data_7GUT
# 
_entry.id   7GUT 
# 
_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   7GUT         pdb_00007gut 10.2210/pdb7gut/pdb 
WWPDB D_1001406664 ?            ?                   
# 
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                        7GUT 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              Rob.vanMontfort@icr.ac.uk 
_pdbx_contact_author.name_first         Rob 
_pdbx_contact_author.name_last          'van Montfort' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodrigues, M.J.'      1 0000-0003-1243-903X 
'Le Bihan, Y.V.'       2 0000-0002-6850-9706 
'van Montfort, R.L.M.' 3 0000-0002-5688-3450 
# 
_citation.id                        primary 
_citation.title                     
'Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.' 
_citation.journal_abbrev            J.Appl.Crystallogr. 
_citation.journal_volume            57 
_citation.page_first                1951 
_citation.page_last                 1965 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39628887 
_citation.pdbx_database_id_DOI      10.1107/S1600576724010549 
_citation.journal_id_ASTM           JACGAR 
_citation.country                   DK 
_citation.journal_id_ISSN           0021-8898 
_citation.journal_id_CSD            0228 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodrigues, M.J.'      1 0000-0003-1243-903X 
primary 'Cabry, M.'            2 0000-0002-9070-5498 
primary 'Collie, G.'           3 0000-0002-0406-922X 
primary 'Carter, M.'           4 ?                   
primary 'McAndrew, C.'         5 0000-0002-1366-088X 
primary 'Owen, R.L.'           6 0000-0002-2104-7057 
primary 'Bellenie, B.R.'       7 0000-0001-9987-3079 
primary 'Le Bihan, Y.V.'       8 0000-0002-6850-9706 
primary 'van Montfort, R.L.M.' 9 0000-0002-5688-3450 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'B-cell lymphoma 6 protein'                                            14536.915 1   ? ? ? ? 
2 polymer     syn 'WVIP tetrapeptide'                                                    610.744   1   ? ? ? ? 
3 non-polymer syn '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' 339.575   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                         35.453    1   ? ? ? ? 
5 non-polymer nat 'DIMETHYL SULFOXIDE'                                                   78.133    1   ? ? ? ? 
6 water       nat water                                                                  18.015    185 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'BCL-6,B-cell lymphoma 5 protein,BCL-5,Protein LAZ-3,Zinc finger and BTB domain-containing protein 27,Zinc finger protein 51' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
A ? 
2 'polypeptide(L)' no yes '(ACE)WVIPA' XWVIPA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' A1ACA 
4 'CHLORIDE ION'                                                         CL    
5 'DIMETHYL SULFOXIDE'                                                   DMS   
6 water                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   ALA n 
1 5   ASP n 
1 6   SER n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  PHE n 
1 11  THR n 
1 12  ARG n 
1 13  HIS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  LEU n 
1 19  LEU n 
1 20  ASN n 
1 21  LEU n 
1 22  ASN n 
1 23  ARG n 
1 24  LEU n 
1 25  ARG n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  THR n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  ILE n 
1 36  VAL n 
1 37  VAL n 
1 38  SER n 
1 39  ARG n 
1 40  GLU n 
1 41  GLN n 
1 42  PHE n 
1 43  ARG n 
1 44  ALA n 
1 45  HIS n 
1 46  LYS n 
1 47  THR n 
1 48  VAL n 
1 49  LEU n 
1 50  MET n 
1 51  ALA n 
1 52  CYS n 
1 53  SER n 
1 54  GLY n 
1 55  LEU n 
1 56  PHE n 
1 57  TYR n 
1 58  SER n 
1 59  ILE n 
1 60  PHE n 
1 61  THR n 
1 62  ASP n 
1 63  GLN n 
1 64  LEU n 
1 65  LYS n 
1 66  CYS n 
1 67  ASN n 
1 68  LEU n 
1 69  SER n 
1 70  VAL n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ASP n 
1 75  PRO n 
1 76  GLU n 
1 77  ILE n 
1 78  ASN n 
1 79  PRO n 
1 80  GLU n 
1 81  GLY n 
1 82  PHE n 
1 83  CYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  ASP n 
1 88  PHE n 
1 89  MET n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ARG n 
1 94  LEU n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLU n 
1 99  GLY n 
1 100 ASN n 
1 101 ILE n 
1 102 MET n 
1 103 ALA n 
1 104 VAL n 
1 105 MET n 
1 106 ALA n 
1 107 THR n 
1 108 ALA n 
1 109 MET n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 MET n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 VAL n 
1 118 ASP n 
1 119 THR n 
1 120 CYS n 
1 121 ARG n 
1 122 LYS n 
1 123 PHE n 
1 124 ILE n 
1 125 LYS n 
1 126 ALA n 
1 127 SER n 
1 128 GLU n 
2 1   ACE n 
2 2   TRP n 
2 3   VAL n 
2 4   ILE n 
2 5   PRO n 
2 6   ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCL6, BCL5, LAZ3, ZBTB27, ZNF51' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21-AI 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET48b 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 6 'synthetic construct' ? 32630 ? 
3 2 sample ? ? 'synthetic construct' ? 32630 ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ACA non-polymer         . '5-[(5-bromo-2-chloropyrimidin-4-yl)amino]-1,3-dihydro-2H-indol-2-one' ? 'C12 H8 Br Cl N4 O' 339.575 
ACE   non-polymer         . 'ACETYL GROUP'                                                         ? 'C2 H4 O'           44.053  
ALA   'L-peptide linking' y ALANINE                                                                ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE                                                               ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                             ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                        ? 'C4 H7 N O4'        133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                         ? 'Cl -1'             35.453  
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'      121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                   ? 'C2 H6 O S'         78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                  ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                                             ? 'C5 H11 N O2 S'     149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                                                                ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE                                                                 ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE                                                              ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                             ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE                                                               ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE                                                                 ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLY 3   4   ?   ?   ?   A . n 
A 1 4   ALA 4   5   ?   ?   ?   A . n 
A 1 5   ASP 5   6   6   ASP ASP A . n 
A 1 6   SER 6   7   7   SER SER A . n 
A 1 7   CYS 7   8   8   CYS CYS A . n 
A 1 8   ILE 8   9   9   ILE ILE A . n 
A 1 9   GLN 9   10  10  GLN GLN A . n 
A 1 10  PHE 10  11  11  PHE PHE A . n 
A 1 11  THR 11  12  12  THR THR A . n 
A 1 12  ARG 12  13  13  ARG ARG A . n 
A 1 13  HIS 13  14  14  HIS HIS A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ASP 16  17  17  ASP ASP A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  ASN 20  21  21  ASN ASN A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  ARG 23  24  24  ARG ARG A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  ARG 25  26  26  ARG ARG A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  THR 31  32  32  THR THR A . n 
A 1 32  ASP 32  33  33  ASP ASP A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  VAL 36  37  37  VAL VAL A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  SER 38  39  39  SER SER A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLN 41  42  42  GLN GLN A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  ALA 44  45  45  ALA ALA A . n 
A 1 45  HIS 45  46  46  HIS HIS A . n 
A 1 46  LYS 46  47  47  LYS LYS A . n 
A 1 47  THR 47  48  48  THR THR A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  MET 50  51  51  MET MET A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  CYS 52  53  53  CYS CYS A . n 
A 1 53  SER 53  54  54  SER SER A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  PHE 60  61  61  PHE PHE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  ASN 67  68  68  ASN ASN A . n 
A 1 68  LEU 68  69  69  LEU LEU A . n 
A 1 69  SER 69  70  70  SER SER A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ILE 71  72  72  ILE ILE A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  ASP 74  75  75  ASP ASP A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLU 76  77  77  GLU GLU A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  PRO 79  80  80  PRO PRO A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  CYS 83  84  84  CYS CYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  LEU 85  86  86  LEU LEU A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  PHE 88  89  89  PHE PHE A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  ASN 95  96  96  ASN ASN A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ARG 97  98  98  ARG ARG A . n 
A 1 98  GLU 98  99  99  GLU GLU A . n 
A 1 99  GLY 99  100 100 GLY GLY A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 MET 102 103 103 MET MET A . n 
A 1 103 ALA 103 104 104 ALA ALA A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 MET 105 106 106 MET MET A . n 
A 1 106 ALA 106 107 107 ALA ALA A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 MET 109 110 110 MET MET A . n 
A 1 110 TYR 110 111 111 TYR TYR A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLN 112 113 113 GLN GLN A . n 
A 1 113 MET 113 114 114 MET MET A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 HIS 115 116 116 HIS HIS A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 VAL 117 118 118 VAL VAL A . n 
A 1 118 ASP 118 119 119 ASP ASP A . n 
A 1 119 THR 119 120 120 THR THR A . n 
A 1 120 CYS 120 121 121 CYS CYS A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 PHE 123 124 124 PHE PHE A . n 
A 1 124 ILE 124 125 125 ILE ILE A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 SER 127 128 128 SER SER A . n 
A 1 128 GLU 128 129 129 GLU GLU A . n 
B 2 1   ACE 1   0   0   ACE ACE D . n 
B 2 2   TRP 2   1   1   TRP TRP D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ILE 4   3   3   ILE ILE D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   ALA 6   5   5   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1ACA 1   201 1   A1ACA 763 A . 
D 4 CL    1   202 1   CL    CL  A . 
E 5 DMS   1   101 1   DMS   DMS D . 
F 6 HOH   1   301 178 HOH   HOH A . 
F 6 HOH   2   302 7   HOH   HOH A . 
F 6 HOH   3   303 19  HOH   HOH A . 
F 6 HOH   4   304 45  HOH   HOH A . 
F 6 HOH   5   305 140 HOH   HOH A . 
F 6 HOH   6   306 94  HOH   HOH A . 
F 6 HOH   7   307 166 HOH   HOH A . 
F 6 HOH   8   308 100 HOH   HOH A . 
F 6 HOH   9   309 173 HOH   HOH A . 
F 6 HOH   10  310 202 HOH   HOH A . 
F 6 HOH   11  311 29  HOH   HOH A . 
F 6 HOH   12  312 106 HOH   HOH A . 
F 6 HOH   13  313 83  HOH   HOH A . 
F 6 HOH   14  314 247 HOH   HOH A . 
F 6 HOH   15  315 99  HOH   HOH A . 
F 6 HOH   16  316 90  HOH   HOH A . 
F 6 HOH   17  317 75  HOH   HOH A . 
F 6 HOH   18  318 47  HOH   HOH A . 
F 6 HOH   19  319 142 HOH   HOH A . 
F 6 HOH   20  320 179 HOH   HOH A . 
F 6 HOH   21  321 84  HOH   HOH A . 
F 6 HOH   22  322 37  HOH   HOH A . 
F 6 HOH   23  323 119 HOH   HOH A . 
F 6 HOH   24  324 193 HOH   HOH A . 
F 6 HOH   25  325 20  HOH   HOH A . 
F 6 HOH   26  326 139 HOH   HOH A . 
F 6 HOH   27  327 237 HOH   HOH A . 
F 6 HOH   28  328 87  HOH   HOH A . 
F 6 HOH   29  329 101 HOH   HOH A . 
F 6 HOH   30  330 91  HOH   HOH A . 
F 6 HOH   31  331 6   HOH   HOH A . 
F 6 HOH   32  332 239 HOH   HOH A . 
F 6 HOH   33  333 132 HOH   HOH A . 
F 6 HOH   34  334 14  HOH   HOH A . 
F 6 HOH   35  335 151 HOH   HOH A . 
F 6 HOH   36  336 117 HOH   HOH A . 
F 6 HOH   37  337 27  HOH   HOH A . 
F 6 HOH   38  338 40  HOH   HOH A . 
F 6 HOH   39  339 17  HOH   HOH A . 
F 6 HOH   40  340 242 HOH   HOH A . 
F 6 HOH   41  341 4   HOH   HOH A . 
F 6 HOH   42  342 196 HOH   HOH A . 
F 6 HOH   43  343 243 HOH   HOH A . 
F 6 HOH   44  344 28  HOH   HOH A . 
F 6 HOH   45  345 144 HOH   HOH A . 
F 6 HOH   46  346 34  HOH   HOH A . 
F 6 HOH   47  347 42  HOH   HOH A . 
F 6 HOH   48  348 24  HOH   HOH A . 
F 6 HOH   49  349 86  HOH   HOH A . 
F 6 HOH   50  350 85  HOH   HOH A . 
F 6 HOH   51  351 44  HOH   HOH A . 
F 6 HOH   52  352 5   HOH   HOH A . 
F 6 HOH   53  353 96  HOH   HOH A . 
F 6 HOH   54  354 93  HOH   HOH A . 
F 6 HOH   55  355 133 HOH   HOH A . 
F 6 HOH   56  356 122 HOH   HOH A . 
F 6 HOH   57  357 89  HOH   HOH A . 
F 6 HOH   58  358 141 HOH   HOH A . 
F 6 HOH   59  359 50  HOH   HOH A . 
F 6 HOH   60  360 12  HOH   HOH A . 
F 6 HOH   61  361 175 HOH   HOH A . 
F 6 HOH   62  362 97  HOH   HOH A . 
F 6 HOH   63  363 51  HOH   HOH A . 
F 6 HOH   64  364 124 HOH   HOH A . 
F 6 HOH   65  365 145 HOH   HOH A . 
F 6 HOH   66  366 244 HOH   HOH A . 
F 6 HOH   67  367 15  HOH   HOH A . 
F 6 HOH   68  368 30  HOH   HOH A . 
F 6 HOH   69  369 25  HOH   HOH A . 
F 6 HOH   70  370 207 HOH   HOH A . 
F 6 HOH   71  371 177 HOH   HOH A . 
F 6 HOH   72  372 103 HOH   HOH A . 
F 6 HOH   73  373 192 HOH   HOH A . 
F 6 HOH   74  374 170 HOH   HOH A . 
F 6 HOH   75  375 180 HOH   HOH A . 
F 6 HOH   76  376 223 HOH   HOH A . 
F 6 HOH   77  377 131 HOH   HOH A . 
F 6 HOH   78  378 21  HOH   HOH A . 
F 6 HOH   79  379 186 HOH   HOH A . 
F 6 HOH   80  380 39  HOH   HOH A . 
F 6 HOH   81  381 169 HOH   HOH A . 
F 6 HOH   82  382 194 HOH   HOH A . 
F 6 HOH   83  383 245 HOH   HOH A . 
F 6 HOH   84  384 229 HOH   HOH A . 
F 6 HOH   85  385 74  HOH   HOH A . 
F 6 HOH   86  386 157 HOH   HOH A . 
F 6 HOH   87  387 191 HOH   HOH A . 
F 6 HOH   88  388 105 HOH   HOH A . 
F 6 HOH   89  389 70  HOH   HOH A . 
F 6 HOH   90  390 167 HOH   HOH A . 
F 6 HOH   91  391 55  HOH   HOH A . 
F 6 HOH   92  392 241 HOH   HOH A . 
F 6 HOH   93  393 16  HOH   HOH A . 
F 6 HOH   94  394 76  HOH   HOH A . 
F 6 HOH   95  395 185 HOH   HOH A . 
F 6 HOH   96  396 174 HOH   HOH A . 
F 6 HOH   97  397 32  HOH   HOH A . 
F 6 HOH   98  398 165 HOH   HOH A . 
F 6 HOH   99  399 205 HOH   HOH A . 
F 6 HOH   100 400 22  HOH   HOH A . 
F 6 HOH   101 401 120 HOH   HOH A . 
F 6 HOH   102 402 92  HOH   HOH A . 
F 6 HOH   103 403 212 HOH   HOH A . 
F 6 HOH   104 404 61  HOH   HOH A . 
F 6 HOH   105 405 35  HOH   HOH A . 
F 6 HOH   106 406 190 HOH   HOH A . 
F 6 HOH   107 407 129 HOH   HOH A . 
F 6 HOH   108 408 69  HOH   HOH A . 
F 6 HOH   109 409 60  HOH   HOH A . 
F 6 HOH   110 410 82  HOH   HOH A . 
F 6 HOH   111 411 43  HOH   HOH A . 
F 6 HOH   112 412 64  HOH   HOH A . 
F 6 HOH   113 413 108 HOH   HOH A . 
F 6 HOH   114 414 176 HOH   HOH A . 
F 6 HOH   115 415 26  HOH   HOH A . 
F 6 HOH   116 416 36  HOH   HOH A . 
F 6 HOH   117 417 67  HOH   HOH A . 
F 6 HOH   118 418 46  HOH   HOH A . 
F 6 HOH   119 419 215 HOH   HOH A . 
F 6 HOH   120 420 56  HOH   HOH A . 
F 6 HOH   121 421 88  HOH   HOH A . 
F 6 HOH   122 422 110 HOH   HOH A . 
F 6 HOH   123 423 236 HOH   HOH A . 
F 6 HOH   124 424 68  HOH   HOH A . 
F 6 HOH   125 425 204 HOH   HOH A . 
F 6 HOH   126 426 57  HOH   HOH A . 
F 6 HOH   127 427 65  HOH   HOH A . 
F 6 HOH   128 428 95  HOH   HOH A . 
F 6 HOH   129 429 41  HOH   HOH A . 
F 6 HOH   130 430 116 HOH   HOH A . 
F 6 HOH   131 431 168 HOH   HOH A . 
F 6 HOH   132 432 147 HOH   HOH A . 
F 6 HOH   133 433 135 HOH   HOH A . 
F 6 HOH   134 434 187 HOH   HOH A . 
F 6 HOH   135 435 227 HOH   HOH A . 
F 6 HOH   136 436 200 HOH   HOH A . 
F 6 HOH   137 437 214 HOH   HOH A . 
F 6 HOH   138 438 123 HOH   HOH A . 
F 6 HOH   139 439 248 HOH   HOH A . 
F 6 HOH   140 440 231 HOH   HOH A . 
F 6 HOH   141 441 228 HOH   HOH A . 
F 6 HOH   142 442 71  HOH   HOH A . 
F 6 HOH   143 443 121 HOH   HOH A . 
F 6 HOH   144 444 63  HOH   HOH A . 
F 6 HOH   145 445 225 HOH   HOH A . 
F 6 HOH   146 446 171 HOH   HOH A . 
F 6 HOH   147 447 203 HOH   HOH A . 
F 6 HOH   148 448 238 HOH   HOH A . 
F 6 HOH   149 449 234 HOH   HOH A . 
F 6 HOH   150 450 181 HOH   HOH A . 
F 6 HOH   151 451 220 HOH   HOH A . 
F 6 HOH   152 452 125 HOH   HOH A . 
F 6 HOH   153 453 158 HOH   HOH A . 
F 6 HOH   154 454 114 HOH   HOH A . 
F 6 HOH   155 455 79  HOH   HOH A . 
F 6 HOH   156 456 217 HOH   HOH A . 
F 6 HOH   157 457 81  HOH   HOH A . 
F 6 HOH   158 458 246 HOH   HOH A . 
F 6 HOH   159 459 221 HOH   HOH A . 
F 6 HOH   160 460 235 HOH   HOH A . 
F 6 HOH   161 461 58  HOH   HOH A . 
F 6 HOH   162 462 107 HOH   HOH A . 
F 6 HOH   163 463 115 HOH   HOH A . 
F 6 HOH   164 464 216 HOH   HOH A . 
F 6 HOH   165 465 230 HOH   HOH A . 
F 6 HOH   166 466 182 HOH   HOH A . 
F 6 HOH   167 467 188 HOH   HOH A . 
F 6 HOH   168 468 113 HOH   HOH A . 
F 6 HOH   169 469 183 HOH   HOH A . 
F 6 HOH   170 470 213 HOH   HOH A . 
F 6 HOH   171 471 201 HOH   HOH A . 
F 6 HOH   172 472 48  HOH   HOH A . 
F 6 HOH   173 473 148 HOH   HOH A . 
F 6 HOH   174 474 206 HOH   HOH A . 
F 6 HOH   175 475 172 HOH   HOH A . 
F 6 HOH   176 476 211 HOH   HOH A . 
G 6 HOH   1   201 62  HOH   HOH D . 
G 6 HOH   2   202 78  HOH   HOH D . 
G 6 HOH   3   203 23  HOH   HOH D . 
G 6 HOH   4   204 38  HOH   HOH D . 
G 6 HOH   5   205 53  HOH   HOH D . 
G 6 HOH   6   206 73  HOH   HOH D . 
G 6 HOH   7   207 240 HOH   HOH D . 
G 6 HOH   8   208 49  HOH   HOH D . 
G 6 HOH   9   209 195 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 A LYS 126 ? CG  ? A LYS 125 CG  
8  1 Y 1 A LYS 126 ? CD  ? A LYS 125 CD  
9  1 Y 1 A LYS 126 ? CE  ? A LYS 125 CE  
10 1 Y 1 A LYS 126 ? NZ  ? A LYS 125 NZ  
11 1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
12 1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
13 1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
14 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com phasing           
http://www.globalphasing.com/buster/                ?   ? 
5 PDB_EXTRACT 3.24   'Sep. 1, 2017' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.entry_id           7GUT 
_cell.length_a           67.570 
_cell.length_b           67.570 
_cell.length_c           166.460 
_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                         7GUT 
_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          7GUT 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.62 
_exptl_crystal.density_percent_sol   66.03 
_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                     7GUT 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.910 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23604 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.064 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.100 
_reflns.B_iso_Wilson_estimate        28.130 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.068 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     214323 
_reflns.pdbx_scaling_rejects         1633 
_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  ? 11813 1276 ? 1.047 ? ? ? 9.300 ? 2.400  ? ? ? ? ? ? 100.000 1.108 0.357 0.827 ? 
1 2 9.090 33.910 ? 1489  227  ? 0.039 ? ? ? 6.600 ? 37.900 ? ? ? ? ? ? 98.700  0.042 0.015 0.998 ? 
# 
_refine.entry_id                                 7GUT 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             33.9100 
_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                     23539 
_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                          0.1850 
_refine.ls_R_factor_R_work                       0.1840 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2120 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1400 
_refine.ls_number_reflns_R_free                  1210 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               31.9400 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.0375 
_refine.aniso_B[2][2]                            0.0375 
_refine.aniso_B[3][3]                            -0.0750 
_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               0.9580 
_refine.correlation_coeff_Fo_to_Fc_free          0.9380 
_refine.overall_SU_R_Cruickshank_DPI             0.0890 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0890 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1020 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0980 
_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                                114.090 
_refine.B_iso_min                                14.970 
_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                        7GUT 
_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                        33.9100 
_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           26.82 
_refine_hist.pdbx_B_iso_mean_solvent          47.15 
_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      1674 ?      ? 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           ?    3.380  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.570 ? ?      ?            
# 
_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               99.8600 
_refine_ls_shell.number_reflns_R_work             2685 
_refine_ls_shell.R_factor_all                     0.3600 
_refine_ls_shell.R_factor_R_work                  0.3598 
_refine_ls_shell.R_factor_R_free                  0.3649 
_refine_ls_shell.percent_reflns_R_free            4.4800 
_refine_ls_shell.number_reflns_R_free             126 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2811 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUT 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 2.50 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUT 
_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 7GUT       7GUT   ? 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 7GUT A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUT D 1 ? 6   ? 7GUT   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 7GUT GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUT PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUT GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7390  ? 
1 MORE         -64   ? 
1 'SSA (A^2)'  12950 ? 
# 
_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 33.7850000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5173365337 0.0000000000 0.0000000000 -1.0000000000 27.7433333333 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ARG A 12  ? ARG A 27  ? ARG A 13  ARG A 28  1 ? 16 
HELX_P HELX_P2 AA2 HIS A 45  ? SER A 53  ? HIS A 46  SER A 54  1 ? 9  
HELX_P HELX_P3 AA3 SER A 53  ? THR A 61  ? SER A 54  THR A 62  1 ? 9  
HELX_P HELX_P4 AA4 LEU A 64  ? LEU A 68  ? LEU A 65  LEU A 69  5 ? 5  
HELX_P HELX_P5 AA5 ASN A 78  ? SER A 92  ? ASN A 79  SER A 93  1 ? 15 
HELX_P HELX_P6 AA6 ASN A 100 ? GLN A 112 ? ASN A 101 GLN A 113 1 ? 13 
HELX_P HELX_P7 AA7 MET A 113 ? GLU A 128 ? MET A 114 GLU A 129 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N A ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O PHE A 42 ? O PHE A 43 N ILE A 35 ? N ILE A 36 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GUT 
_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 61.96 -118.91 
2 1 SER A 39  ? B 39.33 66.67   
3 1 ARG A 40  ? B 74.79 -23.12  
4 1 SER A 93  ? A 75.81 -3.29   
5 1 GLN A 113 ? ? 61.65 61.87   
# 
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 374 ? F HOH . 
2 1 A HOH 381 ? F HOH . 
3 1 A HOH 460 ? F HOH . 
4 1 A HOH 465 ? F HOH . 
5 1 A HOH 469 ? F HOH . 
6 1 A HOH 471 ? 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 0.0149  -0.0527 -0.0741 -0.0417 0.0289  -0.0204 0.9521 1.6834  1.8622 
0.4235 -0.3207 1.0985 0.1352 -0.0690 -0.0663 -0.0447 0.0968  0.0840 0.2294  -0.0197 -0.0021 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1139 0.1341  -0.0449 -0.0344 -0.0115 -0.0925 0.7980 -0.2509 0.0000 
0.0131 -0.2193 0.3024 0.0268 -0.0110 -0.0158 -0.0166 -0.0022 0.0190 -0.0189 0.0068  -0.0108 
# 
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                    7GUT 
_atom_sites.fract_transf_matrix[1][1]   0.014799 
_atom_sites.fract_transf_matrix[1][2]   0.008544 
_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]   0.017089 
_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]   0.006007 
_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   ? 17.259 -21.183 -4.878 1.00 61.88  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.188 -22.084 -5.562 1.00 60.68  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.734 -23.558 -5.464 1.00 59.97  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.709 -23.860 -4.842 1.00 60.77  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.617 -21.915 -4.985 1.00 61.63  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.725 -22.002 -6.025 1.00 74.87  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.865 -23.076 -6.664 1.00 74.77  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.461 -21.002 -6.193 1.00 81.98  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.498 -24.464 -6.092 1.00 50.90  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.249 -25.900 -6.069 1.00 48.15  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.237 -26.602 -5.087 1.00 43.94  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.532 -27.784 -5.253 1.00 43.01  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.370 -26.471 -7.478 1.00 53.92  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.653 -26.224 -8.033 1.00 65.34  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.715 -25.883 -4.051 1.00 35.34  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.655 -26.451 -3.083 1.00 31.96  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.037 -27.613 -2.281 1.00 33.21  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.817 -27.677 -2.115 1.00 32.69  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.166 -25.365 -2.133 1.00 32.37  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.359 -24.203 -2.864 1.00 37.37  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.881 -28.515 -1.780 1.00 25.57  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.510 -29.517 -0.778 1.00 23.09  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.129 -28.987 0.516  1.00 24.98  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.075 -28.189 0.462  1.00 23.71  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.871 -30.992 -1.092 1.00 26.37  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.389 -31.168 -1.358 1.00 26.94  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.037 -31.509 -2.266 1.00 25.28  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.887 -32.632 -1.494 1.00 29.80  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.659 -29.432 1.684  0.66 19.98  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.552 -29.371 1.654  0.34 20.75  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.213 -28.940 2.954  0.66 19.55  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 20.973 -28.882 2.955  0.34 19.92  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.548 -30.087 3.889  0.66 22.58  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.368 -30.011 3.884  0.34 23.69  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.775 -31.041 3.980  0.66 23.28  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.665 -31.016 3.965  0.34 23.97  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.220 -27.955 3.628  0.66 21.35  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.840 -28.056 3.573  0.34 21.04  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.464 -27.713 5.139  0.66 27.53  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.322 -27.067 4.628  0.34 18.05  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.071 -26.348 5.630  0.66 45.09  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.565 -27.185 5.929  0.34 34.58  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.619 -25.485 4.872  0.66 37.00  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.338 -27.348 5.963  0.34 29.92  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.270 -26.109 6.922  0.66 38.74  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.286 -27.078 7.036  0.34 32.53  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.689 -29.991 4.590  0.66 19.93  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.486 -29.833 4.590  0.34 20.75  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.053 -31.008 5.568  0.66 19.02  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 22.987 -30.813 5.547  0.34 20.17  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.589 -30.503 6.927  0.66 22.17  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.494 -30.369 6.902  0.34 22.98  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.170 -29.551 7.474  0.66 21.71  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.936 -29.330 7.414  0.34 22.51  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.564 -31.317 5.529  0.66 19.74  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.519 -30.909 5.458  0.34 21.41  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 24.936 -32.523 6.357  0.66 20.47  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 24.984 -31.674 4.239  0.34 23.42  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.559 -33.804 5.962  0.66 22.34  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.694 -31.220 2.954  0.34 27.13  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.727 -32.391 7.494  0.66 20.99  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.724 -32.841 4.372  0.34 26.50  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 24.896 -34.921 6.738  0.66 23.46  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.119 -31.927 1.829  0.34 28.37  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.048 -33.502 8.277  0.66 23.02  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.151 -33.550 3.240  0.34 29.98  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.636 -34.759 7.895  0.66 21.41  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.848 -33.085 1.979  0.34 28.02  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.510 -31.110 7.443  1.00 19.62  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.847 -30.739 8.705  1.00 19.93  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.804 -30.491 9.883  1.00 21.55  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.693 -29.462 10.570 1.00 21.30  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.784 -31.775 9.076  1.00 24.88  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.887 -31.938 7.958  1.00 26.62  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 18.989 -31.377 10.340 1.00 29.47  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.742 -31.424 10.086 1.00 19.08  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.654 -31.339 11.239 1.00 18.98  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.886 -30.434 11.027 1.00 20.48  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.719 -30.354 11.939 1.00 19.89  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.136 -32.756 11.628 1.00 23.30  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.060 -33.718 12.171 1.00 34.46  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.489 -33.282 13.509 1.00 54.27  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.464 -33.354 14.601 1.00 66.75  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.308 -32.763 15.783 1.00 77.65  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.236 -32.889 16.721 1.00 65.34  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.228 -32.030 16.030 1.00 60.71  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.029 -29.787 9.854  1.00 16.90  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.263 -29.046 9.561  1.00 17.49  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.569 -27.949 10.573 1.00 19.65  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.703 -27.884 11.081 1.00 18.83  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.260 -28.486 8.123  1.00 17.26  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.520 -27.732 7.822  1.00 19.22  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.702 -28.400 7.601  1.00 19.88  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.732 -26.401 7.690  1.00 19.78  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.609 -27.467 7.344  1.00 19.08  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.076 -26.244 7.389  1.00 18.41  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.583 -27.071 10.855 1.00 16.89  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.824 -25.956 11.792 1.00 16.87  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.234 -26.463 13.188 1.00 18.43  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.155 -25.910 13.791 1.00 16.61  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.595 -25.050 11.871 1.00 18.07  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.576 -27.518 13.674 0.42 17.28  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.574 -27.526 13.674 0.30 16.99  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.571 -27.515 13.692 0.28 16.56  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.874 -28.093 14.984 0.42 17.06  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.861 -28.127 14.978 0.30 16.91  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.893 -28.068 15.010 0.28 16.24  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.282 -28.693 15.005 0.42 20.98  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.268 -28.714 15.010 0.30 21.13  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.281 -28.717 15.024 0.28 20.83  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.005 -28.519 15.992 0.42 19.00  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 27.977 -28.554 16.007 0.30 19.62  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 27.995 -28.590 16.022 0.28 19.31  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.833 -29.148 15.350 0.42 20.44  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.838 -29.213 15.300 0.30 20.28  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.817 -29.043 15.476 0.28 19.01  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.096 -29.683 16.636 0.42 22.22  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.535 -28.669 15.398 0.30 23.68  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.734 -30.170 14.621 0.28 19.64  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.676 -29.377 13.910 1.00 18.82  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.004 -30.001 13.791 1.00 18.81  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.072 -28.913 13.762 1.00 19.37  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.126 -29.076 14.380 1.00 19.16  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.090 -30.879 12.535 1.00 20.20  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.311 -32.190 12.634 1.00 25.38  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.791 -32.499 13.735 1.00 24.73  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.214 -32.894 11.614 1.00 27.55  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.797 -27.798 13.053 1.00 15.38  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.759 -26.685 13.006 1.00 14.97  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 30.974 -26.154 14.429 1.00 19.15  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.109 -25.990 14.873 1.00 17.80  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.279 -25.569 12.036 1.00 16.83  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.047 -24.255 12.257 1.00 17.22  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.371 -26.024 10.572 1.00 16.69  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.878 -25.908 15.142 1.00 16.69  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 29.975 -25.354 16.496 1.00 17.63  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.710 -26.307 17.448 1.00 18.03  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.562 -25.850 18.233 1.00 16.60  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.595 -24.973 17.028 1.00 17.99  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.621 -24.069 18.284 1.00 21.41  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.182 -22.676 17.964 1.00 21.32  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.233 -23.947 18.876 1.00 24.65  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.425 -27.606 17.333 1.00 16.65  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.096 -28.629 18.130 1.00 17.54  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.609 -28.541 17.875 1.00 20.25  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.391 -28.530 18.840 1.00 19.81  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.560 -30.002 17.749 1.00 19.50  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.169 -31.190 18.481 1.00 27.38  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.842 -31.118 19.979 1.00 29.84  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.600 -32.497 17.919 1.00 31.96  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.017 -28.401 16.591 1.00 17.61  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.442 -28.283 16.266 1.00 16.43  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.055 -26.985 16.774 1.00 19.17  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.182 -26.990 17.254 1.00 18.64  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.666 -28.476 14.779 1.00 18.19  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.629 -29.946 14.400 1.00 28.08  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.862 -30.839 15.230 1.00 23.59  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.330 -30.230 13.144 1.00 22.78  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.310 -25.881 16.704 1.00 17.56  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.808 -24.609 17.244 1.00 17.18  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.024 -24.759 18.758 1.00 19.21  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.002 -24.218 19.292 1.00 18.99  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.834 -23.458 16.937 1.00 17.38  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.735 -23.120 15.438 1.00 19.07  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.607 -22.110 15.178 1.00 19.62  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.099 -22.656 14.842 1.00 21.67  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.114 -25.490 19.447 1.00 17.75  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.278 -25.701 20.899 1.00 18.41  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.508 -26.569 21.202 1.00 22.24  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.214 -26.311 22.179 1.00 22.58  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.027 -26.316 21.524 1.00 19.19  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.038 -26.179 23.037 1.00 26.63  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.557 -25.203 23.599 1.00 23.67  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.487 -27.163 23.709 1.00 27.06  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.787 -27.568 20.338 1.00 20.05  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 36.972 -28.425 20.462 1.00 20.61  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.231 -27.569 20.334 1.00 23.63  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.176 -27.755 21.099 1.00 22.97  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 36.961 -29.525 19.396 1.00 20.84  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 35.958 -30.619 19.723 1.00 23.12  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.767 -31.559 18.537 1.00 25.33  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 34.927 -32.697 18.905 1.00 33.10  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.257 -33.452 18.041 1.00 44.64  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.271 -33.162 16.743 1.00 32.87  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.550 -34.486 18.468 1.00 39.78  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.235 -26.604 19.386 1.00 20.11  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.366 -25.693 19.227 1.00 20.49  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.513 -24.844 20.486 1.00 23.82  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.637 -24.671 20.981 1.00 24.39  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.176 -24.770 18.023 1.00 20.12  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.192 -25.453 16.648 1.00 23.43  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.104 -24.409 15.542 1.00 23.17  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.442 -26.341 16.476 1.00 23.65  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.371 -24.349 21.032 1.00 20.03  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.422 -23.564 22.269 1.00 20.48  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.050 -24.380 23.433 1.00 25.57  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 39.944 -23.867 24.131 1.00 26.42  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.028 -23.066 22.667 1.00 20.74  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.142 -22.178 23.909 1.00 24.50  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.845 -21.547 24.302 1.00 29.18  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.830 -22.530 24.657 1.00 25.67  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.201 -22.581 25.828 1.00 35.06  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.543 -21.756 26.813 1.00 29.32  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.247 -23.473 26.032 1.00 27.28  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.577 -25.622 23.633 0.39 23.28  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.579 -25.630 23.619 0.28 23.08  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.576 -25.622 23.635 0.33 23.37  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.045 -26.525 24.692 0.39 24.31  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.031 -26.576 24.648 0.28 24.08  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.045 -26.532 24.687 0.33 24.49  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.556 -26.796 24.619 0.39 29.84  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.545 -26.791 24.609 0.28 29.60  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.559 -26.780 24.617 0.33 29.82  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.203 -26.923 25.661 0.39 30.88  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.178 -26.895 25.662 0.28 30.48  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.207 -26.885 25.661 0.33 30.74  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.255 -27.830 24.680 0.39 27.30  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.338 -27.923 24.469 0.28 27.21  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.289 -27.856 24.620 0.33 27.96  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.607 -28.677 23.598 0.39 32.45  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 36.965 -27.875 24.816 0.28 32.76  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.741 -28.766 25.610 0.33 36.34  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.116 -26.848 23.394 1.00 26.17  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.549 -27.087 23.171 1.00 27.63  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.340 -25.792 22.975 1.00 29.49  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.549 -25.838 22.710 1.00 30.43  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.722 -28.052 21.992 1.00 28.46  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 41.984 -29.375 22.187 1.00 34.65  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 41.971 -30.201 20.924 1.00 38.22  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.331 -30.579 20.539 1.00 48.38  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.712 -30.812 19.290 1.00 63.34  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 44.970 -31.133 19.022 1.00 53.12  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.845 -30.698 18.297 1.00 47.05  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.659 -24.639 23.129 1.00 23.64  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.210 -23.298 22.982 1.00 24.37  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.842 -23.078 21.587 1.00 28.77  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 44.909 -22.465 21.457 1.00 30.06  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.203 -22.986 24.130 1.00 27.43  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.520 -21.513 24.276 1.00 34.27  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.609 -20.686 24.060 1.00 34.20  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.672 -21.190 24.607 1.00 37.11  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.194 -23.614 20.556 1.00 23.30  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.689 -23.528 19.181 1.00 23.38  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.089 -22.323 18.465 1.00 25.94  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 41.858 -22.186 18.372 1.00 22.07  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.462 -24.844 18.393 1.00 26.35  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.250 -26.033 19.030 1.00 28.11  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.813 -24.662 16.887 1.00 25.30  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.771 -27.395 18.520 1.00 29.88  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 43.981 -21.438 17.973 1.00 25.09  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.622 -20.245 17.204 1.00 25.12  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.711 -19.253 17.953 1.00 25.10  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.142 -18.356 17.334 1.00 22.52  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.057 -20.587 15.826 1.00 25.73  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.113 -21.114 14.804 1.00 33.10  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.507 -21.211 13.457 1.00 33.86  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.319 -20.213 14.715 1.00 40.17  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.690 -19.334 19.285 1.00 22.21  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.032 -18.321 20.117 1.00 21.13  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.850 -17.030 19.911 1.00 26.60  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.081 -17.084 19.748 1.00 26.39  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 41.984 -18.759 21.575 1.00 26.37  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.310 -19.105 21.973 1.00 29.83  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.010 -19.950 21.796 1.00 25.06  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.170 -15.898 19.798 1.00 23.43  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.826 -14.643 19.443 1.00 23.34  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.493 -13.491 20.344 1.00 25.51  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.835 -12.351 20.032 1.00 25.46  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.499 -14.297 17.977 1.00 23.95  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.012 -14.318 17.633 1.00 31.01  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.178 -14.384 18.567 1.00 26.20  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.688 -14.286 16.441 1.00 36.29  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.821 -13.765 21.465 1.00 20.64  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.509 -12.709 22.431 1.00 20.47  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.344 -13.319 23.815 1.00 24.80  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 40.950 -14.496 23.947 1.00 24.41  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.230 -11.896 21.993 1.00 23.15  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 38.943 -12.721 22.138 1.00 21.41  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.099 -10.553 22.737 1.00 23.49  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.634 -12.509 24.842 0.60 22.48  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.628 -12.525 24.848 0.40 21.48  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.415 -12.825 26.249 0.60 22.40  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.363 -12.904 26.227 0.40 20.95  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.339 -11.838 26.719 0.60 24.74  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.397 -11.866 26.814 0.40 24.48  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.466 -10.630 26.480 0.60 24.80  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.620 -10.657 26.684 0.40 24.84  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.707 -12.684 27.112 0.60 27.81  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.611 -13.219 27.099 0.40 25.46  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.443 -13.020 28.582 0.60 28.15  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.498 -11.996 27.307 0.40 25.82  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.833 -13.547 26.570 0.60 28.22  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.216 -13.837 28.439 0.40 25.44  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.289 -12.350 27.374 1.00 20.30  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.234 -11.534 27.974 1.00 20.98  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.514 -11.557 29.457 1.00 25.84  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.527 -12.641 30.066 1.00 25.28  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.802 -12.064 27.654 1.00 22.35  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.577 -12.237 26.125 1.00 21.91  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.731 -11.156 28.286 1.00 23.76  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.823 -10.952 25.237 1.00 21.70  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.755 -10.373 30.031 1.00 22.48  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.068 -10.252 31.454 1.00 22.89  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.817 -9.834  32.199 1.00 27.80  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.222 -8.798  31.888 1.00 26.67  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.268 -9.297  31.713 1.00 27.39  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.578 -9.191  33.211 1.00 27.89  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.514 -9.764  30.953 1.00 28.26  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.431 -10.637 33.201 1.00 25.21  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.240 -10.403 34.006 1.00 25.05  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.746 -10.419 35.431 1.00 32.10  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 36.897 -11.491 36.023 1.00 28.79  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.134 -11.460 33.727 1.00 28.08  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.806 -11.028 34.340 1.00 28.47  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 34.974 -11.700 32.222 1.00 26.78  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.143 -9.235  35.938 0.54 32.84  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.004 -9.209  35.964 0.46 31.99  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.742 -9.055  37.267 0.54 34.19  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.541 -8.948  37.297 0.46 33.05  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.075 -9.842  37.352 0.54 35.65  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.621 -9.967  37.669 0.46 35.52  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 39.973 -9.576  36.554 0.54 35.05  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.417 -10.856 38.502 0.46 35.37  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.761 -9.448  38.375 0.54 39.83  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.427 -8.832  38.329 0.46 37.23  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.531 -8.748  38.270 0.54 54.67  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.757 -7.594  38.156 0.46 44.08  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.183 -10.825 38.275 0.54 31.69  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.732 -9.878  36.924 0.46 30.38  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.384 -11.644 38.478 0.54 31.36  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 40.966 -10.664 36.989 0.46 30.61  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.486 -12.833 37.514 0.54 32.68  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.823 -12.086 36.411 0.46 32.61  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.519 -13.511 37.499 0.54 32.08  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.839 -12.619 35.961 0.46 33.16  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.483 -12.125 39.941 0.54 31.85  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.611 -10.671 38.389 0.46 31.59  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 40.960 -11.059 40.916 0.54 38.35  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.165 -9.298  38.771 0.46 42.77  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.268 -11.669 42.268 0.54 40.50  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.146 -9.351  39.923 0.46 50.39  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.498 -10.657 43.297 0.54 41.73  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.582 -8.012  40.328 0.46 57.20  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.686 -10.157 43.623 0.54 56.87  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 42.976 -7.269  41.251 0.46 68.48  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.789 -9.249  44.582 0.54 46.12  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 41.893 -7.720  41.871 0.46 52.95  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.781 -10.555 42.985 0.54 44.31  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.445 -6.066  41.554 0.46 55.51  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.421 -13.095 36.721 0.54 26.83  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.588 -12.670 36.346 0.46 28.27  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.400 -14.222 35.788 0.54 25.91  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.349 -13.994 35.735 0.46 27.54  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.681 -13.802 34.350 0.54 29.39  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.491 -13.840 34.218 0.46 30.17  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.368 -12.679 33.952 0.54 27.59  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 38.921 -12.912 33.645 0.46 28.29  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.063 -14.987 35.878 0.54 26.71  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 37.957 -14.549 36.100 0.46 28.64  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.783 -15.568 37.258 0.54 40.89  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.865 -15.085 37.520 0.46 40.37  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.140 -17.033 37.413 0.54 77.25  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.130 -16.572 37.638 0.46 74.41  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.400 -17.887 36.872 0.54 77.71  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.214 -16.942 38.144 0.46 76.45  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.159 -17.327 38.079 0.54 77.83  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.256 -17.368 37.223 0.46 74.29  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.260 -14.732 33.570 1.00 26.39  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.584 -14.597 32.155 1.00 25.57  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 39.958 -15.727 31.366 1.00 27.50  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.026 -16.877 31.802 1.00 27.18  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.109 -14.623 31.979 1.00 28.20  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.806 -13.377 32.519 1.00 44.83  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.276 -13.304 32.182 1.00 62.11  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.841 -14.147 31.469 1.00 55.43  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 44.931 -12.280 32.697 1.00 63.82  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.375 -15.409 30.192 1.00 21.79  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.717 -16.405 29.331 1.00 22.08  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.229 -16.224 27.929 1.00 26.13  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.073 -15.137 27.363 1.00 26.83  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.191 -16.201 29.342 1.00 22.63  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.574 -16.335 30.713 1.00 24.27  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.465 -15.232 31.559 1.00 26.65  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.094 -17.561 31.158 1.00 26.97  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 35.909 -15.360 32.832 1.00 28.28  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.533 -17.687 32.433 1.00 30.13  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.445 -16.586 33.261 1.00 28.39  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.863 -17.261 27.374 1.00 23.07  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.371 -17.208 26.006 1.00 21.54  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.233 -17.596 25.045 1.00 24.41  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.440 -18.504 25.339 1.00 23.39  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.585 -18.142 25.835 1.00 23.01  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.813 -17.674 26.671 1.00 29.53  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.134 -18.152 26.072 1.00 35.74  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.202 -17.830 24.642 1.00 47.83  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.694 -16.705 24.131 1.00 60.24  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.266 -15.805 24.917 1.00 52.69  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.661 -16.495 22.823 1.00 43.30  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.154 -16.934 23.886 1.00 21.35  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.075 -17.244 22.925 1.00 20.78  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.473 -16.836 21.525 1.00 22.76  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.577 -16.327 21.316 1.00 21.63  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.781 -16.524 23.326 1.00 21.42  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.569 -17.090 20.568 1.00 19.60  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.719 -16.688 19.181 1.00 18.26  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.822 -15.456 18.994 1.00 20.19  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.605 -15.523 19.279 1.00 19.49  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.246 -17.809 18.240 1.00 17.95  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.012 -19.081 18.423 1.00 20.48  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.540 -20.102 19.250 1.00 21.63  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.247 -19.418 17.969 1.00 21.89  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.472 -21.045 19.216 1.00 21.56  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.525 -20.669 18.472 1.00 21.39  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.413 -14.342 18.549 1.00 20.41  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.665 -13.092 18.295 1.00 19.56  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.427 -13.371 17.426 1.00 21.34  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.344 -12.886 17.746 1.00 18.80  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.552 -12.052 17.575 1.00 21.70  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.569 -11.420 18.517 1.00 23.73  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.528 -10.561 17.712 1.00 22.47  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.591 -10.018 18.620 1.00 26.80  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.583 -9.265  17.832 1.00 26.50  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.577 -14.160 16.354 1.00 19.05  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.445 -14.401 15.454 1.00 18.87  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.268 -15.067 16.148 1.00 19.35  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.128 -14.696 15.873 1.00 19.60  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.871 -15.139 14.195 1.00 24.74  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.530 -16.336 14.588 1.00 25.69  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.730 -14.252 13.271 1.00 25.87  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.524 -16.030 17.040 1.00 16.21  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.446 -16.725 17.759 1.00 16.30  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.776 -15.745 18.719 1.00 18.41  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.538 -15.706 18.801 1.00 16.92  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 32.962 -17.985 18.491 1.00 17.53  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.831 -18.612 19.337 1.00 17.95  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.480 -19.011 17.462 1.00 17.68  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.584 -14.952 19.446 1.00 17.41  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.012 -13.951 20.347 1.00 17.07  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.102 -12.968 19.594 1.00 19.87  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 29.986 -12.698 20.051 1.00 19.76  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.120 -13.165 21.081 1.00 16.66  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.115 -13.957 21.965 1.00 19.50  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.153 -13.000 22.594 1.00 19.89  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.376 -14.751 23.060 1.00 21.29  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.551 -12.478 18.423 1.00 17.02  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.757 -11.554 17.607 1.00 17.92  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.464 -12.204 17.123 1.00 21.87  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.401 -11.573 17.156 1.00 21.29  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.560 -11.095 16.392 1.00 19.72  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.784 -10.287 16.773 1.00 21.03  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.865 -10.224 15.334 1.00 24.74  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.120 -8.883  14.491 1.00 22.18  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.548 -13.488 16.716 1.00 18.58  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.396 -14.235 16.201 1.00 18.14  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.316 -14.438 17.296 1.00 20.86  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.161 -14.675 16.961 1.00 21.07  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.853 -15.599 15.642 1.00 18.17  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.704 -14.358 18.592 1.00 17.27  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.788 -14.619 19.703 1.00 17.74  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.317 -13.408 20.495 1.00 21.21  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.372 -13.550 21.274 1.00 19.48  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.441 -15.615 20.656 1.00 17.19  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.803 -17.220 19.917 1.00 19.47  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.044 -12.288 20.407 1.00 18.64  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.851 -11.146 21.300 1.00 18.35  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.866 -9.838  20.551 1.00 22.18  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.841 -9.544  19.841 1.00 20.03  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 27.988 -11.185 22.319 1.00 20.05  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.299 -9.951  22.938 1.00 22.04  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.818 -9.028  20.752 1.00 20.41  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.754 -7.691  20.160 1.00 20.12  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.881 -6.808  20.663 1.00 22.88  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.455 -6.027  19.891 1.00 21.74  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.272 -6.988  21.946 1.00 20.62  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.395 -6.211  22.498 1.00 20.68  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.734 -6.558  21.800 1.00 23.33  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.428 -5.641  21.347 1.00 21.66  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.498 -6.395  24.028 1.00 20.38  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.564 -5.508  24.700 1.00 26.10  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.149 -4.022  24.689 1.00 27.37  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.840 -5.980  26.108 1.00 24.10  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.072 -7.860  21.681 1.00 19.60  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.321 -8.268  21.010 1.00 18.46  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.298 -7.913  19.545 1.00 22.10  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.328 -7.517  19.011 1.00 20.91  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.669 -9.744  21.250 1.00 19.36  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.094 -9.967  22.685 1.00 19.98  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.137 -9.228  23.247 1.00 21.39  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.463 -10.925 23.473 1.00 20.65  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.495 -9.394  24.600 1.00 21.80  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.865 -11.141 24.799 1.00 22.57  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 32.876 -10.378 25.354 1.00 20.50  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.114 -7.982  18.901 1.00 19.49  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 29.998 -7.587  17.479 1.00 20.50  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.416 -6.121  17.316 1.00 24.33  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.215 -5.808  16.429 1.00 22.11  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.556 -7.820  17.003 1.00 22.44  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.279 -7.303  15.615 1.00 25.60  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 28.941 -7.828  14.508 1.00 26.42  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.352 -6.289  15.405 1.00 29.83  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.684 -7.350  13.219 1.00 27.54  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.084 -5.809  14.128 1.00 32.93  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.743 -6.351  13.040 1.00 38.20  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.446 -5.876  11.796 1.00 43.76  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.875 -5.235  18.173 0.53 22.45  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.876 -5.236  18.178 0.47 22.28  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.193 -3.807  18.173 0.53 23.04  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.195 -3.808  18.186 0.47 22.84  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.689 -3.572  18.479 0.53 27.89  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.697 -3.597  18.458 0.47 27.63  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.334 -2.794  17.779 0.53 29.43  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.346 -2.851  17.728 0.47 28.93  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.299 -3.072  19.167 0.53 25.30  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.359 -3.086  19.239 0.47 25.10  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 27.964 -3.041  18.690 0.53 28.40  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.710 -1.713  19.298 0.47 29.05  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.241 -4.275  19.490 1.00 24.06  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.658 -4.147  19.886 1.00 23.34  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.606 -4.528  18.751 1.00 26.17  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.477 -3.731  18.382 1.00 27.69  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 33.993 -4.978  21.185 1.00 25.29  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.236 -4.433  22.418 1.00 24.95  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.528 -4.998  21.447 1.00 24.33  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.309 -5.376  23.635 1.00 27.51  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.435 -5.728  18.188 1.00 21.98  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.417 -6.170  17.215 1.00 21.70  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.204 -5.626  15.805 1.00 25.81  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.052 -5.886  14.945 1.00 26.75  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.579 -7.698  17.238 1.00 21.83  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 35.988 -8.193  18.618 1.00 22.47  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.197 -7.803  19.189 1.00 25.74  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.163 -9.047  19.339 1.00 22.79  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.565 -8.251  20.471 1.00 26.34  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.542 -9.516  20.606 1.00 25.51  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.739 -9.115  21.164 1.00 24.41  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.128 -4.849  15.562 1.00 23.91  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 33.969 -4.158  14.262 1.00 24.04  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.504 -2.736  14.391 1.00 30.50  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.585 -2.008  13.394 1.00 29.62  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.538 -4.186  13.703 1.00 31.13  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.627 -3.673  14.675 1.00 28.05  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.112 -5.574  13.209 1.00 26.89  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 34.904 -2.338  15.620 1.00 26.86  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.506 -1.021  15.820 1.00 28.42  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 36.921 -1.063  15.244 1.00 34.09  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.677 -1.973  15.577 1.00 31.51  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.525 -0.646  17.309 1.00 29.37  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.236 0.668   17.528 1.00 38.34  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.597 1.717   17.348 1.00 43.00  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.452 0.643   17.804 1.00 36.75  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.283 -0.063  14.408 1.00 35.48  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.573 0.017   13.718 1.00 36.78  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.792 -0.010  14.649 1.00 39.75  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 40.868 -0.401  14.193 1.00 41.75  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.628 1.225   12.767 1.00 40.42  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.825 1.017   11.484 1.00 56.82  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.643 0.405   15.929 1.00 32.27  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.736 0.315   16.896 1.00 31.70  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.638 -0.947  17.738 1.00 35.25  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.645 -1.618  17.946 1.00 36.75  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.774 1.531   17.852 1.00 32.67  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.390 2.805   17.304 1.00 39.04  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.353 3.908   18.346 1.00 40.08  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 42.832 2.595   16.821 1.00 43.75  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.447 -1.241  18.292 1.00 28.79  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.286 -2.367  19.207 1.00 27.08  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.419 -3.727  18.525 1.00 32.29  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.800 -4.684  19.190 1.00 32.01  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 37.979 -2.278  20.016 1.00 26.88  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 37.887 -1.027  20.903 1.00 27.50  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.608 -1.086  21.735 1.00 26.54  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.286 0.239   22.405 1.00 31.19  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.768 1.259   21.466 1.00 33.22  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.174 -3.796  17.202 1.00 31.09  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.304 -5.043  16.424 1.00 30.78  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.695 -5.671  16.583 1.00 35.86  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 40.827 -6.888  16.424 1.00 36.05  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 38.966 -4.815  14.951 1.00 32.36  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.106 -3.699  14.080 1.00 38.27  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.725 -4.830  16.862 1.00 31.90  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.125 -5.232  16.980 1.00 32.63  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.600 -5.511  18.405 1.00 36.11  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.765 -5.881  18.606 1.00 34.89  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.031 -4.198  16.284 1.00 34.51  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 43.771 -4.145  14.784 1.00 46.21  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.694 -3.071  14.185 1.00 46.83  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.567 -5.301  14.150 1.00 38.18  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.712 -5.346  19.400 1.00 32.84  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.093 -5.607  20.779 1.00 31.29  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.099 -7.103  21.044 1.00 33.61  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.227 -7.821  20.532 1.00 32.26  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.138 -4.906  21.762 1.00 31.26  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.112 -3.373  21.688 1.00 35.58  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.011 -2.820  22.582 1.00 35.35  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.473 -2.770  22.071 1.00 37.31  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.076 -7.577  21.834 0.51 30.88  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.080 -7.567  21.837 0.49 30.61  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.176 -8.997  22.195 0.51 30.48  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.225 -8.976  22.219 0.49 30.14  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.575 -9.235  23.590 0.51 31.34  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.597 -9.228  23.596 0.49 31.22  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.405 -10.384 24.002 0.51 29.27  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.429 -10.379 23.999 0.49 29.16  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.628 -9.465  22.143 0.51 35.60  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.699 -9.370  22.236 0.49 34.69  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.434 -8.737  23.052 0.51 44.11  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.229 -9.380  20.921 0.49 40.41  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.284 -8.139  24.325 1.00 28.23  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.689 -8.178  25.666 1.00 28.05  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.507 -7.205  25.706 1.00 29.07  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.645 -6.032  25.310 1.00 28.11  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.720 -7.839  26.793 1.00 33.05  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.066 -7.860  28.180 1.00 33.11  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 44.939 -8.767  26.758 1.00 33.50  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.368 -7.688  26.216 1.00 22.45  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.158 -6.889  26.419 1.00 22.72  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.763 -7.010  27.884 1.00 26.12  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.526 -8.126  28.366 1.00 26.43  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 37.992 -7.265  25.458 1.00 24.24  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.380 -7.083  23.943 1.00 25.36  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.685 -6.527  25.822 1.00 25.60  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.764 -5.634  23.472 1.00 28.07  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.651 -5.864  28.578 1.00 23.91  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.263 -5.831  29.979 1.00 23.90  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.787 -5.509  30.096 1.00 26.00  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.357 -4.440  29.652 1.00 24.89  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.079 -4.788  30.764 1.00 28.54  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.556 -4.981  30.683 1.00 45.93  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.090 -6.019  31.061 1.00 36.31  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.252 -3.966  30.214 1.00 41.65  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.011 -6.418  30.695 1.00 22.15  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.588 -6.174  30.890 1.00 21.51  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.351 -5.270  32.091 1.00 25.74  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.225 -5.123  32.960 1.00 25.63  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.771 -7.478  31.047 1.00 20.66  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.837 -8.518  29.897 1.00 23.37  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.698 -9.553  30.044 1.00 24.07  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.797 -7.858  28.504 1.00 21.94  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.150 -4.696  32.159 1.00 23.22  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.727 -3.827  33.264 1.00 23.81  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 32.945 -4.578  34.598 1.00 27.59  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.636 -5.772  34.667 1.00 26.63  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.252 -3.453  33.073 1.00 24.94  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.710 -2.432  34.058 1.00 32.82  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.589 -2.767  35.255 1.00 33.47  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.367 -1.322  33.626 1.00 31.98  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.502 -3.925  35.639 1.00 28.35  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.756 -4.648  36.909 1.00 29.15  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.534 -5.238  37.592 1.00 32.00  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.699 -6.096  38.455 1.00 32.66  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.449 -3.612  37.803 1.00 32.13  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.181 -2.290  37.176 1.00 36.87  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 33.966 -2.520  35.711 1.00 30.88  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.321 -4.806  37.220 1.00 29.00  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.081 -5.331  37.801 1.00 30.46  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.787 -6.745  37.251 1.00 30.17  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 28.972 -7.463  37.819 1.00 29.75  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.896 -4.394  37.477 1.00 33.11  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.756 -4.438  38.477 1.00 52.83  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 27.976 -3.567  39.700 1.00 78.97  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.039 -2.326  39.544 1.00 79.51  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.087 -4.127  40.815 1.00 71.44  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.429 -7.132  36.144 1.00 25.31  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.175 -8.434  35.531 1.00 24.41  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.752 -9.561  36.353 1.00 27.93  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 31.922 -9.535  36.736 1.00 27.18  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.630 -8.466  34.055 1.00 26.50  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 29.939 -7.336  33.241 1.00 26.71  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.389 -9.845  33.435 1.00 24.56  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.353 -7.310  33.269 1.00 30.94  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 29.910 -10.538 36.613 1.00 27.98  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.215 -11.734 37.385 1.00 28.94  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 30.981 -12.765 36.534 1.00 28.73  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.476 -13.163 35.486 1.00 26.62  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 28.911 -12.323 37.928 1.00 30.04  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.119 -13.583 38.712 1.00 42.93  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.825 -14.670 38.231 1.00 33.07  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.658 -13.461 39.924 1.00 35.56  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.195 -13.213 36.955 1.00 26.99  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 32.947 -14.195 36.145 1.00 25.98  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.201 -15.509 35.884 1.00 28.58  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.293 -16.044 34.775 1.00 27.10  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.221 -14.422 36.961 1.00 29.34  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.362 -13.176 37.801 1.00 34.30  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 32.960 -12.815 38.155 1.00 30.28  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.446 -16.018 36.884 1.00 25.63  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.690 -17.256 36.686 1.00 25.38  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.592 -17.070 35.613 1.00 27.18  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.468 -17.913 34.731 1.00 25.00  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.110 -17.791 38.003 1.00 27.87  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.486 -19.159 37.768 1.00 33.06  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.678 -19.777 38.893 1.00 54.39  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.691 -21.024 38.996 1.00 51.61  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.019 -19.034 39.653 1.00 46.68  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.851 -15.953 35.682 1.00 25.33  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.834 -15.618 34.689 1.00 24.64  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.438 -15.554 33.294 1.00 25.45  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.875 -16.093 32.320 1.00 22.75  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.621 -14.928 33.194 1.00 21.28  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.312 -14.860 31.900 1.00 19.81  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.701 -16.275 31.439 1.00 22.11  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.500 -16.619 30.271 1.00 20.82  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.561 -13.939 31.965 1.00 21.38  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.183 -13.826 30.591 1.00 21.35  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.601 -13.023 29.610 1.00 24.63  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.245 -14.648 30.221 1.00 22.50  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.105 -13.005 28.305 1.00 25.33  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.761 -14.615 28.921 1.00 24.00  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.173 -13.810 27.965 1.00 23.11  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.264 -17.083 32.341 1.00 22.65  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.667 -18.453 32.015 1.00 24.13  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.497 -19.282 31.437 1.00 24.89  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.654 -19.968 30.410 1.00 23.12  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.283 -19.133 33.233 1.00 27.15  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.000 -20.754 32.862 1.00 32.38  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.316 -19.198 32.102 1.00 22.38  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.102 -19.908 31.694 1.00 20.79  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.708 -19.454 30.293 1.00 21.73  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.383 -20.281 29.430 1.00 21.36  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 26.982 -19.659 32.736 1.00 23.78  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.292 -20.451 34.043 1.00 24.46  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.582 -19.986 32.158 1.00 23.73  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.544 -19.977 35.255 1.00 29.28  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.781 -18.148 30.058 1.00 18.66  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.426 -17.614 28.733 1.00 18.31  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.425 -17.970 27.664 1.00 21.62  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.016 -18.241 26.536 1.00 20.02  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.162 -16.115 28.801 1.00 18.93  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.866 -15.754 29.571 1.00 23.74  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.784 -14.282 29.762 1.00 23.81  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.586 -16.249 28.845 1.00 24.49  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.736 -17.965 27.990 1.00 19.16  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.766 -18.368 27.021 1.00 18.66  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.544 -19.842 26.619 1.00 21.73  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.581 -20.181 25.435 1.00 19.60  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.156 -18.146 27.628 1.00 18.83  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.330 -18.451 26.672 1.00 22.37  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.288 -17.549 25.423 1.00 22.08  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.682 -18.310 27.419 1.00 24.34  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.276 -20.709 27.603 1.00 19.41  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 29.957 -22.101 27.305 1.00 19.65  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.732 -22.190 26.384 1.00 21.29  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.742 -22.980 25.449 1.00 21.40  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.674 -22.845 28.605 1.00 22.23  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.913 -23.174 29.415 1.00 33.52  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.031 -23.090 28.856 1.00 33.94  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.764 -23.526 30.605 1.00 32.07  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.671 -21.413 26.670 1.00 19.78  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.475 -21.372 25.816 1.00 17.58  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.849 -20.982 24.381 1.00 18.04  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.369 -21.603 23.419 1.00 17.51  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.425 -20.398 26.378 1.00 18.21  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.312 -20.121 25.392 1.00 18.38  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.355 -21.088 25.110 1.00 21.00  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.294 -18.937 24.653 1.00 21.16  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.365 -20.857 24.153 1.00 20.32  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.296 -18.708 23.688 1.00 23.61  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.342 -19.671 23.449 1.00 21.54  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.659 -19.926 24.224 1.00 16.06  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.058 -19.502 22.864 1.00 15.36  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.610 -20.647 22.042 1.00 19.53  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.288 -20.764 20.861 1.00 18.94  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.156 -18.437 22.963 1.00 15.83  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.650 -17.139 23.558 1.00 17.35  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 29.982 -15.891 23.481 1.00 20.96  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.306 -14.648 24.662 1.00 21.79  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.480 -21.462 22.659 1.00 16.37  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.160 -22.556 21.955 1.00 16.32  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.422 -23.872 21.932 1.00 20.31  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.907 -24.832 21.323 1.00 19.51  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.547 -22.781 22.571 1.00 17.84  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.586 -21.790 22.088 1.00 18.87  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.731 -20.545 22.702 1.00 20.37  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.447 -22.108 21.032 1.00 19.75  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.700 -19.631 22.268 1.00 20.32  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.460 -21.228 20.632 1.00 20.26  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.551 -19.976 21.222 1.00 22.74  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.577 -19.156 20.837 1.00 20.30  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.281 -23.958 22.631 1.00 17.05  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.582 -25.250 22.710 1.00 17.67  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.070 -25.252 22.477 1.00 20.13  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.516 -26.342 22.266 1.00 19.12  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.777 -25.916 24.103 1.00 20.90  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.098 -25.155 25.107 1.00 20.72  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.240 -26.160 24.479 1.00 20.21  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.409 -24.076 22.555 0.67 16.99  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.413 -24.076 22.586 0.33 16.87  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 23.936 -23.876 22.510 0.67 16.90  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 23.954 -23.862 22.525 0.33 16.91  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.285 -24.276 23.849 0.67 19.58  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.266 -24.360 23.817 0.33 20.89  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.090 -24.070 24.015 0.67 18.84  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.040 -24.350 23.899 0.33 21.04  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.262 -24.670 21.385 0.67 17.80  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.328 -24.499 21.280 0.33 18.82  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.883 -24.501 20.126 0.67 15.43  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.018 -25.872 21.461 0.33 21.44  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.076 -24.795 24.815 0.67 18.15  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.069 -24.757 24.831 0.33 18.36  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.546 -25.239 26.109 0.67 18.32  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.591 -25.282 26.115 0.33 18.76  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.777 -24.198 27.175 0.67 22.29  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.799 -24.246 27.211 0.33 22.69  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.902 -23.719 27.355 0.67 19.99  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.927 -23.790 27.424 0.33 21.30  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.167 -26.576 26.545 0.67 20.94  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.313 -26.603 26.473 0.33 20.14  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.898 -27.738 25.579 0.67 27.25  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.201 -27.702 25.404 0.33 26.85  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.879 -28.882 25.829 0.67 33.99  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.034 -28.633 25.658 0.33 30.83  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.777 -29.394 27.199 0.67 42.97  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.896 -29.663 24.622 0.33 34.38  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 23.954 -30.368 27.570 0.67 53.90  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.194 -30.948 24.792 0.33 46.51  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.165 -30.955 26.678 0.67 43.04  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.020 -31.813 23.802 0.33 35.47  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 23.915 -30.767 28.832 0.67 40.07  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.650 -31.382 25.959 0.33 30.59  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.711 -23.870 27.898 1.00 19.91  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.759 -22.864 28.957 1.00 19.71  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.541 -23.496 30.308 1.00 24.87  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.475 -24.084 30.547 1.00 23.74  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.698 -21.789 28.678 1.00 20.58  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.726 -20.574 29.625 1.00 23.66  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 22.992 -19.735 29.387 1.00 21.90  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.463 -19.724 29.467 1.00 26.71  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.536 -23.366 31.207 1.00 23.59  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.422 -23.926 32.565 1.00 25.00  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.710 -22.915 33.490 1.00 29.49  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.347 -22.224 34.285 1.00 29.03  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.804 -24.343 33.100 1.00 29.93  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.761 -24.977 34.482 1.00 45.43  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.750 -25.531 34.906 1.00 37.36  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.858 -24.896 35.218 1.00 38.94  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.394 -22.798 33.322 1.00 27.18  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.562 -21.864 34.073 1.00 28.57  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.046 -22.525 35.342 1.00 32.25  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.397 -23.578 35.287 1.00 31.29  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.435 -21.369 33.157 1.00 29.70  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.720 -20.085 33.513 1.00 36.05  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.723 -18.894 33.623 1.00 36.47  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.623 -19.804 32.482 1.00 35.77  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.422 -21.949 36.501 1.00 29.41  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.070 -22.473 37.826 1.00 31.31  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.535 -21.359 38.711 1.00 32.96  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.859 -20.186 38.490 1.00 30.53  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.298 -23.129 38.497 1.00 33.89  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.917 -24.288 37.707 1.00 39.29  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.151 -24.885 38.374 1.00 56.95  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.863 -25.475 39.687 1.00 74.14  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.472 -26.733 39.886 1.00 94.71  ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.226 -27.170 41.115 1.00 81.93  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.308 -27.558 38.857 1.00 84.92  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.708 -21.703 39.711 1.00 30.87  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.171 -20.684 40.623 1.00 31.16  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.282 -19.777 41.194 1.00 35.07  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.102 -18.560 41.267 1.00 35.16  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.389 -21.355 41.773 1.00 34.25  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.720 -20.377 42.721 1.00 44.11  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.002 -21.018 43.895 1.00 72.62  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.580 -21.924 44.541 1.00 62.62  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.854 -20.604 44.173 1.00 72.87  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.414 -20.377 41.557 1.00 33.33  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.547 -19.666 42.148 1.00 34.23  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.343 -18.775 41.212 1.00 35.61  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.081 -17.898 41.670 1.00 35.29  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.202 -18.970 39.893 1.00 31.08  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 22.976 -18.160 38.951 1.00 28.80  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.128 -17.306 37.997 1.00 31.59  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.697 -16.503 37.250 1.00 30.29  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 23.945 -19.072 38.172 1.00 28.22  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.286 -20.006 37.174 1.00 36.53  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.232 -19.708 36.616 1.00 26.55  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 23.918 -21.139 36.891 1.00 28.87  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.787 -17.511 37.969 1.00 28.71  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.913 -16.846 36.985 1.00 28.50  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.026 -15.319 36.978 1.00 29.32  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.026 -14.720 35.890 1.00 27.34  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.433 -17.292 37.049 1.00 32.73  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.625 -16.710 35.850 1.00 32.84  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.783 -17.007 38.410 1.00 33.00  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.443 -17.537 35.412 1.00 35.29  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.126 -14.688 38.158 1.00 27.61  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.252 -13.233 38.192 1.00 27.99  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.555 -12.753 37.548 1.00 30.41  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.519 -11.815 36.745 1.00 28.61  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.079 -12.680 39.619 1.00 31.97  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.705 -12.988 40.221 1.00 38.55  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.288 -12.539 39.177 1.00 44.27  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.265 -10.756 39.396 1.00 42.91  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.698 -13.422 37.858 1.00 28.38  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.008 -13.060 37.281 1.00 27.96  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.025 -13.358 35.791 1.00 28.70  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.554 -12.564 35.016 1.00 26.69  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.132 -13.822 37.968 1.00 29.38  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.452 -14.501 35.385 1.00 23.71  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.402 -14.857 33.955 1.00 21.58  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.585 -13.828 33.167 1.00 24.88  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.063 -13.372 32.119 1.00 23.23  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.909 -16.318 33.753 1.00 24.66  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.604 -16.617 32.275 1.00 22.72  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.954 -17.293 34.277 1.00 25.14  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.382 -13.458 33.660 0.20 23.35  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.380 -13.452 33.661 0.80 23.60  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.524 -12.478 32.990 0.20 24.02  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.552 -12.474 32.948 0.80 24.54  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.227 -11.130 32.846 0.20 28.01  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.251 -11.119 32.836 0.80 27.41  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.219 -10.559 31.755 0.20 27.00  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.242 -10.517 31.761 0.80 25.54  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.189 -12.305 33.724 0.20 27.61  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.179 -12.305 33.598 0.80 28.02  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.222 -11.426 32.971 0.20 31.80  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.265 -11.386 32.798 0.80 31.89  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.714 -11.123 33.892 0.20 37.29  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.578 -11.361 33.442 0.80 36.40  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.150 -9.685  33.066 0.20 34.74  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.794 -10.397 35.020 0.80 34.73  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.841 -10.636 33.939 1.00 25.59  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.569 -9.352  33.948 1.00 26.31  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.744 -9.387  32.945 1.00 27.10  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 23.944 -8.424  32.178 1.00 25.65  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.070 -9.050  35.351 1.00 28.02  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.481 -10.522 32.905 1.00 22.81  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.592 -10.676 31.963 1.00 22.39  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.054 -10.711 30.517 1.00 24.57  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.635 -10.064 29.647 1.00 22.26  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.518 -11.865 32.334 1.00 26.59  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.813 -11.845 33.739 1.00 25.30  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.839 -11.855 31.543 1.00 26.02  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 23.945 -11.463 30.261 1.00 21.54  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.369 -11.547 28.908 1.00 20.23  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.836 -10.178 28.447 1.00 24.02  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 22.966 -9.836  27.272 1.00 23.15  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.274 -12.620 28.853 1.00 21.16  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.305 -9.352  29.379 1.00 22.39  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.851 -8.019  28.977 1.00 21.60  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.046 -7.142  28.537 1.00 24.47  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.009 -6.507  27.486 1.00 24.58  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.072 -7.357  30.134 1.00 24.33  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.710 -7.992  30.371 1.00 29.04  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 18.999 -7.425  31.941 1.00 36.39  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.722 -5.683  31.532 1.00 34.36  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.119 -7.169  29.320 1.00 22.67  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.356 -6.429  29.044 1.00 22.10  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 25.965 -6.903  27.703 1.00 24.73  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.359 -6.075  26.871 1.00 23.97  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.339 -6.709  30.176 1.00 22.89  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.747 -6.204  29.940 1.00 23.18  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.048 -4.844  30.028 1.00 26.14  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.795 -7.093  29.694 1.00 22.38  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.356 -4.378  29.840 1.00 24.18  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.104 -6.644  29.534 1.00 22.75  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.380 -5.285  29.615 1.00 24.81  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.680 -4.882  29.498 1.00 24.68  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.035 -8.230  27.503 1.00 21.54  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.599 -8.815  26.276 1.00 19.60  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.668 -8.701  25.073 1.00 22.46  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.085 -8.984  23.945 1.00 22.22  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.005 -10.287 26.508 1.00 18.39  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.148 -10.555 27.512 1.00 20.73  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.430 -12.084 27.621 1.00 20.97  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.445 -9.842  27.089 1.00 22.78  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.399 -8.325  25.305 1.00 20.13  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.395 -8.208  24.236 1.00 21.13  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.167 -9.570  23.558 1.00 24.42  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.441 -9.762  22.372 1.00 23.21  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.737 -7.092  23.232 1.00 22.41  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 23.941 -5.713  23.886 1.00 23.40  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.631 -4.742  22.956 1.00 32.85  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.531 -4.838  21.741 1.00 28.04  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.368 -3.798  23.510 1.00 32.49  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.696 -10.520 24.362 1.00 21.81  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.365 -11.894 23.953 1.00 21.44  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.864 -12.059 24.211 1.00 26.79  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.423 -12.539 25.267 1.00 24.17  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.229 -12.875 24.749 1.00 22.49  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.720 -12.712 24.447 1.00 23.05  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.757 -13.781 25.454 1.00 25.48  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.416 -15.426 24.640 1.00 22.45  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.079 -11.540 23.262 1.00 26.77  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.616 -11.404 23.365 1.00 27.92  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.857 -12.675 23.724 1.00 28.90  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 16.973 -12.603 24.570 1.00 28.26  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.018 -10.786 22.090 1.00 30.49  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.555 -9.392  21.809 1.00 43.23  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.189 -13.820 23.109 1.00 25.72  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.455 -15.061 23.405 1.00 27.16  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.692 -15.534 24.840 1.00 28.37  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.746 -15.988 25.501 1.00 29.05  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.774 -16.144 22.376 1.00 28.89  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.327 -15.783 20.996 1.00 33.61  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 15.994 -15.548 20.710 1.00 37.15  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.044 -15.678 19.853 1.00 35.23  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 15.946 -15.267 19.418 1.00 36.95  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.152 -15.342 18.858 1.00 36.14  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 18.942 -15.373 25.335 1.00 22.82  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.286 -15.727 26.717 1.00 22.64  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.511 -14.823 27.682 1.00 28.30  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.916 -15.317 28.649 1.00 25.93  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.808 -15.735 27.012 1.00 25.30  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.062 -15.978 28.505 1.00 25.23  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.516 -16.792 26.169 1.00 24.76  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.501 -13.499 27.413 1.00 24.93  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.742 -12.551 28.253 1.00 25.28  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.258 -12.981 28.327 1.00 30.73  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.714 -13.071 29.419 1.00 29.68  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.911 -11.074 27.795 1.00 28.24  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.064 -10.130 28.664 1.00 28.96  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.379 -10.655 27.836 1.00 26.98  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.665 -13.332 27.173 0.61 29.18  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.626 -13.218 27.160 0.39 28.88  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.283 -13.795 27.055 0.61 29.91  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.223 -13.625 27.024 0.39 29.80  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 13.974 -15.022 27.934 0.61 32.73  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.856 -14.832 27.893 0.39 33.65  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 12.999 -14.972 28.688 0.61 33.07  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.845 -14.786 28.594 0.39 34.32  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.930 -14.064 25.581 0.61 31.86  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.889 -13.917 25.546 0.39 31.64  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.478 -14.441 25.354 0.61 44.01  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.657 -12.702 24.665 0.39 42.32  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.594 -13.628 25.694 0.61 46.94  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.261 -11.644 25.199 0.39 44.99  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.229 -15.544 24.827 0.61 48.95  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.847 -12.817 23.435 0.39 48.25  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.797 -16.105 27.864 0.61 28.04  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.685 -15.894 27.863 0.39 29.16  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.532 -17.300 28.696 0.61 28.06  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.439 -17.124 28.627 0.39 29.38  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.737 -17.010 30.185 0.61 30.78  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.648 -16.899 30.131 0.39 31.86  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 14.058 -17.613 31.013 0.61 30.81  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.869 -17.427 30.924 0.39 32.25  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.285 -18.561 28.233 0.61 28.00  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.233 -18.300 28.054 0.39 35.07  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.682 -19.696 28.874 0.61 27.44  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.219 -18.212 26.628 0.39 34.55  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.787 -18.529 28.554 0.61 22.54  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.647 -19.638 28.462 0.39 34.74  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.672 -16.103 30.521 1.00 27.56  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.923 -15.736 31.934 1.00 27.96  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.700 -15.032 32.492 1.00 34.74  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.242 -15.387 33.590 1.00 33.13  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.162 -14.855 32.048 1.00 27.23  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.716 -15.749 31.851 1.00 29.57  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.148 -14.063 31.720 0.48 32.95  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.154 -14.051 31.737 0.52 33.33  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.946 -13.296 32.070 0.48 34.23  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 12.955 -13.305 32.130 0.52 34.75  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.760 -14.231 32.335 0.48 38.05  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.753 -14.237 32.348 0.52 38.23  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.048 -14.059 33.327 0.48 38.49  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 11.028 -14.074 33.331 0.52 38.61  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.584 -12.304 30.950 0.48 34.97  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.625 -12.216 31.101 0.52 36.34  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.531 -11.123 30.837 0.48 46.50  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.398 -10.922 31.324 0.52 50.53  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.934 -9.979  30.037 0.48 58.45  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.686 -9.728  30.707 0.52 62.27  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.947 -8.981  29.687 0.48 61.63  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.830 -9.694  29.249 0.52 67.56  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.293 -7.950  30.453 0.48 70.92  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.615 -8.848  28.590 0.52 77.22  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.701 -7.756  31.625 0.48 62.91  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.333 -7.945  29.249 0.52 61.94  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.233 -7.106  30.051 0.48 50.04  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.684 -8.893  27.267 0.52 61.82  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.579 -15.233 31.459 1.00 34.07  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.500 -16.227 31.545 1.00 35.40  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.667 -17.139 32.758 1.00 38.60  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.694  -17.354 33.486 1.00 38.67  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.381 -17.025 30.239 1.00 37.51  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.835  -16.175 29.098 1.00 55.81  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.739  -16.916 27.780 1.00 66.62  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.308  -15.976 26.679 1.00 79.70  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.448  -16.652 25.675 1.00 92.76  ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.905 -17.630 33.009 1.00 33.77  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.187 -18.490 34.168 1.00 34.12  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 11.995 -17.733 35.478 1.00 38.83  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.474 -18.306 36.439 1.00 37.70  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.588 -19.103 34.083 1.00 33.95  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.705 -20.378 33.267 1.00 35.15  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.113 -20.482 32.009 1.00 37.86  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.471 -21.447 33.724 1.00 37.77  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.241 -21.654 31.249 1.00 38.86  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.603 -22.615 32.959 1.00 39.46  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 13.992 -22.708 31.727 1.00 37.07  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.361 -16.436 35.503 1.00 34.74  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.154 -15.592 36.696 1.00 35.84  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.654 -15.355 36.948 1.00 43.08  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.198 -15.507 38.089 1.00 43.62  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 12.991 -14.286 36.622 1.00 38.08  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.487 -14.622 36.774 1.00 37.00  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.547 -13.255 37.702 1.00 40.70  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.438 -13.591 36.219 1.00 41.12  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.888  -15.034 35.876 1.00 41.37  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.444  -14.790 35.948 1.00 43.84  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.687  -16.019 36.474 1.00 47.94  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.721  -15.862 37.214 1.00 47.83  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.888  -14.349 34.587 1.00 47.32  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.155  -17.235 36.127 1.00 43.28  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.532  -18.479 36.595 1.00 44.71  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.688  -18.707 38.112 1.00 50.92  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.809  -19.303 38.721 1.00 51.88  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.095  -19.666 35.824 1.00 43.92  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.804  -18.260 38.709 1.00 49.08  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.090  -18.471 40.130 1.00 51.59  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.515  -17.400 41.075 1.00 59.73  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.530  -17.607 42.292 1.00 61.91  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.591 -18.632 40.354 1.00 55.07  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 10.989 -19.984 40.182 1.00 65.58  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 7.989  -16.279 40.532 1.00 56.33  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.423  -15.197 41.351 1.00 73.99  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 5.990  -15.482 41.826 1.00 114.09 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.570  -16.634 41.902 1.00 81.42  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.524  -13.833 40.638 1.00 74.53  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.504  -13.604 39.530 1.00 83.88  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.673  -12.354 38.685 1.00 102.47 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.812  -11.839 38.580 1.00 89.23  ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.659  -11.898 38.109 1.00 96.23  ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.179 -35.044 5.841  1.00 25.84  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.263 -33.905 6.327  1.00 26.64  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.384 -36.280 6.712  1.00 25.75  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.909 -35.277 4.559  0.66 23.96  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.926 -35.278 4.553  0.34 24.97  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.694 -34.222 3.574  0.66 23.04  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.653 -34.205 3.600  0.34 24.58  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.184 -34.071 3.281  0.66 27.46  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.145 -34.050 3.421  0.34 27.18  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.468 -35.077 3.187  0.66 27.99  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.396 -35.033 3.505  0.34 26.69  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.478 -34.550 2.281  0.66 21.86  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.344 -34.432 2.231  0.34 23.87  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 22.976 -34.540 2.469  0.66 22.06  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.747 -35.518 1.385  0.34 25.08  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.760 -35.576 2.890  0.66 24.57  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.141 -36.821 1.332  0.34 28.29  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.861 -33.428 2.258  0.66 21.77  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.664 -35.388 0.446  0.34 24.96  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.074 -35.169 2.978  0.66 23.54  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.349 -37.522 0.456  0.34 27.91  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.166 -33.861 2.584  0.66 24.61  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.434 -36.668 -0.104 0.34 29.12  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.672 -32.087 1.873  0.66 22.53  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.826 -34.325 0.062  0.34 25.81  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.285 -33.023 2.469  0.66 24.14  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.425 -36.908 -1.044 0.34 28.31  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.781 -31.266 1.743  0.66 23.32  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.826 -34.566 -0.868 0.34 27.38  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.067 -31.731 2.046  0.66 23.93  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.633 -35.844 -1.409 0.34 27.89  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.702 -32.824 3.149  1.00 22.53  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.273 -32.520 2.902  1.00 22.70  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.129 -31.466 1.793  1.00 24.88  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.114 -30.795 1.436  1.00 23.89  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.572 -32.016 4.207  1.00 26.37  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.610 -33.071 5.323  1.00 26.24  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.161 -30.676 4.694  1.00 25.84  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.889 -31.288 1.319  1.00 23.62  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.502 -30.207 0.429  1.00 22.67  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.131 -29.067 1.422  1.00 26.34  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.104 -29.183 2.108  1.00 26.30  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.289 -30.590 -0.469 1.00 24.19  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.599 -31.854 -1.369 1.00 22.21  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.849 -29.359 -1.319 1.00 26.12  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.922 -31.734 -2.315 1.00 26.53  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.936 -27.981 1.533  1.00 25.80  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.607 -26.920 2.509  1.00 26.03  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.366 -26.105 2.123  1.00 29.36  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.066 -25.961 0.937  1.00 27.92  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.872 -26.052 2.527  1.00 27.77  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.450 -26.230 1.126  1.00 31.88  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.201 -27.683 0.819  1.00 27.74  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.616 -25.633 3.123  1.00 28.60  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.443 -10.198 16.486 1.00 22.33  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.845 -8.934  16.519 1.00 21.99  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.826 -8.653  17.422 1.00 24.23  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.392 -9.667  18.272 1.00 24.74  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.222 -10.853 19.836 1.00 28.21  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.935 -10.946 18.209 1.00 24.04  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.201 -10.293 11.929 1.00 25.45  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.357 -10.619 13.266 1.00 24.59  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.324 -10.266 14.161 1.00 23.29  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.220 -11.805 19.212 1.00 26.41  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.396 -11.117 20.706 1.00 28.14  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.391 -9.637  19.251 1.00 26.13  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 24.962 -11.219 17.311 1.00 22.25  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.343 -10.592 15.479 1.00 21.03  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.226 -9.654  13.684 1.00 25.82  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.201 -9.411  12.386 1.00 27.71  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.747 -8.648  11.810 0.71 29.62  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 28.916 -11.515 13.849 0.87 23.84  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.105 -9.676  11.461 1.00 26.74  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.323 -15.386 22.684 1.00 34.10  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.512 -35.312 -1.288 0.66 37.85  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.184 -35.118 -0.702 0.66 39.43  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.560 -34.336 -0.237 0.66 36.07  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 17.981 -36.903 -0.728 0.66 37.09  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 35.517 -25.781 25.525 1.00 34.71  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 25.747 -3.522  26.485 1.00 30.85  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 38.293 -14.968 15.495 1.00 31.48  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 26.785 -32.006 16.153 1.00 37.24  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 41.014 -21.669 25.193 1.00 37.09  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 20.754 -5.894  26.202 1.00 35.81  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 22.729 -5.495  19.883 1.00 46.99  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 44.938 -11.330 18.740 1.00 58.88  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 10.886 -20.670 37.600 1.00 46.97  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 37.140 -12.381 40.293 1.00 56.17  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 37.807 2.319   19.867 1.00 32.69  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 16.383 -27.464 -3.225 1.00 42.14  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 21.614 -29.481 -5.231 1.00 33.15  ? 313 HOH   A O   1 
HETATM 1214 O  O   A HOH   F 6 .   ? 19.036 -22.910 4.373  0.67 43.73  ? 314 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 6 .   ? 15.433 -10.069 25.003 1.00 45.51  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 29.735 -32.204 9.505  1.00 43.69  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 20.305 -13.581 20.626 1.00 41.32  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 37.610 -20.463 27.000 1.00 31.47  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 43.534 -6.642  32.027 1.00 43.90  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 33.258 -20.791 29.571 1.00 39.79  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 19.889 -9.688  37.100 1.00 35.58  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 28.327 -9.012  39.941 1.00 42.71  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 21.441 -27.124 14.652 0.50 32.86  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 32.756 -24.508 32.153 1.00 52.59  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 36.746 -5.786  12.330 1.00 32.04  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 23.361 -5.884  32.915 1.00 33.05  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 28.767 -21.914 41.555 1.00 61.52  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 31.598 -0.979  15.905 1.00 39.01  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 22.628 -27.716 17.769 1.00 47.50  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 25.615 -2.996  20.070 1.00 51.03  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 22.928 -28.226 12.648 1.00 20.35  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 41.348 -12.794 14.268 1.00 73.05  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 30.256 1.377   33.929 1.00 61.60  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 27.307 -28.216 18.625 1.00 22.66  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 41.197 -1.494  11.725 1.00 54.06  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 23.202 -17.019 44.242 1.00 56.68  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 27.199 -10.230 35.895 1.00 34.22  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 17.880 -29.424 7.688  1.00 28.67  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 41.211 -16.945 15.196 1.00 30.81  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 21.529 -30.053 14.173 1.00 66.93  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 21.886 -25.007 18.337 1.00 20.43  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 26.951 -35.317 11.600 1.00 49.96  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 34.388 -23.899 29.978 1.00 69.22  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 37.845 -16.585 13.145 0.50 22.61  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 12.262 -18.065 25.902 1.00 52.61  ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 30.395 -0.702  37.060 1.00 40.91  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 28.250 -23.754 31.697 1.00 35.87  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 17.944 -34.500 8.301  1.00 30.73  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 24.881 -26.816 19.017 1.00 30.18  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 28.965 -31.111 7.190  1.00 31.38  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 23.956 -15.913 21.289 1.00 26.13  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 29.310 -27.437 20.623 1.00 20.89  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 20.881 -7.400  19.851 1.00 39.62  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 42.340 -10.514 15.478 1.00 44.45  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 12.782 -20.609 42.333 1.00 48.04  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 43.835 -4.384  25.775 1.00 39.93  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 10.767 -11.584 34.562 1.00 44.28  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 28.440 -24.323 34.360 1.00 48.26  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 26.090 -21.936 38.619 1.00 32.72  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 26.081 -22.681 29.965 1.00 24.50  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 45.771 -14.272 21.557 1.00 48.35  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 30.612 -28.924 22.619 1.00 35.91  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 46.749 -21.484 18.350 1.00 42.80  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 44.242 -12.780 41.349 1.00 45.53  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 28.814 -0.521  16.925 1.00 64.85  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 26.855 -16.678 38.658 1.00 44.68  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 20.175 -15.986 40.880 1.00 32.23  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 37.252 -6.460  34.386 1.00 37.20  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 34.061 -8.005  35.727 1.00 30.88  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 46.069 -15.730 27.616 1.00 57.73  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 47.091 -25.286 21.620 1.00 44.06  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 41.229 -7.795  46.430 1.00 51.03  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 17.921 -24.417 39.649 1.00 38.02  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 34.740 -18.954 13.872 0.50 17.17  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 14.280 -16.953 23.475 1.00 39.62  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 10.315 -11.699 39.903 1.00 58.90  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 27.035 -2.453  16.072 1.00 57.25  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 38.908 -18.883 33.475 1.00 41.23  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 24.026 -28.648 21.528 1.00 46.25  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 45.134 -12.616 23.574 1.00 42.58  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 27.573 -23.093 13.871 0.50 25.08  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 34.762 -29.213 26.031 1.00 57.68  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 11.693 -15.449 40.521 1.00 67.54  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 45.430 -10.878 30.250 1.00 53.76  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 44.526 -16.410 29.736 1.00 47.96  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 29.619 -22.677 36.844 1.00 58.05  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 19.825 -25.601 41.185 1.00 71.00  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 26.012 -19.223 41.703 1.00 53.71  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 46.223 -19.012 19.692 1.00 45.79  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 26.111 -8.120  9.032  1.00 38.05  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 41.219 -7.039  35.931 1.00 38.76  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 17.333 -24.505 -2.087 1.00 60.37  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 31.815 -31.891 14.483 1.00 32.62  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 43.784 -10.634 35.129 1.00 66.82  ? 394 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 6 .   ? 36.829 -2.191  11.557 1.00 52.66  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 47.234 -6.705  20.393 1.00 63.91  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 23.593 -15.683 17.899 1.00 38.48  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 16.795 -6.522  27.654 1.00 59.30  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 41.927 -6.089  11.866 1.00 59.44  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 40.346 -19.629 29.023 1.00 32.15  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 45.677 -17.052 17.294 1.00 60.49  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 33.080 -29.809 21.462 1.00 40.06  ? 402 HOH   A O   1 
HETATM 1303 O  O   A HOH   F 6 .   ? 12.143 -20.823 27.899 0.66 41.20  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 27.192 -25.382 28.441 1.00 53.34  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 30.365 -10.671 40.585 1.00 36.48  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 35.185 1.828   13.535 1.00 49.39  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 44.507 -8.775  17.950 1.00 57.97  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 4.283  -20.551 37.789 1.00 56.59  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 35.099 -29.688 23.385 1.00 41.56  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 25.593 -4.675  17.959 1.00 45.96  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 41.232 -17.042 35.172 1.00 40.66  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 46.052 -8.952  44.063 1.00 45.03  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 26.555 -30.816 18.987 1.00 57.98  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 46.922 -20.298 21.951 1.00 57.66  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 22.909 -15.031 40.382 1.00 29.38  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 32.190 -15.744 39.805 1.00 30.20  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 21.033 -23.312 42.056 1.00 42.16  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 26.927 -1.631  22.044 1.00 49.47  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 19.595 -27.311 10.034 1.00 48.16  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 33.519 -0.371  20.190 1.00 38.54  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 32.362 -9.025  39.733 1.00 54.30  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 33.988 -32.937 21.825 1.00 58.31  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 33.509 -33.015 12.097 1.00 40.19  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 29.431 -0.875  22.278 1.00 48.78  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 41.973 -8.065  13.759 1.00 54.83  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 25.630 -16.167 41.059 1.00 45.44  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 34.508 -18.931 36.131 1.00 62.47  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 39.854 -5.564  33.959 1.00 35.52  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 45.709 -5.537  23.696 1.00 44.04  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 42.715 -18.235 30.704 1.00 44.09  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 22.232 -10.437 14.666 1.00 39.42  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 23.411 -30.529 19.300 1.00 61.66  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 31.792 -26.187 27.137 1.00 48.92  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 26.339 -29.512 22.687 1.00 55.01  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 31.876 -0.080  13.348 1.00 57.91  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 44.359 -4.330  28.950 1.00 61.37  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 36.963 -31.637 23.418 1.00 69.08  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 22.954 -3.175  26.846 1.00 61.13  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 27.004 -34.395 18.005 1.00 59.09  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 19.476 -31.845 13.998 1.00 59.08  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 28.730 -2.738  13.069 1.00 66.28  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 36.551 -24.506 27.631 1.00 47.66  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 30.542 -34.375 14.899 1.00 50.95  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 47.859 -23.558 19.711 1.00 54.37  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 19.787 -8.175  24.559 1.00 47.52  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 35.372 -4.266  10.619 1.00 42.82  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 24.460 -21.724 41.029 1.00 52.26  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 34.152 -17.678 39.367 1.00 54.48  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 46.657 -14.705 18.274 1.00 61.64  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 32.081 -1.163  22.341 1.00 53.90  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 32.872 -3.342  10.158 1.00 54.87  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 47.138 -11.879 25.266 1.00 58.63  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 11.923 -18.803 22.660 1.00 60.66  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 35.890 -21.253 30.496 1.00 53.46  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 19.409 -7.773  35.289 1.00 48.47  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 46.954 -12.558 28.358 1.00 56.22  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 25.337 -5.683  34.947 1.00 54.22  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 45.490 -8.407  31.315 1.00 58.86  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 17.174 -8.068  25.152 1.00 62.70  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 43.929 -13.647 13.871 0.50 63.15  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 20.133 -35.300 10.126 1.00 35.23  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 19.861 -14.939 43.344 1.00 47.67  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 17.049 -28.158 9.932  1.00 45.04  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 43.123 -3.081  33.973 1.00 57.65  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 19.083 -28.222 13.799 0.50 64.37  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 32.541 -20.625 36.942 1.00 62.00  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 28.342 -29.804 24.522 1.00 60.43  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 32.160 -23.897 34.846 1.00 60.54  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 33.785 -11.183 41.615 0.50 60.12  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 12.460 -18.239 20.009 1.00 58.96  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 33.785 -14.136 41.615 0.50 38.41  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 21.222 -5.813  34.765 1.00 45.72  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 16.803 -6.896  34.875 1.00 63.67  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 45.050 -12.267 15.943 1.00 62.04  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 39.255 -5.730  11.420 1.00 49.58  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   F 6 .   ? 16.623 -29.978 12.350 1.00 53.43  ? 476 HOH   A O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 12.174 -24.187 0.062  1.00 44.98  ? 201 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 14.917 -25.717 -1.748 1.00 41.12  ? 202 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 22.579 -33.997 8.830  1.00 31.99  ? 203 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 17.691 -36.179 6.027  1.00 38.44  ? 204 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 20.768 -38.202 4.011  1.00 43.53  ? 205 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 11.392 -23.573 3.221  1.00 48.97  ? 206 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 20.767 -39.470 -2.111 1.00 49.18  ? 207 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 10.590 -24.641 5.605  1.00 52.52  ? 208 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.609 -36.480 10.009 1.00 47.45  ? 209 HOH   D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP A 5   ? 0.7741 0.9360 0.6410 0.0283  -0.1258 -0.0147 6   ASP A N   
2    C CA  . ASP A 5   ? 0.7657 0.9226 0.6173 0.0122  -0.1168 -0.0176 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7390 0.9248 0.6146 0.0017  -0.1125 -0.0331 6   ASP A C   
4    O O   . ASP A 5   ? 0.7320 0.9413 0.6355 0.0056  -0.1157 -0.0416 6   ASP A O   
5    C CB  . ASP A 5   ? 0.7895 0.9195 0.6328 0.0041  -0.1005 -0.0118 6   ASP A CB  
6    C CG  . ASP A 5   ? 0.9736 1.0852 0.7858 -0.0066 -0.0950 -0.0082 6   ASP A CG  
7    O OD1 . ASP A 5   ? 0.9684 1.0924 0.7801 -0.0175 -0.0920 -0.0169 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.0808 1.1650 0.8692 -0.0051 -0.0925 0.0024  6   ASP A OD2 
9    N N   . SER A 6   ? 0.6290 0.8119 0.4933 -0.0124 -0.1044 -0.0375 7   SER A N   
10   C CA  . SER A 6   ? 0.5811 0.7850 0.4635 -0.0241 -0.0982 -0.0517 7   SER A CA  
11   C C   . SER A 6   ? 0.5278 0.7196 0.4221 -0.0336 -0.0805 -0.0543 7   SER A C   
12   O O   . SER A 6   ? 0.5125 0.7099 0.4117 -0.0453 -0.0723 -0.0636 7   SER A O   
13   C CB  . SER A 6   ? 0.6592 0.8684 0.5209 -0.0327 -0.1018 -0.0562 7   SER A CB  
14   O OG  . SER A 6   ? 0.8214 1.0051 0.6562 -0.0391 -0.0943 -0.0490 7   SER A OG  
15   N N   . CYS A 7   ? 0.4228 0.5982 0.3219 -0.0281 -0.0753 -0.0464 8   CYS A N   
16   C CA  . CYS A 7   ? 0.3807 0.5441 0.2896 -0.0350 -0.0609 -0.0480 8   CYS A CA  
17   C C   . CYS A 7   ? 0.3831 0.5619 0.3169 -0.0406 -0.0553 -0.0593 8   CYS A C   
18   O O   . CYS A 7   ? 0.3650 0.5636 0.3136 -0.0372 -0.0615 -0.0649 8   CYS A O   
19   C CB  . CYS A 7   ? 0.3923 0.5370 0.3006 -0.0276 -0.0581 -0.0379 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.4749 0.5929 0.3521 -0.0265 -0.0574 -0.0258 8   CYS A SG  
21   N N   . ILE A 8   ? 0.2882 0.4571 0.2262 -0.0490 -0.0435 -0.0630 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2489 0.4223 0.2059 -0.0542 -0.0361 -0.0711 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2775 0.4333 0.2385 -0.0496 -0.0306 -0.0638 9   ILE A C   
24   O O   . ILE A 8   ? 0.2702 0.4110 0.2196 -0.0459 -0.0302 -0.0553 9   ILE A O   
25   C CB  . ILE A 8   ? 0.2901 0.4634 0.2482 -0.0660 -0.0279 -0.0812 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3077 0.4621 0.2537 -0.0689 -0.0212 -0.0781 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.2699 0.4641 0.2264 -0.0713 -0.0335 -0.0902 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3445 0.4945 0.2932 -0.0787 -0.0120 -0.0879 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2090 0.3654 0.1846 -0.0511 -0.0255 -0.0676 10  GLN A N   
30   N N   B GLN A 9   ? 0.2181 0.3760 0.1941 -0.0507 -0.0263 -0.0677 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2084 0.3481 0.1861 -0.0473 -0.0208 -0.0611 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2115 0.3543 0.1910 -0.0467 -0.0218 -0.0617 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2488 0.3776 0.2314 -0.0543 -0.0113 -0.0659 10  GLN A C   
34   C C   B GLN A 9   ? 0.2617 0.3930 0.2455 -0.0539 -0.0121 -0.0661 10  GLN A C   
35   O O   A GLN A 9   ? 0.2524 0.3895 0.2426 -0.0611 -0.0081 -0.0747 10  GLN A O   
36   O O   B GLN A 9   ? 0.2604 0.3992 0.2513 -0.0610 -0.0085 -0.0751 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2253 0.3730 0.2128 -0.0395 -0.0252 -0.0586 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2182 0.3719 0.2092 -0.0399 -0.0261 -0.0610 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.3065 0.4403 0.2992 -0.0383 -0.0187 -0.0554 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.1860 0.3240 0.1759 -0.0334 -0.0241 -0.0524 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5279 0.6616 0.5238 -0.0286 -0.0228 -0.0493 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.3899 0.5302 0.3936 -0.0345 -0.0191 -0.0565 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4233 0.5654 0.4171 -0.0211 -0.0314 -0.0464 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3202 0.4793 0.3374 -0.0351 -0.0206 -0.0642 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.4503 0.5723 0.4494 -0.0283 -0.0170 -0.0472 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3711 0.4931 0.3716 -0.0351 -0.0128 -0.0521 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2234 0.3331 0.2010 -0.0527 -0.0071 -0.0604 11  PHE A N   
48   N N   B PHE A 10  ? 0.2325 0.3447 0.2111 -0.0519 -0.0081 -0.0602 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2160 0.3114 0.1952 -0.0573 0.0001  -0.0634 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2300 0.3269 0.2094 -0.0563 -0.0007 -0.0626 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2562 0.3461 0.2400 -0.0546 0.0019  -0.0601 11  PHE A C   
52   C C   B PHE A 10  ? 0.2658 0.3574 0.2501 -0.0540 0.0013  -0.0599 11  PHE A C   
53   O O   A PHE A 10  ? 0.2542 0.3358 0.2351 -0.0486 0.0004  -0.0528 11  PHE A O   
54   O O   B PHE A 10  ? 0.2627 0.3478 0.2449 -0.0478 -0.0006 -0.0525 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2327 0.3126 0.2049 -0.0565 0.0025  -0.0611 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2532 0.3353 0.2251 -0.0548 0.0010  -0.0593 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2473 0.3111 0.2192 -0.0600 0.0083  -0.0647 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2785 0.3645 0.2467 -0.0595 0.0019  -0.0650 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.2709 0.3347 0.2432 -0.0672 0.0123  -0.0730 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3225 0.4222 0.2861 -0.0601 -0.0025 -0.0655 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.2604 0.3074 0.2297 -0.0558 0.0093  -0.0598 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3215 0.3960 0.2894 -0.0628 0.0071  -0.0699 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.2927 0.3369 0.2616 -0.0698 0.0175  -0.0755 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3387 0.4417 0.2974 -0.0656 -0.0008 -0.0715 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.2934 0.3224 0.2590 -0.0578 0.0131  -0.0621 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3651 0.4434 0.3304 -0.0674 0.0089  -0.0765 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.2743 0.3003 0.2390 -0.0644 0.0174  -0.0695 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3370 0.4300 0.2977 -0.0694 0.0055  -0.0775 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2199 0.3150 0.2105 -0.0602 0.0057  -0.0667 12  THR A N   
70   C CA  . THR A 11  ? 0.2232 0.3154 0.2187 -0.0601 0.0091  -0.0662 12  THR A CA  
71   C C   . THR A 11  ? 0.2541 0.3236 0.2411 -0.0573 0.0117  -0.0590 12  THR A C   
72   O O   . THR A 11  ? 0.2507 0.3193 0.2395 -0.0524 0.0107  -0.0543 12  THR A O   
73   C CB  . THR A 11  ? 0.2825 0.3791 0.2835 -0.0703 0.0161  -0.0763 12  THR A CB  
74   O OG1 . THR A 11  ? 0.2932 0.4145 0.3037 -0.0728 0.0125  -0.0842 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3393 0.4348 0.3455 -0.0719 0.0211  -0.0776 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2317 0.2834 0.2098 -0.0597 0.0144  -0.0586 13  ARG A N   
77   C CA  . ARG A 12  ? 0.2404 0.2709 0.2099 -0.0568 0.0156  -0.0527 13  ARG A CA  
78   C C   . ARG A 12  ? 0.2608 0.2892 0.2283 -0.0490 0.0104  -0.0461 13  ARG A C   
79   O O   . ARG A 12  ? 0.2603 0.2736 0.2218 -0.0462 0.0102  -0.0423 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3050 0.3152 0.2651 -0.0612 0.0195  -0.0554 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.4496 0.4531 0.4065 -0.0710 0.0271  -0.0614 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.7047 0.6999 0.6574 -0.0733 0.0311  -0.0594 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.8760 0.8459 0.8142 -0.0695 0.0300  -0.0526 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.0190 0.9801 0.9511 -0.0696 0.0318  -0.0490 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.8756 0.8141 0.7931 -0.0660 0.0294  -0.0432 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.7967 0.7725 0.7376 -0.0729 0.0356  -0.0519 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2096 0.2520 0.1806 -0.0461 0.0065  -0.0454 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2191 0.2584 0.1870 -0.0412 0.0036  -0.0407 14  HIS A CA  
89   C C   . HIS A 13  ? 0.2494 0.2816 0.2157 -0.0370 0.0031  -0.0348 14  HIS A C   
90   O O   . HIS A 13  ? 0.2434 0.2657 0.2065 -0.0349 0.0027  -0.0331 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2120 0.2644 0.1795 -0.0405 0.0006  -0.0406 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.2397 0.2877 0.2028 -0.0378 -0.0002 -0.0370 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.2498 0.2931 0.2125 -0.0391 0.0016  -0.0405 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2482 0.2958 0.2074 -0.0345 -0.0017 -0.0315 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2409 0.2833 0.2008 -0.0376 0.0016  -0.0379 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2334 0.2767 0.1895 -0.0353 0.0000  -0.0320 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2114 0.2496 0.1809 -0.0353 0.0027  -0.0328 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2140 0.2452 0.1819 -0.0317 0.0030  -0.0279 15  ALA A CA  
99   C C   . ALA A 14  ? 0.2403 0.2566 0.2035 -0.0336 0.0057  -0.0278 15  ALA A C   
100  O O   . ALA A 14  ? 0.2213 0.2293 0.1805 -0.0312 0.0049  -0.0247 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2243 0.2644 0.1980 -0.0291 0.0026  -0.0272 15  ALA A CB  
102  N N   A SER A 15  ? 0.2275 0.2396 0.1895 -0.0383 0.0089  -0.0315 16  SER A N   
103  N N   B SER A 15  ? 0.2238 0.2359 0.1858 -0.0383 0.0089  -0.0316 16  SER A N   
104  N N   C SER A 15  ? 0.2184 0.2303 0.1804 -0.0383 0.0089  -0.0315 16  SER A N   
105  C CA  A SER A 15  ? 0.2338 0.2279 0.1866 -0.0406 0.0112  -0.0309 16  SER A CA  
106  C CA  B SER A 15  ? 0.2318 0.2259 0.1846 -0.0407 0.0112  -0.0310 16  SER A CA  
107  C CA  C SER A 15  ? 0.2235 0.2173 0.1761 -0.0405 0.0111  -0.0308 16  SER A CA  
108  C C   A SER A 15  ? 0.2891 0.2722 0.2360 -0.0376 0.0075  -0.0298 16  SER A C   
109  C C   B SER A 15  ? 0.2909 0.2739 0.2378 -0.0377 0.0076  -0.0299 16  SER A C   
110  C C   C SER A 15  ? 0.2873 0.2700 0.2340 -0.0377 0.0076  -0.0298 16  SER A C   
111  O O   A SER A 15  ? 0.2703 0.2414 0.2103 -0.0354 0.0057  -0.0271 16  SER A O   
112  O O   B SER A 15  ? 0.2782 0.2490 0.2180 -0.0356 0.0059  -0.0272 16  SER A O   
113  O O   C SER A 15  ? 0.2746 0.2449 0.2142 -0.0356 0.0058  -0.0272 16  SER A O   
114  C CB  A SER A 15  ? 0.2789 0.2685 0.2291 -0.0478 0.0166  -0.0356 16  SER A CB  
115  C CB  B SER A 15  ? 0.2768 0.2665 0.2271 -0.0479 0.0166  -0.0358 16  SER A CB  
116  C CB  C SER A 15  ? 0.2611 0.2501 0.2109 -0.0477 0.0167  -0.0352 16  SER A CB  
117  O OG  A SER A 15  ? 0.3133 0.2814 0.2498 -0.0504 0.0190  -0.0340 16  SER A OG  
118  O OG  B SER A 15  ? 0.3130 0.3154 0.2715 -0.0506 0.0202  -0.0388 16  SER A OG  
119  O OG  C SER A 15  ? 0.2681 0.2592 0.2190 -0.0508 0.0172  -0.0395 16  SER A OG  
120  N N   . ASP A 16  ? 0.2586 0.2472 0.2093 -0.0374 0.0061  -0.0329 17  ASP A N   
121  C CA  . ASP A 16  ? 0.2615 0.2429 0.2104 -0.0338 0.0028  -0.0339 17  ASP A CA  
122  C C   . ASP A 16  ? 0.2656 0.2524 0.2181 -0.0293 -0.0005 -0.0318 17  ASP A C   
123  O O   . ASP A 16  ? 0.2661 0.2453 0.2167 -0.0254 -0.0039 -0.0319 17  ASP A O   
124  C CB  . ASP A 16  ? 0.2753 0.2633 0.2288 -0.0355 0.0035  -0.0391 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.3458 0.3242 0.2943 -0.0406 0.0072  -0.0427 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.3453 0.3093 0.2852 -0.0430 0.0094  -0.0410 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.3700 0.3544 0.3221 -0.0432 0.0087  -0.0478 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2093 0.2088 0.1663 -0.0297 0.0004  -0.0302 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2024 0.2053 0.1611 -0.0273 -0.0008 -0.0285 18  VAL A CA  
130  C C   . VAL A 17  ? 0.2600 0.2533 0.2143 -0.0258 -0.0017 -0.0257 18  VAL A C   
131  O O   . VAL A 17  ? 0.2435 0.2346 0.1984 -0.0236 -0.0042 -0.0269 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2225 0.2351 0.1821 -0.0282 0.0007  -0.0261 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2284 0.2395 0.1865 -0.0273 0.0013  -0.0237 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2172 0.2387 0.1782 -0.0302 0.0009  -0.0293 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2314 0.2205 0.1822 -0.0274 0.0006  -0.0231 19  LEU A N   
136  C CA  . LEU A 18  ? 0.2485 0.2280 0.1934 -0.0271 0.0007  -0.0208 19  LEU A CA  
137  C C   . LEU A 18  ? 0.2605 0.2268 0.1976 -0.0258 -0.0029 -0.0216 19  LEU A C   
138  O O   . LEU A 18  ? 0.2449 0.2070 0.1788 -0.0238 -0.0060 -0.0211 19  LEU A O   
139  C CB  . LEU A 18  ? 0.2539 0.2324 0.1975 -0.0298 0.0051  -0.0196 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3015 0.2723 0.2397 -0.0302 0.0066  -0.0177 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.2972 0.2734 0.2395 -0.0279 0.0064  -0.0162 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.3430 0.3127 0.2808 -0.0336 0.0121  -0.0186 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.2466 0.2060 0.1801 -0.0267 -0.0031 -0.0231 20  LEU A N   
144  C CA  . LEU A 19  ? 0.2667 0.2097 0.1902 -0.0240 -0.0076 -0.0233 20  LEU A CA  
145  C C   . LEU A 19  ? 0.2966 0.2456 0.2272 -0.0177 -0.0141 -0.0259 20  LEU A C   
146  O O   . LEU A 19  ? 0.2957 0.2366 0.2203 -0.0138 -0.0197 -0.0253 20  LEU A O   
147  C CB  . LEU A 19  ? 0.2956 0.2301 0.2151 -0.0262 -0.0056 -0.0252 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4071 0.3197 0.3134 -0.0225 -0.0102 -0.0247 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.4510 0.3441 0.3387 -0.0247 -0.0102 -0.0204 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.4691 0.3729 0.3721 -0.0258 -0.0065 -0.0274 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.2537 0.2182 0.1970 -0.0172 -0.0131 -0.0295 21  ASN A N   
152  C CA  . ASN A 20  ? 0.2326 0.2060 0.1854 -0.0127 -0.0174 -0.0342 21  ASN A CA  
153  C C   . ASN A 20  ? 0.2645 0.2444 0.2197 -0.0130 -0.0182 -0.0339 21  ASN A C   
154  O O   . ASN A 20  ? 0.2557 0.2378 0.2146 -0.0088 -0.0238 -0.0376 21  ASN A O   
155  C CB  . ASN A 20  ? 0.2470 0.2338 0.2105 -0.0141 -0.0144 -0.0389 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.3745 0.3546 0.3378 -0.0120 -0.0154 -0.0421 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.3248 0.2899 0.2816 -0.0073 -0.0201 -0.0418 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3027 0.2916 0.2711 -0.0155 -0.0111 -0.0452 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2437 0.2266 0.1971 -0.0175 -0.0130 -0.0302 22  LEU A N   
160  C CA  . LEU A 21  ? 0.2376 0.2236 0.1914 -0.0188 -0.0124 -0.0300 22  LEU A CA  
161  C C   . LEU A 21  ? 0.2701 0.2448 0.2148 -0.0167 -0.0174 -0.0288 22  LEU A C   
162  O O   . LEU A 21  ? 0.2652 0.2440 0.2123 -0.0157 -0.0208 -0.0320 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2405 0.2277 0.1923 -0.0228 -0.0060 -0.0258 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.2570 0.2536 0.2140 -0.0247 -0.0023 -0.0263 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.2657 0.2608 0.2190 -0.0261 0.0018  -0.0213 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.2849 0.2903 0.2482 -0.0263 -0.0015 -0.0316 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.2602 0.2206 0.1934 -0.0169 -0.0175 -0.0249 23  ASN A N   
168  C CA  . ASN A 22  ? 0.2780 0.2240 0.1975 -0.0157 -0.0222 -0.0231 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3275 0.2706 0.2468 -0.0084 -0.0322 -0.0264 23  ASN A C   
170  O O   . ASN A 22  ? 0.3348 0.2747 0.2484 -0.0059 -0.0386 -0.0272 23  ASN A O   
171  C CB  . ASN A 22  ? 0.2982 0.2276 0.2031 -0.0194 -0.0184 -0.0189 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4034 0.3173 0.2910 -0.0207 -0.0207 -0.0166 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.3644 0.2828 0.2523 -0.0210 -0.0222 -0.0175 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4214 0.3154 0.2916 -0.0223 -0.0207 -0.0139 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.2967 0.2421 0.2231 -0.0045 -0.0341 -0.0291 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3029 0.2473 0.2328 0.0043  -0.0439 -0.0335 24  ARG A CA  
177  C C   . ARG A 23  ? 0.3291 0.2939 0.2748 0.0064  -0.0474 -0.0404 24  ARG A C   
178  O O   . ARG A 23  ? 0.3210 0.2854 0.2663 0.0130  -0.0573 -0.0436 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3032 0.2483 0.2404 0.0069  -0.0428 -0.0364 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.3456 0.2674 0.2656 0.0057  -0.0411 -0.0312 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.3703 0.2941 0.2981 0.0058  -0.0376 -0.0347 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.4826 0.3820 0.3931 0.0042  -0.0357 -0.0309 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.6288 0.5264 0.5410 0.0001  -0.0295 -0.0328 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.4669 0.3858 0.3960 -0.0026 -0.0250 -0.0375 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.5811 0.4545 0.4761 -0.0026 -0.0270 -0.0301 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.2748 0.2564 0.2329 0.0003  -0.0395 -0.0431 25  LEU A N   
187  C CA  . LEU A 24  ? 0.2688 0.2688 0.2407 -0.0007 -0.0400 -0.0505 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3149 0.3114 0.2786 -0.0023 -0.0429 -0.0491 25  LEU A C   
189  O O   . LEU A 24  ? 0.3165 0.3228 0.2873 0.0010  -0.0499 -0.0560 25  LEU A O   
190  C CB  . LEU A 24  ? 0.2574 0.2694 0.2375 -0.0085 -0.0294 -0.0519 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.2942 0.3131 0.2830 -0.0086 -0.0258 -0.0551 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.2866 0.3148 0.2789 -0.0168 -0.0161 -0.0559 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.2888 0.3179 0.2919 -0.0017 -0.0323 -0.0650 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.2763 0.2595 0.2253 -0.0073 -0.0377 -0.0413 26  ARG A N   
195  C CA  . ARG A 25  ? 0.2870 0.2649 0.2262 -0.0098 -0.0394 -0.0402 26  ARG A CA  
196  C C   . ARG A 25  ? 0.3578 0.3268 0.2871 -0.0026 -0.0521 -0.0409 26  ARG A C   
197  O O   . ARG A 25  ? 0.3654 0.3420 0.2966 -0.0016 -0.0581 -0.0460 26  ARG A O   
198  C CB  . ARG A 25  ? 0.2992 0.2638 0.2252 -0.0157 -0.0314 -0.0328 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.3515 0.3114 0.2678 -0.0192 -0.0319 -0.0330 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.4176 0.3669 0.3240 -0.0251 -0.0229 -0.0279 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.3827 0.3166 0.2763 -0.0248 -0.0223 -0.0227 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.5125 0.4309 0.3885 -0.0283 -0.0210 -0.0200 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.4430 0.3594 0.3117 -0.0313 -0.0216 -0.0218 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4225 0.3270 0.2872 -0.0299 -0.0183 -0.0163 26  ARG A NH2 
205  N N   A SER A 26  ? 0.3385 0.2904 0.2558 0.0023  -0.0562 -0.0361 27  SER A N   
206  N N   B SER A 26  ? 0.3358 0.2878 0.2533 0.0023  -0.0561 -0.0361 27  SER A N   
207  N N   C SER A 26  ? 0.3396 0.2916 0.2569 0.0023  -0.0562 -0.0361 27  SER A N   
208  C CA  A SER A 26  ? 0.3615 0.2983 0.2639 0.0101  -0.0687 -0.0348 27  SER A CA  
209  C CA  B SER A 26  ? 0.3586 0.2952 0.2612 0.0103  -0.0686 -0.0348 27  SER A CA  
210  C CA  C SER A 26  ? 0.3638 0.3006 0.2662 0.0102  -0.0687 -0.0348 27  SER A CA  
211  C C   A SER A 26  ? 0.4210 0.3737 0.3389 0.0198  -0.0808 -0.0437 27  SER A C   
212  C C   B SER A 26  ? 0.4180 0.3707 0.3359 0.0197  -0.0807 -0.0436 27  SER A C   
213  C C   C SER A 26  ? 0.4207 0.3736 0.3387 0.0197  -0.0808 -0.0437 27  SER A C   
214  O O   A SER A 26  ? 0.4388 0.3869 0.3475 0.0256  -0.0926 -0.0448 27  SER A O   
215  O O   B SER A 26  ? 0.4338 0.3819 0.3424 0.0252  -0.0922 -0.0447 27  SER A O   
216  O O   C SER A 26  ? 0.4369 0.3854 0.3458 0.0254  -0.0924 -0.0449 27  SER A O   
217  C CB  A SER A 26  ? 0.4122 0.3258 0.2992 0.0126  -0.0687 -0.0285 27  SER A CB  
218  C CB  B SER A 26  ? 0.4091 0.3251 0.2996 0.0134  -0.0687 -0.0293 27  SER A CB  
219  C CB  C SER A 26  ? 0.4199 0.3344 0.3080 0.0129  -0.0688 -0.0288 27  SER A CB  
220  O OG  A SER A 26  ? 0.4704 0.3906 0.3719 0.0182  -0.0698 -0.0321 27  SER A OG  
221  O OG  B SER A 26  ? 0.4907 0.3899 0.3642 0.0050  -0.0593 -0.0223 27  SER A OG  
222  O OG  C SER A 26  ? 0.5387 0.4336 0.4086 0.0212  -0.0812 -0.0265 27  SER A OG  
223  N N   . ARG A 27  ? 0.3601 0.3327 0.3016 0.0213  -0.0780 -0.0508 28  ARG A N   
224  C CA  . ARG A 27  ? 0.3652 0.3577 0.3269 0.0298  -0.0876 -0.0619 28  ARG A CA  
225  C C   . ARG A 27  ? 0.3741 0.3927 0.3538 0.0232  -0.0836 -0.0713 28  ARG A C   
226  O O   . ARG A 27  ? 0.3718 0.4121 0.3722 0.0281  -0.0895 -0.0830 28  ARG A O   
227  C CB  . ARG A 27  ? 0.3695 0.3665 0.3453 0.0348  -0.0861 -0.0657 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.4632 0.4326 0.4207 0.0406  -0.0893 -0.0575 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.5027 0.4762 0.4734 0.0426  -0.0845 -0.0613 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.6172 0.6100 0.6110 0.0525  -0.0926 -0.0735 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.7942 0.8037 0.8087 0.0518  -0.0866 -0.0819 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.6509 0.6794 0.6881 0.0608  -0.0936 -0.0947 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.5887 0.5972 0.6019 0.0420  -0.0735 -0.0787 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.3033 0.3195 0.2753 0.0120  -0.0733 -0.0670 29  ASP A N   
235  C CA  . ASP A 28  ? 0.3025 0.3372 0.2863 0.0034  -0.0669 -0.0743 29  ASP A CA  
236  C C   . ASP A 28  ? 0.3438 0.3993 0.3502 -0.0002 -0.0592 -0.0833 29  ASP A C   
237  O O   . ASP A 28  ? 0.3475 0.4241 0.3704 -0.0033 -0.0587 -0.0950 29  ASP A O   
238  C CB  . ASP A 28  ? 0.3378 0.3817 0.3228 0.0064  -0.0781 -0.0816 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.4186 0.4749 0.4087 -0.0049 -0.0700 -0.0874 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.4242 0.4701 0.4051 -0.0141 -0.0576 -0.0808 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.4433 0.5197 0.4471 -0.0044 -0.0762 -0.0993 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.2762 0.3260 0.2829 -0.0004 -0.0528 -0.0789 30  ILE A N   
243  C CA  . ILE A 29  ? 0.2660 0.3322 0.2899 -0.0044 -0.0449 -0.0866 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3009 0.3651 0.3197 -0.0165 -0.0308 -0.0828 30  ILE A C   
245  O O   . ILE A 29  ? 0.2621 0.3101 0.2662 -0.0187 -0.0261 -0.0718 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3038 0.3661 0.3312 0.0023  -0.0467 -0.0857 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3235 0.3871 0.3574 0.0160  -0.0614 -0.0909 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.2808 0.3580 0.3223 -0.0042 -0.0362 -0.0929 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.3513 0.4021 0.3818 0.0230  -0.0633 -0.0873 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.2806 0.3612 0.3115 -0.0243 -0.0241 -0.0927 31  LEU A N   
251  C CA  . LEU A 30  ? 0.2841 0.3612 0.3090 -0.0359 -0.0104 -0.0903 31  LEU A CA  
252  C C   . LEU A 30  ? 0.2952 0.3554 0.3030 -0.0398 -0.0071 -0.0806 31  LEU A C   
253  O O   . LEU A 30  ? 0.2684 0.3197 0.2674 -0.0468 0.0029  -0.0757 31  LEU A O   
254  C CB  . LEU A 30  ? 0.2940 0.3672 0.3163 -0.0380 -0.0033 -0.0865 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.3753 0.4672 0.4151 -0.0395 -0.0007 -0.0991 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.3893 0.4753 0.4219 -0.0441 0.0077  -0.0948 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.4554 0.5638 0.5071 -0.0485 0.0055  -0.1123 31  LEU A CD2 
258  N N   . THR A 31  ? 0.2616 0.3177 0.2645 -0.0355 -0.0154 -0.0793 32  THR A N   
259  C CA  . THR A 31  ? 0.2569 0.2998 0.2460 -0.0401 -0.0116 -0.0733 32  THR A CA  
260  C C   . THR A 31  ? 0.3214 0.3730 0.3161 -0.0506 -0.0029 -0.0819 32  THR A C   
261  O O   . THR A 31  ? 0.3073 0.3780 0.3173 -0.0527 -0.0045 -0.0943 32  THR A O   
262  C CB  . THR A 31  ? 0.3276 0.3651 0.3093 -0.0343 -0.0223 -0.0717 32  THR A CB  
263  O OG1 . THR A 31  ? 0.3611 0.4163 0.3558 -0.0310 -0.0315 -0.0831 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3194 0.3423 0.2905 -0.0263 -0.0282 -0.0622 32  THR A CG2 
265  N N   . ASP A 32  ? 0.2898 0.3275 0.2731 -0.0575 0.0070  -0.0762 33  ASP A N   
266  C CA  . ASP A 32  ? 0.2873 0.3274 0.2719 -0.0688 0.0177  -0.0832 33  ASP A CA  
267  C C   . ASP A 32  ? 0.3227 0.3503 0.2964 -0.0742 0.0224  -0.0813 33  ASP A C   
268  O O   . ASP A 32  ? 0.3243 0.3478 0.2952 -0.0842 0.0331  -0.0853 33  ASP A O   
269  C CB  . ASP A 32  ? 0.2991 0.3318 0.2790 -0.0734 0.0280  -0.0792 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.3995 0.4132 0.3655 -0.0682 0.0291  -0.0649 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.3436 0.3484 0.3034 -0.0631 0.0247  -0.0585 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.4696 0.4784 0.4310 -0.0696 0.0341  -0.0610 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.2661 0.2859 0.2323 -0.0685 0.0156  -0.0757 34  VAL A N   
274  C CA  . VAL A 33  ? 0.2712 0.2795 0.2272 -0.0737 0.0202  -0.0752 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3277 0.3360 0.2789 -0.0683 0.0096  -0.0744 34  VAL A C   
276  O O   . VAL A 33  ? 0.3232 0.3310 0.2732 -0.0596 0.0007  -0.0693 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3165 0.3029 0.2601 -0.0745 0.0300  -0.0647 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.2991 0.2771 0.2372 -0.0652 0.0250  -0.0543 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3279 0.3019 0.2628 -0.0818 0.0382  -0.0666 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3004 0.3071 0.2466 -0.0743 0.0110  -0.0796 35  VAL A N   
281  N N   B VAL A 34  ? 0.2878 0.2945 0.2339 -0.0742 0.0109  -0.0795 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3042 0.3067 0.2402 -0.0716 0.0029  -0.0788 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.2860 0.2881 0.2219 -0.0710 0.0025  -0.0782 35  VAL A CA  
284  C C   A VAL A 34  ? 0.3449 0.3276 0.2677 -0.0763 0.0132  -0.0733 35  VAL A C   
285  C C   B VAL A 34  ? 0.3414 0.3248 0.2639 -0.0763 0.0124  -0.0739 35  VAL A C   
286  O O   A VAL A 34  ? 0.3470 0.3252 0.2700 -0.0842 0.0240  -0.0768 35  VAL A O   
287  O O   B VAL A 34  ? 0.3470 0.3271 0.2699 -0.0847 0.0225  -0.0784 35  VAL A O   
288  C CB  A VAL A 34  ? 0.3653 0.3845 0.3067 -0.0752 -0.0047 -0.0913 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.3356 0.3551 0.2768 -0.0709 -0.0091 -0.0890 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.3772 0.3891 0.3032 -0.0726 -0.0138 -0.0895 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.3351 0.3641 0.2819 -0.0822 -0.0024 -0.1009 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.3573 0.3989 0.3160 -0.0700 -0.0142 -0.0991 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.3437 0.3540 0.2689 -0.0660 -0.0193 -0.0849 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.2966 0.2668 0.2078 -0.0716 0.0107  -0.0656 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3145 0.2678 0.2147 -0.0751 0.0197  -0.0620 36  ILE A CA  
296  C C   . ILE A 35  ? 0.3804 0.3324 0.2690 -0.0785 0.0145  -0.0665 36  ILE A C   
297  O O   . ILE A 35  ? 0.3756 0.3279 0.2568 -0.0736 0.0039  -0.0643 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3368 0.2790 0.2334 -0.0690 0.0221  -0.0521 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3267 0.2723 0.2337 -0.0646 0.0245  -0.0475 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.3624 0.2897 0.2509 -0.0723 0.0321  -0.0506 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3237 0.2660 0.2349 -0.0692 0.0344  -0.0492 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.3401 0.2888 0.2252 -0.0871 0.0218  -0.0730 37  VAL A N   
303  C CA  . VAL A 36  ? 0.3499 0.2975 0.2225 -0.0920 0.0174  -0.0786 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4228 0.3517 0.2817 -0.0946 0.0261  -0.0746 37  VAL A C   
305  O O   . VAL A 36  ? 0.4108 0.3302 0.2724 -0.0979 0.0389  -0.0745 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4013 0.3603 0.2792 -0.1012 0.0191  -0.0909 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4124 0.3712 0.2759 -0.1063 0.0134  -0.0971 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.3994 0.3803 0.2940 -0.0988 0.0110  -0.0968 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.3973 0.3197 0.2407 -0.0931 0.0195  -0.0719 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4054 0.3112 0.2351 -0.0965 0.0280  -0.0695 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5018 0.4052 0.3127 -0.1029 0.0221  -0.0751 38  VAL A C   
312  O O   . VAL A 37  ? 0.4653 0.3663 0.2622 -0.0997 0.0107  -0.0720 38  VAL A O   
313  C CB  . VAL A 37  ? 0.4473 0.3457 0.2740 -0.0900 0.0274  -0.0604 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.4596 0.3438 0.2783 -0.0943 0.0396  -0.0600 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4221 0.3279 0.2674 -0.0826 0.0280  -0.0554 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5113 0.4152 0.3212 -0.1117 0.0288  -0.0838 39  SER A N   
317  N N   B SER A 38  ? 0.5014 0.4035 0.3105 -0.1119 0.0301  -0.0833 39  SER A N   
318  C CA  A SER A 38  ? 0.5342 0.4380 0.3268 -0.1192 0.0235  -0.0912 39  SER A CA  
319  C CA  B SER A 38  ? 0.5210 0.4220 0.3127 -0.1199 0.0261  -0.0909 39  SER A CA  
320  C C   A SER A 38  ? 0.5468 0.4674 0.3404 -0.1148 0.0049  -0.0941 39  SER A C   
321  C C   B SER A 38  ? 0.5506 0.4632 0.3358 -0.1154 0.0067  -0.0917 39  SER A C   
322  O O   A SER A 38  ? 0.5272 0.4645 0.3400 -0.1136 0.0027  -0.0990 39  SER A O   
323  O O   B SER A 38  ? 0.5587 0.4621 0.3230 -0.1134 -0.0021 -0.0876 39  SER A O   
324  C CB  A SER A 38  ? 0.6196 0.5056 0.3883 -0.1224 0.0261  -0.0879 39  SER A CB  
325  C CB  B SER A 38  ? 0.5867 0.4692 0.3587 -0.1255 0.0346  -0.0898 39  SER A CB  
326  O OG  A SER A 38  ? 0.8105 0.6843 0.5824 -0.1255 0.0430  -0.0870 39  SER A OG  
327  O OG  B SER A 38  ? 0.6732 0.5483 0.4532 -0.1306 0.0517  -0.0934 39  SER A OG  
328  N N   A ARG A 39  ? 0.5053 0.4206 0.2781 -0.1119 -0.0082 -0.0912 40  ARG A N   
329  N N   B ARG A 39  ? 0.4727 0.4047 0.2768 -0.1128 0.0005  -0.0967 40  ARG A N   
330  C CA  A ARG A 39  ? 0.4968 0.4262 0.2686 -0.1052 -0.0280 -0.0938 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.4684 0.4182 0.2764 -0.1069 -0.0178 -0.1005 40  ARG A CA  
332  C C   A ARG A 39  ? 0.5082 0.4422 0.2914 -0.0925 -0.0371 -0.0862 40  ARG A C   
333  C C   B ARG A 39  ? 0.4933 0.4424 0.3031 -0.0941 -0.0285 -0.0909 40  ARG A C   
334  O O   A ARG A 39  ? 0.4945 0.4422 0.2822 -0.0849 -0.0534 -0.0890 40  ARG A O   
335  O O   B ARG A 39  ? 0.4899 0.4568 0.3132 -0.0874 -0.0405 -0.0946 40  ARG A O   
336  C CB  A ARG A 39  ? 0.5173 0.4353 0.2576 -0.1072 -0.0392 -0.0938 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.4865 0.4385 0.2753 -0.1112 -0.0290 -0.1075 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.6010 0.5235 0.3326 -0.1189 -0.0369 -0.1053 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.6236 0.5844 0.4171 -0.1240 -0.0207 -0.1206 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.6419 0.5556 0.3414 -0.1191 -0.0521 -0.1052 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.7205 0.6926 0.5016 -0.1271 -0.0354 -0.1303 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.6615 0.5758 0.3481 -0.1320 -0.0478 -0.1157 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.8033 0.7825 0.5877 -0.1411 -0.0256 -0.1436 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.8438 0.7794 0.5374 -0.1352 -0.0573 -0.1281 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 0.9578 0.9209 0.7232 -0.1518 -0.0153 -0.1460 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7128 0.6470 0.3926 -0.1482 -0.0521 -0.1377 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.7767 0.7166 0.5185 -0.1506 -0.0128 -0.1363 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.6692 0.6293 0.3849 -0.1260 -0.0714 -0.1322 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.7899 0.7597 0.5595 -0.1647 -0.0062 -0.1591 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.4358 0.3593 0.2242 -0.0897 -0.0269 -0.0774 41  GLU A N   
351  N N   B GLU A 40  ? 0.4485 0.3784 0.2472 -0.0910 -0.0232 -0.0801 41  GLU A N   
352  C CA  A GLU A 40  ? 0.4200 0.3462 0.2181 -0.0788 -0.0337 -0.0704 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.4399 0.3667 0.2399 -0.0802 -0.0311 -0.0712 41  GLU A CA  
354  C C   A GLU A 40  ? 0.4493 0.3913 0.2761 -0.0768 -0.0273 -0.0725 41  GLU A C   
355  C C   B GLU A 40  ? 0.4595 0.3998 0.2869 -0.0764 -0.0257 -0.0710 41  GLU A C   
356  O O   A GLU A 40  ? 0.4234 0.3658 0.2593 -0.0835 -0.0136 -0.0751 41  GLU A O   
357  O O   B GLU A 40  ? 0.4333 0.3716 0.2700 -0.0814 -0.0114 -0.0711 41  GLU A O   
358  C CB  A GLU A 40  ? 0.4424 0.3471 0.2253 -0.0772 -0.0284 -0.0599 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.4678 0.3714 0.2490 -0.0809 -0.0244 -0.0618 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.6395 0.5247 0.3896 -0.0798 -0.0343 -0.0570 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.6325 0.5193 0.3819 -0.0835 -0.0319 -0.0602 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.1073 0.9843 0.8434 -0.0701 -0.0504 -0.0509 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.0711 0.9494 0.8067 -0.0738 -0.0473 -0.0534 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.1171 0.9835 0.8521 -0.0661 -0.0475 -0.0433 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.0974 0.9815 0.8259 -0.0687 -0.0638 -0.0565 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.1170 0.9976 0.8428 -0.0661 -0.0662 -0.0540 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.0750 0.9407 0.8070 -0.0710 -0.0430 -0.0455 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4036 0.3564 0.2427 -0.0674 -0.0372 -0.0711 42  GLN A N   
369  C CA  . GLN A 41  ? 0.3803 0.3474 0.2439 -0.0650 -0.0327 -0.0727 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4062 0.3670 0.2718 -0.0565 -0.0346 -0.0636 42  GLN A C   
371  O O   . GLN A 41  ? 0.4079 0.3622 0.2625 -0.0494 -0.0461 -0.0598 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4001 0.3914 0.2800 -0.0630 -0.0430 -0.0836 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.6063 0.6079 0.4892 -0.0734 -0.0389 -0.0949 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.8090 0.8382 0.7127 -0.0731 -0.0464 -0.1080 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.7150 0.7575 0.6335 -0.0645 -0.0545 -0.1094 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.8262 0.8659 0.7327 -0.0831 -0.0432 -0.1194 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.3293 0.2909 0.2077 -0.0572 -0.0236 -0.0603 43  PHE A N   
378  C CA  . PHE A 42  ? 0.3334 0.2905 0.2150 -0.0504 -0.0240 -0.0527 43  PHE A CA  
379  C C   . PHE A 42  ? 0.3728 0.3448 0.2751 -0.0492 -0.0207 -0.0556 43  PHE A C   
380  O O   . PHE A 42  ? 0.3790 0.3525 0.2879 -0.0550 -0.0099 -0.0571 43  PHE A O   
381  C CB  . PHE A 42  ? 0.3486 0.2896 0.2215 -0.0532 -0.0129 -0.0454 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.3820 0.3070 0.2332 -0.0566 -0.0131 -0.0433 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4160 0.3367 0.2600 -0.0644 -0.0065 -0.0474 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.4255 0.3376 0.2616 -0.0531 -0.0187 -0.0377 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.4489 0.3544 0.2711 -0.0688 -0.0057 -0.0463 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.4791 0.3740 0.2916 -0.0580 -0.0176 -0.0361 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.4601 0.3526 0.2660 -0.0659 -0.0112 -0.0405 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3279 0.3094 0.2392 -0.0419 -0.0297 -0.0568 44  ARG A N   
389  C CA  . ARG A 43  ? 0.2975 0.2933 0.2275 -0.0414 -0.0263 -0.0603 44  ARG A CA  
390  C C   . ARG A 43  ? 0.3370 0.3238 0.2664 -0.0393 -0.0197 -0.0517 44  ARG A C   
391  O O   . ARG A 43  ? 0.3313 0.3064 0.2508 -0.0350 -0.0229 -0.0451 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3069 0.3186 0.2489 -0.0342 -0.0385 -0.0674 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.3828 0.4092 0.3298 -0.0361 -0.0458 -0.0784 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.4462 0.4966 0.4151 -0.0314 -0.0531 -0.0896 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.5916 0.6504 0.5752 -0.0361 -0.0416 -0.0920 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.7423 0.8115 0.7353 -0.0466 -0.0309 -0.0997 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.6443 0.7203 0.6374 -0.0536 -0.0303 -0.1076 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.5240 0.5962 0.5250 -0.0509 -0.0205 -0.1002 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.2937 0.2851 0.2322 -0.0429 -0.0106 -0.0520 45  ALA A N   
400  C CA  . ALA A 44  ? 0.2888 0.2737 0.2269 -0.0408 -0.0055 -0.0444 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3077 0.3011 0.2560 -0.0433 0.0004  -0.0468 45  ALA A C   
402  O O   . ALA A 44  ? 0.2871 0.2913 0.2434 -0.0477 0.0018  -0.0548 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3051 0.2756 0.2331 -0.0433 0.0020  -0.0382 45  ALA A CB  
404  N N   . HIS A 45  ? 0.2693 0.2584 0.2169 -0.0413 0.0039  -0.0406 46  HIS A N   
405  C CA  . HIS A 45  ? 0.2496 0.2426 0.2017 -0.0440 0.0100  -0.0409 46  HIS A CA  
406  C C   . HIS A 45  ? 0.2811 0.2612 0.2247 -0.0468 0.0182  -0.0352 46  HIS A C   
407  O O   . HIS A 45  ? 0.2768 0.2484 0.2153 -0.0431 0.0183  -0.0289 46  HIS A O   
408  C CB  . HIS A 45  ? 0.2437 0.2397 0.1987 -0.0393 0.0072  -0.0377 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.2701 0.2753 0.2327 -0.0349 -0.0010 -0.0428 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.2883 0.2872 0.2462 -0.0294 -0.0079 -0.0398 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.2796 0.2985 0.2536 -0.0353 -0.0030 -0.0514 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.2821 0.2892 0.2478 -0.0252 -0.0149 -0.0454 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.2714 0.2925 0.2488 -0.0281 -0.0124 -0.0532 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.2852 0.2631 0.2273 -0.0532 0.0254  -0.0381 47  LYS A N   
415  C CA  . LYS A 46  ? 0.2829 0.2451 0.2153 -0.0550 0.0332  -0.0327 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3085 0.2651 0.2373 -0.0487 0.0323  -0.0242 47  LYS A C   
417  O O   . LYS A 46  ? 0.2810 0.2278 0.2055 -0.0449 0.0336  -0.0191 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3126 0.2708 0.2411 -0.0636 0.0417  -0.0368 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.3363 0.2980 0.2675 -0.0711 0.0445  -0.0457 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.3218 0.2815 0.2503 -0.0815 0.0540  -0.0516 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.3724 0.3396 0.3062 -0.0899 0.0567  -0.0627 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.3692 0.3362 0.3014 -0.1020 0.0673  -0.0704 47  LYS A NZ  
423  N N   . THR A 47  ? 0.2759 0.2404 0.2076 -0.0475 0.0299  -0.0239 48  THR A N   
424  C CA  . THR A 47  ? 0.2759 0.2371 0.2041 -0.0422 0.0284  -0.0169 48  THR A CA  
425  C C   . THR A 47  ? 0.2802 0.2429 0.2120 -0.0358 0.0237  -0.0138 48  THR A C   
426  O O   . THR A 47  ? 0.2861 0.2434 0.2153 -0.0313 0.0240  -0.0087 48  THR A O   
427  C CB  . THR A 47  ? 0.3469 0.3165 0.2765 -0.0434 0.0272  -0.0183 48  THR A CB  
428  O OG1 . THR A 47  ? 0.3510 0.3338 0.2912 -0.0430 0.0224  -0.0243 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.3659 0.3298 0.2874 -0.0508 0.0344  -0.0202 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2365 0.2057 0.1736 -0.0354 0.0194  -0.0172 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2375 0.2060 0.1756 -0.0317 0.0166  -0.0150 49  VAL A CA  
432  C C   . VAL A 48  ? 0.2685 0.2278 0.2030 -0.0317 0.0207  -0.0138 49  VAL A C   
433  O O   . VAL A 48  ? 0.2498 0.2075 0.1856 -0.0284 0.0217  -0.0113 49  VAL A O   
434  C CB  . VAL A 48  ? 0.2511 0.2238 0.1911 -0.0315 0.0112  -0.0183 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.2590 0.2268 0.1960 -0.0300 0.0105  -0.0164 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.2484 0.2298 0.1935 -0.0304 0.0077  -0.0202 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.2585 0.2132 0.1899 -0.0359 0.0233  -0.0168 50  LEU A N   
438  C CA  . LEU A 49  ? 0.2587 0.2035 0.1862 -0.0367 0.0283  -0.0165 50  LEU A CA  
439  C C   . LEU A 49  ? 0.2969 0.2343 0.2237 -0.0327 0.0325  -0.0123 50  LEU A C   
440  O O   . LEU A 49  ? 0.2960 0.2300 0.2246 -0.0293 0.0345  -0.0113 50  LEU A O   
441  C CB  . LEU A 49  ? 0.2559 0.1972 0.1797 -0.0428 0.0310  -0.0214 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.2895 0.2381 0.2134 -0.0456 0.0252  -0.0265 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.2955 0.2430 0.2173 -0.0521 0.0282  -0.0326 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3147 0.2601 0.2340 -0.0439 0.0221  -0.0254 50  LEU A CD2 
445  N N   . MET A 50  ? 0.2628 0.1976 0.1865 -0.0329 0.0337  -0.0101 51  MET A N   
446  C CA  . MET A 50  ? 0.2789 0.2036 0.1984 -0.0279 0.0359  -0.0049 51  MET A CA  
447  C C   . MET A 50  ? 0.3243 0.2567 0.2500 -0.0201 0.0310  -0.0018 51  MET A C   
448  O O   . MET A 50  ? 0.3180 0.2454 0.2454 -0.0138 0.0317  0.0003  51  MET A O   
449  C CB  . MET A 50  ? 0.3066 0.2253 0.2174 -0.0310 0.0378  -0.0030 51  MET A CB  
450  C CG  . MET A 50  ? 0.3276 0.2387 0.2329 -0.0399 0.0444  -0.0074 51  MET A CG  
451  S SD  . MET A 50  ? 0.3776 0.2875 0.2747 -0.0465 0.0472  -0.0078 51  MET A SD  
452  C CE  . MET A 50  ? 0.3594 0.2441 0.2394 -0.0426 0.0513  0.0006  51  MET A CE  
453  N N   . ALA A 51  ? 0.2767 0.2221 0.2070 -0.0206 0.0261  -0.0027 52  ALA A N   
454  C CA  . ALA A 51  ? 0.2658 0.2209 0.2026 -0.0151 0.0216  -0.0013 52  ALA A CA  
455  C C   . ALA A 51  ? 0.2966 0.2549 0.2412 -0.0132 0.0229  -0.0041 52  ALA A C   
456  O O   . ALA A 51  ? 0.2942 0.2602 0.2460 -0.0082 0.0208  -0.0042 52  ALA A O   
457  C CB  . ALA A 51  ? 0.2617 0.2279 0.2008 -0.0178 0.0176  -0.0029 52  ALA A CB  
458  N N   . CYS A 52  ? 0.2534 0.2068 0.1961 -0.0180 0.0266  -0.0072 53  CYS A N   
459  C CA  . CYS A 52  ? 0.2573 0.2123 0.2045 -0.0187 0.0294  -0.0107 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3041 0.2503 0.2516 -0.0175 0.0354  -0.0124 53  CYS A C   
461  O O   . CYS A 52  ? 0.2795 0.2284 0.2323 -0.0177 0.0388  -0.0163 53  CYS A O   
462  C CB  . CYS A 52  ? 0.2524 0.2067 0.1942 -0.0252 0.0287  -0.0132 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.2782 0.2411 0.2207 -0.0258 0.0225  -0.0127 53  CYS A SG  
464  N N   . SER A 53  ? 0.2773 0.2124 0.2185 -0.0178 0.0378  -0.0107 54  SER A N   
465  C CA  . SER A 53  ? 0.2779 0.2020 0.2174 -0.0184 0.0445  -0.0132 54  SER A CA  
466  C C   . SER A 53  ? 0.3317 0.2434 0.2678 -0.0133 0.0464  -0.0097 54  SER A C   
467  O O   . SER A 53  ? 0.3094 0.2148 0.2370 -0.0158 0.0457  -0.0067 54  SER A O   
468  C CB  . SER A 53  ? 0.3038 0.2232 0.2348 -0.0275 0.0467  -0.0164 54  SER A CB  
469  O OG  . SER A 53  ? 0.3349 0.2417 0.2608 -0.0303 0.0531  -0.0187 54  SER A OG  
470  N N   . GLY A 54  ? 0.3090 0.2156 0.2507 -0.0064 0.0495  -0.0108 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3129 0.2025 0.2490 -0.0002 0.0515  -0.0072 55  GLY A CA  
472  C C   . GLY A 54  ? 0.3575 0.2305 0.2815 -0.0085 0.0584  -0.0083 55  GLY A C   
473  O O   . GLY A 54  ? 0.3517 0.2096 0.2646 -0.0084 0.0597  -0.0041 55  GLY A O   
474  N N   . LEU A 55  ? 0.3278 0.2035 0.2521 -0.0171 0.0629  -0.0145 56  LEU A N   
475  C CA  . LEU A 55  ? 0.3362 0.1994 0.2501 -0.0263 0.0691  -0.0174 56  LEU A CA  
476  C C   . LEU A 55  ? 0.3711 0.2372 0.2781 -0.0330 0.0663  -0.0157 56  LEU A C   
477  O O   . LEU A 55  ? 0.3578 0.2098 0.2555 -0.0366 0.0709  -0.0149 56  LEU A O   
478  C CB  . LEU A 55  ? 0.3309 0.1979 0.2454 -0.0339 0.0730  -0.0247 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4104 0.2661 0.3153 -0.0437 0.0795  -0.0295 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4345 0.2693 0.3360 -0.0409 0.0883  -0.0301 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.3835 0.2460 0.2862 -0.0518 0.0802  -0.0360 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3168 0.2001 0.2281 -0.0347 0.0594  -0.0158 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3015 0.1904 0.2094 -0.0403 0.0568  -0.0159 57  PHE A CA  
484  C C   . PHE A 56  ? 0.3517 0.2335 0.2546 -0.0367 0.0564  -0.0100 57  PHE A C   
485  O O   . PHE A 56  ? 0.3406 0.2174 0.2364 -0.0433 0.0597  -0.0111 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3050 0.2119 0.2188 -0.0416 0.0494  -0.0177 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3123 0.2221 0.2250 -0.0473 0.0494  -0.0235 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.3329 0.2389 0.2410 -0.0551 0.0532  -0.0291 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3182 0.2339 0.2326 -0.0456 0.0457  -0.0239 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.3382 0.2467 0.2434 -0.0601 0.0521  -0.0346 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.3443 0.2599 0.2533 -0.0510 0.0450  -0.0285 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3206 0.2333 0.2250 -0.0576 0.0474  -0.0337 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3181 0.1990 0.2235 -0.0267 0.0529  -0.0046 58  TYR A N   
494  C CA  . TYR A 57  ? 0.3368 0.2083 0.2337 -0.0223 0.0514  0.0020  58  TYR A CA  
495  C C   . TYR A 57  ? 0.3985 0.2450 0.2811 -0.0251 0.0594  0.0035  58  TYR A C   
496  O O   . TYR A 57  ? 0.3776 0.2147 0.2479 -0.0305 0.0620  0.0055  58  TYR A O   
497  C CB  . TYR A 57  ? 0.3578 0.2338 0.2611 -0.0099 0.0452  0.0063  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4057 0.2695 0.2976 -0.0035 0.0421  0.0137  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.4177 0.2847 0.3015 -0.0075 0.0395  0.0163  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.4658 0.3138 0.3538 0.0071  0.0416  0.0178  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.4414 0.2948 0.3103 -0.0022 0.0364  0.0236  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5144 0.3484 0.3883 0.0142  0.0372  0.0255  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.5840 0.4204 0.4471 0.0090  0.0346  0.0287  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.6655 0.4862 0.5112 0.0156  0.0300  0.0366  58  TYR A OH  
505  N N   A SER A 58  ? 0.3784 0.2130 0.2617 -0.0223 0.0642  0.0018  59  SER A N   
506  N N   B SER A 58  ? 0.3761 0.2107 0.2595 -0.0223 0.0642  0.0018  59  SER A N   
507  C CA  A SER A 58  ? 0.3993 0.2071 0.2688 -0.0250 0.0728  0.0024  59  SER A CA  
508  C CA  B SER A 58  ? 0.3968 0.2046 0.2664 -0.0251 0.0729  0.0024  59  SER A CA  
509  C C   A SER A 58  ? 0.4638 0.2695 0.3266 -0.0405 0.0802  -0.0037 59  SER A C   
510  C C   B SER A 58  ? 0.4603 0.2664 0.3232 -0.0405 0.0800  -0.0037 59  SER A C   
511  O O   A SER A 58  ? 0.4945 0.2814 0.3421 -0.0461 0.0863  -0.0019 59  SER A O   
512  O O   B SER A 58  ? 0.4879 0.2757 0.3356 -0.0461 0.0859  -0.0018 59  SER A O   
513  C CB  A SER A 58  ? 0.4291 0.2281 0.3042 -0.0191 0.0766  -0.0002 59  SER A CB  
514  C CB  B SER A 58  ? 0.4263 0.2258 0.3016 -0.0199 0.0769  -0.0007 59  SER A CB  
515  O OG  A SER A 58  ? 0.4665 0.2650 0.3474 -0.0041 0.0705  0.0048  59  SER A OG  
516  O OG  B SER A 58  ? 0.4902 0.2619 0.3516 -0.0232 0.0862  -0.0008 59  SER A OG  
517  N N   . ILE A 59  ? 0.4052 0.2303 0.2787 -0.0474 0.0793  -0.0113 60  ILE A N   
518  C CA  . ILE A 59  ? 0.3955 0.2247 0.2668 -0.0613 0.0844  -0.0192 60  ILE A CA  
519  C C   . ILE A 59  ? 0.4307 0.2654 0.2981 -0.0671 0.0839  -0.0190 60  ILE A C   
520  O O   . ILE A 59  ? 0.4577 0.2798 0.3146 -0.0769 0.0924  -0.0220 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4091 0.2596 0.2921 -0.0651 0.0802  -0.0267 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4071 0.2500 0.2910 -0.0633 0.0838  -0.0292 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.3934 0.2538 0.2771 -0.0779 0.0825  -0.0359 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4310 0.2919 0.3222 -0.0654 0.0784  -0.0343 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.3692 0.2216 0.2442 -0.0620 0.0752  -0.0162 61  PHE A N   
526  C CA  . PHE A 60  ? 0.3637 0.2240 0.2369 -0.0685 0.0754  -0.0182 61  PHE A CA  
527  C C   . PHE A 60  ? 0.4274 0.2688 0.2843 -0.0674 0.0786  -0.0107 61  PHE A C   
528  O O   . PHE A 60  ? 0.4392 0.2849 0.2923 -0.0748 0.0810  -0.0132 61  PHE A O   
529  C CB  . PHE A 60  ? 0.3517 0.2383 0.2394 -0.0656 0.0659  -0.0205 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.3511 0.2526 0.2500 -0.0678 0.0625  -0.0278 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.3902 0.2968 0.2911 -0.0781 0.0667  -0.0374 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.3500 0.2600 0.2561 -0.0602 0.0552  -0.0256 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.3909 0.3104 0.2997 -0.0792 0.0619  -0.0438 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.3792 0.2993 0.2908 -0.0623 0.0515  -0.0314 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.3634 0.2881 0.2759 -0.0711 0.0540  -0.0401 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4140 0.2341 0.2605 -0.0584 0.0788  -0.0024 62  THR A N   
537  C CA  . THR A 61  ? 0.4305 0.2266 0.2560 -0.0572 0.0816  0.0055  62  THR A CA  
538  C C   . THR A 61  ? 0.5279 0.2950 0.3361 -0.0658 0.0939  0.0042  62  THR A C   
539  O O   . THR A 61  ? 0.5330 0.2740 0.3185 -0.0678 0.0987  0.0101  62  THR A O   
540  C CB  . THR A 61  ? 0.5238 0.3129 0.3462 -0.0411 0.0728  0.0156  62  THR A CB  
541  O OG1 . THR A 61  ? 0.4840 0.2678 0.3140 -0.0325 0.0722  0.0159  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.4574 0.2723 0.2921 -0.0353 0.0623  0.0169  62  THR A CG2 
543  N N   . ASP A 62  ? 0.4781 0.2479 0.2946 -0.0720 0.0994  -0.0039 63  ASP A N   
544  C CA  . ASP A 62  ? 0.5117 0.2553 0.3128 -0.0825 0.1124  -0.0073 63  ASP A CA  
545  C C   . ASP A 62  ? 0.5840 0.3318 0.3793 -0.0994 0.1204  -0.0147 63  ASP A C   
546  O O   . ASP A 62  ? 0.5354 0.3136 0.3483 -0.1052 0.1173  -0.0234 63  ASP A O   
547  C CB  . ASP A 62  ? 0.5186 0.2665 0.3309 -0.0851 0.1157  -0.0151 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.6457 0.3680 0.4429 -0.0980 0.1301  -0.0204 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.7210 0.4107 0.5022 -0.0928 0.1351  -0.0141 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.6203 0.3546 0.4213 -0.1133 0.1363  -0.0313 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.6206 0.3369 0.3907 -0.1075 0.1312  -0.0118 64  GLN A N   
552  C CA  . GLN A 63  ? 0.6398 0.3563 0.4013 -0.1253 0.1415  -0.0193 64  GLN A CA  
553  C C   . GLN A 63  ? 0.6643 0.4032 0.4428 -0.1405 0.1483  -0.0359 64  GLN A C   
554  O O   . GLN A 63  ? 0.6826 0.4378 0.4657 -0.1531 0.1530  -0.0452 64  GLN A O   
555  C CB  . GLN A 63  ? 0.7124 0.3844 0.4391 -0.1319 0.1533  -0.0127 64  GLN A CB  
556  C CG  . GLN A 63  ? 0.9319 0.5874 0.6394 -0.1207 0.1460  0.0016  64  GLN A CG  
557  N N   . LEU A 64  ? 0.5658 0.3065 0.3537 -0.1397 0.1488  -0.0407 65  LEU A N   
558  C CA  . LEU A 64  ? 0.5448 0.3099 0.3498 -0.1526 0.1525  -0.0567 65  LEU A CA  
559  C C   . LEU A 64  ? 0.5685 0.3712 0.3998 -0.1436 0.1380  -0.0601 65  LEU A C   
560  O O   . LEU A 64  ? 0.5723 0.4043 0.4198 -0.1508 0.1356  -0.0715 65  LEU A O   
561  C CB  . LEU A 64  ? 0.5662 0.3111 0.3639 -0.1596 0.1626  -0.0618 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.6658 0.3777 0.4400 -0.1757 0.1805  -0.0652 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.6866 0.3804 0.4560 -0.1818 0.1896  -0.0710 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.7175 0.4482 0.4967 -0.1947 0.1887  -0.0790 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.4857 0.2871 0.3209 -0.1284 0.1286  -0.0514 66  LYS A N   
566  C CA  . LYS A 65  ? 0.4474 0.2786 0.3028 -0.1209 0.1161  -0.0542 66  LYS A CA  
567  C C   . LYS A 65  ? 0.5018 0.3565 0.3684 -0.1153 0.1060  -0.0523 66  LYS A C   
568  O O   . LYS A 65  ? 0.4842 0.3650 0.3669 -0.1135 0.0973  -0.0582 66  LYS A O   
569  C CB  . LYS A 65  ? 0.4476 0.2701 0.3035 -0.1085 0.1113  -0.0471 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.4648 0.2673 0.3127 -0.1141 0.1210  -0.0512 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.4526 0.2514 0.3043 -0.1020 0.1163  -0.0461 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.5231 0.2966 0.3653 -0.1051 0.1269  -0.0486 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.5655 0.3055 0.3912 -0.1009 0.1340  -0.0404 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.4936 0.3378 0.3500 -0.1129 0.1072  -0.0447 67  CYS A N   
575  C CA  . CYS A 66  ? 0.4799 0.3444 0.3453 -0.1086 0.0991  -0.0435 67  CYS A CA  
576  C C   . CYS A 66  ? 0.5297 0.4218 0.4110 -0.1182 0.0990  -0.0573 67  CYS A C   
577  O O   . CYS A 66  ? 0.5202 0.4345 0.4152 -0.1127 0.0898  -0.0587 67  CYS A O   
578  C CB  . CYS A 66  ? 0.5118 0.3579 0.3597 -0.1077 0.1025  -0.0347 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.5999 0.4259 0.4285 -0.1265 0.1195  -0.0408 67  CYS A SG  
580  N N   . ASN A 67  ? 0.4805 0.3710 0.3605 -0.1326 0.1094  -0.0684 68  ASN A N   
581  C CA  . ASN A 67  ? 0.4752 0.3930 0.3718 -0.1430 0.1106  -0.0841 68  ASN A CA  
582  C C   . ASN A 67  ? 0.5063 0.4459 0.4198 -0.1425 0.1033  -0.0940 68  ASN A C   
583  O O   . ASN A 67  ? 0.4768 0.4423 0.4067 -0.1492 0.1020  -0.1081 68  ASN A O   
584  C CB  . ASN A 67  ? 0.5068 0.4121 0.3922 -0.1608 0.1272  -0.0924 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.6669 0.5542 0.5348 -0.1623 0.1332  -0.0841 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.6928 0.5494 0.5372 -0.1708 0.1457  -0.0802 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.5572 0.4602 0.4334 -0.1537 0.1242  -0.0806 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.4695 0.3995 0.3789 -0.1346 0.0983  -0.0873 69  LEU A N   
589  C CA  . LEU A 68  ? 0.4401 0.3878 0.3610 -0.1343 0.0909  -0.0955 69  LEU A CA  
590  C C   . LEU A 68  ? 0.4569 0.4281 0.3922 -0.1228 0.0753  -0.0948 69  LEU A C   
591  O O   . LEU A 68  ? 0.4422 0.4085 0.3750 -0.1123 0.0699  -0.0837 69  LEU A O   
592  C CB  . LEU A 68  ? 0.4500 0.3780 0.3599 -0.1311 0.0924  -0.0895 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.5185 0.4201 0.4134 -0.1417 0.1077  -0.0908 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.5249 0.4073 0.4107 -0.1358 0.1085  -0.0842 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.5346 0.4480 0.4351 -0.1581 0.1152  -0.1076 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4093 0.4051 0.3588 -0.1247 0.0676  -0.1068 70  SER A N   
597  N N   B SER A 69  ? 0.4058 0.4017 0.3554 -0.1248 0.0677  -0.1069 70  SER A N   
598  C CA  A SER A 69  ? 0.3937 0.4092 0.3551 -0.1133 0.0519  -0.1066 70  SER A CA  
599  C CA  B SER A 69  ? 0.3891 0.4052 0.3508 -0.1137 0.0520  -0.1072 70  SER A CA  
600  C C   A SER A 69  ? 0.4082 0.4195 0.3633 -0.1067 0.0429  -0.1025 70  SER A C   
601  C C   B SER A 69  ? 0.4065 0.4181 0.3618 -0.1069 0.0429  -0.1028 70  SER A C   
602  O O   A SER A 69  ? 0.3781 0.3974 0.3366 -0.0965 0.0302  -0.0993 70  SER A O   
603  O O   B SER A 69  ? 0.3766 0.3962 0.3353 -0.0966 0.0302  -0.0995 70  SER A O   
604  C CB  A SER A 69  ? 0.4421 0.4875 0.4232 -0.1170 0.0472  -0.1225 70  SER A CB  
605  C CB  B SER A 69  ? 0.4304 0.4763 0.4116 -0.1181 0.0476  -0.1236 70  SER A CB  
606  O OG  A SER A 69  ? 0.5452 0.6004 0.5303 -0.1263 0.0487  -0.1351 70  SER A OG  
607  O OG  B SER A 69  ? 0.4985 0.5503 0.4864 -0.1237 0.0556  -0.1280 70  SER A OG  
608  N N   . VAL A 70  ? 0.3771 0.3741 0.3215 -0.1135 0.0503  -0.1032 71  VAL A N   
609  C CA  . VAL A 70  ? 0.3799 0.3703 0.3156 -0.1101 0.0447  -0.1004 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4066 0.3699 0.3279 -0.1113 0.0558  -0.0917 71  VAL A C   
611  O O   . VAL A 70  ? 0.4001 0.3511 0.3170 -0.1201 0.0684  -0.0944 71  VAL A O   
612  C CB  . VAL A 70  ? 0.4370 0.4423 0.3762 -0.1178 0.0409  -0.1142 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.4453 0.4412 0.3715 -0.1153 0.0359  -0.1110 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.4274 0.4620 0.3836 -0.1149 0.0285  -0.1244 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3285 0.2820 0.2427 -0.1027 0.0513  -0.0823 72  ILE A N   
616  C CA  . ILE A 71  ? 0.3430 0.2738 0.2466 -0.1017 0.0601  -0.0754 72  ILE A CA  
617  C C   . ILE A 71  ? 0.3891 0.3178 0.2853 -0.1018 0.0565  -0.0771 72  ILE A C   
618  O O   . ILE A 71  ? 0.3911 0.3266 0.2863 -0.0956 0.0462  -0.0740 72  ILE A O   
619  C CB  . ILE A 71  ? 0.3656 0.2867 0.2686 -0.0919 0.0606  -0.0634 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.3789 0.2995 0.2852 -0.0928 0.0647  -0.0615 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.3920 0.2933 0.2873 -0.0889 0.0678  -0.0579 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.4209 0.3255 0.3201 -0.1022 0.0780  -0.0647 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.3676 0.2842 0.2566 -0.1094 0.0658  -0.0818 73  ASN A N   
624  C CA  . ASN A 72  ? 0.3719 0.2845 0.2515 -0.1115 0.0645  -0.0844 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4065 0.3007 0.2806 -0.1066 0.0719  -0.0772 73  ASN A C   
626  O O   . ASN A 72  ? 0.3978 0.2767 0.2713 -0.1077 0.0830  -0.0763 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4322 0.3446 0.3077 -0.1239 0.0705  -0.0962 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.6425 0.5762 0.5263 -0.1297 0.0640  -0.1062 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.5140 0.4649 0.4008 -0.1256 0.0502  -0.1079 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.5875 0.5198 0.4750 -0.1396 0.0741  -0.1139 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.3590 0.2538 0.2288 -0.1011 0.0661  -0.0727 74  LEU A N   
632  C CA  . LEU A 73  ? 0.3562 0.2374 0.2236 -0.0970 0.0733  -0.0682 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4165 0.2870 0.2745 -0.1049 0.0819  -0.0752 74  LEU A C   
634  O O   . LEU A 73  ? 0.4161 0.2910 0.2666 -0.1133 0.0795  -0.0828 74  LEU A O   
635  C CB  . LEU A 73  ? 0.3446 0.2297 0.2107 -0.0903 0.0663  -0.0619 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.3726 0.2678 0.2475 -0.0822 0.0580  -0.0550 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.3823 0.2765 0.2556 -0.0767 0.0556  -0.0496 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.3521 0.2450 0.2366 -0.0785 0.0627  -0.0517 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.3885 0.2460 0.2476 -0.1018 0.0914  -0.0737 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4025 0.2483 0.2539 -0.1085 0.1015  -0.0809 75  ASP A CA  
641  C C   . ASP A 74  ? 0.4530 0.3043 0.2908 -0.1152 0.0959  -0.0850 75  ASP A C   
642  O O   . ASP A 74  ? 0.4397 0.2973 0.2749 -0.1110 0.0878  -0.0798 75  ASP A O   
643  C CB  . ASP A 74  ? 0.4180 0.2534 0.2761 -0.1011 0.1102  -0.0783 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.5238 0.3459 0.3772 -0.1067 0.1227  -0.0865 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.5351 0.3585 0.3781 -0.1139 0.1236  -0.0918 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.5158 0.3245 0.3747 -0.1036 0.1317  -0.0876 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.4676 0.3153 0.2945 -0.1258 0.0996  -0.0940 76  PRO A N   
648  C CA  . PRO A 75  ? 0.4821 0.3334 0.2920 -0.1320 0.0927  -0.0973 76  PRO A CA  
649  C C   . PRO A 75  ? 0.5237 0.3675 0.3247 -0.1312 0.0962  -0.0950 76  PRO A C   
650  O O   . PRO A 75  ? 0.5374 0.3819 0.3215 -0.1348 0.0887  -0.0948 76  PRO A O   
651  C CB  . PRO A 75  ? 0.5241 0.3719 0.3250 -0.1441 0.0984  -0.1085 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.5841 0.4209 0.3960 -0.1444 0.1122  -0.1112 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5022 0.3414 0.3297 -0.1333 0.1099  -0.1019 76  PRO A CD  
654  N N   . GLU A 76  ? 0.4846 0.3209 0.2962 -0.1266 0.1073  -0.0938 77  GLU A N   
655  C CA  . GLU A 76  ? 0.5064 0.3379 0.3132 -0.1267 0.1128  -0.0937 77  GLU A CA  
656  C C   . GLU A 76  ? 0.4996 0.3385 0.3082 -0.1196 0.1030  -0.0847 77  GLU A C   
657  O O   . GLU A 76  ? 0.4983 0.3338 0.2984 -0.1219 0.1054  -0.0845 77  GLU A O   
658  C CB  . GLU A 76  ? 0.5371 0.3617 0.3594 -0.1223 0.1269  -0.0968 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.7907 0.6094 0.6073 -0.1275 0.1378  -0.1032 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.1299 0.9385 0.9322 -0.1396 0.1473  -0.1138 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.1362 0.9379 0.9470 -0.1393 0.1558  -0.1190 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.0427 0.8484 0.8233 -0.1497 0.1462  -0.1169 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.4315 0.2796 0.2506 -0.1120 0.0932  -0.0781 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4170 0.2717 0.2389 -0.1052 0.0845  -0.0702 78  ILE A CA  
665  C C   . ILE A 77  ? 0.4687 0.3224 0.2702 -0.1092 0.0741  -0.0686 78  ILE A C   
666  O O   . ILE A 77  ? 0.4612 0.3177 0.2539 -0.1122 0.0657  -0.0707 78  ILE A O   
667  C CB  . ILE A 77  ? 0.4346 0.2987 0.2737 -0.0961 0.0785  -0.0645 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.4329 0.2935 0.2882 -0.0910 0.0884  -0.0649 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4069 0.2777 0.2486 -0.0897 0.0699  -0.0572 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.4846 0.3426 0.3482 -0.0869 0.0971  -0.0655 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.4735 0.3225 0.2673 -0.1092 0.0746  -0.0655 79  ASN A N   
672  C CA  . ASN A 78  ? 0.4958 0.3378 0.2661 -0.1124 0.0657  -0.0624 79  ASN A CA  
673  C C   . ASN A 78  ? 0.4890 0.3387 0.2640 -0.1037 0.0512  -0.0552 79  ASN A C   
674  O O   . ASN A 78  ? 0.4548 0.3107 0.2459 -0.0970 0.0518  -0.0510 79  ASN A O   
675  C CB  . ASN A 78  ? 0.5166 0.3482 0.2767 -0.1174 0.0750  -0.0627 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.6936 0.5123 0.4251 -0.1213 0.0671  -0.0586 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.5695 0.3865 0.3004 -0.1173 0.0630  -0.0528 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.6126 0.4204 0.3181 -0.1292 0.0643  -0.0615 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.4710 0.3215 0.2330 -0.1032 0.0376  -0.0547 80  PRO A N   
680  C CA  . PRO A 79  ? 0.4534 0.3119 0.2219 -0.0941 0.0240  -0.0492 80  PRO A CA  
681  C C   . PRO A 79  ? 0.4912 0.3412 0.2533 -0.0905 0.0225  -0.0423 80  PRO A C   
682  O O   . PRO A 79  ? 0.4643 0.3231 0.2423 -0.0829 0.0184  -0.0385 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5011 0.3600 0.2537 -0.0946 0.0102  -0.0516 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.5660 0.4241 0.3132 -0.1039 0.0174  -0.0596 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5208 0.3666 0.2633 -0.1103 0.0334  -0.0600 80  PRO A CD  
686  N N   . GLU A 80  ? 0.4678 0.3001 0.2060 -0.0974 0.0269  -0.0414 81  GLU A N   
687  C CA  . GLU A 80  ? 0.4707 0.2928 0.2010 -0.0963 0.0276  -0.0359 81  GLU A CA  
688  C C   . GLU A 80  ? 0.4815 0.3140 0.2373 -0.0942 0.0386  -0.0362 81  GLU A C   
689  O O   . GLU A 80  ? 0.4497 0.2860 0.2144 -0.0883 0.0348  -0.0319 81  GLU A O   
690  C CB  . GLU A 80  ? 0.5212 0.3198 0.2177 -0.1062 0.0320  -0.0357 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.5948 0.3805 0.2808 -0.1057 0.0319  -0.0300 81  GLU A CG  
692  C CD  . GLU A 80  ? 0.8847 0.6448 0.5372 -0.1174 0.0401  -0.0298 81  GLU A CD  
693  O OE1 . GLU A 80  ? 0.8623 0.6044 0.4942 -0.1167 0.0345  -0.0238 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 0.7903 0.5469 0.4366 -0.1277 0.0528  -0.0360 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.4523 0.2899 0.2202 -0.0982 0.0514  -0.0419 82  GLY A N   
696  C CA  . GLY A 81  ? 0.4313 0.2805 0.2246 -0.0946 0.0603  -0.0430 82  GLY A CA  
697  C C   . GLY A 81  ? 0.4294 0.2934 0.2443 -0.0843 0.0525  -0.0392 82  GLY A C   
698  O O   . GLY A 81  ? 0.3883 0.2594 0.2166 -0.0794 0.0525  -0.0365 82  GLY A O   
699  N N   . PHE A 82  ? 0.3741 0.2429 0.1914 -0.0821 0.0459  -0.0396 83  PHE A N   
700  C CA  . PHE A 82  ? 0.3451 0.2269 0.1804 -0.0741 0.0394  -0.0369 83  PHE A CA  
701  C C   . PHE A 82  ? 0.3751 0.2579 0.2071 -0.0693 0.0290  -0.0319 83  PHE A C   
702  O O   . PHE A 82  ? 0.3509 0.2423 0.1977 -0.0636 0.0279  -0.0292 83  PHE A O   
703  C CB  . PHE A 82  ? 0.3625 0.2495 0.2002 -0.0749 0.0357  -0.0403 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.3521 0.2515 0.2076 -0.0685 0.0317  -0.0385 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.3876 0.2903 0.2580 -0.0657 0.0392  -0.0376 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.3638 0.2707 0.2204 -0.0647 0.0203  -0.0374 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.3893 0.3010 0.2723 -0.0608 0.0360  -0.0353 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.3737 0.2919 0.2461 -0.0600 0.0182  -0.0365 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.3581 0.2779 0.2421 -0.0588 0.0263  -0.0351 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.3921 0.2648 0.2038 -0.0711 0.0211  -0.0309 84  CYS A N   
711  C CA  . CYS A 83  ? 0.4135 0.2833 0.2198 -0.0657 0.0109  -0.0263 84  CYS A CA  
712  C C   . CYS A 83  ? 0.4232 0.2897 0.2329 -0.0656 0.0167  -0.0233 84  CYS A C   
713  O O   . CYS A 83  ? 0.3947 0.2681 0.2155 -0.0595 0.0122  -0.0208 84  CYS A O   
714  C CB  . CYS A 83  ? 0.4659 0.3203 0.2452 -0.0674 0.0017  -0.0252 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.5365 0.3850 0.3087 -0.0582 -0.0130 -0.0200 84  CYS A SG  
716  N N   . ILE A 84  ? 0.3974 0.2545 0.1982 -0.0731 0.0277  -0.0250 85  ILE A N   
717  C CA  . ILE A 84  ? 0.3766 0.2322 0.1812 -0.0752 0.0351  -0.0246 85  ILE A CA  
718  C C   . ILE A 84  ? 0.3724 0.2477 0.2057 -0.0691 0.0374  -0.0252 85  ILE A C   
719  O O   . ILE A 84  ? 0.3636 0.2435 0.2045 -0.0661 0.0358  -0.0233 85  ILE A O   
720  C CB  . ILE A 84  ? 0.4219 0.2673 0.2146 -0.0857 0.0480  -0.0291 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.4503 0.2712 0.2078 -0.0926 0.0451  -0.0269 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4141 0.2667 0.2209 -0.0882 0.0582  -0.0322 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.5205 0.3300 0.2618 -0.1041 0.0570  -0.0321 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3257 0.2107 0.1727 -0.0672 0.0407  -0.0277 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3083 0.2086 0.1787 -0.0608 0.0421  -0.0274 86  LEU A CA  
726  C C   . LEU A 85  ? 0.3452 0.2533 0.2228 -0.0543 0.0326  -0.0237 86  LEU A C   
727  O O   . LEU A 85  ? 0.3175 0.2351 0.2082 -0.0500 0.0321  -0.0223 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3119 0.2156 0.1919 -0.0604 0.0489  -0.0307 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.3737 0.2743 0.2540 -0.0654 0.0603  -0.0361 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.3723 0.2729 0.2597 -0.0645 0.0663  -0.0396 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.3748 0.2857 0.2699 -0.0630 0.0642  -0.0377 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3173 0.2231 0.1875 -0.0537 0.0251  -0.0233 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3054 0.2200 0.1836 -0.0482 0.0167  -0.0216 87  LEU A CA  
734  C C   . LEU A 86  ? 0.3459 0.2582 0.2214 -0.0457 0.0123  -0.0190 87  LEU A C   
735  O O   . LEU A 86  ? 0.3118 0.2335 0.1994 -0.0417 0.0105  -0.0179 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3098 0.2242 0.1816 -0.0484 0.0094  -0.0239 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.3469 0.2732 0.2298 -0.0433 0.0016  -0.0248 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.3345 0.2713 0.2333 -0.0425 0.0072  -0.0252 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.3727 0.3015 0.2508 -0.0435 -0.0064 -0.0291 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3274 0.2251 0.1851 -0.0490 0.0113  -0.0180 88  ASP A N   
741  C CA  . ASP A 87  ? 0.3345 0.2256 0.1867 -0.0480 0.0090  -0.0157 88  ASP A CA  
742  C C   . ASP A 87  ? 0.3475 0.2477 0.2137 -0.0491 0.0166  -0.0165 88  ASP A C   
743  O O   . ASP A 87  ? 0.3450 0.2500 0.2181 -0.0460 0.0138  -0.0156 88  ASP A O   
744  C CB  . ASP A 87  ? 0.3829 0.2522 0.2095 -0.0534 0.0094  -0.0144 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.5349 0.3936 0.3449 -0.0502 -0.0020 -0.0128 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.5326 0.4028 0.3540 -0.0430 -0.0108 -0.0136 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.5315 0.3704 0.3165 -0.0549 -0.0022 -0.0114 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3260 0.2290 0.1967 -0.0533 0.0260  -0.0191 89  PHE A N   
749  C CA  . PHE A 88  ? 0.2888 0.2039 0.1754 -0.0532 0.0321  -0.0212 89  PHE A CA  
750  C C   . PHE A 88  ? 0.2837 0.2142 0.1876 -0.0459 0.0275  -0.0197 89  PHE A C   
751  O O   . PHE A 88  ? 0.2713 0.2102 0.1839 -0.0442 0.0269  -0.0199 89  PHE A O   
752  C CB  . PHE A 88  ? 0.2941 0.2120 0.1859 -0.0568 0.0418  -0.0256 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.2839 0.2184 0.1962 -0.0536 0.0455  -0.0285 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3143 0.2534 0.2303 -0.0572 0.0489  -0.0316 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3107 0.2558 0.2376 -0.0467 0.0445  -0.0279 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.2927 0.2502 0.2290 -0.0535 0.0505  -0.0352 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3306 0.2909 0.2753 -0.0419 0.0455  -0.0301 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3000 0.2681 0.2503 -0.0450 0.0479  -0.0341 89  PHE A CZ  
759  N N   . MET A 89  ? 0.2562 0.1900 0.1639 -0.0426 0.0252  -0.0187 90  MET A N   
760  C CA  . MET A 89  ? 0.2394 0.1847 0.1596 -0.0372 0.0220  -0.0171 90  MET A CA  
761  C C   . MET A 89  ? 0.2906 0.2395 0.2120 -0.0351 0.0160  -0.0160 90  MET A C   
762  O O   . MET A 89  ? 0.2768 0.2354 0.2075 -0.0324 0.0154  -0.0155 90  MET A O   
763  C CB  . MET A 89  ? 0.2460 0.1902 0.1654 -0.0364 0.0207  -0.0169 90  MET A CB  
764  C CG  . MET A 89  ? 0.2664 0.2067 0.1862 -0.0378 0.0273  -0.0183 90  MET A CG  
765  S SD  . MET A 89  ? 0.3130 0.2517 0.2319 -0.0384 0.0269  -0.0189 90  MET A SD  
766  C CE  . MET A 89  ? 0.3280 0.2571 0.2428 -0.0417 0.0355  -0.0218 90  MET A CE  
767  N N   . TYR A 90  ? 0.2566 0.1974 0.1680 -0.0357 0.0110  -0.0159 91  TYR A N   
768  C CA  . TYR A 90  ? 0.2548 0.1977 0.1677 -0.0328 0.0050  -0.0158 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3092 0.2455 0.2169 -0.0346 0.0059  -0.0158 91  TYR A C   
770  O O   . TYR A 90  ? 0.2986 0.2352 0.2076 -0.0320 0.0016  -0.0161 91  TYR A O   
771  C CB  . TYR A 90  ? 0.2778 0.2158 0.1843 -0.0305 -0.0023 -0.0167 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.2839 0.2331 0.2000 -0.0290 -0.0039 -0.0189 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3036 0.2523 0.2182 -0.0317 -0.0007 -0.0197 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.2882 0.2479 0.2144 -0.0259 -0.0073 -0.0212 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.2976 0.2549 0.2197 -0.0321 -0.0007 -0.0226 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.2888 0.2582 0.2229 -0.0264 -0.0073 -0.0247 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.3216 0.2894 0.2532 -0.0299 -0.0036 -0.0251 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.2856 0.2618 0.2239 -0.0320 -0.0024 -0.0295 91  TYR A OH  
779  N N   . THR A 91  ? 0.2721 0.2018 0.1737 -0.0397 0.0122  -0.0163 92  THR A N   
780  C CA  . THR A 91  ? 0.2854 0.2064 0.1797 -0.0436 0.0146  -0.0171 92  THR A CA  
781  C C   . THR A 91  ? 0.3115 0.2400 0.2132 -0.0488 0.0231  -0.0206 92  THR A C   
782  O O   . THR A 91  ? 0.3010 0.2256 0.1997 -0.0528 0.0256  -0.0226 92  THR A O   
783  C CB  . THR A 91  ? 0.3417 0.2395 0.2130 -0.0475 0.0142  -0.0156 92  THR A CB  
784  O OG1 . THR A 91  ? 0.3429 0.2365 0.2080 -0.0531 0.0210  -0.0168 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.3387 0.2280 0.2011 -0.0414 0.0039  -0.0131 92  THR A CG2 
786  N N   A SER A 92  ? 0.2650 0.2039 0.1766 -0.0488 0.0275  -0.0223 93  SER A N   
787  N N   B SER A 92  ? 0.2637 0.2022 0.1749 -0.0489 0.0276  -0.0223 93  SER A N   
788  C CA  A SER A 92  ? 0.2572 0.2062 0.1789 -0.0527 0.0354  -0.0274 93  SER A CA  
789  C CA  B SER A 92  ? 0.2575 0.2062 0.1790 -0.0527 0.0353  -0.0274 93  SER A CA  
790  C C   A SER A 92  ? 0.3005 0.2352 0.2083 -0.0620 0.0436  -0.0307 93  SER A C   
791  C C   B SER A 92  ? 0.3172 0.2517 0.2248 -0.0623 0.0437  -0.0307 93  SER A C   
792  O O   A SER A 92  ? 0.2852 0.2286 0.2019 -0.0665 0.0516  -0.0367 93  SER A O   
793  O O   B SER A 92  ? 0.3135 0.2565 0.2296 -0.0673 0.0516  -0.0370 93  SER A O   
794  C CB  A SER A 92  ? 0.2606 0.2223 0.1933 -0.0531 0.0353  -0.0305 93  SER A CB  
795  C CB  B SER A 92  ? 0.2725 0.2359 0.2068 -0.0519 0.0345  -0.0301 93  SER A CB  
796  O OG  A SER A 92  ? 0.2242 0.1964 0.1655 -0.0461 0.0281  -0.0277 93  SER A OG  
797  O OG  B SER A 92  ? 0.3118 0.2659 0.2370 -0.0588 0.0376  -0.0325 93  SER A OG  
798  N N   A ARG A 93  ? 0.2969 0.2100 0.1827 -0.0649 0.0417  -0.0271 94  ARG A N   
799  N N   B ARG A 93  ? 0.2994 0.2127 0.1853 -0.0649 0.0418  -0.0272 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3118 0.2064 0.1780 -0.0749 0.0495  -0.0293 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3179 0.2117 0.1833 -0.0748 0.0491  -0.0290 94  ARG A CA  
802  C C   A ARG A 93  ? 0.3665 0.2553 0.2251 -0.0761 0.0515  -0.0290 94  ARG A C   
803  C C   B ARG A 93  ? 0.3723 0.2600 0.2297 -0.0763 0.0514  -0.0289 94  ARG A C   
804  O O   A ARG A 93  ? 0.3403 0.2254 0.1940 -0.0705 0.0436  -0.0246 94  ARG A O   
805  O O   B ARG A 93  ? 0.3580 0.2415 0.2098 -0.0709 0.0435  -0.0245 94  ARG A O   
806  C CB  A ARG A 93  ? 0.3613 0.2313 0.2030 -0.0775 0.0457  -0.0252 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.3511 0.2210 0.1929 -0.0763 0.0442  -0.0245 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4390 0.3109 0.2856 -0.0780 0.0454  -0.0264 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.4330 0.3062 0.2811 -0.0752 0.0424  -0.0251 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.5398 0.3872 0.3646 -0.0756 0.0380  -0.0209 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.4889 0.3533 0.3291 -0.0869 0.0534  -0.0303 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.6736 0.4913 0.4676 -0.0834 0.0419  -0.0190 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.5306 0.3986 0.3772 -0.0868 0.0524  -0.0319 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.8236 0.6231 0.6012 -0.0942 0.0512  -0.0214 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.6990 0.5428 0.5256 -0.0898 0.0519  -0.0298 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.6779 0.4882 0.4691 -0.0985 0.0572  -0.0267 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.5550 0.4034 0.3893 -0.0902 0.0520  -0.0325 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.6692 0.4386 0.4147 -0.1018 0.0548  -0.0190 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5173 0.3304 0.3145 -0.0925 0.0512  -0.0250 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.3366 0.2253 0.1947 -0.0843 0.0627  -0.0350 95  LEU A N   
821  C CA  . LEU A 94  ? 0.3383 0.2214 0.1893 -0.0871 0.0670  -0.0366 95  LEU A CA  
822  C C   . LEU A 94  ? 0.4215 0.2802 0.2433 -0.0989 0.0738  -0.0377 95  LEU A C   
823  O O   . LEU A 94  ? 0.4090 0.2649 0.2280 -0.1087 0.0846  -0.0435 95  LEU A O   
824  C CB  . LEU A 94  ? 0.3342 0.2380 0.2100 -0.0860 0.0749  -0.0439 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.3751 0.2756 0.2482 -0.0876 0.0800  -0.0466 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.3528 0.2531 0.2263 -0.0789 0.0702  -0.0404 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.3997 0.3183 0.2968 -0.0871 0.0895  -0.0557 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4188 0.2596 0.2178 -0.0988 0.0679  -0.0328 96  ASN A N   
829  C CA  . ASN A 95  ? 0.4570 0.2706 0.2223 -0.1100 0.0732  -0.0326 96  ASN A CA  
830  C C   . ASN A 95  ? 0.5134 0.3289 0.2783 -0.1183 0.0854  -0.0399 96  ASN A C   
831  O O   . ASN A 95  ? 0.5143 0.3223 0.2666 -0.1185 0.0826  -0.0386 96  ASN A O   
832  C CB  . ASN A 95  ? 0.5348 0.3282 0.2743 -0.1052 0.0595  -0.0243 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.7553 0.5164 0.4544 -0.1157 0.0627  -0.0225 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.6616 0.4102 0.3478 -0.1277 0.0753  -0.0262 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.6851 0.4319 0.3625 -0.1119 0.0514  -0.0174 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.4743 0.3025 0.2557 -0.1247 0.0987  -0.0487 97  LEU A N   
837  C CA  . LEU A 96  ? 0.4884 0.3220 0.2753 -0.1322 0.1119  -0.0580 97  LEU A CA  
838  C C   . LEU A 96  ? 0.5540 0.3629 0.3086 -0.1490 0.1239  -0.0617 97  LEU A C   
839  O O   . LEU A 96  ? 0.5472 0.3482 0.2935 -0.1576 0.1307  -0.0640 97  LEU A O   
840  C CB  . LEU A 96  ? 0.4799 0.3433 0.3050 -0.1285 0.1188  -0.0668 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.5493 0.4270 0.3933 -0.1288 0.1285  -0.0764 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.5547 0.4313 0.3995 -0.1197 0.1205  -0.0713 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5234 0.4306 0.4051 -0.1227 0.1320  -0.0845 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.5304 0.3241 0.2629 -0.1545 0.1261  -0.0619 98  ARG A N   
845  C CA  . ARG A 97  ? 0.5762 0.3421 0.2713 -0.1712 0.1370  -0.0645 98  ARG A CA  
846  C C   . ARG A 97  ? 0.5948 0.3653 0.2924 -0.1792 0.1500  -0.0746 98  ARG A C   
847  O O   . ARG A 97  ? 0.5511 0.3386 0.2703 -0.1700 0.1462  -0.0760 98  ARG A O   
848  C CB  . ARG A 97  ? 0.6329 0.3677 0.2868 -0.1703 0.1236  -0.0527 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.7058 0.4324 0.3546 -0.1618 0.1105  -0.0430 98  ARG A CG  
850  C CD  . ARG A 97  ? 0.9519 0.6493 0.5626 -0.1583 0.0955  -0.0321 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.1971 0.8586 0.7613 -0.1734 0.1033  -0.0315 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.4763 1.1099 1.0125 -0.1820 0.1081  -0.0287 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.3413 0.9399 0.8319 -0.1967 0.1159  -0.0280 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.3452 0.9842 0.8970 -0.1769 0.1059  -0.0268 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.5811 0.3355 0.2563 -0.1970 0.1665  -0.0823 99  GLU A N   
856  C CA  . GLU A 98  ? 0.5834 0.3410 0.2595 -0.2061 0.1806  -0.0935 99  GLU A CA  
857  C C   . GLU A 98  ? 0.6395 0.3901 0.3028 -0.2003 0.1705  -0.0881 99  GLU A C   
858  O O   . GLU A 98  ? 0.6279 0.3950 0.3132 -0.1973 0.1755  -0.0955 99  GLU A O   
859  C CB  . GLU A 98  ? 0.6422 0.3753 0.2840 -0.2283 0.1987  -0.1006 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.7652 0.5023 0.4085 -0.2397 0.2159  -0.1144 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.1475 0.8584 0.7532 -0.2635 0.2350  -0.1219 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.0491 0.7239 0.6062 -0.2713 0.2300  -0.1117 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.1395 0.8654 0.7639 -0.2744 0.2551  -0.1386 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.6368 0.3637 0.2659 -0.1982 0.1559  -0.0760 100 GLY A N   
865  C CA  . GLY A 99  ? 0.6556 0.3755 0.2693 -0.1938 0.1448  -0.0713 100 GLY A CA  
866  C C   . GLY A 99  ? 0.6539 0.3982 0.3009 -0.1767 0.1319  -0.0682 100 GLY A C   
867  O O   . GLY A 99  ? 0.6511 0.3958 0.2938 -0.1748 0.1271  -0.0685 100 GLY A O   
868  N N   . ASN A 100 ? 0.5792 0.3433 0.2583 -0.1652 0.1269  -0.0657 101 ASN A N   
869  C CA  . ASN A 100 ? 0.5341 0.3186 0.2416 -0.1500 0.1154  -0.0623 101 ASN A CA  
870  C C   . ASN A 100 ? 0.5465 0.3576 0.2961 -0.1433 0.1230  -0.0692 101 ASN A C   
871  O O   . ASN A 100 ? 0.5183 0.3434 0.2891 -0.1320 0.1155  -0.0669 101 ASN A O   
872  C CB  . ASN A 100 ? 0.5283 0.3109 0.2329 -0.1396 0.0980  -0.0513 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.6263 0.4160 0.3458 -0.1366 0.0992  -0.0498 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.4854 0.2923 0.2311 -0.1370 0.1094  -0.0567 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.5382 0.3160 0.2428 -0.1328 0.0880  -0.0415 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5037 0.3218 0.2654 -0.1498 0.1373  -0.0777 102 ILE A N   
877  C CA  . ILE A 101 ? 0.4786 0.3231 0.2811 -0.1414 0.1422  -0.0843 102 ILE A CA  
878  C C   . ILE A 101 ? 0.4795 0.3338 0.3006 -0.1347 0.1443  -0.0887 102 ILE A C   
879  O O   . ILE A 101 ? 0.4395 0.3107 0.2886 -0.1216 0.1387  -0.0870 102 ILE A O   
880  C CB  . ILE A 101 ? 0.5253 0.3787 0.3397 -0.1501 0.1575  -0.0954 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5021 0.3854 0.3604 -0.1379 0.1579  -0.1010 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.5378 0.3801 0.3359 -0.1659 0.1746  -0.1064 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.5233 0.4206 0.3971 -0.1424 0.1654  -0.1087 102 ILE A CD1 
884  N N   . MET A 102 ? 0.4675 0.3097 0.2716 -0.1438 0.1523  -0.0941 103 MET A N   
885  C CA  . MET A 102 ? 0.4649 0.3135 0.2850 -0.1383 0.1552  -0.0988 103 MET A CA  
886  C C   . MET A 102 ? 0.4948 0.3439 0.3168 -0.1274 0.1402  -0.0891 103 MET A C   
887  O O   . MET A 102 ? 0.4599 0.3204 0.3067 -0.1166 0.1389  -0.0896 103 MET A O   
888  C CB  . MET A 102 ? 0.5263 0.3616 0.3269 -0.1517 0.1680  -0.1079 103 MET A CB  
889  C CG  . MET A 102 ? 0.6082 0.4456 0.4112 -0.1633 0.1858  -0.1203 103 MET A CG  
890  S SD  . MET A 102 ? 0.6541 0.5211 0.5068 -0.1526 0.1937  -0.1306 103 MET A SD  
891  C CE  . MET A 102 ? 0.6293 0.5002 0.5009 -0.1457 0.1999  -0.1387 103 MET A CE  
892  N N   . ALA A 103 ? 0.4820 0.3185 0.2779 -0.1299 0.1287  -0.0806 104 ALA A N   
893  C CA  . ALA A 103 ? 0.4752 0.3141 0.2732 -0.1211 0.1149  -0.0731 104 ALA A CA  
894  C C   . ALA A 103 ? 0.4718 0.3252 0.2933 -0.1087 0.1067  -0.0670 104 ALA A C   
895  O O   . ALA A 103 ? 0.4387 0.2997 0.2756 -0.1002 0.1021  -0.0648 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5082 0.3329 0.2751 -0.1257 0.1038  -0.0671 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4074 0.2634 0.2300 -0.1087 0.1057  -0.0646 105 VAL A N   
898  C CA  . VAL A 104 ? 0.3687 0.2389 0.2125 -0.0978 0.0983  -0.0595 105 VAL A CA  
899  C C   . VAL A 104 ? 0.3954 0.2809 0.2689 -0.0897 0.1039  -0.0640 105 VAL A C   
900  O O   . VAL A 104 ? 0.3675 0.2605 0.2545 -0.0797 0.0965  -0.0592 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4103 0.2789 0.2476 -0.1010 0.0973  -0.0573 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.3720 0.2577 0.2337 -0.0910 0.0920  -0.0544 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.4317 0.2833 0.2402 -0.1044 0.0877  -0.0503 105 VAL A CG2 
904  N N   A MET A 105 ? 0.3718 0.2610 0.2545 -0.0938 0.1167  -0.0736 106 MET A N   
905  N N   B MET A 105 ? 0.3749 0.2642 0.2577 -0.0938 0.1167  -0.0736 106 MET A N   
906  C CA  A MET A 105 ? 0.3660 0.2693 0.2774 -0.0845 0.1213  -0.0789 106 MET A CA  
907  C CA  B MET A 105 ? 0.3725 0.2759 0.2841 -0.0841 0.1208  -0.0786 106 MET A CA  
908  C C   A MET A 105 ? 0.4172 0.3153 0.3319 -0.0781 0.1194  -0.0771 106 MET A C   
909  C C   B MET A 105 ? 0.4096 0.3076 0.3242 -0.0780 0.1192  -0.0769 106 MET A C   
910  O O   A MET A 105 ? 0.3962 0.3015 0.3280 -0.0663 0.1143  -0.0737 106 MET A O   
911  O O   B MET A 105 ? 0.3779 0.2829 0.3096 -0.0662 0.1143  -0.0736 106 MET A O   
912  C CB  A MET A 105 ? 0.4067 0.3152 0.3273 -0.0908 0.1361  -0.0917 106 MET A CB  
913  C CB  B MET A 105 ? 0.4108 0.3206 0.3334 -0.0896 0.1353  -0.0912 106 MET A CB  
914  C CG  A MET A 105 ? 0.4433 0.3686 0.3964 -0.0789 0.1390  -0.0979 106 MET A CG  
915  C CG  B MET A 105 ? 0.4435 0.3698 0.3985 -0.0770 0.1374  -0.0968 106 MET A CG  
916  S SD  A MET A 105 ? 0.5050 0.4392 0.4728 -0.0859 0.1572  -0.1158 106 MET A SD  
917  S SD  B MET A 105 ? 0.4895 0.4298 0.4638 -0.0826 0.1539  -0.1143 106 MET A SD  
918  C CE  A MET A 105 ? 0.4577 0.4038 0.4583 -0.0674 0.1558  -0.1197 106 MET A CE  
919  C CE  B MET A 105 ? 0.4800 0.4022 0.4374 -0.0936 0.1675  -0.1224 106 MET A CE  
920  N N   . ALA A 106 ? 0.3972 0.2816 0.2936 -0.0865 0.1236  -0.0796 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4086 0.2859 0.3054 -0.0833 0.1236  -0.0793 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4185 0.2966 0.3144 -0.0765 0.1108  -0.0693 107 ALA A C   
923  O O   . ALA A 106 ? 0.3966 0.2743 0.3037 -0.0685 0.1097  -0.0675 107 ALA A O   
924  C CB  . ALA A 106 ? 0.4421 0.3059 0.3167 -0.0957 0.1295  -0.0843 107 ALA A CB  
925  N N   . THR A 107 ? 0.3687 0.2469 0.2511 -0.0796 0.1014  -0.0633 108 THR A N   
926  C CA  . THR A 107 ? 0.3622 0.2434 0.2453 -0.0740 0.0900  -0.0555 108 THR A CA  
927  C C   . THR A 107 ? 0.3795 0.2715 0.2826 -0.0630 0.0866  -0.0514 108 THR A C   
928  O O   . THR A 107 ? 0.3482 0.2404 0.2571 -0.0571 0.0829  -0.0476 108 THR A O   
929  C CB  . THR A 107 ? 0.4222 0.3008 0.2872 -0.0787 0.0804  -0.0513 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4165 0.2841 0.2608 -0.0886 0.0833  -0.0554 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4131 0.2959 0.2797 -0.0743 0.0699  -0.0462 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3351 0.2358 0.2475 -0.0610 0.0883  -0.0527 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3084 0.2211 0.2392 -0.0507 0.0841  -0.0496 109 ALA A CA  
934  C C   . ALA A 108 ? 0.3515 0.2640 0.2970 -0.0419 0.0881  -0.0517 109 ALA A C   
935  O O   . ALA A 108 ? 0.3371 0.2522 0.2902 -0.0328 0.0822  -0.0463 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3142 0.2375 0.2522 -0.0521 0.0859  -0.0527 109 ALA A CB  
937  N N   . MET A 109 ? 0.3323 0.2390 0.2795 -0.0446 0.0981  -0.0593 110 MET A N   
938  C CA  . MET A 109 ? 0.3192 0.2222 0.2791 -0.0351 0.1017  -0.0613 110 MET A CA  
939  C C   . MET A 109 ? 0.3635 0.2527 0.3136 -0.0335 0.0984  -0.0551 110 MET A C   
940  O O   . MET A 109 ? 0.3637 0.2500 0.3201 -0.0235 0.0946  -0.0504 110 MET A O   
941  C CB  . MET A 109 ? 0.3536 0.2530 0.3176 -0.0392 0.1142  -0.0722 110 MET A CB  
942  C CG  . MET A 109 ? 0.4030 0.3180 0.3823 -0.0393 0.1193  -0.0805 110 MET A CG  
943  S SD  . MET A 109 ? 0.4978 0.4080 0.4769 -0.0490 0.1360  -0.0948 110 MET A SD  
944  C CE  . MET A 109 ? 0.4694 0.3718 0.4644 -0.0349 0.1390  -0.0975 110 MET A CE  
945  N N   . TYR A 110 ? 0.3490 0.2300 0.2823 -0.0440 0.0994  -0.0554 111 TYR A N   
946  C CA  . TYR A 110 ? 0.3487 0.2186 0.2723 -0.0458 0.0975  -0.0519 111 TYR A CA  
947  C C   . TYR A 110 ? 0.3798 0.2551 0.3046 -0.0406 0.0876  -0.0433 111 TYR A C   
948  O O   . TYR A 110 ? 0.3732 0.2399 0.2976 -0.0362 0.0872  -0.0396 111 TYR A O   
949  C CB  . TYR A 110 ? 0.3654 0.2319 0.2726 -0.0584 0.0981  -0.0552 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.3738 0.2346 0.2724 -0.0625 0.0952  -0.0534 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4164 0.2637 0.3129 -0.0642 0.1026  -0.0567 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.3630 0.2317 0.2556 -0.0655 0.0857  -0.0499 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.3956 0.2386 0.2844 -0.0701 0.1014  -0.0569 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.3701 0.2369 0.2572 -0.0703 0.0838  -0.0508 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4010 0.2555 0.2862 -0.0734 0.0920  -0.0545 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4011 0.2552 0.2813 -0.0802 0.0912  -0.0571 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3356 0.2229 0.2601 -0.0417 0.0805  -0.0405 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3083 0.2021 0.2341 -0.0377 0.0717  -0.0336 112 LEU A CA  
959  C C   . LEU A 111 ? 0.3390 0.2377 0.2768 -0.0266 0.0690  -0.0299 112 LEU A C   
960  O O   . LEU A 111 ? 0.3350 0.2368 0.2726 -0.0231 0.0627  -0.0242 112 LEU A O   
961  C CB  . LEU A 111 ? 0.2916 0.1947 0.2124 -0.0423 0.0651  -0.0325 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3271 0.2264 0.2341 -0.0513 0.0635  -0.0349 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.3297 0.2356 0.2315 -0.0530 0.0557  -0.0328 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.3550 0.2514 0.2590 -0.0532 0.0618  -0.0344 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3052 0.2057 0.2539 -0.0211 0.0735  -0.0338 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3111 0.2187 0.2731 -0.0091 0.0696  -0.0316 113 GLN A CA  
967  C C   . GLN A 112 ? 0.3457 0.2698 0.3124 -0.0086 0.0621  -0.0292 113 GLN A C   
968  O O   . GLN A 112 ? 0.3298 0.2565 0.2956 -0.0038 0.0550  -0.0231 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3333 0.2271 0.2911 -0.0012 0.0675  -0.0255 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.3542 0.2286 0.3065 -0.0021 0.0760  -0.0284 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.4838 0.3396 0.4247 0.0013  0.0750  -0.0217 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.4233 0.2793 0.3629 0.0087  0.0680  -0.0150 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.4886 0.3268 0.4189 -0.0052 0.0826  -0.0237 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3086 0.2420 0.2780 -0.0150 0.0648  -0.0344 114 MET A N   
975  C CA  . MET A 113 ? 0.2981 0.2454 0.2712 -0.0166 0.0600  -0.0340 114 MET A CA  
976  C C   . MET A 113 ? 0.3561 0.3164 0.3456 -0.0143 0.0645  -0.0420 114 MET A C   
977  O O   . MET A 113 ? 0.3228 0.2844 0.3112 -0.0227 0.0717  -0.0486 114 MET A O   
978  C CB  . MET A 113 ? 0.3179 0.2605 0.2762 -0.0275 0.0600  -0.0336 114 MET A CB  
979  C CG  . MET A 113 ? 0.3316 0.2659 0.2780 -0.0290 0.0550  -0.0278 114 MET A CG  
980  S SD  . MET A 113 ? 0.3698 0.2988 0.2997 -0.0390 0.0527  -0.0280 114 MET A SD  
981  C CE  . MET A 113 ? 0.3266 0.2662 0.2601 -0.0378 0.0465  -0.0257 114 MET A CE  
982  N N   . GLU A 114 ? 0.3479 0.3171 0.3523 -0.0026 0.0606  -0.0420 115 GLU A N   
983  C CA  . GLU A 114 ? 0.3503 0.3349 0.3756 0.0028  0.0637  -0.0511 115 GLU A CA  
984  C C   . GLU A 114 ? 0.3549 0.3557 0.3876 -0.0054 0.0672  -0.0587 115 GLU A C   
985  O O   . GLU A 114 ? 0.3411 0.3486 0.3842 -0.0091 0.0762  -0.0689 115 GLU A O   
986  C CB  . GLU A 114 ? 0.3760 0.3684 0.4142 0.0185  0.0550  -0.0485 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.5466 0.5191 0.5768 0.0269  0.0536  -0.0422 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3147 0.3208 0.3418 -0.0093 0.0615  -0.0546 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3269 0.3458 0.3592 -0.0182 0.0657  -0.0620 116 HIS A CA  
990  C C   . HIS A 115 ? 0.3516 0.3576 0.3687 -0.0323 0.0759  -0.0655 116 HIS A C   
991  O O   . HIS A 115 ? 0.3554 0.3692 0.3792 -0.0399 0.0849  -0.0755 116 HIS A O   
992  C CB  . HIS A 115 ? 0.3478 0.3732 0.3768 -0.0187 0.0575  -0.0570 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.3979 0.4379 0.4411 -0.0061 0.0479  -0.0552 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4281 0.4890 0.4943 0.0004  0.0477  -0.0643 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4219 0.4585 0.4581 0.0003  0.0382  -0.0460 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4215 0.4898 0.4925 0.0118  0.0365  -0.0594 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4226 0.4758 0.4747 0.0113  0.0312  -0.0482 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.2949 0.2812 0.2910 -0.0360 0.0747  -0.0581 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3038 0.2750 0.2812 -0.0484 0.0824  -0.0602 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.3732 0.3444 0.3577 -0.0506 0.0934  -0.0695 117 VAL A C   
1001 O O   . VAL A 116 ? 0.3455 0.3148 0.3249 -0.0616 0.1033  -0.0771 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.3509 0.3042 0.3063 -0.0507 0.0769  -0.0514 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.3621 0.2997 0.2970 -0.0624 0.0838  -0.0541 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3457 0.2998 0.2952 -0.0495 0.0675  -0.0444 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3269 0.2983 0.3220 -0.0407 0.0925  -0.0693 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3280 0.2997 0.3326 -0.0411 0.1031  -0.0790 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.3833 0.3752 0.4090 -0.0427 0.1103  -0.0914 118 VAL A C   
1008 O O   . VAL A 117 ? 0.3711 0.3616 0.3948 -0.0531 0.1225  -0.1011 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.3640 0.3312 0.3775 -0.0283 0.1004  -0.0766 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.3691 0.3368 0.3945 -0.0280 0.1119  -0.0881 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.3615 0.3095 0.3541 -0.0300 0.0959  -0.0669 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.3513 0.3621 0.3954 -0.0340 0.1028  -0.0916 119 ASP A N   
1013 N N   B ASP A 118 ? 0.3469 0.3580 0.3924 -0.0330 0.1029  -0.0919 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.3448 0.3794 0.4123 -0.0348 0.1078  -0.1043 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.3423 0.3778 0.4122 -0.0331 0.1076  -0.1047 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.3847 0.4179 0.4408 -0.0532 0.1185  -0.1111 119 ASP A C   
1017 C C   B ASP A 118 ? 0.3943 0.4298 0.4545 -0.0513 0.1186  -0.1122 119 ASP A C   
1018 O O   A ASP A 118 ? 0.3823 0.4246 0.4497 -0.0603 0.1310  -0.1248 119 ASP A O   
1019 O O   B ASP A 118 ? 0.3950 0.4411 0.4681 -0.0577 0.1307  -0.1262 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.3575 0.4112 0.4418 -0.0229 0.0953  -0.1014 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.3540 0.4082 0.4401 -0.0213 0.0950  -0.1016 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.4923 0.5752 0.6049 -0.0222 0.0988  -0.1161 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.4819 0.5418 0.5843 -0.0022 0.0859  -0.0992 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.5182 0.6130 0.6522 -0.0163 0.1043  -0.1272 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.5131 0.5707 0.6255 0.0034  0.0915  -0.1051 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.5502 0.6449 0.6646 -0.0275 0.0963  -0.1174 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.5546 0.6199 0.6587 0.0073  0.0734  -0.0915 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.3374 0.3576 0.3703 -0.0613 0.1144  -0.1020 120 THR A N   
1029 N N   B THR A 119 ? 0.3498 0.3719 0.3864 -0.0596 0.1148  -0.1032 120 THR A N   
1030 C CA  A THR A 119 ? 0.3454 0.3584 0.3625 -0.0788 0.1245  -0.1072 120 THR A CA  
1031 C CA  B THR A 119 ? 0.3597 0.3755 0.3810 -0.0769 0.1242  -0.1080 120 THR A CA  
1032 C C   A THR A 119 ? 0.3932 0.3863 0.3898 -0.0905 0.1360  -0.1103 120 THR A C   
1033 C C   B THR A 119 ? 0.4050 0.4005 0.4050 -0.0893 0.1361  -0.1112 120 THR A C   
1034 O O   A THR A 119 ? 0.3965 0.3874 0.3866 -0.1049 0.1489  -0.1198 120 THR A O   
1035 O O   B THR A 119 ? 0.4108 0.4067 0.4078 -0.1030 0.1494  -0.1218 120 THR A O   
1036 C CB  A THR A 119 ? 0.3545 0.3570 0.3524 -0.0830 0.1170  -0.0974 120 THR A CB  
1037 C CB  B THR A 119 ? 0.4409 0.4472 0.4444 -0.0796 0.1155  -0.0975 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.3523 0.3505 0.3398 -0.0990 0.1279  -0.1048 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4227 0.4459 0.4441 -0.0664 0.1035  -0.0934 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.3031 0.2803 0.2731 -0.0826 0.1096  -0.0840 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.4403 0.4448 0.4348 -0.0950 0.1246  -0.1041 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.3614 0.3395 0.3464 -0.0855 0.1321  -0.1029 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.3796 0.3389 0.3438 -0.0965 0.1422  -0.1061 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.4542 0.4267 0.4390 -0.0990 0.1563  -0.1218 121 CYS A C   
1045 O O   . CYS A 120 ? 0.4407 0.4055 0.4126 -0.1143 0.1700  -0.1305 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.3796 0.3239 0.3310 -0.0901 0.1344  -0.0964 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.4249 0.3511 0.3473 -0.0913 0.1208  -0.0810 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4148 0.4064 0.4309 -0.0839 0.1530  -0.1260 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4197 0.4111 0.4356 -0.0840 0.1531  -0.1260 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4165 0.4248 0.4593 -0.0820 0.1643  -0.1420 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4238 0.4313 0.4655 -0.0827 0.1649  -0.1422 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.4555 0.4807 0.5096 -0.0940 0.1759  -0.1563 122 ARG A C   
1053 C C   B ARG A 121 ? 0.4578 0.4829 0.5117 -0.0942 0.1761  -0.1564 122 ARG A C   
1054 O O   A ARG A 121 ? 0.4595 0.4865 0.5164 -0.1049 0.1918  -0.1703 122 ARG A O   
1055 O O   B ARG A 121 ? 0.4609 0.4882 0.5180 -0.1051 0.1920  -0.1705 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4098 0.4354 0.4834 -0.0607 0.1546  -0.1419 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.4285 0.4518 0.5003 -0.0617 0.1559  -0.1422 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.5645 0.5725 0.6296 -0.0502 0.1480  -0.1319 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6168 0.6222 0.6809 -0.0538 0.1537  -0.1361 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7021 0.7226 0.7960 -0.0306 0.1427  -0.1350 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.7509 0.7694 0.8455 -0.0354 0.1511  -0.1418 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.7530 0.7536 0.8350 -0.0210 0.1349  -0.1230 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.8119 0.8385 0.9165 -0.0192 0.1347  -0.1318 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 0.8788 0.8625 0.9533 -0.0220 0.1421  -0.1250 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 0.9414 0.9536 1.0391 -0.0072 0.1249  -0.1200 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.7761 0.7604 0.8537 -0.0317 0.1571  -0.1384 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.7602 0.7503 0.8430 -0.0092 0.1297  -0.1172 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.6242 0.5897 0.6873 -0.0146 0.1354  -0.1143 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.7419 0.7609 0.8461 0.0059  0.1108  -0.1114 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.3994 0.4364 0.4588 -0.0934 0.1689  -0.1535 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4071 0.4609 0.4772 -0.1056 0.1791  -0.1669 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.4668 0.4969 0.5028 -0.1284 0.1928  -0.1685 123 LYS A C   
1073 O O   . LYS A 122 ? 0.4630 0.5009 0.5053 -0.1422 0.2096  -0.1847 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.4242 0.4945 0.5065 -0.0989 0.1671  -0.1626 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.6345 0.7326 0.7535 -0.0780 0.1559  -0.1655 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.7626 0.8770 0.8917 -0.0715 0.1433  -0.1613 123 LYS A CD  
1077 C CE  . LYS A 122 ? 0.9105 1.0477 1.0700 -0.0495 0.1302  -0.1620 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.0576 1.2255 1.2412 -0.0464 0.1244  -0.1701 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.4278 0.4282 0.4269 -0.1324 0.1857  -0.1525 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.4546 0.4269 0.4150 -0.1523 0.1960  -0.1514 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.5213 0.4827 0.4712 -0.1619 0.2101  -0.1600 124 PHE A C   
1082 O O   . PHE A 123 ? 0.5167 0.4672 0.4486 -0.1809 0.2259  -0.1689 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.4729 0.4180 0.3993 -0.1508 0.1824  -0.1326 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.4898 0.4343 0.4113 -0.1517 0.1754  -0.1265 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.5037 0.4767 0.4580 -0.1420 0.1697  -0.1302 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.5459 0.4602 0.4291 -0.1609 0.1731  -0.1166 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.5183 0.4904 0.4677 -0.1435 0.1638  -0.1254 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.5695 0.4814 0.4483 -0.1611 0.1669  -0.1114 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.5185 0.4596 0.4306 -0.1531 0.1630  -0.1161 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.4651 0.4291 0.4260 -0.1497 0.2056  -0.1583 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.4840 0.4396 0.4382 -0.1577 0.2193  -0.1678 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.5572 0.5374 0.5422 -0.1635 0.2367  -0.1896 125 ILE A C   
1093 O O   . ILE A 124 ? 0.5724 0.5430 0.5419 -0.1816 0.2543  -0.2007 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.5133 0.4632 0.4702 -0.1437 0.2103  -0.1604 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.5207 0.4440 0.4413 -0.1443 0.1975  -0.1425 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.5464 0.4938 0.5062 -0.1498 0.2258  -0.1737 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.5711 0.4930 0.4981 -0.1286 0.1844  -0.1327 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.5107 0.5230 0.5383 -0.1485 0.2315  -0.1963 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.5197 0.5620 0.5841 -0.1506 0.2453  -0.2185 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.5744 0.6183 0.6289 -0.1734 0.2614  -0.2302 126 LYS A C   
1101 O O   . LYS A 125 ? 0.5650 0.6203 0.6320 -0.1853 0.2802  -0.2498 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.5381 0.6133 0.6464 -0.1285 0.2324  -0.2210 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.5279 0.5582 0.5582 -0.1803 0.2550  -0.2188 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.5527 0.5783 0.5677 -0.2030 0.2702  -0.2280 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.6562 0.6492 0.6293 -0.2258 0.2876  -0.2308 127 ALA A C   
1106 O O   . ALA A 126 ? 0.6690 0.6637 0.6383 -0.2461 0.3071  -0.2463 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.5522 0.5670 0.5496 -0.2029 0.2579  -0.2137 127 ALA A CB  
1108 N N   . SER A 127 ? 0.6536 0.6170 0.5942 -0.2234 0.2808  -0.2164 128 SER A N   
1109 C CA  . SER A 127 ? 0.7118 0.6413 0.6073 -0.2438 0.2942  -0.2167 128 SER A CA  
1110 C C   . SER A 127 ? 0.8092 0.7452 0.7151 -0.2499 0.3109  -0.2332 128 SER A C   
1111 O O   . SER A 127 ? 0.8574 0.7678 0.7270 -0.2699 0.3256  -0.2371 128 SER A O   
1112 C CB  . SER A 127 ? 0.7814 0.6762 0.6346 -0.2394 0.2779  -0.1941 128 SER A CB  
1113 O OG  . SER A 127 ? 0.9317 0.8052 0.7547 -0.2467 0.2725  -0.1830 128 SER A OG  
1114 N N   . GLU A 128 ? 0.7395 0.7078 0.6930 -0.2330 0.3091  -0.2431 129 GLU A N   
1115 C CA  . GLU A 128 ? 0.9557 0.9318 0.9239 -0.2365 0.3248  -0.2600 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.4497 1.4468 1.4384 -0.2537 0.3491  -0.2859 129 GLU A C   
1117 O O   . GLU A 128 ? 1.0415 1.0353 1.0168 -0.2704 0.3577  -0.2898 129 GLU A O   
1118 C CB  . GLU A 128 ? 0.9428 0.9394 0.9497 -0.2105 0.3127  -0.2593 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.0290 1.0671 1.0910 -0.1944 0.3089  -0.2710 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.2485 1.3016 1.3435 -0.1668 0.2939  -0.2669 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.0949 1.1260 1.1695 -0.1574 0.2808  -0.2493 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.1428 1.2295 1.2840 -0.1544 0.2949  -0.2817 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.1963 0.4479 0.2662 -0.0355 -0.0117 -0.0898 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2091 0.4607 0.2790 -0.0355 -0.0117 -0.0898 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.1856 0.4354 0.2545 -0.0352 -0.0116 -0.0914 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2049 0.4549 0.2739 -0.0352 -0.0116 -0.0914 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2412 0.4908 0.3112 -0.0355 -0.0120 -0.0914 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2375 0.4874 0.3076 -0.0356 -0.0120 -0.0913 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2478 0.4968 0.3188 -0.0357 -0.0127 -0.0909 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2312 0.4808 0.3023 -0.0359 -0.0126 -0.0907 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.1719 0.4191 0.2397 -0.0347 -0.0122 -0.0921 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.1973 0.4445 0.2651 -0.0346 -0.0122 -0.0921 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.1750 0.4220 0.2412 -0.0344 -0.0119 -0.0928 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2124 0.4587 0.2819 -0.0347 -0.0133 -0.0921 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2067 0.4538 0.2729 -0.0345 -0.0123 -0.0923 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.2525 0.4984 0.3239 -0.0349 -0.0139 -0.0918 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.1720 0.4187 0.2363 -0.0341 -0.0107 -0.0944 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2105 0.4571 0.2807 -0.0344 -0.0136 -0.0927 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.1944 0.4416 0.2583 -0.0341 -0.0117 -0.0938 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.2468 0.4930 0.3209 -0.0350 -0.0144 -0.0926 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2085 0.4554 0.2711 -0.0340 -0.0106 -0.0953 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.2622 0.5092 0.3351 -0.0346 -0.0142 -0.0933 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.1818 0.4282 0.2461 -0.0338 -0.0095 -0.0952 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2214 0.4685 0.2908 -0.0339 -0.0133 -0.0928 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2034 0.4499 0.2638 -0.0336 -0.0094 -0.0975 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.2507 0.4996 0.3254 -0.0342 -0.0143 -0.0946 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.1924 0.4383 0.2553 -0.0335 -0.0081 -0.0969 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.2405 0.4889 0.3108 -0.0333 -0.0136 -0.0936 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2008 0.4468 0.2616 -0.0335 -0.0080 -0.0984 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.2457 0.4954 0.3185 -0.0335 -0.0140 -0.0947 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.1786 0.4286 0.2487 -0.0354 -0.0115 -0.0922 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.1806 0.4307 0.2513 -0.0355 -0.0119 -0.0925 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2087 0.4576 0.2790 -0.0344 -0.0115 -0.0928 2   VAL D C   
1157 O O   . VAL B 3   ? 0.1965 0.4447 0.2666 -0.0339 -0.0106 -0.0927 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2254 0.4786 0.2979 -0.0368 -0.0117 -0.0930 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2228 0.4782 0.2958 -0.0378 -0.0121 -0.0921 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2173 0.4728 0.2917 -0.0370 -0.0103 -0.0941 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.1927 0.4417 0.2632 -0.0340 -0.0120 -0.0931 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.1806 0.4294 0.2513 -0.0328 -0.0115 -0.0927 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2259 0.4756 0.2992 -0.0337 -0.0107 -0.0933 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2248 0.4757 0.2988 -0.0347 -0.0114 -0.0943 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.1999 0.4496 0.2697 -0.0319 -0.0122 -0.0931 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.1747 0.4253 0.2437 -0.0314 -0.0127 -0.0935 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2240 0.4743 0.2943 -0.0303 -0.0116 -0.0920 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.2294 0.4803 0.2981 -0.0306 -0.0126 -0.0925 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2184 0.4681 0.2939 -0.0336 -0.0091 -0.0931 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2191 0.4710 0.2990 -0.0347 -0.0081 -0.0945 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.2606 0.5124 0.3426 -0.0342 -0.0083 -0.0943 4   PRO D C   
1172 O O   . PRO B 5   ? 0.2435 0.4935 0.3238 -0.0324 -0.0084 -0.0926 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.2402 0.4922 0.3226 -0.0343 -0.0058 -0.0947 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.2946 0.5432 0.3736 -0.0326 -0.0058 -0.0927 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.2436 0.4919 0.3184 -0.0326 -0.0080 -0.0923 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.2489 0.5034 0.3345 -0.0358 -0.0085 -0.0963 5   ALA D N   
# 
