.3068 -0.0818 0.1277  -0.0845 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4415 0.3199 0.3110 -0.0754 0.1143  -0.0746 107 ALA A C   
923  O O   . ALA A 106 ? 0.4129 0.2920 0.2949 -0.0672 0.1129  -0.0728 107 ALA A O   
924  C CB  . ALA A 106 ? 0.4662 0.3288 0.3122 -0.0936 0.1334  -0.0895 107 ALA A CB  
925  N N   . THR A 107 ? 0.4049 0.2833 0.2610 -0.0785 0.1049  -0.0685 108 THR A N   
926  C CA  . THR A 107 ? 0.3913 0.2731 0.2488 -0.0732 0.0930  -0.0608 108 THR A CA  
927  C C   . THR A 107 ? 0.4003 0.2940 0.2790 -0.0626 0.0898  -0.0566 108 THR A C   
928  O O   . THR A 107 ? 0.3647 0.2589 0.2498 -0.0568 0.0857  -0.0529 108 THR A O   
929  C CB  . THR A 107 ? 0.4321 0.3107 0.2708 -0.0779 0.0835  -0.0566 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4375 0.3040 0.2543 -0.0873 0.0862  -0.0608 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4174 0.3007 0.2585 -0.0735 0.0724  -0.0516 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3625 0.2652 0.2506 -0.0609 0.0920  -0.0577 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3365 0.2521 0.2442 -0.0510 0.0880  -0.0547 109 ALA A CA  
934  C C   . ALA A 108 ? 0.3696 0.2855 0.2924 -0.0421 0.0917  -0.0569 109 ALA A C   
935  O O   . ALA A 108 ? 0.3535 0.2723 0.2842 -0.0333 0.0854  -0.0515 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3392 0.2656 0.2541 -0.0527 0.0905  -0.0577 109 ALA A CB  
937  N N   . MET A 109 ? 0.3490 0.2591 0.2733 -0.0443 0.1018  -0.0646 110 MET A N   
938  C CA  . MET A 109 ? 0.3433 0.2499 0.2805 -0.0347 0.1051  -0.0668 110 MET A CA  
939  C C   . MET A 109 ? 0.3873 0.2797 0.3145 -0.0332 0.1012  -0.0607 110 MET A C   
940  O O   . MET A 109 ? 0.3817 0.2713 0.3156 -0.0233 0.0973  -0.0561 110 MET A O   
941  C CB  . MET A 109 ? 0.3829 0.2856 0.3234 -0.0384 0.1178  -0.0777 110 MET A CB  
942  C CG  . MET A 109 ? 0.4355 0.3543 0.3917 -0.0384 0.1235  -0.0859 110 MET A CG  
943  S SD  . MET A 109 ? 0.5385 0.4521 0.4940 -0.0472 0.1406  -0.1003 110 MET A SD  
944  C CE  . MET A 109 ? 0.5102 0.4171 0.4826 -0.0324 0.1428  -0.1032 110 MET A CE  
945  N N   . TYR A 110 ? 0.3628 0.2465 0.2725 -0.0435 0.1018  -0.0608 111 TYR A N   
946  C CA  . TYR A 110 ? 0.3642 0.2367 0.2643 -0.0454 0.0993  -0.0574 111 TYR A CA  
947  C C   . TYR A 110 ? 0.3990 0.2773 0.3010 -0.0406 0.0894  -0.0489 111 TYR A C   
948  O O   . TYR A 110 ? 0.3803 0.2502 0.2823 -0.0363 0.0886  -0.0452 111 TYR A O   
949  C CB  . TYR A 110 ? 0.3803 0.2484 0.2632 -0.0577 0.0998  -0.0607 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.3890 0.2511 0.2633 -0.0619 0.0963  -0.0591 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4351 0.2836 0.3073 -0.0634 0.1032  -0.0624 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.3792 0.2493 0.2479 -0.0650 0.0868  -0.0556 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.4072 0.2511 0.2719 -0.0694 0.1015  -0.0626 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.3802 0.2484 0.2437 -0.0700 0.0843  -0.0565 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4252 0.2808 0.2866 -0.0730 0.0921  -0.0604 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4133 0.2684 0.2701 -0.0799 0.0908  -0.0630 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3569 0.2475 0.2591 -0.0418 0.0826  -0.0460 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3301 0.2275 0.2341 -0.0383 0.0737  -0.0390 112 LEU A CA  
959  C C   . LEU A 111 ? 0.3661 0.2690 0.2829 -0.0274 0.0713  -0.0353 112 LEU A C   
960  O O   . LEU A 111 ? 0.3567 0.2628 0.2737 -0.0241 0.0649  -0.0296 112 LEU A O   
961  C CB  . LEU A 111 ? 0.3182 0.2246 0.2170 -0.0430 0.0675  -0.0378 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3512 0.2533 0.2357 -0.0517 0.0656  -0.0403 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.3476 0.2562 0.2268 -0.0533 0.0579  -0.0380 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.3854 0.2844 0.2671 -0.0537 0.0635  -0.0400 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3290 0.2339 0.2566 -0.0218 0.0760  -0.0393 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3228 0.2351 0.2643 -0.0099 0.0722  -0.0371 113 GLN A CA  
967  C C   . GLN A 112 ? 0.3610 0.2901 0.3078 -0.0096 0.0651  -0.0346 113 GLN A C   
968  O O   . GLN A 112 ? 0.3501 0.2822 0.2968 -0.0048 0.0579  -0.0286 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3354 0.2338 0.2724 -0.0024 0.0696  -0.0311 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.3806 0.2596 0.3123 -0.0023 0.0777  -0.0342 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.5198 0.3801 0.4402 0.0009  0.0763  -0.0275 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.4494 0.3101 0.3690 0.0081  0.0693  -0.0209 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.4911 0.3332 0.4003 -0.0055 0.0835  -0.0295 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3222 0.2604 0.2713 -0.0161 0.0682  -0.0398 114 MET A N   
975  C CA  . MET A 113 ? 0.3114 0.2637 0.2646 -0.0179 0.0637  -0.0392 114 MET A CA  
976  C C   . MET A 113 ? 0.3727 0.3385 0.3426 -0.0156 0.0687  -0.0472 114 MET A C   
977  O O   . MET A 113 ? 0.3434 0.3102 0.3116 -0.0240 0.0762  -0.0537 114 MET A O   
978  C CB  . MET A 113 ? 0.3296 0.2767 0.2673 -0.0287 0.0638  -0.0386 114 MET A CB  
979  C CG  . MET A 113 ? 0.3497 0.2885 0.2756 -0.0301 0.0582  -0.0328 114 MET A CG  
980  S SD  . MET A 113 ? 0.3923 0.3251 0.3009 -0.0400 0.0561  -0.0330 114 MET A SD  
981  C CE  . MET A 113 ? 0.3512 0.2948 0.2637 -0.0392 0.0503  -0.0306 114 MET A CE  
982  N N   . GLU A 114 ? 0.3608 0.3359 0.3463 -0.0040 0.0647  -0.0475 115 GLU A N   
983  C CA  . GLU A 114 ? 0.3692 0.3602 0.3761 0.0014  0.0683  -0.0568 115 GLU A CA  
984  C C   . GLU A 114 ? 0.3657 0.3732 0.3802 -0.0071 0.0722  -0.0641 115 GLU A C   
985  O O   . GLU A 114 ? 0.3491 0.3639 0.3743 -0.0105 0.0814  -0.0745 115 GLU A O   
986  C CB  . GLU A 114 ? 0.3978 0.3971 0.4186 0.0170  0.0593  -0.0546 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.5815 0.5607 0.5940 0.0258  0.0575  -0.0485 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3251 0.3377 0.3341 -0.0111 0.0664  -0.0598 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3395 0.3650 0.3540 -0.0203 0.0711  -0.0670 116 HIS A CA  
990  C C   . HIS A 115 ? 0.3662 0.3782 0.3645 -0.0343 0.0816  -0.0704 116 HIS A C   
991  O O   . HIS A 115 ? 0.3687 0.3887 0.3738 -0.0421 0.0911  -0.0803 116 HIS A O   
992  C CB  . HIS A 115 ? 0.3603 0.3921 0.3717 -0.0211 0.0628  -0.0620 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.4159 0.4626 0.4422 -0.0086 0.0528  -0.0602 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4508 0.5190 0.5009 -0.0019 0.0525  -0.0694 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4452 0.4881 0.4643 -0.0023 0.0426  -0.0509 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4437 0.5191 0.4987 0.0093  0.0409  -0.0644 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4463 0.5058 0.4817 0.0087  0.0354  -0.0531 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.3049 0.2966 0.2814 -0.0378 0.0802  -0.0629 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3143 0.2903 0.2711 -0.0500 0.0882  -0.0649 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.3886 0.3648 0.3525 -0.0520 0.0995  -0.0744 117 VAL A C   
1001 O O   . VAL A 116 ? 0.3760 0.3505 0.3349 -0.0628 0.1100  -0.0820 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.3652 0.3226 0.2993 -0.0521 0.0823  -0.0561 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.3798 0.3207 0.2922 -0.0636 0.0895  -0.0588 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3591 0.3171 0.2872 -0.0511 0.0726  -0.0490 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3409 0.3177 0.3156 -0.0418 0.0983  -0.0744 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3438 0.3209 0.3278 -0.0418 0.1091  -0.0842 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.3991 0.3970 0.4049 -0.0436 0.1169  -0.0967 118 VAL A C   
1008 O O   . VAL A 117 ? 0.3851 0.3814 0.3885 -0.0538 0.1297  -0.1064 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.3732 0.3458 0.3660 -0.0288 0.1057  -0.0819 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.3792 0.3523 0.3836 -0.0279 0.1173  -0.0934 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.3725 0.3253 0.3438 -0.0303 0.1006  -0.0720 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.3674 0.3849 0.3927 -0.0353 0.1095  -0.0970 119 ASP A N   
1013 N N   B ASP A 118 ? 0.3654 0.3833 0.3921 -0.0344 0.1095  -0.0973 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.3687 0.4110 0.4184 -0.0363 0.1149  -0.1098 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.3672 0.4103 0.4192 -0.0347 0.1148  -0.1102 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.4031 0.4437 0.4411 -0.0549 0.1262  -0.1162 119 ASP A C   
1017 C C   B ASP A 118 ? 0.4160 0.4589 0.4580 -0.0531 0.1263  -0.1174 119 ASP A C   
1018 O O   A ASP A 118 ? 0.4031 0.4536 0.4529 -0.0619 0.1393  -0.1301 119 ASP A O   
1019 O O   B ASP A 118 ? 0.4191 0.4731 0.4743 -0.0595 0.1390  -0.1315 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.3832 0.4448 0.4505 -0.0247 0.1021  -0.1069 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.3805 0.4428 0.4497 -0.0232 0.1018  -0.1072 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.5243 0.6161 0.6210 -0.0243 0.1059  -0.1215 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.5158 0.5838 0.6015 -0.0038 0.0922  -0.1048 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.5487 0.6533 0.6675 -0.0180 0.1113  -0.1329 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.5466 0.6128 0.6423 0.0022  0.0977  -0.1111 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.5832 0.6865 0.6817 -0.0302 0.1035  -0.1226 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.6011 0.6740 0.6884 0.0054  0.0792  -0.0969 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.3516 0.3783 0.3658 -0.0631 0.1220  -0.1069 120 THR A N   
1029 N N   B THR A 119 ? 0.3684 0.3972 0.3862 -0.0617 0.1225  -0.1082 120 THR A N   
1030 C CA  A THR A 119 ? 0.3638 0.3831 0.3619 -0.0808 0.1327  -0.1119 120 THR A CA  
1031 C CA  B THR A 119 ? 0.3795 0.4015 0.3816 -0.0792 0.1326  -0.1128 120 THR A CA  
1032 C C   A THR A 119 ? 0.4186 0.4173 0.3949 -0.0923 0.1447  -0.1150 120 THR A C   
1033 C C   B THR A 119 ? 0.4306 0.4316 0.4103 -0.0912 0.1449  -0.1159 120 THR A C   
1034 O O   A THR A 119 ? 0.4184 0.4150 0.3882 -0.1068 0.1583  -0.1245 120 THR A O   
1035 O O   B THR A 119 ? 0.4349 0.4364 0.4114 -0.1050 0.1588  -0.1265 120 THR A O   
1036 C CB  A THR A 119 ? 0.3760 0.3844 0.3547 -0.0853 0.1250  -0.1020 120 THR A CB  
1037 C CB  B THR A 119 ? 0.4542 0.4662 0.4381 -0.0823 0.1237  -0.1022 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.3991 0.4025 0.3666 -0.1018 0.1366  -0.1091 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4225 0.4520 0.4253 -0.0694 0.1112  -0.0981 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.3213 0.3038 0.2713 -0.0844 0.1170  -0.0884 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.4569 0.4664 0.4313 -0.0982 0.1335  -0.1086 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.3897 0.3728 0.3535 -0.0870 0.1404  -0.1078 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.4120 0.3753 0.3537 -0.0974 0.1506  -0.1108 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.4692 0.4463 0.4319 -0.0997 0.1652  -0.1266 121 CYS A C   
1045 O O   . CYS A 120 ? 0.4631 0.4322 0.4124 -0.1149 0.1795  -0.1352 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.4176 0.3654 0.3459 -0.0906 0.1422  -0.1012 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.4622 0.3909 0.3607 -0.0919 0.1281  -0.0857 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4240 0.4213 0.4191 -0.0845 0.1615  -0.1309 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4275 0.4245 0.4223 -0.0846 0.1616  -0.1309 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4306 0.4451 0.4526 -0.0824 0.1733  -0.1471 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4355 0.4492 0.4564 -0.0831 0.1739  -0.1473 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.4742 0.5063 0.5084 -0.0947 0.1857  -0.1613 122 ARG A C   
1053 C C   B ARG A 121 ? 0.4752 0.5073 0.5093 -0.0948 0.1859  -0.1614 122 ARG A C   
1054 O O   A ARG A 121 ? 0.4764 0.5111 0.5141 -0.1050 0.2022  -0.1755 122 ARG A O   
1055 O O   B ARG A 121 ? 0.4756 0.5107 0.5137 -0.1052 0.2024  -0.1758 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4264 0.4592 0.4804 -0.0611 0.1631  -0.1473 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.4390 0.4693 0.4909 -0.0620 0.1644  -0.1476 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.5942 0.6089 0.6391 -0.0502 0.1557  -0.1374 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6257 0.6374 0.6688 -0.0537 0.1616  -0.1416 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7407 0.7689 0.8152 -0.0304 0.1501  -0.1409 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.7538 0.7793 0.8281 -0.0349 0.1585  -0.1474 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.8154 0.8232 0.8777 -0.0204 0.1416  -0.1291 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.8021 0.8365 0.8874 -0.0192 0.1417  -0.1376 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 0.9642 0.9545 1.0179 -0.0211 0.1486  -0.1311 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 0.9249 0.9448 1.0033 -0.0069 0.1310  -0.1259 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.8489 0.8397 0.9049 -0.0306 0.1640  -0.1445 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.7333 0.7304 0.7960 -0.0083 0.1354  -0.1231 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.7404 0.7121 0.7825 -0.0134 0.1412  -0.1206 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.7228 0.7502 0.8086 0.0057  0.1166  -0.1176 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4219 0.4658 0.4618 -0.0948 0.1786  -0.1583 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4318 0.4932 0.4835 -0.1073 0.1896  -0.1717 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.4965 0.5334 0.5130 -0.1303 0.2041  -0.1733 123 LYS A C   
1073 O O   . LYS A 122 ? 0.4880 0.5334 0.5114 -0.1440 0.2217  -0.1894 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.4476 0.5260 0.5124 -0.1013 0.1773  -0.1673 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.6564 0.7642 0.7597 -0.0805 0.1660  -0.1710 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.8031 0.9279 0.9178 -0.0746 0.1532  -0.1670 123 LYS A CD  
1077 C CE  . LYS A 122 ? 0.9613 1.1096 1.1074 -0.0523 0.1395  -0.1680 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.1041 1.2833 1.2751 -0.0495 0.1332  -0.1757 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.4565 0.4624 0.4346 -0.1344 0.1969  -0.1571 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.4834 0.4599 0.4215 -0.1544 0.2078  -0.1559 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.5488 0.5139 0.4753 -0.1633 0.2222  -0.1643 124 PHE A C   
1082 O O   . PHE A 123 ? 0.5443 0.4977 0.4519 -0.1824 0.2389  -0.1731 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.5051 0.4534 0.4082 -0.1526 0.1935  -0.1368 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.5149 0.4624 0.4132 -0.1543 0.1866  -0.1307 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.5263 0.5032 0.4587 -0.1448 0.1803  -0.1341 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.5671 0.4830 0.4255 -0.1639 0.1847  -0.1210 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.5374 0.5131 0.4649 -0.1471 0.1746  -0.1293 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.5856 0.4988 0.4394 -0.1649 0.1786  -0.1156 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.5314 0.4748 0.4200 -0.1571 0.1741  -0.1201 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.4939 0.4620 0.4317 -0.1504 0.2171  -0.1628 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5156 0.4747 0.4457 -0.1577 0.2310  -0.1722 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.5874 0.5721 0.5491 -0.1635 0.2492  -0.1941 125 ILE A C   
1093 O O   . ILE A 124 ? 0.6042 0.5786 0.5494 -0.1815 0.2675  -0.2050 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.5427 0.4955 0.4747 -0.1431 0.2211  -0.1648 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.5507 0.4757 0.4451 -0.1437 0.2077  -0.1469 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.5710 0.5206 0.5044 -0.1489 0.2368  -0.1781 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.6016 0.5251 0.5023 -0.1279 0.1938  -0.1374 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.5401 0.5585 0.5463 -0.1489 0.2439  -0.2011 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.5494 0.5990 0.5933 -0.1511 0.2586  -0.2235 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.6074 0.6585 0.6416 -0.1745 0.2758  -0.2352 126 LYS A C   
1101 O O   . LYS A 125 ? 0.6021 0.6657 0.6498 -0.1860 0.2954  -0.2549 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.5651 0.6493 0.6550 -0.1293 0.2453  -0.2265 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.5565 0.5932 0.5659 -0.1822 0.2696  -0.2236 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.5795 0.6112 0.5736 -0.2055 0.2857  -0.2326 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.6806 0.6780 0.6307 -0.2278 0.3037  -0.2349 127 ALA A C   
1106 O O   . ALA A 126 ? 0.6918 0.6903 0.6373 -0.2486 0.3241  -0.2501 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.5770 0.5978 0.5538 -0.2059 0.2730  -0.2181 127 ALA A CB  
1108 N N   . SER A 127 ? 0.6770 0.6436 0.5932 -0.2247 0.2963  -0.2205 128 SER A N   
1109 C CA  . SER A 127 ? 0.7381 0.6689 0.6069 -0.2445 0.3100  -0.2204 128 SER A CA  
1110 C C   . SER A 127 ? 0.8419 0.7789 0.7204 -0.2500 0.3271  -0.2368 128 SER A C   
1111 O O   . SER A 127 ? 0.8938 0.8038 0.7342 -0.2696 0.3422  -0.2404 128 SER A O   
1112 C CB  . SER A 127 ? 0.8125 0.7072 0.6377 -0.2397 0.2928  -0.1977 128 SER A CB  
1113 O OG  . SER A 127 ? 0.9657 0.8382 0.7600 -0.2476 0.2877  -0.1865 128 SER A OG  
1114 N N   . GLU A 128 ? 0.7709 0.7419 0.6985 -0.2330 0.3252  -0.2472 129 GLU A N   
1115 C CA  . GLU A 128 ? 0.9899 0.9690 0.9318 -0.2358 0.3412  -0.2641 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.5285 1.5291 1.4912 -0.2534 0.3668  -0.2900 129 GLU A C   
1117 O O   . GLU A 128 ? 1.1295 1.1267 1.0791 -0.2707 0.3761  -0.2936 129 GLU A O   
1118 C CB  . GLU A 128 ? 0.9755 0.9764 0.9574 -0.2094 0.3282  -0.2639 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.0660 1.1107 1.1053 -0.1938 0.3247  -0.2760 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.3094 1.3701 1.3826 -0.1658 0.3084  -0.2721 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.2136 1.2515 1.2656 -0.1559 0.2945  -0.2545 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.2018 1.2978 1.3226 -0.1535 0.3095  -0.2871 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.2237 0.4479 0.2711 -0.0263 -0.0185 -0.0957 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2383 0.4625 0.2857 -0.0263 -0.0185 -0.0957 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.2084 0.4312 0.2550 -0.0259 -0.0185 -0.0970 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2336 0.4565 0.2803 -0.0259 -0.0185 -0.0970 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2661 0.4891 0.3141 -0.0261 -0.0189 -0.0971 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2684 0.4917 0.3165 -0.0262 -0.0188 -0.0970 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2636 0.4862 0.3127 -0.0264 -0.0195 -0.0966 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2591 0.4824 0.3084 -0.0266 -0.0193 -0.0965 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.1976 0.4183 0.2431 -0.0254 -0.0193 -0.0977 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.2274 0.4481 0.2729 -0.0253 -0.0193 -0.0977 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.2008 0.4211 0.2442 -0.0252 -0.0190 -0.0983 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2432 0.4636 0.2906 -0.0254 -0.0204 -0.0978 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2337 0.4537 0.2769 -0.0253 -0.0195 -0.0981 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.2827 0.5027 0.3318 -0.0256 -0.0212 -0.0978 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.1941 0.4142 0.2356 -0.0248 -0.0181 -0.0994 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2439 0.4649 0.2924 -0.0250 -0.0208 -0.0983 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2260 0.4458 0.2664 -0.0249 -0.0189 -0.0993 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.2772 0.4979 0.3291 -0.0255 -0.0219 -0.0987 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2344 0.4541 0.2738 -0.0246 -0.0180 -0.1003 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.2943 0.5160 0.3456 -0.0251 -0.0215 -0.0991 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.2005 0.4205 0.2424 -0.0245 -0.0173 -0.0998 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2554 0.4771 0.3035 -0.0246 -0.0204 -0.0984 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2288 0.4482 0.2659 -0.0243 -0.0171 -0.1020 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.2843 0.5080 0.3376 -0.0246 -0.0216 -0.1003 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.2138 0.4334 0.2543 -0.0241 -0.0163 -0.1010 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.2760 0.4991 0.3252 -0.0240 -0.0206 -0.0991 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2214 0.4407 0.2592 -0.0241 -0.0161 -0.1023 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.2815 0.5059 0.3332 -0.0240 -0.0212 -0.1003 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.2137 0.4372 0.2620 -0.0259 -0.0185 -0.0978 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.2123 0.4362 0.2616 -0.0260 -0.0189 -0.0983 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2405 0.4634 0.2898 -0.0250 -0.0188 -0.0985 2   VAL D C   
1157 O O   . VAL B 3   ? 0.2224 0.4446 0.2714 -0.0246 -0.0183 -0.0982 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2481 0.4751 0.2990 -0.0270 -0.0187 -0.0989 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2426 0.4719 0.2939 -0.0280 -0.0187 -0.0980 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2392 0.4681 0.2920 -0.0269 -0.0178 -0.0999 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.2051 0.4282 0.2547 -0.0248 -0.0192 -0.0989 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.1955 0.4185 0.2457 -0.0238 -0.0191 -0.0986 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2487 0.4725 0.3014 -0.0244 -0.0188 -0.0995 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2440 0.4692 0.2973 -0.0252 -0.0194 -0.1007 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.2153 0.4390 0.2648 -0.0230 -0.0196 -0.0991 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.1920 0.4167 0.2408 -0.0225 -0.0198 -0.0993 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2388 0.4631 0.2893 -0.0218 -0.0194 -0.0982 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.2570 0.4824 0.3056 -0.0219 -0.0199 -0.0981 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2445 0.4683 0.2995 -0.0242 -0.0180 -0.0992 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2508 0.4766 0.3102 -0.0249 -0.0177 -0.1008 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.2879 0.5137 0.3496 -0.0245 -0.0183 -0.1011 4   PRO D C   
1172 O O   . PRO B 5   ? 0.2701 0.4942 0.3306 -0.0233 -0.0185 -0.0994 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.2716 0.4973 0.3335 -0.0245 -0.0162 -0.1006 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.3267 0.5495 0.3856 -0.0234 -0.0162 -0.0982 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.2764 0.4989 0.3309 -0.0234 -0.0173 -0.0978 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.2786 0.5073 0.3439 -0.0256 -0.0188 -0.1035 5   ALA D N   
# 
