data_7GV0
# 
_entry.id   7GV0 
# 
_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   7GV0         pdb_00007gv0 10.2210/pdb7gv0/pdb 
WWPDB D_1001406671 ?            ?                   
# 
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                        7GV0 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              Rob.vanMontfort@icr.ac.uk 
_pdbx_contact_author.name_first         Rob 
_pdbx_contact_author.name_last          'van Montfort' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodrigues, M.J.'      1 0000-0003-1243-903X 
'Le Bihan, Y.V.'       2 0000-0002-6850-9706 
'van Montfort, R.L.M.' 3 0000-0002-5688-3450 
# 
_citation.id                        primary 
_citation.title                     
'Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.' 
_citation.journal_abbrev            J.Appl.Crystallogr. 
_citation.journal_volume            57 
_citation.page_first                1951 
_citation.page_last                 1965 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39628887 
_citation.pdbx_database_id_DOI      10.1107/S1600576724010549 
_citation.journal_id_ASTM           JACGAR 
_citation.country                   DK 
_citation.journal_id_ISSN           0021-8898 
_citation.journal_id_CSD            0228 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodrigues, M.J.'      1 0000-0003-1243-903X 
primary 'Cabry, M.'            2 0000-0002-9070-5498 
primary 'Collie, G.'           3 0000-0002-0406-922X 
primary 'Carter, M.'           4 ?                   
primary 'McAndrew, C.'         5 0000-0002-1366-088X 
primary 'Owen, R.L.'           6 0000-0002-2104-7057 
primary 'Bellenie, B.R.'       7 0000-0001-9987-3079 
primary 'Le Bihan, Y.V.'       8 0000-0002-6850-9706 
primary 'van Montfort, R.L.M.' 9 0000-0002-5688-3450 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'B-cell lymphoma 6 protein'                                            14536.915 1   ? ? ? ? 
2 polymer     syn 'WVIP tetrapeptide'                                                    610.744   1   ? ? ? ? 
3 non-polymer syn '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' 339.575   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                         35.453    1   ? ? ? ? 
5 non-polymer nat 'DIMETHYL SULFOXIDE'                                                   78.133    1   ? ? ? ? 
6 water       nat water                                                                  18.015    185 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'BCL-6,B-cell lymphoma 5 protein,BCL-5,Protein LAZ-3,Zinc finger and BTB domain-containing protein 27,Zinc finger protein 51' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
A ? 
2 'polypeptide(L)' no yes '(ACE)WVIPA' XWVIPA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' A1ACA 
4 'CHLORIDE ION'                                                         CL    
5 'DIMETHYL SULFOXIDE'                                                   DMS   
6 water                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   ALA n 
1 5   ASP n 
1 6   SER n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  PHE n 
1 11  THR n 
1 12  ARG n 
1 13  HIS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  LEU n 
1 19  LEU n 
1 20  ASN n 
1 21  LEU n 
1 22  ASN n 
1 23  ARG n 
1 24  LEU n 
1 25  ARG n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  THR n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  ILE n 
1 36  VAL n 
1 37  VAL n 
1 38  SER n 
1 39  ARG n 
1 40  GLU n 
1 41  GLN n 
1 42  PHE n 
1 43  ARG n 
1 44  ALA n 
1 45  HIS n 
1 46  LYS n 
1 47  THR n 
1 48  VAL n 
1 49  LEU n 
1 50  MET n 
1 51  ALA n 
1 52  CYS n 
1 53  SER n 
1 54  GLY n 
1 55  LEU n 
1 56  PHE n 
1 57  TYR n 
1 58  SER n 
1 59  ILE n 
1 60  PHE n 
1 61  THR n 
1 62  ASP n 
1 63  GLN n 
1 64  LEU n 
1 65  LYS n 
1 66  CYS n 
1 67  ASN n 
1 68  LEU n 
1 69  SER n 
1 70  VAL n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ASP n 
1 75  PRO n 
1 76  GLU n 
1 77  ILE n 
1 78  ASN n 
1 79  PRO n 
1 80  GLU n 
1 81  GLY n 
1 82  PHE n 
1 83  CYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  ASP n 
1 88  PHE n 
1 89  MET n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ARG n 
1 94  LEU n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLU n 
1 99  GLY n 
1 100 ASN n 
1 101 ILE n 
1 102 MET n 
1 103 ALA n 
1 104 VAL n 
1 105 MET n 
1 106 ALA n 
1 107 THR n 
1 108 ALA n 
1 109 MET n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 MET n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 VAL n 
1 118 ASP n 
1 119 THR n 
1 120 CYS n 
1 121 ARG n 
1 122 LYS n 
1 123 PHE n 
1 124 ILE n 
1 125 LYS n 
1 126 ALA n 
1 127 SER n 
1 128 GLU n 
2 1   ACE n 
2 2   TRP n 
2 3   VAL n 
2 4   ILE n 
2 5   PRO n 
2 6   ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCL6, BCL5, LAZ3, ZBTB27, ZNF51' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21-AI 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET48b 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 6 'synthetic construct' ? 32630 ? 
3 2 sample ? ? 'synthetic construct' ? 32630 ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ACA non-polymer         . '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' ? 'C12 H8 Br Cl N4 O' 339.575 
ACE   non-polymer         . 'ACETYL GROUP'                                                         ? 'C2 H4 O'           44.053  
ALA   'L-peptide linking' y ALANINE                                                                ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE                                                               ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                             ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                        ? 'C4 H7 N O4'        133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                         ? 'Cl -1'             35.453  
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'      121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                   ? 'C2 H6 O S'         78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                  ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                                             ? 'C5 H11 N O2 S'     149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                                                                ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE                                                                 ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE                                                              ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                             ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE                                                               ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE                                                                 ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLY 3   4   ?   ?   ?   A . n 
A 1 4   ALA 4   5   ?   ?   ?   A . n 
A 1 5   ASP 5   6   6   ASP ASP A . n 
A 1 6   SER 6   7   7   SER SER A . n 
A 1 7   CYS 7   8   8   CYS CYS A . n 
A 1 8   ILE 8   9   9   ILE ILE A . n 
A 1 9   GLN 9   10  10  GLN GLN A . n 
A 1 10  PHE 10  11  11  PHE PHE A . n 
A 1 11  THR 11  12  12  THR THR A . n 
A 1 12  ARG 12  13  13  ARG ARG A . n 
A 1 13  HIS 13  14  14  HIS HIS A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ASP 16  17  17  ASP ASP A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  ASN 20  21  21  ASN ASN A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  ARG 23  24  24  ARG ARG A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  ARG 25  26  26  ARG ARG A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  THR 31  32  32  THR THR A . n 
A 1 32  ASP 32  33  33  ASP ASP A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  VAL 36  37  37  VAL VAL A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  SER 38  39  39  SER SER A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLN 41  42  42  GLN GLN A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  ALA 44  45  45  ALA ALA A . n 
A 1 45  HIS 45  46  46  HIS HIS A . n 
A 1 46  LYS 46  47  47  LYS LYS A . n 
A 1 47  THR 47  48  48  THR THR A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  MET 50  51  51  MET MET A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  CYS 52  53  53  CYS CYS A . n 
A 1 53  SER 53  54  54  SER SER A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  PHE 60  61  61  PHE PHE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  ASN 67  68  68  ASN ASN A . n 
A 1 68  LEU 68  69  69  LEU LEU A . n 
A 1 69  SER 69  70  70  SER SER A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ILE 71  72  72  ILE ILE A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  ASP 74  75  75  ASP ASP A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLU 76  77  77  GLU GLU A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  PRO 79  80  80  PRO PRO A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  CYS 83  84  84  CYS CYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  LEU 85  86  86  LEU LEU A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  PHE 88  89  89  PHE PHE A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  ASN 95  96  96  ASN ASN A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ARG 97  98  98  ARG ARG A . n 
A 1 98  GLU 98  99  99  GLU GLU A . n 
A 1 99  GLY 99  100 100 GLY GLY A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 MET 102 103 103 MET MET A . n 
A 1 103 ALA 103 104 104 ALA ALA A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 MET 105 106 106 MET MET A . n 
A 1 106 ALA 106 107 107 ALA ALA A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 MET 109 110 110 MET MET A . n 
A 1 110 TYR 110 111 111 TYR TYR A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLN 112 113 113 GLN GLN A . n 
A 1 113 MET 113 114 114 MET MET A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 HIS 115 116 116 HIS HIS A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 VAL 117 118 118 VAL VAL A . n 
A 1 118 ASP 118 119 119 ASP ASP A . n 
A 1 119 THR 119 120 120 THR THR A . n 
A 1 120 CYS 120 121 121 CYS CYS A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 PHE 123 124 124 PHE PHE A . n 
A 1 124 ILE 124 125 125 ILE ILE A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 SER 127 128 128 SER SER A . n 
A 1 128 GLU 128 129 129 GLU GLU A . n 
B 2 1   ACE 1   0   0   ACE ACE D . n 
B 2 2   TRP 2   1   1   TRP TRP D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ILE 4   3   3   ILE ILE D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   ALA 6   5   5   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1ACA 1   201 1   A1ACA 763 A . 
D 4 CL    1   202 1   CL    CL  A . 
E 5 DMS   1   101 1   DMS   DMS D . 
F 6 HOH   1   301 7   HOH   HOH A . 
F 6 HOH   2   302 178 HOH   HOH A . 
F 6 HOH   3   303 45  HOH   HOH A . 
F 6 HOH   4   304 140 HOH   HOH A . 
F 6 HOH   5   305 166 HOH   HOH A . 
F 6 HOH   6   306 90  HOH   HOH A . 
F 6 HOH   7   307 173 HOH   HOH A . 
F 6 HOH   8   308 179 HOH   HOH A . 
F 6 HOH   9   309 94  HOH   HOH A . 
F 6 HOH   10  310 139 HOH   HOH A . 
F 6 HOH   11  311 29  HOH   HOH A . 
F 6 HOH   12  312 19  HOH   HOH A . 
F 6 HOH   13  313 75  HOH   HOH A . 
F 6 HOH   14  314 100 HOH   HOH A . 
F 6 HOH   15  315 106 HOH   HOH A . 
F 6 HOH   16  316 247 HOH   HOH A . 
F 6 HOH   17  317 202 HOH   HOH A . 
F 6 HOH   18  318 99  HOH   HOH A . 
F 6 HOH   19  319 87  HOH   HOH A . 
F 6 HOH   20  320 84  HOH   HOH A . 
F 6 HOH   21  321 142 HOH   HOH A . 
F 6 HOH   22  322 101 HOH   HOH A . 
F 6 HOH   23  323 27  HOH   HOH A . 
F 6 HOH   24  324 132 HOH   HOH A . 
F 6 HOH   25  325 47  HOH   HOH A . 
F 6 HOH   26  326 37  HOH   HOH A . 
F 6 HOH   27  327 40  HOH   HOH A . 
F 6 HOH   28  328 14  HOH   HOH A . 
F 6 HOH   29  329 91  HOH   HOH A . 
F 6 HOH   30  330 17  HOH   HOH A . 
F 6 HOH   31  331 237 HOH   HOH A . 
F 6 HOH   32  332 42  HOH   HOH A . 
F 6 HOH   33  333 119 HOH   HOH A . 
F 6 HOH   34  334 117 HOH   HOH A . 
F 6 HOH   35  335 5   HOH   HOH A . 
F 6 HOH   36  336 83  HOH   HOH A . 
F 6 HOH   37  337 193 HOH   HOH A . 
F 6 HOH   38  338 196 HOH   HOH A . 
F 6 HOH   39  339 34  HOH   HOH A . 
F 6 HOH   40  340 243 HOH   HOH A . 
F 6 HOH   41  341 122 HOH   HOH A . 
F 6 HOH   42  342 6   HOH   HOH A . 
F 6 HOH   43  343 44  HOH   HOH A . 
F 6 HOH   44  344 12  HOH   HOH A . 
F 6 HOH   45  345 4   HOH   HOH A . 
F 6 HOH   46  346 239 HOH   HOH A . 
F 6 HOH   47  347 151 HOH   HOH A . 
F 6 HOH   48  348 86  HOH   HOH A . 
F 6 HOH   49  349 242 HOH   HOH A . 
F 6 HOH   50  350 145 HOH   HOH A . 
F 6 HOH   51  351 85  HOH   HOH A . 
F 6 HOH   52  352 20  HOH   HOH A . 
F 6 HOH   53  353 89  HOH   HOH A . 
F 6 HOH   54  354 51  HOH   HOH A . 
F 6 HOH   55  355 24  HOH   HOH A . 
F 6 HOH   56  356 30  HOH   HOH A . 
F 6 HOH   57  357 244 HOH   HOH A . 
F 6 HOH   58  358 96  HOH   HOH A . 
F 6 HOH   59  359 124 HOH   HOH A . 
F 6 HOH   60  360 50  HOH   HOH A . 
F 6 HOH   61  361 93  HOH   HOH A . 
F 6 HOH   62  362 97  HOH   HOH A . 
F 6 HOH   63  363 175 HOH   HOH A . 
F 6 HOH   64  364 186 HOH   HOH A . 
F 6 HOH   65  365 25  HOH   HOH A . 
F 6 HOH   66  366 21  HOH   HOH A . 
F 6 HOH   67  367 141 HOH   HOH A . 
F 6 HOH   68  368 207 HOH   HOH A . 
F 6 HOH   69  369 103 HOH   HOH A . 
F 6 HOH   70  370 170 HOH   HOH A . 
F 6 HOH   71  371 70  HOH   HOH A . 
F 6 HOH   72  372 76  HOH   HOH A . 
F 6 HOH   73  373 133 HOH   HOH A . 
F 6 HOH   74  374 144 HOH   HOH A . 
F 6 HOH   75  375 177 HOH   HOH A . 
F 6 HOH   76  376 15  HOH   HOH A . 
F 6 HOH   77  377 169 HOH   HOH A . 
F 6 HOH   78  378 180 HOH   HOH A . 
F 6 HOH   79  379 229 HOH   HOH A . 
F 6 HOH   80  380 192 HOH   HOH A . 
F 6 HOH   81  381 74  HOH   HOH A . 
F 6 HOH   82  382 39  HOH   HOH A . 
F 6 HOH   83  383 167 HOH   HOH A . 
F 6 HOH   84  384 28  HOH   HOH A . 
F 6 HOH   85  385 245 HOH   HOH A . 
F 6 HOH   86  386 105 HOH   HOH A . 
F 6 HOH   87  387 55  HOH   HOH A . 
F 6 HOH   88  388 32  HOH   HOH A . 
F 6 HOH   89  389 194 HOH   HOH A . 
F 6 HOH   90  390 131 HOH   HOH A . 
F 6 HOH   91  391 205 HOH   HOH A . 
F 6 HOH   92  392 191 HOH   HOH A . 
F 6 HOH   93  393 108 HOH   HOH A . 
F 6 HOH   94  394 16  HOH   HOH A . 
F 6 HOH   95  395 64  HOH   HOH A . 
F 6 HOH   96  396 174 HOH   HOH A . 
F 6 HOH   97  397 241 HOH   HOH A . 
F 6 HOH   98  398 157 HOH   HOH A . 
F 6 HOH   99  399 92  HOH   HOH A . 
F 6 HOH   100 400 22  HOH   HOH A . 
F 6 HOH   101 401 165 HOH   HOH A . 
F 6 HOH   102 402 129 HOH   HOH A . 
F 6 HOH   103 403 120 HOH   HOH A . 
F 6 HOH   104 404 69  HOH   HOH A . 
F 6 HOH   105 405 67  HOH   HOH A . 
F 6 HOH   106 406 35  HOH   HOH A . 
F 6 HOH   107 407 26  HOH   HOH A . 
F 6 HOH   108 408 185 HOH   HOH A . 
F 6 HOH   109 409 212 HOH   HOH A . 
F 6 HOH   110 410 176 HOH   HOH A . 
F 6 HOH   111 411 60  HOH   HOH A . 
F 6 HOH   112 412 46  HOH   HOH A . 
F 6 HOH   113 413 236 HOH   HOH A . 
F 6 HOH   114 414 43  HOH   HOH A . 
F 6 HOH   115 415 82  HOH   HOH A . 
F 6 HOH   116 416 190 HOH   HOH A . 
F 6 HOH   117 417 36  HOH   HOH A . 
F 6 HOH   118 418 204 HOH   HOH A . 
F 6 HOH   119 419 215 HOH   HOH A . 
F 6 HOH   120 420 88  HOH   HOH A . 
F 6 HOH   121 421 223 HOH   HOH A . 
F 6 HOH   122 422 56  HOH   HOH A . 
F 6 HOH   123 423 57  HOH   HOH A . 
F 6 HOH   124 424 65  HOH   HOH A . 
F 6 HOH   125 425 61  HOH   HOH A . 
F 6 HOH   126 426 68  HOH   HOH A . 
F 6 HOH   127 427 95  HOH   HOH A . 
F 6 HOH   128 428 110 HOH   HOH A . 
F 6 HOH   129 429 147 HOH   HOH A . 
F 6 HOH   130 430 41  HOH   HOH A . 
F 6 HOH   131 431 135 HOH   HOH A . 
F 6 HOH   132 432 116 HOH   HOH A . 
F 6 HOH   133 433 200 HOH   HOH A . 
F 6 HOH   134 434 168 HOH   HOH A . 
F 6 HOH   135 435 214 HOH   HOH A . 
F 6 HOH   136 436 187 HOH   HOH A . 
F 6 HOH   137 437 227 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   142 442 171 HOH   HOH A . 
F 6 HOH   143 443 225 HOH   HOH A . 
F 6 HOH   144 444 121 HOH   HOH A . 
F 6 HOH   145 445 63  HOH   HOH A . 
F 6 HOH   146 446 71  HOH   HOH A . 
F 6 HOH   147 447 234 HOH   HOH A . 
F 6 HOH   148 448 220 HOH   HOH A . 
F 6 HOH   149 449 203 HOH   HOH A . 
F 6 HOH   150 450 125 HOH   HOH A . 
F 6 HOH   151 451 158 HOH   HOH A . 
F 6 HOH   152 452 217 HOH   HOH A . 
F 6 HOH   153 453 181 HOH   HOH A . 
F 6 HOH   154 454 114 HOH   HOH A . 
F 6 HOH   155 455 238 HOH   HOH A . 
F 6 HOH   156 456 235 HOH   HOH A . 
F 6 HOH   157 457 79  HOH   HOH A . 
F 6 HOH   158 458 81  HOH   HOH A . 
F 6 HOH   159 459 246 HOH   HOH A . 
F 6 HOH   160 460 221 HOH   HOH A . 
F 6 HOH   161 461 115 HOH   HOH A . 
F 6 HOH   162 462 107 HOH   HOH A . 
F 6 HOH   163 463 216 HOH   HOH A . 
F 6 HOH   164 464 188 HOH   HOH A . 
F 6 HOH   165 465 183 HOH   HOH A . 
F 6 HOH   166 466 230 HOH   HOH A . 
F 6 HOH   167 467 182 HOH   HOH A . 
F 6 HOH   168 468 201 HOH   HOH A . 
F 6 HOH   169 469 213 HOH   HOH A . 
F 6 HOH   170 470 113 HOH   HOH A . 
F 6 HOH   171 471 48  HOH   HOH A . 
F 6 HOH   172 472 206 HOH   HOH A . 
F 6 HOH   173 473 148 HOH   HOH A . 
F 6 HOH   174 474 172 HOH   HOH A . 
F 6 HOH   175 475 211 HOH   HOH A . 
G 6 HOH   1   201 62  HOH   HOH D . 
G 6 HOH   2   202 38  HOH   HOH D . 
G 6 HOH   3   203 78  HOH   HOH D . 
G 6 HOH   4   204 23  HOH   HOH D . 
G 6 HOH   5   205 73  HOH   HOH D . 
G 6 HOH   6   206 53  HOH   HOH D . 
G 6 HOH   7   207 240 HOH   HOH D . 
G 6 HOH   8   208 49  HOH   HOH D . 
G 6 HOH   9   209 58  HOH   HOH D . 
G 6 HOH   10  210 195 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 A LYS 126 ? CG  ? A LYS 125 CG  
8  1 Y 1 A LYS 126 ? CD  ? A LYS 125 CD  
9  1 Y 1 A LYS 126 ? CE  ? A LYS 125 CE  
10 1 Y 1 A LYS 126 ? NZ  ? A LYS 125 NZ  
11 1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
12 1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
13 1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
14 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com phasing           
http://www.globalphasing.com/buster/                ?   ? 
5 PDB_EXTRACT 3.24   'Sep. 1, 2017' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.entry_id           7GV0 
_cell.length_a           67.770 
_cell.length_b           67.770 
_cell.length_c           166.810 
_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                         7GV0 
_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          7GV0 
_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   66.30 
_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                     7GV0 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             34.000 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23791 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.081 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.100 
_reflns.B_iso_Wilson_estimate        32.550 
_reflns.pdbx_redundancy              9.000 
_reflns.pdbx_Rrim_I_all              0.086 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     215200 
_reflns.pdbx_scaling_rejects         845 
_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  ? 11966 1285 ? 1.422 ? ? ? 9.300 ? 1.500  ? ? ? ? ? ? 100.000 1.504 0.486 0.743 ? 
1 2 9.090 34.000 ? 1507  234  ? 0.050 ? ? ? 6.400 ? 29.400 ? ? ? ? ? ? 98.800  0.055 0.021 0.997 ? 
# 
_refine.entry_id                                 7GV0 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             33.9900 
_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                     23717 
_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                          0.1820 
_refine.ls_R_factor_R_work                       0.1810 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2090 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1500 
_refine.ls_number_reflns_R_free                  1221 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               37.5900 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.2578 
_refine.aniso_B[2][2]                            0.2578 
_refine.aniso_B[3][3]                            -0.5156 
_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          0.9440 
_refine.overall_SU_R_Cruickshank_DPI             0.0870 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0880 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0990 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0970 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                128.210 
_refine.B_iso_min                                19.070 
_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                        7GV0 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.230 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.7500 
_refine_hist.d_res_low                        33.9900 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             185 
_refine_hist.number_atoms_total               1231 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           32.47 
_refine_hist.pdbx_B_iso_mean_solvent          55.26 
_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      1636 ?      ? 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           ?    3.360  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.610 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.7500 
_refine_ls_shell.d_res_low                        1.8300 
_refine_ls_shell.pdbx_total_number_of_bins_used   12 
_refine_ls_shell.percent_reflns_obs               99.6800 
_refine_ls_shell.number_reflns_R_work             2690 
_refine_ls_shell.R_factor_all                     0.3167 
_refine_ls_shell.R_factor_R_work                  0.3140 
_refine_ls_shell.R_factor_R_free                  0.3762 
_refine_ls_shell.percent_reflns_R_free            4.6400 
_refine_ls_shell.number_reflns_R_free             131 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2821 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GV0 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 11.25 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GV0 
_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 7GV0       7GV0   ? 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 7GV0 A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GV0 D 1 ? 6   ? 7GV0   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 7GV0 GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GV0 PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GV0 GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7410  ? 
1 MORE         -64   ? 
1 'SSA (A^2)'  13030 ? 
# 
_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 33.8850000000 0.8660254038 
-0.5000000000 0.0000000000 -58.6905416145 0.0000000000 0.0000000000 -1.0000000000 27.8016666667 
# 
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 ? ? ? ? ? ? ? 1.335 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O PHE A 42 ? O PHE A 43 N ILE A 35 ? N ILE A 36 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GV0 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 39 ? A 61.39 -119.33 
2 1 SER A 39 ? B 38.52 64.14   
3 1 ARG A 40 ? B 75.55 -21.15  
4 1 SER A 93 ? A 75.86 -4.48   
# 
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 377 ? F HOH . 
3 1 A HOH 456 ? F HOH . 
4 1 A HOH 465 ? F HOH . 
5 1 A HOH 466 ? F HOH . 
6 1 A HOH 468 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.2144 -16.5503 24.6837 0.0198  -0.0482 -0.0767 -0.0397 0.0320  -0.0246 1.0608 1.7996  2.0113 
0.4438  -0.2780 1.1938 0.1366 -0.0735 -0.0631 -0.0492 0.1059 0.0954 0.2644  0.0038 -0.0113 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1173 0.1252  -0.0502 -0.0246 -0.0244 -0.0985 0.9871 -0.3794 0.0000 
-0.0436 0.1333  0.0943 0.0154 -0.0038 -0.0116 -0.0009 0.0155 0.0405 -0.0186 0.0121 -0.0126 
# 
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                    7GV0 
_atom_sites.fract_transf_matrix[1][1]   0.014756 
_atom_sites.fract_transf_matrix[1][2]   0.008519 
_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]   0.017039 
_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]   0.005995 
_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   ? 17.300 -21.276 -4.806 1.00 67.62  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.225 -22.149 -5.533 1.00 66.58  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.772 -23.630 -5.485 1.00 66.19  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.708 -23.940 -4.937 1.00 66.91  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.657 -21.989 -4.965 1.00 67.41  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.753 -22.032 -6.020 1.00 81.58  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.920 -23.098 -6.667 1.00 81.98  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.452 -21.008 -6.192 1.00 88.88  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.573 -24.533 -6.076 1.00 57.47  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.315 -25.971 -6.077 1.00 54.77  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.305 -26.702 -5.120 1.00 50.37  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.594 -27.883 -5.309 1.00 49.47  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.399 -26.522 -7.497 1.00 60.50  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.676 -26.295 -8.072 1.00 71.81  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.788 -26.003 -4.075 1.00 41.64  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.724 -26.571 -3.103 1.00 38.39  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.100 -27.722 -2.295 1.00 38.80  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.883 -27.765 -2.117 1.00 39.24  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.220 -25.478 -2.154 1.00 39.20  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.381 -24.289 -2.891 1.00 44.45  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.939 -28.628 -1.783 1.00 30.13  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.569 -29.618 -0.770 1.00 27.36  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.194 -29.080 0.525  1.00 28.79  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.149 -28.293 0.466  1.00 27.28  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.916 -31.101 -1.080 1.00 30.06  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.436 -31.281 -1.328 1.00 29.10  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.092 -31.622 -2.261 1.00 29.89  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.943 -32.738 -1.537 1.00 34.10  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.714 -29.503 1.700  0.66 23.58  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.594 -29.428 1.659  0.34 24.56  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.270 -29.018 2.965  0.66 22.87  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 21.015 -28.937 2.954  0.34 23.56  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.623 -30.172 3.891  0.66 25.79  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.413 -30.071 3.877  0.34 27.28  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.858 -31.128 3.982  0.66 25.88  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.706 -31.072 3.967  0.34 27.40  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.278 -28.050 3.656  0.66 24.62  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.887 -28.108 3.577  0.34 24.82  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.645 -27.705 5.120  0.66 26.10  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.385 -27.115 4.624  0.34 28.76  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.099 -26.396 5.626  0.66 48.06  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.646 -27.247 5.930  0.34 41.45  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.485 -25.618 4.893  0.66 42.38  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.425 -27.439 5.970  0.34 32.13  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.343 -26.106 6.902  0.66 42.68  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.373 -27.125 7.034  0.34 38.03  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.762 -30.077 4.591  0.66 22.94  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.534 -29.897 4.574  0.34 23.94  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.147 -31.093 5.571  0.66 22.44  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.050 -30.873 5.529  0.34 23.79  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.685 -30.592 6.937  0.66 25.09  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.560 -30.430 6.890  0.34 26.16  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.290 -29.660 7.503  0.66 23.39  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.996 -29.382 7.399  0.34 25.24  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.666 -31.389 5.532  0.66 23.32  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.586 -30.958 5.427  0.34 25.28  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 25.046 -32.596 6.360  0.66 24.23  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.051 -31.743 4.219  0.34 27.75  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.664 -33.879 5.970  0.66 27.90  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.799 -31.286 2.927  0.34 31.47  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.820 -32.457 7.509  0.66 25.82  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.721 -32.950 4.371  0.34 30.98  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 25.001 -34.993 6.751  0.66 29.28  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.219 -32.015 1.812  0.34 32.55  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.151 -33.568 8.290  0.66 28.37  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.138 -33.682 3.249  0.34 34.52  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.751 -34.828 7.900  0.66 27.10  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.882 -33.210 1.980  0.34 32.37  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.589 -31.185 7.442  1.00 22.52  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.915 -30.817 8.709  1.00 22.82  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.878 -30.564 9.888  1.00 25.19  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.752 -29.537 10.568 1.00 25.08  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.843 -31.853 9.074  1.00 30.44  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.941 -31.981 7.960  1.00 29.98  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.042 -31.459 10.338 1.00 34.91  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.814 -31.497 10.111 1.00 22.94  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.736 -31.407 11.261 1.00 23.94  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.987 -30.525 11.056 1.00 25.11  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.808 -30.438 11.983 1.00 23.44  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.178 -32.827 11.686 1.00 29.03  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.071 -33.773 12.190 1.00 40.95  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.482 -33.357 13.526 1.00 62.23  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.444 -33.443 14.629 1.00 74.50  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.308 -32.814 15.792 1.00 85.26  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.226 -32.953 16.739 1.00 74.07  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.263 -32.024 16.011 1.00 67.02  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.153 -29.883 9.880  1.00 20.93  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.389 -29.145 9.592  1.00 21.17  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.674 -28.054 10.617 1.00 22.55  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.809 -27.992 11.124 1.00 22.53  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.377 -28.554 8.166  1.00 21.40  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.640 -27.809 7.854  1.00 23.54  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.823 -28.480 7.634  1.00 24.25  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.859 -26.480 7.722  1.00 23.98  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.727 -27.548 7.384  1.00 24.03  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.193 -26.330 7.419  1.00 23.53  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.675 -27.170 10.892 1.00 20.60  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.901 -26.047 11.833 1.00 20.99  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.320 -26.547 13.230 1.00 23.28  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.238 -25.978 13.830 1.00 20.53  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.669 -25.140 11.917 1.00 22.43  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.666 -27.609 13.721 0.42 22.36  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.664 -27.614 13.726 0.30 21.82  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.665 -27.609 13.738 0.28 21.49  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.955 -28.206 15.023 0.42 22.54  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.955 -28.217 15.031 0.30 21.93  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.981 -28.178 15.052 0.28 21.41  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.372 -28.776 15.054 0.42 25.62  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.364 -28.802 15.065 0.30 25.77  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.375 -28.805 15.075 0.28 25.60  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.102 -28.545 16.026 0.42 22.22  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.078 -28.622 16.057 0.30 23.49  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.092 -28.649 16.068 0.28 23.42  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.921 -29.281 15.354 0.42 26.34  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.921 -29.287 15.373 0.30 25.28  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.912 -29.173 15.495 0.28 24.13  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.146 -29.847 16.634 0.42 30.45  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.614 -28.744 15.441 0.30 28.38  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.839 -30.287 14.620 0.28 25.12  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.770 -29.482 13.973 1.00 23.22  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.103 -30.092 13.839 1.00 24.52  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.179 -28.989 13.800 1.00 24.43  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.232 -29.149 14.405 1.00 24.29  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.163 -30.961 12.577 1.00 26.58  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.351 -32.255 12.658 1.00 37.46  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.815 -32.562 13.755 1.00 34.67  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.244 -32.957 11.624 1.00 39.88  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.903 -27.869 13.093 1.00 20.45  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.842 -26.745 13.051 1.00 20.10  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.053 -26.198 14.475 1.00 23.03  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.189 -26.026 14.916 1.00 21.34  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.358 -25.637 12.075 1.00 22.34  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.123 -24.331 12.289 1.00 22.39  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.434 -26.106 10.615 1.00 21.42  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.960 -25.979 15.206 1.00 19.87  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.074 -25.403 16.546 1.00 20.83  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.803 -26.364 17.498 1.00 22.15  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.660 -25.917 18.283 1.00 21.33  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.695 -25.013 17.083 1.00 21.20  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.726 -24.078 18.325 1.00 24.47  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.311 -22.690 17.985 1.00 25.03  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.333 -23.911 18.891 1.00 29.76  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.510 -27.667 17.380 1.00 22.04  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.186 -28.692 18.179 1.00 22.36  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.707 -28.608 17.933 1.00 23.91  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.491 -28.593 18.899 1.00 22.92  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.654 -30.085 17.805 1.00 24.29  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.224 -31.258 18.602 1.00 32.67  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.784 -31.184 20.073 1.00 34.92  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.737 -32.573 18.022 1.00 37.50  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.120 -28.480 16.655 1.00 21.65  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.541 -28.368 16.315 1.00 21.52  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.171 -27.070 16.823 1.00 23.77  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.311 -27.082 17.273 1.00 23.38  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.763 -28.576 14.837 1.00 25.21  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.724 -30.043 14.464 1.00 32.65  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.976 -30.934 15.294 1.00 29.11  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.410 -30.335 13.203 1.00 27.08  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.433 -25.951 16.736 1.00 20.79  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.899 -24.663 17.280 1.00 21.18  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.116 -24.808 18.790 1.00 23.89  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.117 -24.308 19.315 1.00 23.20  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.905 -23.521 16.980 1.00 21.23  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.790 -23.127 15.483 1.00 24.77  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.666 -22.096 15.276 1.00 25.62  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.118 -22.600 14.917 1.00 25.13  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.188 -25.508 19.496 1.00 21.36  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.359 -25.734 20.940 1.00 22.57  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.596 -26.620 21.246 1.00 26.12  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.283 -26.383 22.238 1.00 26.34  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.101 -26.329 21.569 1.00 22.91  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.133 -26.203 23.078 1.00 29.65  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.672 -25.239 23.643 1.00 27.73  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.552 -27.163 23.754 1.00 30.44  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.898 -27.620 20.378 1.00 23.65  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.089 -28.477 20.531 1.00 25.21  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.348 -27.619 20.380 1.00 28.51  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.302 -27.793 21.134 1.00 28.69  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 37.091 -29.580 19.470 1.00 24.02  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 36.055 -30.664 19.772 1.00 26.91  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.895 -31.626 18.601 1.00 32.06  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 35.040 -32.748 18.977 1.00 37.77  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.367 -33.510 18.121 1.00 52.58  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.399 -33.250 16.818 1.00 40.17  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.636 -34.523 18.562 1.00 44.26  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.333 -26.659 19.429 1.00 25.28  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.469 -25.751 19.265 1.00 25.23  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.637 -24.892 20.518 1.00 28.88  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.767 -24.725 21.004 1.00 29.56  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.269 -24.842 18.058 1.00 24.56  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.277 -25.524 16.679 1.00 28.62  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.168 -24.478 15.577 1.00 28.99  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.558 -26.383 16.479 1.00 30.63  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.514 -24.365 21.059 1.00 24.46  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.576 -23.571 22.290 1.00 24.91  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.197 -24.404 23.456 1.00 29.77  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 40.081 -23.893 24.165 1.00 30.31  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.178 -23.076 22.690 1.00 25.92  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.290 -22.159 23.913 1.00 29.84  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.981 -21.564 24.313 1.00 32.50  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.995 -22.571 24.691 1.00 30.39  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.358 -22.606 25.858 1.00 41.75  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.676 -21.748 26.825 1.00 36.83  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.429 -23.521 26.082 1.00 32.20  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.725 -25.645 23.651 0.39 27.97  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.730 -25.659 23.630 0.28 27.85  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.726 -25.647 23.652 0.33 27.84  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.198 -26.543 24.714 0.39 29.26  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.182 -26.615 24.654 0.28 29.16  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.200 -26.549 24.711 0.33 29.12  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.711 -26.816 24.642 0.39 34.96  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.697 -26.818 24.628 0.28 34.81  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.713 -26.811 24.640 0.33 34.83  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.356 -26.936 25.686 0.39 35.90  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.323 -26.919 25.685 0.28 35.67  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.358 -26.924 25.684 0.33 35.70  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.405 -27.846 24.715 0.39 32.43  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.512 -27.970 24.445 0.28 32.63  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.429 -27.864 24.680 0.33 32.31  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.775 -28.710 23.651 0.39 38.08  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.140 -27.965 24.793 0.28 39.44  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.849 -28.732 25.722 0.33 39.43  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.274 -26.891 23.417 1.00 31.35  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.711 -27.130 23.201 1.00 33.10  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.508 -25.836 23.003 1.00 35.87  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.717 -25.886 22.742 1.00 37.06  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.893 -28.109 22.034 1.00 35.28  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.142 -29.423 22.253 1.00 40.64  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.088 -30.262 20.998 1.00 44.93  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.431 -30.636 20.555 1.00 59.04  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.764 -30.836 19.286 1.00 73.91  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 45.011 -31.152 18.963 1.00 64.93  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.860 -30.697 18.329 1.00 58.24  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.834 -24.678 23.168 1.00 29.81  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.392 -23.336 23.022 1.00 30.75  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.991 -23.112 21.611 1.00 35.13  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 45.041 -22.489 21.460 1.00 37.00  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.410 -23.038 24.155 1.00 34.14  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.708 -21.565 24.323 1.00 44.51  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.783 -20.746 24.114 1.00 43.39  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.864 -21.228 24.663 1.00 50.70  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.329 -23.647 20.580 1.00 29.11  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.839 -23.543 19.211 1.00 28.83  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.231 -22.342 18.500 1.00 31.74  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 42.004 -22.220 18.415 1.00 28.58  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.629 -24.858 18.415 1.00 31.73  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.437 -26.029 19.042 1.00 33.52  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.975 -24.658 16.912 1.00 31.20  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 44.004 -27.432 18.532 1.00 38.64  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.110 -21.458 17.984 1.00 30.15  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.745 -20.260 17.226 1.00 30.17  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.841 -19.273 17.992 1.00 31.31  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.236 -18.408 17.367 1.00 29.08  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.161 -20.586 15.843 1.00 30.78  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.193 -21.128 14.807 1.00 38.25  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.597 -21.166 13.457 1.00 38.65  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.439 -20.275 14.738 1.00 44.83  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.825 -19.347 19.335 1.00 27.84  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.149 -18.343 20.160 1.00 27.13  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.979 -17.056 19.969 1.00 33.46  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.209 -17.120 19.843 1.00 33.63  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 42.051 -18.781 21.621 1.00 32.20  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.362 -19.107 22.067 1.00 34.27  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.089 -19.985 21.814 1.00 29.37  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.309 -15.917 19.824 1.00 29.98  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.975 -14.666 19.479 1.00 30.61  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.635 -13.514 20.389 1.00 31.82  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.986 -12.366 20.099 1.00 32.01  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.675 -14.320 18.005 1.00 32.25  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.199 -14.274 17.622 1.00 40.90  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.337 -14.470 18.517 1.00 35.49  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.906 -14.047 16.433 1.00 50.95  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.957 -13.805 21.503 1.00 26.17  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.648 -12.758 22.472 1.00 25.82  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.480 -13.354 23.863 1.00 28.97  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 41.076 -14.520 24.006 1.00 28.10  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.388 -11.912 22.034 1.00 28.76  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 39.076 -12.698 22.184 1.00 27.17  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.311 -10.564 22.780 1.00 29.35  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.781 -12.543 24.883 0.60 25.39  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.785 -12.559 24.894 0.40 25.25  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.560 -12.872 26.284 0.60 25.27  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.525 -12.943 26.272 0.40 24.93  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.492 -11.880 26.759 0.60 28.41  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.559 -11.906 26.866 0.40 28.64  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.627 -10.674 26.518 0.60 28.31  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.796 -10.699 26.756 0.40 28.87  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.864 -12.748 27.132 0.60 30.35  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.779 -13.260 27.142 0.40 29.69  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.606 -13.005 28.619 0.60 30.56  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.656 -12.034 27.374 0.40 30.20  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.947 -13.683 26.615 0.60 30.82  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.387 -13.907 28.468 0.40 29.77  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.436 -12.386 27.407 1.00 24.46  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.385 -11.563 28.011 1.00 25.11  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.674 -11.598 29.502 1.00 30.08  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.680 -12.687 30.111 1.00 29.10  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.940 -12.045 27.688 1.00 27.08  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.684 -12.208 26.162 1.00 26.46  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.898 -11.133 28.338 1.00 27.98  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.990 -10.972 25.271 1.00 26.52  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.906 -10.416 30.078 1.00 27.08  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.222 -10.277 31.501 1.00 27.60  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.959 -9.862  32.243 1.00 31.89  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.346 -8.842  31.907 1.00 30.59  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.410 -9.303  31.760 1.00 32.62  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.722 -9.190  33.257 1.00 33.52  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.660 -9.747  31.009 1.00 33.37  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.572 -10.658 33.255 1.00 29.24  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.374 -10.424 34.060 1.00 29.76  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.860 -10.461 35.499 1.00 36.94  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 37.029 -11.541 36.074 1.00 33.67  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.250 -11.461 33.766 1.00 33.36  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.935 -11.031 34.405 1.00 33.54  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 35.069 -11.682 32.259 1.00 32.38  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.212 -9.282  36.040 0.54 37.26  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.065 -9.257  36.068 0.46 36.42  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.798 -9.116  37.376 0.54 38.91  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.580 -9.004  37.413 0.46 37.82  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.155 -9.873  37.447 0.54 40.33  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.690 -10.003 37.780 0.46 40.21  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 40.045 -9.579  36.648 0.54 39.21  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.521 -10.877 38.637 0.46 40.15  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.824 -9.551  38.476 0.54 44.86  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.452 -8.933  38.435 0.46 42.74  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.567 -8.901  38.363 0.54 59.50  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.766 -7.697  38.299 0.46 51.81  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.287 -10.867 38.351 0.54 36.35  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.791 -9.903  37.009 0.46 34.56  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.508 -11.658 38.538 0.54 36.42  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 41.047 -10.660 37.050 0.46 34.81  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.612 -12.840 37.571 0.54 38.73  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.931 -12.083 36.472 0.46 37.48  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.640 -13.525 37.560 0.54 38.61  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.956 -12.615 36.035 0.46 38.18  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.617 -12.154 39.995 0.54 36.54  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.715 -10.657 38.438 0.46 36.12  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 41.052 -11.083 40.987 0.54 42.75  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.217 -9.267  38.835 0.46 47.61  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.372 -11.690 42.339 0.54 41.50  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.218 -9.307  39.969 0.46 53.98  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.597 -10.669 43.360 0.54 43.90  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.643 -7.962  40.368 0.46 61.01  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.782 -10.149 43.667 0.54 60.62  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.053 -7.233  41.312 0.46 72.73  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.883 -9.229  44.614 0.54 48.16  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 41.996 -7.705  41.962 0.46 57.91  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.875 -10.538 43.021 0.54 50.38  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.511 -6.024  41.607 0.46 58.92  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.555 -13.092 36.775 0.54 33.80  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.704 -12.669 36.396 0.46 32.78  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.531 -14.222 35.840 0.54 32.80  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.469 -13.998 35.790 0.46 32.09  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.817 -13.813 34.398 0.54 34.86  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.612 -13.864 34.266 0.46 34.60  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.495 -12.700 33.987 0.54 32.85  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 39.005 -12.971 33.677 0.46 32.39  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.195 -14.995 35.929 0.54 34.06  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.081 -14.552 36.166 0.46 33.43  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.901 -15.568 37.309 0.54 50.41  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.999 -15.086 37.587 0.46 47.25  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.194 -17.046 37.468 0.54 86.74  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.189 -16.585 37.698 0.46 81.84  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.454 -17.869 36.880 0.54 87.58  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.223 -17.011 38.261 0.46 82.83  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.160 -17.384 38.192 0.54 87.13  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.306 -17.336 37.220 0.46 82.62  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.407 -14.746 33.631 1.00 31.47  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.729 -14.623 32.213 1.00 30.75  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.089 -15.745 31.422 1.00 32.55  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.132 -16.895 31.864 1.00 32.92  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.252 -14.657 32.020 1.00 33.43  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.966 -13.436 32.602 1.00 48.86  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.432 -13.337 32.246 1.00 69.02  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 45.006 -14.167 31.524 1.00 61.31  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 45.074 -12.302 32.758 1.00 71.89  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.504 -15.422 30.255 1.00 26.54  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.853 -16.423 29.387 1.00 26.71  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.365 -16.244 27.981 1.00 30.55  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.206 -15.156 27.415 1.00 30.55  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.319 -16.259 29.396 1.00 27.63  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.690 -16.359 30.764 1.00 29.32  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.588 -15.236 31.588 1.00 31.83  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.227 -17.578 31.246 1.00 32.37  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 36.029 -15.331 32.860 1.00 33.99  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.671 -17.672 32.528 1.00 35.70  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.581 -16.549 33.327 1.00 33.66  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.972 -17.297 27.404 1.00 27.33  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.477 -17.239 26.038 1.00 25.56  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.344 -17.647 25.093 1.00 28.21  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.532 -18.528 25.420 1.00 27.17  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.702 -18.155 25.843 1.00 27.58  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.931 -17.738 26.704 1.00 33.20  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.248 -18.141 26.048 1.00 43.39  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.263 -17.737 24.637 1.00 54.60  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.862 -16.653 24.155 1.00 67.89  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.595 -15.882 24.947 1.00 60.18  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.772 -16.358 22.866 1.00 50.53  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.257 -16.987 23.940 1.00 24.83  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.185 -17.285 22.970 1.00 25.16  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.562 -16.867 21.561 1.00 26.63  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.647 -16.338 21.337 1.00 25.12  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.881 -16.594 23.385 1.00 26.38  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.663 -17.154 20.600 1.00 23.34  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.832 -16.738 19.211 1.00 22.74  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.957 -15.493 19.027 1.00 25.78  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.750 -15.534 19.314 1.00 24.06  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.361 -17.860 18.259 1.00 22.37  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.120 -19.142 18.446 1.00 25.89  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.642 -20.154 19.273 1.00 27.51  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.346 -19.499 17.983 1.00 26.99  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.562 -21.114 19.239 1.00 27.58  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.619 -20.751 18.497 1.00 27.47  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.559 -14.390 18.563 1.00 24.48  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.811 -13.139 18.319 1.00 23.63  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.573 -13.391 17.441 1.00 24.69  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.517 -12.850 17.745 1.00 22.78  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.707 -12.106 17.607 1.00 25.51  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.714 -11.498 18.555 1.00 26.09  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.623 -10.558 17.769 1.00 24.23  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.697 -10.043 18.668 1.00 31.74  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.683 -9.284  17.875 1.00 32.07  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.690 -14.221 16.392 1.00 21.81  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.560 -14.438 15.478 1.00 21.99  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.381 -15.093 16.165 1.00 23.52  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.242 -14.738 15.885 1.00 24.12  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.981 -15.186 14.220 1.00 29.38  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.601 -16.400 14.630 1.00 31.26  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.889 -14.338 13.321 1.00 31.18  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.649 -16.041 17.056 1.00 20.68  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.566 -16.725 17.767 1.00 20.82  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.890 -15.746 18.722 1.00 22.76  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.645 -15.714 18.799 1.00 21.17  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 33.054 -18.015 18.487 1.00 22.48  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.939 -18.615 19.350 1.00 23.36  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.530 -19.057 17.458 1.00 22.17  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.692 -14.953 19.455 1.00 21.10  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.125 -13.941 20.358 1.00 20.87  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.207 -12.956 19.590 1.00 23.20  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.092 -12.662 20.050 1.00 22.78  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.249 -13.163 21.084 1.00 20.58  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.212 -13.970 22.003 1.00 24.04  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.264 -13.042 22.639 1.00 24.01  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.433 -14.721 23.098 1.00 25.48  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.668 -12.475 18.424 1.00 21.19  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.888 -11.562 17.591 1.00 22.75  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.592 -12.207 17.100 1.00 26.95  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.545 -11.549 17.080 1.00 26.98  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.700 -11.084 16.395 1.00 24.11  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.913 -10.273 16.782 1.00 26.39  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.948 -10.179 15.325 1.00 31.16  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.131 -8.884  14.476 1.00 27.64  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.654 -13.500 16.730 1.00 23.71  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.492 -14.232 16.214 1.00 23.09  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.382 -14.430 17.278 1.00 25.50  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.223 -14.660 16.919 1.00 26.82  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.930 -15.596 15.645 1.00 23.68  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.750 -14.361 18.579 1.00 22.13  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.847 -14.623 19.698 1.00 22.19  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.404 -13.406 20.485 1.00 25.66  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.447 -13.530 21.250 1.00 24.82  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.511 -15.623 20.646 1.00 22.22  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.863 -17.232 19.906 1.00 25.53  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.167 -12.299 20.419 1.00 22.22  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.972 -11.156 21.314 1.00 20.90  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.974 -9.844  20.564 1.00 25.58  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.942 -9.554  19.842 1.00 23.72  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.107 -11.174 22.339 1.00 22.67  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.402 -9.929  22.958 1.00 25.73  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.931 -9.036  20.781 1.00 23.99  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.854 -7.702  20.186 1.00 23.78  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.980 -6.808  20.678 1.00 26.57  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.511 -5.991  19.910 1.00 26.65  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.395 -6.991  21.957 1.00 24.71  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.501 -6.208  22.525 1.00 25.58  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.837 -6.544  21.829 1.00 27.10  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.527 -5.616  21.377 1.00 26.02  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.606 -6.385  24.057 1.00 25.36  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.653 -5.504  24.749 1.00 29.67  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.199 -4.023  24.805 1.00 31.15  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.977 -6.038  26.140 1.00 27.57  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.168 -7.859  21.698 1.00 22.57  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.425 -8.242  21.029 1.00 21.94  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.401 -7.898  19.559 1.00 26.30  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.438 -7.516  19.017 1.00 25.80  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.799 -9.700  21.285 1.00 22.58  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.218 -9.927  22.722 1.00 23.71  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.303 -9.238  23.271 1.00 26.47  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.552 -10.856 23.519 1.00 25.30  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.675 -9.433  24.618 1.00 27.24  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.971 -11.102 24.837 1.00 28.07  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 33.011 -10.375 25.384 1.00 26.29  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.211 -7.963  18.922 1.00 23.73  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.081 -7.555  17.512 1.00 25.07  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.516 -6.083  17.354 1.00 29.54  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.322 -5.778  16.469 1.00 28.03  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.633 -7.770  17.042 1.00 26.94  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.371 -7.235  15.656 1.00 30.69  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 28.968 -7.812  14.539 1.00 32.68  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.537 -6.138  15.462 1.00 34.54  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.728 -7.316  13.253 1.00 35.64  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.288 -5.638  14.187 1.00 37.62  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.869 -6.246  13.087 1.00 44.69  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.607 -5.748  11.842 1.00 49.57  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.993 -5.185  18.218 0.53 26.96  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.990 -5.190  18.223 0.47 26.86  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.323 -3.754  18.205 0.53 28.11  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.315 -3.760  18.230 0.47 27.97  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.813 -3.516  18.521 0.53 32.88  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.815 -3.549  18.496 0.47 32.67  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.454 -2.715  17.845 0.53 34.55  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.461 -2.799  17.767 0.47 34.07  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.427 -3.002  19.184 0.53 30.79  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.486 -3.038  19.289 0.47 30.61  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 28.084 -3.031  18.729 0.53 34.85  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.777 -1.650  19.288 0.47 36.24  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.365 -4.234  19.517 1.00 28.73  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.781 -4.124  19.908 1.00 27.85  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.726 -4.511  18.776 1.00 31.10  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.598 -3.715  18.411 1.00 32.26  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.110 -4.945  21.208 1.00 29.29  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.367 -4.379  22.441 1.00 29.91  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.638 -5.005  21.469 1.00 27.41  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.388 -5.363  23.653 1.00 33.10  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.537 -5.703  18.193 1.00 25.88  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.516 -6.145  17.216 1.00 26.83  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.292 -5.618  15.798 1.00 31.13  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.148 -5.864  14.946 1.00 32.26  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.705 -7.659  17.255 1.00 26.78  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.111 -8.159  18.630 1.00 27.22  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.315 -7.763  19.210 1.00 30.32  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.290 -9.026  19.340 1.00 27.75  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.682 -8.222  20.484 1.00 30.78  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.673 -9.510  20.595 1.00 30.25  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.857 -9.093  21.166 1.00 28.47  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.212 -4.853  15.551 1.00 28.18  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 34.053 -4.162  14.257 1.00 29.45  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.614 -2.743  14.398 1.00 36.12  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.706 -1.998  13.406 1.00 36.05  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.623 -4.179  13.713 1.00 35.83  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.742 -3.664  14.703 1.00 32.78  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.178 -5.576  13.241 1.00 32.66  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 35.016 -2.355  15.633 1.00 32.91  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.631 -1.041  15.836 1.00 34.29  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 37.060 -1.093  15.291 1.00 39.05  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.821 -1.983  15.664 1.00 36.04  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.613 -0.627  17.318 1.00 36.17  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.362 0.664   17.551 1.00 47.61  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.754 1.738   17.380 1.00 52.50  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.576 0.600   17.842 1.00 48.05  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.427 -0.123  14.432 1.00 40.76  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.730 -0.052  13.769 1.00 42.37  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.938 -0.083  14.719 1.00 45.89  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 40.996 -0.556  14.303 1.00 47.80  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.805 1.153   12.819 1.00 45.93  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.970 0.968   11.553 1.00 63.10  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.800 0.410   15.970 1.00 38.93  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.892 0.341   16.946 1.00 38.03  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.811 -0.915  17.799 1.00 41.68  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.830 -1.553  18.042 1.00 43.47  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.883 1.547   17.902 1.00 38.80  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.500 2.830   17.388 1.00 45.38  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.376 3.917   18.429 1.00 46.56  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 42.976 2.648   17.012 1.00 50.47  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.622 -1.228  18.329 1.00 35.43  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.465 -2.357  19.247 1.00 33.31  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.614 -3.718  18.578 1.00 38.19  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 40.019 -4.660  19.252 1.00 36.60  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.148 -2.281  20.037 1.00 33.66  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 38.014 -1.054  20.928 1.00 32.90  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.725 -1.126  21.729 1.00 29.35  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.407 0.176   22.440 1.00 36.11  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.890 1.218   21.518 1.00 36.32  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.339 -3.808  17.258 1.00 37.34  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.471 -5.062  16.487 1.00 37.92  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.872 -5.688  16.622 1.00 42.68  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 41.014 -6.902  16.444 1.00 42.80  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.096 -4.850  15.020 1.00 40.13  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.252 -3.801  14.088 1.00 46.68  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.896 -4.848  16.920 1.00 38.74  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.304 -5.234  17.036 1.00 39.38  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.785 -5.528  18.453 1.00 41.82  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.957 -5.872  18.650 1.00 41.13  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.200 -4.177  16.372 1.00 41.27  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 43.978 -4.096  14.875 1.00 56.67  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.881 -3.011  14.300 1.00 55.78  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.844 -5.242  14.212 1.00 44.99  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.902 -5.383  19.445 1.00 37.87  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.295 -5.647  20.822 1.00 36.73  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.280 -7.147  21.100 1.00 38.94  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.392 -7.855  20.607 1.00 37.11  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.359 -4.921  21.806 1.00 36.64  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.351 -3.385  21.743 1.00 41.49  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.294 -2.827  22.670 1.00 41.46  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.736 -2.787  22.068 1.00 43.16  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.256 -7.628  21.886 0.51 36.24  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.261 -7.619  21.888 0.49 36.14  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.346 -9.042  22.264 0.51 35.62  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.391 -9.024  22.283 0.49 35.52  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.732 -9.266  23.653 0.51 36.47  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.762 -9.260  23.661 0.49 36.47  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.518 -10.411 24.055 0.51 34.44  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.562 -10.409 24.061 0.49 34.48  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.796 -9.520  22.226 0.51 40.72  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.860 -9.441  22.288 0.49 40.46  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.602 -8.775  23.123 0.51 49.18  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.393 -9.420  20.975 0.49 47.67  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.462 -8.166  24.391 1.00 33.32  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.853 -8.203  25.726 1.00 32.92  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.674 -7.216  25.764 1.00 34.11  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.848 -6.040  25.402 1.00 33.59  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.887 -7.864  26.854 1.00 38.16  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.229 -7.845  28.237 1.00 38.23  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 45.081 -8.823  26.843 1.00 39.02  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.507 -7.687  26.246 1.00 27.28  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.299 -6.880  26.461 1.00 26.41  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.907 -7.002  27.932 1.00 29.71  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.695 -8.113  28.426 1.00 29.85  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.130 -7.259  25.498 1.00 29.04  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.535 -7.108  23.995 1.00 30.27  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.827 -6.494  25.836 1.00 30.42  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.872 -5.674  23.476 1.00 34.83  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.799 -5.851  28.632 1.00 27.85  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.407 -5.830  30.027 1.00 28.32  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.922 -5.517  30.146 1.00 31.05  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.485 -4.443  29.724 1.00 29.30  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.228 -4.782  30.804 1.00 31.85  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.709 -4.989  30.733 1.00 50.99  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.228 -6.025  31.130 1.00 41.01  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.425 -3.993  30.250 1.00 49.81  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.152 -6.424  30.754 1.00 25.81  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.725 -6.172  30.950 1.00 25.46  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.495 -5.281  32.172 1.00 28.94  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.375 -5.144  33.039 1.00 30.17  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.891 -7.471  31.085 1.00 25.18  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.968 -8.494  29.920 1.00 28.21  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.861 -9.579  30.067 1.00 28.96  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.912 -7.810  28.540 1.00 28.73  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.293 -4.711  32.252 1.00 25.78  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.852 -3.841  33.349 1.00 27.87  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 33.045 -4.600  34.685 1.00 33.01  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.714 -5.785  34.749 1.00 32.34  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.372 -3.467  33.146 1.00 29.73  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.829 -2.434  34.123 1.00 40.47  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.733 -2.745  35.331 1.00 40.96  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.478 -1.326  33.676 1.00 43.12  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.593 -3.956  35.738 1.00 34.00  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.824 -4.685  37.007 1.00 34.11  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.591 -5.258  37.689 1.00 37.13  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.744 -6.113  38.561 1.00 38.42  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.521 -3.649  37.907 1.00 37.10  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.213 -2.327  37.301 1.00 42.89  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.074 -2.559  35.824 1.00 36.81  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.382 -4.819  37.302 1.00 33.53  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.135 -5.335  37.883 1.00 35.34  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.842 -6.744  37.321 1.00 35.39  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 29.005 -7.462  37.870 1.00 34.45  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.960 -4.393  37.543 1.00 38.08  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.814 -4.418  38.540 1.00 59.30  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 28.008 -3.519  39.747 1.00 89.48  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.048 -2.281  39.565 1.00 89.82  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.115 -4.053  40.875 1.00 85.64  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.510 -7.129  36.216 1.00 30.44  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.279 -8.434  35.590 1.00 29.90  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.868 -9.565  36.420 1.00 34.05  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 32.036 -9.525  36.811 1.00 32.84  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.743 -8.467  34.105 1.00 31.63  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 30.029 -7.363  33.279 1.00 32.63  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.513 -9.860  33.479 1.00 28.21  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.416 -7.348  33.351 1.00 38.39  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 30.040 -10.560 36.673 1.00 33.31  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.356 -11.748 37.457 1.00 33.80  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.096 -12.788 36.592 1.00 33.29  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.566 -13.187 35.553 1.00 31.82  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 29.054 -12.331 38.035 1.00 36.64  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.256 -13.610 38.802 1.00 50.14  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.954 -14.693 38.309 1.00 41.36  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.777 -13.511 40.020 1.00 42.74  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.309 -13.248 37.010 1.00 30.51  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 33.052 -14.246 36.206 1.00 30.05  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.290 -15.556 35.953 1.00 33.20  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.393 -16.105 34.855 1.00 32.25  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.322 -14.491 37.032 1.00 33.72  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.467 -13.279 37.894 1.00 38.35  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 33.071 -12.856 38.217 1.00 33.92  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.519 -16.054 36.952 1.00 30.45  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.756 -17.294 36.751 1.00 30.50  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.666 -17.089 35.681 1.00 32.21  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.523 -17.943 34.816 1.00 30.28  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.162 -17.833 38.069 1.00 33.31  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.556 -19.217 37.867 1.00 43.34  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.742 -19.813 39.002 1.00 68.94  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.732 -21.059 39.115 1.00 69.56  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.102 -19.050 39.763 1.00 61.56  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.934 -15.963 35.744 1.00 30.48  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.915 -15.623 34.753 1.00 30.10  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.517 -15.569 33.356 1.00 30.87  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.951 -16.115 32.387 1.00 28.18  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.712 -14.962 33.254 1.00 26.80  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.408 -14.893 31.964 1.00 25.53  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.799 -16.296 31.488 1.00 26.68  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.606 -16.624 30.314 1.00 26.19  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.652 -13.986 32.014 1.00 26.88  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.262 -13.858 30.636 1.00 26.65  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.694 -13.016 29.681 1.00 29.87  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.322 -14.669 30.249 1.00 27.44  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.206 -12.955 28.384 1.00 30.23  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.841 -14.601 28.955 1.00 29.22  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.262 -13.765 28.021 1.00 27.94  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.374 -17.112 32.384 1.00 26.64  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.765 -18.490 32.053 1.00 29.30  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.573 -19.305 31.490 1.00 29.61  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.712 -19.984 30.468 1.00 27.87  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.375 -19.173 33.272 1.00 32.88  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.064 -20.810 32.915 1.00 38.75  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.400 -19.224 32.160 1.00 27.05  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.179 -19.931 31.743 1.00 25.54  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.775 -19.478 30.340 1.00 26.22  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.427 -20.317 29.487 1.00 23.49  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 27.053 -19.704 32.795 1.00 28.47  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.342 -20.530 34.100 1.00 29.06  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.642 -19.998 32.226 1.00 28.30  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.637 -20.021 35.293 1.00 33.87  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.852 -18.173 30.092 1.00 23.26  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.499 -17.617 28.774 1.00 23.12  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.510 -17.972 27.690 1.00 25.44  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.111 -18.269 26.562 1.00 23.52  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.243 -16.122 28.847 1.00 24.32  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.943 -15.752 29.606 1.00 30.16  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.839 -14.281 29.757 1.00 31.22  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.689 -16.265 28.879 1.00 32.75  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.804 -17.972 28.023 1.00 23.67  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.843 -18.377 27.064 1.00 22.86  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.608 -19.852 26.660 1.00 25.33  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.655 -20.193 25.475 1.00 23.77  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.238 -18.162 27.677 1.00 23.05  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.413 -18.464 26.715 1.00 27.69  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.365 -17.567 25.460 1.00 27.00  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.774 -18.332 27.447 1.00 29.99  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.330 -20.725 27.642 1.00 23.12  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 29.990 -22.123 27.360 1.00 23.15  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.778 -22.214 26.429 1.00 24.67  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.807 -23.000 25.487 1.00 24.63  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.696 -22.857 28.671 1.00 26.30  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.932 -23.221 29.479 1.00 41.00  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.053 -23.174 28.911 1.00 42.35  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.778 -23.575 30.675 1.00 41.82  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.715 -21.433 26.698 1.00 23.13  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.517 -21.381 25.841 1.00 21.60  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.895 -20.997 24.397 1.00 22.59  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.423 -21.613 23.423 1.00 20.50  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.484 -20.384 26.408 1.00 22.02  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.366 -20.126 25.422 1.00 22.29  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.405 -21.105 25.165 1.00 24.70  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.330 -18.947 24.674 1.00 25.04  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.403 -20.894 24.217 1.00 24.15  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.319 -18.738 23.716 1.00 27.28  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.376 -19.722 23.485 1.00 25.42  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.718 -19.960 24.251 1.00 19.65  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.129 -19.519 22.906 1.00 19.07  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.696 -20.661 22.083 1.00 22.65  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.370 -20.785 20.909 1.00 22.61  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.207 -18.420 23.004 1.00 20.10  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.677 -17.137 23.586 1.00 21.91  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 30.021 -15.904 23.489 1.00 25.89  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.342 -14.652 24.590 1.00 25.86  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.558 -21.482 22.702 1.00 19.93  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.241 -22.578 22.010 1.00 19.80  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.490 -23.914 21.992 1.00 24.34  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.968 -24.867 21.359 1.00 23.10  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.635 -22.774 22.635 1.00 21.01  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.680 -21.793 22.136 1.00 22.18  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.833 -20.542 22.733 1.00 24.00  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.543 -22.133 21.089 1.00 23.44  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.815 -19.641 22.288 1.00 23.63  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.558 -21.264 20.674 1.00 24.17  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.672 -20.013 21.262 1.00 26.33  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.688 -19.187 20.856 1.00 24.50  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.339 -24.019 22.689 1.00 21.36  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.636 -25.317 22.739 1.00 22.16  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.110 -25.298 22.512 1.00 24.48  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.543 -26.391 22.310 1.00 24.31  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.828 -26.002 24.136 1.00 25.37  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.150 -25.232 25.147 1.00 25.42  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.299 -26.209 24.535 1.00 27.61  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.453 -24.111 22.593 0.67 20.51  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.459 -24.113 22.631 0.33 20.95  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 23.977 -23.923 22.555 0.67 20.49  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 23.996 -23.889 22.589 0.33 21.11  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.332 -24.324 23.899 0.67 23.38  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.314 -24.412 23.875 0.33 24.87  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.136 -24.114 24.068 0.67 23.38  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.085 -24.454 23.941 0.33 24.93  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.311 -24.714 21.419 0.67 20.78  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.352 -24.491 21.336 0.33 23.43  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.960 -24.542 20.171 0.67 20.86  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.071 -25.875 21.473 0.33 28.06  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.121 -24.860 24.866 0.67 21.18  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.120 -24.785 24.899 0.33 22.17  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.581 -25.277 26.170 0.67 21.74  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.647 -25.314 26.184 0.33 22.84  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.830 -24.223 27.231 0.67 26.17  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.858 -24.271 27.278 0.33 26.73  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.959 -23.748 27.403 0.67 25.27  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.987 -23.818 27.494 0.33 25.85  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.166 -26.622 26.620 0.67 24.91  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.376 -26.631 26.541 0.33 24.81  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.863 -27.770 25.654 0.67 29.50  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.265 -27.728 25.473 0.33 32.86  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.847 -28.918 25.862 0.67 36.71  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.105 -28.668 25.728 0.33 38.95  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.773 -29.446 27.226 0.67 45.63  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.950 -29.668 24.669 0.33 41.78  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 23.980 -30.446 27.595 0.67 57.93  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.249 -30.958 24.802 0.33 54.03  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.208 -31.054 26.703 0.67 46.33  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.060 -31.796 23.792 0.33 45.66  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 23.962 -30.854 28.856 0.67 42.97  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.723 -31.422 25.951 0.33 35.98  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.770 -23.887 27.962 1.00 23.97  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.819 -22.875 29.016 1.00 23.36  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.582 -23.515 30.371 1.00 29.40  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.509 -24.087 30.609 1.00 28.38  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.766 -21.802 28.716 1.00 23.86  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.813 -20.573 29.656 1.00 27.30  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.085 -19.727 29.392 1.00 25.79  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.544 -19.731 29.521 1.00 29.86  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.586 -23.418 31.268 1.00 28.35  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.498 -23.986 32.624 1.00 30.21  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.803 -22.982 33.563 1.00 34.98  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.450 -22.297 34.352 1.00 35.40  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.898 -24.398 33.137 1.00 33.71  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.882 -25.005 34.531 1.00 51.91  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.888 -25.581 34.973 1.00 42.34  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.974 -24.864 35.265 1.00 47.01  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.491 -22.861 33.408 1.00 32.06  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.667 -21.921 34.151 1.00 33.51  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.135 -22.576 35.422 1.00 37.08  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.491 -23.636 35.365 1.00 36.52  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.550 -21.435 33.215 1.00 34.39  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.796 -20.176 33.574 1.00 40.76  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.755 -18.961 33.680 1.00 41.05  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.701 -19.920 32.541 1.00 40.95  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.492 -21.986 36.583 1.00 34.95  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.122 -22.502 37.910 1.00 36.80  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.592 -21.376 38.795 1.00 37.91  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.914 -20.201 38.573 1.00 35.22  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.336 -23.165 38.598 1.00 38.47  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.960 -24.322 37.809 1.00 45.30  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.205 -24.902 38.469 1.00 63.37  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.920 -25.527 39.767 1.00 82.84  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.495 -26.778 39.933 1.00 104.19 ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.257 -27.248 41.151 1.00 92.40  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.293 -27.565 38.881 1.00 95.15  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.774 -21.722 39.801 1.00 36.95  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.237 -20.717 40.732 1.00 37.48  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.354 -19.820 41.314 1.00 42.48  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.181 -18.601 41.393 1.00 42.21  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.438 -21.399 41.873 1.00 40.83  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.754 -20.418 42.811 1.00 52.03  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.026 -21.030 43.995 1.00 82.64  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.582 -21.947 44.643 1.00 78.77  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.896 -20.573 44.284 1.00 83.02  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.492 -20.426 41.656 1.00 39.97  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.633 -19.720 42.237 1.00 39.95  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.416 -18.817 41.298 1.00 40.08  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.158 -17.946 41.755 1.00 40.49  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.263 -18.996 39.979 1.00 34.93  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 23.035 -18.188 39.033 1.00 32.55  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.189 -17.334 38.079 1.00 36.28  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.764 -16.536 37.325 1.00 35.09  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 24.003 -19.098 38.252 1.00 31.14  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.352 -20.028 37.250 1.00 39.68  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.291 -19.737 36.692 1.00 31.07  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 23.999 -21.151 36.959 1.00 33.69  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.843 -17.528 38.068 1.00 34.15  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.966 -16.869 37.080 1.00 33.92  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.098 -15.342 37.064 1.00 34.71  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.118 -14.751 35.974 1.00 32.05  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.482 -17.307 37.152 1.00 38.18  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.673 -16.727 35.954 1.00 38.55  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.829 -17.015 38.515 1.00 38.02  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.527 -17.585 35.480 1.00 41.61  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.202 -14.706 38.236 1.00 33.94  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.341 -13.249 38.272 1.00 34.56  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.645 -12.773 37.631 1.00 36.56  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.612 -11.835 36.833 1.00 34.09  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.164 -12.687 39.698 1.00 39.01  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.782 -12.972 40.300 1.00 46.37  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.366 -12.574 39.229 1.00 52.87  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.352 -10.773 39.351 1.00 50.90  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.782 -13.446 37.940 1.00 34.20  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.095 -13.106 37.363 1.00 33.63  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.102 -13.386 35.858 1.00 34.11  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.622 -12.575 35.087 1.00 32.31  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.201 -13.906 38.043 1.00 35.08  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.520 -14.520 35.439 1.00 29.38  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.448 -14.887 34.013 1.00 26.58  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.637 -13.847 33.233 1.00 28.78  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.123 -13.370 32.201 1.00 27.32  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.951 -16.345 33.803 1.00 29.88  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.669 -16.640 32.326 1.00 28.11  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.963 -17.336 34.360 1.00 29.93  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.438 -13.471 33.730 0.20 27.85  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.431 -13.478 33.720 0.80 28.70  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.591 -12.470 33.073 0.20 28.76  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.618 -12.470 33.024 0.80 30.21  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.300 -11.117 32.937 0.20 33.06  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.330 -11.107 32.920 0.80 33.27  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.283 -10.535 31.850 0.20 32.19  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.321 -10.488 31.848 0.80 31.77  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.250 -12.302 33.796 0.20 32.43  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.250 -12.303 33.688 0.80 33.72  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.279 -11.428 33.033 0.20 36.61  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.335 -11.361 32.919 0.80 37.73  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.759 -11.121 33.937 0.20 42.46  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.646 -11.393 33.543 0.80 43.25  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.204 -9.669  33.106 0.20 39.79  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.803 -10.365 35.088 0.80 41.30  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.926 -10.630 34.029 1.00 30.60  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.665 -9.349  34.040 1.00 30.93  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.826 -9.388  33.027 1.00 31.16  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 24.001 -8.439  32.249 1.00 29.35  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.188 -9.055  35.440 1.00 32.27  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.559 -10.520 32.972 1.00 26.85  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.667 -10.673 32.023 1.00 25.76  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.141 -10.710 30.570 1.00 28.56  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.727 -10.046 29.697 1.00 26.25  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.590 -11.858 32.391 1.00 29.44  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.885 -11.830 33.798 1.00 30.15  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.898 -11.851 31.583 1.00 29.99  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 24.035 -11.469 30.312 1.00 26.35  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.446 -11.558 28.967 1.00 25.40  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.925 -10.187 28.501 1.00 27.76  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.116 -9.833  27.333 1.00 25.83  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.346 -12.617 28.926 1.00 26.04  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.358 -9.369  29.423 1.00 26.44  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.923 -8.012  29.048 1.00 26.45  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.126 -7.141  28.613 1.00 29.47  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.080 -6.473  27.581 1.00 29.54  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.154 -7.363  30.210 1.00 29.80  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.777 -7.973  30.402 1.00 34.98  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 19.020 -7.398  31.943 1.00 43.05  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.739 -5.663  31.516 1.00 41.21  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.206 -7.193  29.382 1.00 26.52  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.442 -6.454  29.097 1.00 26.01  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 26.061 -6.923  27.762 1.00 28.56  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.458 -6.095  26.927 1.00 25.53  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.410 -6.692  30.253 1.00 26.53  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.817 -6.183  30.017 1.00 26.48  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.113 -4.823  30.112 1.00 29.77  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.868 -7.069  29.788 1.00 25.89  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.414 -4.351  29.904 1.00 27.11  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.175 -6.612  29.619 1.00 26.09  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.440 -5.254  29.684 1.00 30.17  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.736 -4.848  29.554 1.00 27.44  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.086 -8.243  27.543 1.00 25.96  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.656 -8.835  26.328 1.00 24.22  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.726 -8.727  25.116 1.00 27.43  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.155 -8.986  23.992 1.00 26.54  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.066 -10.298 26.571 1.00 23.36  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.206 -10.568 27.574 1.00 25.91  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.495 -12.092 27.659 1.00 25.87  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.516 -9.817  27.184 1.00 26.98  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.463 -8.333  25.338 1.00 24.91  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.466 -8.196  24.264 1.00 25.21  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.212 -9.554  23.584 1.00 28.42  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.455 -9.750  22.393 1.00 27.93  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.864 -7.091  23.263 1.00 25.95  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 24.018 -5.710  23.924 1.00 29.63  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.713 -4.746  22.996 1.00 40.41  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.568 -4.815  21.782 1.00 34.09  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.494 -3.833  23.543 1.00 37.33  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.764 -10.506 24.402 1.00 24.46  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.436 -11.880 23.982 1.00 24.27  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.937 -12.051 24.246 1.00 30.92  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.519 -12.549 25.298 1.00 29.57  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.307 -12.840 24.790 1.00 24.94  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.777 -12.729 24.429 1.00 26.68  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.794 -13.755 25.484 1.00 30.20  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.449 -15.431 24.723 1.00 27.14  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.128 -11.523 23.308 1.00 30.99  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.660 -11.412 23.403 1.00 33.11  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.909 -12.696 23.753 1.00 33.35  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 17.013 -12.634 24.588 1.00 33.07  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.061 -10.801 22.127 1.00 36.19  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.570 -9.395  21.850 1.00 49.06  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.247 -13.843 23.133 1.00 30.22  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.520 -15.081 23.444 1.00 31.76  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.768 -15.557 24.877 1.00 32.73  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.831 -16.035 25.524 1.00 33.45  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.803 -16.177 22.411 1.00 33.69  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.410 -15.797 21.018 1.00 38.95  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.092 -15.541 20.683 1.00 43.16  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.171 -15.699 19.902 1.00 40.90  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 16.097 -15.255 19.391 1.00 42.81  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.323 -15.344 18.878 1.00 42.08  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 19.006 -15.372 25.394 1.00 26.67  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.344 -15.730 26.781 1.00 26.53  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.551 -14.821 27.727 1.00 31.74  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.920 -15.315 28.664 1.00 30.88  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.869 -15.715 27.096 1.00 29.72  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.118 -16.002 28.581 1.00 30.01  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.616 -16.727 26.225 1.00 28.76  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.560 -13.497 27.467 1.00 28.20  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.799 -12.541 28.292 1.00 29.11  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.307 -12.964 28.366 1.00 34.96  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.755 -13.039 29.462 1.00 34.34  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.985 -11.070 27.824 1.00 31.57  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.140 -10.105 28.676 1.00 32.54  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.458 -10.663 27.879 1.00 30.21  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.709 -13.311 27.212 0.61 33.46  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.678 -13.217 27.199 0.39 33.28  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.321 -13.763 27.091 0.61 35.06  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.272 -13.618 27.060 0.39 34.88  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 14.010 -14.998 27.949 0.61 37.24  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.899 -14.830 27.916 0.39 38.35  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 13.013 -14.970 28.674 0.61 38.10  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.872 -14.797 28.593 0.39 39.39  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.965 -14.014 25.614 0.61 37.50  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.933 -13.895 25.580 0.39 37.05  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.518 -14.410 25.383 0.61 53.11  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.702 -12.669 24.713 0.39 50.05  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.622 -13.601 25.710 0.61 56.96  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.259 -11.631 25.251 0.39 53.25  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.284 -15.525 24.872 0.61 59.04  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.940 -12.756 23.488 0.39 56.36  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.843 -16.073 27.883 0.61 32.16  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.731 -15.891 27.891 0.39 33.66  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.567 -17.271 28.702 0.61 32.66  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.478 -17.122 28.649 0.39 34.07  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.753 -16.990 30.193 0.61 36.08  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.680 -16.898 30.155 0.39 37.14  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.039 -17.580 31.003 0.61 35.36  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.893 -17.427 30.943 0.39 37.13  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.326 -18.535 28.240 0.61 33.27  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.277 -18.301 28.076 0.39 40.09  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.743 -19.659 28.907 0.61 35.78  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.228 -18.237 26.649 0.39 38.82  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.825 -18.491 28.554 0.61 28.66  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.727 -19.642 28.523 0.39 40.53  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.705 -16.101 30.549 1.00 32.87  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.961 -15.732 31.960 1.00 33.63  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.740 -15.025 32.513 1.00 39.24  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.279 -15.384 33.605 1.00 38.91  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.201 -14.857 32.091 1.00 33.53  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.756 -15.754 31.897 1.00 36.05  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.193 -14.048 31.745 0.48 36.86  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.199 -14.035 31.761 0.52 37.05  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.992 -13.279 32.107 0.48 38.75  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 13.002 -13.286 32.163 0.52 39.02  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.805 -14.208 32.367 0.48 43.46  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.797 -14.210 32.377 0.52 43.55  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.063 -14.006 33.333 0.48 43.71  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.040 -14.015 33.333 0.52 43.72  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.619 -12.284 30.996 0.48 40.00  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.664 -12.195 31.141 0.52 40.71  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.570 -11.107 30.865 0.48 52.61  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.426 -10.893 31.366 0.52 54.89  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.961 -9.977  30.056 0.48 66.15  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.714 -9.710  30.727 0.52 67.08  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.961 -8.970  29.694 0.48 71.91  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.852 -9.703  29.268 0.52 72.36  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.306 -7.935  30.456 0.48 83.31  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.639 -8.874  28.590 0.52 82.48  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.727 -7.748  31.636 0.48 74.37  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.362 -7.960  29.228 0.52 67.53  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.230 -7.079  30.042 0.48 65.27  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.703 -8.946  27.268 0.52 66.60  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.638 -15.226 31.505 1.00 39.90  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.546 -16.209 31.594 1.00 41.29  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.685 -17.126 32.807 1.00 44.67  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.698  -17.330 33.518 1.00 43.80  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.414 -17.008 30.290 1.00 43.15  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.850  -16.163 29.155 1.00 62.02  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.728  -16.919 27.849 1.00 74.72  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.308  -15.981 26.744 1.00 89.05  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.456  -16.659 25.735 1.00 101.77 ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.912 -17.640 33.072 1.00 39.94  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.179 -18.503 34.233 1.00 40.29  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 11.978 -17.732 35.542 1.00 45.35  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.408 -18.283 36.490 1.00 45.02  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.582 -19.127 34.149 1.00 40.70  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.710 -20.397 33.320 1.00 42.02  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.156 -20.479 32.044 1.00 45.04  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.453 -21.479 33.785 1.00 44.50  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.276 -21.653 31.281 1.00 45.73  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.587 -22.646 33.013 1.00 45.91  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 13.998 -22.724 31.770 1.00 43.46  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.380 -16.441 35.571 1.00 41.08  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.180 -15.570 36.741 1.00 42.54  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.679 -15.309 36.972 1.00 49.20  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.216 -15.436 38.111 1.00 50.20  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.040 -14.275 36.660 1.00 44.44  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.534 -14.630 36.813 1.00 42.77  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.618 -13.237 37.738 1.00 46.99  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.492 -13.624 36.252 1.00 49.14  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.913  -15.009 35.891 1.00 47.12  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.464  -14.762 35.990 1.00 49.91  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.711  -15.990 36.529 1.00 54.95  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.748  -15.829 37.272 1.00 55.08  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.875  -14.323 34.643 1.00 53.21  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.170  -17.208 36.180 1.00 50.73  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.545  -18.450 36.652 1.00 52.31  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.712  -18.681 38.165 1.00 59.13  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.838  -19.281 38.777 1.00 59.95  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.100  -19.639 35.879 1.00 51.47  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.830  -18.228 38.757 1.00 57.56  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.119  -18.440 40.179 1.00 60.28  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.520  -17.383 41.127 1.00 68.72  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.491  -17.620 42.339 1.00 71.04  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.623 -18.575 40.407 1.00 64.03  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 11.047 -19.917 40.224 1.00 74.73  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.015  -16.247 40.593 1.00 65.51  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.427  -15.172 41.409 1.00 84.68  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 5.993  -15.474 41.878 1.00 128.21 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.592  -16.631 41.995 1.00 95.58  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.511  -13.808 40.692 1.00 85.11  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.483  -13.594 39.588 1.00 95.36  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.645  -12.361 38.718 1.00 116.81 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.778  -11.835 38.610 1.00 111.25 ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.631  -11.929 38.122 1.00 110.23 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.258 -35.139 5.838  1.00 30.18  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.336 -34.000 6.326  1.00 30.83  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.460 -36.374 6.710  1.00 30.54  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.980 -35.377 4.557  0.66 27.81  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.992 -35.373 4.551  0.34 28.35  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.764 -34.328 3.565  0.66 26.86  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.705 -34.300 3.601  0.34 27.73  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.252 -34.181 3.261  0.66 31.53  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.198 -34.148 3.455  0.34 31.01  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.549 -35.194 3.150  0.66 31.52  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.453 -35.127 3.589  0.34 30.20  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.572 -34.652 2.285  0.66 25.88  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.360 -34.532 2.213  0.34 26.84  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.066 -34.641 2.481  0.66 26.05  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.717 -35.599 1.368  0.34 27.77  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.854 -35.677 2.892  0.66 28.67  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.086 -36.908 1.292  0.34 30.86  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.945 -33.531 2.262  0.66 25.34  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.619 -35.437 0.448  0.34 27.84  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.168 -35.268 2.984  0.66 27.58  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.263 -37.585 0.424  0.34 30.59  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.255 -33.960 2.584  0.66 28.64  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.359 -36.706 -0.116 0.34 31.81  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.750 -32.195 1.871  0.66 26.10  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.807 -34.351 0.074  0.34 28.61  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.368 -33.114 2.479  0.66 28.26  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.326 -36.918 -1.036 0.34 31.23  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.859 -31.372 1.731  0.66 27.20  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.780 -34.565 -0.831 0.34 30.25  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.143 -31.826 2.054  0.66 27.82  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.553 -35.833 -1.384 0.34 30.80  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.752 -32.927 3.155  1.00 27.06  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.332 -32.615 2.913  1.00 27.04  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.193 -31.559 1.809  1.00 29.07  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.164 -30.874 1.465  1.00 27.68  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.597 -32.118 4.210  1.00 29.84  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.643 -33.158 5.336  1.00 29.55  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.145 -30.760 4.693  1.00 29.66  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.958 -31.381 1.334  1.00 25.81  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.574 -30.295 0.443  1.00 25.36  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.191 -29.163 1.423  1.00 30.41  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.174 -29.294 2.126  1.00 29.78  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.372 -30.668 -0.463 1.00 27.55  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.656 -31.925 -1.353 1.00 26.24  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.929 -29.428 -1.303 1.00 29.61  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.995 -31.819 -2.316 1.00 31.99  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.983 -28.071 1.510  1.00 30.57  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.651 -27.006 2.472  1.00 31.18  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.406 -26.200 2.105  1.00 34.50  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.099 -26.043 0.928  1.00 33.35  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.919 -26.139 2.495  1.00 32.88  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.518 -26.323 1.125  1.00 37.15  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.216 -27.757 0.752  1.00 32.72  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.741 -25.622 3.116  1.00 33.97  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.515 -10.192 16.501 1.00 27.70  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.932 -8.922  16.546 1.00 26.56  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.913 -8.639  17.446 1.00 27.62  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.472 -9.654  18.291 1.00 29.00  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.296 -10.838 19.850 1.00 33.51  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 24.007 -10.937 18.222 1.00 27.58  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.317 -10.276 11.945 1.00 32.21  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.445 -10.621 13.277 1.00 29.88  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.409 -10.270 14.171 1.00 28.93  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.290 -11.794 19.225 1.00 30.77  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.471 -11.099 20.721 1.00 34.62  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.471 -9.622  19.268 1.00 31.39  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 25.027 -11.213 17.322 1.00 26.28  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.407 -10.602 15.491 1.00 26.46  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.321 -9.649  13.683 1.00 31.43  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.315 -9.398  12.385 1.00 33.44  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.877 -8.625  11.798 0.46 33.94  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 29.004 -11.505 13.855 0.70 28.09  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.233 -9.656  11.470 1.00 31.81  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.351 -15.388 22.701 1.00 39.23  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.582 -35.469 -1.286 0.66 48.50  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.298 -35.240 -0.640 0.66 49.34  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.715 -34.559 -0.272 0.66 47.73  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 18.014 -37.101 -0.787 0.66 48.61  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 25.860 -3.571  26.512 1.00 36.68  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 35.753 -25.866 25.587 1.00 40.36  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 26.812 -32.113 16.171 1.00 45.81  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 41.160 -21.709 25.240 1.00 44.31  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 22.746 -5.472  19.952 1.00 56.16  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 29.814 -32.316 9.565  1.00 51.20  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 44.410 -0.875  17.952 1.00 52.03  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 33.390 -20.972 29.611 1.00 46.50  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 20.836 -5.903  26.221 1.00 43.34  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 23.414 -5.928  32.998 1.00 38.86  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 37.831 2.374   19.846 1.00 42.86  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 38.556 -15.014 15.550 1.00 37.02  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 20.403 -13.568 20.630 1.00 48.04  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 45.111 -11.211 18.915 1.00 64.64  ? 314 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 6 .   ? 16.473 -27.484 -3.287 1.00 52.93  ? 315 HOH   A O   1 
HETATM 1216 O  O   A HOH   F 6 .   ? 19.072 -22.998 4.415  0.67 48.78  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 37.254 -12.531 40.348 1.00 67.47  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 15.464 -10.078 25.073 1.00 51.04  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 31.759 -0.954  15.915 1.00 45.38  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 19.961 -9.718  37.157 1.00 41.41  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 43.714 -6.618  32.015 1.00 53.38  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 22.725 -27.695 17.771 1.00 48.98  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 27.277 -10.257 35.969 1.00 40.48  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 30.381 1.379   33.860 1.00 69.30  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 37.762 -20.572 27.030 1.00 36.48  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 28.425 -9.005  40.026 1.00 49.33  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 17.906 -29.486 7.696  1.00 36.63  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 27.360 -28.274 18.661 1.00 28.47  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 25.734 -3.003  20.120 1.00 60.16  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 41.336 -16.991 15.224 1.00 41.88  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 28.805 -21.922 41.696 1.00 74.36  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 28.301 -23.855 31.773 1.00 41.44  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 21.466 -27.245 14.693 0.50 37.35  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 23.310 -17.102 44.341 1.00 66.21  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 29.430 -27.451 20.681 1.00 26.89  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 21.747 -29.553 -5.256 1.00 39.68  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 32.767 -24.634 32.211 1.00 67.95  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 26.984 -35.383 11.612 1.00 59.25  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 30.464 -0.689  37.114 1.00 52.82  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 34.499 -23.910 29.893 1.00 78.97  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 43.998 -4.399  25.821 1.00 46.04  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 22.987 -28.307 12.682 1.00 25.61  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 24.016 -15.866 21.330 1.00 32.43  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 26.156 -22.699 29.982 1.00 27.75  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 21.962 -25.092 18.364 1.00 25.60  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 41.453 -12.766 14.059 1.00 111.58 ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 41.202 -1.428  11.696 1.00 65.81  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 24.943 -26.883 19.087 1.00 36.47  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 21.511 -30.033 14.201 1.00 74.32  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 28.925 -0.478  16.938 1.00 73.64  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 29.043 -31.218 7.277  1.00 36.17  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 36.900 -5.696  12.283 1.00 39.77  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 10.816 -11.573 34.647 1.00 47.22  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 46.875 -21.693 18.091 1.00 47.91  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 18.105 -34.604 8.332  1.00 34.99  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 37.367 -6.510  34.414 1.00 42.04  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 26.973 -16.714 38.762 1.00 56.17  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 20.926 -7.420  19.977 1.00 49.10  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 44.429 -12.771 41.453 1.00 55.27  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 26.129 -21.984 38.746 1.00 41.12  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 42.524 -10.515 15.518 1.00 55.27  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 30.739 -29.001 22.699 1.00 42.23  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 46.071 -14.236 21.599 1.00 62.27  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 24.153 -28.712 21.603 1.00 55.99  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 34.149 -8.022  35.761 1.00 38.10  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 39.026 -18.892 33.483 1.00 48.76  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 28.601 -24.342 34.445 1.00 56.48  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 46.282 -15.904 27.670 1.00 69.77  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 41.407 -7.838  46.561 1.00 57.89  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 34.843 -19.010 13.901 0.50 25.23  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 46.318 -18.986 19.641 1.00 54.26  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 43.877 -10.721 35.192 1.00 74.14  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 12.664 -20.679 42.542 1.00 59.15  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 12.274 -18.143 25.960 1.00 59.35  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 47.242 -25.228 21.626 1.00 57.06  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 20.339 -16.041 40.991 1.00 38.07  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 27.645 -23.167 13.901 0.50 26.13  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 14.369 -16.905 23.519 1.00 45.42  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 45.520 -10.891 30.326 1.00 58.25  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 17.958 -24.452 39.772 1.00 43.02  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 44.661 -16.408 29.798 1.00 54.33  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 45.298 -12.635 23.643 1.00 51.09  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 26.189 -8.110  9.063  1.00 46.18  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 38.036 -16.684 13.143 0.50 29.80  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 11.624 -15.377 40.610 1.00 81.38  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 26.077 -19.276 41.787 1.00 60.68  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 41.269 -7.061  36.007 1.00 46.82  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 23.703 -15.727 17.819 1.00 42.67  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 34.794 -29.078 26.042 1.00 67.77  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 27.171 -2.400  16.059 1.00 66.97  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 42.176 -5.944  11.941 1.00 75.60  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 19.888 -25.572 41.331 1.00 80.54  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 26.502 -30.846 19.015 1.00 62.68  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 31.907 -31.984 14.558 1.00 38.71  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 46.105 -9.049  44.196 1.00 52.81  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 47.461 -6.763  20.360 1.00 70.41  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 17.353 -24.641 -2.163 1.00 68.22  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 29.657 -22.757 36.909 1.00 66.20  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 33.168 -29.881 21.524 1.00 43.64  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 40.436 -19.687 29.069 1.00 37.18  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 16.812 -6.524  27.606 1.00 68.41  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 44.639 -8.733  17.919 1.00 71.57  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 45.821 -17.132 17.344 1.00 63.44  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 4.225  -20.442 37.926 1.00 68.62  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 21.147 -23.297 42.153 1.00 52.80  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 30.486 -10.683 40.670 1.00 44.87  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 23.007 -15.046 40.465 1.00 33.67  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 37.065 -2.322  11.572 1.00 61.92  ? 408 HOH   A O   1 
HETATM 1309 O  O   A HOH   F 6 .   ? 12.125 -20.824 27.957 0.66 47.91  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 46.938 -20.195 21.969 1.00 64.86  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 35.156 -29.827 23.454 1.00 46.91  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 27.077 -1.691  22.081 1.00 56.24  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 33.535 -33.027 12.078 1.00 47.17  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 41.278 -17.167 35.280 1.00 45.11  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 25.586 -4.622  17.961 1.00 51.82  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 35.285 1.880   13.560 1.00 58.21  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 32.237 -15.724 39.909 1.00 37.87  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 42.091 -8.114  13.829 1.00 58.73  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 19.652 -27.331 10.101 1.00 57.94  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 32.449 -9.018  39.834 1.00 61.95  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 10.476 -11.761 40.132 1.00 68.82  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 33.580 -0.369  20.156 1.00 46.03  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 25.627 -16.122 41.167 1.00 55.27  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 34.519 -18.848 36.360 1.00 66.97  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 27.399 -25.624 28.386 1.00 58.74  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 29.569 -0.815  22.323 1.00 62.23  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 39.909 -5.577  34.006 1.00 46.64  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 33.950 -32.838 21.986 1.00 65.33  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 23.613 -30.621 19.380 1.00 69.34  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 45.916 -5.561  23.792 1.00 49.89  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 31.878 -26.193 27.126 1.00 57.55  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 42.879 -18.301 30.767 1.00 50.45  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 44.455 -4.279  28.981 1.00 69.90  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 22.318 -10.614 14.687 1.00 48.55  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 37.184 -31.627 23.417 1.00 81.69  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 26.485 -29.600 22.717 1.00 60.64  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 31.965 0.001   13.360 1.00 65.53  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 23.098 -3.136  26.792 1.00 65.76  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 26.929 -34.657 18.018 1.00 68.08  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 28.804 -2.655  13.056 1.00 81.03  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 19.478 -31.811 13.864 1.00 68.89  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 35.350 -4.212  10.685 1.00 49.04  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 19.783 -8.224  24.663 1.00 52.31  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 30.679 -34.397 14.930 1.00 62.61  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 48.076 -23.440 19.774 1.00 64.31  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 36.863 -24.528 27.660 1.00 60.64  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 46.763 -14.741 18.398 1.00 67.23  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 47.471 -28.570 17.707 1.00 61.75  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 24.530 -21.832 41.133 1.00 59.45  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 47.212 -11.903 25.436 1.00 65.37  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 12.008 -18.857 22.765 1.00 66.82  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 47.110 -12.641 28.530 1.00 63.39  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 32.222 -1.124  22.376 1.00 59.00  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 35.928 -21.270 30.602 1.00 62.55  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 34.117 -17.734 39.616 1.00 66.99  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 44.017 -13.714 13.901 0.50 93.66  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 19.501 -7.717  35.407 1.00 55.62  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 25.384 -5.768  35.009 1.00 65.81  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 45.623 -8.445  31.415 1.00 65.46  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 17.107 -7.970  25.002 1.00 66.56  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 17.097 -28.187 9.898  1.00 51.90  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 19.940 -14.975 43.452 1.00 52.46  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 43.273 -3.042  34.026 1.00 59.43  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 28.283 -29.919 24.748 1.00 71.71  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 33.885 -11.119 41.703 0.50 69.64  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 19.113 -28.320 13.827 0.50 65.15  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 32.573 -20.669 36.978 1.00 74.84  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 33.885 -14.031 41.703 0.50 43.56  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 12.613 -18.286 20.006 1.00 65.71  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 32.040 -23.902 34.980 1.00 74.78  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 21.298 -5.759  34.783 1.00 54.08  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 45.196 -12.369 15.967 1.00 77.32  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 16.804 -6.911  34.997 1.00 77.32  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 39.505 -5.529  11.545 1.00 73.20  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 16.708 -30.179 12.458 1.00 60.41  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   G 6 .   ? 12.173 -24.354 0.047  1.00 53.00  ? 201 HOH   D O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 17.751 -36.288 6.065  1.00 42.06  ? 202 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 14.928 -25.857 -1.772 1.00 47.04  ? 203 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 22.638 -34.089 8.846  1.00 35.03  ? 204 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 11.539 -23.605 3.070  1.00 57.65  ? 205 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 20.878 -38.405 4.018  1.00 51.66  ? 206 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 20.803 -39.508 -2.109 1.00 59.14  ? 207 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 10.692 -24.744 5.510  1.00 59.44  ? 208 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 20.184 -35.354 10.128 1.00 42.15  ? 209 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.648 -36.543 9.994  1.00 53.42  ? 210 HOH   D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP A 5   ? 0.8318 1.0278 0.7098 0.0306  -0.1300 -0.0222 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8260 1.0171 0.6866 0.0146  -0.1212 -0.0249 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8032 1.0238 0.6878 0.0036  -0.1168 -0.0417 6   ASP A C   
4    O O   . ASP A 5   ? 0.7946 1.0399 0.7080 0.0076  -0.1206 -0.0512 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8491 1.0120 0.7000 0.0060  -0.1043 -0.0183 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0457 1.1906 0.8633 -0.0044 -0.0994 -0.0139 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0468 1.2047 0.8633 -0.0155 -0.0961 -0.0234 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1557 1.2729 0.9483 -0.0024 -0.0976 -0.0021 6   ASP A OD2 
9    N N   . SER A 6   ? 0.6978 0.9154 0.5705 -0.0109 -0.1079 -0.0463 7   SER A N   
10   C CA  . SER A 6   ? 0.6503 0.8893 0.5415 -0.0229 -0.1015 -0.0619 7   SER A CA  
11   C C   . SER A 6   ? 0.5952 0.8208 0.4978 -0.0330 -0.0829 -0.0647 7   SER A C   
12   O O   . SER A 6   ? 0.5804 0.8116 0.4875 -0.0448 -0.0747 -0.0749 7   SER A O   
13   C CB  . SER A 6   ? 0.7273 0.9739 0.5975 -0.0310 -0.1062 -0.0669 7   SER A CB  
14   O OG  . SER A 6   ? 0.8885 1.1102 0.7299 -0.0375 -0.0988 -0.0593 7   SER A OG  
15   N N   . CYS A 7   ? 0.4891 0.6968 0.3963 -0.0275 -0.0772 -0.0561 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4494 0.6435 0.3659 -0.0346 -0.0623 -0.0577 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4413 0.6495 0.3834 -0.0405 -0.0562 -0.0698 8   CYS A C   
18   O O   . CYS A 7   ? 0.4349 0.6630 0.3929 -0.0372 -0.0624 -0.0757 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4665 0.6409 0.3822 -0.0269 -0.0594 -0.0465 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5523 0.7010 0.4358 -0.0253 -0.0595 -0.0332 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3340 0.5310 0.2799 -0.0489 -0.0441 -0.0739 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2918 0.4912 0.2567 -0.0544 -0.0362 -0.0824 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3154 0.4952 0.2834 -0.0497 -0.0303 -0.0742 9   ILE A C   
24   O O   . ILE A 8   ? 0.3053 0.4703 0.2611 -0.0457 -0.0301 -0.0650 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3259 0.5247 0.2916 -0.0663 -0.0280 -0.0935 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3245 0.5040 0.2773 -0.0686 -0.0215 -0.0903 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3165 0.5378 0.2813 -0.0718 -0.0339 -0.1035 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3889 0.5635 0.3433 -0.0784 -0.0128 -0.1013 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2450 0.4234 0.2275 -0.0515 -0.0248 -0.0780 10  GLN A N   
30   N N   B GLN A 9   ? 0.2565 0.4370 0.2396 -0.0510 -0.0257 -0.0780 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2417 0.4017 0.2255 -0.0477 -0.0197 -0.0707 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2486 0.4123 0.2344 -0.0470 -0.0209 -0.0713 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2821 0.4285 0.2695 -0.0550 -0.0100 -0.0758 10  GLN A C   
34   C C   B GLN A 9   ? 0.2994 0.4489 0.2883 -0.0545 -0.0109 -0.0760 10  GLN A C   
35   O O   A GLN A 9   ? 0.2782 0.4320 0.2731 -0.0624 -0.0065 -0.0852 10  GLN A O   
36   O O   B GLN A 9   ? 0.2963 0.4525 0.2924 -0.0622 -0.0070 -0.0856 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2577 0.4257 0.2521 -0.0403 -0.0236 -0.0680 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2568 0.4314 0.2549 -0.0405 -0.0248 -0.0704 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2814 0.4319 0.2785 -0.0385 -0.0170 -0.0631 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3129 0.4706 0.3092 -0.0339 -0.0225 -0.0609 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5568 0.7100 0.5594 -0.0291 -0.0210 -0.0576 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4689 0.6272 0.4788 -0.0356 -0.0167 -0.0650 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4802 0.6461 0.4841 -0.0217 -0.0299 -0.0559 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3396 0.5172 0.3639 -0.0371 -0.0177 -0.0735 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.4926 0.6318 0.4971 -0.0287 -0.0149 -0.0546 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.4338 0.5718 0.4392 -0.0361 -0.0103 -0.0601 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2548 0.3807 0.2360 -0.0530 -0.0059 -0.0699 11  PHE A N   
48   N N   B PHE A 10  ? 0.2661 0.3951 0.2486 -0.0522 -0.0070 -0.0696 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2543 0.3628 0.2357 -0.0577 0.0015  -0.0729 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2704 0.3813 0.2522 -0.0566 0.0005  -0.0720 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2889 0.3902 0.2742 -0.0555 0.0038  -0.0691 11  PHE A C   
52   C C   B PHE A 10  ? 0.3013 0.4052 0.2876 -0.0548 0.0031  -0.0688 11  PHE A C   
53   O O   A PHE A 10  ? 0.2714 0.3639 0.2535 -0.0492 0.0025  -0.0611 11  PHE A O   
54   O O   B PHE A 10  ? 0.2924 0.3900 0.2764 -0.0482 0.0012  -0.0608 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2734 0.3657 0.2469 -0.0560 0.0032  -0.0706 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2971 0.3930 0.2706 -0.0543 0.0016  -0.0686 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2919 0.3652 0.2636 -0.0594 0.0088  -0.0744 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3278 0.4287 0.2980 -0.0586 0.0021  -0.0751 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3387 0.4109 0.3106 -0.0669 0.0127  -0.0835 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3708 0.4878 0.3372 -0.0592 -0.0025 -0.0758 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3196 0.3740 0.2874 -0.0549 0.0097  -0.0690 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3733 0.4612 0.3425 -0.0619 0.0069  -0.0810 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3654 0.4147 0.3322 -0.0694 0.0177  -0.0861 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3844 0.5059 0.3463 -0.0644 -0.0011 -0.0828 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3606 0.3939 0.3232 -0.0567 0.0132  -0.0715 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.4173 0.5100 0.3843 -0.0662 0.0083  -0.0885 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3464 0.3756 0.3077 -0.0637 0.0173  -0.0795 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3853 0.4956 0.3489 -0.0681 0.0049  -0.0897 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2526 0.3584 0.2447 -0.0620 0.0082  -0.0759 12  THR A N   
70   C CA  . THR A 11  ? 0.2562 0.3578 0.2528 -0.0626 0.0124  -0.0752 12  THR A CA  
71   C C   . THR A 11  ? 0.2981 0.3747 0.2845 -0.0593 0.0149  -0.0672 12  THR A C   
72   O O   . THR A 11  ? 0.2960 0.3723 0.2844 -0.0545 0.0143  -0.0622 12  THR A O   
73   C CB  . THR A 11  ? 0.3500 0.4549 0.3519 -0.0739 0.0200  -0.0858 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3312 0.4634 0.3445 -0.0764 0.0163  -0.0943 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.4056 0.5085 0.4124 -0.0765 0.0260  -0.0870 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2797 0.3363 0.2557 -0.0614 0.0172  -0.0668 13  ARG A N   
77   C CA  . ARG A 12  ? 0.3036 0.3368 0.2692 -0.0581 0.0181  -0.0604 13  ARG A CA  
78   C C   . ARG A 12  ? 0.3195 0.3514 0.2833 -0.0492 0.0123  -0.0535 13  ARG A C   
79   O O   . ARG A 12  ? 0.3064 0.3215 0.2628 -0.0461 0.0118  -0.0492 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3797 0.3893 0.3338 -0.0627 0.0218  -0.0632 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.5346 0.5363 0.4850 -0.0739 0.0301  -0.0697 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.8092 0.8012 0.7543 -0.0773 0.0352  -0.0673 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.9796 0.9434 0.9078 -0.0732 0.0338  -0.0600 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.1212 1.0758 1.0426 -0.0734 0.0359  -0.0558 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.9935 0.9227 0.8980 -0.0694 0.0331  -0.0495 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8810 0.8525 0.8128 -0.0770 0.0403  -0.0585 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2592 0.3078 0.2281 -0.0459 0.0081  -0.0528 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2639 0.3105 0.2300 -0.0402 0.0047  -0.0480 14  HIS A CA  
89   C C   . HIS A 13  ? 0.2844 0.3236 0.2487 -0.0359 0.0043  -0.0415 14  HIS A C   
90   O O   . HIS A 13  ? 0.2890 0.3176 0.2494 -0.0332 0.0035  -0.0397 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2609 0.3239 0.2284 -0.0392 0.0015  -0.0479 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.2904 0.3503 0.2537 -0.0358 0.0003  -0.0442 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.3013 0.3564 0.2639 -0.0365 0.0014  -0.0482 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2967 0.3576 0.2568 -0.0326 -0.0012 -0.0381 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2990 0.3548 0.2593 -0.0347 0.0013  -0.0454 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2931 0.3507 0.2502 -0.0329 0.0001  -0.0389 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2562 0.3023 0.2243 -0.0348 0.0046  -0.0391 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2641 0.3029 0.2304 -0.0311 0.0050  -0.0337 15  ALA A CA  
99   C C   . ALA A 14  ? 0.3012 0.3223 0.2609 -0.0329 0.0077  -0.0334 15  ALA A C   
100  O O   . ALA A 14  ? 0.2708 0.2833 0.2261 -0.0301 0.0066  -0.0300 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2767 0.3256 0.2500 -0.0290 0.0052  -0.0329 15  ALA A CB  
102  N N   A SER A 15  ? 0.2925 0.3072 0.2498 -0.0383 0.0113  -0.0373 16  SER A N   
103  N N   B SER A 15  ? 0.2857 0.3004 0.2430 -0.0383 0.0113  -0.0374 16  SER A N   
104  N N   C SER A 15  ? 0.2815 0.2961 0.2387 -0.0383 0.0113  -0.0373 16  SER A N   
105  C CA  A SER A 15  ? 0.3056 0.2994 0.2514 -0.0407 0.0136  -0.0366 16  SER A CA  
106  C CA  B SER A 15  ? 0.2979 0.2915 0.2436 -0.0408 0.0136  -0.0366 16  SER A CA  
107  C CA  C SER A 15  ? 0.2915 0.2850 0.2371 -0.0406 0.0136  -0.0364 16  SER A CA  
108  C C   A SER A 15  ? 0.3510 0.3327 0.2899 -0.0367 0.0089  -0.0355 16  SER A C   
109  C C   B SER A 15  ? 0.3531 0.3344 0.2918 -0.0368 0.0090  -0.0355 16  SER A C   
110  C C   C SER A 15  ? 0.3509 0.3321 0.2896 -0.0368 0.0089  -0.0355 16  SER A C   
111  O O   A SER A 15  ? 0.3149 0.2837 0.2459 -0.0340 0.0067  -0.0324 16  SER A O   
112  O O   B SER A 15  ? 0.3314 0.2992 0.2618 -0.0342 0.0068  -0.0325 16  SER A O   
113  O O   C SER A 15  ? 0.3308 0.2982 0.2610 -0.0342 0.0068  -0.0325 16  SER A O   
114  C CB  A SER A 15  ? 0.3570 0.3447 0.2992 -0.0490 0.0196  -0.0415 16  SER A CB  
115  C CB  B SER A 15  ? 0.3437 0.3310 0.2857 -0.0490 0.0197  -0.0415 16  SER A CB  
116  C CB  C SER A 15  ? 0.3295 0.3163 0.2712 -0.0489 0.0198  -0.0411 16  SER A CB  
117  O OG  A SER A 15  ? 0.4226 0.3856 0.3486 -0.0521 0.0222  -0.0398 16  SER A OG  
118  O OG  B SER A 15  ? 0.3751 0.3767 0.3266 -0.0527 0.0242  -0.0447 16  SER A OG  
119  O OG  C SER A 15  ? 0.3409 0.3297 0.2839 -0.0520 0.0200  -0.0458 16  SER A OG  
120  N N   . ASP A 16  ? 0.3172 0.3048 0.2603 -0.0361 0.0070  -0.0390 17  ASP A N   
121  C CA  . ASP A 16  ? 0.3370 0.3169 0.2779 -0.0314 0.0025  -0.0404 17  ASP A CA  
122  C C   . ASP A 16  ? 0.3317 0.3192 0.2772 -0.0261 -0.0011 -0.0381 17  ASP A C   
123  O O   . ASP A 16  ? 0.3338 0.3127 0.2766 -0.0215 -0.0052 -0.0384 17  ASP A O   
124  C CB  . ASP A 16  ? 0.3586 0.3463 0.3050 -0.0329 0.0030  -0.0463 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.5021 0.4785 0.4427 -0.0388 0.0069  -0.0501 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.4759 0.4354 0.4061 -0.0420 0.0096  -0.0480 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.5289 0.5124 0.4739 -0.0414 0.0082  -0.0558 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2740 0.2770 0.2259 -0.0267 0.0002  -0.0364 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2672 0.2751 0.2215 -0.0240 -0.0012 -0.0345 18  VAL A CA  
130  C C   . VAL A 17  ? 0.3098 0.3066 0.2587 -0.0224 -0.0021 -0.0312 18  VAL A C   
131  O O   . VAL A 17  ? 0.2892 0.2835 0.2381 -0.0196 -0.0052 -0.0326 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2905 0.3108 0.2475 -0.0252 0.0007  -0.0319 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2915 0.3115 0.2476 -0.0241 0.0012  -0.0292 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2745 0.3057 0.2339 -0.0271 0.0007  -0.0355 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2731 0.2642 0.2177 -0.0247 0.0009  -0.0283 19  LEU A N   
136  C CA  . LEU A 18  ? 0.2911 0.2715 0.2288 -0.0244 0.0011  -0.0257 19  LEU A CA  
137  C C   . LEU A 18  ? 0.3165 0.2808 0.2441 -0.0227 -0.0032 -0.0266 19  LEU A C   
138  O O   . LEU A 18  ? 0.3090 0.2686 0.2328 -0.0202 -0.0068 -0.0260 19  LEU A O   
139  C CB  . LEU A 18  ? 0.2967 0.2756 0.2330 -0.0280 0.0065  -0.0241 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3429 0.3136 0.2733 -0.0285 0.0084  -0.0220 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.3456 0.3237 0.2817 -0.0257 0.0079  -0.0203 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.4104 0.3800 0.3405 -0.0327 0.0148  -0.0227 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.3197 0.2753 0.2425 -0.0237 -0.0035 -0.0283 20  LEU A N   
144  C CA  . LEU A 19  ? 0.3342 0.2705 0.2448 -0.0205 -0.0088 -0.0285 20  LEU A CA  
145  C C   . LEU A 19  ? 0.3491 0.2921 0.2672 -0.0129 -0.0164 -0.0315 20  LEU A C   
146  O O   . LEU A 19  ? 0.3423 0.2757 0.2530 -0.0084 -0.0228 -0.0310 20  LEU A O   
147  C CB  . LEU A 19  ? 0.3639 0.2896 0.2693 -0.0229 -0.0068 -0.0306 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4843 0.3838 0.3732 -0.0190 -0.0123 -0.0299 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.5272 0.4046 0.3949 -0.0227 -0.0111 -0.0250 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.5500 0.4394 0.4354 -0.0221 -0.0091 -0.0329 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.3095 0.2707 0.2425 -0.0120 -0.0157 -0.0356 21  ASN A N   
152  C CA  . ASN A 20  ? 0.3009 0.2725 0.2443 -0.0064 -0.0209 -0.0410 21  ASN A CA  
153  C C   . ASN A 20  ? 0.3258 0.3052 0.2722 -0.0065 -0.0218 -0.0406 21  ASN A C   
154  O O   . ASN A 20  ? 0.3188 0.3006 0.2690 -0.0015 -0.0282 -0.0449 21  ASN A O   
155  C CB  . ASN A 20  ? 0.3382 0.3257 0.2940 -0.0077 -0.0179 -0.0463 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.4355 0.4146 0.3903 -0.0052 -0.0196 -0.0501 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.3995 0.3606 0.3459 0.0000  -0.0250 -0.0499 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3592 0.3490 0.3205 -0.0090 -0.0150 -0.0536 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2867 0.2707 0.2324 -0.0119 -0.0156 -0.0364 22  LEU A N   
160  C CA  . LEU A 21  ? 0.2901 0.2781 0.2366 -0.0133 -0.0148 -0.0359 22  LEU A CA  
161  C C   . LEU A 21  ? 0.3327 0.3068 0.2682 -0.0109 -0.0201 -0.0346 22  LEU A C   
162  O O   . LEU A 21  ? 0.3217 0.3001 0.2597 -0.0091 -0.0242 -0.0381 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2902 0.2806 0.2358 -0.0182 -0.0075 -0.0311 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.3287 0.3313 0.2813 -0.0204 -0.0034 -0.0315 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.3408 0.3423 0.2906 -0.0225 0.0016  -0.0258 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.3275 0.3404 0.2871 -0.0216 -0.0028 -0.0369 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.3109 0.2680 0.2327 -0.0117 -0.0198 -0.0302 23  ASN A N   
168  C CA  . ASN A 22  ? 0.3372 0.2772 0.2431 -0.0103 -0.0248 -0.0282 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3841 0.3197 0.2885 -0.0018 -0.0363 -0.0320 23  ASN A C   
170  O O   . ASN A 22  ? 0.3909 0.3218 0.2881 0.0013  -0.0433 -0.0328 23  ASN A O   
171  C CB  . ASN A 22  ? 0.3532 0.2744 0.2428 -0.0149 -0.0202 -0.0235 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4512 0.3544 0.3210 -0.0162 -0.0227 -0.0209 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.4249 0.3333 0.2954 -0.0162 -0.0244 -0.0219 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4753 0.3559 0.3254 -0.0185 -0.0222 -0.0179 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.3495 0.2876 0.2615 0.0027  -0.0389 -0.0352 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3692 0.3051 0.2838 0.0129  -0.0503 -0.0403 24  ARG A CA  
177  C C   . ARG A 23  ? 0.3973 0.3564 0.3297 0.0156  -0.0543 -0.0480 24  ARG A C   
178  O O   . ARG A 23  ? 0.4001 0.3584 0.3317 0.0232  -0.0651 -0.0517 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3512 0.2879 0.2738 0.0159  -0.0497 -0.0438 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.4030 0.3133 0.3063 0.0138  -0.0474 -0.0380 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.4645 0.3772 0.3765 0.0143  -0.0442 -0.0421 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.5527 0.4374 0.4449 0.0119  -0.0422 -0.0378 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.7404 0.6229 0.6346 0.0074  -0.0356 -0.0398 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.5685 0.4756 0.4823 0.0050  -0.0310 -0.0452 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.6508 0.5057 0.5253 0.0040  -0.0331 -0.0367 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.3447 0.3239 0.2920 0.0090  -0.0454 -0.0507 25  LEU A N   
187  C CA  . LEU A 24  ? 0.3318 0.3321 0.2947 0.0085  -0.0463 -0.0587 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3825 0.3784 0.3364 0.0068  -0.0493 -0.0571 25  LEU A C   
189  O O   . LEU A 24  ? 0.3851 0.3915 0.3465 0.0110  -0.0572 -0.0647 25  LEU A O   
190  C CB  . LEU A 24  ? 0.3149 0.3302 0.2882 -0.0001 -0.0349 -0.0599 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.3602 0.3840 0.3434 -0.0001 -0.0312 -0.0636 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.3589 0.3950 0.3474 -0.0091 -0.0206 -0.0641 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.3768 0.4120 0.3750 0.0078  -0.0387 -0.0750 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.3363 0.3182 0.2750 0.0008  -0.0431 -0.0485 26  ARG A N   
195  C CA  . ARG A 25  ? 0.3474 0.3234 0.2755 -0.0017 -0.0448 -0.0472 26  ARG A CA  
196  C C   . ARG A 25  ? 0.4171 0.3812 0.3328 0.0065  -0.0587 -0.0482 26  ARG A C   
197  O O   . ARG A 25  ? 0.4209 0.3926 0.3382 0.0080  -0.0654 -0.0536 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3698 0.3314 0.2839 -0.0087 -0.0356 -0.0389 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.4245 0.3810 0.3284 -0.0124 -0.0359 -0.0391 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.4655 0.4105 0.3590 -0.0192 -0.0259 -0.0331 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.4498 0.3769 0.3281 -0.0192 -0.0252 -0.0276 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.6060 0.5157 0.4647 -0.0231 -0.0233 -0.0246 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.5468 0.4545 0.3981 -0.0262 -0.0237 -0.0264 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4948 0.3884 0.3401 -0.0252 -0.0205 -0.0205 26  ARG A NH2 
205  N N   A SER A 26  ? 0.4055 0.3500 0.3073 0.0114  -0.0631 -0.0431 27  SER A N   
206  N N   B SER A 26  ? 0.4038 0.3484 0.3058 0.0115  -0.0631 -0.0432 27  SER A N   
207  N N   C SER A 26  ? 0.4039 0.3483 0.3056 0.0115  -0.0631 -0.0431 27  SER A N   
208  C CA  A SER A 26  ? 0.4338 0.3601 0.3180 0.0202  -0.0768 -0.0420 27  SER A CA  
209  C CA  B SER A 26  ? 0.4325 0.3585 0.3170 0.0205  -0.0768 -0.0419 27  SER A CA  
210  C CA  C SER A 26  ? 0.4319 0.3582 0.3162 0.0202  -0.0769 -0.0420 27  SER A CA  
211  C C   A SER A 26  ? 0.4949 0.4381 0.3954 0.0313  -0.0905 -0.0520 27  SER A C   
212  C C   B SER A 26  ? 0.4930 0.4361 0.3936 0.0312  -0.0903 -0.0519 27  SER A C   
213  C C   C SER A 26  ? 0.4932 0.4364 0.3937 0.0313  -0.0905 -0.0520 27  SER A C   
214  O O   A SER A 26  ? 0.5125 0.4494 0.4021 0.0378  -0.1033 -0.0533 27  SER A O   
215  O O   B SER A 26  ? 0.5098 0.4464 0.3991 0.0375  -0.1029 -0.0531 27  SER A O   
216  O O   C SER A 26  ? 0.5099 0.4469 0.3996 0.0378  -0.1032 -0.0533 27  SER A O   
217  C CB  A SER A 26  ? 0.4885 0.3886 0.3551 0.0223  -0.0769 -0.0351 27  SER A CB  
218  C CB  B SER A 26  ? 0.4883 0.3917 0.3597 0.0236  -0.0771 -0.0363 27  SER A CB  
219  C CB  C SER A 26  ? 0.4866 0.3872 0.3539 0.0226  -0.0770 -0.0353 27  SER A CB  
220  O OG  A SER A 26  ? 0.5526 0.4596 0.4345 0.0288  -0.0789 -0.0394 27  SER A OG  
221  O OG  B SER A 26  ? 0.5872 0.4716 0.4398 0.0141  -0.0667 -0.0283 27  SER A OG  
222  O OG  C SER A 26  ? 0.5920 0.4691 0.4371 0.0312  -0.0905 -0.0327 27  SER A OG  
223  N N   . ARG A 27  ? 0.4330 0.3986 0.3596 0.0333  -0.0879 -0.0599 28  ARG A N   
224  C CA  . ARG A 27  ? 0.4409 0.4279 0.3889 0.0432  -0.0989 -0.0723 28  ARG A CA  
225  C C   . ARG A 27  ? 0.4592 0.4760 0.4277 0.0365  -0.0948 -0.0823 28  ARG A C   
226  O O   . ARG A 27  ? 0.4590 0.4993 0.4498 0.0423  -0.1016 -0.0953 28  ARG A O   
227  C CB  . ARG A 27  ? 0.4616 0.4540 0.4249 0.0488  -0.0980 -0.0768 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.5473 0.5078 0.4891 0.0547  -0.1016 -0.0678 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.5956 0.5604 0.5511 0.0568  -0.0968 -0.0718 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.7587 0.7450 0.7394 0.0678  -0.1055 -0.0856 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.9330 0.9388 0.9364 0.0666  -0.0988 -0.0947 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.8040 0.8311 0.8319 0.0765  -0.1063 -0.1091 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.7351 0.7406 0.7371 0.0554  -0.0844 -0.0904 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.3855 0.4006 0.3467 0.0242  -0.0833 -0.0772 29  ASP A N   
235  C CA  . ASP A 28  ? 0.3856 0.4221 0.3608 0.0151  -0.0765 -0.0849 29  ASP A CA  
236  C C   . ASP A 28  ? 0.4246 0.4853 0.4251 0.0112  -0.0681 -0.0945 29  ASP A C   
237  O O   . ASP A 28  ? 0.4344 0.5184 0.4529 0.0080  -0.0677 -0.1069 29  ASP A O   
238  C CB  . ASP A 28  ? 0.4250 0.4709 0.4013 0.0192  -0.0890 -0.0931 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.5495 0.6095 0.5321 0.0071  -0.0804 -0.0989 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.5418 0.5914 0.5154 -0.0033 -0.0666 -0.0913 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.6159 0.6974 0.6131 0.0082  -0.0874 -0.1119 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.3501 0.4052 0.3509 0.0105  -0.0611 -0.0896 30  ILE A N   
243  C CA  . ILE A 29  ? 0.3332 0.4082 0.3538 0.0063  -0.0529 -0.0982 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3715 0.4462 0.3882 -0.0072 -0.0375 -0.0936 30  ILE A C   
245  O O   . ILE A 29  ? 0.3425 0.3997 0.3438 -0.0100 -0.0321 -0.0815 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3701 0.4412 0.3943 0.0134  -0.0550 -0.0978 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3907 0.4620 0.4208 0.0285  -0.0712 -0.1043 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.3518 0.4413 0.3923 0.0063  -0.0438 -0.1056 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.4615 0.5187 0.4879 0.0365  -0.0740 -0.1011 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.3403 0.4342 0.3710 -0.0154 -0.0303 -0.1040 31  LEU A N   
251  C CA  . LEU A 30  ? 0.3429 0.4349 0.3686 -0.0283 -0.0156 -0.1008 31  LEU A CA  
252  C C   . LEU A 30  ? 0.3695 0.4430 0.3773 -0.0328 -0.0119 -0.0900 31  LEU A C   
253  O O   . LEU A 30  ? 0.3468 0.4119 0.3463 -0.0405 -0.0011 -0.0840 31  LEU A O   
254  C CB  . LEU A 30  ? 0.3523 0.4413 0.3757 -0.0310 -0.0078 -0.0964 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.4337 0.5438 0.4757 -0.0321 -0.0055 -0.1101 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.4425 0.5482 0.4778 -0.0379 0.0041  -0.1055 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.5057 0.6357 0.5620 -0.0410 0.0003  -0.1245 31  LEU A CD2 
258  N N   . THR A 31  ? 0.3296 0.3969 0.3312 -0.0280 -0.0207 -0.0887 32  THR A N   
259  C CA  . THR A 31  ? 0.3304 0.3830 0.3174 -0.0331 -0.0164 -0.0818 32  THR A CA  
260  C C   . THR A 31  ? 0.4045 0.4681 0.3989 -0.0441 -0.0077 -0.0908 32  THR A C   
261  O O   . THR A 31  ? 0.3943 0.4787 0.4049 -0.0455 -0.0102 -0.1042 32  THR A O   
262  C CB  . THR A 31  ? 0.4010 0.4447 0.3779 -0.0266 -0.0276 -0.0797 32  THR A CB  
263  O OG1 . THR A 31  ? 0.4170 0.4785 0.4065 -0.0224 -0.0379 -0.0919 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3747 0.4018 0.3395 -0.0183 -0.0334 -0.0698 32  THR A CG2 
265  N N   . ASP A 32  ? 0.3686 0.4185 0.3522 -0.0520 0.0032  -0.0845 33  ASP A N   
266  C CA  . ASP A 32  ? 0.3740 0.4283 0.3606 -0.0640 0.0141  -0.0917 33  ASP A CA  
267  C C   . ASP A 32  ? 0.3976 0.4383 0.3731 -0.0697 0.0190  -0.0894 33  ASP A C   
268  O O   . ASP A 32  ? 0.4016 0.4393 0.3754 -0.0806 0.0299  -0.0935 33  ASP A O   
269  C CB  . ASP A 32  ? 0.3977 0.4467 0.3810 -0.0697 0.0252  -0.0875 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.5192 0.5474 0.4875 -0.0654 0.0275  -0.0721 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.4564 0.4742 0.4178 -0.0591 0.0224  -0.0651 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.6499 0.6728 0.6130 -0.0686 0.0344  -0.0680 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.3325 0.3630 0.2988 -0.0634 0.0119  -0.0834 34  VAL A N   
274  C CA  . VAL A 33  ? 0.3356 0.3538 0.2916 -0.0688 0.0165  -0.0828 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3785 0.3945 0.3276 -0.0628 0.0055  -0.0822 34  VAL A C   
276  O O   . VAL A 33  ? 0.3692 0.3831 0.3154 -0.0536 -0.0034 -0.0768 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3843 0.3802 0.3282 -0.0707 0.0275  -0.0715 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.3701 0.3554 0.3068 -0.0613 0.0231  -0.0603 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3986 0.3821 0.3345 -0.0787 0.0358  -0.0738 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3356 0.3496 0.2796 -0.0688 0.0068  -0.0878 35  VAL A N   
281  N N   B VAL A 34  ? 0.3338 0.3479 0.2778 -0.0687 0.0065  -0.0878 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3401 0.3479 0.2720 -0.0655 -0.0018 -0.0870 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.3360 0.3435 0.2678 -0.0649 -0.0023 -0.0865 35  VAL A CA  
284  C C   A VAL A 34  ? 0.3912 0.3784 0.3097 -0.0708 0.0092  -0.0811 35  VAL A C   
285  C C   B VAL A 34  ? 0.3940 0.3819 0.3121 -0.0708 0.0083  -0.0818 35  VAL A C   
286  O O   A VAL A 34  ? 0.3906 0.3744 0.3109 -0.0793 0.0202  -0.0847 35  VAL A O   
287  O O   B VAL A 34  ? 0.3970 0.3828 0.3170 -0.0797 0.0184  -0.0866 35  VAL A O   
288  C CB  A VAL A 34  ? 0.3969 0.4220 0.3343 -0.0682 -0.0106 -0.1006 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.3889 0.4138 0.3254 -0.0639 -0.0150 -0.0983 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.4087 0.4240 0.3283 -0.0657 -0.0195 -0.0991 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.3895 0.4252 0.3329 -0.0755 -0.0086 -0.1109 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.3894 0.4374 0.3441 -0.0617 -0.0215 -0.1084 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.4000 0.4132 0.3179 -0.0581 -0.0260 -0.0940 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.3504 0.3232 0.2556 -0.0661 0.0071  -0.0729 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3684 0.3235 0.2622 -0.0701 0.0169  -0.0691 36  ILE A CA  
296  C C   . ILE A 35  ? 0.4367 0.3891 0.3171 -0.0730 0.0110  -0.0741 36  ILE A C   
297  O O   . ILE A 35  ? 0.4279 0.3791 0.2986 -0.0677 0.0001  -0.0718 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3988 0.3417 0.2884 -0.0645 0.0205  -0.0585 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3856 0.3328 0.2870 -0.0604 0.0234  -0.0534 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.4180 0.3456 0.2995 -0.0683 0.0311  -0.0572 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3844 0.3307 0.2925 -0.0655 0.0330  -0.0552 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.4007 0.3500 0.2783 -0.0818 0.0183  -0.0809 37  VAL A N   
303  C CA  . VAL A 36  ? 0.4127 0.3599 0.2762 -0.0863 0.0136  -0.0871 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4785 0.4058 0.3274 -0.0893 0.0233  -0.0829 37  VAL A C   
305  O O   . VAL A 36  ? 0.4635 0.3819 0.3168 -0.0929 0.0366  -0.0825 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4700 0.4295 0.3400 -0.0955 0.0149  -0.1002 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4873 0.4453 0.3411 -0.1002 0.0087  -0.1071 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4659 0.4485 0.3536 -0.0930 0.0062  -0.1067 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.4538 0.3728 0.2843 -0.0877 0.0167  -0.0802 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4713 0.3727 0.2868 -0.0916 0.0261  -0.0778 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5708 0.4680 0.3648 -0.0975 0.0197  -0.0838 38  VAL A C   
312  O O   . VAL A 37  ? 0.5360 0.4295 0.3136 -0.0939 0.0077  -0.0805 38  VAL A O   
313  C CB  . VAL A 37  ? 0.5210 0.4139 0.3326 -0.0855 0.0266  -0.0681 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.5310 0.4094 0.3338 -0.0905 0.0398  -0.0679 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4989 0.4002 0.3312 -0.0783 0.0276  -0.0625 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5749 0.4727 0.3682 -0.1064 0.0264  -0.0930 39  SER A N   
317  N N   B SER A 38  ? 0.5651 0.4610 0.3576 -0.1066 0.0278  -0.0925 39  SER A N   
318  C CA  A SER A 38  ? 0.6027 0.4992 0.3765 -0.1134 0.0204  -0.1009 39  SER A CA  
319  C CA  B SER A 38  ? 0.5902 0.4837 0.3631 -0.1143 0.0234  -0.1005 39  SER A CA  
320  C C   A SER A 38  ? 0.6150 0.5282 0.3893 -0.1083 0.0006  -0.1041 39  SER A C   
321  C C   B SER A 38  ? 0.6197 0.5240 0.3842 -0.1091 0.0027  -0.1016 39  SER A C   
322  O O   A SER A 38  ? 0.5876 0.5190 0.3834 -0.1070 -0.0019 -0.1093 39  SER A O   
323  O O   B SER A 38  ? 0.6307 0.5241 0.3708 -0.1073 -0.0064 -0.0976 39  SER A O   
324  C CB  A SER A 38  ? 0.6936 0.5706 0.4404 -0.1168 0.0234  -0.0974 39  SER A CB  
325  C CB  B SER A 38  ? 0.6663 0.5402 0.4175 -0.1201 0.0327  -0.0994 39  SER A CB  
326  O OG  A SER A 38  ? 0.8814 0.7469 0.6325 -0.1203 0.0414  -0.0963 39  SER A OG  
327  O OG  B SER A 38  ? 0.7800 0.6476 0.5411 -0.1258 0.0505  -0.1036 39  SER A OG  
328  N N   A ARG A 39  ? 0.5747 0.4810 0.3253 -0.1048 -0.0132 -0.1012 40  ARG A N   
329  N N   B ARG A 39  ? 0.5341 0.4592 0.3199 -0.1060 -0.0041 -0.1067 40  ARG A N   
330  C CA  A ARG A 39  ? 0.5716 0.4918 0.3205 -0.0974 -0.0344 -0.1042 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.5301 0.4732 0.3196 -0.0994 -0.0235 -0.1110 40  ARG A CA  
332  C C   A ARG A 39  ? 0.5955 0.5202 0.3559 -0.0844 -0.0437 -0.0960 40  ARG A C   
333  C C   B ARG A 39  ? 0.5640 0.5058 0.3543 -0.0863 -0.0347 -0.1009 40  ARG A C   
334  O O   A ARG A 39  ? 0.5883 0.5262 0.3525 -0.0760 -0.0613 -0.0990 40  ARG A O   
335  O O   B ARG A 39  ? 0.5621 0.5224 0.3663 -0.0790 -0.0478 -0.1049 40  ARG A O   
336  C CB  A ARG A 39  ? 0.5893 0.4959 0.3029 -0.0988 -0.0464 -0.1043 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.5532 0.4977 0.3216 -0.1032 -0.0357 -0.1189 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.6697 0.5806 0.3740 -0.1105 -0.0441 -0.1164 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.6935 0.6473 0.4680 -0.1162 -0.0270 -0.1326 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.6695 0.5694 0.3379 -0.1102 -0.0603 -0.1167 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.7751 0.7400 0.5359 -0.1187 -0.0429 -0.1433 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.7039 0.6048 0.3593 -0.1232 -0.0560 -0.1281 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.8598 0.8327 0.6257 -0.1328 -0.0330 -0.1575 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.9053 0.8287 0.5692 -0.1257 -0.0664 -0.1415 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 1.0204 0.9768 0.7661 -0.1437 -0.0226 -0.1604 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7525 0.6748 0.4027 -0.1387 -0.0610 -0.1520 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.8498 0.7817 0.5690 -0.1427 -0.0200 -0.1503 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.7592 0.7080 0.4470 -0.1158 -0.0815 -0.1459 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.8410 0.8050 0.5928 -0.1568 -0.0135 -0.1743 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.5344 0.4489 0.3009 -0.0824 -0.0324 -0.0866 41  GLU A N   
351  N N   B GLU A 40  ? 0.5152 0.4368 0.2933 -0.0838 -0.0285 -0.0893 41  GLU A N   
352  C CA  A GLU A 40  ? 0.5179 0.4346 0.2939 -0.0713 -0.0393 -0.0790 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.5079 0.4254 0.2862 -0.0729 -0.0365 -0.0797 41  GLU A CA  
354  C C   A GLU A 40  ? 0.5271 0.4621 0.3353 -0.0694 -0.0329 -0.0810 41  GLU A C   
355  C C   B GLU A 40  ? 0.5243 0.4574 0.3331 -0.0691 -0.0310 -0.0793 41  GLU A C   
356  O O   A GLU A 40  ? 0.4971 0.4341 0.3167 -0.0765 -0.0185 -0.0837 41  GLU A O   
357  O O   B GLU A 40  ? 0.4927 0.4249 0.3128 -0.0744 -0.0158 -0.0789 41  GLU A O   
358  C CB  A GLU A 40  ? 0.5473 0.4408 0.3061 -0.0704 -0.0330 -0.0676 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.5401 0.4327 0.2974 -0.0744 -0.0288 -0.0697 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.7739 0.6452 0.4961 -0.0732 -0.0389 -0.0646 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.7335 0.6068 0.4550 -0.0769 -0.0366 -0.0681 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.2439 1.1035 0.9485 -0.0632 -0.0552 -0.0576 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.1812 1.0426 0.8857 -0.0670 -0.0520 -0.0603 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.2580 1.1071 0.9625 -0.0598 -0.0513 -0.0495 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.1963 1.0607 0.8901 -0.0610 -0.0702 -0.0631 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.2533 1.1135 0.9438 -0.0585 -0.0724 -0.0606 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.1960 1.0450 0.8981 -0.0649 -0.0463 -0.0520 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4762 0.4224 0.2969 -0.0595 -0.0435 -0.0796 42  GLN A N   
369  C CA  . GLN A 41  ? 0.4525 0.4151 0.3006 -0.0571 -0.0390 -0.0812 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4773 0.4327 0.3268 -0.0488 -0.0403 -0.0714 42  GLN A C   
371  O O   . GLN A 41  ? 0.4894 0.4360 0.3253 -0.0413 -0.0522 -0.0673 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4722 0.4603 0.3378 -0.0541 -0.0506 -0.0929 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.6625 0.6622 0.5319 -0.0644 -0.0474 -0.1051 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.9002 0.9298 0.7926 -0.0637 -0.0555 -0.1193 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.7926 0.8363 0.7006 -0.0547 -0.0640 -0.1210 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.9315 0.9722 0.8277 -0.0739 -0.0523 -0.1313 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.3955 0.3531 0.2597 -0.0502 -0.0284 -0.0678 43  PHE A N   
378  C CA  . PHE A 42  ? 0.3982 0.3512 0.2656 -0.0436 -0.0285 -0.0596 43  PHE A CA  
379  C C   . PHE A 42  ? 0.4332 0.4035 0.3240 -0.0423 -0.0253 -0.0627 43  PHE A C   
380  O O   . PHE A 42  ? 0.4294 0.4028 0.3287 -0.0487 -0.0139 -0.0641 43  PHE A O   
381  C CB  . PHE A 42  ? 0.4185 0.3546 0.2768 -0.0470 -0.0164 -0.0515 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.4541 0.3720 0.2881 -0.0509 -0.0159 -0.0494 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4892 0.4034 0.3166 -0.0589 -0.0089 -0.0538 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.5039 0.4064 0.3196 -0.0476 -0.0217 -0.0435 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.5303 0.4276 0.3337 -0.0637 -0.0076 -0.0528 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.5611 0.4446 0.3507 -0.0530 -0.0201 -0.0419 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.5377 0.4197 0.3215 -0.0610 -0.0131 -0.0468 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3864 0.3660 0.2860 -0.0343 -0.0349 -0.0639 44  ARG A N   
389  C CA  . ARG A 43  ? 0.3514 0.3477 0.2721 -0.0339 -0.0313 -0.0676 44  ARG A CA  
390  C C   . ARG A 43  ? 0.3881 0.3754 0.3084 -0.0324 -0.0241 -0.0583 44  ARG A C   
391  O O   . ARG A 43  ? 0.3836 0.3569 0.2917 -0.0283 -0.0270 -0.0512 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3672 0.3802 0.3004 -0.0259 -0.0445 -0.0756 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.4320 0.4597 0.3698 -0.0267 -0.0533 -0.0874 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.5443 0.5983 0.5060 -0.0219 -0.0606 -0.0997 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.6776 0.7416 0.6554 -0.0280 -0.0476 -0.1018 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.8370 0.9153 0.8273 -0.0387 -0.0375 -0.1107 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.7350 0.8235 0.7281 -0.0446 -0.0391 -0.1207 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.6129 0.6950 0.6119 -0.0444 -0.0256 -0.1106 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.3393 0.3334 0.2708 -0.0365 -0.0145 -0.0585 45  ALA A N   
400  C CA  . ALA A 44  ? 0.3455 0.3334 0.2772 -0.0350 -0.0085 -0.0504 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3563 0.3551 0.3003 -0.0379 -0.0023 -0.0527 45  ALA A C   
402  O O   . ALA A 44  ? 0.3303 0.3411 0.2831 -0.0422 -0.0011 -0.0610 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3694 0.3422 0.2906 -0.0380 -0.0003 -0.0435 45  ALA A CB  
404  N N   . HIS A 45  ? 0.3160 0.3110 0.2598 -0.0361 0.0015  -0.0460 46  HIS A N   
405  C CA  . HIS A 45  ? 0.3043 0.3055 0.2543 -0.0394 0.0079  -0.0464 46  HIS A CA  
406  C C   . HIS A 45  ? 0.3495 0.3382 0.2919 -0.0430 0.0168  -0.0402 46  HIS A C   
407  O O   . HIS A 45  ? 0.3328 0.3118 0.2695 -0.0396 0.0175  -0.0335 46  HIS A O   
408  C CB  . HIS A 45  ? 0.2976 0.3021 0.2505 -0.0346 0.0053  -0.0432 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.3370 0.3500 0.2966 -0.0294 -0.0037 -0.0489 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.3626 0.3669 0.3157 -0.0236 -0.0107 -0.0457 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.3418 0.3700 0.3136 -0.0291 -0.0064 -0.0582 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.3584 0.3706 0.3187 -0.0185 -0.0186 -0.0520 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.3470 0.3757 0.3208 -0.0211 -0.0165 -0.0605 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.3332 0.3213 0.2755 -0.0498 0.0240  -0.0431 47  LYS A N   
415  C CA  . LYS A 46  ? 0.3307 0.3031 0.2639 -0.0522 0.0322  -0.0371 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3472 0.3140 0.2769 -0.0463 0.0319  -0.0280 47  LYS A C   
417  O O   . LYS A 46  ? 0.3283 0.2839 0.2534 -0.0429 0.0339  -0.0226 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3561 0.3262 0.2869 -0.0613 0.0406  -0.0412 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.3613 0.3351 0.2950 -0.0686 0.0429  -0.0507 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.3391 0.3110 0.2704 -0.0798 0.0529  -0.0561 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.4296 0.4096 0.3667 -0.0880 0.0550  -0.0680 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.4334 0.4148 0.3701 -0.1009 0.0657  -0.0757 47  LYS A NZ  
423  N N   . THR A 47  ? 0.3066 0.2825 0.2396 -0.0448 0.0292  -0.0277 48  THR A N   
424  C CA  . THR A 47  ? 0.3111 0.2837 0.2406 -0.0398 0.0282  -0.0202 48  THR A CA  
425  C C   . THR A 47  ? 0.3296 0.3021 0.2618 -0.0333 0.0239  -0.0170 48  THR A C   
426  O O   . THR A 47  ? 0.3397 0.3069 0.2698 -0.0290 0.0244  -0.0116 48  THR A O   
427  C CB  . THR A 47  ? 0.4008 0.3833 0.3320 -0.0410 0.0269  -0.0217 48  THR A CB  
428  O OG1 . THR A 47  ? 0.4171 0.4124 0.3582 -0.0398 0.0217  -0.0282 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.4271 0.4062 0.3516 -0.0490 0.0340  -0.0239 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2904 0.2683 0.2269 -0.0325 0.0195  -0.0208 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2930 0.2687 0.2295 -0.0288 0.0171  -0.0187 49  VAL A CA  
432  C C   . VAL A 48  ? 0.3221 0.2877 0.2549 -0.0290 0.0215  -0.0172 49  VAL A C   
433  O O   . VAL A 48  ? 0.3021 0.2659 0.2364 -0.0259 0.0230  -0.0146 49  VAL A O   
434  C CB  . VAL A 48  ? 0.3129 0.2914 0.2497 -0.0281 0.0113  -0.0223 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.3277 0.2995 0.2602 -0.0270 0.0111  -0.0203 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.3042 0.2921 0.2462 -0.0267 0.0075  -0.0243 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.3038 0.2644 0.2334 -0.0329 0.0239  -0.0203 50  LEU A N   
438  C CA  . LEU A 49  ? 0.3056 0.2558 0.2315 -0.0339 0.0292  -0.0201 50  LEU A CA  
439  C C   . LEU A 49  ? 0.3371 0.2807 0.2637 -0.0302 0.0337  -0.0155 50  LEU A C   
440  O O   . LEU A 49  ? 0.3325 0.2720 0.2609 -0.0268 0.0361  -0.0146 50  LEU A O   
441  C CB  . LEU A 49  ? 0.3044 0.2509 0.2265 -0.0399 0.0315  -0.0253 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.3466 0.2994 0.2673 -0.0422 0.0252  -0.0307 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.3471 0.2992 0.2660 -0.0485 0.0275  -0.0372 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3688 0.3164 0.2831 -0.0405 0.0227  -0.0296 50  LEU A CD2 
445  N N   . MET A 50  ? 0.3129 0.2550 0.2373 -0.0306 0.0345  -0.0130 51  MET A N   
446  C CA  . MET A 50  ? 0.3369 0.2696 0.2581 -0.0258 0.0368  -0.0074 51  MET A CA  
447  C C   . MET A 50  ? 0.3854 0.3259 0.3129 -0.0180 0.0321  -0.0042 51  MET A C   
448  O O   . MET A 50  ? 0.3867 0.3219 0.3163 -0.0116 0.0328  -0.0019 51  MET A O   
449  C CB  . MET A 50  ? 0.3585 0.2861 0.2716 -0.0293 0.0385  -0.0051 51  MET A CB  
450  C CG  . MET A 50  ? 0.3918 0.3116 0.2994 -0.0383 0.0448  -0.0096 51  MET A CG  
451  S SD  . MET A 50  ? 0.4550 0.3745 0.3544 -0.0451 0.0474  -0.0094 51  MET A SD  
452  C CE  . MET A 50  ? 0.4243 0.3186 0.3074 -0.0408 0.0509  0.0002  51  MET A CE  
453  N N   . ALA A 51  ? 0.3384 0.2924 0.2702 -0.0185 0.0273  -0.0053 52  ALA A N   
454  C CA  . ALA A 51  ? 0.3249 0.2888 0.2634 -0.0130 0.0232  -0.0040 52  ALA A CA  
455  C C   . ALA A 51  ? 0.3521 0.3186 0.2982 -0.0110 0.0249  -0.0071 52  ALA A C   
456  O O   . ALA A 51  ? 0.3635 0.3382 0.3175 -0.0060 0.0230  -0.0074 52  ALA A O   
457  C CB  . ALA A 51  ? 0.3280 0.3034 0.2683 -0.0156 0.0190  -0.0056 52  ALA A CB  
458  N N   . CYS A 52  ? 0.3123 0.2728 0.2559 -0.0157 0.0288  -0.0105 53  CYS A N   
459  C CA  . CYS A 52  ? 0.3115 0.2727 0.2588 -0.0166 0.0322  -0.0144 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3582 0.3104 0.3064 -0.0154 0.0383  -0.0163 53  CYS A C   
461  O O   . CYS A 52  ? 0.3449 0.2997 0.2984 -0.0158 0.0424  -0.0207 53  CYS A O   
462  C CB  . CYS A 52  ? 0.3150 0.2742 0.2551 -0.0232 0.0316  -0.0171 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.3541 0.3216 0.2941 -0.0240 0.0252  -0.0164 53  CYS A SG  
464  N N   . SER A 53  ? 0.3203 0.2614 0.2625 -0.0158 0.0403  -0.0145 54  SER A N   
465  C CA  . SER A 53  ? 0.3078 0.2375 0.2487 -0.0163 0.0470  -0.0174 54  SER A CA  
466  C C   . SER A 53  ? 0.3717 0.2896 0.3107 -0.0108 0.0484  -0.0136 54  SER A C   
467  O O   . SER A 53  ? 0.3529 0.2648 0.2837 -0.0132 0.0472  -0.0100 54  SER A O   
468  C CB  . SER A 53  ? 0.3354 0.2593 0.2665 -0.0252 0.0491  -0.0206 54  SER A CB  
469  O OG  . SER A 53  ? 0.3800 0.2910 0.3066 -0.0277 0.0554  -0.0232 54  SER A OG  
470  N N   . GLY A 54  ? 0.3510 0.2640 0.2967 -0.0039 0.0517  -0.0151 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3552 0.2515 0.2968 0.0027  0.0530  -0.0112 55  GLY A CA  
472  C C   . GLY A 54  ? 0.4006 0.2793 0.3298 -0.0055 0.0596  -0.0121 55  GLY A C   
473  O O   . GLY A 54  ? 0.4103 0.2733 0.3290 -0.0050 0.0604  -0.0073 55  GLY A O   
474  N N   . LEU A 55  ? 0.3766 0.2573 0.3049 -0.0142 0.0644  -0.0188 56  LEU A N   
475  C CA  . LEU A 55  ? 0.3955 0.2631 0.3134 -0.0234 0.0703  -0.0218 56  LEU A CA  
476  C C   . LEU A 55  ? 0.4162 0.2868 0.3266 -0.0303 0.0671  -0.0195 56  LEU A C   
477  O O   . LEU A 55  ? 0.4102 0.2664 0.3119 -0.0341 0.0714  -0.0184 56  LEU A O   
478  C CB  . LEU A 55  ? 0.3918 0.2624 0.3092 -0.0310 0.0747  -0.0298 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4536 0.3123 0.3613 -0.0407 0.0808  -0.0349 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4798 0.3176 0.3859 -0.0377 0.0894  -0.0361 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.4260 0.2917 0.3299 -0.0490 0.0813  -0.0419 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3518 0.2400 0.2656 -0.0321 0.0604  -0.0194 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3432 0.2371 0.2532 -0.0379 0.0576  -0.0192 57  PHE A CA  
484  C C   . PHE A 56  ? 0.4018 0.2896 0.3076 -0.0345 0.0569  -0.0127 57  PHE A C   
485  O O   . PHE A 56  ? 0.3993 0.2826 0.2983 -0.0414 0.0598  -0.0135 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3439 0.2556 0.2584 -0.0393 0.0504  -0.0214 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3583 0.2721 0.2705 -0.0447 0.0504  -0.0277 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.3958 0.3063 0.3036 -0.0526 0.0535  -0.0336 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3766 0.2952 0.2893 -0.0429 0.0473  -0.0283 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.4062 0.3187 0.3100 -0.0573 0.0521  -0.0396 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.4143 0.3320 0.3202 -0.0481 0.0464  -0.0333 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3942 0.3092 0.2956 -0.0546 0.0481  -0.0388 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3685 0.2556 0.2775 -0.0244 0.0536  -0.0071 58  TYR A N   
494  C CA  . TYR A 57  ? 0.3911 0.2692 0.2921 -0.0201 0.0518  0.0001  58  TYR A CA  
495  C C   . TYR A 57  ? 0.4610 0.3134 0.3482 -0.0232 0.0594  0.0019  58  TYR A C   
496  O O   . TYR A 57  ? 0.4489 0.2923 0.3237 -0.0291 0.0618  0.0044  58  TYR A O   
497  C CB  . TYR A 57  ? 0.4111 0.2936 0.3190 -0.0074 0.0458  0.0044  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4663 0.3367 0.3631 -0.0011 0.0423  0.0125  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.4924 0.3679 0.3814 -0.0049 0.0390  0.0157  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.5225 0.3747 0.4149 0.0090  0.0421  0.0167  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.5394 0.4013 0.4136 0.0001  0.0357  0.0236  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5712 0.4088 0.4493 0.0159  0.0374  0.0252  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6626 0.5050 0.5303 0.0109  0.0341  0.0290  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.7359 0.5619 0.5856 0.0170  0.0292  0.0377  58  TYR A OH  
505  N N   A SER A 58  ? 0.4323 0.2716 0.3205 -0.0204 0.0643  -0.0002 59  SER A N   
506  N N   B SER A 58  ? 0.4309 0.2704 0.3193 -0.0204 0.0642  -0.0002 59  SER A N   
507  C CA  A SER A 58  ? 0.4606 0.2720 0.3353 -0.0233 0.0725  0.0007  59  SER A CA  
508  C CA  B SER A 58  ? 0.4586 0.2704 0.3336 -0.0233 0.0725  0.0006  59  SER A CA  
509  C C   A SER A 58  ? 0.5240 0.3335 0.3918 -0.0393 0.0798  -0.0055 59  SER A C   
510  C C   B SER A 58  ? 0.5211 0.3311 0.3890 -0.0392 0.0796  -0.0054 59  SER A C   
511  O O   A SER A 58  ? 0.5567 0.3468 0.4093 -0.0455 0.0858  -0.0033 59  SER A O   
512  O O   B SER A 58  ? 0.5501 0.3415 0.4028 -0.0453 0.0851  -0.0030 59  SER A O   
513  C CB  A SER A 58  ? 0.4960 0.2973 0.3767 -0.0168 0.0763  -0.0024 59  SER A CB  
514  C CB  B SER A 58  ? 0.4930 0.2956 0.3743 -0.0178 0.0766  -0.0032 59  SER A CB  
515  O OG  A SER A 58  ? 0.5446 0.3471 0.4325 -0.0014 0.0698  0.0023  59  SER A OG  
516  O OG  B SER A 58  ? 0.5788 0.3518 0.4464 -0.0203 0.0850  -0.0026 59  SER A OG  
517  N N   . ILE A 59  ? 0.4615 0.2908 0.3394 -0.0460 0.0791  -0.0136 60  ILE A N   
518  C CA  . ILE A 59  ? 0.4496 0.2835 0.3252 -0.0602 0.0840  -0.0218 60  ILE A CA  
519  C C   . ILE A 59  ? 0.4898 0.3303 0.3614 -0.0665 0.0834  -0.0211 60  ILE A C   
520  O O   . ILE A 59  ? 0.5120 0.3402 0.3737 -0.0770 0.0917  -0.0241 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4571 0.3121 0.3436 -0.0635 0.0801  -0.0301 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4677 0.3137 0.3549 -0.0615 0.0839  -0.0332 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.4294 0.2954 0.3167 -0.0764 0.0818  -0.0395 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4999 0.3641 0.3936 -0.0627 0.0784  -0.0387 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.4153 0.2741 0.2941 -0.0610 0.0749  -0.0181 61  PHE A N   
526  C CA  . PHE A 60  ? 0.4249 0.2929 0.3018 -0.0680 0.0751  -0.0199 61  PHE A CA  
527  C C   . PHE A 60  ? 0.4908 0.3404 0.3516 -0.0673 0.0780  -0.0115 61  PHE A C   
528  O O   . PHE A 60  ? 0.5046 0.3595 0.3614 -0.0754 0.0806  -0.0138 61  PHE A O   
529  C CB  . PHE A 60  ? 0.4106 0.3057 0.3014 -0.0650 0.0659  -0.0227 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.4077 0.3173 0.3092 -0.0666 0.0624  -0.0308 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.4446 0.3593 0.3482 -0.0770 0.0664  -0.0409 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.4096 0.3271 0.3175 -0.0584 0.0551  -0.0288 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.4437 0.3711 0.3547 -0.0776 0.0613  -0.0480 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.4364 0.3636 0.3492 -0.0601 0.0513  -0.0352 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.4121 0.3438 0.3258 -0.0689 0.0535  -0.0444 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4642 0.2917 0.3150 -0.0582 0.0780  -0.0026 62  THR A N   
537  C CA  . THR A 61  ? 0.4953 0.2988 0.3250 -0.0575 0.0805  0.0062  62  THR A CA  
538  C C   . THR A 61  ? 0.5955 0.3690 0.4081 -0.0670 0.0926  0.0050  62  THR A C   
539  O O   . THR A 61  ? 0.6112 0.3580 0.4007 -0.0698 0.0974  0.0116  62  THR A O   
540  C CB  . THR A 61  ? 0.5796 0.3756 0.4063 -0.0410 0.0716  0.0166  62  THR A CB  
541  O OG1 . THR A 61  ? 0.5404 0.3300 0.3753 -0.0321 0.0710  0.0163  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.5260 0.3494 0.3654 -0.0347 0.0612  0.0176  62  THR A CG2 
543  N N   . ASP A 62  ? 0.5510 0.3270 0.3725 -0.0730 0.0981  -0.0038 63  ASP A N   
544  C CA  . ASP A 62  ? 0.5825 0.3314 0.3890 -0.0843 0.1109  -0.0072 63  ASP A CA  
545  C C   . ASP A 62  ? 0.6426 0.3976 0.4436 -0.1024 0.1192  -0.0149 63  ASP A C   
546  O O   . ASP A 62  ? 0.5879 0.3745 0.4068 -0.1081 0.1164  -0.0245 63  ASP A O   
547  C CB  . ASP A 62  ? 0.6018 0.3530 0.4194 -0.0860 0.1142  -0.0155 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.7601 0.4855 0.5633 -0.1000 0.1283  -0.0211 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.8389 0.5297 0.6260 -0.0954 0.1334  -0.0146 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.7595 0.4989 0.5673 -0.1157 0.1344  -0.0326 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.6830 0.4066 0.4590 -0.1115 0.1296  -0.0112 64  GLN A N   
552  C CA  . GLN A 63  ? 0.7055 0.4313 0.4733 -0.1306 0.1402  -0.0190 64  GLN A CA  
553  C C   . GLN A 63  ? 0.7362 0.4856 0.5220 -0.1457 0.1469  -0.0366 64  GLN A C   
554  O O   . GLN A 63  ? 0.7512 0.5213 0.5438 -0.1581 0.1509  -0.0464 64  GLN A O   
555  C CB  . GLN A 63  ? 0.7774 0.4578 0.5101 -0.1387 0.1520  -0.0115 64  GLN A CB  
556  C CG  . GLN A 63  ? 1.0074 0.6702 0.7198 -0.1270 0.1445  0.0041  64  GLN A CG  
557  N N   . LEU A 64  ? 0.6458 0.3935 0.4398 -0.1450 0.1481  -0.0419 65  LEU A N   
558  C CA  . LEU A 64  ? 0.6203 0.3929 0.4319 -0.1579 0.1519  -0.0590 65  LEU A CA  
559  C C   . LEU A 64  ? 0.6447 0.4562 0.4827 -0.1480 0.1374  -0.0635 65  LEU A C   
560  O O   . LEU A 64  ? 0.6517 0.4938 0.5062 -0.1554 0.1353  -0.0760 65  LEU A O   
561  C CB  . LEU A 64  ? 0.6396 0.3902 0.4444 -0.1644 0.1613  -0.0640 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.7419 0.4588 0.5236 -0.1819 0.1791  -0.0670 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.7654 0.4613 0.5423 -0.1865 0.1873  -0.0722 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.7970 0.5356 0.5851 -0.2025 0.1879  -0.0823 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.5653 0.3744 0.4067 -0.1316 0.1278  -0.0545 66  LYS A N   
566  C CA  . LYS A 65  ? 0.5216 0.3610 0.3831 -0.1231 0.1153  -0.0581 66  LYS A CA  
567  C C   . LYS A 65  ? 0.5712 0.4360 0.4437 -0.1173 0.1053  -0.0564 66  LYS A C   
568  O O   . LYS A 65  ? 0.5369 0.4284 0.4252 -0.1153 0.0967  -0.0633 66  LYS A O   
569  C CB  . LYS A 65  ? 0.5294 0.3588 0.3909 -0.1097 0.1102  -0.0507 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.5293 0.3374 0.3835 -0.1148 0.1194  -0.0548 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.4848 0.2881 0.3424 -0.1017 0.1145  -0.0497 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.5819 0.3593 0.4310 -0.1047 0.1246  -0.0526 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.6014 0.3440 0.4344 -0.1011 0.1318  -0.0438 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.5672 0.4221 0.4295 -0.1151 0.1064  -0.0478 67  CYS A N   
575  C CA  . CYS A 66  ? 0.5643 0.4411 0.4355 -0.1105 0.0985  -0.0467 67  CYS A CA  
576  C C   . CYS A 66  ? 0.6094 0.5155 0.4968 -0.1203 0.0984  -0.0615 67  CYS A C   
577  O O   . CYS A 66  ? 0.5987 0.5280 0.4994 -0.1144 0.0893  -0.0633 67  CYS A O   
578  C CB  . CYS A 66  ? 0.6040 0.4629 0.4578 -0.1099 0.1018  -0.0367 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.6993 0.5399 0.5345 -0.1301 0.1187  -0.0424 67  CYS A SG  
580  N N   . ASN A 67  ? 0.5599 0.4651 0.4469 -0.1353 0.1087  -0.0731 68  ASN A N   
581  C CA  . ASN A 67  ? 0.5527 0.4869 0.4568 -0.1459 0.1099  -0.0900 68  ASN A CA  
582  C C   . ASN A 67  ? 0.5705 0.5266 0.4917 -0.1445 0.1020  -0.1008 68  ASN A C   
583  O O   . ASN A 67  ? 0.5470 0.5305 0.4852 -0.1514 0.1007  -0.1162 68  ASN A O   
584  C CB  . ASN A 67  ? 0.5840 0.5065 0.4776 -0.1653 0.1270  -0.0982 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.7908 0.6959 0.6666 -0.1683 0.1339  -0.0895 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.7980 0.6712 0.6501 -0.1777 0.1465  -0.0846 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.6344 0.5568 0.5184 -0.1599 0.1255  -0.0866 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.5257 0.4707 0.4424 -0.1358 0.0966  -0.0939 69  LEU A N   
589  C CA  . LEU A 68  ? 0.5017 0.4641 0.4297 -0.1347 0.0886  -0.1032 69  LEU A CA  
590  C C   . LEU A 68  ? 0.5175 0.5033 0.4588 -0.1220 0.0726  -0.1026 69  LEU A C   
591  O O   . LEU A 68  ? 0.4974 0.4775 0.4353 -0.1111 0.0675  -0.0909 69  LEU A O   
592  C CB  . LEU A 68  ? 0.5118 0.4523 0.4280 -0.1317 0.0904  -0.0970 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.5869 0.5005 0.4890 -0.1434 0.1059  -0.0983 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.5965 0.4896 0.4892 -0.1374 0.1066  -0.0920 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.6015 0.5283 0.5102 -0.1606 0.1134  -0.1161 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4700 0.4812 0.4257 -0.1231 0.0643  -0.1157 70  SER A N   
597  N N   B SER A 69  ? 0.4688 0.4799 0.4244 -0.1232 0.0644  -0.1158 70  SER A N   
598  C CA  A SER A 69  ? 0.4523 0.4826 0.4185 -0.1105 0.0481  -0.1159 70  SER A CA  
599  C CA  B SER A 69  ? 0.4508 0.4817 0.4174 -0.1109 0.0481  -0.1164 70  SER A CA  
600  C C   A SER A 69  ? 0.4681 0.4915 0.4262 -0.1032 0.0388  -0.1116 70  SER A C   
601  C C   B SER A 69  ? 0.4678 0.4917 0.4261 -0.1034 0.0388  -0.1119 70  SER A C   
602  O O   A SER A 69  ? 0.4397 0.4695 0.3993 -0.0920 0.0259  -0.1079 70  SER A O   
603  O O   B SER A 69  ? 0.4398 0.4703 0.3999 -0.0922 0.0258  -0.1085 70  SER A O   
604  C CB  A SER A 69  ? 0.4993 0.5616 0.4862 -0.1138 0.0425  -0.1329 70  SER A CB  
605  C CB  B SER A 69  ? 0.4958 0.5585 0.4829 -0.1147 0.0429  -0.1340 70  SER A CB  
606  O OG  A SER A 69  ? 0.6017 0.6739 0.5930 -0.1233 0.0438  -0.1465 70  SER A OG  
607  O OG  B SER A 69  ? 0.5820 0.6525 0.5769 -0.1214 0.0517  -0.1385 70  SER A OG  
608  N N   . VAL A 70  ? 0.4366 0.4451 0.3842 -0.1105 0.0464  -0.1124 71  VAL A N   
609  C CA  . VAL A 70  ? 0.4380 0.4377 0.3752 -0.1064 0.0406  -0.1094 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4673 0.4386 0.3902 -0.1084 0.0525  -0.1002 71  VAL A C   
611  O O   . VAL A 70  ? 0.4655 0.4256 0.3853 -0.1182 0.0653  -0.1032 71  VAL A O   
612  C CB  . VAL A 70  ? 0.4982 0.5130 0.4389 -0.1137 0.0360  -0.1243 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.5079 0.5109 0.4336 -0.1110 0.0313  -0.1212 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.4933 0.5385 0.4508 -0.1097 0.0225  -0.1351 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3876 0.3471 0.3018 -0.0993 0.0487  -0.0901 72  ILE A N   
616  C CA  . ILE A 71  ? 0.3880 0.3238 0.2916 -0.0987 0.0581  -0.0828 72  ILE A CA  
617  C C   . ILE A 71  ? 0.4340 0.3662 0.3286 -0.0984 0.0543  -0.0849 72  ILE A C   
618  O O   . ILE A 71  ? 0.4345 0.3731 0.3265 -0.0918 0.0439  -0.0819 72  ILE A O   
619  C CB  . ILE A 71  ? 0.4247 0.3507 0.3278 -0.0891 0.0591  -0.0699 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.4383 0.3657 0.3463 -0.0904 0.0630  -0.0676 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.4518 0.3568 0.3473 -0.0863 0.0670  -0.0641 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.5032 0.4148 0.4055 -0.1001 0.0762  -0.0701 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.4169 0.3367 0.3047 -0.1062 0.0637  -0.0900 73  ASN A N   
624  C CA  . ASN A 72  ? 0.4282 0.3428 0.3052 -0.1078 0.0623  -0.0930 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4709 0.3664 0.3423 -0.1030 0.0703  -0.0854 73  ASN A C   
626  O O   . ASN A 72  ? 0.4536 0.3340 0.3259 -0.1045 0.0817  -0.0845 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4740 0.3887 0.3476 -0.1202 0.0678  -0.1057 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.7060 0.6431 0.5882 -0.1258 0.0603  -0.1162 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.5735 0.5275 0.4572 -0.1211 0.0461  -0.1180 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.6891 0.6264 0.5771 -0.1362 0.0700  -0.1241 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.4067 0.3020 0.2721 -0.0974 0.0649  -0.0809 74  LEU A N   
632  C CA  . LEU A 73  ? 0.4078 0.2889 0.2706 -0.0935 0.0730  -0.0764 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4589 0.3288 0.3119 -0.1014 0.0816  -0.0843 74  LEU A C   
634  O O   . LEU A 73  ? 0.4759 0.3501 0.3205 -0.1095 0.0785  -0.0923 74  LEU A O   
635  C CB  . LEU A 73  ? 0.4042 0.2884 0.2642 -0.0866 0.0666  -0.0697 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.4360 0.3307 0.3050 -0.0787 0.0584  -0.0621 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.4469 0.3404 0.3130 -0.0733 0.0562  -0.0564 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.4392 0.3325 0.3201 -0.0752 0.0633  -0.0584 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.4226 0.2795 0.2772 -0.0985 0.0917  -0.0830 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4558 0.3006 0.3027 -0.1051 0.1021  -0.0910 75  ASP A CA  
641  C C   . ASP A 74  ? 0.5247 0.3741 0.3553 -0.1115 0.0966  -0.0953 75  ASP A C   
642  O O   . ASP A 74  ? 0.5159 0.3708 0.3422 -0.1074 0.0890  -0.0897 75  ASP A O   
643  C CB  . ASP A 74  ? 0.4800 0.3148 0.3349 -0.0977 0.1115  -0.0885 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.6220 0.4433 0.4726 -0.1032 0.1243  -0.0978 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.6321 0.4541 0.4702 -0.1106 0.1256  -0.1038 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.6572 0.4655 0.5156 -0.0998 0.1331  -0.0990 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.5424 0.3879 0.3615 -0.1219 0.0999  -0.1052 76  PRO A N   
648  C CA  . PRO A 75  ? 0.5498 0.3975 0.3488 -0.1280 0.0931  -0.1087 76  PRO A CA  
649  C C   . PRO A 75  ? 0.5942 0.4337 0.3827 -0.1276 0.0979  -0.1066 76  PRO A C   
650  O O   . PRO A 75  ? 0.6174 0.4564 0.3861 -0.1314 0.0906  -0.1065 76  PRO A O   
651  C CB  . PRO A 75  ? 0.5918 0.4360 0.3819 -0.1398 0.0981  -0.1208 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.6640 0.4979 0.4679 -0.1401 0.1122  -0.1238 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5799 0.4174 0.4012 -0.1294 0.1096  -0.1137 76  PRO A CD  
654  N N   . GLU A 76  ? 0.5467 0.3796 0.3476 -0.1232 0.1099  -0.1056 77  GLU A N   
655  C CA  . GLU A 76  ? 0.5733 0.4013 0.3683 -0.1238 0.1166  -0.1059 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5714 0.4064 0.3670 -0.1170 0.1072  -0.0959 77  GLU A C   
657  O O   . GLU A 76  ? 0.5640 0.3953 0.3498 -0.1198 0.1107  -0.0958 77  GLU A O   
658  C CB  . GLU A 76  ? 0.6036 0.4262 0.4170 -0.1193 0.1313  -0.1096 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.8765 0.6934 0.6833 -0.1250 0.1435  -0.1171 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.2669 1.0734 1.0596 -0.1367 0.1533  -0.1289 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.2694 1.0698 1.0735 -0.1355 0.1614  -0.1347 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.2277 1.0304 0.9959 -0.1473 0.1530  -0.1325 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.5018 0.3462 0.3086 -0.1093 0.0965  -0.0885 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4922 0.3429 0.3009 -0.1027 0.0879  -0.0798 78  ILE A CA  
665  C C   . ILE A 77  ? 0.5537 0.4015 0.3385 -0.1068 0.0771  -0.0779 78  ILE A C   
666  O O   . ILE A 77  ? 0.5409 0.3910 0.3160 -0.1094 0.0679  -0.0800 78  ILE A O   
667  C CB  . ILE A 77  ? 0.5043 0.3653 0.3324 -0.0933 0.0813  -0.0733 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.5111 0.3701 0.3585 -0.0881 0.0913  -0.0737 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4584 0.3256 0.2879 -0.0871 0.0726  -0.0652 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.5819 0.4388 0.4379 -0.0846 0.1012  -0.0750 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.5494 0.3918 0.3244 -0.1074 0.0782  -0.0743 79  ASN A N   
672  C CA  . ASN A 78  ? 0.5677 0.4010 0.3156 -0.1108 0.0690  -0.0709 79  ASN A CA  
673  C C   . ASN A 78  ? 0.5573 0.3976 0.3099 -0.1016 0.0538  -0.0629 79  ASN A C   
674  O O   . ASN A 78  ? 0.5308 0.3777 0.3007 -0.0953 0.0551  -0.0582 79  ASN A O   
675  C CB  . ASN A 78  ? 0.6116 0.4336 0.3469 -0.1170 0.0798  -0.0714 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.7986 0.6051 0.5013 -0.1212 0.0717  -0.0666 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.6886 0.4926 0.3901 -0.1175 0.0679  -0.0601 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.7188 0.5127 0.3925 -0.1289 0.0685  -0.0696 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.5273 0.3670 0.2650 -0.1004 0.0390  -0.0620 80  PRO A N   
680  C CA  . PRO A 79  ? 0.5169 0.3639 0.2608 -0.0907 0.0246  -0.0559 80  PRO A CA  
681  C C   . PRO A 79  ? 0.5630 0.3999 0.2987 -0.0880 0.0238  -0.0484 80  PRO A C   
682  O O   . PRO A 79  ? 0.5423 0.3883 0.2948 -0.0801 0.0193  -0.0441 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5700 0.4157 0.2955 -0.0905 0.0092  -0.0584 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.6307 0.4761 0.3505 -0.0996 0.0161  -0.0670 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5794 0.4135 0.2957 -0.1071 0.0341  -0.0678 80  PRO A CD  
686  N N   . GLU A 80  ? 0.5435 0.3610 0.2525 -0.0957 0.0293  -0.0475 81  GLU A N   
687  C CA  . GLU A 80  ? 0.5514 0.3570 0.2506 -0.0954 0.0307  -0.0414 81  GLU A CA  
688  C C   . GLU A 80  ? 0.5592 0.3776 0.2871 -0.0940 0.0428  -0.0419 81  GLU A C   
689  O O   . GLU A 80  ? 0.5307 0.3523 0.2674 -0.0884 0.0390  -0.0371 81  GLU A O   
690  C CB  . GLU A 80  ? 0.6081 0.3878 0.2696 -0.1064 0.0359  -0.0411 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.7449 0.5092 0.3928 -0.1068 0.0361  -0.0346 81  GLU A CG  
692  C CD  . GLU A 80  ? 1.0907 0.8272 0.7014 -0.1200 0.0455  -0.0344 81  GLU A CD  
693  O OE1 . GLU A 80  ? 1.1135 0.8290 0.7003 -0.1200 0.0401  -0.0277 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 1.0000 0.7344 0.6045 -0.1309 0.0592  -0.0413 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.5301 0.3558 0.2724 -0.0983 0.0563  -0.0482 82  GLY A N   
696  C CA  . GLY A 81  ? 0.5112 0.3505 0.2818 -0.0950 0.0661  -0.0496 82  GLY A CA  
697  C C   . GLY A 81  ? 0.5077 0.3629 0.3024 -0.0840 0.0574  -0.0453 82  GLY A C   
698  O O   . GLY A 81  ? 0.4662 0.3292 0.2753 -0.0794 0.0578  -0.0424 82  GLY A O   
699  N N   . PHE A 82  ? 0.4534 0.3138 0.2511 -0.0808 0.0495  -0.0457 83  PHE A N   
700  C CA  . PHE A 82  ? 0.4258 0.3004 0.2436 -0.0722 0.0422  -0.0427 83  PHE A CA  
701  C C   . PHE A 82  ? 0.4419 0.3163 0.2554 -0.0672 0.0314  -0.0372 83  PHE A C   
702  O O   . PHE A 82  ? 0.4270 0.3112 0.2570 -0.0616 0.0303  -0.0342 83  PHE A O   
703  C CB  . PHE A 82  ? 0.4398 0.3204 0.2612 -0.0721 0.0375  -0.0463 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.4255 0.3200 0.2672 -0.0654 0.0331  -0.0442 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.4587 0.3581 0.3179 -0.0629 0.0411  -0.0435 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.4329 0.3345 0.2754 -0.0609 0.0209  -0.0429 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.4552 0.3648 0.3288 -0.0579 0.0377  -0.0410 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.4451 0.3595 0.3055 -0.0562 0.0185  -0.0420 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.4233 0.3409 0.2975 -0.0554 0.0272  -0.0406 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.4533 0.3155 0.2435 -0.0687 0.0228  -0.0359 84  CYS A N   
711  C CA  . CYS A 83  ? 0.4908 0.3485 0.2740 -0.0632 0.0121  -0.0309 84  CYS A CA  
712  C C   . CYS A 83  ? 0.4949 0.3488 0.2813 -0.0641 0.0192  -0.0276 84  CYS A C   
713  O O   . CYS A 83  ? 0.4665 0.3276 0.2649 -0.0580 0.0145  -0.0249 84  CYS A O   
714  C CB  . CYS A 83  ? 0.5524 0.3918 0.3050 -0.0646 0.0023  -0.0297 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.6328 0.4635 0.3759 -0.0551 -0.0134 -0.0239 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4691 0.3133 0.2456 -0.0727 0.0313  -0.0294 85  ILE A N   
717  C CA  . ILE A 84  ? 0.4490 0.2918 0.2295 -0.0758 0.0398  -0.0289 85  ILE A CA  
718  C C   . ILE A 84  ? 0.4394 0.3045 0.2522 -0.0696 0.0424  -0.0297 85  ILE A C   
719  O O   . ILE A 84  ? 0.4007 0.2703 0.2214 -0.0670 0.0411  -0.0276 85  ILE A O   
720  C CB  . ILE A 84  ? 0.4943 0.3262 0.2612 -0.0875 0.0540  -0.0337 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.5245 0.3282 0.2515 -0.0949 0.0511  -0.0311 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4840 0.3246 0.2668 -0.0911 0.0658  -0.0372 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.5946 0.3874 0.3048 -0.1070 0.0638  -0.0367 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3925 0.2695 0.2216 -0.0672 0.0455  -0.0325 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3759 0.2707 0.2317 -0.0606 0.0470  -0.0323 86  LEU A CA  
726  C C   . LEU A 85  ? 0.3999 0.3030 0.2639 -0.0533 0.0364  -0.0283 86  LEU A C   
727  O O   . LEU A 85  ? 0.3672 0.2808 0.2455 -0.0491 0.0359  -0.0267 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3856 0.2855 0.2530 -0.0600 0.0540  -0.0361 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.4603 0.3575 0.3282 -0.0657 0.0666  -0.0421 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.4698 0.3689 0.3475 -0.0640 0.0726  -0.0461 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.4841 0.3926 0.3677 -0.0639 0.0710  -0.0437 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3813 0.2811 0.2368 -0.0520 0.0280  -0.0277 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3651 0.2741 0.2292 -0.0458 0.0186  -0.0260 87  LEU A CA  
734  C C   . LEU A 86  ? 0.3989 0.3044 0.2591 -0.0436 0.0142  -0.0230 87  LEU A C   
735  O O   . LEU A 86  ? 0.3711 0.2872 0.2448 -0.0394 0.0122  -0.0219 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3703 0.2784 0.2270 -0.0453 0.0103  -0.0284 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.4206 0.3417 0.2897 -0.0394 0.0016  -0.0293 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.4012 0.3354 0.2892 -0.0387 0.0073  -0.0297 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.4509 0.3740 0.3144 -0.0387 -0.0076 -0.0339 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3835 0.2720 0.2231 -0.0474 0.0136  -0.0219 88  ASP A N   
741  C CA  . ASP A 87  ? 0.3890 0.2691 0.2216 -0.0468 0.0114  -0.0194 88  ASP A CA  
742  C C   . ASP A 87  ? 0.3994 0.2902 0.2479 -0.0486 0.0199  -0.0203 88  ASP A C   
743  O O   . ASP A 87  ? 0.3947 0.2906 0.2506 -0.0453 0.0167  -0.0193 88  ASP A O   
744  C CB  . ASP A 87  ? 0.4469 0.3022 0.2503 -0.0530 0.0123  -0.0179 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.6440 0.4859 0.4279 -0.0488 -0.0004 -0.0161 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.6530 0.5069 0.4493 -0.0405 -0.0106 -0.0169 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.6713 0.4908 0.4270 -0.0541 -0.0004 -0.0145 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3765 0.2715 0.2307 -0.0534 0.0303  -0.0231 89  PHE A N   
749  C CA  . PHE A 88  ? 0.3465 0.2555 0.2187 -0.0539 0.0372  -0.0255 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3465 0.2732 0.2386 -0.0458 0.0320  -0.0239 89  PHE A C   
751  O O   . PHE A 88  ? 0.3137 0.2495 0.2155 -0.0444 0.0314  -0.0241 89  PHE A O   
752  C CB  . PHE A 88  ? 0.3484 0.2614 0.2268 -0.0579 0.0478  -0.0302 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.3379 0.2697 0.2393 -0.0552 0.0522  -0.0334 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3660 0.3019 0.2706 -0.0598 0.0564  -0.0368 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3626 0.3074 0.2815 -0.0476 0.0509  -0.0331 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.3447 0.3011 0.2718 -0.0564 0.0584  -0.0409 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3786 0.3406 0.3175 -0.0431 0.0522  -0.0357 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3507 0.3203 0.2947 -0.0472 0.0553  -0.0399 89  PHE A CZ  
759  N N   . MET A 89  ? 0.3063 0.2371 0.2032 -0.0419 0.0290  -0.0228 90  MET A N   
760  C CA  . MET A 89  ? 0.2897 0.2339 0.2012 -0.0360 0.0253  -0.0211 90  MET A CA  
761  C C   . MET A 89  ? 0.3336 0.2811 0.2458 -0.0336 0.0187  -0.0199 90  MET A C   
762  O O   . MET A 89  ? 0.3258 0.2844 0.2488 -0.0310 0.0181  -0.0195 90  MET A O   
763  C CB  . MET A 89  ? 0.3028 0.2467 0.2144 -0.0345 0.0235  -0.0209 90  MET A CB  
764  C CG  . MET A 89  ? 0.3262 0.2669 0.2392 -0.0360 0.0306  -0.0225 90  MET A CG  
765  S SD  . MET A 89  ? 0.3770 0.3168 0.2900 -0.0359 0.0292  -0.0230 90  MET A SD  
766  C CE  . MET A 89  ? 0.3807 0.3113 0.2906 -0.0391 0.0383  -0.0260 90  MET A CE  
767  N N   . TYR A 90  ? 0.3066 0.2440 0.2068 -0.0339 0.0131  -0.0198 91  TYR A N   
768  C CA  . TYR A 90  ? 0.3041 0.2430 0.2053 -0.0305 0.0063  -0.0198 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3665 0.2972 0.2611 -0.0329 0.0075  -0.0196 91  TYR A C   
770  O O   . TYR A 90  ? 0.3504 0.2811 0.2462 -0.0300 0.0027  -0.0202 91  TYR A O   
771  C CB  . TYR A 90  ? 0.3240 0.2569 0.2175 -0.0274 -0.0020 -0.0207 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.3304 0.2767 0.2354 -0.0252 -0.0041 -0.0231 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3538 0.3003 0.2579 -0.0280 -0.0008 -0.0240 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.3389 0.2969 0.2550 -0.0216 -0.0083 -0.0258 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.3425 0.2996 0.2559 -0.0279 -0.0013 -0.0271 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.3410 0.3108 0.2666 -0.0217 -0.0087 -0.0295 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.3693 0.3381 0.2931 -0.0252 -0.0049 -0.0299 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.3399 0.3190 0.2719 -0.0271 -0.0041 -0.0345 91  TYR A OH  
779  N N   . THR A 91  ? 0.3338 0.2566 0.2211 -0.0391 0.0149  -0.0201 92  THR A N   
780  C CA  . THR A 91  ? 0.3502 0.2627 0.2290 -0.0437 0.0177  -0.0210 92  THR A CA  
781  C C   . THR A 91  ? 0.3738 0.2951 0.2611 -0.0501 0.0275  -0.0247 92  THR A C   
782  O O   . THR A 91  ? 0.3748 0.2908 0.2581 -0.0549 0.0304  -0.0268 92  THR A O   
783  C CB  . THR A 91  ? 0.4087 0.2943 0.2609 -0.0479 0.0172  -0.0191 92  THR A CB  
784  O OG1 . THR A 91  ? 0.4130 0.2945 0.2585 -0.0542 0.0249  -0.0203 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.4439 0.3196 0.2857 -0.0407 0.0056  -0.0165 92  THR A CG2 
786  N N   A SER A 92  ? 0.3155 0.2492 0.2145 -0.0502 0.0325  -0.0266 93  SER A N   
787  N N   B SER A 92  ? 0.3215 0.2546 0.2199 -0.0504 0.0326  -0.0265 93  SER A N   
788  C CA  A SER A 92  ? 0.3079 0.2527 0.2180 -0.0552 0.0416  -0.0321 93  SER A CA  
789  C CA  B SER A 92  ? 0.3159 0.2605 0.2258 -0.0552 0.0416  -0.0320 93  SER A CA  
790  C C   A SER A 92  ? 0.3554 0.2838 0.2491 -0.0657 0.0508  -0.0354 93  SER A C   
791  C C   B SER A 92  ? 0.3745 0.3026 0.2679 -0.0660 0.0509  -0.0355 93  SER A C   
792  O O   A SER A 92  ? 0.3490 0.2870 0.2523 -0.0710 0.0598  -0.0419 93  SER A O   
793  O O   B SER A 92  ? 0.3693 0.3065 0.2716 -0.0722 0.0598  -0.0422 93  SER A O   
794  C CB  A SER A 92  ? 0.3030 0.2614 0.2252 -0.0559 0.0416  -0.0354 93  SER A CB  
795  C CB  B SER A 92  ? 0.3348 0.2958 0.2596 -0.0545 0.0409  -0.0351 93  SER A CB  
796  O OG  A SER A 92  ? 0.2966 0.2669 0.2290 -0.0480 0.0335  -0.0324 93  SER A OG  
797  O OG  B SER A 92  ? 0.4007 0.3507 0.3147 -0.0620 0.0439  -0.0374 93  SER A OG  
798  N N   A ARG A 93  ? 0.3442 0.2480 0.2127 -0.0685 0.0484  -0.0314 94  ARG A N   
799  N N   B ARG A 93  ? 0.3564 0.2606 0.2253 -0.0684 0.0485  -0.0314 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3653 0.2487 0.2119 -0.0796 0.0572  -0.0336 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3801 0.2623 0.2255 -0.0794 0.0567  -0.0332 94  ARG A CA  
802  C C   A ARG A 93  ? 0.4261 0.3037 0.2645 -0.0804 0.0593  -0.0333 94  ARG A C   
803  C C   B ARG A 93  ? 0.4341 0.3103 0.2710 -0.0807 0.0591  -0.0331 94  ARG A C   
804  O O   A ARG A 93  ? 0.4177 0.2915 0.2510 -0.0737 0.0503  -0.0287 94  ARG A O   
805  O O   B ARG A 93  ? 0.4266 0.2981 0.2574 -0.0742 0.0503  -0.0285 94  ARG A O   
806  C CB  A ARG A 93  ? 0.4243 0.2792 0.2428 -0.0827 0.0533  -0.0291 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.4232 0.2779 0.2417 -0.0808 0.0510  -0.0281 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4801 0.3368 0.3040 -0.0837 0.0531  -0.0304 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.5218 0.3795 0.3472 -0.0797 0.0489  -0.0287 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.5885 0.4179 0.3885 -0.0806 0.0445  -0.0245 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.6056 0.4530 0.4215 -0.0930 0.0608  -0.0339 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.7242 0.5201 0.4894 -0.0891 0.0485  -0.0220 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.6373 0.4889 0.4612 -0.0929 0.0596  -0.0357 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.8934 0.6682 0.6395 -0.1013 0.0583  -0.0241 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.8087 0.6335 0.6107 -0.0961 0.0585  -0.0333 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.7378 0.5239 0.4988 -0.1062 0.0647  -0.0297 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.6977 0.5282 0.5090 -0.0965 0.0584  -0.0364 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.7271 0.4684 0.4374 -0.1094 0.0619  -0.0211 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.6026 0.3930 0.3716 -0.0988 0.0574  -0.0279 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.3984 0.2763 0.2360 -0.0896 0.0717  -0.0397 95  LEU A N   
821  C CA  . LEU A 94  ? 0.3949 0.2677 0.2251 -0.0923 0.0763  -0.0416 95  LEU A CA  
822  C C   . LEU A 94  ? 0.4913 0.3370 0.2887 -0.1054 0.0840  -0.0426 95  LEU A C   
823  O O   . LEU A 94  ? 0.4804 0.3233 0.2746 -0.1165 0.0961  -0.0487 95  LEU A O   
824  C CB  . LEU A 94  ? 0.3837 0.2806 0.2422 -0.0913 0.0850  -0.0496 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.4290 0.3234 0.2851 -0.0925 0.0901  -0.0527 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.4092 0.3039 0.2668 -0.0821 0.0788  -0.0461 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.4458 0.3607 0.3281 -0.0926 0.1008  -0.0628 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4933 0.3188 0.2651 -0.1047 0.0773  -0.0371 96  ASN A N   
829  C CA  . ASN A 95  ? 0.5398 0.3347 0.2735 -0.1167 0.0827  -0.0365 96  ASN A CA  
830  C C   . ASN A 95  ? 0.5994 0.3973 0.3323 -0.1257 0.0959  -0.0443 96  ASN A C   
831  O O   . ASN A 95  ? 0.6119 0.4019 0.3313 -0.1252 0.0926  -0.0431 96  ASN A O   
832  C CB  . ASN A 95  ? 0.6009 0.3732 0.3065 -0.1106 0.0672  -0.0274 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.8583 0.5951 0.5190 -0.1218 0.0705  -0.0252 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.7472 0.4695 0.3922 -0.1354 0.0841  -0.0286 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.8088 0.5306 0.4467 -0.1170 0.0582  -0.0200 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.5518 0.3640 0.3025 -0.1334 0.1108  -0.0539 97  LEU A N   
837  C CA  . LEU A 96  ? 0.5654 0.3851 0.3225 -0.1414 0.1251  -0.0640 97  LEU A CA  
838  C C   . LEU A 96  ? 0.6316 0.4244 0.3527 -0.1599 0.1384  -0.0678 97  LEU A C   
839  O O   . LEU A 96  ? 0.6309 0.4144 0.3421 -0.1699 0.1460  -0.0698 97  LEU A O   
840  C CB  . LEU A 96  ? 0.5514 0.4044 0.3509 -0.1378 0.1326  -0.0736 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.6192 0.4895 0.4401 -0.1385 0.1435  -0.0846 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.6219 0.4925 0.4455 -0.1278 0.1347  -0.0798 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5970 0.4998 0.4591 -0.1327 0.1476  -0.0935 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.6177 0.3951 0.3153 -0.1654 0.1410  -0.0683 98  ARG A N   
845  C CA  . ARG A 97  ? 0.6649 0.4123 0.3212 -0.1838 0.1532  -0.0711 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6755 0.4298 0.3352 -0.1920 0.1672  -0.0823 98  ARG A C   
847  O O   . ARG A 97  ? 0.6269 0.4005 0.3110 -0.1815 0.1628  -0.0843 98  ARG A O   
848  C CB  . ARG A 97  ? 0.7132 0.4251 0.3234 -0.1827 0.1388  -0.0582 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.8052 0.5066 0.4095 -0.1737 0.1243  -0.0474 98  ARG A CG  
850  C CD  . ARG A 97  ? 1.0590 0.7275 0.6213 -0.1691 0.1076  -0.0354 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.3359 0.9649 0.8466 -0.1857 0.1161  -0.0342 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.6262 1.2254 1.1072 -0.1957 0.1218  -0.0310 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.5067 1.0673 0.9369 -0.2117 0.1301  -0.0296 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.5032 1.1092 1.0030 -0.1909 0.1200  -0.0294 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.6774 0.4147 0.3117 -0.2116 0.1852  -0.0903 99  GLU A N   
856  C CA  . GLU A 98  ? 0.6824 0.4244 0.3173 -0.2213 0.2005  -0.1026 99  GLU A CA  
857  C C   . GLU A 98  ? 0.7531 0.4871 0.3737 -0.2141 0.1890  -0.0970 99  GLU A C   
858  O O   . GLU A 98  ? 0.7352 0.4883 0.3804 -0.2105 0.1941  -0.1055 99  GLU A O   
859  C CB  . GLU A 98  ? 0.7462 0.4623 0.3430 -0.2459 0.2206  -0.1101 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.8848 0.6078 0.4843 -0.2579 0.2393  -0.1255 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.2953 0.9911 0.8536 -0.2842 0.2605  -0.1336 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.2776 0.9331 0.7821 -0.2930 0.2557  -0.1223 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.2870 1.0013 0.8662 -0.2959 0.2822  -0.1519 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.7426 0.4498 0.3262 -0.2112 0.1729  -0.0835 100 GLY A N   
865  C CA  . GLY A 99  ? 0.7504 0.4498 0.3177 -0.2053 0.1603  -0.0787 100 GLY A CA  
866  C C   . GLY A 99  ? 0.7306 0.4567 0.3357 -0.1862 0.1460  -0.0758 100 GLY A C   
867  O O   . GLY A 99  ? 0.7369 0.4637 0.3378 -0.1831 0.1402  -0.0764 100 GLY A O   
868  N N   . ASN A 100 ? 0.6463 0.3938 0.2870 -0.1743 0.1410  -0.0733 101 ASN A N   
869  C CA  . ASN A 100 ? 0.5981 0.3678 0.2708 -0.1573 0.1280  -0.0700 101 ASN A CA  
870  C C   . ASN A 100 ? 0.6197 0.4196 0.3393 -0.1504 0.1363  -0.0777 101 ASN A C   
871  O O   . ASN A 100 ? 0.5914 0.4068 0.3350 -0.1377 0.1276  -0.0754 101 ASN A O   
872  C CB  . ASN A 100 ? 0.5827 0.3486 0.2519 -0.1461 0.1092  -0.0578 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.6830 0.4563 0.3682 -0.1438 0.1108  -0.0560 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5578 0.3507 0.2719 -0.1448 0.1222  -0.0635 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.6174 0.3765 0.2860 -0.1395 0.0985  -0.0466 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5857 0.3939 0.3180 -0.1584 0.1522  -0.0871 102 ILE A N   
877  C CA  . ILE A 101 ? 0.5577 0.3957 0.3353 -0.1498 0.1576  -0.0945 102 ILE A CA  
878  C C   . ILE A 101 ? 0.5566 0.4066 0.3557 -0.1418 0.1590  -0.0996 102 ILE A C   
879  O O   . ILE A 101 ? 0.5064 0.3748 0.3366 -0.1276 0.1525  -0.0979 102 ILE A O   
880  C CB  . ILE A 101 ? 0.6041 0.4523 0.3941 -0.1601 0.1747  -0.1066 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5816 0.4630 0.4203 -0.1473 0.1752  -0.1129 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.6117 0.4492 0.3837 -0.1771 0.1933  -0.1186 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.6101 0.5063 0.4647 -0.1529 0.1834  -0.1206 102 ILE A CD1 
884  N N   . MET A 102 ? 0.5570 0.3948 0.3380 -0.1508 0.1672  -0.1056 103 MET A N   
885  C CA  . MET A 102 ? 0.5558 0.4019 0.3554 -0.1441 0.1696  -0.1111 103 MET A CA  
886  C C   . MET A 102 ? 0.5803 0.4262 0.3827 -0.1319 0.1529  -0.1007 103 MET A C   
887  O O   . MET A 102 ? 0.5353 0.3943 0.3658 -0.1202 0.1510  -0.1015 103 MET A O   
888  C CB  . MET A 102 ? 0.6236 0.4565 0.4022 -0.1580 0.1832  -0.1213 103 MET A CB  
889  C CG  . MET A 102 ? 0.7150 0.5513 0.4958 -0.1710 0.2030  -0.1349 103 MET A CG  
890  S SD  . MET A 102 ? 0.7680 0.6375 0.6031 -0.1604 0.2113  -0.1461 103 MET A SD  
891  C CE  . MET A 102 ? 0.7326 0.6094 0.5921 -0.1507 0.2161  -0.1552 103 MET A CE  
892  N N   . ALA A 103 ? 0.5651 0.3959 0.3385 -0.1341 0.1405  -0.0912 104 ALA A N   
893  C CA  . ALA A 103 ? 0.5563 0.3890 0.3324 -0.1241 0.1249  -0.0829 104 ALA A CA  
894  C C   . ALA A 103 ? 0.5484 0.3967 0.3510 -0.1111 0.1163  -0.0762 104 ALA A C   
895  O O   . ALA A 103 ? 0.5166 0.3737 0.3373 -0.1017 0.1109  -0.0741 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5921 0.4077 0.3333 -0.1285 0.1129  -0.0759 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4875 0.3381 0.2907 -0.1118 0.1160  -0.0734 105 VAL A N   
898  C CA  . VAL A 104 ? 0.4392 0.3049 0.2658 -0.1007 0.1083  -0.0679 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4499 0.3335 0.3099 -0.0923 0.1141  -0.0732 105 VAL A C   
900  O O   . VAL A 104 ? 0.4235 0.3153 0.2991 -0.0815 0.1059  -0.0681 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4845 0.3475 0.3031 -0.1049 0.1079  -0.0653 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.4472 0.3285 0.2924 -0.0945 0.1022  -0.0620 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.5030 0.3456 0.2886 -0.1087 0.0980  -0.0576 105 VAL A CG2 
904  N N   A MET A 105 ? 0.4332 0.3219 0.3031 -0.0971 0.1281  -0.0839 106 MET A N   
905  N N   B MET A 105 ? 0.4439 0.3327 0.3140 -0.0970 0.1281  -0.0839 106 MET A N   
906  C CA  A MET A 105 ? 0.4285 0.3336 0.3307 -0.0874 0.1329  -0.0901 106 MET A CA  
907  C CA  B MET A 105 ? 0.4466 0.3519 0.3492 -0.0869 0.1324  -0.0897 106 MET A CA  
908  C C   A MET A 105 ? 0.4829 0.3832 0.3900 -0.0798 0.1300  -0.0884 106 MET A C   
909  C C   B MET A 105 ? 0.4856 0.3859 0.3927 -0.0796 0.1297  -0.0882 106 MET A C   
910  O O   A MET A 105 ? 0.4625 0.3712 0.3895 -0.0673 0.1243  -0.0849 106 MET A O   
911  O O   B MET A 105 ? 0.4574 0.3656 0.3841 -0.0672 0.1241  -0.0848 106 MET A O   
912  C CB  A MET A 105 ? 0.4694 0.3813 0.3815 -0.0945 0.1492  -0.1042 106 MET A CB  
913  C CB  B MET A 105 ? 0.4848 0.3978 0.3986 -0.0934 0.1483  -0.1037 106 MET A CB  
914  C CG  A MET A 105 ? 0.5038 0.4352 0.4522 -0.0820 0.1520  -0.1114 106 MET A CG  
915  C CG  B MET A 105 ? 0.5174 0.4491 0.4672 -0.0804 0.1507  -0.1104 106 MET A CG  
916  S SD  A MET A 105 ? 0.5686 0.5115 0.5334 -0.0897 0.1717  -0.1312 106 MET A SD  
917  S SD  B MET A 105 ? 0.5750 0.5233 0.5449 -0.0873 0.1686  -0.1294 106 MET A SD  
918  C CE  A MET A 105 ? 0.5176 0.4747 0.5195 -0.0696 0.1695  -0.1360 106 MET A CE  
919  C CE  B MET A 105 ? 0.5614 0.4925 0.5155 -0.0975 0.1830  -0.1392 106 MET A CE  
920  N N   . ALA A 106 ? 0.4633 0.3489 0.3505 -0.0881 0.1340  -0.0910 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4692 0.3479 0.3580 -0.0839 0.1329  -0.0909 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4721 0.3511 0.3608 -0.0764 0.1188  -0.0798 107 ALA A C   
923  O O   . ALA A 106 ? 0.4442 0.3240 0.3469 -0.0675 0.1171  -0.0780 107 ALA A O   
924  C CB  . ALA A 106 ? 0.4994 0.3634 0.3634 -0.0964 0.1386  -0.0962 107 ALA A CB  
925  N N   . THR A 107 ? 0.4230 0.3008 0.2963 -0.0796 0.1091  -0.0728 108 THR A N   
926  C CA  . THR A 107 ? 0.4079 0.2883 0.2823 -0.0733 0.0966  -0.0642 108 THR A CA  
927  C C   . THR A 107 ? 0.4319 0.3245 0.3286 -0.0621 0.0930  -0.0596 108 THR A C   
928  O O   . THR A 107 ? 0.4000 0.2932 0.3042 -0.0556 0.0884  -0.0555 108 THR A O   
929  C CB  . THR A 107 ? 0.4630 0.3390 0.3165 -0.0781 0.0867  -0.0593 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4838 0.3475 0.3142 -0.0882 0.0898  -0.0638 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4678 0.3480 0.3238 -0.0728 0.0750  -0.0535 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3977 0.2995 0.3037 -0.0608 0.0955  -0.0610 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3744 0.2896 0.3010 -0.0504 0.0912  -0.0578 109 ALA A CA  
934  C C   . ALA A 108 ? 0.3981 0.3145 0.3421 -0.0411 0.0949  -0.0604 109 ALA A C   
935  O O   . ALA A 108 ? 0.3698 0.2890 0.3224 -0.0317 0.0882  -0.0544 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3768 0.3027 0.3100 -0.0528 0.0942  -0.0613 109 ALA A CB  
937  N N   . MET A 109 ? 0.3821 0.2936 0.3288 -0.0437 0.1055  -0.0691 110 MET A N   
938  C CA  . MET A 109 ? 0.3782 0.2868 0.3400 -0.0336 0.1087  -0.0718 110 MET A CA  
939  C C   . MET A 109 ? 0.4246 0.3186 0.3767 -0.0314 0.1043  -0.0649 110 MET A C   
940  O O   . MET A 109 ? 0.4236 0.3148 0.3840 -0.0209 0.1001  -0.0600 110 MET A O   
941  C CB  . MET A 109 ? 0.4203 0.3258 0.3862 -0.0379 0.1220  -0.0840 110 MET A CB  
942  C CG  . MET A 109 ? 0.4747 0.3973 0.4569 -0.0382 0.1280  -0.0929 110 MET A CG  
943  S SD  . MET A 109 ? 0.5780 0.4970 0.5609 -0.0477 0.1458  -0.1091 110 MET A SD  
944  C CE  . MET A 109 ? 0.5505 0.4628 0.5526 -0.0320 0.1475  -0.1124 110 MET A CE  
945  N N   . TYR A 110 ? 0.3965 0.2812 0.3301 -0.0419 0.1048  -0.0648 111 TYR A N   
946  C CA  . TYR A 110 ? 0.3969 0.2701 0.3212 -0.0433 0.1019  -0.0608 111 TYR A CA  
947  C C   . TYR A 110 ? 0.4270 0.3055 0.3527 -0.0380 0.0914  -0.0511 111 TYR A C   
948  O O   . TYR A 110 ? 0.3911 0.2613 0.3177 -0.0333 0.0903  -0.0470 111 TYR A O   
949  C CB  . TYR A 110 ? 0.4114 0.2796 0.3171 -0.0559 0.1028  -0.0643 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.4158 0.2775 0.3129 -0.0597 0.0989  -0.0620 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4621 0.3104 0.3585 -0.0610 0.1059  -0.0657 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.4083 0.2774 0.2979 -0.0628 0.0891  -0.0579 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.4325 0.2761 0.3215 -0.0666 0.1039  -0.0654 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.4133 0.2802 0.2977 -0.0673 0.0863  -0.0585 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4692 0.3239 0.3532 -0.0701 0.0942  -0.0625 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4364 0.2907 0.3157 -0.0767 0.0926  -0.0648 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3905 0.2810 0.3150 -0.0392 0.0847  -0.0479 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3657 0.2629 0.2916 -0.0352 0.0754  -0.0401 112 LEU A CA  
959  C C   . LEU A 111 ? 0.3997 0.3030 0.3394 -0.0241 0.0727  -0.0362 112 LEU A C   
960  O O   . LEU A 111 ? 0.3874 0.2939 0.3272 -0.0205 0.0659  -0.0299 112 LEU A O   
961  C CB  . LEU A 111 ? 0.3545 0.2600 0.2731 -0.0402 0.0691  -0.0388 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3937 0.2941 0.2966 -0.0491 0.0671  -0.0411 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.3937 0.2997 0.2894 -0.0509 0.0593  -0.0386 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.4091 0.3064 0.3095 -0.0507 0.0647  -0.0405 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3629 0.2687 0.3147 -0.0185 0.0777  -0.0408 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3591 0.2729 0.3258 -0.0063 0.0736  -0.0386 113 GLN A CA  
967  C C   . GLN A 112 ? 0.3926 0.3235 0.3637 -0.0061 0.0665  -0.0359 113 GLN A C   
968  O O   . GLN A 112 ? 0.3854 0.3195 0.3564 -0.0009 0.0588  -0.0292 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3744 0.2742 0.3375 0.0017  0.0705  -0.0318 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.4288 0.3091 0.3878 0.0015  0.0787  -0.0353 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.5753 0.4365 0.5236 0.0052  0.0768  -0.0279 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.4952 0.3569 0.4432 0.0130  0.0694  -0.0206 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.5460 0.3890 0.4834 -0.0017 0.0838  -0.0299 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3392 0.2788 0.3114 -0.0132 0.0701  -0.0415 114 MET A N   
975  C CA  . MET A 113 ? 0.3311 0.2847 0.3063 -0.0153 0.0657  -0.0409 114 MET A CA  
976  C C   . MET A 113 ? 0.4048 0.3727 0.3974 -0.0135 0.0711  -0.0498 114 MET A C   
977  O O   . MET A 113 ? 0.3883 0.3570 0.3782 -0.0226 0.0791  -0.0569 114 MET A O   
978  C CB  . MET A 113 ? 0.3475 0.2947 0.3053 -0.0266 0.0660  -0.0401 114 MET A CB  
979  C CG  . MET A 113 ? 0.3765 0.3152 0.3221 -0.0274 0.0597  -0.0335 114 MET A CG  
980  S SD  . MET A 113 ? 0.4300 0.3611 0.3562 -0.0377 0.0579  -0.0337 114 MET A SD  
981  C CE  . MET A 113 ? 0.3872 0.3285 0.3157 -0.0373 0.0520  -0.0312 114 MET A CE  
982  N N   . GLU A 114 ? 0.3964 0.3748 0.4063 -0.0014 0.0669  -0.0503 115 GLU A N   
983  C CA  . GLU A 114 ? 0.4099 0.4056 0.4424 0.0038  0.0707  -0.0606 115 GLU A CA  
984  C C   . GLU A 114 ? 0.4053 0.4174 0.4442 -0.0056 0.0752  -0.0685 115 GLU A C   
985  O O   . GLU A 114 ? 0.3956 0.4154 0.4455 -0.0096 0.0850  -0.0799 115 GLU A O   
986  C CB  . GLU A 114 ? 0.4407 0.4457 0.4886 0.0201  0.0612  -0.0581 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.6126 0.5976 0.6538 0.0296  0.0587  -0.0516 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3664 0.3832 0.3986 -0.0098 0.0694  -0.0636 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3803 0.4097 0.4166 -0.0199 0.0748  -0.0714 116 HIS A CA  
990  C C   . HIS A 115 ? 0.4035 0.4181 0.4218 -0.0348 0.0858  -0.0749 116 HIS A C   
991  O O   . HIS A 115 ? 0.4079 0.4307 0.4324 -0.0435 0.0958  -0.0856 116 HIS A O   
992  C CB  . HIS A 115 ? 0.4037 0.4397 0.4367 -0.0206 0.0663  -0.0660 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.4599 0.5115 0.5087 -0.0073 0.0557  -0.0638 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4971 0.5717 0.5711 -0.0003 0.0554  -0.0736 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4884 0.5359 0.5298 -0.0005 0.0451  -0.0536 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4885 0.5705 0.5677 0.0116  0.0432  -0.0679 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4916 0.5568 0.5503 0.0110  0.0375  -0.0557 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.3415 0.3346 0.3372 -0.0382 0.0842  -0.0669 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3524 0.3287 0.3268 -0.0512 0.0926  -0.0691 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.4152 0.3929 0.3980 -0.0534 0.1044  -0.0795 117 VAL A C   
1001 O O   . VAL A 116 ? 0.4066 0.3829 0.3838 -0.0652 0.1155  -0.0880 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.4076 0.3638 0.3579 -0.0529 0.0863  -0.0594 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.4249 0.3636 0.3517 -0.0654 0.0938  -0.0622 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3977 0.3537 0.3413 -0.0513 0.0759  -0.0513 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3658 0.3447 0.3610 -0.0426 0.1028  -0.0796 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3732 0.3537 0.3792 -0.0428 0.1140  -0.0906 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.4324 0.4350 0.4609 -0.0452 0.1223  -0.1042 118 VAL A C   
1008 O O   . VAL A 117 ? 0.4259 0.4273 0.4517 -0.0564 0.1357  -0.1149 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.4019 0.3787 0.4190 -0.0288 0.1100  -0.0881 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.4091 0.3876 0.4396 -0.0280 0.1220  -0.1010 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.3991 0.3549 0.3939 -0.0300 0.1046  -0.0774 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.4000 0.4228 0.4487 -0.0364 0.1147  -0.1044 119 ASP A N   
1013 N N   B ASP A 118 ? 0.3970 0.4202 0.4471 -0.0355 0.1146  -0.1047 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.4032 0.4520 0.4770 -0.0379 0.1206  -0.1183 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.3998 0.4495 0.4760 -0.0363 0.1204  -0.1188 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.4360 0.4827 0.4962 -0.0578 0.1326  -0.1252 119 ASP A C   
1017 C C   B ASP A 118 ? 0.4479 0.4971 0.5123 -0.0560 0.1326  -0.1264 119 ASP A C   
1018 O O   A ASP A 118 ? 0.4390 0.4969 0.5116 -0.0656 0.1461  -0.1404 119 ASP A O   
1019 O O   B ASP A 118 ? 0.4521 0.5139 0.5305 -0.0631 0.1459  -0.1419 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.4210 0.4900 0.5138 -0.0254 0.1074  -0.1153 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.4145 0.4841 0.5090 -0.0239 0.1070  -0.1155 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.5982 0.6987 0.7209 -0.0255 0.1117  -0.1312 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.5704 0.6470 0.6841 -0.0034 0.0968  -0.1133 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.6342 0.7490 0.7809 -0.0192 0.1174  -0.1438 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.6070 0.6833 0.7329 0.0027  0.1026  -0.1208 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.6693 0.7812 0.7929 -0.0319 0.1096  -0.1322 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.6483 0.7295 0.7636 0.0067  0.0833  -0.1045 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.3855 0.4166 0.4197 -0.0663 0.1283  -0.1148 120 THR A N   
1029 N N   B THR A 119 ? 0.4025 0.4358 0.4405 -0.0649 0.1288  -0.1162 120 THR A N   
1030 C CA  A THR A 119 ? 0.4007 0.4236 0.4168 -0.0853 0.1395  -0.1200 120 THR A CA  
1031 C CA  B THR A 119 ? 0.4163 0.4420 0.4364 -0.0837 0.1395  -0.1210 120 THR A CA  
1032 C C   A THR A 119 ? 0.4584 0.4606 0.4520 -0.0977 0.1521  -0.1236 120 THR A C   
1033 C C   B THR A 119 ? 0.4701 0.4744 0.4667 -0.0967 0.1522  -0.1245 120 THR A C   
1034 O O   A THR A 119 ? 0.4519 0.4528 0.4388 -0.1133 0.1665  -0.1341 120 THR A O   
1035 O O   B THR A 119 ? 0.4710 0.4761 0.4637 -0.1118 0.1669  -0.1359 120 THR A O   
1036 C CB  A THR A 119 ? 0.4200 0.4299 0.4144 -0.0900 0.1316  -0.1089 120 THR A CB  
1037 C CB  B THR A 119 ? 0.5030 0.5170 0.5033 -0.0866 0.1302  -0.1091 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.4581 0.4621 0.4394 -0.1078 0.1439  -0.1163 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4738 0.5065 0.4948 -0.0728 0.1174  -0.1051 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.3807 0.3631 0.3452 -0.0886 0.1232  -0.0942 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.5140 0.5240 0.5021 -0.1040 0.1405  -0.1155 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.4274 0.4132 0.4082 -0.0920 0.1473  -0.1157 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.4513 0.4172 0.4092 -0.1032 0.1579  -0.1191 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.5096 0.4913 0.4901 -0.1061 0.1731  -0.1365 121 CYS A C   
1045 O O   . CYS A 120 ? 0.5129 0.4868 0.4788 -0.1226 0.1881  -0.1458 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.4600 0.4096 0.4044 -0.0957 0.1490  -0.1088 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.5096 0.4379 0.4221 -0.0965 0.1342  -0.0917 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4606 0.4639 0.4761 -0.0899 0.1692  -0.1415 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4632 0.4662 0.4784 -0.0900 0.1693  -0.1415 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4684 0.4910 0.5129 -0.0881 0.1816  -0.1594 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4725 0.4943 0.5159 -0.0889 0.1821  -0.1596 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.5182 0.5591 0.5740 -0.1017 0.1947  -0.1747 122 ARG A C   
1053 C C   B ARG A 121 ? 0.5193 0.5602 0.5751 -0.1019 0.1949  -0.1748 122 ARG A C   
1054 O O   A ARG A 121 ? 0.5186 0.5636 0.5786 -0.1129 0.2119  -0.1903 122 ARG A O   
1055 O O   B ARG A 121 ? 0.5185 0.5638 0.5789 -0.1131 0.2121  -0.1906 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4660 0.5082 0.5455 -0.0655 0.1709  -0.1600 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.4765 0.5162 0.5539 -0.0663 0.1721  -0.1603 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.6344 0.6583 0.7061 -0.0533 0.1626  -0.1493 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6645 0.6860 0.7351 -0.0570 0.1690  -0.1543 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7900 0.8289 0.8945 -0.0323 0.1564  -0.1534 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.8022 0.8393 0.9074 -0.0372 0.1653  -0.1610 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.8737 0.8916 0.9670 -0.0211 0.1470  -0.1406 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.8624 0.9080 0.9791 -0.0204 0.1477  -0.1501 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 1.0263 1.0268 1.1122 -0.0214 0.1539  -0.1430 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 0.9977 1.0280 1.1080 -0.0070 0.1361  -0.1373 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.9117 0.9136 1.0002 -0.0319 0.1700  -0.1578 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.8213 0.8284 0.9163 -0.0082 0.1402  -0.1342 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.8078 0.7891 0.8831 -0.0126 0.1458  -0.1316 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.7915 0.8292 0.9096 0.0064  0.1211  -0.1280 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4680 0.5198 0.5283 -0.1020 0.1878  -0.1710 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4758 0.5458 0.5472 -0.1159 0.1996  -0.1855 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.5397 0.5843 0.5734 -0.1406 0.2148  -0.1871 123 LYS A C   
1073 O O   . LYS A 122 ? 0.5230 0.5775 0.5637 -0.1555 0.2332  -0.2047 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.4893 0.5761 0.5741 -0.1092 0.1871  -0.1807 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.7043 0.8221 0.8303 -0.0871 0.1752  -0.1847 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.8556 0.9904 0.9931 -0.0808 0.1623  -0.1804 123 LYS A CD  
1077 C CE  . LYS A 122 ? 1.0174 1.1773 1.1890 -0.0571 0.1479  -0.1815 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.1591 1.3513 1.3565 -0.0545 0.1421  -0.1901 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.5045 0.5158 0.4974 -0.1449 0.2073  -0.1694 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.5334 0.5140 0.4835 -0.1665 0.2188  -0.1680 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.6044 0.5752 0.5436 -0.1763 0.2339  -0.1778 124 PHE A C   
1082 O O   . PHE A 123 ? 0.6097 0.5706 0.5304 -0.1970 0.2518  -0.1880 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.5614 0.5108 0.4741 -0.1645 0.2040  -0.1471 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.5808 0.5281 0.4878 -0.1656 0.1964  -0.1399 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.5969 0.5747 0.5400 -0.1550 0.1899  -0.1435 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.6376 0.5511 0.5022 -0.1758 0.1942  -0.1290 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.6081 0.5838 0.5456 -0.1570 0.1837  -0.1380 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.6584 0.5680 0.5179 -0.1764 0.1877  -0.1229 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.6046 0.5457 0.5009 -0.1678 0.1831  -0.1278 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.5453 0.5189 0.4965 -0.1624 0.2282  -0.1759 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5683 0.5348 0.5132 -0.1699 0.2423  -0.1865 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.6318 0.6270 0.6107 -0.1762 0.2610  -0.2104 125 ILE A C   
1093 O O   . ILE A 124 ? 0.6529 0.6392 0.6153 -0.1954 0.2802  -0.2226 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.5931 0.5536 0.5417 -0.1538 0.2314  -0.1786 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.5952 0.5257 0.5041 -0.1541 0.2175  -0.1589 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.6248 0.5841 0.5764 -0.1598 0.2474  -0.1933 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.6741 0.6027 0.5905 -0.1366 0.2025  -0.1485 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.5782 0.6083 0.6038 -0.1606 0.2554  -0.2179 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.5893 0.6529 0.6542 -0.1637 0.2709  -0.2425 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.6568 0.7216 0.7093 -0.1892 0.2891  -0.2546 126 LYS A C   
1101 O O   . LYS A 125 ? 0.6498 0.7280 0.7151 -0.2024 0.3096  -0.2759 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.6027 0.7024 0.7167 -0.1406 0.2575  -0.2463 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.6176 0.6663 0.6435 -0.1970 0.2826  -0.2416 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.6454 0.6885 0.6535 -0.2223 0.2997  -0.2510 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.7588 0.7673 0.7206 -0.2466 0.3183  -0.2535 127 ALA A C   
1106 O O   . ALA A 126 ? 0.7702 0.7810 0.7267 -0.2691 0.3398  -0.2699 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.6457 0.6754 0.6345 -0.2226 0.2867  -0.2349 127 ALA A CB  
1108 N N   . SER A 127 ? 0.7612 0.7377 0.6882 -0.2430 0.3104  -0.2380 128 SER A N   
1109 C CA  . SER A 127 ? 0.8242 0.7647 0.7015 -0.2647 0.3248  -0.2380 128 SER A CA  
1110 C C   . SER A 127 ? 0.9239 0.8740 0.8131 -0.2712 0.3430  -0.2568 128 SER A C   
1111 O O   . SER A 127 ? 0.9751 0.8990 0.8250 -0.2931 0.3594  -0.2614 128 SER A O   
1112 C CB  . SER A 127 ? 0.8997 0.8015 0.7315 -0.2592 0.3070  -0.2134 128 SER A CB  
1113 O OG  . SER A 127 ? 1.0548 0.9317 0.8530 -0.2671 0.3010  -0.2003 128 SER A OG  
1114 N N   . GLU A 128 ? 0.8541 0.8397 0.7954 -0.2527 0.3406  -0.2681 129 GLU A N   
1115 C CA  . GLU A 128 ? 1.0874 1.0843 1.0456 -0.2560 0.3573  -0.2874 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.6236 1.6447 1.6033 -0.2755 0.3839  -0.3154 129 GLU A C   
1117 O O   . GLU A 128 ? 1.2178 1.2335 1.1804 -0.2948 0.3941  -0.3188 129 GLU A O   
1118 C CB  . GLU A 128 ? 1.0705 1.0906 1.0727 -0.2275 0.3437  -0.2879 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.1652 1.2305 1.2274 -0.2110 0.3400  -0.3010 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.4188 1.5010 1.5185 -0.1806 0.3228  -0.2972 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.3635 1.4215 1.4422 -0.1696 0.3082  -0.2784 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.3063 1.4258 1.4563 -0.1678 0.3236  -0.3136 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.2489 0.4933 0.3144 -0.0258 -0.0230 -0.0975 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2558 0.5001 0.3212 -0.0258 -0.0230 -0.0975 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.2377 0.4805 0.3022 -0.0252 -0.0233 -0.0985 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2486 0.4916 0.3133 -0.0253 -0.0233 -0.0985 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2960 0.5392 0.3628 -0.0255 -0.0242 -0.0982 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2892 0.5328 0.3563 -0.0255 -0.0240 -0.0981 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2955 0.5385 0.3636 -0.0259 -0.0252 -0.0976 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2783 0.5222 0.3469 -0.0261 -0.0249 -0.0974 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.2269 0.4675 0.2888 -0.0247 -0.0245 -0.0991 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.2390 0.4797 0.3013 -0.0247 -0.0245 -0.0991 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.2304 0.4705 0.2891 -0.0244 -0.0238 -0.0997 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2504 0.4907 0.3142 -0.0247 -0.0263 -0.0993 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2641 0.5037 0.3217 -0.0246 -0.0238 -0.0998 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.2893 0.5290 0.3541 -0.0249 -0.0275 -0.0998 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.2221 0.4622 0.2786 -0.0239 -0.0230 -0.1001 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2504 0.4915 0.3157 -0.0245 -0.0272 -0.0995 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2517 0.4908 0.3054 -0.0242 -0.0229 -0.1006 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.2849 0.5251 0.3524 -0.0247 -0.0290 -0.1007 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2653 0.5047 0.3182 -0.0238 -0.0224 -0.1008 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.3000 0.5414 0.3674 -0.0244 -0.0287 -0.1006 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.2312 0.4717 0.2890 -0.0236 -0.0227 -0.0998 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2597 0.5017 0.3256 -0.0243 -0.0268 -0.0990 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2616 0.5008 0.3115 -0.0233 -0.0215 -0.1014 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.2913 0.5343 0.3608 -0.0241 -0.0295 -0.1014 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.2457 0.4860 0.3017 -0.0231 -0.0220 -0.1000 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.2796 0.5230 0.3469 -0.0240 -0.0275 -0.0993 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2552 0.4948 0.3070 -0.0230 -0.0213 -0.1009 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.2857 0.5298 0.3546 -0.0239 -0.0287 -0.1006 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.2388 0.4827 0.3067 -0.0252 -0.0238 -0.0986 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.2377 0.4822 0.3074 -0.0254 -0.0244 -0.0985 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2636 0.5072 0.3337 -0.0248 -0.0246 -0.0984 2   VAL D C   
1157 O O   . VAL B 3   ? 0.2461 0.4893 0.3161 -0.0243 -0.0243 -0.0982 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2712 0.5193 0.3435 -0.0259 -0.0240 -0.0992 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2663 0.5174 0.3390 -0.0266 -0.0239 -0.0983 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2674 0.5174 0.3421 -0.0254 -0.0230 -0.1006 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.2218 0.4657 0.2930 -0.0248 -0.0252 -0.0982 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.2155 0.4597 0.2884 -0.0244 -0.0253 -0.0975 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2779 0.5230 0.3544 -0.0246 -0.0249 -0.0984 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2694 0.5157 0.3464 -0.0250 -0.0252 -0.0995 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.2432 0.4880 0.3156 -0.0242 -0.0258 -0.0971 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.2270 0.4725 0.2976 -0.0239 -0.0263 -0.0974 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2679 0.5141 0.3429 -0.0238 -0.0257 -0.0957 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.2994 0.5467 0.3694 -0.0232 -0.0266 -0.0967 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2789 0.5242 0.3585 -0.0242 -0.0245 -0.0984 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2843 0.5315 0.3690 -0.0243 -0.0244 -0.1003 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.3249 0.5725 0.4132 -0.0243 -0.0253 -0.1002 4   PRO D C   
1172 O O   . PRO B 5   ? 0.3110 0.5573 0.3989 -0.0240 -0.0255 -0.0979 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.3048 0.5518 0.3926 -0.0238 -0.0238 -0.1003 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.3604 0.6055 0.4455 -0.0235 -0.0241 -0.0973 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.3066 0.5511 0.3857 -0.0237 -0.0243 -0.0969 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.3161 0.5663 0.4084 -0.0245 -0.0257 -0.1029 5   ALA D N   
# 
