data_7GV2
# 
_entry.id   7GV2 
# 
_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   7GV2         pdb_00007gv2 10.2210/pdb7gv2/pdb 
WWPDB D_1001406673 ?            ?                   
# 
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                        7GV2 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              Rob.vanMontfort@icr.ac.uk 
_pdbx_contact_author.name_first         Rob 
_pdbx_contact_author.name_last          'van Montfort' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodrigues, M.J.'      1 0000-0003-1243-903X 
'Le Bihan, Y.V.'       2 0000-0002-6850-9706 
'van Montfort, R.L.M.' 3 0000-0002-5688-3450 
# 
_citation.id                        primary 
_citation.title                     
'Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.' 
_citation.journal_abbrev            J.Appl.Crystallogr. 
_citation.journal_volume            57 
_citation.page_first                1951 
_citation.page_last                 1965 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39628887 
_citation.pdbx_database_id_DOI      10.1107/S1600576724010549 
_citation.journal_id_ASTM           JACGAR 
_citation.country                   DK 
_citation.journal_id_ISSN           0021-8898 
_citation.journal_id_CSD            0228 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodrigues, M.J.'      1 0000-0003-1243-903X 
primary 'Cabry, M.'            2 0000-0002-9070-5498 
primary 'Collie, G.'           3 0000-0002-0406-922X 
primary 'Carter, M.'           4 ?                   
primary 'McAndrew, C.'         5 0000-0002-1366-088X 
primary 'Owen, R.L.'           6 0000-0002-2104-7057 
primary 'Bellenie, B.R.'       7 0000-0001-9987-3079 
primary 'Le Bihan, Y.V.'       8 0000-0002-6850-9706 
primary 'van Montfort, R.L.M.' 9 0000-0002-5688-3450 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'B-cell lymphoma 6 protein'                                            14536.915 1   ? ? ? ? 
2 polymer     syn 'WVIP tetrapeptide'                                                    610.744   1   ? ? ? ? 
3 non-polymer syn '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' 339.575   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                         35.453    1   ? ? ? ? 
5 non-polymer nat 'DIMETHYL SULFOXIDE'                                                   78.133    1   ? ? ? ? 
6 water       nat water                                                                  18.015    185 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'BCL-6,B-cell lymphoma 5 protein,BCL-5,Protein LAZ-3,Zinc finger and BTB domain-containing protein 27,Zinc finger protein 51' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
A ? 
2 'polypeptide(L)' no yes '(ACE)WVIPA' XWVIPA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' A1ACA 
4 'CHLORIDE ION'                                                         CL    
5 'DIMETHYL SULFOXIDE'                                                   DMS   
6 water                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   ALA n 
1 5   ASP n 
1 6   SER n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  PHE n 
1 11  THR n 
1 12  ARG n 
1 13  HIS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  LEU n 
1 19  LEU n 
1 20  ASN n 
1 21  LEU n 
1 22  ASN n 
1 23  ARG n 
1 24  LEU n 
1 25  ARG n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  THR n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  ILE n 
1 36  VAL n 
1 37  VAL n 
1 38  SER n 
1 39  ARG n 
1 40  GLU n 
1 41  GLN n 
1 42  PHE n 
1 43  ARG n 
1 44  ALA n 
1 45  HIS n 
1 46  LYS n 
1 47  THR n 
1 48  VAL n 
1 49  LEU n 
1 50  MET n 
1 51  ALA n 
1 52  CYS n 
1 53  SER n 
1 54  GLY n 
1 55  LEU n 
1 56  PHE n 
1 57  TYR n 
1 58  SER n 
1 59  ILE n 
1 60  PHE n 
1 61  THR n 
1 62  ASP n 
1 63  GLN n 
1 64  LEU n 
1 65  LYS n 
1 66  CYS n 
1 67  ASN n 
1 68  LEU n 
1 69  SER n 
1 70  VAL n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ASP n 
1 75  PRO n 
1 76  GLU n 
1 77  ILE n 
1 78  ASN n 
1 79  PRO n 
1 80  GLU n 
1 81  GLY n 
1 82  PHE n 
1 83  CYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  ASP n 
1 88  PHE n 
1 89  MET n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ARG n 
1 94  LEU n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLU n 
1 99  GLY n 
1 100 ASN n 
1 101 ILE n 
1 102 MET n 
1 103 ALA n 
1 104 VAL n 
1 105 MET n 
1 106 ALA n 
1 107 THR n 
1 108 ALA n 
1 109 MET n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 MET n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 VAL n 
1 118 ASP n 
1 119 THR n 
1 120 CYS n 
1 121 ARG n 
1 122 LYS n 
1 123 PHE n 
1 124 ILE n 
1 125 LYS n 
1 126 ALA n 
1 127 SER n 
1 128 GLU n 
2 1   ACE n 
2 2   TRP n 
2 3   VAL n 
2 4   ILE n 
2 5   PRO n 
2 6   ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCL6, BCL5, LAZ3, ZBTB27, ZNF51' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21-AI 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET48b 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 6 'synthetic construct' ? 32630 ? 
3 2 sample ? ? 'synthetic construct' ? 32630 ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ACA non-polymer         . '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' ? 'C12 H8 Br Cl N4 O' 339.575 
ACE   non-polymer         . 'ACETYL GROUP'                                                         ? 'C2 H4 O'           44.053  
ALA   'L-peptide linking' y ALANINE                                                                ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE                                                               ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                             ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                        ? 'C4 H7 N O4'        133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                         ? 'Cl -1'             35.453  
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'      121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                   ? 'C2 H6 O S'         78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                  ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                                             ? 'C5 H11 N O2 S'     149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                                                                ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE                                                                 ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE                                                              ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                             ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE                                                               ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE                                                                 ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLY 3   4   ?   ?   ?   A . n 
A 1 4   ALA 4   5   ?   ?   ?   A . n 
A 1 5   ASP 5   6   6   ASP ASP A . n 
A 1 6   SER 6   7   7   SER SER A . n 
A 1 7   CYS 7   8   8   CYS CYS A . n 
A 1 8   ILE 8   9   9   ILE ILE A . n 
A 1 9   GLN 9   10  10  GLN GLN A . n 
A 1 10  PHE 10  11  11  PHE PHE A . n 
A 1 11  THR 11  12  12  THR THR A . n 
A 1 12  ARG 12  13  13  ARG ARG A . n 
A 1 13  HIS 13  14  14  HIS HIS A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ASP 16  17  17  ASP ASP A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  ASN 20  21  21  ASN ASN A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  ARG 23  24  24  ARG ARG A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  ARG 25  26  26  ARG ARG A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  THR 31  32  32  THR THR A . n 
A 1 32  ASP 32  33  33  ASP ASP A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  VAL 36  37  37  VAL VAL A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  SER 38  39  39  SER SER A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLN 41  42  42  GLN GLN A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  ALA 44  45  45  ALA ALA A . n 
A 1 45  HIS 45  46  46  HIS HIS A . n 
A 1 46  LYS 46  47  47  LYS LYS A . n 
A 1 47  THR 47  48  48  THR THR A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  MET 50  51  51  MET MET A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  CYS 52  53  53  CYS CYS A . n 
A 1 53  SER 53  54  54  SER SER A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  PHE 60  61  61  PHE PHE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  ASN 67  68  68  ASN ASN A . n 
A 1 68  LEU 68  69  69  LEU LEU A . n 
A 1 69  SER 69  70  70  SER SER A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ILE 71  72  72  ILE ILE A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  ASP 74  75  75  ASP ASP A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLU 76  77  77  GLU GLU A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  PRO 79  80  80  PRO PRO A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  CYS 83  84  84  CYS CYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  LEU 85  86  86  LEU LEU A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  PHE 88  89  89  PHE PHE A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  ASN 95  96  96  ASN ASN A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ARG 97  98  98  ARG ARG A . n 
A 1 98  GLU 98  99  99  GLU GLU A . n 
A 1 99  GLY 99  100 100 GLY GLY A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 MET 102 103 103 MET MET A . n 
A 1 103 ALA 103 104 104 ALA ALA A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 MET 105 106 106 MET MET A . n 
A 1 106 ALA 106 107 107 ALA ALA A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 MET 109 110 110 MET MET A . n 
A 1 110 TYR 110 111 111 TYR TYR A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLN 112 113 113 GLN GLN A . n 
A 1 113 MET 113 114 114 MET MET A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 HIS 115 116 116 HIS HIS A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 VAL 117 118 118 VAL VAL A . n 
A 1 118 ASP 118 119 119 ASP ASP A . n 
A 1 119 THR 119 120 120 THR THR A . n 
A 1 120 CYS 120 121 121 CYS CYS A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 PHE 123 124 124 PHE PHE A . n 
A 1 124 ILE 124 125 125 ILE ILE A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 SER 127 128 128 SER SER A . n 
A 1 128 GLU 128 129 129 GLU GLU A . n 
B 2 1   ACE 1   0   0   ACE ACE D . n 
B 2 2   TRP 2   1   1   TRP TRP D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ILE 4   3   3   ILE ILE D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   ALA 6   5   5   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1ACA 1   201 1   A1ACA 763 A . 
D 4 CL    1   202 1   CL    CL  A . 
E 5 DMS   1   101 1   DMS   DMS D . 
F 6 HOH   1   301 178 HOH   HOH A . 
F 6 HOH   2   302 7   HOH   HOH A . 
F 6 HOH   3   303 94  HOH   HOH A . 
F 6 HOH   4   304 166 HOH   HOH A . 
F 6 HOH   5   305 19  HOH   HOH A . 
F 6 HOH   6   306 173 HOH   HOH A . 
F 6 HOH   7   307 29  HOH   HOH A . 
F 6 HOH   8   308 45  HOH   HOH A . 
F 6 HOH   9   309 47  HOH   HOH A . 
F 6 HOH   10  310 106 HOH   HOH A . 
F 6 HOH   11  311 90  HOH   HOH A . 
F 6 HOH   12  312 140 HOH   HOH A . 
F 6 HOH   13  313 100 HOH   HOH A . 
F 6 HOH   14  314 202 HOH   HOH A . 
F 6 HOH   15  315 139 HOH   HOH A . 
F 6 HOH   16  316 40  HOH   HOH A . 
F 6 HOH   17  317 179 HOH   HOH A . 
F 6 HOH   18  318 101 HOH   HOH A . 
F 6 HOH   19  319 99  HOH   HOH A . 
F 6 HOH   20  320 142 HOH   HOH A . 
F 6 HOH   21  321 247 HOH   HOH A . 
F 6 HOH   22  322 83  HOH   HOH A . 
F 6 HOH   23  323 87  HOH   HOH A . 
F 6 HOH   24  324 132 HOH   HOH A . 
F 6 HOH   25  325 6   HOH   HOH A . 
F 6 HOH   26  326 91  HOH   HOH A . 
F 6 HOH   27  327 119 HOH   HOH A . 
F 6 HOH   28  328 75  HOH   HOH A . 
F 6 HOH   29  329 37  HOH   HOH A . 
F 6 HOH   30  330 84  HOH   HOH A . 
F 6 HOH   31  331 193 HOH   HOH A . 
F 6 HOH   32  332 14  HOH   HOH A . 
F 6 HOH   33  333 237 HOH   HOH A . 
F 6 HOH   34  334 196 HOH   HOH A . 
F 6 HOH   35  335 27  HOH   HOH A . 
F 6 HOH   36  336 239 HOH   HOH A . 
F 6 HOH   37  337 42  HOH   HOH A . 
F 6 HOH   38  338 17  HOH   HOH A . 
F 6 HOH   39  339 242 HOH   HOH A . 
F 6 HOH   40  340 244 HOH   HOH A . 
F 6 HOH   41  341 243 HOH   HOH A . 
F 6 HOH   42  342 50  HOH   HOH A . 
F 6 HOH   43  343 145 HOH   HOH A . 
F 6 HOH   44  344 117 HOH   HOH A . 
F 6 HOH   45  345 44  HOH   HOH A . 
F 6 HOH   46  346 5   HOH   HOH A . 
F 6 HOH   47  347 20  HOH   HOH A . 
F 6 HOH   48  348 151 HOH   HOH A . 
F 6 HOH   49  349 4   HOH   HOH A . 
F 6 HOH   50  350 86  HOH   HOH A . 
F 6 HOH   51  351 15  HOH   HOH A . 
F 6 HOH   52  352 30  HOH   HOH A . 
F 6 HOH   53  353 34  HOH   HOH A . 
F 6 HOH   54  354 93  HOH   HOH A . 
F 6 HOH   55  355 96  HOH   HOH A . 
F 6 HOH   56  356 124 HOH   HOH A . 
F 6 HOH   57  357 97  HOH   HOH A . 
F 6 HOH   58  358 122 HOH   HOH A . 
F 6 HOH   59  359 144 HOH   HOH A . 
F 6 HOH   60  360 175 HOH   HOH A . 
F 6 HOH   61  361 85  HOH   HOH A . 
F 6 HOH   62  362 51  HOH   HOH A . 
F 6 HOH   63  363 141 HOH   HOH A . 
F 6 HOH   64  364 12  HOH   HOH A . 
F 6 HOH   65  365 89  HOH   HOH A . 
F 6 HOH   66  366 103 HOH   HOH A . 
F 6 HOH   67  367 207 HOH   HOH A . 
F 6 HOH   68  368 133 HOH   HOH A . 
F 6 HOH   69  369 24  HOH   HOH A . 
F 6 HOH   70  370 170 HOH   HOH A . 
F 6 HOH   71  371 192 HOH   HOH A . 
F 6 HOH   72  372 180 HOH   HOH A . 
F 6 HOH   73  373 245 HOH   HOH A . 
F 6 HOH   74  374 21  HOH   HOH A . 
F 6 HOH   75  375 25  HOH   HOH A . 
F 6 HOH   76  376 76  HOH   HOH A . 
F 6 HOH   77  377 131 HOH   HOH A . 
F 6 HOH   78  378 186 HOH   HOH A . 
F 6 HOH   79  379 39  HOH   HOH A . 
F 6 HOH   80  380 167 HOH   HOH A . 
F 6 HOH   81  381 229 HOH   HOH A . 
F 6 HOH   82  382 105 HOH   HOH A . 
F 6 HOH   83  383 108 HOH   HOH A . 
F 6 HOH   84  384 129 HOH   HOH A . 
F 6 HOH   85  385 16  HOH   HOH A . 
F 6 HOH   86  386 165 HOH   HOH A . 
F 6 HOH   87  387 169 HOH   HOH A . 
F 6 HOH   88  388 28  HOH   HOH A . 
F 6 HOH   89  389 212 HOH   HOH A . 
F 6 HOH   90  390 177 HOH   HOH A . 
F 6 HOH   91  391 191 HOH   HOH A . 
F 6 HOH   92  392 157 HOH   HOH A . 
F 6 HOH   93  393 70  HOH   HOH A . 
F 6 HOH   94  394 69  HOH   HOH A . 
F 6 HOH   95  395 74  HOH   HOH A . 
F 6 HOH   96  396 55  HOH   HOH A . 
F 6 HOH   97  397 32  HOH   HOH A . 
F 6 HOH   98  398 22  HOH   HOH A . 
F 6 HOH   99  399 194 HOH   HOH A . 
F 6 HOH   100 400 241 HOH   HOH A . 
F 6 HOH   101 401 64  HOH   HOH A . 
F 6 HOH   102 402 92  HOH   HOH A . 
F 6 HOH   103 403 205 HOH   HOH A . 
F 6 HOH   104 404 185 HOH   HOH A . 
F 6 HOH   105 405 26  HOH   HOH A . 
F 6 HOH   106 406 35  HOH   HOH A . 
F 6 HOH   107 407 43  HOH   HOH A . 
F 6 HOH   108 408 82  HOH   HOH A . 
F 6 HOH   109 409 174 HOH   HOH A . 
F 6 HOH   110 410 60  HOH   HOH A . 
F 6 HOH   111 411 190 HOH   HOH A . 
F 6 HOH   112 412 176 HOH   HOH A . 
F 6 HOH   113 413 46  HOH   HOH A . 
F 6 HOH   114 414 120 HOH   HOH A . 
F 6 HOH   115 415 67  HOH   HOH A . 
F 6 HOH   116 416 36  HOH   HOH A . 
F 6 HOH   117 417 204 HOH   HOH A . 
F 6 HOH   118 418 215 HOH   HOH A . 
F 6 HOH   119 419 236 HOH   HOH A . 
F 6 HOH   120 420 61  HOH   HOH A . 
F 6 HOH   121 421 88  HOH   HOH A . 
F 6 HOH   122 422 110 HOH   HOH A . 
F 6 HOH   123 423 65  HOH   HOH A . 
F 6 HOH   124 424 56  HOH   HOH A . 
F 6 HOH   125 425 57  HOH   HOH A . 
F 6 HOH   126 426 223 HOH   HOH A . 
F 6 HOH   127 427 147 HOH   HOH A . 
F 6 HOH   128 428 135 HOH   HOH A . 
F 6 HOH   129 429 68  HOH   HOH A . 
F 6 HOH   130 430 95  HOH   HOH A . 
F 6 HOH   131 431 116 HOH   HOH A . 
F 6 HOH   132 432 41  HOH   HOH A . 
F 6 HOH   133 433 168 HOH   HOH A . 
F 6 HOH   134 434 187 HOH   HOH A . 
F 6 HOH   135 435 227 HOH   HOH A . 
F 6 HOH   136 436 214 HOH   HOH A . 
F 6 HOH   137 437 200 HOH   HOH A . 
F 6 HOH   138 438 123 HOH   HOH A . 
F 6 HOH   139 439 248 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   143 443 225 HOH   HOH A . 
F 6 HOH   144 444 171 HOH   HOH A . 
F 6 HOH   145 445 71  HOH   HOH A . 
F 6 HOH   146 446 63  HOH   HOH A . 
F 6 HOH   147 447 220 HOH   HOH A . 
F 6 HOH   148 448 234 HOH   HOH A . 
F 6 HOH   149 449 203 HOH   HOH A . 
F 6 HOH   150 450 181 HOH   HOH A . 
F 6 HOH   151 451 158 HOH   HOH A . 
F 6 HOH   152 452 79  HOH   HOH A . 
F 6 HOH   153 453 238 HOH   HOH A . 
F 6 HOH   154 454 217 HOH   HOH A . 
F 6 HOH   155 455 125 HOH   HOH A . 
F 6 HOH   156 456 235 HOH   HOH A . 
F 6 HOH   157 457 114 HOH   HOH A . 
F 6 HOH   158 458 81  HOH   HOH A . 
F 6 HOH   159 459 246 HOH   HOH A . 
F 6 HOH   160 460 58  HOH   HOH A . 
F 6 HOH   161 461 216 HOH   HOH A . 
F 6 HOH   162 462 221 HOH   HOH A . 
F 6 HOH   163 463 115 HOH   HOH A . 
F 6 HOH   164 464 107 HOH   HOH A . 
F 6 HOH   165 465 183 HOH   HOH A . 
F 6 HOH   166 466 188 HOH   HOH A . 
F 6 HOH   167 467 230 HOH   HOH A . 
F 6 HOH   168 468 201 HOH   HOH A . 
F 6 HOH   169 469 182 HOH   HOH A . 
F 6 HOH   170 470 113 HOH   HOH A . 
F 6 HOH   171 471 148 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 23  HOH   HOH D . 
G 6 HOH   3   203 78  HOH   HOH D . 
G 6 HOH   4   204 38  HOH   HOH D . 
G 6 HOH   5   205 73  HOH   HOH D . 
G 6 HOH   6   206 53  HOH   HOH D . 
G 6 HOH   7   207 240 HOH   HOH D . 
G 6 HOH   8   208 49  HOH   HOH D . 
G 6 HOH   9   209 195 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           7GV2 
_cell.length_a           67.790 
_cell.length_b           67.790 
_cell.length_c           166.890 
_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                         7GV2 
_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          7GV2 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.65 
_exptl_crystal.density_percent_sol   66.34 
_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                     7GV2 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             34.010 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23807 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.082 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.700 
_reflns.B_iso_Wilson_estimate        33.540 
_reflns.pdbx_redundancy              9.000 
_reflns.pdbx_Rrim_I_all              0.087 
_reflns.pdbx_Rpim_I_all              0.029 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     215281 
_reflns.pdbx_scaling_rejects         822 
_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  ? 11947 1282 ? 1.902 ? ? ? 9.300 ? 1.200  ? ? ? ? ? ? 100.000 2.012 0.650 0.597 ? 
1 2 9.090 34.010 ? 1500  236  ? 0.048 ? ? ? 6.400 ? 30.500 ? ? ? ? ? ? 98.800  0.052 0.020 0.998 ? 
# 
_refine.entry_id                                 7GV2 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             34.0100 
_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                     23740 
_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                          0.1800 
_refine.ls_R_factor_R_work                       0.1790 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2030 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1500 
_refine.ls_number_reflns_R_free                  1222 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               38.4500 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.6338 
_refine.aniso_B[2][2]                            -0.6338 
_refine.aniso_B[3][3]                            1.2677 
_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               0.9620 
_refine.correlation_coeff_Fo_to_Fc_free          0.9460 
_refine.overall_SU_R_Cruickshank_DPI             0.0860 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0850 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0980 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0940 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                129.720 
_refine.B_iso_min                                19.450 
_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                        7GV2 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.230 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.7500 
_refine_hist.d_res_low                        34.0100 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             185 
_refine_hist.number_atoms_total               1231 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           33.61 
_refine_hist.pdbx_B_iso_mean_solvent          56.36 
_refine_hist.pdbx_number_atoms_protein        1022 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' t_dihedral_angle_d        445  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              235  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1233 ?      ? 20.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 162  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        8    ?      ? 1.000  HARMONIC     
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1624 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1233 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1689 0.880  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.300  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.630 ? ?      ?            
# 
_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               99.9300 
_refine_ls_shell.number_reflns_R_work             2695 
_refine_ls_shell.R_factor_all                     0.3129 
_refine_ls_shell.R_factor_R_work                  0.3122 
_refine_ls_shell.R_factor_R_free                  0.3278 
_refine_ls_shell.percent_reflns_R_free            4.6700 
_refine_ls_shell.number_reflns_R_free             132 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2827 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GV2 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 13.75 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GV2 
_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 7GV2       7GV2   ? 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 7GV2 A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GV2 D 1 ? 6   ? 7GV2   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 7GV2 GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GV2 PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GV2 GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7390  ? 
1 MORE         -64   ? 
1 'SSA (A^2)'  13020 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_545 x,x-y-1,-z+1/6 0.5000000000 0.8660254038 0.0000000000 33.8950000000 0.8660254038 
-0.5000000000 0.0000000000 -58.7078621225 0.0000000000 0.0000000000 -1.0000000000 27.8150000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ARG A 12  ? ARG A 27  ? ARG A 13  ARG A 28  1 ? 16 
HELX_P HELX_P2 AA2 HIS A 45  ? SER A 53  ? HIS A 46  SER A 54  1 ? 9  
HELX_P HELX_P3 AA3 SER A 53  ? THR A 61  ? SER A 54  THR A 62  1 ? 9  
HELX_P HELX_P4 AA4 LEU A 64  ? LEU A 68  ? LEU A 65  LEU A 69  5 ? 5  
HELX_P HELX_P5 AA5 ASN A 78  ? SER A 92  ? ASN A 79  SER A 93  1 ? 15 
HELX_P HELX_P6 AA6 ASN A 100 ? GLN A 112 ? ASN A 101 GLN A 113 1 ? 13 
HELX_P HELX_P7 AA7 MET A 113 ? GLU A 128 ? MET A 114 GLU A 129 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N A ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
# 
_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                   7GV2 
_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 62.06 -119.35 
2 1 SER A 39 ? B 37.88 66.48   
3 1 ARG A 40 ? B 75.16 -22.09  
4 1 SER A 93 ? A 75.76 -2.49   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 370 ? F HOH . 
2 1 A HOH 387 ? F HOH . 
3 1 A HOH 456 ? F HOH . 
4 1 A HOH 465 ? F HOH . 
5 1 A HOH 467 ? F HOH . 
6 1 A HOH 468 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.2144 -16.5503 24.6837 0.0041  -0.0665 -0.0429 -0.0429 0.0283  -0.0205 1.0894 1.8190  1.9922 
0.4857  -0.3361 1.1392 0.1473 -0.0874 -0.0599 -0.0572 0.1021  0.0949 0.2551  -0.0068 -0.0077 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1360 0.1104  -0.0236 -0.0441 -0.0070 -0.0810 0.6525 -0.3259 0.0140 
-0.0939 0.0535  0.5149 0.0289 -0.0108 -0.0182 -0.0019 -0.0036 0.0361 -0.0407 -0.0096 -0.0040 
# 
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                    7GV2 
_atom_sites.fract_transf_matrix[1][1]   0.014751 
_atom_sites.fract_transf_matrix[1][2]   0.008517 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017033 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005992 
_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   ? 17.320 -21.258 -4.815 1.00 69.34  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.234 -22.140 -5.541 1.00 68.24  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.771 -23.616 -5.485 1.00 67.76  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.705 -23.917 -4.936 1.00 68.52  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.668 -21.993 -4.976 1.00 69.05  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.759 -22.030 -6.035 1.00 83.36  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.898 -23.079 -6.715 1.00 83.70  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.483 -21.018 -6.177 1.00 90.88  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.569 -24.525 -6.071 1.00 58.90  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.306 -25.960 -6.068 1.00 56.03  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.300 -26.694 -5.116 1.00 51.40  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.585 -27.874 -5.311 1.00 50.45  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.384 -26.512 -7.487 1.00 61.39  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.661 -26.291 -8.062 1.00 72.46  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.796 -25.998 -4.073 1.00 42.69  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.735 -26.572 -3.108 1.00 39.69  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.121 -27.737 -2.302 1.00 39.28  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.897 -27.809 -2.145 1.00 39.66  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.243 -25.483 -2.162 1.00 40.42  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.402 -24.297 -2.907 1.00 45.77  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.968 -28.637 -1.795 1.00 30.81  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.613 -29.640 -0.788 1.00 27.97  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.225 -29.103 0.519  1.00 29.60  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.183 -28.314 0.474  1.00 28.76  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.961 -31.122 -1.096 1.00 30.61  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.492 -31.313 -1.321 1.00 30.62  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.114 -31.654 -2.282 1.00 31.37  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.958 -32.759 -1.568 1.00 36.97  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.736 -29.540 1.684  0.66 25.16  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.611 -29.452 1.649  0.34 25.69  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.273 -29.045 2.959  0.66 24.08  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 21.019 -28.955 2.950  0.34 24.47  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.617 -30.189 3.904  0.66 27.01  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.412 -30.083 3.882  0.34 27.73  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.846 -31.144 4.007  0.66 27.87  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.707 -31.088 3.972  0.34 28.15  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.274 -28.061 3.623  0.66 25.73  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.882 -28.127 3.560  0.34 25.78  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.524 -27.800 5.127  0.66 30.21  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.354 -27.143 4.628  0.34 26.26  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.077 -26.448 5.622  0.66 51.63  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.584 -27.274 5.920  0.34 40.46  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.467 -25.656 4.901  0.66 44.83  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.366 -27.480 5.932  0.34 31.01  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.390 -26.146 6.879  0.66 48.17  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.283 -27.135 7.040  0.34 37.13  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.758 -30.086 4.601  0.66 24.79  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.533 -29.908 4.578  0.34 24.51  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.139 -31.101 5.578  0.66 23.27  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.038 -30.887 5.532  0.34 23.57  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.681 -30.608 6.941  0.66 25.53  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.558 -30.446 6.890  0.34 26.16  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.276 -29.680 7.513  0.66 23.53  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.998 -29.405 7.403  0.34 24.85  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.656 -31.411 5.521  0.66 23.90  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.571 -30.991 5.426  0.34 24.71  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 25.048 -32.620 6.341  0.66 24.75  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.031 -31.780 4.219  0.34 26.83  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.672 -33.902 5.948  0.66 27.88  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.759 -31.335 2.927  0.34 30.37  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.836 -32.484 7.480  0.66 25.22  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.764 -32.950 4.371  0.34 30.02  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 25.022 -35.018 6.721  0.66 28.88  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.183 -32.062 1.812  0.34 31.62  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.162 -33.594 8.264  0.66 27.46  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.192 -33.677 3.250  0.34 33.41  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.762 -34.854 7.877  0.66 26.49  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.901 -33.224 1.981  0.34 31.31  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.587 -31.190 7.438  1.00 23.26  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.939 -30.812 8.712  1.00 23.52  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.892 -30.587 9.904  1.00 26.28  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.779 -29.558 10.588 1.00 25.71  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.851 -31.830 9.084  1.00 31.29  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.964 -31.976 7.959  1.00 33.12  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.045 -31.401 10.327 1.00 35.53  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.825 -31.523 10.130 1.00 23.71  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.729 -31.439 11.287 1.00 24.18  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.974 -30.544 11.078 1.00 25.75  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.791 -30.439 12.005 1.00 24.28  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.188 -32.856 11.693 1.00 29.01  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.073 -33.804 12.198 1.00 38.70  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.481 -33.384 13.532 1.00 60.47  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.441 -33.474 14.637 1.00 73.37  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.322 -32.822 15.790 1.00 83.96  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.237 -32.967 16.738 1.00 72.30  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.295 -32.005 15.998 1.00 65.11  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.135 -29.923 9.891  1.00 22.10  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.362 -29.159 9.607  1.00 21.86  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.655 -28.056 10.628 1.00 24.46  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.790 -27.979 11.124 1.00 22.62  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.353 -28.588 8.168  1.00 21.81  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.608 -27.824 7.869  1.00 23.68  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.794 -28.483 7.662  1.00 23.85  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.805 -26.494 7.711  1.00 23.85  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.694 -27.545 7.404  1.00 23.57  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.150 -26.325 7.437  1.00 23.01  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.670 -27.170 10.896 1.00 21.19  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.896 -26.044 11.843 1.00 21.40  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.320 -26.542 13.251 1.00 23.22  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.251 -25.987 13.853 1.00 21.28  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.646 -25.169 11.916 1.00 22.69  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.657 -27.594 13.748 0.42 22.35  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.657 -27.603 13.744 0.30 21.80  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.655 -27.594 13.760 0.28 21.75  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.956 -28.177 15.056 0.42 22.33  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.939 -28.214 15.044 0.30 21.78  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.973 -28.158 15.075 0.28 21.72  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.367 -28.771 15.066 0.42 25.58  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.350 -28.799 15.071 0.30 25.65  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.363 -28.802 15.084 0.28 25.66  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.097 -28.579 16.045 0.42 22.77  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.063 -28.629 16.064 0.30 23.64  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.082 -28.668 16.078 0.28 23.76  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.925 -29.244 15.416 0.42 26.93  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.919 -29.307 15.351 0.30 25.73  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.902 -29.148 15.522 0.28 25.85  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.207 -29.817 16.683 0.42 31.08  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.618 -28.762 15.476 0.30 29.40  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.838 -30.273 14.662 0.28 30.26  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.750 -29.474 13.974 1.00 23.13  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.087 -30.099 13.831 1.00 23.68  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.164 -29.004 13.797 1.00 23.99  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.213 -29.166 14.422 1.00 23.73  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.161 -30.961 12.559 1.00 25.65  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.375 -32.270 12.646 1.00 36.27  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.826 -32.569 13.738 1.00 35.41  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.294 -32.987 11.618 1.00 39.36  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.893 -27.886 13.085 1.00 20.09  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.855 -26.763 13.044 1.00 19.45  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.082 -26.234 14.478 1.00 24.15  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.217 -26.044 14.913 1.00 22.45  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.395 -25.619 12.084 1.00 21.66  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.190 -24.327 12.322 1.00 21.52  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.480 -26.049 10.614 1.00 22.27  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.990 -25.968 15.191 1.00 21.52  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.090 -25.407 16.550 1.00 22.41  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.818 -26.366 17.516 1.00 23.10  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.668 -25.925 18.301 1.00 21.73  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.701 -25.017 17.061 1.00 23.11  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.714 -24.153 18.341 1.00 26.97  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.319 -22.790 18.075 1.00 26.53  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.297 -23.991 18.885 1.00 30.68  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.522 -27.662 17.405 1.00 21.35  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.194 -28.705 18.189 1.00 22.70  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.709 -28.619 17.932 1.00 25.12  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.484 -28.619 18.892 1.00 25.23  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.677 -30.080 17.776 1.00 25.05  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.224 -31.274 18.561 1.00 33.70  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.825 -31.178 20.041 1.00 36.42  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.656 -32.572 18.008 1.00 38.14  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.122 -28.477 16.655 1.00 21.49  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.549 -28.375 16.340 1.00 20.42  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.168 -27.080 16.841 1.00 23.02  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.301 -27.080 17.317 1.00 23.59  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.798 -28.594 14.856 1.00 22.30  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.752 -30.057 14.483 1.00 33.14  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.962 -30.947 15.320 1.00 30.33  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.491 -30.340 13.215 1.00 28.22  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.428 -25.976 16.765 1.00 21.92  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.951 -24.707 17.286 1.00 21.65  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.163 -24.837 18.808 1.00 23.82  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.135 -24.298 19.345 1.00 23.55  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 34.007 -23.543 16.966 1.00 21.73  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.864 -23.189 15.469 1.00 24.26  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.784 -22.124 15.278 1.00 26.10  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.207 -22.762 14.847 1.00 26.60  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.233 -25.529 19.506 1.00 21.45  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.382 -25.745 20.958 1.00 22.14  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.615 -26.628 21.263 1.00 26.49  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.320 -26.378 22.243 1.00 27.32  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.125 -26.358 21.570 1.00 24.75  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.133 -26.243 23.084 1.00 31.72  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.647 -25.279 23.656 1.00 28.55  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.574 -27.224 23.751 1.00 32.73  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.897 -27.620 20.405 1.00 24.51  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.080 -28.483 20.532 1.00 25.01  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.345 -27.642 20.373 1.00 29.06  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.293 -27.824 21.130 1.00 29.45  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 37.062 -29.605 19.484 1.00 24.87  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 36.056 -30.709 19.822 1.00 28.21  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.862 -31.641 18.634 1.00 29.15  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 35.032 -32.789 18.994 1.00 38.56  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.379 -33.549 18.124 1.00 55.34  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.407 -33.262 16.827 1.00 43.27  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.675 -34.589 18.544 1.00 47.96  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.346 -26.676 19.422 1.00 24.54  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.506 -25.785 19.264 1.00 25.43  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.675 -24.932 20.525 1.00 29.47  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.805 -24.744 21.012 1.00 29.27  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.325 -24.865 18.063 1.00 25.13  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.320 -25.544 16.678 1.00 29.91  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.175 -24.495 15.578 1.00 29.52  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.568 -26.404 16.476 1.00 31.65  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.544 -24.413 21.058 1.00 25.53  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.579 -23.635 22.291 1.00 26.24  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.191 -24.448 23.468 1.00 31.35  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 40.073 -23.931 24.172 1.00 31.78  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.178 -23.122 22.663 1.00 26.17  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.288 -22.268 23.934 1.00 30.07  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 36.012 -21.593 24.314 1.00 34.85  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.987 -22.556 24.696 1.00 33.30  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.377 -22.586 25.876 1.00 43.66  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.732 -21.740 26.839 1.00 35.63  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.422 -23.470 26.108 1.00 33.39  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.725 -25.691 23.666 0.39 28.82  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.727 -25.702 23.650 0.28 28.76  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.726 -25.694 23.667 0.33 29.02  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.187 -26.581 24.740 0.39 30.07  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.170 -26.642 24.690 0.28 29.98  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.186 -26.593 24.734 0.33 30.37  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.698 -26.860 24.675 0.39 36.29  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.684 -26.857 24.664 0.28 36.05  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.698 -26.857 24.673 0.33 36.32  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.341 -26.974 25.721 0.39 37.67  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.312 -26.944 25.721 0.28 37.23  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.340 -26.965 25.720 0.33 37.59  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.390 -27.880 24.741 0.39 33.38  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.481 -27.990 24.508 0.28 33.38  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.415 -27.907 24.690 0.33 34.15  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.716 -28.714 23.641 0.39 39.43  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.106 -27.945 24.841 0.28 39.49  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.816 -28.783 25.732 0.33 43.36  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.262 -26.935 23.453 1.00 32.46  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.696 -27.174 23.233 1.00 34.09  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.475 -25.871 23.029 1.00 36.79  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.678 -25.908 22.751 1.00 37.57  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.867 -28.132 22.050 1.00 35.87  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.139 -29.459 22.260 1.00 40.83  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.098 -30.300 21.005 1.00 47.40  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.447 -30.626 20.540 1.00 60.62  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.764 -30.815 19.265 1.00 75.45  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 45.016 -31.086 18.920 1.00 63.48  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.841 -30.705 18.324 1.00 61.09  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.793 -24.720 23.182 1.00 30.71  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.361 -23.373 23.038 1.00 31.79  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.995 -23.133 21.632 1.00 35.93  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 45.034 -22.479 21.501 1.00 37.43  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.354 -23.063 24.188 1.00 35.48  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.679 -21.589 24.333 1.00 45.31  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.765 -20.755 24.124 1.00 44.27  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.842 -21.267 24.659 1.00 50.88  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.365 -23.677 20.597 1.00 28.77  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.851 -23.563 19.217 1.00 28.54  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.242 -22.352 18.507 1.00 31.15  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 42.015 -22.234 18.407 1.00 27.18  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.616 -24.874 18.425 1.00 31.63  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.430 -26.057 19.025 1.00 33.93  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.917 -24.680 16.908 1.00 31.46  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.928 -27.432 18.538 1.00 39.12  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.118 -21.460 18.003 1.00 29.98  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.755 -20.266 17.231 1.00 30.50  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.854 -19.270 17.991 1.00 31.58  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.260 -18.388 17.368 1.00 29.15  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.177 -20.606 15.848 1.00 31.49  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.230 -21.099 14.806 1.00 39.44  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.611 -21.226 13.460 1.00 40.65  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.392 -20.153 14.680 1.00 46.19  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.835 -19.349 19.332 1.00 28.48  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.164 -18.342 20.164 1.00 27.85  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.985 -17.056 19.961 1.00 34.04  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.216 -17.116 19.819 1.00 34.06  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 42.100 -18.784 21.631 1.00 32.13  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.419 -19.114 22.058 1.00 35.56  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.145 -19.981 21.843 1.00 31.54  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.308 -15.920 19.829 1.00 29.95  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.990 -14.669 19.493 1.00 30.02  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.654 -13.519 20.409 1.00 31.88  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 43.004 -12.375 20.108 1.00 32.03  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.695 -14.296 18.028 1.00 31.20  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.217 -14.310 17.634 1.00 41.93  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.355 -14.423 18.535 1.00 37.53  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.929 -14.219 16.429 1.00 53.16  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.978 -13.803 21.526 1.00 26.71  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.652 -12.756 22.501 1.00 26.42  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.487 -13.364 23.885 1.00 30.09  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 41.079 -14.535 24.018 1.00 29.50  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.379 -11.930 22.064 1.00 28.71  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 39.083 -12.738 22.204 1.00 26.67  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.264 -10.584 22.815 1.00 29.02  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.792 -12.553 24.906 0.60 27.38  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.784 -12.570 24.917 0.40 26.97  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.590 -12.853 26.317 0.60 27.31  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.535 -12.943 26.300 0.40 26.70  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.506 -11.872 26.792 0.60 29.52  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.568 -11.906 26.891 0.40 29.64  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.626 -10.665 26.560 0.60 29.89  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.796 -10.699 26.779 0.40 30.09  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.895 -12.705 27.162 0.60 32.87  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.798 -13.248 27.159 0.40 31.81  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.634 -12.978 28.642 0.60 33.01  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.693 -12.029 27.334 0.40 32.36  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.996 -13.624 26.649 0.60 33.50  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.423 -13.848 28.511 0.40 31.80  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.446 -12.390 27.420 1.00 25.33  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.393 -11.570 28.019 1.00 25.22  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.673 -11.576 29.514 1.00 30.62  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.690 -12.649 30.136 1.00 30.08  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.949 -12.053 27.704 1.00 26.83  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.727 -12.228 26.170 1.00 26.38  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.929 -11.071 28.310 1.00 28.58  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.985 -10.933 25.291 1.00 27.24  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.906 -10.389 30.076 1.00 27.70  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.209 -10.256 31.507 1.00 27.77  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.956 -9.829  32.262 1.00 33.41  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.365 -8.783  31.962 1.00 31.20  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.422 -9.320  31.780 1.00 32.85  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.706 -9.212  33.281 1.00 33.20  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.669 -9.821  31.056 1.00 33.55  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.565 -10.642 33.258 1.00 30.41  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.379 -10.427 34.081 1.00 29.98  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.876 -10.477 35.519 1.00 37.92  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 37.039 -11.560 36.089 1.00 35.02  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.263 -11.460 33.764 1.00 32.74  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.948 -11.038 34.407 1.00 32.90  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 35.093 -11.640 32.252 1.00 31.57  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.237 -9.303  36.068 0.54 38.46  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.106 -9.274  36.082 0.46 37.36  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.818 -9.143  37.411 0.54 40.24  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.639 -9.005  37.418 0.46 38.68  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.175 -9.898  37.482 0.54 41.87  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.727 -10.018 37.789 0.46 41.12  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 40.068 -9.593  36.691 0.54 40.97  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.534 -10.910 38.623 0.46 40.90  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.842 -9.595  38.503 0.54 46.15  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.527 -8.886  38.452 0.46 43.15  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.550 -9.031  38.338 0.54 60.98  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.864 -7.642  38.286 0.46 50.56  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.304 -10.898 38.382 0.54 38.13  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.834 -9.917  37.035 0.46 36.15  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.523 -11.693 38.568 0.54 38.33  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 41.076 -10.690 37.091 0.46 36.58  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.625 -12.882 37.603 0.54 40.49  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.945 -12.109 36.505 0.46 38.25  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.651 -13.573 37.604 0.54 40.31  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.968 -12.643 36.067 0.46 38.47  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.641 -12.183 40.027 0.54 38.87  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.723 -10.698 38.488 0.46 38.74  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 41.081 -11.110 41.013 0.54 45.63  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.213 -9.308  38.898 0.46 49.60  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.417 -11.723 42.358 0.54 47.26  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.210 -9.340  40.034 0.46 58.39  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.633 -10.710 43.389 0.54 51.12  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.648 -7.991  40.405 0.46 64.52  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.811 -10.167 43.686 0.54 62.70  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.065 -7.239  41.335 0.46 76.48  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.905 -9.261  44.648 0.54 50.79  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 42.008 -7.692  42.000 0.46 61.92  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.902 -10.519 43.017 0.54 47.69  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.532 -6.028  41.604 0.46 63.73  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.568 -13.135 36.799 0.54 35.03  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.715 -12.690 36.424 0.46 33.93  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.544 -14.260 35.861 0.54 33.72  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.481 -14.015 35.813 0.46 33.23  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.819 -13.841 34.422 0.54 35.65  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.627 -13.871 34.293 0.46 35.33  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.491 -12.729 34.012 0.54 33.81  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 39.046 -12.953 33.710 0.46 33.04  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.212 -15.045 35.949 0.54 34.72  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.094 -14.581 36.185 0.46 34.59  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.919 -15.631 37.323 0.54 50.89  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 38.008 -15.114 37.606 0.46 48.89  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.217 -17.110 37.467 0.54 87.49  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.204 -16.612 37.722 0.46 84.14  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.470 -17.930 36.883 0.54 87.45  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.248 -17.031 38.271 0.46 85.85  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.194 -17.451 38.173 0.54 88.32  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.316 -17.367 37.263 0.46 85.24  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.402 -14.768 33.651 1.00 31.65  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.729 -14.629 32.239 1.00 30.92  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.100 -15.745 31.436 1.00 33.28  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.137 -16.895 31.879 1.00 32.86  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.257 -14.640 32.067 1.00 33.63  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.955 -13.419 32.657 1.00 51.01  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.417 -13.313 32.291 1.00 70.55  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.986 -14.140 31.561 1.00 63.65  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 45.059 -12.276 32.798 1.00 72.03  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.508 -15.413 30.269 1.00 27.56  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.850 -16.403 29.398 1.00 27.19  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.360 -16.243 27.987 1.00 31.53  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.216 -15.163 27.413 1.00 31.67  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.323 -16.203 29.402 1.00 28.22  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.707 -16.340 30.773 1.00 29.93  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.577 -15.235 31.611 1.00 31.78  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.237 -17.570 31.220 1.00 32.58  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 36.036 -15.367 32.893 1.00 33.61  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.693 -17.701 32.503 1.00 35.83  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.588 -16.597 33.328 1.00 33.52  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.974 -17.295 27.430 1.00 28.06  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.481 -17.244 26.057 1.00 26.83  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.350 -17.634 25.100 1.00 29.82  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.546 -18.529 25.403 1.00 28.07  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.708 -18.164 25.884 1.00 28.81  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.938 -17.708 26.718 1.00 36.59  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.252 -18.136 26.073 1.00 46.59  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.277 -17.752 24.656 1.00 56.00  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.861 -16.665 24.165 1.00 68.84  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.577 -15.874 24.951 1.00 63.11  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.781 -16.390 22.871 1.00 49.32  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.271 -16.973 23.941 1.00 26.32  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.196 -17.276 22.979 1.00 25.76  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.570 -16.857 21.574 1.00 27.39  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.654 -16.299 21.358 1.00 26.30  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.887 -16.585 23.402 1.00 26.16  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.672 -17.152 20.620 1.00 23.88  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.813 -16.755 19.224 1.00 22.98  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.944 -15.501 19.043 1.00 24.67  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.733 -15.544 19.328 1.00 24.18  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.323 -17.879 18.287 1.00 23.10  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.105 -19.143 18.455 1.00 26.56  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.627 -20.187 19.236 1.00 28.19  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.354 -19.456 18.020 1.00 28.43  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.578 -21.115 19.222 1.00 28.07  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.642 -20.718 18.509 1.00 28.10  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.552 -14.397 18.589 1.00 23.32  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.811 -13.138 18.332 1.00 23.57  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.565 -13.404 17.460 1.00 26.36  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.487 -12.888 17.762 1.00 24.61  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.709 -12.117 17.602 1.00 26.24  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.733 -11.474 18.530 1.00 31.08  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.664 -10.573 17.732 1.00 30.66  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.753 -10.057 18.631 1.00 33.34  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.712 -9.215  17.881 1.00 33.01  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.710 -14.190 16.380 1.00 24.30  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.579 -14.441 15.471 1.00 24.26  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.399 -15.089 16.170 1.00 24.61  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.264 -14.683 15.924 1.00 24.13  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 35.008 -15.212 14.228 1.00 28.04  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.598 -16.433 14.653 1.00 31.38  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.955 -14.379 13.329 1.00 30.39  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.648 -16.071 17.051 1.00 21.43  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.557 -16.738 17.789 1.00 20.92  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.886 -15.743 18.747 1.00 23.59  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.652 -15.690 18.802 1.00 22.06  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 33.043 -18.007 18.524 1.00 23.19  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.904 -18.601 19.373 1.00 23.67  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.540 -19.045 17.503 1.00 23.45  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.695 -14.933 19.471 1.00 22.29  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.128 -13.926 20.370 1.00 21.75  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.216 -12.949 19.612 1.00 24.35  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.098 -12.679 20.066 1.00 24.65  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.240 -13.150 21.099 1.00 21.66  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.192 -13.960 22.003 1.00 24.91  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.270 -13.025 22.601 1.00 24.83  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.413 -14.698 23.106 1.00 27.26  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.653 -12.486 18.425 1.00 22.14  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.868 -11.548 17.597 1.00 23.52  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.586 -12.186 17.100 1.00 26.94  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.535 -11.547 17.104 1.00 27.22  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.678 -11.081 16.393 1.00 25.38  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.895 -10.282 16.776 1.00 28.44  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.969 -10.182 15.332 1.00 32.57  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.204 -8.872  14.515 1.00 29.26  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.660 -13.469 16.708 1.00 23.56  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.499 -14.203 16.196 1.00 23.10  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.408 -14.409 17.279 1.00 27.29  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.243 -14.626 16.930 1.00 27.65  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.959 -15.560 15.628 1.00 23.39  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.796 -14.365 18.577 1.00 22.38  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.885 -14.627 19.708 1.00 23.67  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.412 -13.407 20.497 1.00 26.97  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.447 -13.543 21.262 1.00 25.06  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.545 -15.618 20.659 1.00 23.45  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.883 -17.234 19.924 1.00 25.86  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.167 -12.297 20.445 1.00 24.01  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.959 -11.155 21.337 1.00 23.46  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.966 -9.846  20.585 1.00 27.38  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.940 -9.549  19.872 1.00 25.94  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.089 -11.173 22.372 1.00 24.40  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.380 -9.932  22.996 1.00 27.92  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.918 -9.040  20.793 1.00 24.80  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.849 -7.709  20.198 1.00 25.21  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.968 -6.814  20.704 1.00 28.06  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.513 -5.998  19.940 1.00 27.31  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.371 -6.995  21.992 1.00 26.25  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.493 -6.206  22.538 1.00 25.96  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.840 -6.556  21.839 1.00 28.37  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.545 -5.649  21.378 1.00 25.79  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.607 -6.394  24.069 1.00 25.55  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.679 -5.501  24.740 1.00 31.27  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.274 -4.011  24.727 1.00 32.77  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.976 -5.973  26.142 1.00 32.02  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.171 -7.854  21.723 1.00 24.09  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.435 -8.233  21.057 1.00 22.90  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.420 -7.891  19.581 1.00 26.57  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.453 -7.516  19.033 1.00 25.85  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.795 -9.700  21.301 1.00 23.88  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.221 -9.933  22.734 1.00 24.14  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.293 -9.227  23.287 1.00 26.82  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.581 -10.886 23.520 1.00 25.43  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.660 -9.411  24.633 1.00 26.92  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.990 -11.114 24.845 1.00 27.78  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 33.018 -10.370 25.393 1.00 25.38  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.240 -7.969  18.943 1.00 24.31  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.118 -7.580  17.528 1.00 25.26  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.537 -6.097  17.377 1.00 29.11  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.330 -5.768  16.488 1.00 27.23  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.670 -7.798  17.067 1.00 27.36  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.397 -7.274  15.682 1.00 31.60  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 29.035 -7.816  14.572 1.00 33.48  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.510 -6.221  15.479 1.00 35.54  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.785 -7.333  13.286 1.00 35.98  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.250 -5.733  14.202 1.00 38.79  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.878 -6.304  13.109 1.00 46.37  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.604 -5.825  11.862 1.00 52.03  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 30.005 -5.219  18.246 0.53 27.34  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 30.004 -5.218  18.246 0.47 27.36  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.325 -3.788  18.246 0.53 28.25  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.330 -3.790  18.244 0.47 28.35  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.814 -3.540  18.545 0.53 33.62  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.827 -3.575  18.508 0.47 33.42  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.434 -2.716  17.881 0.53 35.35  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.465 -2.815  17.784 0.47 34.85  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.438 -3.046  19.242 0.53 30.50  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.500 -3.052  19.292 0.47 31.08  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 28.099 -3.010  18.775 0.53 32.93  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.788 -1.663  19.272 0.47 36.52  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.383 -4.269  19.522 1.00 29.58  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.803 -4.156  19.916 1.00 28.85  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.751 -4.532  18.779 1.00 32.05  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.645 -3.749  18.452 1.00 32.95  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.135 -4.988  21.212 1.00 30.99  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.406 -4.434  22.457 1.00 31.01  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.668 -5.076  21.459 1.00 29.78  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.469 -5.402  23.677 1.00 33.16  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.573 -5.719  18.193 1.00 27.06  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.550 -6.175  17.220 1.00 27.54  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.329 -5.627  15.806 1.00 32.31  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.173 -5.876  14.938 1.00 33.62  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.686 -7.702  17.261 1.00 27.38  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.114 -8.192  18.634 1.00 27.86  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.316 -7.771  19.201 1.00 31.23  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.324 -9.084  19.349 1.00 28.90  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.699 -8.209  20.477 1.00 31.85  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.715 -9.535  20.616 1.00 31.53  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.898 -9.097  21.172 1.00 30.18  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.263 -4.832  15.581 1.00 30.14  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 34.101 -4.150  14.288 1.00 30.38  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.641 -2.724  14.410 1.00 36.58  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.711 -1.997  13.414 1.00 37.04  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.676 -4.183  13.733 1.00 37.98  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.771 -3.659  14.699 1.00 35.15  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.257 -5.568  13.241 1.00 33.61  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 35.053 -2.324  15.633 1.00 32.33  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.658 -1.001  15.830 1.00 33.32  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 37.078 -1.061  15.273 1.00 39.93  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.824 -1.971  15.628 1.00 37.94  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.669 -0.614  17.318 1.00 34.45  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.412 0.684   17.544 1.00 48.76  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.799 1.751   17.367 1.00 53.54  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.622 0.628   17.837 1.00 51.27  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.464 -0.061  14.445 1.00 41.25  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.765 0.008   13.774 1.00 42.70  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.978 -0.027  14.721 1.00 46.33  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 41.045 -0.459  14.286 1.00 48.72  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.834 1.214   12.825 1.00 46.33  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.999 1.027   11.559 1.00 63.67  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.830 0.412   15.994 1.00 38.75  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.916 0.329   16.976 1.00 38.50  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.821 -0.925  17.840 1.00 41.62  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.842 -1.555  18.105 1.00 42.93  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.932 1.555   17.922 1.00 39.51  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.545 2.847   17.416 1.00 46.71  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.366 3.949   18.443 1.00 47.34  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 43.034 2.690   17.092 1.00 51.65  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.618 -1.253  18.350 1.00 34.60  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.469 -2.377  19.276 1.00 33.53  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.602 -3.735  18.591 1.00 38.66  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.977 -4.699  19.257 1.00 36.97  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.168 -2.282  20.097 1.00 34.39  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 38.039 -1.004  20.941 1.00 34.26  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.783 -1.096  21.812 1.00 33.57  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.427 0.220   22.474 1.00 39.49  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.925 1.235   21.517 1.00 41.89  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.353 -3.804  17.259 1.00 38.13  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.481 -5.055  16.481 1.00 38.62  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.870 -5.688  16.632 1.00 42.80  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 41.003 -6.904  16.465 1.00 43.19  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.126 -4.841  15.008 1.00 40.81  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.275 -3.764  14.094 1.00 47.29  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.899 -4.850  16.919 1.00 38.18  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.303 -5.236  17.048 1.00 38.84  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.768 -5.538  18.473 1.00 41.89  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.928 -5.914  18.674 1.00 40.70  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.203 -4.169  16.394 1.00 40.97  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 44.015 -4.120  14.888 1.00 57.53  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.949 -3.050  14.284 1.00 58.16  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.875 -5.278  14.247 1.00 47.60  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.877 -5.390  19.463 1.00 38.91  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.260 -5.661  20.843 1.00 37.93  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.275 -7.162  21.114 1.00 39.49  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.392 -7.882  20.623 1.00 38.03  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.309 -4.953  21.832 1.00 37.87  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.289 -3.413  21.790 1.00 42.82  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.226 -2.870  22.733 1.00 42.95  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.665 -2.814  22.131 1.00 45.03  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.264 -7.632  21.891 0.51 36.48  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.267 -7.622  21.894 0.49 36.47  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.364 -9.049  22.262 0.51 36.25  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.409 -9.030  22.282 0.49 36.27  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.759 -9.285  23.657 0.51 37.58  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.782 -9.279  23.663 0.49 37.62  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.582 -10.433 24.064 0.51 35.91  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.615 -10.429 24.067 0.49 35.97  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.814 -9.523  22.209 0.51 41.14  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.881 -9.433  22.290 0.49 41.18  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.643 -8.761  23.069 0.51 49.26  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.396 -9.468  20.969 0.49 48.58  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.463 -8.189  24.390 1.00 34.16  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.869 -8.220  25.735 1.00 33.25  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.686 -7.242  25.784 1.00 34.15  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.834 -6.067  25.402 1.00 33.79  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.907 -7.888  26.856 1.00 38.99  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.262 -7.913  28.249 1.00 39.44  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 45.123 -8.817  26.809 1.00 39.51  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.534 -7.724  26.283 1.00 27.30  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.323 -6.925  26.487 1.00 27.27  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.919 -7.040  27.955 1.00 31.15  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.687 -8.147  28.445 1.00 29.94  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.161 -7.294  25.512 1.00 29.04  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.569 -7.114  24.004 1.00 30.38  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.847 -6.552  25.847 1.00 29.70  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.899 -5.661  23.513 1.00 34.14  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.797 -5.897  28.639 1.00 28.95  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.397 -5.847  30.035 1.00 29.04  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.919 -5.520  30.150 1.00 31.55  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.484 -4.462  29.697 1.00 30.58  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.220 -4.800  30.813 1.00 33.59  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.704 -4.992  30.740 1.00 51.59  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.239 -6.037  31.102 1.00 41.73  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.403 -3.971  30.293 1.00 47.61  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.147 -6.416  30.763 1.00 26.65  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.728 -6.163  30.960 1.00 25.99  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.491 -5.272  32.189 1.00 30.69  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.374 -5.128  33.042 1.00 30.87  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.927 -7.477  31.083 1.00 25.19  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 34.011 -8.486  29.921 1.00 28.68  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.894 -9.544  30.059 1.00 28.66  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.925 -7.806  28.549 1.00 27.66  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.292 -4.689  32.273 1.00 28.24  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.855 -3.825  33.374 1.00 29.50  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 33.075 -4.581  34.702 1.00 33.77  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.761 -5.775  34.756 1.00 32.52  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.366 -3.496  33.177 1.00 31.19  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.817 -2.464  34.142 1.00 41.96  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.690 -2.782  35.346 1.00 43.43  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.491 -1.348  33.691 1.00 42.40  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.627 -3.939  35.758 1.00 34.46  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.868 -4.676  37.024 1.00 35.27  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.631 -5.265  37.696 1.00 38.70  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.777 -6.151  38.536 1.00 39.45  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.569 -3.648  37.932 1.00 38.40  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.279 -2.317  37.326 1.00 43.34  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.090 -2.535  35.849 1.00 37.15  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.424 -4.822  37.317 1.00 35.62  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.174 -5.345  37.884 1.00 37.15  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.885 -6.757  37.336 1.00 36.96  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 29.065 -7.481  37.900 1.00 35.74  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 29.003 -4.404  37.533 1.00 39.99  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.841 -4.441  38.512 1.00 60.61  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 28.003 -3.544  39.725 1.00 90.27  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.076 -2.306  39.546 1.00 89.86  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.047 -4.079  40.858 1.00 84.24  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.539 -7.142  36.231 1.00 30.63  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.278 -8.456  35.629 1.00 29.58  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.861 -9.586  36.457 1.00 33.98  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 32.036 -9.570  36.824 1.00 33.58  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.732 -8.490  34.145 1.00 31.52  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 30.010 -7.383  33.324 1.00 32.75  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.523 -9.885  33.517 1.00 29.26  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.417 -7.364  33.383 1.00 39.02  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 30.023 -10.575 36.711 1.00 34.17  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.346 -11.761 37.488 1.00 34.53  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.106 -12.777 36.613 1.00 34.37  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.581 -13.170 35.571 1.00 31.64  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 29.040 -12.366 38.043 1.00 37.85  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.245 -13.647 38.805 1.00 53.48  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.895 -14.722 38.328 1.00 44.31  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.814 -13.556 40.006 1.00 46.20  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.313 -13.247 37.029 1.00 32.51  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 33.051 -14.232 36.209 1.00 32.05  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.297 -15.547 35.964 1.00 34.29  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.401 -16.105 34.867 1.00 32.48  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.341 -14.465 37.007 1.00 35.65  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.474 -13.266 37.893 1.00 40.70  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 33.076 -12.883 38.242 1.00 36.41  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.521 -16.032 36.959 1.00 31.74  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.763 -17.273 36.766 1.00 30.69  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.661 -17.087 35.699 1.00 32.56  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.517 -17.941 34.827 1.00 30.89  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.187 -17.808 38.088 1.00 33.27  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.610 -19.205 37.893 1.00 42.20  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.745 -19.780 39.000 1.00 69.21  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.721 -21.025 39.130 1.00 68.00  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.080 -19.002 39.722 1.00 61.69  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.922 -15.969 35.768 1.00 30.00  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.909 -15.633 34.768 1.00 29.35  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.530 -15.571 33.379 1.00 30.50  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.975 -16.114 32.409 1.00 28.64  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.719 -14.940 33.274 1.00 26.55  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.417 -14.888 31.978 1.00 25.08  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.788 -16.301 31.497 1.00 28.46  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.554 -16.640 30.335 1.00 26.41  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.684 -13.986 32.038 1.00 26.36  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.295 -13.847 30.661 1.00 26.43  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.712 -13.018 29.703 1.00 28.70  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.358 -14.659 30.268 1.00 27.08  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.226 -12.949 28.403 1.00 29.56  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.867 -14.595 28.967 1.00 28.84  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.286 -13.756 28.035 1.00 27.67  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.378 -17.109 32.381 1.00 29.28  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.773 -18.483 32.062 1.00 30.56  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.592 -19.318 31.498 1.00 31.06  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.747 -20.017 30.480 1.00 29.18  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.395 -19.150 33.283 1.00 33.90  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.094 -20.784 32.934 1.00 39.73  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.409 -19.205 32.147 1.00 27.65  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.183 -19.915 31.750 1.00 26.05  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.788 -19.457 30.347 1.00 26.19  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.425 -20.282 29.501 1.00 25.08  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 27.061 -19.676 32.797 1.00 29.05  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.376 -20.473 34.115 1.00 29.65  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.654 -20.025 32.234 1.00 28.96  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.625 -19.975 35.326 1.00 37.73  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.865 -18.148 30.106 1.00 22.83  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.507 -17.614 28.783 1.00 22.99  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.511 -17.965 27.705 1.00 27.11  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.105 -18.239 26.572 1.00 24.76  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.237 -16.119 28.851 1.00 23.53  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.938 -15.760 29.618 1.00 28.71  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.845 -14.287 29.761 1.00 29.89  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.674 -16.291 28.901 1.00 30.52  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.824 -17.995 28.044 1.00 23.38  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.858 -18.404 27.090 1.00 23.25  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.639 -19.872 26.681 1.00 25.59  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.656 -20.211 25.489 1.00 23.65  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.257 -18.158 27.685 1.00 23.39  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.427 -18.452 26.715 1.00 27.73  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.388 -17.523 25.473 1.00 26.58  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.795 -18.316 27.440 1.00 29.31  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.352 -20.730 27.663 1.00 24.05  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 30.006 -22.119 27.389 1.00 24.60  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.779 -22.205 26.454 1.00 27.09  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.794 -22.994 25.516 1.00 26.48  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.717 -22.844 28.701 1.00 28.06  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.954 -23.226 29.502 1.00 42.23  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.077 -23.184 28.930 1.00 43.20  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.800 -23.588 30.695 1.00 43.99  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.717 -21.425 26.723 1.00 23.88  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.523 -21.395 25.861 1.00 22.31  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.905 -20.999 24.418 1.00 22.81  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.414 -21.592 23.453 1.00 22.03  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.464 -20.417 26.411 1.00 22.98  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.362 -20.138 25.414 1.00 23.21  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.388 -21.097 25.139 1.00 25.97  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.344 -18.951 24.684 1.00 25.90  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.402 -20.858 24.181 1.00 26.29  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.355 -18.719 23.719 1.00 27.85  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.390 -19.668 23.480 1.00 26.36  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.746 -19.966 24.263 1.00 19.54  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.142 -19.542 22.907 1.00 19.46  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.712 -20.691 22.086 1.00 23.20  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.395 -20.804 20.904 1.00 22.89  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.226 -18.446 23.007 1.00 20.28  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.692 -17.148 23.588 1.00 22.49  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 30.042 -15.914 23.491 1.00 27.05  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.349 -14.597 24.589 1.00 27.39  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.576 -21.514 22.706 1.00 20.71  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.255 -22.603 22.015 1.00 20.95  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.508 -23.915 21.997 1.00 25.43  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.985 -24.870 21.372 1.00 23.91  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.641 -22.822 22.632 1.00 22.54  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.686 -21.834 22.150 1.00 23.97  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.826 -20.582 22.754 1.00 25.91  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.530 -22.144 21.081 1.00 24.84  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.796 -19.670 22.316 1.00 25.96  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.547 -21.267 20.680 1.00 25.88  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.647 -20.017 21.270 1.00 28.71  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.664 -19.180 20.874 1.00 26.51  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.357 -23.996 22.686 1.00 21.66  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.659 -25.294 22.762 1.00 22.02  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.146 -25.296 22.528 1.00 24.94  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.586 -26.381 22.308 1.00 25.13  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.861 -25.964 24.161 1.00 27.67  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.181 -25.212 25.173 1.00 26.25  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.338 -26.191 24.548 1.00 27.91  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.493 -24.128 22.617 0.67 21.66  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.494 -24.124 22.653 0.33 21.39  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 24.018 -23.925 22.580 0.67 21.88  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 24.032 -23.908 22.594 0.33 21.45  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.367 -24.334 23.918 0.67 24.30  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.339 -24.403 23.887 0.33 25.32  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.161 -24.155 24.073 0.67 23.27  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.110 -24.379 23.971 0.33 25.15  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.334 -24.696 21.446 0.67 23.78  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.404 -24.539 21.346 0.33 23.41  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.982 -24.558 20.197 0.67 20.98  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.093 -25.912 21.529 0.33 25.13  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.155 -24.848 24.889 0.67 21.94  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.137 -24.817 24.897 0.33 22.58  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.596 -25.283 26.178 0.67 23.15  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.646 -25.335 26.181 0.33 23.58  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.837 -24.246 27.239 0.67 26.92  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.861 -24.297 27.274 0.33 27.28  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.967 -23.771 27.412 0.67 25.11  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.992 -23.843 27.477 0.33 26.09  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.171 -26.630 26.632 0.67 25.95  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.348 -26.662 26.549 0.33 25.58  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.870 -27.785 25.680 0.67 30.51  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.224 -27.760 25.486 0.33 32.88  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.870 -28.919 25.890 0.67 40.20  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.096 -28.728 25.779 0.33 38.61  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.806 -29.448 27.254 0.67 50.97  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.949 -29.748 24.736 0.33 39.27  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 24.014 -30.446 27.628 0.67 63.14  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.245 -31.036 24.888 0.33 51.71  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.228 -31.047 26.743 0.67 50.44  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.067 -31.886 23.887 0.33 41.22  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 24.006 -30.857 28.887 0.67 48.98  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.696 -31.487 26.051 0.33 33.96  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.778 -23.919 27.971 1.00 24.29  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.824 -22.912 29.031 1.00 24.83  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.593 -23.550 30.391 1.00 29.83  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.532 -24.147 30.617 1.00 28.57  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.782 -21.825 28.732 1.00 25.74  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.780 -20.616 29.689 1.00 29.05  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.044 -19.756 29.473 1.00 26.88  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.517 -19.783 29.524 1.00 30.48  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.591 -23.442 31.291 1.00 29.36  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.490 -23.999 32.651 1.00 30.76  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.808 -22.981 33.585 1.00 35.33  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.471 -22.279 34.357 1.00 34.69  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.873 -24.438 33.175 1.00 35.35  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.832 -25.051 34.568 1.00 51.54  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.824 -25.613 35.004 1.00 43.87  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.929 -24.948 35.296 1.00 43.64  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.492 -22.855 33.438 1.00 32.08  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.665 -21.917 34.188 1.00 33.97  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.145 -22.581 35.455 1.00 38.37  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.511 -23.649 35.398 1.00 36.93  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.533 -21.426 33.275 1.00 34.99  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.816 -20.143 33.618 1.00 41.10  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.811 -18.952 33.706 1.00 41.17  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.718 -19.874 32.587 1.00 40.95  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.513 -21.999 36.613 1.00 36.10  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.154 -22.519 37.941 1.00 38.15  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.623 -21.394 38.824 1.00 39.58  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.984 -20.225 38.624 1.00 37.02  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.373 -23.177 38.618 1.00 39.84  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.988 -24.335 37.826 1.00 46.45  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.237 -24.910 38.482 1.00 64.37  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.958 -25.538 39.779 1.00 83.14  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.518 -26.784 39.942 1.00 104.41 ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.285 -27.257 41.160 1.00 92.60  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.294 -27.561 38.888 1.00 94.38  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.784 -21.733 39.818 1.00 38.18  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.241 -20.724 40.746 1.00 38.41  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.355 -19.818 41.330 1.00 42.77  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.192 -18.597 41.379 1.00 43.12  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.426 -21.398 41.878 1.00 41.82  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.729 -20.413 42.801 1.00 53.14  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.001 -21.026 43.985 1.00 85.00  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.565 -21.934 44.641 1.00 79.86  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.866 -20.582 44.268 1.00 87.36  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.484 -20.422 41.690 1.00 40.20  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.627 -19.718 42.263 1.00 40.73  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.421 -18.830 41.322 1.00 42.30  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.170 -17.968 41.786 1.00 42.64  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.268 -19.004 39.995 1.00 36.32  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 23.055 -18.192 39.054 1.00 34.45  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.216 -17.333 38.095 1.00 37.01  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.788 -16.535 37.343 1.00 34.86  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 24.029 -19.104 38.279 1.00 33.38  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.387 -20.054 37.281 1.00 42.99  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.311 -19.796 36.742 1.00 32.00  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 24.052 -21.171 36.986 1.00 34.73  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.873 -17.517 38.087 1.00 34.62  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 20.001 -16.866 37.095 1.00 34.08  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.108 -15.343 37.082 1.00 35.87  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.137 -14.755 35.994 1.00 33.01  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.527 -17.333 37.166 1.00 38.43  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.698 -16.740 35.989 1.00 38.97  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.883 -17.083 38.546 1.00 38.29  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.556 -17.595 35.526 1.00 39.96  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.198 -14.706 38.255 1.00 34.45  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.315 -13.246 38.275 1.00 35.15  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.613 -12.768 37.623 1.00 37.41  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.577 -11.825 36.823 1.00 35.44  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.142 -12.673 39.699 1.00 40.09  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.775 -12.972 40.316 1.00 47.51  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.335 -12.635 39.258 1.00 53.83  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.376 -10.842 39.194 1.00 51.80  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.753 -13.437 37.935 1.00 34.42  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.071 -13.082 37.373 1.00 33.54  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.102 -13.386 35.876 1.00 33.72  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.637 -12.597 35.099 1.00 31.57  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.181 -13.849 38.084 1.00 34.88  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.510 -14.524 35.465 1.00 28.89  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.471 -14.883 34.037 1.00 27.15  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.655 -13.840 33.252 1.00 29.88  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.125 -13.392 32.196 1.00 28.29  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.944 -16.335 33.846 1.00 30.29  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.620 -16.643 32.381 1.00 28.14  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.952 -17.343 34.386 1.00 30.96  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.452 -13.468 33.750 0.20 28.74  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.453 -13.464 33.753 0.80 29.00  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.593 -12.484 33.087 0.20 29.67  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.616 -12.485 33.056 0.80 30.52  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.297 -11.137 32.947 0.20 33.55  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.321 -11.133 32.940 0.80 33.18  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.278 -10.559 31.861 0.20 32.50  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.307 -10.539 31.864 0.80 31.54  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.252 -12.312 33.812 0.20 33.60  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.253 -12.303 33.721 0.80 34.70  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.283 -11.436 33.046 0.20 38.05  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.323 -11.412 32.902 0.80 39.19  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.740 -11.151 33.919 0.20 44.14  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.634 -11.412 33.527 0.80 45.02  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.208 -9.682  33.114 0.20 41.53  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.820 -10.374 35.059 0.80 43.33  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.931 -10.655 34.035 1.00 31.11  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.663 -9.367  34.031 1.00 31.65  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.829 -9.397  33.020 1.00 32.36  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 24.032 -8.428  32.260 1.00 31.05  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.178 -9.053  35.427 1.00 33.18  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.568 -10.526 32.984 1.00 27.72  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.682 -10.683 32.043 1.00 27.25  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.147 -10.716 30.599 1.00 28.90  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.726 -10.062 29.734 1.00 27.20  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.595 -11.877 32.403 1.00 32.18  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.892 -11.862 33.802 1.00 31.29  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.910 -11.871 31.619 1.00 31.13  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 24.042 -11.466 30.334 1.00 25.82  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.461 -11.538 28.981 1.00 24.78  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.936 -10.177 28.503 1.00 28.14  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.074 -9.846  27.323 1.00 27.11  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.361 -12.599 28.928 1.00 25.61  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.393 -9.355  29.421 1.00 26.98  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.943 -8.007  29.043 1.00 27.30  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.139 -7.139  28.620 1.00 30.29  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.103 -6.475  27.582 1.00 30.37  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.160 -7.353  30.198 1.00 30.67  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.780 -7.975  30.412 1.00 35.44  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 19.022 -7.416  31.968 1.00 43.14  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.722 -5.679  31.568 1.00 40.98  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.214 -7.192  29.403 1.00 28.30  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.454 -6.453  29.134 1.00 27.57  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 26.068 -6.922  27.792 1.00 29.45  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.461 -6.090  26.967 1.00 28.31  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.429 -6.711  30.283 1.00 27.42  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.838 -6.209  30.042 1.00 27.62  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.137 -4.847  30.104 1.00 30.77  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.883 -7.099  29.806 1.00 27.45  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.443 -4.384  29.903 1.00 29.71  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.189 -6.651  29.638 1.00 27.62  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.464 -5.293  29.692 1.00 31.30  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.756 -4.886  29.537 1.00 30.76  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.114 -8.253  27.567 1.00 25.65  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.674 -8.837  26.345 1.00 24.32  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.751 -8.715  25.131 1.00 27.90  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.172 -9.009  24.008 1.00 27.14  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.080 -10.307 26.580 1.00 22.89  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.230 -10.572 27.573 1.00 25.32  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.507 -12.093 27.674 1.00 26.38  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.536 -9.815  27.156 1.00 26.73  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.481 -8.317  25.353 1.00 25.59  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.481 -8.180  24.286 1.00 26.28  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.230 -9.539  23.601 1.00 29.15  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.478 -9.715  22.405 1.00 28.18  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.866 -7.072  23.282 1.00 27.89  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 24.000 -5.681  23.919 1.00 29.21  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.710 -4.717  22.994 1.00 39.31  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.624 -4.815  21.771 1.00 34.06  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.459 -3.782  23.554 1.00 39.15  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.798 -10.506 24.409 1.00 26.27  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.448 -11.877 24.000 1.00 26.06  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.945 -12.031 24.257 1.00 32.10  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.501 -12.508 25.318 1.00 29.79  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.297 -12.883 24.780 1.00 27.23  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.783 -12.731 24.495 1.00 28.43  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.829 -13.783 25.513 1.00 30.77  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.469 -15.459 24.747 1.00 27.64  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.157 -11.511 23.306 1.00 32.40  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.692 -11.382 23.408 1.00 34.44  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.926 -12.663 23.758 1.00 35.17  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 17.019 -12.595 24.583 1.00 34.05  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.093 -10.755 22.137 1.00 37.40  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.601 -9.348  21.868 1.00 50.78  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.267 -13.807 23.151 1.00 31.40  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.547 -15.055 23.440 1.00 32.81  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.781 -15.542 24.867 1.00 33.82  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.836 -16.010 25.510 1.00 34.89  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.869 -16.137 22.409 1.00 34.72  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.405 -15.785 21.031 1.00 39.63  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.070 -15.522 20.766 1.00 43.29  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.108 -15.688 19.879 1.00 41.22  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 16.008 -15.248 19.472 1.00 43.22  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.204 -15.352 18.894 1.00 42.20  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 19.023 -15.393 25.379 1.00 27.16  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.335 -15.748 26.772 1.00 27.77  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.543 -14.843 27.729 1.00 33.45  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.908 -15.348 28.665 1.00 31.18  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.857 -15.735 27.080 1.00 30.11  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.112 -15.975 28.571 1.00 29.85  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.588 -16.771 26.231 1.00 29.39  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.559 -13.511 27.487 1.00 30.31  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.798 -12.549 28.306 1.00 30.42  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.315 -12.968 28.370 1.00 35.60  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.766 -13.053 29.465 1.00 35.07  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.987 -11.079 27.838 1.00 33.60  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.126 -10.111 28.664 1.00 34.79  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.455 -10.670 27.918 1.00 31.90  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.720 -13.308 27.214 0.61 33.41  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.685 -13.207 27.201 0.39 33.35  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.332 -13.767 27.094 0.61 34.89  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.278 -13.611 27.068 0.39 34.87  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 14.018 -14.994 27.973 0.61 37.98  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.913 -14.827 27.926 0.39 38.88  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 13.046 -14.939 28.730 0.61 38.52  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.897 -14.793 28.621 0.39 39.84  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.982 -14.041 25.619 0.61 37.44  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.929 -13.885 25.590 0.39 37.10  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.531 -14.424 25.385 0.61 53.38  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.697 -12.658 24.725 0.39 50.26  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.641 -13.615 25.724 0.61 57.15  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.270 -11.617 25.270 0.39 53.23  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.288 -15.528 24.853 0.61 60.20  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.921 -12.746 23.498 0.39 56.98  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.833 -16.080 27.901 0.61 33.47  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.747 -15.885 27.893 0.39 34.38  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.556 -17.270 28.728 0.61 33.87  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.503 -17.120 28.645 0.39 34.72  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.750 -16.985 30.214 0.61 37.26  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.691 -16.900 30.155 0.39 37.84  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.026 -17.553 31.026 0.61 37.31  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.890 -17.419 30.932 0.39 38.09  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.305 -18.535 28.276 0.61 33.10  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.313 -18.288 28.074 0.39 39.55  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.661 -19.664 28.884 0.61 35.89  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.265 -18.226 26.646 0.39 39.46  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.789 -18.533 28.656 0.61 29.82  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.770 -19.636 28.517 0.39 40.14  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.716 -16.110 30.566 1.00 33.33  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.955 -15.748 31.983 1.00 34.00  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.737 -15.039 32.537 1.00 40.31  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.276 -15.397 33.630 1.00 38.83  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.201 -14.879 32.120 1.00 33.58  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.743 -15.792 31.926 1.00 36.08  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.195 -14.063 31.768 0.48 38.29  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.198 -14.050 31.784 0.52 38.74  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.997 -13.290 32.110 0.48 39.95  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 13.002 -13.298 32.170 0.52 40.61  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.808 -14.220 32.377 0.48 43.98  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.801 -14.228 32.393 0.52 44.23  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.091 -14.036 33.364 0.48 44.02  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.071 -14.055 33.372 0.52 44.20  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.642 -12.304 30.983 0.48 41.19  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.668 -12.222 31.131 0.52 42.99  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.597 -11.131 30.857 0.48 51.90  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.430 -10.919 31.338 0.52 57.64  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.986 -9.984  30.072 0.48 64.07  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.700 -9.741  30.713 0.52 69.28  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.990 -8.982  29.708 0.48 67.39  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.830 -9.724  29.253 0.52 75.40  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.341 -7.948  30.468 0.48 76.49  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.617 -8.894  28.576 0.52 85.54  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.764 -7.756  31.648 0.48 67.33  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.346 -7.987  29.217 0.52 70.75  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.269 -7.098  30.052 0.48 56.62  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.675 -8.957  27.253 0.52 69.27  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.626 -15.232 31.509 1.00 40.10  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.532 -16.218 31.610 1.00 41.98  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.684 -17.148 32.817 1.00 45.66  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.690  -17.409 33.498 1.00 45.86  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.384 -17.018 30.304 1.00 44.19  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.841  -16.164 29.164 1.00 65.18  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.678  -16.923 27.863 1.00 77.42  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.270  -15.981 26.755 1.00 91.35  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.453  -16.662 25.718 1.00 103.98 ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.921 -17.633 33.094 1.00 40.65  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.192 -18.496 34.254 1.00 41.19  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 11.999 -17.726 35.563 1.00 46.30  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.448 -18.279 36.520 1.00 46.51  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.590 -19.124 34.172 1.00 41.48  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.721 -20.392 33.341 1.00 43.25  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.162 -20.477 32.066 1.00 46.38  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.456 -21.479 33.810 1.00 46.07  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.303 -21.640 31.295 1.00 46.91  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.598 -22.641 33.035 1.00 47.82  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 14.019 -22.713 31.787 1.00 45.36  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.399 -16.436 35.590 1.00 41.49  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.197 -15.578 36.774 1.00 42.88  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.697 -15.323 37.020 1.00 50.48  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.244 -15.443 38.164 1.00 52.03  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.049 -14.283 36.687 1.00 44.96  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.544 -14.644 36.815 1.00 43.43  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.638 -13.245 37.770 1.00 48.29  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.503 -13.618 36.269 1.00 49.00  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.925  -15.029 35.944 1.00 48.43  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.478  -14.784 36.022 1.00 51.17  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.712  -16.008 36.551 1.00 56.00  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.747  -15.840 37.293 1.00 56.69  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.914  -14.342 34.665 1.00 54.44  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.164  -17.227 36.199 1.00 51.36  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.541  -18.476 36.655 1.00 52.98  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.708  -18.710 38.169 1.00 59.27  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.849  -19.337 38.776 1.00 59.76  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.111  -19.658 35.881 1.00 52.28  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.813  -18.229 38.763 1.00 57.99  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.123  -18.425 40.182 1.00 60.81  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.505  -17.383 41.131 1.00 69.24  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.429  -17.650 42.334 1.00 71.70  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.633 -18.512 40.393 1.00 64.13  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 11.096 -19.838 40.190 1.00 73.66  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.037  -16.225 40.607 1.00 65.95  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.432  -15.161 41.423 1.00 87.79  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 5.996  -15.476 41.881 1.00 129.72 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.613  -16.636 42.028 1.00 96.51  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.507  -13.793 40.714 1.00 88.40  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.488  -13.584 39.601 1.00 98.67  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.642  -12.339 38.743 1.00 120.16 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.774  -11.813 38.631 1.00 113.27 ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.622  -11.902 38.163 1.00 114.09 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.256 -35.148 5.855  1.00 30.77  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.337 -34.011 6.342  1.00 31.71  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.464 -36.381 6.727  1.00 29.87  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.975 -35.384 4.575  0.66 27.97  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.999 -35.380 4.568  0.34 29.37  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.761 -34.331 3.583  0.66 27.19  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.729 -34.303 3.616  0.34 29.28  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.255 -34.181 3.301  0.66 31.26  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.225 -34.154 3.441  0.34 31.44  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.538 -35.187 3.247  0.66 31.17  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.486 -35.139 3.549  0.34 30.82  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.544 -34.661 2.287  0.66 26.13  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.419 -34.532 2.246  0.34 28.88  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.045 -34.645 2.467  0.66 26.19  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.807 -35.606 1.396  0.34 30.29  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.835 -35.680 2.879  0.66 28.58  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.181 -36.915 1.339  0.34 33.44  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.924 -33.530 2.255  0.66 25.87  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.719 -35.459 0.466  0.34 30.32  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.146 -35.264 2.981  0.66 27.54  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.375 -37.603 0.464  0.34 33.09  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.232 -33.958 2.575  0.66 28.72  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.472 -36.733 -0.093 0.34 34.48  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.728 -32.193 1.868  0.66 26.64  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.907 -34.379 0.075  0.34 31.43  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.347 -33.122 2.442  0.66 28.34  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.458 -36.954 -1.034 0.34 33.83  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.836 -31.376 1.706  0.66 27.51  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.895 -34.603 -0.848 0.34 33.04  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.120 -31.825 2.037  0.66 28.09  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.683 -35.876 -1.397 0.34 33.65  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.773 -32.934 3.143  1.00 26.54  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.339 -32.641 2.902  1.00 26.58  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.189 -31.581 1.800  1.00 29.02  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.160 -30.893 1.461  1.00 28.29  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.629 -32.140 4.209  1.00 29.80  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.671 -33.191 5.328  1.00 30.17  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.209 -30.794 4.700  1.00 29.13  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.951 -31.394 1.333  1.00 27.32  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.567 -30.311 0.440  1.00 27.44  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.195 -29.165 1.425  1.00 32.46  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.185 -29.287 2.135  1.00 32.47  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.359 -30.682 -0.468 1.00 29.53  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.657 -31.953 -1.354 1.00 27.46  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.948 -29.446 -1.319 1.00 31.20  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.941 -31.853 -2.330 1.00 33.47  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.980 -28.066 1.502  1.00 31.49  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.653 -27.005 2.475  1.00 32.08  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.401 -26.208 2.102  1.00 36.68  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.100 -26.070 0.922  1.00 35.24  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.917 -26.132 2.478  1.00 33.47  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.463 -26.294 1.068  1.00 37.62  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.221 -27.750 0.754  1.00 33.45  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.707 -25.636 3.104  1.00 35.95  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.508 -10.175 16.510 1.00 28.57  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.917 -8.907  16.547 1.00 27.95  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.893 -8.624  17.443 1.00 31.26  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.449 -9.637  18.288 1.00 31.61  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.278 -10.815 19.857 1.00 34.74  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.988 -10.918 18.228 1.00 30.15  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.304 -10.291 11.948 1.00 30.52  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.449 -10.613 13.286 1.00 28.74  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.416 -10.263 14.183 1.00 29.74  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.274 -11.772 19.236 1.00 32.71  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.451 -11.075 20.731 1.00 35.23  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.445 -9.603  19.265 1.00 32.10  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 25.016 -11.195 17.332 1.00 27.97  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.412 -10.578 15.507 1.00 26.93  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.323 -9.649  13.694 1.00 32.54  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.308 -9.405  12.396 1.00 34.42  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.863 -8.635  11.813 0.44 35.03  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 29.002 -11.515 13.854 0.66 27.52  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.216 -9.672  11.474 1.00 34.20  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.383 -15.379 22.712 1.00 40.29  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.534 -35.419 -1.261 0.66 49.52  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.249 -35.185 -0.614 0.66 50.38  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.682 -34.542 -0.234 0.66 49.36  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 17.944 -37.063 -0.791 0.66 49.12  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 35.708 -25.841 25.603 1.00 42.49  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 25.882 -3.547  26.543 1.00 37.34  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 20.838 -5.919  26.302 1.00 42.90  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 22.736 -5.524  20.026 1.00 53.91  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 38.554 -15.011 15.503 1.00 39.50  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 44.426 -0.891  17.988 1.00 54.93  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 37.841 2.403   19.822 1.00 42.85  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 26.827 -32.154 16.186 1.00 46.13  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 37.742 -20.513 27.012 1.00 37.31  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 16.462 -27.586 -3.238 1.00 52.63  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 29.877 -32.331 9.558  1.00 52.91  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 41.170 -21.731 25.249 1.00 48.43  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 45.061 -11.169 18.873 1.00 63.12  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 37.273 -12.511 40.379 1.00 64.14  ? 314 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 6 .   ? 23.514 -5.907  33.045 1.00 39.83  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 17.925 -29.505 7.710  1.00 36.49  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 33.362 -20.924 29.629 1.00 48.75  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 22.721 -27.762 17.810 1.00 51.22  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 15.498 -10.111 25.038 1.00 51.97  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 43.711 -6.663  31.987 1.00 51.11  ? 320 HOH   A O   1 
HETATM 1221 O  O   A HOH   F 6 .   ? 19.089 -23.045 4.327  0.67 50.30  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 21.680 -29.578 -5.246 1.00 40.48  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 31.740 -0.967  15.941 1.00 45.63  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 30.388 1.343   33.942 1.00 71.33  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 22.961 -28.290 12.667 1.00 25.14  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 25.693 -3.000  20.067 1.00 59.31  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 21.525 -27.233 14.683 0.50 38.18  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 20.426 -13.583 20.611 1.00 54.63  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 28.351 -8.992  40.038 1.00 49.11  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 19.877 -9.730  37.144 1.00 43.13  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 32.825 -24.538 32.239 1.00 63.72  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 27.342 -28.280 18.666 1.00 29.10  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 28.909 -21.828 41.724 1.00 78.58  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 27.049 -35.409 11.669 1.00 62.74  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 27.211 -10.243 35.970 1.00 41.34  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 41.433 -12.840 14.131 1.00 110.78 ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 28.297 -23.893 31.738 1.00 44.56  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 41.320 -16.937 15.255 1.00 40.00  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 21.530 -30.000 14.222 1.00 77.18  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 26.944 -16.693 38.803 1.00 55.20  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 34.563 -23.898 29.817 1.00 75.75  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 26.178 -21.951 38.738 1.00 42.96  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 29.012 -0.369  16.991 1.00 76.41  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 23.396 -17.216 44.408 1.00 67.24  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 24.055 -15.908 21.364 1.00 35.40  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 29.442 -27.475 20.683 1.00 27.62  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 36.888 -5.735  12.287 1.00 41.88  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 41.217 -1.473  11.724 1.00 70.95  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 21.961 -25.053 18.379 1.00 24.89  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 24.955 -26.911 19.097 1.00 38.13  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 20.247 -16.055 41.001 1.00 39.13  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 37.399 -6.471  34.392 1.00 44.64  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 30.326 -0.692  37.144 1.00 58.54  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 42.538 -10.612 15.621 1.00 54.45  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 20.855 -7.395  19.860 1.00 53.84  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 44.448 -12.766 41.463 1.00 56.36  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 30.720 -29.033 22.723 1.00 43.11  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 44.009 -4.385  25.858 1.00 51.06  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 12.211 -18.094 25.941 1.00 61.33  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 46.017 -14.237 21.600 1.00 60.89  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 29.109 -31.224 7.254  1.00 37.06  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 46.899 -21.630 18.180 1.00 52.19  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 28.544 -24.406 34.460 1.00 57.11  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 26.188 -22.739 30.018 1.00 30.82  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 10.815 -11.542 34.614 1.00 51.44  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 41.380 -7.822  46.514 1.00 58.52  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 46.306 -15.954 27.661 1.00 75.20  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 12.743 -20.674 42.422 1.00 60.51  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 18.048 -34.613 8.344  1.00 36.46  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 34.818 -19.037 13.908 0.50 26.99  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 37.584 3.323   15.848 1.00 46.50  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 14.377 -16.911 23.553 1.00 46.44  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 11.592 -15.275 40.642 1.00 82.21  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 39.054 -18.945 33.499 1.00 47.37  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 34.190 -8.014  35.730 1.00 38.58  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 43.878 -10.736 35.180 1.00 72.18  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 27.168 -2.385  16.160 1.00 68.52  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 24.105 -28.725 21.655 1.00 56.65  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 45.373 -12.639 23.686 1.00 51.35  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 26.182 -8.121  9.079  1.00 44.16  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 45.554 -10.906 30.341 1.00 57.98  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 26.142 -19.327 41.796 1.00 61.50  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 26.499 -30.866 19.010 1.00 62.65  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 44.607 -8.668  17.940 1.00 67.60  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 31.908 -31.951 14.576 1.00 39.42  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 16.658 -6.520  27.602 1.00 63.64  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 27.718 -23.135 13.907 0.50 29.72  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 38.042 -16.692 13.131 0.50 29.47  ? 388 HOH   A O   1 
HETATM 1289 O  O   A HOH   F 6 .   ? 12.180 -20.849 27.987 0.66 48.70  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 47.266 -25.242 21.628 1.00 53.88  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 19.899 -25.619 41.352 1.00 80.08  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 29.710 -22.663 36.948 1.00 67.77  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 46.399 -19.029 19.711 1.00 55.43  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 4.315  -20.487 37.940 1.00 67.11  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 44.678 -16.425 29.784 1.00 57.42  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 41.289 -7.032  36.037 1.00 46.73  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 23.719 -15.753 17.853 1.00 44.55  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 40.476 -19.645 29.092 1.00 38.08  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 34.765 -29.215 26.103 1.00 66.57  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 17.408 -24.677 -2.163 1.00 69.53  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 46.169 -9.034  44.243 1.00 56.25  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 33.128 -29.871 21.569 1.00 43.87  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 42.171 -5.898  11.874 1.00 72.36  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 37.085 -2.356  11.619 1.00 61.08  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 22.979 -15.019 40.478 1.00 36.61  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 30.382 -10.685 40.702 1.00 46.80  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 41.311 -17.150 35.252 1.00 48.87  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 25.664 -4.675  17.965 1.00 53.24  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 47.544 -6.739  20.383 1.00 70.18  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 35.172 -29.831 23.495 1.00 45.67  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 35.292 1.853   13.567 1.00 60.85  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 46.981 -20.226 22.055 1.00 68.05  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 27.050 -1.700  22.024 1.00 57.04  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 45.940 -17.086 17.321 1.00 75.47  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 21.183 -23.349 42.163 1.00 50.55  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 32.221 -15.752 39.943 1.00 39.31  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 42.094 -8.106  13.839 1.00 63.65  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 19.657 -27.358 10.067 1.00 53.89  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 33.588 -33.130 12.141 1.00 50.40  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 27.385 -25.585 28.486 1.00 61.50  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 32.419 -9.088  39.901 1.00 63.70  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 34.019 -32.919 21.962 1.00 65.28  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 34.490 -18.782 36.377 1.00 65.74  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 33.548 -0.359  20.173 1.00 47.67  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 25.689 -16.151 41.182 1.00 54.15  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 10.557 -11.799 40.213 1.00 66.13  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 23.607 -30.592 19.358 1.00 68.59  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 31.813 -26.047 27.167 1.00 60.00  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 29.504 -0.753  22.349 1.00 63.52  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 39.955 -5.568  34.033 1.00 45.13  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 42.819 -18.326 30.771 1.00 52.70  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 45.896 -5.557  23.838 1.00 52.06  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 22.330 -10.559 14.650 1.00 49.14  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 26.488 -29.526 22.722 1.00 59.33  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 32.048 -0.040  13.387 1.00 70.27  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 37.193 -31.642 23.446 1.00 85.84  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 44.470 -4.288  29.064 1.00 66.70  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 23.181 -3.161  26.836 1.00 69.20  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 26.997 -34.525 18.035 1.00 69.68  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 28.811 -2.661  13.118 1.00 77.03  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 19.489 -31.760 13.865 1.00 72.38  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 30.671 -34.366 14.933 1.00 67.25  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 19.830 -8.190  24.660 1.00 55.77  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 35.393 -4.220  10.652 1.00 53.43  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 36.911 -24.542 27.676 1.00 64.80  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 48.067 -23.505 19.734 1.00 62.85  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 47.517 -28.558 17.688 1.00 62.80  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 46.740 -14.683 18.366 1.00 65.30  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 24.544 -21.882 41.130 1.00 61.38  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 32.148 -1.078  22.371 1.00 58.67  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 11.986 -18.945 22.866 1.00 69.09  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 19.496 -7.798  35.312 1.00 56.24  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 34.169 -17.652 39.673 1.00 70.62  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 47.073 -12.597 28.541 1.00 64.04  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 47.334 -11.914 25.425 1.00 70.62  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 44.005 -13.733 13.908 0.50 98.41  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 35.868 -21.304 30.658 1.00 63.72  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 25.436 -5.721  34.988 1.00 63.97  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 45.695 -8.421  31.373 1.00 68.67  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 20.131 -35.388 10.149 1.00 43.74  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 43.267 -3.057  33.968 1.00 61.25  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 17.158 -8.030  25.034 1.00 64.89  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 17.112 -28.213 9.946  1.00 54.55  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 19.977 -14.940 43.456 1.00 53.66  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 33.895 -11.226 41.722 0.50 62.21  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 28.326 -29.879 24.709 1.00 75.97  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 19.145 -28.325 13.875 0.50 73.09  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 33.895 -14.030 41.723 0.50 43.86  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 32.650 -20.712 36.997 1.00 79.72  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 32.087 -23.899 35.052 1.00 76.88  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 16.758 -6.918  35.020 1.00 80.31  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 21.261 -5.785  34.799 1.00 55.03  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 12.535 -18.349 19.934 1.00 66.71  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 45.262 -12.458 15.974 1.00 77.68  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 39.487 -5.556  11.509 1.00 71.41  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   F 6 .   ? 16.710 -30.126 12.439 1.00 62.97  ? 476 HOH   A O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 12.184 -24.332 0.100  1.00 57.44  ? 201 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 22.651 -34.079 8.856  1.00 36.44  ? 202 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 14.970 -25.857 -1.785 1.00 46.31  ? 203 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 17.737 -36.370 6.038  1.00 45.62  ? 204 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 11.503 -23.588 3.158  1.00 55.87  ? 205 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 20.860 -38.360 4.025  1.00 51.12  ? 206 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 20.876 -39.575 -2.085 1.00 60.40  ? 207 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 10.612 -24.764 5.525  1.00 60.12  ? 208 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.689 -36.534 9.975  1.00 50.92  ? 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   ? 0.8468 1.0317 0.7563 0.0235  -0.1369 -0.0180 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8409 1.0198 0.7321 0.0068  -0.1275 -0.0214 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8173 1.0254 0.7320 -0.0048 -0.1228 -0.0386 6   ASP A C   
4    O O   . ASP A 5   ? 0.8088 1.0421 0.7525 -0.0007 -0.1271 -0.0477 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8637 1.0137 0.7461 -0.0010 -0.1100 -0.0154 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0629 1.1935 0.9111 -0.0117 -0.1046 -0.0113 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0640 1.2068 0.9095 -0.0235 -0.1012 -0.0210 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1754 1.2782 0.9993 -0.0093 -0.1025 0.0006  6   ASP A OD2 
9    N N   . SER A 6   ? 0.7108 0.9145 0.6127 -0.0198 -0.1132 -0.0438 7   SER A N   
10   C CA  . SER A 6   ? 0.6615 0.8862 0.5812 -0.0325 -0.1064 -0.0597 7   SER A CA  
11   C C   . SER A 6   ? 0.6037 0.8141 0.5353 -0.0420 -0.0871 -0.0630 7   SER A C   
12   O O   . SER A 6   ? 0.5888 0.8040 0.5241 -0.0544 -0.0782 -0.0737 7   SER A O   
13   C CB  . SER A 6   ? 0.7346 0.9663 0.6316 -0.0418 -0.1108 -0.0650 7   SER A CB  
14   O OG  . SER A 6   ? 0.8932 1.0987 0.7612 -0.0483 -0.1028 -0.0578 7   SER A OG  
15   N N   . CYS A 7   ? 0.4972 0.6900 0.4348 -0.0355 -0.0814 -0.0544 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4605 0.6392 0.4082 -0.0421 -0.0658 -0.0563 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4419 0.6350 0.4155 -0.0481 -0.0596 -0.0686 8   CYS A C   
18   O O   . CYS A 7   ? 0.4344 0.6486 0.4237 -0.0452 -0.0663 -0.0745 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4761 0.6355 0.4243 -0.0334 -0.0632 -0.0449 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5634 0.6965 0.4791 -0.0315 -0.0632 -0.0315 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3374 0.5184 0.3150 -0.0564 -0.0466 -0.0729 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2939 0.4777 0.2912 -0.0618 -0.0384 -0.0816 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3192 0.4841 0.3215 -0.0560 -0.0327 -0.0733 9   ILE A C   
24   O O   . ILE A 8   ? 0.3176 0.4672 0.3081 -0.0515 -0.0324 -0.0639 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3276 0.5099 0.3254 -0.0743 -0.0292 -0.0931 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3388 0.5004 0.3242 -0.0766 -0.0215 -0.0901 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3306 0.5355 0.3260 -0.0810 -0.0352 -0.1034 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.4206 0.5770 0.4073 -0.0870 -0.0119 -0.1015 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2579 0.4225 0.2757 -0.0575 -0.0274 -0.0771 10  GLN A N   
30   N N   B GLN A 9   ? 0.2636 0.4303 0.2820 -0.0569 -0.0285 -0.0770 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2490 0.3960 0.2698 -0.0527 -0.0225 -0.0697 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2522 0.4028 0.2747 -0.0520 -0.0238 -0.0701 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2891 0.4225 0.3146 -0.0598 -0.0122 -0.0748 10  GLN A C   
34   C C   B GLN A 9   ? 0.2967 0.4333 0.3235 -0.0593 -0.0133 -0.0750 10  GLN A C   
35   O O   A GLN A 9   ? 0.2950 0.4360 0.3280 -0.0675 -0.0085 -0.0844 10  GLN A O   
36   O O   B GLN A 9   ? 0.2974 0.4410 0.3313 -0.0673 -0.0092 -0.0848 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2632 0.4196 0.2950 -0.0448 -0.0276 -0.0667 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2604 0.4233 0.2958 -0.0451 -0.0288 -0.0690 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.3230 0.4642 0.3605 -0.0428 -0.0209 -0.0627 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2720 0.4187 0.3070 -0.0377 -0.0268 -0.0594 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5920 0.7352 0.6343 -0.0327 -0.0257 -0.0562 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4462 0.5951 0.4961 -0.0390 -0.0215 -0.0637 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.5016 0.6574 0.5444 -0.0253 -0.0350 -0.0542 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3151 0.4840 0.3792 -0.0407 -0.0230 -0.0722 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.5521 0.6812 0.5969 -0.0316 -0.0197 -0.0527 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.4116 0.5407 0.4584 -0.0388 -0.0150 -0.0586 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2697 0.3824 0.2899 -0.0573 -0.0077 -0.0687 11  PHE A N   
48   N N   B PHE A 10  ? 0.2646 0.3807 0.2860 -0.0565 -0.0090 -0.0684 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2555 0.3515 0.2772 -0.0618 0.0002  -0.0718 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2583 0.3568 0.2804 -0.0608 -0.0009 -0.0709 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2844 0.3743 0.3111 -0.0590 0.0019  -0.0678 11  PHE A C   
52   C C   B PHE A 10  ? 0.2912 0.3839 0.3188 -0.0583 0.0010  -0.0675 11  PHE A C   
53   O O   A PHE A 10  ? 0.2629 0.3442 0.2870 -0.0523 0.0004  -0.0596 11  PHE A O   
54   O O   B PHE A 10  ? 0.2772 0.3639 0.3031 -0.0513 -0.0012 -0.0592 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2716 0.3506 0.2858 -0.0602 0.0029  -0.0694 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2807 0.3632 0.2948 -0.0585 0.0011  -0.0674 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2888 0.3491 0.3025 -0.0636 0.0093  -0.0732 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3078 0.3940 0.3176 -0.0635 0.0025  -0.0742 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3289 0.3879 0.3425 -0.0715 0.0138  -0.0825 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3492 0.4509 0.3539 -0.0646 -0.0023 -0.0751 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3016 0.3437 0.3128 -0.0586 0.0102  -0.0674 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3530 0.4255 0.3623 -0.0668 0.0083  -0.0797 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3503 0.3869 0.3602 -0.0740 0.0196  -0.0851 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3658 0.4707 0.3649 -0.0705 -0.0001 -0.0823 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3381 0.3597 0.3455 -0.0604 0.0145  -0.0697 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3958 0.4718 0.4020 -0.0717 0.0107  -0.0874 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3277 0.3450 0.3337 -0.0677 0.0192  -0.0781 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3653 0.4580 0.3664 -0.0743 0.0071  -0.0889 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2516 0.3469 0.2854 -0.0653 0.0059  -0.0747 12  THR A N   
70   C CA  . THR A 11  ? 0.2542 0.3461 0.2933 -0.0653 0.0093  -0.0736 12  THR A CA  
71   C C   . THR A 11  ? 0.3003 0.3677 0.3306 -0.0618 0.0122  -0.0656 12  THR A C   
72   O O   . THR A 11  ? 0.2923 0.3597 0.3249 -0.0565 0.0109  -0.0604 12  THR A O   
73   C CB  . THR A 11  ? 0.3493 0.4455 0.3941 -0.0765 0.0167  -0.0845 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3603 0.4830 0.4150 -0.0795 0.0128  -0.0931 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.4011 0.4968 0.4519 -0.0783 0.0217  -0.0855 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2778 0.3249 0.2983 -0.0640 0.0153  -0.0652 13  ARG A N   
77   C CA  . ARG A 12  ? 0.2943 0.3186 0.3059 -0.0605 0.0165  -0.0585 13  ARG A CA  
78   C C   . ARG A 12  ? 0.3152 0.3380 0.3250 -0.0515 0.0109  -0.0513 13  ARG A C   
79   O O   . ARG A 12  ? 0.3040 0.3107 0.3076 -0.0481 0.0105  -0.0466 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3666 0.3678 0.3678 -0.0651 0.0210  -0.0613 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.4928 0.4870 0.4908 -0.0762 0.0292  -0.0681 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.7727 0.7584 0.7663 -0.0792 0.0335  -0.0656 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.9504 0.9087 0.9286 -0.0748 0.0323  -0.0578 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.0891 1.0395 1.0614 -0.0746 0.0337  -0.0534 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.9548 0.8808 0.9116 -0.0705 0.0312  -0.0467 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8413 0.8090 0.8237 -0.0778 0.0371  -0.0563 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2625 0.3010 0.2763 -0.0485 0.0066  -0.0508 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2613 0.2973 0.2722 -0.0426 0.0035  -0.0456 14  HIS A CA  
89   C C   . HIS A 13  ? 0.2969 0.3261 0.3065 -0.0378 0.0025  -0.0388 14  HIS A C   
90   O O   . HIS A 13  ? 0.2780 0.2968 0.2846 -0.0350 0.0021  -0.0365 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2556 0.3067 0.2664 -0.0418 0.0001  -0.0458 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.2820 0.3293 0.2886 -0.0383 -0.0008 -0.0417 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.2861 0.3278 0.2923 -0.0390 0.0012  -0.0454 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2848 0.3334 0.2879 -0.0347 -0.0028 -0.0356 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2834 0.3252 0.2869 -0.0370 0.0010  -0.0423 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2768 0.3208 0.2768 -0.0349 -0.0010 -0.0358 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2517 0.2884 0.2650 -0.0365 0.0020  -0.0366 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2571 0.2870 0.2691 -0.0324 0.0020  -0.0309 15  ALA A CA  
99   C C   . ALA A 14  ? 0.2875 0.3005 0.2942 -0.0342 0.0049  -0.0304 15  ALA A C   
100  O O   . ALA A 14  ? 0.2671 0.2716 0.2698 -0.0313 0.0038  -0.0267 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2676 0.3081 0.2863 -0.0303 0.0015  -0.0305 15  ALA A CB  
102  N N   A SER A 15  ? 0.2789 0.2863 0.2838 -0.0396 0.0085  -0.0344 16  SER A N   
103  N N   B SER A 15  ? 0.2721 0.2794 0.2769 -0.0396 0.0085  -0.0345 16  SER A N   
104  N N   C SER A 15  ? 0.2715 0.2787 0.2763 -0.0396 0.0085  -0.0344 16  SER A N   
105  C CA  A SER A 15  ? 0.2887 0.2762 0.2834 -0.0420 0.0109  -0.0334 16  SER A CA  
106  C CA  B SER A 15  ? 0.2818 0.2692 0.2765 -0.0421 0.0110  -0.0335 16  SER A CA  
107  C CA  C SER A 15  ? 0.2811 0.2684 0.2757 -0.0419 0.0109  -0.0332 16  SER A CA  
108  C C   A SER A 15  ? 0.3359 0.3113 0.3246 -0.0382 0.0070  -0.0319 16  SER A C   
109  C C   B SER A 15  ? 0.3370 0.3121 0.3255 -0.0384 0.0071  -0.0320 16  SER A C   
110  C C   C SER A 15  ? 0.3373 0.3122 0.3257 -0.0383 0.0071  -0.0320 16  SER A C   
111  O O   A SER A 15  ? 0.3071 0.2698 0.2884 -0.0355 0.0049  -0.0285 16  SER A O   
112  O O   B SER A 15  ? 0.3184 0.2806 0.2994 -0.0358 0.0051  -0.0286 16  SER A O   
113  O O   C SER A 15  ? 0.3201 0.2817 0.3008 -0.0358 0.0051  -0.0286 16  SER A O   
114  C CB  A SER A 15  ? 0.3501 0.3317 0.3414 -0.0502 0.0169  -0.0385 16  SER A CB  
115  C CB  B SER A 15  ? 0.3348 0.3167 0.3263 -0.0503 0.0169  -0.0388 16  SER A CB  
116  C CB  C SER A 15  ? 0.3366 0.3179 0.3277 -0.0501 0.0170  -0.0381 16  SER A CB  
117  O OG  A SER A 15  ? 0.4155 0.3733 0.3919 -0.0529 0.0192  -0.0364 16  SER A OG  
118  O OG  B SER A 15  ? 0.3738 0.3694 0.3739 -0.0539 0.0208  -0.0421 16  SER A OG  
119  O OG  C SER A 15  ? 0.3917 0.3743 0.3837 -0.0534 0.0177  -0.0430 16  SER A OG  
120  N N   . ASP A 16  ? 0.3020 0.2826 0.2944 -0.0378 0.0058  -0.0355 17  ASP A N   
121  C CA  . ASP A 16  ? 0.3121 0.2845 0.3030 -0.0333 0.0022  -0.0365 17  ASP A CA  
122  C C   . ASP A 16  ? 0.3123 0.2917 0.3075 -0.0280 -0.0015 -0.0338 17  ASP A C   
123  O O   . ASP A 16  ? 0.3125 0.2833 0.3057 -0.0235 -0.0052 -0.0335 17  ASP A O   
124  C CB  . ASP A 16  ? 0.3332 0.3125 0.3290 -0.0351 0.0033  -0.0425 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.4732 0.4414 0.4635 -0.0410 0.0075  -0.0466 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.4706 0.4234 0.4516 -0.0440 0.0099  -0.0445 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.5092 0.4833 0.5031 -0.0438 0.0093  -0.0526 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2563 0.2503 0.2565 -0.0285 -0.0007 -0.0324 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2459 0.2445 0.2484 -0.0255 -0.0022 -0.0303 18  VAL A CA  
130  C C   . VAL A 17  ? 0.3104 0.2988 0.3083 -0.0238 -0.0035 -0.0267 18  VAL A C   
131  O O   . VAL A 17  ? 0.2893 0.2756 0.2880 -0.0211 -0.0063 -0.0275 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2696 0.2798 0.2734 -0.0266 -0.0008 -0.0279 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2684 0.2779 0.2712 -0.0252 -0.0005 -0.0251 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2737 0.2935 0.2789 -0.0286 -0.0003 -0.0316 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2799 0.2639 0.2738 -0.0260 -0.0011 -0.0240 19  LEU A N   
136  C CA  . LEU A 18  ? 0.2965 0.2707 0.2841 -0.0258 -0.0012 -0.0212 19  LEU A CA  
137  C C   . LEU A 18  ? 0.3133 0.2723 0.2922 -0.0243 -0.0051 -0.0215 19  LEU A C   
138  O O   . LEU A 18  ? 0.2985 0.2532 0.2740 -0.0220 -0.0086 -0.0205 19  LEU A O   
139  C CB  . LEU A 18  ? 0.3061 0.2796 0.2923 -0.0293 0.0035  -0.0201 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3597 0.3252 0.3400 -0.0300 0.0051  -0.0178 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.3505 0.3223 0.3353 -0.0272 0.0045  -0.0162 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.4067 0.3719 0.3869 -0.0341 0.0111  -0.0191 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.2954 0.2458 0.2700 -0.0254 -0.0050 -0.0232 20  LEU A N   
144  C CA  . LEU A 19  ? 0.3222 0.2543 0.2861 -0.0224 -0.0097 -0.0228 20  LEU A CA  
145  C C   . LEU A 19  ? 0.3480 0.2866 0.3199 -0.0150 -0.0167 -0.0252 20  LEU A C   
146  O O   . LEU A 19  ? 0.3544 0.2842 0.3199 -0.0108 -0.0229 -0.0240 20  LEU A O   
147  C CB  . LEU A 19  ? 0.3566 0.2789 0.3164 -0.0248 -0.0073 -0.0252 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4794 0.3766 0.4244 -0.0212 -0.0120 -0.0240 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.5273 0.4043 0.4523 -0.0245 -0.0116 -0.0190 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.5404 0.4271 0.4816 -0.0248 -0.0077 -0.0272 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.2919 0.2472 0.2777 -0.0141 -0.0156 -0.0294 21  ASN A N   
152  C CA  . ASN A 20  ? 0.2717 0.2364 0.2679 -0.0086 -0.0204 -0.0340 21  ASN A CA  
153  C C   . ASN A 20  ? 0.3009 0.2737 0.2999 -0.0087 -0.0216 -0.0334 21  ASN A C   
154  O O   . ASN A 20  ? 0.3059 0.2811 0.3092 -0.0038 -0.0277 -0.0367 21  ASN A O   
155  C CB  . ASN A 20  ? 0.2869 0.2658 0.2947 -0.0096 -0.0170 -0.0396 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.4271 0.3974 0.4345 -0.0074 -0.0177 -0.0432 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.3997 0.3528 0.3998 -0.0025 -0.0226 -0.0423 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3595 0.3397 0.3729 -0.0109 -0.0130 -0.0474 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2863 0.2632 0.2835 -0.0138 -0.0162 -0.0298 22  LEU A N   
160  C CA  . LEU A 21  ? 0.2810 0.2625 0.2791 -0.0150 -0.0160 -0.0294 22  LEU A CA  
161  C C   . LEU A 21  ? 0.3160 0.2851 0.3040 -0.0130 -0.0214 -0.0275 22  LEU A C   
162  O O   . LEU A 21  ? 0.3102 0.2839 0.3009 -0.0117 -0.0253 -0.0303 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2818 0.2658 0.2781 -0.0197 -0.0093 -0.0254 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.3085 0.3030 0.3104 -0.0216 -0.0051 -0.0262 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.3334 0.3268 0.3315 -0.0236 -0.0008 -0.0212 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.3324 0.3367 0.3415 -0.0227 -0.0044 -0.0315 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.2955 0.2488 0.2706 -0.0139 -0.0212 -0.0233 23  ASN A N   
168  C CA  . ASN A 22  ? 0.3145 0.2520 0.2746 -0.0130 -0.0263 -0.0208 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3709 0.3047 0.3310 -0.0048 -0.0371 -0.0236 23  ASN A C   
170  O O   . ASN A 22  ? 0.3845 0.3150 0.3384 -0.0021 -0.0442 -0.0238 23  ASN A O   
171  C CB  . ASN A 22  ? 0.3589 0.2785 0.3032 -0.0175 -0.0220 -0.0166 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4591 0.3620 0.3844 -0.0193 -0.0247 -0.0136 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.4170 0.3251 0.3425 -0.0196 -0.0265 -0.0143 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4853 0.3665 0.3919 -0.0215 -0.0244 -0.0106 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.3426 0.2781 0.3104 -0.0003 -0.0389 -0.0265 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3481 0.2820 0.3201 0.0095  -0.0493 -0.0305 24  ARG A CA  
177  C C   . ARG A 23  ? 0.3862 0.3425 0.3757 0.0123  -0.0533 -0.0376 24  ARG A C   
178  O O   . ARG A 23  ? 0.3911 0.3472 0.3807 0.0194  -0.0639 -0.0403 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3440 0.2771 0.3237 0.0127  -0.0479 -0.0339 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.4013 0.3084 0.3621 0.0109  -0.0458 -0.0285 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.4099 0.3186 0.3792 0.0111  -0.0416 -0.0328 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.5442 0.4259 0.4950 0.0090  -0.0395 -0.0290 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.7570 0.6360 0.7095 0.0048  -0.0327 -0.0316 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.5903 0.4924 0.5612 0.0023  -0.0278 -0.0374 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.6786 0.5309 0.6127 0.0017  -0.0301 -0.0288 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.3181 0.2932 0.3210 0.0060  -0.0448 -0.0409 25  LEU A N   
187  C CA  . LEU A 24  ? 0.3174 0.3130 0.3357 0.0056  -0.0458 -0.0486 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3727 0.3652 0.3820 0.0037  -0.0495 -0.0467 25  LEU A C   
189  O O   . LEU A 24  ? 0.3637 0.3672 0.3812 0.0074  -0.0571 -0.0534 25  LEU A O   
190  C CB  . LEU A 24  ? 0.3061 0.3153 0.3333 -0.0025 -0.0346 -0.0506 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.3612 0.3773 0.3977 -0.0024 -0.0303 -0.0544 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.3517 0.3783 0.3916 -0.0111 -0.0199 -0.0553 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.3745 0.4013 0.4268 0.0052  -0.0367 -0.0644 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.3325 0.3115 0.3261 -0.0024 -0.0439 -0.0389 26  ARG A N   
195  C CA  . ARG A 25  ? 0.3468 0.3206 0.3295 -0.0053 -0.0460 -0.0372 26  ARG A CA  
196  C C   . ARG A 25  ? 0.4187 0.3821 0.3904 0.0022  -0.0596 -0.0371 26  ARG A C   
197  O O   . ARG A 25  ? 0.4208 0.3924 0.3943 0.0031  -0.0662 -0.0418 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3552 0.3153 0.3237 -0.0123 -0.0371 -0.0300 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.4099 0.3652 0.3674 -0.0163 -0.0382 -0.0299 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.4773 0.4222 0.4245 -0.0233 -0.0284 -0.0251 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.4683 0.3960 0.4011 -0.0235 -0.0274 -0.0198 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.6113 0.5227 0.5249 -0.0277 -0.0261 -0.0169 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.5125 0.4227 0.4185 -0.0311 -0.0270 -0.0187 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4907 0.3866 0.3915 -0.0297 -0.0231 -0.0132 26  ARG A NH2 
205  N N   A SER A 26  ? 0.3973 0.3417 0.3562 0.0071  -0.0637 -0.0320 27  SER A N   
206  N N   B SER A 26  ? 0.3963 0.3409 0.3554 0.0072  -0.0637 -0.0321 27  SER A N   
207  N N   C SER A 26  ? 0.3998 0.3443 0.3587 0.0072  -0.0637 -0.0320 27  SER A N   
208  C CA  A SER A 26  ? 0.4240 0.3518 0.3668 0.0152  -0.0771 -0.0298 27  SER A CA  
209  C CA  B SER A 26  ? 0.4229 0.3503 0.3659 0.0155  -0.0771 -0.0298 27  SER A CA  
210  C CA  C SER A 26  ? 0.4278 0.3555 0.3707 0.0153  -0.0771 -0.0298 27  SER A CA  
211  C C   A SER A 26  ? 0.4916 0.4360 0.4514 0.0261  -0.0903 -0.0384 27  SER A C   
212  C C   B SER A 26  ? 0.4885 0.4329 0.4483 0.0261  -0.0901 -0.0384 27  SER A C   
213  C C   C SER A 26  ? 0.4919 0.4364 0.4517 0.0261  -0.0902 -0.0384 27  SER A C   
214  O O   A SER A 26  ? 0.5138 0.4535 0.4638 0.0320  -0.1030 -0.0388 27  SER A O   
215  O O   B SER A 26  ? 0.5084 0.4480 0.4582 0.0317  -0.1027 -0.0387 27  SER A O   
216  O O   C SER A 26  ? 0.5128 0.4525 0.4628 0.0319  -0.1029 -0.0388 27  SER A O   
217  C CB  A SER A 26  ? 0.4801 0.3822 0.4062 0.0176  -0.0768 -0.0232 27  SER A CB  
218  C CB  B SER A 26  ? 0.4778 0.3824 0.4080 0.0187  -0.0769 -0.0242 27  SER A CB  
219  C CB  C SER A 26  ? 0.4892 0.3919 0.4163 0.0179  -0.0768 -0.0234 27  SER A CB  
220  O OG  A SER A 26  ? 0.5492 0.4577 0.4913 0.0238  -0.0774 -0.0271 27  SER A OG  
221  O OG  B SER A 26  ? 0.5673 0.4543 0.4790 0.0091  -0.0667 -0.0173 27  SER A OG  
222  O OG  C SER A 26  ? 0.6199 0.5007 0.5267 0.0260  -0.0899 -0.0199 27  SER A OG  
223  N N   . ARG A 27  ? 0.4275 0.3928 0.4129 0.0285  -0.0872 -0.0462 28  ARG A N   
224  C CA  . ARG A 27  ? 0.4337 0.4201 0.4413 0.0382  -0.0976 -0.0573 28  ARG A CA  
225  C C   . ARG A 27  ? 0.4520 0.4671 0.4788 0.0314  -0.0936 -0.0670 28  ARG A C   
226  O O   . ARG A 27  ? 0.4465 0.4849 0.4961 0.0369  -0.0997 -0.0789 28  ARG A O   
227  C CB  . ARG A 27  ? 0.4496 0.4403 0.4729 0.0440  -0.0954 -0.0617 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.5293 0.4893 0.5327 0.0501  -0.0989 -0.0530 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.6069 0.5699 0.6243 0.0527  -0.0934 -0.0573 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.7583 0.7429 0.8022 0.0632  -0.1009 -0.0701 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.9329 0.9350 0.9986 0.0621  -0.0933 -0.0791 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.7656 0.7892 0.8571 0.0713  -0.0996 -0.0925 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.7529 0.7528 0.8153 0.0514  -0.0793 -0.0759 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.3784 0.3917 0.3966 0.0191  -0.0828 -0.0629 29  ASP A N   
235  C CA  . ASP A 28  ? 0.3808 0.4150 0.4119 0.0101  -0.0763 -0.0707 29  ASP A CA  
236  C C   . ASP A 28  ? 0.4174 0.4744 0.4735 0.0069  -0.0678 -0.0806 29  ASP A C   
237  O O   . ASP A 28  ? 0.4231 0.5027 0.4966 0.0034  -0.0672 -0.0923 29  ASP A O   
238  C CB  . ASP A 28  ? 0.4238 0.4681 0.4560 0.0133  -0.0888 -0.0775 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.5416 0.6003 0.5795 0.0012  -0.0806 -0.0838 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.5353 0.5834 0.5633 -0.0089 -0.0672 -0.0776 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.6000 0.6805 0.6529 0.0020  -0.0876 -0.0958 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.3286 0.3795 0.3852 0.0068  -0.0607 -0.0767 30  ILE A N   
243  C CA  . ILE A 29  ? 0.3134 0.3821 0.3889 0.0029  -0.0519 -0.0851 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3488 0.4161 0.4186 -0.0101 -0.0369 -0.0816 30  ILE A C   
245  O O   . ILE A 29  ? 0.3096 0.3597 0.3636 -0.0128 -0.0318 -0.0706 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3529 0.4166 0.4322 0.0102  -0.0532 -0.0845 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3790 0.4440 0.4663 0.0248  -0.0685 -0.0898 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.3407 0.4200 0.4347 0.0035  -0.0415 -0.0922 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.4511 0.5009 0.5344 0.0324  -0.0704 -0.0861 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.3236 0.4089 0.4065 -0.0182 -0.0298 -0.0917 31  LEU A N   
251  C CA  . LEU A 30  ? 0.3333 0.4157 0.4099 -0.0305 -0.0154 -0.0895 31  LEU A CA  
252  C C   . LEU A 30  ? 0.3590 0.4239 0.4171 -0.0352 -0.0122 -0.0796 31  LEU A C   
253  O O   . LEU A 30  ? 0.3342 0.3901 0.3831 -0.0427 -0.0017 -0.0745 31  LEU A O   
254  C CB  . LEU A 30  ? 0.3483 0.4264 0.4220 -0.0326 -0.0076 -0.0859 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.4360 0.5339 0.5285 -0.0339 -0.0042 -0.0991 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.4560 0.5479 0.5409 -0.0387 0.0050  -0.0952 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.5114 0.6271 0.6165 -0.0433 0.0023  -0.1121 31  LEU A CD2 
258  N N   . THR A 31  ? 0.3231 0.3833 0.3757 -0.0310 -0.0212 -0.0778 32  THR A N   
259  C CA  . THR A 31  ? 0.3247 0.3711 0.3622 -0.0363 -0.0175 -0.0716 32  THR A CA  
260  C C   . THR A 31  ? 0.3975 0.4542 0.4416 -0.0472 -0.0088 -0.0805 32  THR A C   
261  O O   . THR A 31  ? 0.3855 0.4626 0.4461 -0.0488 -0.0109 -0.0930 32  THR A O   
262  C CB  . THR A 31  ? 0.3841 0.4239 0.4128 -0.0305 -0.0289 -0.0693 32  THR A CB  
263  O OG1 . THR A 31  ? 0.4169 0.4751 0.4592 -0.0268 -0.0389 -0.0805 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3857 0.4096 0.4032 -0.0222 -0.0348 -0.0598 32  THR A CG2 
265  N N   . ASP A 32  ? 0.3544 0.3971 0.3867 -0.0548 0.0019  -0.0749 33  ASP A N   
266  C CA  . ASP A 32  ? 0.3531 0.3998 0.3877 -0.0666 0.0126  -0.0823 33  ASP A CA  
267  C C   . ASP A 32  ? 0.3848 0.4186 0.4079 -0.0726 0.0172  -0.0805 33  ASP A C   
268  O O   . ASP A 32  ? 0.3887 0.4190 0.4094 -0.0832 0.0282  -0.0848 33  ASP A O   
269  C CB  . ASP A 32  ? 0.3718 0.4115 0.4022 -0.0716 0.0239  -0.0789 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.5194 0.5389 0.5350 -0.0666 0.0256  -0.0645 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.4694 0.4789 0.4779 -0.0612 0.0209  -0.0576 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.6646 0.6794 0.6757 -0.0683 0.0314  -0.0609 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.3253 0.3502 0.3396 -0.0670 0.0101  -0.0747 34  VAL A N   
274  C CA  . VAL A 33  ? 0.3292 0.3422 0.3325 -0.0729 0.0146  -0.0742 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3781 0.3902 0.3751 -0.0677 0.0035  -0.0732 34  VAL A C   
276  O O   . VAL A 33  ? 0.3717 0.3823 0.3667 -0.0585 -0.0055 -0.0676 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3701 0.3602 0.3605 -0.0741 0.0254  -0.0639 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.3497 0.3299 0.3336 -0.0647 0.0207  -0.0533 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3811 0.3587 0.3627 -0.0823 0.0338  -0.0663 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3459 0.3568 0.3375 -0.0744 0.0047  -0.0787 35  VAL A N   
281  N N   B VAL A 34  ? 0.3408 0.3518 0.3323 -0.0743 0.0045  -0.0787 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3504 0.3566 0.3304 -0.0723 -0.0038 -0.0780 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.3430 0.3489 0.3228 -0.0716 -0.0044 -0.0773 35  VAL A CA  
284  C C   A VAL A 34  ? 0.3902 0.3756 0.3559 -0.0777 0.0072  -0.0729 35  VAL A C   
285  C C   B VAL A 34  ? 0.3914 0.3778 0.3570 -0.0777 0.0062  -0.0734 35  VAL A C   
286  O O   A VAL A 34  ? 0.3960 0.3772 0.3625 -0.0862 0.0184  -0.0768 35  VAL A O   
287  O O   B VAL A 34  ? 0.3978 0.3813 0.3642 -0.0867 0.0167  -0.0784 35  VAL A O   
288  C CB  A VAL A 34  ? 0.4129 0.4373 0.3986 -0.0762 -0.0122 -0.0906 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.3997 0.4241 0.3848 -0.0715 -0.0170 -0.0881 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.4232 0.4394 0.3916 -0.0747 -0.0214 -0.0889 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.4009 0.4362 0.3926 -0.0836 -0.0102 -0.1005 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.4071 0.4546 0.4111 -0.0697 -0.0230 -0.0976 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.4088 0.4232 0.3761 -0.0670 -0.0280 -0.0838 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.3459 0.3176 0.2989 -0.0732 0.0049  -0.0649 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3544 0.3085 0.2956 -0.0775 0.0148  -0.0619 36  ILE A CA  
296  C C   . ILE A 35  ? 0.4278 0.3802 0.3556 -0.0818 0.0092  -0.0666 36  ILE A C   
297  O O   . ILE A 35  ? 0.4240 0.3762 0.3429 -0.0770 -0.0019 -0.0639 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3802 0.3218 0.3174 -0.0714 0.0182  -0.0520 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3694 0.3146 0.3184 -0.0662 0.0208  -0.0473 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.4102 0.3364 0.3392 -0.0757 0.0294  -0.0516 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3793 0.3217 0.3339 -0.0709 0.0313  -0.0493 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.3930 0.3423 0.3173 -0.0912 0.0168  -0.0736 37  VAL A N   
303  C CA  . VAL A 36  ? 0.3990 0.3471 0.3090 -0.0971 0.0123  -0.0794 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4822 0.4103 0.3772 -0.1005 0.0221  -0.0762 37  VAL A C   
305  O O   . VAL A 36  ? 0.4563 0.3746 0.3547 -0.1041 0.0358  -0.0768 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4571 0.4180 0.3729 -0.1067 0.0132  -0.0922 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4674 0.4277 0.3665 -0.1129 0.0072  -0.0984 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4525 0.4366 0.3858 -0.1033 0.0036  -0.0975 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.4523 0.3734 0.3298 -0.0994 0.0152  -0.0731 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4578 0.3613 0.3199 -0.1037 0.0243  -0.0713 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5665 0.4673 0.4071 -0.1109 0.0177  -0.0769 38  VAL A C   
312  O O   . VAL A 37  ? 0.5358 0.4340 0.3609 -0.1077 0.0055  -0.0730 38  VAL A O   
313  C CB  . VAL A 37  ? 0.4965 0.3917 0.3559 -0.0967 0.0245  -0.0619 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.5065 0.3869 0.3568 -0.1019 0.0378  -0.0625 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4721 0.3749 0.3525 -0.0883 0.0256  -0.0567 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5737 0.4751 0.4126 -0.1207 0.0247  -0.0863 39  SER A N   
317  N N   B SER A 38  ? 0.5607 0.4601 0.3988 -0.1209 0.0262  -0.0859 39  SER A N   
318  C CA  A SER A 38  ? 0.6029 0.5041 0.4220 -0.1294 0.0189  -0.0939 39  SER A CA  
319  C CA  B SER A 38  ? 0.5844 0.4826 0.4028 -0.1303 0.0219  -0.0937 39  SER A CA  
320  C C   A SER A 38  ? 0.6172 0.5363 0.4373 -0.1246 -0.0013 -0.0959 39  SER A C   
321  C C   B SER A 38  ? 0.6138 0.5241 0.4245 -0.1255 0.0009  -0.0935 39  SER A C   
322  O O   A SER A 38  ? 0.5928 0.5297 0.4340 -0.1231 -0.0038 -0.1009 39  SER A O   
323  O O   B SER A 38  ? 0.6220 0.5225 0.4093 -0.1241 -0.0085 -0.0889 39  SER A O   
324  C CB  A SER A 38  ? 0.6928 0.5751 0.4854 -0.1335 0.0219  -0.0907 39  SER A CB  
325  C CB  B SER A 38  ? 0.6548 0.5334 0.4514 -0.1370 0.0316  -0.0934 39  SER A CB  
326  O OG  A SER A 38  ? 0.8836 0.7531 0.6804 -0.1361 0.0400  -0.0901 39  SER A OG  
327  O OG  B SER A 38  ? 0.7480 0.6194 0.5538 -0.1427 0.0499  -0.0986 39  SER A OG  
328  N N   A ARG A 39  ? 0.5793 0.4928 0.3766 -0.1218 -0.0155 -0.0921 40  ARG A N   
329  N N   B ARG A 39  ? 0.5369 0.4678 0.3687 -0.1221 -0.0060 -0.0981 40  ARG A N   
330  C CA  A ARG A 39  ? 0.5772 0.5058 0.3735 -0.1148 -0.0370 -0.0938 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.5347 0.4846 0.3707 -0.1158 -0.0257 -0.1011 40  ARG A CA  
332  C C   A ARG A 39  ? 0.5988 0.5318 0.4077 -0.1005 -0.0466 -0.0851 40  ARG A C   
333  C C   B ARG A 39  ? 0.5554 0.5043 0.3937 -0.1018 -0.0372 -0.0904 40  ARG A C   
334  O O   A ARG A 39  ? 0.5904 0.5375 0.4036 -0.0923 -0.0645 -0.0870 40  ARG A O   
335  O O   B ARG A 39  ? 0.5470 0.5148 0.4000 -0.0943 -0.0503 -0.0935 40  ARG A O   
336  C CB  A ARG A 39  ? 0.5996 0.5163 0.3610 -0.1177 -0.0491 -0.0933 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.5683 0.5208 0.3828 -0.1212 -0.0380 -0.1080 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.6870 0.6086 0.4381 -0.1309 -0.0467 -0.1056 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.7015 0.6628 0.5203 -0.1352 -0.0288 -0.1220 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.7223 0.6351 0.4382 -0.1320 -0.0633 -0.1049 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.8132 0.7871 0.6184 -0.1395 -0.0447 -0.1317 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.7759 0.6895 0.4770 -0.1466 -0.0588 -0.1164 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.8869 0.8686 0.6960 -0.1546 -0.0342 -0.1462 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.9120 0.8489 0.6215 -0.1504 -0.0685 -0.1291 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 1.0508 1.0161 0.8390 -0.1667 -0.0232 -0.1499 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7669 0.7023 0.4605 -0.1649 -0.0630 -0.1397 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.8833 0.8242 0.6452 -0.1661 -0.0206 -0.1405 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.7047 0.6678 0.4397 -0.1404 -0.0830 -0.1328 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.8852 0.8577 0.6784 -0.1806 -0.0134 -0.1640 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.5313 0.4531 0.3466 -0.0972 -0.0354 -0.0765 41  GLU A N   
351  N N   B GLU A 40  ? 0.5114 0.4399 0.3381 -0.0986 -0.0312 -0.0795 41  GLU A N   
352  C CA  A GLU A 40  ? 0.5104 0.4344 0.3365 -0.0850 -0.0425 -0.0686 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.5031 0.4279 0.3315 -0.0867 -0.0394 -0.0697 41  GLU A CA  
354  C C   A GLU A 40  ? 0.5187 0.4595 0.3764 -0.0820 -0.0357 -0.0709 41  GLU A C   
355  C C   B GLU A 40  ? 0.5149 0.4540 0.3735 -0.0817 -0.0338 -0.0696 41  GLU A C   
356  O O   A GLU A 40  ? 0.4917 0.4331 0.3596 -0.0889 -0.0210 -0.0743 41  GLU A O   
357  O O   B GLU A 40  ? 0.4829 0.4202 0.3521 -0.0867 -0.0184 -0.0704 41  GLU A O   
358  C CB  A GLU A 40  ? 0.5363 0.4371 0.3458 -0.0834 -0.0365 -0.0578 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.5355 0.4355 0.3434 -0.0878 -0.0319 -0.0603 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.7600 0.6400 0.5336 -0.0873 -0.0424 -0.0545 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.7342 0.6165 0.5070 -0.0915 -0.0399 -0.0582 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.2323 1.1019 0.9900 -0.0772 -0.0590 -0.0466 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.1892 1.0609 0.9468 -0.0814 -0.0555 -0.0497 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.2356 1.0939 0.9931 -0.0730 -0.0550 -0.0389 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.2124 1.0888 0.9606 -0.0760 -0.0737 -0.0514 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.2461 1.1184 0.9911 -0.0733 -0.0763 -0.0486 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.2083 1.0669 0.9636 -0.0785 -0.0499 -0.0418 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4599 0.4118 0.3311 -0.0716 -0.0463 -0.0689 42  GLN A N   
369  C CA  . GLN A 41  ? 0.4364 0.4036 0.3348 -0.0682 -0.0416 -0.0706 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4679 0.4278 0.3689 -0.0589 -0.0429 -0.0611 42  GLN A C   
371  O O   . GLN A 41  ? 0.4694 0.4214 0.3578 -0.0516 -0.0549 -0.0563 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4562 0.4492 0.3723 -0.0656 -0.0530 -0.0814 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.6717 0.6761 0.5902 -0.0768 -0.0495 -0.0933 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.9016 0.9357 0.8433 -0.0763 -0.0575 -0.1064 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.8041 0.8522 0.7621 -0.0667 -0.0661 -0.1075 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.9156 0.9609 0.8602 -0.0874 -0.0538 -0.1183 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.3905 0.3511 0.3056 -0.0593 -0.0309 -0.0582 43  PHE A N   
378  C CA  . PHE A 42  ? 0.3863 0.3416 0.3050 -0.0518 -0.0309 -0.0503 43  PHE A CA  
379  C C   . PHE A 42  ? 0.4283 0.3996 0.3701 -0.0496 -0.0277 -0.0532 43  PHE A C   
380  O O   . PHE A 42  ? 0.4267 0.4003 0.3762 -0.0556 -0.0163 -0.0553 43  PHE A O   
381  C CB  . PHE A 42  ? 0.4081 0.3464 0.3177 -0.0551 -0.0188 -0.0434 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.4434 0.3647 0.3290 -0.0595 -0.0188 -0.0413 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4708 0.3880 0.3486 -0.0682 -0.0116 -0.0459 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.4873 0.3944 0.3563 -0.0561 -0.0247 -0.0352 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.5073 0.4085 0.3611 -0.0737 -0.0108 -0.0450 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.5431 0.4322 0.3861 -0.0619 -0.0237 -0.0335 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.5169 0.4040 0.3527 -0.0709 -0.0166 -0.0386 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3782 0.3587 0.3294 -0.0414 -0.0372 -0.0538 44  ARG A N   
389  C CA  . ARG A 43  ? 0.3506 0.3464 0.3226 -0.0401 -0.0335 -0.0575 44  ARG A CA  
390  C C   . ARG A 43  ? 0.3917 0.3779 0.3633 -0.0378 -0.0262 -0.0490 44  ARG A C   
391  O O   . ARG A 43  ? 0.3777 0.3508 0.3382 -0.0337 -0.0292 -0.0422 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3656 0.3783 0.3508 -0.0322 -0.0465 -0.0643 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.4572 0.4857 0.4475 -0.0342 -0.0548 -0.0752 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.5672 0.6213 0.5817 -0.0290 -0.0621 -0.0864 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.6784 0.7410 0.7085 -0.0339 -0.0492 -0.0890 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.8328 0.9085 0.8743 -0.0444 -0.0389 -0.0980 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.7562 0.8420 0.7996 -0.0512 -0.0401 -0.1071 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.5819 0.6602 0.6318 -0.0490 -0.0272 -0.0985 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.3421 0.3339 0.3242 -0.0413 -0.0166 -0.0498 45  ALA A N   
400  C CA  . ALA A 44  ? 0.3375 0.3221 0.3193 -0.0391 -0.0107 -0.0424 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3511 0.3451 0.3444 -0.0412 -0.0044 -0.0449 45  ALA A C   
402  O O   . ALA A 44  ? 0.3307 0.3362 0.3325 -0.0457 -0.0028 -0.0528 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3512 0.3208 0.3219 -0.0421 -0.0028 -0.0364 45  ALA A CB  
404  N N   . HIS A 45  ? 0.3084 0.2978 0.3011 -0.0389 -0.0006 -0.0388 46  HIS A N   
405  C CA  . HIS A 45  ? 0.2935 0.2877 0.2917 -0.0414 0.0057  -0.0392 46  HIS A CA  
406  C C   . HIS A 45  ? 0.3220 0.3035 0.3118 -0.0448 0.0145  -0.0338 46  HIS A C   
407  O O   . HIS A 45  ? 0.3208 0.2930 0.3049 -0.0414 0.0149  -0.0276 46  HIS A O   
408  C CB  . HIS A 45  ? 0.2932 0.2900 0.2943 -0.0363 0.0032  -0.0361 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.3315 0.3372 0.3404 -0.0315 -0.0052 -0.0411 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.3565 0.3548 0.3600 -0.0259 -0.0123 -0.0379 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.3462 0.3666 0.3675 -0.0314 -0.0075 -0.0499 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.3495 0.3559 0.3612 -0.0211 -0.0196 -0.0436 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.3405 0.3623 0.3651 -0.0237 -0.0173 -0.0516 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.3055 0.2858 0.2946 -0.0514 0.0217  -0.0369 47  LYS A N   
415  C CA  . LYS A 46  ? 0.3171 0.2816 0.2966 -0.0536 0.0299  -0.0316 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3557 0.3142 0.3315 -0.0471 0.0294  -0.0230 47  LYS A C   
417  O O   . LYS A 46  ? 0.3386 0.2865 0.3098 -0.0436 0.0311  -0.0179 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3529 0.3145 0.3295 -0.0623 0.0385  -0.0356 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.4121 0.3775 0.3915 -0.0702 0.0412  -0.0447 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.4082 0.3716 0.3850 -0.0808 0.0511  -0.0503 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.4373 0.4093 0.4200 -0.0897 0.0534  -0.0618 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.4341 0.4052 0.4151 -0.1024 0.0648  -0.0692 47  LYS A NZ  
423  N N   . THR A 47  ? 0.3259 0.2926 0.3047 -0.0456 0.0270  -0.0226 48  THR A N   
424  C CA  . THR A 47  ? 0.3278 0.2912 0.3030 -0.0402 0.0256  -0.0156 48  THR A CA  
425  C C   . THR A 47  ? 0.3309 0.2950 0.3093 -0.0339 0.0210  -0.0126 48  THR A C   
426  O O   . THR A 47  ? 0.3276 0.2858 0.3033 -0.0296 0.0216  -0.0076 48  THR A O   
427  C CB  . THR A 47  ? 0.3719 0.3446 0.3489 -0.0411 0.0243  -0.0172 48  THR A CB  
428  O OG1 . THR A 47  ? 0.4064 0.3919 0.3939 -0.0401 0.0192  -0.0230 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.4053 0.3741 0.3753 -0.0489 0.0315  -0.0196 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2870 0.2571 0.2702 -0.0334 0.0166  -0.0161 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2810 0.2495 0.2646 -0.0299 0.0140  -0.0141 49  VAL A CA  
432  C C   . VAL A 48  ? 0.3191 0.2781 0.2991 -0.0304 0.0183  -0.0129 49  VAL A C   
433  O O   . VAL A 48  ? 0.2999 0.2571 0.2813 -0.0272 0.0197  -0.0106 49  VAL A O   
434  C CB  . VAL A 48  ? 0.3082 0.2800 0.2929 -0.0297 0.0084  -0.0172 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.3174 0.2834 0.2984 -0.0287 0.0081  -0.0154 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.3067 0.2873 0.2968 -0.0281 0.0048  -0.0191 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.3054 0.2596 0.2821 -0.0347 0.0210  -0.0158 50  LEU A N   
438  C CA  . LEU A 49  ? 0.3031 0.2472 0.2760 -0.0359 0.0263  -0.0159 50  LEU A CA  
439  C C   . LEU A 49  ? 0.3383 0.2754 0.3114 -0.0318 0.0307  -0.0117 50  LEU A C   
440  O O   . LEU A 49  ? 0.3426 0.2761 0.3178 -0.0284 0.0330  -0.0110 50  LEU A O   
441  C CB  . LEU A 49  ? 0.3043 0.2451 0.2734 -0.0423 0.0288  -0.0207 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.3435 0.2912 0.3118 -0.0450 0.0225  -0.0255 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.3433 0.2907 0.3096 -0.0519 0.0251  -0.0317 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3767 0.3201 0.3391 -0.0438 0.0199  -0.0244 50  LEU A CD2 
445  N N   . MET A 50  ? 0.3119 0.2469 0.2825 -0.0316 0.0316  -0.0091 51  MET A N   
446  C CA  . MET A 50  ? 0.3339 0.2589 0.3009 -0.0263 0.0339  -0.0038 51  MET A CA  
447  C C   . MET A 50  ? 0.3724 0.3053 0.3458 -0.0184 0.0290  -0.0008 51  MET A C   
448  O O   . MET A 50  ? 0.3770 0.3048 0.3526 -0.0119 0.0297  0.0012  51  MET A O   
449  C CB  . MET A 50  ? 0.3623 0.2815 0.3207 -0.0294 0.0357  -0.0015 51  MET A CB  
450  C CG  . MET A 50  ? 0.4053 0.3169 0.3582 -0.0385 0.0423  -0.0058 51  MET A CG  
451  S SD  . MET A 50  ? 0.4609 0.3713 0.4052 -0.0450 0.0451  -0.0056 51  MET A SD  
452  C CE  . MET A 50  ? 0.4329 0.3180 0.3608 -0.0406 0.0489  0.0032  51  MET A CE  
453  N N   . ALA A 51  ? 0.3239 0.2699 0.3015 -0.0189 0.0240  -0.0017 52  ALA A N   
454  C CA  . ALA A 51  ? 0.3124 0.2685 0.2967 -0.0133 0.0195  -0.0006 52  ALA A CA  
455  C C   . ALA A 51  ? 0.3617 0.3210 0.3541 -0.0117 0.0211  -0.0038 52  ALA A C   
456  O O   . ALA A 51  ? 0.3610 0.3284 0.3612 -0.0065 0.0190  -0.0042 52  ALA A O   
457  C CB  . ALA A 51  ? 0.3119 0.2791 0.2978 -0.0160 0.0154  -0.0021 52  ALA A CB  
458  N N   . CYS A 52  ? 0.3021 0.2560 0.2922 -0.0168 0.0250  -0.0071 53  CYS A N   
459  C CA  . CYS A 52  ? 0.3166 0.2718 0.3110 -0.0180 0.0283  -0.0112 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3610 0.3074 0.3564 -0.0169 0.0347  -0.0132 53  CYS A C   
461  O O   . CYS A 52  ? 0.3339 0.2832 0.3350 -0.0174 0.0385  -0.0176 53  CYS A O   
462  C CB  . CYS A 52  ? 0.3165 0.2702 0.3041 -0.0249 0.0276  -0.0136 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.3443 0.3064 0.3321 -0.0254 0.0212  -0.0128 53  CYS A SG  
464  N N   . SER A 53  ? 0.3294 0.2644 0.3186 -0.0173 0.0371  -0.0115 54  SER A N   
465  C CA  . SER A 53  ? 0.3266 0.2503 0.3145 -0.0180 0.0442  -0.0144 54  SER A CA  
466  C C   . SER A 53  ? 0.3810 0.2926 0.3668 -0.0123 0.0459  -0.0107 54  SER A C   
467  O O   . SER A 53  ? 0.3677 0.2729 0.3449 -0.0146 0.0448  -0.0071 54  SER A O   
468  C CB  . SER A 53  ? 0.3435 0.2618 0.3217 -0.0275 0.0465  -0.0176 54  SER A CB  
469  O OG  . SER A 53  ? 0.3940 0.2994 0.3675 -0.0305 0.0532  -0.0202 54  SER A OG  
470  N N   . GLY A 54  ? 0.3477 0.2544 0.3404 -0.0054 0.0494  -0.0123 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3600 0.2496 0.3484 0.0014  0.0512  -0.0084 55  GLY A CA  
472  C C   . GLY A 54  ? 0.4062 0.2782 0.3819 -0.0071 0.0583  -0.0095 55  GLY A C   
473  O O   . GLY A 54  ? 0.4055 0.2616 0.3705 -0.0064 0.0594  -0.0047 55  GLY A O   
474  N N   . LEU A 55  ? 0.3826 0.2570 0.3576 -0.0164 0.0632  -0.0162 56  LEU A N   
475  C CA  . LEU A 55  ? 0.3871 0.2483 0.3511 -0.0260 0.0695  -0.0191 56  LEU A CA  
476  C C   . LEU A 55  ? 0.4192 0.2834 0.3754 -0.0327 0.0660  -0.0167 56  LEU A C   
477  O O   . LEU A 55  ? 0.3943 0.2442 0.3416 -0.0364 0.0706  -0.0156 56  LEU A O   
478  C CB  . LEU A 55  ? 0.3809 0.2456 0.3444 -0.0345 0.0739  -0.0272 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4607 0.3135 0.4139 -0.0449 0.0805  -0.0322 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4876 0.3188 0.4387 -0.0420 0.0898  -0.0333 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.4692 0.3289 0.4187 -0.0539 0.0813  -0.0392 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3580 0.2397 0.3176 -0.0345 0.0589  -0.0165 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3424 0.2297 0.2980 -0.0401 0.0559  -0.0161 57  PHE A CA  
484  C C   . PHE A 56  ? 0.3925 0.2731 0.3437 -0.0360 0.0553  -0.0096 57  PHE A C   
485  O O   . PHE A 56  ? 0.3873 0.2633 0.3315 -0.0426 0.0582  -0.0103 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3472 0.2527 0.3076 -0.0416 0.0483  -0.0178 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3501 0.2584 0.3085 -0.0478 0.0483  -0.0240 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.3867 0.2917 0.3405 -0.0561 0.0518  -0.0297 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3643 0.2782 0.3237 -0.0463 0.0447  -0.0245 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.3885 0.2961 0.3383 -0.0616 0.0505  -0.0354 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.3963 0.3100 0.3491 -0.0523 0.0439  -0.0293 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3685 0.2795 0.3165 -0.0593 0.0461  -0.0346 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3630 0.2429 0.3175 -0.0256 0.0518  -0.0041 58  TYR A N   
494  C CA  . TYR A 57  ? 0.3808 0.2516 0.3273 -0.0207 0.0499  0.0030  58  TYR A CA  
495  C C   . TYR A 57  ? 0.4428 0.2877 0.3755 -0.0236 0.0581  0.0046  58  TYR A C   
496  O O   . TYR A 57  ? 0.4264 0.2617 0.3465 -0.0289 0.0606  0.0072  58  TYR A O   
497  C CB  . TYR A 57  ? 0.4035 0.2789 0.3573 -0.0080 0.0437  0.0072  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4649 0.3281 0.4076 -0.0011 0.0403  0.0152  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.4902 0.3575 0.4245 -0.0048 0.0371  0.0185  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.5216 0.3677 0.4610 0.0096  0.0401  0.0195  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.5313 0.3851 0.4509 0.0007  0.0337  0.0263  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5722 0.4041 0.4976 0.0170  0.0353  0.0280  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6707 0.5063 0.5848 0.0119  0.0320  0.0317  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.7536 0.5733 0.6500 0.0185  0.0270  0.0405  58  TYR A OH  
505  N N   A SER A 58  ? 0.4240 0.2565 0.3582 -0.0211 0.0633  0.0023  59  SER A N   
506  N N   B SER A 58  ? 0.4243 0.2569 0.3585 -0.0211 0.0633  0.0023  59  SER A N   
507  C CA  A SER A 58  ? 0.4493 0.2541 0.3701 -0.0239 0.0722  0.0031  59  SER A CA  
508  C CA  B SER A 58  ? 0.4505 0.2554 0.3714 -0.0240 0.0722  0.0030  59  SER A CA  
509  C C   A SER A 58  ? 0.5206 0.3229 0.4337 -0.0399 0.0796  -0.0030 59  SER A C   
510  C C   B SER A 58  ? 0.5179 0.3208 0.4311 -0.0399 0.0794  -0.0029 59  SER A C   
511  O O   A SER A 58  ? 0.5543 0.3368 0.4522 -0.0456 0.0859  -0.0008 59  SER A O   
512  O O   B SER A 58  ? 0.5474 0.3314 0.4455 -0.0455 0.0852  -0.0005 59  SER A O   
513  C CB  A SER A 58  ? 0.4790 0.2740 0.4060 -0.0181 0.0766  -0.0003 59  SER A CB  
514  C CB  B SER A 58  ? 0.4861 0.2817 0.4132 -0.0189 0.0769  -0.0008 59  SER A CB  
515  O OG  A SER A 58  ? 0.5073 0.3023 0.4416 -0.0025 0.0705  0.0045  59  SER A OG  
516  O OG  B SER A 58  ? 0.5696 0.3353 0.4828 -0.0213 0.0860  -0.0001 59  SER A OG  
517  N N   . ILE A 59  ? 0.4594 0.2819 0.3825 -0.0474 0.0787  -0.0109 60  ILE A N   
518  C CA  . ILE A 59  ? 0.4495 0.2766 0.3700 -0.0618 0.0836  -0.0190 60  ILE A CA  
519  C C   . ILE A 59  ? 0.4894 0.3225 0.4057 -0.0675 0.0828  -0.0181 60  ILE A C   
520  O O   . ILE A 59  ? 0.5081 0.3293 0.4145 -0.0780 0.0913  -0.0214 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4657 0.3146 0.3971 -0.0660 0.0794  -0.0270 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4685 0.3091 0.4006 -0.0648 0.0835  -0.0304 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.4463 0.3067 0.3784 -0.0790 0.0809  -0.0360 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4874 0.3467 0.4259 -0.0671 0.0778  -0.0359 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.4178 0.2689 0.3412 -0.0619 0.0738  -0.0149 61  PHE A N   
526  C CA  . PHE A 60  ? 0.4216 0.2816 0.3432 -0.0683 0.0737  -0.0165 61  PHE A CA  
527  C C   . PHE A 60  ? 0.4938 0.3347 0.3991 -0.0670 0.0769  -0.0083 61  PHE A C   
528  O O   . PHE A 60  ? 0.5103 0.3557 0.4113 -0.0744 0.0793  -0.0104 61  PHE A O   
529  C CB  . PHE A 60  ? 0.4058 0.2929 0.3416 -0.0649 0.0639  -0.0187 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.4033 0.3053 0.3499 -0.0676 0.0605  -0.0266 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.4439 0.3507 0.3921 -0.0784 0.0649  -0.0362 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.4111 0.3221 0.3647 -0.0600 0.0529  -0.0248 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.4448 0.3648 0.4005 -0.0800 0.0600  -0.0431 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.4395 0.3605 0.3980 -0.0625 0.0492  -0.0310 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.4206 0.3461 0.3798 -0.0718 0.0518  -0.0397 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4772 0.2956 0.3724 -0.0579 0.0773  0.0002  62  THR A N   
537  C CA  . THR A 61  ? 0.4953 0.2895 0.3695 -0.0565 0.0799  0.0088  62  THR A CA  
538  C C   . THR A 61  ? 0.5897 0.3536 0.4466 -0.0656 0.0925  0.0076  62  THR A C   
539  O O   . THR A 61  ? 0.6120 0.3493 0.4461 -0.0675 0.0972  0.0143  62  THR A O   
540  C CB  . THR A 61  ? 0.5948 0.3820 0.4664 -0.0399 0.0709  0.0191  62  THR A CB  
541  O OG1 . THR A 61  ? 0.5582 0.3392 0.4381 -0.0311 0.0705  0.0190  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.5264 0.3406 0.4102 -0.0339 0.0601  0.0203  62  THR A CG2 
543  N N   . ASP A 62  ? 0.5322 0.2986 0.3977 -0.0723 0.0984  -0.0012 63  ASP A N   
544  C CA  . ASP A 62  ? 0.5590 0.2979 0.4091 -0.0834 0.1118  -0.0045 63  ASP A CA  
545  C C   . ASP A 62  ? 0.6427 0.3873 0.4871 -0.1010 0.1199  -0.0119 63  ASP A C   
546  O O   . ASP A 62  ? 0.6011 0.3774 0.4632 -0.1068 0.1166  -0.0211 63  ASP A O   
547  C CB  . ASP A 62  ? 0.5682 0.3109 0.4298 -0.0862 0.1155  -0.0132 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.7630 0.4798 0.6099 -0.1002 0.1303  -0.0189 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.8402 0.5226 0.6714 -0.0952 0.1359  -0.0127 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.7889 0.5193 0.6399 -0.1160 0.1363  -0.0302 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.6785 0.3910 0.4977 -0.1098 0.1310  -0.0088 64  GLN A N   
552  C CA  . GLN A 63  ? 0.6992 0.4132 0.5098 -0.1284 0.1414  -0.0163 64  GLN A CA  
553  C C   . GLN A 63  ? 0.7315 0.4692 0.5597 -0.1441 0.1483  -0.0337 64  GLN A C   
554  O O   . GLN A 63  ? 0.7535 0.5102 0.5874 -0.1566 0.1524  -0.0430 64  GLN A O   
555  C CB  . GLN A 63  ? 0.7722 0.4404 0.5478 -0.1356 0.1536  -0.0090 64  GLN A CB  
556  C CG  . GLN A 63  ? 1.0042 0.6550 0.7600 -0.1233 0.1458  0.0066  64  GLN A CG  
557  N N   . LEU A 64  ? 0.6321 0.3704 0.4696 -0.1437 0.1492  -0.0391 65  LEU A N   
558  C CA  . LEU A 64  ? 0.6147 0.3784 0.4696 -0.1571 0.1528  -0.0559 65  LEU A CA  
559  C C   . LEU A 64  ? 0.6325 0.4351 0.5137 -0.1478 0.1378  -0.0599 65  LEU A C   
560  O O   . LEU A 64  ? 0.6334 0.4666 0.5310 -0.1555 0.1355  -0.0719 65  LEU A O   
561  C CB  . LEU A 64  ? 0.6373 0.3791 0.4849 -0.1647 0.1632  -0.0614 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.7478 0.4550 0.5718 -0.1813 0.1816  -0.0644 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.7648 0.4504 0.5833 -0.1859 0.1903  -0.0692 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.8016 0.5294 0.6316 -0.2020 0.1905  -0.0796 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.5429 0.3437 0.4278 -0.1317 0.1281  -0.0510 66  LYS A N   
566  C CA  . LYS A 65  ? 0.5125 0.3441 0.4175 -0.1241 0.1153  -0.0543 66  LYS A CA  
567  C C   . LYS A 65  ? 0.5656 0.4217 0.4816 -0.1178 0.1048  -0.0520 66  LYS A C   
568  O O   . LYS A 65  ? 0.5298 0.4130 0.4618 -0.1159 0.0957  -0.0581 66  LYS A O   
569  C CB  . LYS A 65  ? 0.5265 0.3483 0.4317 -0.1116 0.1106  -0.0475 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.5350 0.3348 0.4319 -0.1175 0.1210  -0.0519 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.5261 0.3223 0.4270 -0.1053 0.1162  -0.0475 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.6131 0.3825 0.5048 -0.1085 0.1273  -0.0503 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.6603 0.3951 0.5364 -0.1038 0.1346  -0.0416 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.5659 0.4113 0.4717 -0.1151 0.1061  -0.0438 67  CYS A N   
575  C CA  . CYS A 66  ? 0.5620 0.4287 0.4767 -0.1102 0.0977  -0.0423 67  CYS A CA  
576  C C   . CYS A 66  ? 0.5998 0.4956 0.5308 -0.1200 0.0974  -0.0564 67  CYS A C   
577  O O   . CYS A 66  ? 0.5926 0.5113 0.5371 -0.1140 0.0880  -0.0577 67  CYS A O   
578  C CB  . CYS A 66  ? 0.6018 0.4498 0.4989 -0.1089 0.1011  -0.0327 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.6968 0.5253 0.5747 -0.1283 0.1183  -0.0383 67  CYS A SG  
580  N N   . ASN A 67  ? 0.5419 0.4367 0.4722 -0.1350 0.1078  -0.0677 68  ASN A N   
581  C CA  . ASN A 67  ? 0.5349 0.4584 0.4823 -0.1457 0.1090  -0.0839 68  ASN A CA  
582  C C   . ASN A 67  ? 0.5603 0.5065 0.5248 -0.1451 0.1009  -0.0940 68  ASN A C   
583  O O   . ASN A 67  ? 0.5303 0.5040 0.5121 -0.1518 0.0992  -0.1084 68  ASN A O   
584  C CB  . ASN A 67  ? 0.5697 0.4808 0.5062 -0.1645 0.1263  -0.0922 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.7910 0.6847 0.7103 -0.1667 0.1331  -0.0843 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.8173 0.6796 0.7130 -0.1759 0.1461  -0.0802 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.6565 0.5675 0.5846 -0.1580 0.1242  -0.0813 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.5276 0.4634 0.4875 -0.1370 0.0956  -0.0874 69  LEU A N   
589  C CA  . LEU A 68  ? 0.5054 0.4594 0.4766 -0.1369 0.0876  -0.0960 69  LEU A CA  
590  C C   . LEU A 68  ? 0.5123 0.4905 0.4977 -0.1247 0.0713  -0.0952 69  LEU A C   
591  O O   . LEU A 68  ? 0.4965 0.4692 0.4791 -0.1135 0.0659  -0.0838 69  LEU A O   
592  C CB  . LEU A 68  ? 0.5156 0.4485 0.4749 -0.1343 0.0894  -0.0904 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.5922 0.4980 0.5368 -0.1457 0.1054  -0.0921 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.6035 0.4895 0.5387 -0.1403 0.1063  -0.0864 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.6138 0.5326 0.5645 -0.1631 0.1128  -0.1094 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4606 0.4648 0.4607 -0.1268 0.0632  -0.1076 70  SER A N   
597  N N   B SER A 69  ? 0.4606 0.4646 0.4606 -0.1269 0.0633  -0.1076 70  SER A N   
598  C CA  A SER A 69  ? 0.4472 0.4713 0.4589 -0.1146 0.0467  -0.1072 70  SER A CA  
599  C CA  B SER A 69  ? 0.4472 0.4719 0.4592 -0.1150 0.0468  -0.1077 70  SER A CA  
600  C C   A SER A 69  ? 0.4683 0.4872 0.4722 -0.1082 0.0373  -0.1030 70  SER A C   
601  C C   B SER A 69  ? 0.4687 0.4879 0.4728 -0.1084 0.0373  -0.1033 70  SER A C   
602  O O   A SER A 69  ? 0.4438 0.4702 0.4504 -0.0974 0.0241  -0.0993 70  SER A O   
603  O O   B SER A 69  ? 0.4442 0.4713 0.4512 -0.0976 0.0240  -0.0997 70  SER A O   
604  C CB  A SER A 69  ? 0.4916 0.5475 0.5243 -0.1180 0.0413  -0.1231 70  SER A CB  
605  C CB  B SER A 69  ? 0.4918 0.5482 0.5246 -0.1192 0.0419  -0.1242 70  SER A CB  
606  O OG  A SER A 69  ? 0.5892 0.6560 0.6263 -0.1287 0.0432  -0.1365 70  SER A OG  
607  O OG  B SER A 69  ? 0.5809 0.6436 0.6213 -0.1242 0.0502  -0.1282 70  SER A OG  
608  N N   . VAL A 70  ? 0.4338 0.4378 0.4264 -0.1158 0.0449  -0.1040 71  VAL A N   
609  C CA  . VAL A 70  ? 0.4282 0.4246 0.4104 -0.1128 0.0391  -0.1013 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4541 0.4219 0.4215 -0.1146 0.0512  -0.0931 71  VAL A C   
611  O O   . VAL A 70  ? 0.4549 0.4105 0.4185 -0.1240 0.0643  -0.0963 71  VAL A O   
612  C CB  . VAL A 70  ? 0.4943 0.5070 0.4800 -0.1211 0.0345  -0.1155 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.5083 0.5109 0.4792 -0.1193 0.0291  -0.1125 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.4847 0.5282 0.4883 -0.1177 0.0212  -0.1253 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3738 0.3304 0.3328 -0.1058 0.0471  -0.0834 72  ILE A N   
616  C CA  . ILE A 71  ? 0.3852 0.3179 0.3332 -0.1052 0.0567  -0.0770 72  ILE A CA  
617  C C   . ILE A 71  ? 0.4382 0.3681 0.3772 -0.1060 0.0531  -0.0789 72  ILE A C   
618  O O   . ILE A 71  ? 0.4213 0.3579 0.3583 -0.0996 0.0425  -0.0756 72  ILE A O   
619  C CB  . ILE A 71  ? 0.4110 0.3333 0.3590 -0.0947 0.0578  -0.0646 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.4263 0.3489 0.3790 -0.0951 0.0618  -0.0624 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.4290 0.3302 0.3692 -0.0919 0.0659  -0.0595 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.4817 0.3876 0.4279 -0.1046 0.0756  -0.0654 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.4171 0.3344 0.3486 -0.1143 0.0629  -0.0843 73  ASN A N   
624  C CA  . ASN A 72  ? 0.4234 0.3359 0.3440 -0.1172 0.0620  -0.0874 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4635 0.3565 0.3786 -0.1123 0.0704  -0.0806 73  ASN A C   
626  O O   . ASN A 72  ? 0.4563 0.3335 0.3720 -0.1133 0.0821  -0.0801 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4824 0.3952 0.3987 -0.1307 0.0680  -0.1000 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.7000 0.6355 0.6249 -0.1366 0.0604  -0.1097 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.5683 0.5217 0.4956 -0.1322 0.0457  -0.1107 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.6482 0.5829 0.5778 -0.1469 0.0706  -0.1178 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.4033 0.2964 0.3128 -0.1071 0.0647  -0.0762 74  LEU A N   
632  C CA  . LEU A 73  ? 0.4006 0.2793 0.3077 -0.1032 0.0730  -0.0723 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4673 0.3348 0.3639 -0.1122 0.0822  -0.0806 74  LEU A C   
634  O O   . LEU A 73  ? 0.4708 0.3432 0.3588 -0.1213 0.0793  -0.0883 74  LEU A O   
635  C CB  . LEU A 73  ? 0.3898 0.2724 0.2950 -0.0960 0.0658  -0.0656 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.4273 0.3202 0.3422 -0.0870 0.0571  -0.0578 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.4282 0.3199 0.3409 -0.0814 0.0547  -0.0522 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.4115 0.3017 0.3378 -0.0825 0.0623  -0.0543 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.4403 0.2941 0.3384 -0.1093 0.0929  -0.0799 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4632 0.3048 0.3530 -0.1169 0.1039  -0.0883 75  ASP A CA  
641  C C   . ASP A 74  ? 0.5207 0.3680 0.3942 -0.1246 0.0978  -0.0924 75  ASP A C   
642  O O   . ASP A 74  ? 0.5039 0.3575 0.3741 -0.1201 0.0894  -0.0865 75  ASP A O   
643  C CB  . ASP A 74  ? 0.4853 0.3164 0.3833 -0.1090 0.1134  -0.0862 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.6280 0.4451 0.5213 -0.1154 0.1271  -0.0959 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.6503 0.4685 0.5311 -0.1238 0.1285  -0.1018 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.6357 0.4390 0.5363 -0.1119 0.1367  -0.0974 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.5348 0.3785 0.3960 -0.1364 0.1016  -0.1022 76  PRO A N   
648  C CA  . PRO A 75  ? 0.5505 0.3978 0.3918 -0.1436 0.0942  -0.1054 76  PRO A CA  
649  C C   . PRO A 75  ? 0.6000 0.4392 0.4314 -0.1432 0.0988  -0.1034 76  PRO A C   
650  O O   . PRO A 75  ? 0.6157 0.4555 0.4279 -0.1472 0.0907  -0.1025 76  PRO A O   
651  C CB  . PRO A 75  ? 0.5946 0.4386 0.4259 -0.1569 0.0999  -0.1176 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.6567 0.4890 0.5011 -0.1570 0.1150  -0.1213 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5713 0.4063 0.4338 -0.1444 0.1124  -0.1112 76  PRO A CD  
654  N N   . GLU A 76  ? 0.5595 0.3908 0.4031 -0.1383 0.1112  -0.1031 77  GLU A N   
655  C CA  . GLU A 76  ? 0.5823 0.4084 0.4206 -0.1387 0.1177  -0.1034 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5770 0.4106 0.4168 -0.1310 0.1073  -0.0932 77  GLU A C   
657  O O   . GLU A 76  ? 0.5660 0.3959 0.3961 -0.1338 0.1103  -0.0931 77  GLU A O   
658  C CB  . GLU A 76  ? 0.6145 0.4338 0.4711 -0.1337 0.1331  -0.1075 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.8796 0.6930 0.7303 -0.1396 0.1455  -0.1151 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.2638 1.0665 1.0996 -0.1528 0.1564  -0.1273 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.2574 1.0531 1.1038 -0.1520 0.1654  -0.1333 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.1965 0.9960 1.0081 -0.1644 0.1562  -0.1309 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.4897 0.3330 0.3412 -0.1223 0.0965  -0.0855 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4734 0.3231 0.3275 -0.1148 0.0873  -0.0765 78  ILE A CA  
665  C C   . ILE A 77  ? 0.5375 0.3856 0.3682 -0.1196 0.0759  -0.0741 78  ILE A C   
666  O O   . ILE A 77  ? 0.5344 0.3858 0.3555 -0.1226 0.0664  -0.0756 78  ILE A O   
667  C CB  . ILE A 77  ? 0.4882 0.3478 0.3618 -0.1043 0.0805  -0.0699 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.4985 0.3549 0.3910 -0.0984 0.0912  -0.0709 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4565 0.3228 0.3325 -0.0972 0.0711  -0.0616 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.5757 0.4295 0.4773 -0.0945 0.1011  -0.0725 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.5445 0.3875 0.3664 -0.1198 0.0767  -0.0706 79  ASN A N   
672  C CA  . ASN A 78  ? 0.5603 0.3957 0.3560 -0.1236 0.0670  -0.0667 79  ASN A CA  
673  C C   . ASN A 78  ? 0.5537 0.3970 0.3551 -0.1137 0.0513  -0.0582 79  ASN A C   
674  O O   . ASN A 78  ? 0.5113 0.3607 0.3304 -0.1062 0.0524  -0.0537 79  ASN A O   
675  C CB  . ASN A 78  ? 0.6101 0.4343 0.3939 -0.1295 0.0773  -0.0674 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.8231 0.6333 0.5754 -0.1340 0.0687  -0.0621 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.7081 0.5158 0.4599 -0.1298 0.0650  -0.0557 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.7444 0.5433 0.4678 -0.1427 0.0650  -0.0647 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.5348 0.3788 0.3218 -0.1131 0.0363  -0.0566 80  PRO A N   
680  C CA  . PRO A 79  ? 0.5238 0.3758 0.3182 -0.1027 0.0217  -0.0498 80  PRO A CA  
681  C C   . PRO A 79  ? 0.5578 0.4000 0.3450 -0.0992 0.0204  -0.0423 80  PRO A C   
682  O O   . PRO A 79  ? 0.5264 0.3772 0.3305 -0.0904 0.0157  -0.0379 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5750 0.4275 0.3519 -0.1034 0.0063  -0.0514 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.6416 0.4934 0.4113 -0.1138 0.0135  -0.0603 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5932 0.4323 0.3581 -0.1211 0.0314  -0.0619 80  PRO A CD  
686  N N   . GLU A 80  ? 0.5404 0.3640 0.3017 -0.1073 0.0259  -0.0417 81  GLU A N   
687  C CA  . GLU A 80  ? 0.5338 0.3459 0.2863 -0.1062 0.0268  -0.0356 81  GLU A CA  
688  C C   . GLU A 80  ? 0.5445 0.3677 0.3250 -0.1037 0.0389  -0.0367 81  GLU A C   
689  O O   . GLU A 80  ? 0.5191 0.3455 0.3090 -0.0972 0.0349  -0.0319 81  GLU A O   
690  C CB  . GLU A 80  ? 0.5871 0.3745 0.3026 -0.1177 0.0315  -0.0353 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.7095 0.4818 0.4120 -0.1171 0.0308  -0.0286 81  GLU A CG  
692  C CD  . GLU A 80  ? 1.0720 0.8181 0.7395 -0.1307 0.0407  -0.0288 81  GLU A CD  
693  O OE1 . GLU A 80  ? 1.0710 0.7971 0.7157 -0.1307 0.0354  -0.0219 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 0.9792 0.7234 0.6413 -0.1419 0.0547  -0.0364 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.5057 0.3348 0.2993 -0.1081 0.0527  -0.0436 82  GLY A N   
696  C CA  . GLY A 81  ? 0.4840 0.3255 0.3057 -0.1038 0.0624  -0.0455 82  GLY A CA  
697  C C   . GLY A 81  ? 0.4856 0.3424 0.3309 -0.0921 0.0537  -0.0411 82  GLY A C   
698  O O   . GLY A 81  ? 0.4546 0.3188 0.3147 -0.0865 0.0538  -0.0383 82  GLY A O   
699  N N   . PHE A 82  ? 0.4328 0.2950 0.2809 -0.0893 0.0462  -0.0413 83  PHE A N   
700  C CA  . PHE A 82  ? 0.4030 0.2788 0.2710 -0.0800 0.0389  -0.0380 83  PHE A CA  
701  C C   . PHE A 82  ? 0.4469 0.3232 0.3115 -0.0746 0.0279  -0.0320 83  PHE A C   
702  O O   . PHE A 82  ? 0.4125 0.2977 0.2934 -0.0682 0.0270  -0.0292 83  PHE A O   
703  C CB  . PHE A 82  ? 0.4163 0.2981 0.2871 -0.0805 0.0343  -0.0413 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.4062 0.3011 0.2969 -0.0730 0.0301  -0.0392 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.4281 0.3267 0.3357 -0.0699 0.0382  -0.0389 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.4114 0.3140 0.3035 -0.0685 0.0177  -0.0372 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.4311 0.3392 0.3529 -0.0642 0.0349  -0.0363 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.4237 0.3384 0.3335 -0.0630 0.0154  -0.0362 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.4040 0.3206 0.3269 -0.0616 0.0243  -0.0353 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.4681 0.3337 0.3106 -0.0766 0.0191  -0.0302 84  CYS A N   
711  C CA  . CYS A 83  ? 0.4876 0.3494 0.3241 -0.0708 0.0082  -0.0247 84  CYS A CA  
712  C C   . CYS A 83  ? 0.4942 0.3518 0.3340 -0.0708 0.0149  -0.0218 84  CYS A C   
713  O O   . CYS A 83  ? 0.4642 0.3285 0.3160 -0.0640 0.0100  -0.0189 84  CYS A O   
714  C CB  . CYS A 83  ? 0.5452 0.3906 0.3522 -0.0730 -0.0017 -0.0229 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.6243 0.4621 0.4232 -0.0632 -0.0174 -0.0163 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4572 0.3055 0.2879 -0.0793 0.0270  -0.0242 85  ILE A N   
717  C CA  . ILE A 84  ? 0.4363 0.2826 0.2709 -0.0818 0.0353  -0.0242 85  ILE A CA  
718  C C   . ILE A 84  ? 0.4207 0.2879 0.2867 -0.0747 0.0378  -0.0252 85  ILE A C   
719  O O   . ILE A 84  ? 0.4023 0.2739 0.2766 -0.0716 0.0366  -0.0233 85  ILE A O   
720  C CB  . ILE A 84  ? 0.4822 0.3179 0.3036 -0.0936 0.0493  -0.0294 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.5115 0.3209 0.2942 -0.1017 0.0461  -0.0265 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4737 0.3167 0.3100 -0.0965 0.0606  -0.0332 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.6233 0.4216 0.3887 -0.1146 0.0592  -0.0325 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3693 0.2475 0.2506 -0.0725 0.0412  -0.0283 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3573 0.2519 0.2643 -0.0652 0.0428  -0.0284 86  LEU A CA  
726  C C   . LEU A 85  ? 0.4040 0.3067 0.3192 -0.0577 0.0324  -0.0240 86  LEU A C   
727  O O   . LEU A 85  ? 0.3663 0.2789 0.2957 -0.0528 0.0318  -0.0226 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3591 0.2580 0.2770 -0.0648 0.0501  -0.0324 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.4254 0.3215 0.3437 -0.0707 0.0626  -0.0388 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.4370 0.3342 0.3644 -0.0693 0.0689  -0.0429 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.4397 0.3464 0.3736 -0.0683 0.0667  -0.0407 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3606 0.2604 0.2671 -0.0569 0.0239  -0.0229 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3533 0.2620 0.2684 -0.0504 0.0147  -0.0207 87  LEU A CA  
734  C C   . LEU A 86  ? 0.3848 0.2904 0.2970 -0.0478 0.0101  -0.0177 87  LEU A C   
735  O O   . LEU A 86  ? 0.3526 0.2681 0.2781 -0.0431 0.0084  -0.0166 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3573 0.2660 0.2656 -0.0505 0.0067  -0.0225 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.4038 0.3251 0.3246 -0.0444 -0.0017 -0.0230 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.3795 0.3125 0.3181 -0.0432 0.0042  -0.0238 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.4246 0.3489 0.3403 -0.0445 -0.0108 -0.0269 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3772 0.2669 0.2697 -0.0518 0.0094  -0.0164 88  ASP A N   
741  C CA  . ASP A 87  ? 0.3888 0.2705 0.2752 -0.0510 0.0073  -0.0138 88  ASP A CA  
742  C C   . ASP A 87  ? 0.4121 0.3036 0.3138 -0.0521 0.0157  -0.0153 88  ASP A C   
743  O O   . ASP A 87  ? 0.4001 0.2963 0.3095 -0.0485 0.0128  -0.0144 88  ASP A O   
744  C CB  . ASP A 87  ? 0.4498 0.3082 0.3082 -0.0575 0.0080  -0.0122 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.6395 0.4858 0.4794 -0.0540 -0.0045 -0.0095 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.6437 0.5018 0.4959 -0.0456 -0.0144 -0.0098 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.6779 0.5030 0.4904 -0.0596 -0.0046 -0.0077 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3683 0.2636 0.2752 -0.0569 0.0258  -0.0187 89  PHE A N   
749  C CA  . PHE A 88  ? 0.3384 0.2467 0.2627 -0.0567 0.0325  -0.0215 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3327 0.2577 0.2762 -0.0483 0.0274  -0.0199 89  PHE A C   
751  O O   . PHE A 88  ? 0.3167 0.2505 0.2698 -0.0465 0.0270  -0.0203 89  PHE A O   
752  C CB  . PHE A 88  ? 0.3436 0.2558 0.2739 -0.0609 0.0430  -0.0266 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.3329 0.2632 0.2858 -0.0574 0.0470  -0.0302 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3650 0.2998 0.3218 -0.0615 0.0510  -0.0338 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3575 0.2996 0.3267 -0.0498 0.0459  -0.0299 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.3551 0.3098 0.3341 -0.0575 0.0527  -0.0379 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3704 0.3289 0.3591 -0.0447 0.0470  -0.0325 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3468 0.3134 0.3414 -0.0483 0.0498  -0.0369 89  PHE A CZ  
759  N N   . MET A 89  ? 0.2886 0.2174 0.2363 -0.0445 0.0245  -0.0187 90  MET A N   
760  C CA  . MET A 89  ? 0.2788 0.2201 0.2404 -0.0382 0.0210  -0.0171 90  MET A CA  
761  C C   . MET A 89  ? 0.3248 0.2692 0.2874 -0.0357 0.0146  -0.0157 90  MET A C   
762  O O   . MET A 89  ? 0.3141 0.2689 0.2869 -0.0327 0.0140  -0.0154 90  MET A O   
763  C CB  . MET A 89  ? 0.2895 0.2303 0.2508 -0.0371 0.0194  -0.0167 90  MET A CB  
764  C CG  . MET A 89  ? 0.3182 0.2557 0.2805 -0.0387 0.0265  -0.0185 90  MET A CG  
765  S SD  . MET A 89  ? 0.3766 0.3129 0.3384 -0.0389 0.0255  -0.0188 90  MET A SD  
766  C CE  . MET A 89  ? 0.3849 0.3120 0.3436 -0.0424 0.0350  -0.0222 90  MET A CE  
767  N N   . TYR A 90  ? 0.3002 0.2352 0.2516 -0.0363 0.0092  -0.0151 91  TYR A N   
768  C CA  . TYR A 90  ? 0.3023 0.2387 0.2551 -0.0328 0.0028  -0.0147 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3636 0.2923 0.3106 -0.0350 0.0040  -0.0147 91  TYR A C   
770  O O   . TYR A 90  ? 0.3438 0.2724 0.2924 -0.0320 -0.0004 -0.0150 91  TYR A O   
771  C CB  . TYR A 90  ? 0.3264 0.2575 0.2724 -0.0301 -0.0052 -0.0149 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.3368 0.2804 0.2934 -0.0279 -0.0072 -0.0171 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3618 0.3056 0.3170 -0.0310 -0.0040 -0.0179 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.3404 0.2951 0.3082 -0.0242 -0.0107 -0.0194 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.3563 0.3100 0.3201 -0.0309 -0.0042 -0.0208 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.3470 0.3126 0.3236 -0.0243 -0.0110 -0.0228 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.3840 0.3487 0.3582 -0.0280 -0.0074 -0.0233 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.3504 0.3247 0.3323 -0.0299 -0.0064 -0.0276 91  TYR A OH  
779  N N   . THR A 91  ? 0.3203 0.2421 0.2606 -0.0411 0.0110  -0.0155 92  THR A N   
780  C CA  . THR A 91  ? 0.3309 0.2426 0.2630 -0.0456 0.0138  -0.0165 92  THR A CA  
781  C C   . THR A 91  ? 0.3625 0.2824 0.3026 -0.0515 0.0230  -0.0207 92  THR A C   
782  O O   . THR A 91  ? 0.3676 0.2828 0.3044 -0.0560 0.0259  -0.0229 92  THR A O   
783  C CB  . THR A 91  ? 0.4192 0.3057 0.3263 -0.0499 0.0132  -0.0143 92  THR A CB  
784  O OG1 . THR A 91  ? 0.4050 0.2874 0.3050 -0.0565 0.0206  -0.0157 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.4287 0.3058 0.3261 -0.0431 0.0020  -0.0109 92  THR A CG2 
786  N N   A SER A 92  ? 0.3136 0.2451 0.2642 -0.0517 0.0277  -0.0228 93  SER A N   
787  N N   B SER A 92  ? 0.3105 0.2417 0.2607 -0.0518 0.0278  -0.0228 93  SER A N   
788  C CA  A SER A 92  ? 0.3092 0.2517 0.2706 -0.0564 0.0364  -0.0287 93  SER A CA  
789  C CA  B SER A 92  ? 0.3038 0.2462 0.2652 -0.0564 0.0363  -0.0286 93  SER A CA  
790  C C   A SER A 92  ? 0.3501 0.2772 0.2961 -0.0669 0.0453  -0.0320 93  SER A C   
791  C C   B SER A 92  ? 0.3631 0.2900 0.3090 -0.0671 0.0453  -0.0321 93  SER A C   
792  O O   A SER A 92  ? 0.3308 0.2673 0.2862 -0.0722 0.0540  -0.0389 93  SER A O   
793  O O   B SER A 92  ? 0.3548 0.2910 0.3098 -0.0729 0.0540  -0.0391 93  SER A O   
794  C CB  A SER A 92  ? 0.3248 0.2805 0.2981 -0.0568 0.0364  -0.0323 93  SER A CB  
795  C CB  B SER A 92  ? 0.3189 0.2766 0.2941 -0.0555 0.0356  -0.0318 93  SER A CB  
796  O OG  A SER A 92  ? 0.2826 0.2493 0.2652 -0.0490 0.0286  -0.0293 93  SER A OG  
797  O OG  B SER A 92  ? 0.3477 0.2946 0.3127 -0.0631 0.0390  -0.0343 93  SER A OG  
798  N N   A ARG A 93  ? 0.3360 0.2397 0.2581 -0.0700 0.0431  -0.0278 94  ARG A N   
799  N N   B ARG A 93  ? 0.3439 0.2478 0.2661 -0.0700 0.0432  -0.0278 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3647 0.2490 0.2657 -0.0813 0.0518  -0.0301 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3710 0.2542 0.2709 -0.0811 0.0512  -0.0297 94  ARG A CA  
802  C C   A ARG A 93  ? 0.4171 0.2958 0.3099 -0.0826 0.0537  -0.0297 94  ARG A C   
803  C C   B ARG A 93  ? 0.4225 0.3000 0.3139 -0.0828 0.0536  -0.0295 94  ARG A C   
804  O O   A ARG A 93  ? 0.3972 0.2722 0.2847 -0.0763 0.0451  -0.0248 94  ARG A O   
805  O O   B ARG A 93  ? 0.4108 0.2841 0.2964 -0.0767 0.0450  -0.0246 94  ARG A O   
806  C CB  A ARG A 93  ? 0.4182 0.2752 0.2925 -0.0845 0.0481  -0.0253 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.4137 0.2704 0.2879 -0.0829 0.0461  -0.0243 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4738 0.3321 0.3534 -0.0852 0.0481  -0.0268 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.5031 0.3623 0.3840 -0.0815 0.0443  -0.0250 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.6129 0.4449 0.4698 -0.0822 0.0399  -0.0203 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5824 0.4309 0.4537 -0.0945 0.0560  -0.0304 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.7710 0.5710 0.5945 -0.0907 0.0437  -0.0176 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.5871 0.4390 0.4659 -0.0942 0.0550  -0.0323 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.9382 0.7177 0.7433 -0.1025 0.0533  -0.0199 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.7604 0.5861 0.6182 -0.0975 0.0545  -0.0297 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.7690 0.5591 0.5885 -0.1071 0.0599  -0.0258 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.6230 0.4536 0.4897 -0.0976 0.0546  -0.0329 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.7810 0.5283 0.5515 -0.1107 0.0567  -0.0166 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5574 0.3499 0.3833 -0.1008 0.0538  -0.0242 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.3841 0.2629 0.2758 -0.0919 0.0659  -0.0364 95  LEU A N   
821  C CA  . LEU A 94  ? 0.3952 0.2690 0.2794 -0.0951 0.0705  -0.0382 95  LEU A CA  
822  C C   . LEU A 94  ? 0.4779 0.3255 0.3301 -0.1084 0.0780  -0.0392 95  LEU A C   
823  O O   . LEU A 94  ? 0.4639 0.3085 0.3131 -0.1192 0.0896  -0.0454 95  LEU A O   
824  C CB  . LEU A 94  ? 0.3900 0.2867 0.3015 -0.0938 0.0790  -0.0466 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.4337 0.3277 0.3424 -0.0960 0.0847  -0.0500 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.4061 0.2999 0.3153 -0.0863 0.0741  -0.0433 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.4365 0.3504 0.3713 -0.0957 0.0951  -0.0602 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4867 0.3151 0.3138 -0.1085 0.0715  -0.0334 96  ASN A N   
829  C CA  . ASN A 95  ? 0.5264 0.3257 0.3167 -0.1209 0.0770  -0.0328 96  ASN A CA  
830  C C   . ASN A 95  ? 0.5837 0.3857 0.3729 -0.1301 0.0899  -0.0409 96  ASN A C   
831  O O   . ASN A 95  ? 0.5823 0.3773 0.3584 -0.1301 0.0865  -0.0394 96  ASN A O   
832  C CB  . ASN A 95  ? 0.6012 0.3786 0.3635 -0.1157 0.0619  -0.0231 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.8322 0.5754 0.5508 -0.1275 0.0653  -0.0208 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.7444 0.4739 0.4484 -0.1409 0.0790  -0.0247 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.7446 0.4733 0.4403 -0.1236 0.0531  -0.0148 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.5324 0.3477 0.3390 -0.1374 0.1046  -0.0509 97  LEU A N   
837  C CA  . LEU A 96  ? 0.5521 0.3741 0.3644 -0.1458 0.1190  -0.0613 97  LEU A CA  
838  C C   . LEU A 96  ? 0.6283 0.4241 0.4054 -0.1644 0.1319  -0.0650 97  LEU A C   
839  O O   . LEU A 96  ? 0.6163 0.4029 0.3840 -0.1737 0.1389  -0.0670 97  LEU A O   
840  C CB  . LEU A 96  ? 0.5407 0.3943 0.3944 -0.1418 0.1266  -0.0713 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.6059 0.4756 0.4802 -0.1422 0.1373  -0.0822 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.6062 0.4757 0.4822 -0.1321 0.1284  -0.0769 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5798 0.4809 0.4950 -0.1359 0.1415  -0.0913 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.6127 0.3932 0.3659 -0.1707 0.1344  -0.0654 98  ARG A N   
845  C CA  . ARG A 97  ? 0.6619 0.4131 0.3744 -0.1894 0.1463  -0.0681 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6771 0.4344 0.3925 -0.1982 0.1605  -0.0795 98  ARG A C   
847  O O   . ARG A 97  ? 0.6313 0.4064 0.3691 -0.1882 0.1561  -0.0813 98  ARG A O   
848  C CB  . ARG A 97  ? 0.7095 0.4272 0.3772 -0.1888 0.1318  -0.0547 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.7979 0.5063 0.4608 -0.1791 0.1172  -0.0436 98  ARG A CG  
850  C CD  . ARG A 97  ? 1.0488 0.7262 0.6708 -0.1752 0.1006  -0.0310 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.3160 0.9552 0.8876 -0.1921 0.1088  -0.0297 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.6042 1.2150 1.1480 -0.2017 0.1146  -0.0267 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.4836 1.0570 0.9777 -0.2180 0.1227  -0.0252 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.4681 1.0861 1.0318 -0.1962 0.1134  -0.0255 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.6729 0.4138 0.3640 -0.2178 0.1784  -0.0880 99  GLU A N   
856  C CA  . GLU A 98  ? 0.6742 0.4193 0.3658 -0.2282 0.1941  -0.1006 99  GLU A CA  
857  C C   . GLU A 98  ? 0.7369 0.4744 0.4138 -0.2223 0.1832  -0.0950 99  GLU A C   
858  O O   . GLU A 98  ? 0.7271 0.4829 0.4283 -0.2187 0.1884  -0.1035 99  GLU A O   
859  C CB  . GLU A 98  ? 0.7379 0.4581 0.3930 -0.2528 0.2140  -0.1085 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.8786 0.6046 0.5360 -0.2654 0.2331  -0.1242 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.3043 1.0036 0.9215 -0.2917 0.2539  -0.1324 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.2698 0.9305 0.8340 -0.3007 0.2486  -0.1209 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.3216 1.0380 0.9596 -0.3033 0.2758  -0.1509 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.7251 0.4372 0.3651 -0.2202 0.1672  -0.0812 100 GLY A N   
865  C CA  . GLY A 99  ? 0.7398 0.4448 0.3632 -0.2154 0.1548  -0.0761 100 GLY A CA  
866  C C   . GLY A 99  ? 0.7390 0.4697 0.3986 -0.1963 0.1407  -0.0729 100 GLY A C   
867  O O   . GLY A 99  ? 0.7449 0.4760 0.3992 -0.1943 0.1352  -0.0733 100 GLY A O   
868  N N   . ASN A 100 ? 0.6443 0.3959 0.3398 -0.1832 0.1355  -0.0704 101 ASN A N   
869  C CA  . ASN A 100 ? 0.6032 0.3762 0.3295 -0.1662 0.1228  -0.0668 101 ASN A CA  
870  C C   . ASN A 100 ? 0.6108 0.4123 0.3832 -0.1586 0.1311  -0.0749 101 ASN A C   
871  O O   . ASN A 100 ? 0.5707 0.3872 0.3664 -0.1459 0.1229  -0.0725 101 ASN A O   
872  C CB  . ASN A 100 ? 0.5916 0.3617 0.3148 -0.1546 0.1037  -0.0542 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.7058 0.4826 0.4450 -0.1511 0.1048  -0.0523 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5514 0.3461 0.3182 -0.1519 0.1164  -0.0602 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.6106 0.3746 0.3344 -0.1463 0.0920  -0.0425 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5737 0.3827 0.3590 -0.1659 0.1469  -0.0846 102 ILE A N   
877  C CA  . ILE A 101 ? 0.5426 0.3797 0.3724 -0.1565 0.1524  -0.0920 102 ILE A CA  
878  C C   . ILE A 101 ? 0.5546 0.4029 0.4053 -0.1493 0.1548  -0.0975 102 ILE A C   
879  O O   . ILE A 101 ? 0.5024 0.3683 0.3835 -0.1347 0.1485  -0.0957 102 ILE A O   
880  C CB  . ILE A 101 ? 0.5907 0.4369 0.4327 -0.1663 0.1690  -0.1040 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5708 0.4490 0.4610 -0.1531 0.1701  -0.1107 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.5992 0.4335 0.4219 -0.1843 0.1877  -0.1159 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.5731 0.4656 0.4795 -0.1578 0.1778  -0.1183 102 ILE A CD1 
884  N N   . MET A 102 ? 0.5468 0.3830 0.3792 -0.1594 0.1636  -0.1038 103 MET A N   
885  C CA  . MET A 102 ? 0.5469 0.3908 0.3978 -0.1531 0.1669  -0.1096 103 MET A CA  
886  C C   . MET A 102 ? 0.5746 0.4187 0.4280 -0.1410 0.1504  -0.0989 103 MET A C   
887  O O   . MET A 102 ? 0.5364 0.3928 0.4174 -0.1290 0.1491  -0.0998 103 MET A O   
888  C CB  . MET A 102 ? 0.6210 0.4514 0.4508 -0.1680 0.1810  -0.1200 103 MET A CB  
889  C CG  . MET A 102 ? 0.7137 0.5464 0.5452 -0.1811 0.2006  -0.1336 103 MET A CG  
890  S SD  . MET A 102 ? 0.7653 0.6294 0.6504 -0.1698 0.2093  -0.1449 103 MET A SD  
891  C CE  . MET A 102 ? 0.7285 0.6000 0.6396 -0.1588 0.2133  -0.1526 103 MET A CE  
892  N N   . ALA A 103 ? 0.5510 0.3813 0.3756 -0.1437 0.1378  -0.0891 104 ALA A N   
893  C CA  . ALA A 103 ? 0.5385 0.3709 0.3651 -0.1340 0.1224  -0.0807 104 ALA A CA  
894  C C   . ALA A 103 ? 0.5271 0.3746 0.3796 -0.1199 0.1134  -0.0737 104 ALA A C   
895  O O   . ALA A 103 ? 0.4914 0.3470 0.3612 -0.1103 0.1080  -0.0714 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5722 0.3890 0.3641 -0.1394 0.1104  -0.0735 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4647 0.3146 0.3184 -0.1199 0.1125  -0.0709 105 VAL A N   
898  C CA  . VAL A 104 ? 0.4300 0.2946 0.3070 -0.1077 0.1043  -0.0652 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4481 0.3293 0.3580 -0.0988 0.1106  -0.0707 105 VAL A C   
900  O O   . VAL A 104 ? 0.4200 0.3093 0.3455 -0.0875 0.1024  -0.0655 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4729 0.3353 0.3427 -0.1115 0.1038  -0.0627 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.4308 0.3110 0.3273 -0.1004 0.0983  -0.0597 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.4983 0.3419 0.3361 -0.1156 0.0935  -0.0546 105 VAL A CG2 
904  N N   A MET A 105 ? 0.4289 0.3145 0.3488 -0.1037 0.1247  -0.0816 106 MET A N   
905  N N   B MET A 105 ? 0.4321 0.3177 0.3520 -0.1037 0.1248  -0.0816 106 MET A N   
906  C CA  A MET A 105 ? 0.4249 0.3257 0.3766 -0.0937 0.1300  -0.0879 106 MET A CA  
907  C CA  B MET A 105 ? 0.4355 0.3365 0.3875 -0.0933 0.1295  -0.0876 106 MET A CA  
908  C C   A MET A 105 ? 0.4742 0.3700 0.4304 -0.0865 0.1278  -0.0863 106 MET A C   
909  C C   B MET A 105 ? 0.4697 0.3653 0.4256 -0.0864 0.1275  -0.0861 106 MET A C   
910  O O   A MET A 105 ? 0.4518 0.3555 0.4276 -0.0736 0.1223  -0.0828 106 MET A O   
911  O O   B MET A 105 ? 0.4399 0.3432 0.4152 -0.0735 0.1221  -0.0826 106 MET A O   
912  C CB  A MET A 105 ? 0.4693 0.3762 0.4311 -0.1009 0.1464  -0.1022 106 MET A CB  
913  C CB  B MET A 105 ? 0.4823 0.3902 0.4458 -0.0998 0.1456  -0.1017 106 MET A CB  
914  C CG  A MET A 105 ? 0.5075 0.4327 0.5055 -0.0879 0.1496  -0.1093 106 MET A CG  
915  C CG  B MET A 105 ? 0.5211 0.4471 0.5207 -0.0861 0.1481  -0.1082 106 MET A CG  
916  S SD  A MET A 105 ? 0.5751 0.5115 0.5906 -0.0954 0.1695  -0.1291 106 MET A SD  
917  S SD  B MET A 105 ? 0.5827 0.5245 0.6034 -0.0926 0.1661  -0.1272 106 MET A SD  
918  C CE  A MET A 105 ? 0.5257 0.4747 0.5776 -0.0752 0.1680  -0.1336 106 MET A CE  
919  C CE  B MET A 105 ? 0.5727 0.4966 0.5771 -0.1038 0.1811  -0.1369 106 MET A CE  
920  N N   . ALA A 106 ? 0.4550 0.3363 0.3908 -0.0958 0.1320  -0.0889 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4638 0.3380 0.4008 -0.0920 0.1317  -0.0889 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4726 0.3474 0.4093 -0.0841 0.1175  -0.0776 107 ALA A C   
923  O O   . ALA A 106 ? 0.4517 0.3264 0.4017 -0.0751 0.1162  -0.0758 107 ALA A O   
924  C CB  . ALA A 106 ? 0.4962 0.3561 0.4083 -0.1056 0.1378  -0.0943 107 ALA A CB  
925  N N   . THR A 107 ? 0.4192 0.2936 0.3405 -0.0873 0.1072  -0.0705 108 THR A N   
926  C CA  . THR A 107 ? 0.4120 0.2893 0.3342 -0.0807 0.0945  -0.0616 108 THR A CA  
927  C C   . THR A 107 ? 0.4216 0.3104 0.3662 -0.0686 0.0909  -0.0571 108 THR A C   
928  O O   . THR A 107 ? 0.3975 0.2867 0.3492 -0.0619 0.0867  -0.0530 108 THR A O   
929  C CB  . THR A 107 ? 0.4822 0.3563 0.3841 -0.0857 0.0841  -0.0563 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4824 0.3451 0.3613 -0.0968 0.0872  -0.0606 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4669 0.3454 0.3707 -0.0804 0.0724  -0.0502 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3762 0.2741 0.3306 -0.0666 0.0930  -0.0586 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3519 0.2625 0.3270 -0.0552 0.0885  -0.0553 109 ALA A CA  
934  C C   . ALA A 108 ? 0.3886 0.2998 0.3809 -0.0457 0.0927  -0.0579 109 ALA A C   
935  O O   . ALA A 108 ? 0.3715 0.2857 0.3728 -0.0356 0.0861  -0.0520 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3563 0.2780 0.3388 -0.0570 0.0909  -0.0587 109 ALA A CB  
937  N N   . MET A 109 ? 0.3750 0.2806 0.3696 -0.0488 0.1037  -0.0666 110 MET A N   
938  C CA  . MET A 109 ? 0.3752 0.2773 0.3848 -0.0387 0.1077  -0.0693 110 MET A CA  
939  C C   . MET A 109 ? 0.4213 0.3089 0.4208 -0.0368 0.1038  -0.0626 110 MET A C   
940  O O   . MET A 109 ? 0.4206 0.3051 0.4282 -0.0258 0.0998  -0.0576 110 MET A O   
941  C CB  . MET A 109 ? 0.4176 0.3162 0.4316 -0.0436 0.1216  -0.0817 110 MET A CB  
942  C CG  . MET A 109 ? 0.4669 0.3822 0.4975 -0.0437 0.1274  -0.0907 110 MET A CG  
943  S SD  . MET A 109 ? 0.5656 0.4767 0.5967 -0.0543 0.1459  -0.1071 110 MET A SD  
944  C CE  . MET A 109 ? 0.5343 0.4379 0.5847 -0.0390 0.1493  -0.1107 110 MET A CE  
945  N N   . TYR A 110 ? 0.4053 0.2840 0.3859 -0.0480 0.1045  -0.0627 111 TYR A N   
946  C CA  . TYR A 110 ? 0.4032 0.2705 0.3739 -0.0497 0.1021  -0.0587 111 TYR A CA  
947  C C   . TYR A 110 ? 0.4247 0.2975 0.3968 -0.0435 0.0910  -0.0489 111 TYR A C   
948  O O   . TYR A 110 ? 0.4128 0.2770 0.3857 -0.0385 0.0903  -0.0449 111 TYR A O   
949  C CB  . TYR A 110 ? 0.4090 0.2721 0.3608 -0.0633 0.1027  -0.0621 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.4166 0.2737 0.3593 -0.0672 0.0989  -0.0597 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4614 0.3047 0.4031 -0.0687 0.1066  -0.0634 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.4141 0.2792 0.3495 -0.0702 0.0886  -0.0553 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.4521 0.2909 0.3858 -0.0745 0.1047  -0.0630 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.4188 0.2820 0.3485 -0.0749 0.0859  -0.0556 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4699 0.3206 0.3987 -0.0780 0.0944  -0.0598 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4648 0.3152 0.3886 -0.0846 0.0929  -0.0618 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3727 0.2580 0.3439 -0.0444 0.0834  -0.0454 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3531 0.2450 0.3258 -0.0397 0.0737  -0.0375 112 LEU A CA  
959  C C   . LEU A 111 ? 0.3920 0.2894 0.3787 -0.0278 0.0710  -0.0336 112 LEU A C   
960  O O   . LEU A 111 ? 0.3811 0.2821 0.3678 -0.0237 0.0639  -0.0272 112 LEU A O   
961  C CB  . LEU A 111 ? 0.3342 0.2352 0.3001 -0.0447 0.0668  -0.0359 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3718 0.2684 0.3220 -0.0543 0.0648  -0.0380 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.3852 0.2881 0.3288 -0.0560 0.0565  -0.0352 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.3916 0.2851 0.3390 -0.0559 0.0627  -0.0371 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3579 0.2575 0.3569 -0.0221 0.0762  -0.0383 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3591 0.2663 0.3732 -0.0093 0.0721  -0.0359 113 GLN A CA  
967  C C   . GLN A 112 ? 0.3882 0.3127 0.4068 -0.0085 0.0642  -0.0331 113 GLN A C   
968  O O   . GLN A 112 ? 0.3750 0.3024 0.3934 -0.0029 0.0564  -0.0263 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3854 0.2783 0.3960 -0.0009 0.0695  -0.0292 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.4100 0.2832 0.4166 -0.0011 0.0784  -0.0327 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.5481 0.4019 0.5435 0.0027  0.0769  -0.0253 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.4819 0.3361 0.4763 0.0106  0.0692  -0.0177 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.5560 0.3914 0.5403 -0.0044 0.0848  -0.0276 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3482 0.2818 0.3681 -0.0159 0.0673  -0.0386 114 MET A N   
975  C CA  . MET A 113 ? 0.3396 0.2876 0.3629 -0.0177 0.0624  -0.0381 114 MET A CA  
976  C C   . MET A 113 ? 0.4055 0.3674 0.4467 -0.0155 0.0676  -0.0470 114 MET A C   
977  O O   . MET A 113 ? 0.3765 0.3395 0.4157 -0.0248 0.0756  -0.0543 114 MET A O   
978  C CB  . MET A 113 ? 0.3619 0.3045 0.3682 -0.0292 0.0623  -0.0373 114 MET A CB  
979  C CG  . MET A 113 ? 0.3844 0.3181 0.3779 -0.0305 0.0565  -0.0308 114 MET A CG  
980  S SD  . MET A 113 ? 0.4226 0.3497 0.3969 -0.0412 0.0541  -0.0306 114 MET A SD  
981  C CE  . MET A 113 ? 0.3785 0.3160 0.3557 -0.0402 0.0478  -0.0280 114 MET A CE  
982  N N   . GLU A 114 ? 0.4004 0.3722 0.4585 -0.0031 0.0633  -0.0471 115 GLU A N   
983  C CA  . GLU A 114 ? 0.4130 0.4016 0.4941 0.0023  0.0672  -0.0572 115 GLU A CA  
984  C C   . GLU A 114 ? 0.4142 0.4197 0.5022 -0.0068 0.0710  -0.0651 115 GLU A C   
985  O O   . GLU A 114 ? 0.3937 0.4069 0.4933 -0.0108 0.0808  -0.0765 115 GLU A O   
986  C CB  . GLU A 114 ? 0.4424 0.4398 0.5388 0.0190  0.0578  -0.0544 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.6210 0.5981 0.7105 0.0284  0.0562  -0.0479 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3672 0.3776 0.4482 -0.0109 0.0648  -0.0604 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3793 0.4026 0.4648 -0.0207 0.0694  -0.0680 116 HIS A CA  
990  C C   . HIS A 115 ? 0.4025 0.4118 0.4708 -0.0360 0.0804  -0.0719 116 HIS A C   
991  O O   . HIS A 115 ? 0.4109 0.4286 0.4861 -0.0444 0.0901  -0.0826 116 HIS A O   
992  C CB  . HIS A 115 ? 0.4028 0.4323 0.4842 -0.0211 0.0604  -0.0623 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.4540 0.4999 0.5517 -0.0077 0.0501  -0.0606 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4845 0.5527 0.6075 -0.0009 0.0503  -0.0705 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4775 0.5203 0.5683 -0.0005 0.0394  -0.0507 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4788 0.5555 0.6079 0.0113  0.0382  -0.0652 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4779 0.5389 0.5867 0.0110  0.0320  -0.0532 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.3328 0.3210 0.3781 -0.0399 0.0791  -0.0639 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3527 0.3249 0.3775 -0.0534 0.0876  -0.0664 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.4217 0.3947 0.4547 -0.0561 0.0997  -0.0769 117 VAL A C   
1001 O O   . VAL A 116 ? 0.3950 0.3668 0.4229 -0.0680 0.1106  -0.0854 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.3969 0.3497 0.3976 -0.0555 0.0815  -0.0567 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.4067 0.3426 0.3846 -0.0684 0.0890  -0.0596 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3899 0.3428 0.3838 -0.0538 0.0710  -0.0487 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3778 0.3512 0.4226 -0.0456 0.0989  -0.0770 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3752 0.3496 0.4311 -0.0460 0.1104  -0.0879 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.4259 0.4219 0.5046 -0.0479 0.1183  -0.1013 118 VAL A C   
1008 O O   . VAL A 117 ? 0.4205 0.4152 0.4967 -0.0594 0.1317  -0.1120 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.4133 0.3835 0.4799 -0.0321 0.1072  -0.0854 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.4232 0.3947 0.5038 -0.0314 0.1196  -0.0982 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.4063 0.3558 0.4501 -0.0338 0.1022  -0.0750 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.3848 0.4008 0.4837 -0.0384 0.1103  -0.1012 119 ASP A N   
1013 N N   B ASP A 118 ? 0.3834 0.3998 0.4838 -0.0374 0.1103  -0.1015 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.3866 0.4283 0.5109 -0.0395 0.1159  -0.1149 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.3851 0.4277 0.5120 -0.0378 0.1158  -0.1154 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.4307 0.4706 0.5418 -0.0595 0.1275  -0.1220 119 ASP A C   
1017 C C   B ASP A 118 ? 0.4399 0.4822 0.5552 -0.0575 0.1275  -0.1231 119 ASP A C   
1018 O O   A ASP A 118 ? 0.4301 0.4802 0.5534 -0.0673 0.1412  -0.1370 119 ASP A O   
1019 O O   B ASP A 118 ? 0.4434 0.4975 0.5728 -0.0647 0.1408  -0.1384 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.4060 0.4679 0.5488 -0.0267 0.1023  -0.1115 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.4006 0.4632 0.5457 -0.0250 0.1021  -0.1118 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.5874 0.6804 0.7606 -0.0264 0.1063  -0.1271 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.5588 0.6280 0.7229 -0.0044 0.0924  -0.1094 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.6225 0.7291 0.8197 -0.0203 0.1124  -0.1393 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.5928 0.6607 0.7689 0.0014  0.0987  -0.1165 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.6694 0.7742 0.8436 -0.0323 0.1035  -0.1280 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.6417 0.7160 0.8074 0.0059  0.0787  -0.1005 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.3869 0.4124 0.4723 -0.0680 0.1229  -0.1120 120 THR A N   
1029 N N   B THR A 119 ? 0.3966 0.4239 0.4856 -0.0664 0.1232  -0.1131 120 THR A N   
1030 C CA  A THR A 119 ? 0.4004 0.4183 0.4683 -0.0869 0.1337  -0.1175 120 THR A CA  
1031 C CA  B THR A 119 ? 0.4092 0.4294 0.4808 -0.0850 0.1333  -0.1180 120 THR A CA  
1032 C C   A THR A 119 ? 0.4576 0.4548 0.5033 -0.0998 0.1464  -0.1212 120 THR A C   
1033 C C   B THR A 119 ? 0.4633 0.4625 0.5119 -0.0986 0.1463  -0.1218 120 THR A C   
1034 O O   A THR A 119 ? 0.4604 0.4568 0.5005 -0.1152 0.1606  -0.1319 120 THR A O   
1035 O O   B THR A 119 ? 0.4671 0.4675 0.5127 -0.1134 0.1607  -0.1334 120 THR A O   
1036 C CB  A THR A 119 ? 0.4018 0.4076 0.4482 -0.0914 0.1255  -0.1065 120 THR A CB  
1037 C CB  B THR A 119 ? 0.4806 0.4898 0.5323 -0.0877 0.1236  -0.1062 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.4419 0.4440 0.4778 -0.1087 0.1373  -0.1146 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4668 0.4940 0.5384 -0.0735 0.1106  -0.1018 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.3799 0.3580 0.3952 -0.0915 0.1180  -0.0923 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.4929 0.4989 0.5334 -0.1046 0.1333  -0.1127 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.4180 0.3985 0.4500 -0.0948 0.1421  -0.1132 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.4405 0.4014 0.4499 -0.1068 0.1532  -0.1169 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.5081 0.4837 0.5401 -0.1098 0.1686  -0.1342 121 CYS A C   
1045 O O   . CYS A 120 ? 0.4967 0.4645 0.5144 -0.1265 0.1835  -0.1436 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.4453 0.3900 0.4405 -0.1001 0.1448  -0.1066 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.4943 0.4190 0.4577 -0.1011 0.1298  -0.0895 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4640 0.4602 0.5306 -0.0934 0.1651  -0.1389 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4699 0.4658 0.5363 -0.0935 0.1653  -0.1389 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4691 0.4837 0.5651 -0.0914 0.1776  -0.1565 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4782 0.4919 0.5730 -0.0922 0.1783  -0.1567 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.5102 0.5428 0.6180 -0.1046 0.1903  -0.1716 122 ARG A C   
1053 C C   B ARG A 121 ? 0.5135 0.5461 0.6211 -0.1049 0.1906  -0.1718 122 ARG A C   
1054 O O   A ARG A 121 ? 0.5089 0.5440 0.6198 -0.1165 0.2077  -0.1870 122 ARG A O   
1055 O O   B ARG A 121 ? 0.5111 0.5464 0.6221 -0.1168 0.2080  -0.1873 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4670 0.5005 0.5976 -0.0684 0.1671  -0.1564 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.4912 0.5223 0.6198 -0.0695 0.1686  -0.1570 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.6115 0.6266 0.7338 -0.0567 0.1596  -0.1458 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6853 0.6980 0.8070 -0.0606 0.1662  -0.1509 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7499 0.7792 0.9052 -0.0357 0.1544  -0.1498 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.8161 0.8437 0.9725 -0.0408 0.1635  -0.1575 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.8027 0.8113 0.9466 -0.0247 0.1456  -0.1371 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.8868 0.9233 1.0549 -0.0232 0.1456  -0.1465 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 0.9265 0.9171 1.0625 -0.0257 0.1533  -0.1395 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 1.0224 1.0438 1.1839 -0.0100 0.1346  -0.1336 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.8096 0.8007 0.9479 -0.0367 0.1697  -0.1542 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.8483 0.8460 0.9937 -0.0120 0.1395  -0.1308 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.6849 0.6565 0.8100 -0.0170 0.1456  -0.1282 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.8112 0.8401 0.9805 0.0041  0.1193  -0.1242 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4554 0.4999 0.5684 -0.1040 0.1826  -0.1682 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4692 0.5318 0.5938 -0.1175 0.1940  -0.1825 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.5368 0.5744 0.6238 -0.1424 0.2087  -0.1843 123 LYS A C   
1073 O O   . LYS A 122 ? 0.5338 0.5809 0.6280 -0.1574 0.2268  -0.2017 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.4869 0.5670 0.6250 -0.1103 0.1810  -0.1778 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.7293 0.8393 0.9079 -0.0877 0.1691  -0.1810 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.8745 1.0024 1.0649 -0.0811 0.1559  -0.1769 123 LYS A CD  
1077 C CE  . LYS A 122 ? 1.0318 1.1838 1.2554 -0.0573 0.1415  -0.1772 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.1721 1.3567 1.4218 -0.0539 0.1351  -0.1854 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.4976 0.5028 0.5439 -0.1468 0.2011  -0.1669 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.5285 0.5039 0.5325 -0.1686 0.2123  -0.1657 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.6004 0.5653 0.5935 -0.1790 0.2278  -0.1755 124 PHE A C   
1082 O O   . PHE A 123 ? 0.6126 0.5673 0.5873 -0.1997 0.2453  -0.1857 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.5546 0.5002 0.5213 -0.1669 0.1974  -0.1451 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.5792 0.5234 0.5406 -0.1673 0.1893  -0.1378 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.5970 0.5712 0.5941 -0.1562 0.1826  -0.1413 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.6398 0.5515 0.5593 -0.1778 0.1870  -0.1271 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.6061 0.5786 0.5977 -0.1574 0.1758  -0.1355 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.6645 0.5730 0.5793 -0.1777 0.1800  -0.1208 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.6111 0.5504 0.5622 -0.1683 0.1752  -0.1255 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.5350 0.5021 0.5393 -0.1658 0.2227  -0.1736 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5576 0.5166 0.5549 -0.1744 0.2376  -0.1843 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.6337 0.6196 0.6648 -0.1806 0.2566  -0.2081 125 ILE A C   
1093 O O   . ILE A 124 ? 0.6621 0.6384 0.6765 -0.2001 0.2757  -0.2202 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.5850 0.5379 0.5855 -0.1590 0.2276  -0.1766 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.5883 0.5127 0.5493 -0.1595 0.2132  -0.1568 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.6273 0.5774 0.6300 -0.1659 0.2443  -0.1912 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.6574 0.5795 0.6249 -0.1426 0.1991  -0.1465 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.5808 0.6009 0.6585 -0.1645 0.2512  -0.2153 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.5914 0.6438 0.7090 -0.1670 0.2666  -0.2393 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.6557 0.7099 0.7620 -0.1918 0.2839  -0.2516 126 LYS A C   
1101 O O   . LYS A 125 ? 0.6560 0.7226 0.7755 -0.2049 0.3046  -0.2728 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.6049 0.6926 0.7712 -0.1431 0.2529  -0.2422 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.6104 0.6502 0.6908 -0.1991 0.2767  -0.2389 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.6382 0.6730 0.7017 -0.2237 0.2928  -0.2483 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.7447 0.7452 0.7623 -0.2485 0.3115  -0.2513 127 ALA A C   
1106 O O   . ALA A 126 ? 0.7520 0.7542 0.7645 -0.2706 0.3324  -0.2674 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.6399 0.6624 0.6840 -0.2234 0.2790  -0.2322 127 ALA A CB  
1108 N N   . SER A 127 ? 0.7504 0.7197 0.7332 -0.2457 0.3040  -0.2361 128 SER A N   
1109 C CA  . SER A 127 ? 0.8145 0.7480 0.7479 -0.2678 0.3183  -0.2362 128 SER A CA  
1110 C C   . SER A 127 ? 0.9146 0.8564 0.8598 -0.2751 0.3373  -0.2552 128 SER A C   
1111 O O   . SER A 127 ? 0.9670 0.8835 0.8739 -0.2979 0.3542  -0.2606 128 SER A O   
1112 C CB  . SER A 127 ? 0.8836 0.7806 0.7723 -0.2625 0.3003  -0.2119 128 SER A CB  
1113 O OG  . SER A 127 ? 1.0232 0.8967 0.8788 -0.2696 0.2932  -0.1984 128 SER A OG  
1114 N N   . GLU A 128 ? 0.8448 0.8201 0.8409 -0.2564 0.3352  -0.2658 129 GLU A N   
1115 C CA  . GLU A 128 ? 1.1126 1.0977 1.1255 -0.2605 0.3529  -0.2852 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.6285 1.6367 1.6634 -0.2794 0.3792  -0.3129 129 GLU A C   
1117 O O   . GLU A 128 ? 1.2149 1.2184 1.2335 -0.2979 0.3884  -0.3162 129 GLU A O   
1118 C CB  . GLU A 128 ? 1.0983 1.1058 1.1547 -0.2323 0.3404  -0.2855 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.1936 1.2453 1.3101 -0.2150 0.3366  -0.2980 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.4479 1.5159 1.6016 -0.1848 0.3204  -0.2940 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.3756 1.4202 1.5080 -0.1743 0.3061  -0.2753 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.3421 1.4463 1.5465 -0.1716 0.3217  -0.3100 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.2326 0.4833 0.3468 -0.0456 -0.0065 -0.0803 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2503 0.5010 0.3645 -0.0456 -0.0065 -0.0803 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.2237 0.4728 0.3366 -0.0452 -0.0063 -0.0811 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2501 0.4993 0.3631 -0.0452 -0.0063 -0.0811 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2746 0.5236 0.3895 -0.0452 -0.0073 -0.0804 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2768 0.5261 0.3919 -0.0453 -0.0072 -0.0804 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2729 0.5218 0.3896 -0.0453 -0.0085 -0.0800 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2682 0.5176 0.3852 -0.0455 -0.0083 -0.0798 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.2117 0.4589 0.3221 -0.0448 -0.0075 -0.0823 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.2465 0.4937 0.3570 -0.0448 -0.0074 -0.0822 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.2135 0.4607 0.3209 -0.0450 -0.0067 -0.0840 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2637 0.5108 0.3764 -0.0444 -0.0097 -0.0821 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2437 0.4913 0.3508 -0.0450 -0.0076 -0.0850 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.3028 0.5504 0.4173 -0.0446 -0.0115 -0.0826 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.2105 0.4572 0.3150 -0.0450 -0.0047 -0.0856 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2636 0.5108 0.3776 -0.0436 -0.0105 -0.0820 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2318 0.4793 0.3351 -0.0450 -0.0062 -0.0876 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.2968 0.5455 0.4149 -0.0439 -0.0131 -0.0829 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2474 0.4944 0.3493 -0.0450 -0.0043 -0.0881 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.3147 0.5633 0.4321 -0.0431 -0.0123 -0.0828 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.2207 0.4666 0.3248 -0.0449 -0.0031 -0.0853 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2782 0.5247 0.3912 -0.0429 -0.0098 -0.0817 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2439 0.4905 0.3424 -0.0451 -0.0022 -0.0907 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.3050 0.5552 0.4250 -0.0417 -0.0131 -0.0836 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.2329 0.4781 0.3342 -0.0451 -0.0011 -0.0872 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.2979 0.5451 0.4123 -0.0415 -0.0108 -0.0823 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2410 0.4868 0.3396 -0.0452 -0.0004 -0.0901 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.3037 0.5531 0.4216 -0.0408 -0.0121 -0.0834 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.2150 0.4638 0.3297 -0.0450 -0.0066 -0.0807 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.2152 0.4638 0.3310 -0.0448 -0.0077 -0.0810 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2474 0.4938 0.3613 -0.0437 -0.0077 -0.0813 2   VAL D C   
1157 O O   . VAL B 3   ? 0.2391 0.4844 0.3514 -0.0436 -0.0066 -0.0810 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2537 0.5060 0.3725 -0.0460 -0.0075 -0.0814 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2567 0.5120 0.3774 -0.0471 -0.0074 -0.0805 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2441 0.4985 0.3643 -0.0461 -0.0061 -0.0819 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.2261 0.4718 0.3401 -0.0429 -0.0089 -0.0820 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.2289 0.4726 0.3412 -0.0417 -0.0091 -0.0821 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2913 0.5362 0.4060 -0.0427 -0.0091 -0.0828 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2901 0.5370 0.4066 -0.0434 -0.0102 -0.0844 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.2559 0.4990 0.3673 -0.0399 -0.0103 -0.0835 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.2291 0.4734 0.3408 -0.0388 -0.0105 -0.0836 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2784 0.5194 0.3877 -0.0382 -0.0107 -0.0833 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.3057 0.5503 0.4158 -0.0383 -0.0102 -0.0822 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2789 0.5233 0.3942 -0.0429 -0.0078 -0.0821 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2840 0.5312 0.4037 -0.0438 -0.0080 -0.0833 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.3426 0.5885 0.4626 -0.0431 -0.0101 -0.0845 4   PRO D C   
1172 O O   . PRO B 5   ? 0.3269 0.5687 0.4432 -0.0415 -0.0106 -0.0837 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.3014 0.5482 0.4222 -0.0438 -0.0057 -0.0825 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.3573 0.5992 0.4728 -0.0427 -0.0052 -0.0806 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.3053 0.5474 0.4182 -0.0425 -0.0063 -0.0806 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.3304 0.5805 0.4551 -0.0443 -0.0115 -0.0868 5   ALA D N   
# 
