data_7GUZ
# 
_entry.id   7GUZ 
# 
_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   7GUZ         pdb_00007guz 10.2210/pdb7guz/pdb 
WWPDB D_1001406670 ?            ?                   
# 
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                        7GUZ 
_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 45  HOH   HOH A . 
F 6 HOH   4   304 166 HOH   HOH A . 
F 6 HOH   5   305 94  HOH   HOH A . 
F 6 HOH   6   306 140 HOH   HOH A . 
F 6 HOH   7   307 29  HOH   HOH A . 
F 6 HOH   8   308 106 HOH   HOH A . 
F 6 HOH   9   309 173 HOH   HOH A . 
F 6 HOH   10  310 179 HOH   HOH A . 
F 6 HOH   11  311 84  HOH   HOH A . 
F 6 HOH   12  312 19  HOH   HOH A . 
F 6 HOH   13  313 90  HOH   HOH A . 
F 6 HOH   14  314 202 HOH   HOH A . 
F 6 HOH   15  315 247 HOH   HOH A . 
F 6 HOH   16  316 47  HOH   HOH A . 
F 6 HOH   17  317 101 HOH   HOH A . 
F 6 HOH   18  318 100 HOH   HOH A . 
F 6 HOH   19  319 99  HOH   HOH A . 
F 6 HOH   20  320 132 HOH   HOH A . 
F 6 HOH   21  321 37  HOH   HOH A . 
F 6 HOH   22  322 142 HOH   HOH A . 
F 6 HOH   23  323 139 HOH   HOH A . 
F 6 HOH   24  324 87  HOH   HOH A . 
F 6 HOH   25  325 83  HOH   HOH A . 
F 6 HOH   26  326 75  HOH   HOH A . 
F 6 HOH   27  327 119 HOH   HOH A . 
F 6 HOH   28  328 193 HOH   HOH A . 
F 6 HOH   29  329 27  HOH   HOH A . 
F 6 HOH   30  330 40  HOH   HOH A . 
F 6 HOH   31  331 91  HOH   HOH A . 
F 6 HOH   32  332 237 HOH   HOH A . 
F 6 HOH   33  333 4   HOH   HOH A . 
F 6 HOH   34  334 117 HOH   HOH A . 
F 6 HOH   35  335 5   HOH   HOH A . 
F 6 HOH   36  336 42  HOH   HOH A . 
F 6 HOH   37  337 6   HOH   HOH A . 
F 6 HOH   38  338 34  HOH   HOH A . 
F 6 HOH   39  339 14  HOH   HOH A . 
F 6 HOH   40  340 17  HOH   HOH A . 
F 6 HOH   41  341 243 HOH   HOH A . 
F 6 HOH   42  342 20  HOH   HOH A . 
F 6 HOH   43  343 44  HOH   HOH A . 
F 6 HOH   44  344 12  HOH   HOH A . 
F 6 HOH   45  345 239 HOH   HOH A . 
F 6 HOH   46  346 86  HOH   HOH A . 
F 6 HOH   47  347 242 HOH   HOH A . 
F 6 HOH   48  348 122 HOH   HOH A . 
F 6 HOH   49  349 24  HOH   HOH A . 
F 6 HOH   50  350 151 HOH   HOH A . 
F 6 HOH   51  351 85  HOH   HOH A . 
F 6 HOH   52  352 89  HOH   HOH A . 
F 6 HOH   53  353 96  HOH   HOH A . 
F 6 HOH   54  354 30  HOH   HOH A . 
F 6 HOH   55  355 124 HOH   HOH A . 
F 6 HOH   56  356 51  HOH   HOH A . 
F 6 HOH   57  357 145 HOH   HOH A . 
F 6 HOH   58  358 196 HOH   HOH A . 
F 6 HOH   59  359 175 HOH   HOH A . 
F 6 HOH   60  360 93  HOH   HOH A . 
F 6 HOH   61  361 141 HOH   HOH A . 
F 6 HOH   62  362 170 HOH   HOH A . 
F 6 HOH   63  363 177 HOH   HOH A . 
F 6 HOH   64  364 97  HOH   HOH A . 
F 6 HOH   65  365 207 HOH   HOH A . 
F 6 HOH   66  366 50  HOH   HOH A . 
F 6 HOH   67  367 103 HOH   HOH A . 
F 6 HOH   68  368 180 HOH   HOH A . 
F 6 HOH   69  369 244 HOH   HOH A . 
F 6 HOH   70  370 25  HOH   HOH A . 
F 6 HOH   71  371 21  HOH   HOH A . 
F 6 HOH   72  372 133 HOH   HOH A . 
F 6 HOH   73  373 169 HOH   HOH A . 
F 6 HOH   74  374 186 HOH   HOH A . 
F 6 HOH   75  375 15  HOH   HOH A . 
F 6 HOH   76  376 74  HOH   HOH A . 
F 6 HOH   77  377 144 HOH   HOH A . 
F 6 HOH   78  378 105 HOH   HOH A . 
F 6 HOH   79  379 28  HOH   HOH A . 
F 6 HOH   80  380 131 HOH   HOH A . 
F 6 HOH   81  381 76  HOH   HOH A . 
F 6 HOH   82  382 205 HOH   HOH A . 
F 6 HOH   83  383 245 HOH   HOH A . 
F 6 HOH   84  384 167 HOH   HOH A . 
F 6 HOH   85  385 229 HOH   HOH A . 
F 6 HOH   86  386 70  HOH   HOH A . 
F 6 HOH   87  387 39  HOH   HOH A . 
F 6 HOH   88  388 192 HOH   HOH A . 
F 6 HOH   89  389 191 HOH   HOH A . 
F 6 HOH   90  390 194 HOH   HOH A . 
F 6 HOH   91  391 55  HOH   HOH A . 
F 6 HOH   92  392 16  HOH   HOH A . 
F 6 HOH   93  393 241 HOH   HOH A . 
F 6 HOH   94  394 32  HOH   HOH A . 
F 6 HOH   95  395 212 HOH   HOH A . 
F 6 HOH   96  396 92  HOH   HOH A . 
F 6 HOH   97  397 165 HOH   HOH A . 
F 6 HOH   98  398 108 HOH   HOH A . 
F 6 HOH   99  399 22  HOH   HOH A . 
F 6 HOH   100 400 157 HOH   HOH A . 
F 6 HOH   101 401 174 HOH   HOH A . 
F 6 HOH   102 402 64  HOH   HOH A . 
F 6 HOH   103 403 60  HOH   HOH A . 
F 6 HOH   104 404 185 HOH   HOH A . 
F 6 HOH   105 405 69  HOH   HOH A . 
F 6 HOH   106 406 35  HOH   HOH A . 
F 6 HOH   107 407 223 HOH   HOH A . 
F 6 HOH   108 408 129 HOH   HOH A . 
F 6 HOH   109 409 82  HOH   HOH A . 
F 6 HOH   110 410 26  HOH   HOH A . 
F 6 HOH   111 411 43  HOH   HOH A . 
F 6 HOH   112 412 120 HOH   HOH A . 
F 6 HOH   113 413 176 HOH   HOH A . 
F 6 HOH   114 414 67  HOH   HOH A . 
F 6 HOH   115 415 236 HOH   HOH A . 
F 6 HOH   116 416 88  HOH   HOH A . 
F 6 HOH   117 417 36  HOH   HOH A . 
F 6 HOH   118 418 215 HOH   HOH A . 
F 6 HOH   119 419 190 HOH   HOH A . 
F 6 HOH   120 420 61  HOH   HOH A . 
F 6 HOH   121 421 46  HOH   HOH A . 
F 6 HOH   122 422 204 HOH   HOH A . 
F 6 HOH   123 423 68  HOH   HOH A . 
F 6 HOH   124 424 95  HOH   HOH A . 
F 6 HOH   125 425 57  HOH   HOH A . 
F 6 HOH   126 426 56  HOH   HOH A . 
F 6 HOH   127 427 65  HOH   HOH A . 
F 6 HOH   128 428 41  HOH   HOH A . 
F 6 HOH   129 429 147 HOH   HOH A . 
F 6 HOH   130 430 110 HOH   HOH A . 
F 6 HOH   131 431 116 HOH   HOH A . 
F 6 HOH   132 432 168 HOH   HOH A . 
F 6 HOH   133 433 187 HOH   HOH A . 
F 6 HOH   134 434 214 HOH   HOH A . 
F 6 HOH   135 435 200 HOH   HOH A . 
F 6 HOH   136 436 135 HOH   HOH A . 
F 6 HOH   137 437 227 HOH   HOH A . 
F 6 HOH   138 438 123 HOH   HOH A . 
F 6 HOH   139 439 248 HOH   HOH A . 
F 6 HOH   140 440 228 HOH   HOH A . 
F 6 HOH   141 441 231 HOH   HOH A . 
F 6 HOH   142 442 63  HOH   HOH A . 
F 6 HOH   143 443 121 HOH   HOH A . 
F 6 HOH   144 444 225 HOH   HOH A . 
F 6 HOH   145 445 71  HOH   HOH A . 
F 6 HOH   146 446 171 HOH   HOH A . 
F 6 HOH   147 447 234 HOH   HOH A . 
F 6 HOH   148 448 203 HOH   HOH A . 
F 6 HOH   149 449 220 HOH   HOH A . 
F 6 HOH   150 450 158 HOH   HOH A . 
F 6 HOH   151 451 114 HOH   HOH A . 
F 6 HOH   152 452 125 HOH   HOH A . 
F 6 HOH   153 453 217 HOH   HOH A . 
F 6 HOH   154 454 181 HOH   HOH A . 
F 6 HOH   155 455 238 HOH   HOH A . 
F 6 HOH   156 456 79  HOH   HOH A . 
F 6 HOH   157 457 235 HOH   HOH A . 
F 6 HOH   158 458 81  HOH   HOH A . 
F 6 HOH   159 459 246 HOH   HOH A . 
F 6 HOH   160 460 221 HOH   HOH A . 
F 6 HOH   161 461 58  HOH   HOH A . 
F 6 HOH   162 462 115 HOH   HOH A . 
F 6 HOH   163 463 107 HOH   HOH A . 
F 6 HOH   164 464 216 HOH   HOH A . 
F 6 HOH   165 465 182 HOH   HOH A . 
F 6 HOH   166 466 188 HOH   HOH A . 
F 6 HOH   167 467 230 HOH   HOH A . 
F 6 HOH   168 468 183 HOH   HOH A . 
F 6 HOH   169 469 201 HOH   HOH A . 
F 6 HOH   170 470 113 HOH   HOH A . 
F 6 HOH   171 471 148 HOH   HOH A . 
F 6 HOH   172 472 213 HOH   HOH A . 
F 6 HOH   173 473 48  HOH   HOH A . 
F 6 HOH   174 474 206 HOH   HOH A . 
F 6 HOH   175 475 172 HOH   HOH A . 
F 6 HOH   176 476 211 HOH   HOH A . 
G 6 HOH   1   201 62  HOH   HOH D . 
G 6 HOH   2   202 38  HOH   HOH D . 
G 6 HOH   3   203 23  HOH   HOH D . 
G 6 HOH   4   204 78  HOH   HOH D . 
G 6 HOH   5   205 73  HOH   HOH D . 
G 6 HOH   6   206 53  HOH   HOH D . 
G 6 HOH   7   207 240 HOH   HOH D . 
G 6 HOH   8   208 49  HOH   HOH D . 
G 6 HOH   9   209 195 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           7GUZ 
_cell.length_a           67.640 
_cell.length_b           67.640 
_cell.length_c           166.590 
_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                         7GUZ 
_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          7GUZ 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.63 
_exptl_crystal.density_percent_sol   66.13 
_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                     7GUZ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.940 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   23674 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.071 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.200 
_reflns.B_iso_Wilson_estimate        32.320 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.075 
_reflns.pdbx_Rpim_I_all              0.025 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     215336 
_reflns.pdbx_scaling_rejects         994 
_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  ? 11990 1280 ? 1.664 ? ? ? 9.400 ? 1.400  ? ? ? ? ? ? 100.000 1.759 0.565 0.706 ? 
1 2 9.090 33.940 ? 1508  228  ? 0.028 ? ? ? 6.600 ? 44.500 ? ? ? ? ? ? 98.700  0.031 0.013 0.993 ? 
# 
_refine.entry_id                                 7GUZ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.7500 
_refine.ls_d_res_low                             33.9400 
_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                     23605 
_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                          0.1810 
_refine.ls_R_factor_R_work                       0.1800 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2050 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1500 
_refine.ls_number_reflns_R_free                  1215 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               36.9700 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.4370 
_refine.aniso_B[2][2]                            0.4370 
_refine.aniso_B[3][3]                            -0.8741 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9630 
_refine.correlation_coeff_Fo_to_Fc_free          0.9450 
_refine.overall_SU_R_Cruickshank_DPI             0.0870 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0860 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0990 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0950 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                128.230 
_refine.B_iso_min                                18.820 
_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                        7GUZ 
_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                        33.9400 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             185 
_refine_hist.number_atoms_total               1231 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           32.10 
_refine_hist.pdbx_B_iso_mean_solvent          54.39 
_refine_hist.pdbx_number_atoms_protein        1022 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' t_dihedral_angle_d        445  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              235  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1233 ?      ? 20.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 162  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        8    ?      ? 1.000  HARMONIC     
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1652 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1233 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1689 0.890  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.350  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    14.700 ? ?      ?            
# 
_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               99.8900 
_refine_ls_shell.number_reflns_R_work             2693 
_refine_ls_shell.R_factor_all                     0.3436 
_refine_ls_shell.R_factor_R_work                  0.3433 
_refine_ls_shell.R_factor_R_free                  0.3493 
_refine_ls_shell.percent_reflns_R_free            4.6100 
_refine_ls_shell.number_reflns_R_free             130 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2823 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUZ 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 2 at 10.00 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUZ 
_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 7GUZ       7GUZ   ? 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 7GUZ A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUZ D 1 ? 6   ? 7GUZ   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 7GUZ GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUZ PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUZ 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)'  12990 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_545 x,x-y-1,-z+1/6 0.5000000000 0.8660254038 0.0000000000 33.8200000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5779583120 0.0000000000 0.0000000000 -1.0000000000 27.7650000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ARG A 12  ? ARG A 27  ? ARG A 13  ARG A 28  1 ? 16 
HELX_P HELX_P2 AA2 HIS A 45  ? SER A 53  ? HIS A 46  SER A 54  1 ? 9  
HELX_P HELX_P3 AA3 SER A 53  ? THR A 61  ? SER A 54  THR A 62  1 ? 9  
HELX_P HELX_P4 AA4 LEU A 64  ? LEU A 68  ? LEU A 65  LEU A 69  5 ? 5  
HELX_P HELX_P5 AA5 ASN A 78  ? SER A 92  ? ASN A 79  SER A 93  1 ? 15 
HELX_P HELX_P6 AA6 ASN A 100 ? GLN A 112 ? ASN A 101 GLN A 113 1 ? 13 
HELX_P HELX_P7 AA7 MET A 113 ? GLU A 128 ? MET A 114 GLU A 129 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N A ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O PHE A 42 ? O PHE A 43 N ILE A 35 ? N ILE A 36 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GUZ 
_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 61.81   -118.95 
2 1 SER A 39  ? B 39.24   65.42   
3 1 ARG A 40  ? B 74.67   -21.40  
4 1 SER A 93  ? A 76.43   -4.91   
5 1 GLN A 113 ? ? 62.82   60.27   
6 1 MET A 114 ? ? -117.56 79.86   
# 
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 362 ? F HOH . 
2 1 A HOH 373 ? F HOH . 
3 1 A HOH 457 ? F HOH . 
4 1 A HOH 467 ? F HOH . 
5 1 A HOH 468 ? F HOH . 
6 1 A HOH 469 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.2144 -16.5503 24.6837 0.0191  -0.0442 -0.0825 -0.0404 0.0301  -0.0263 0.9769 1.7982  1.9999 
0.4175 -0.3023 1.1515 0.1329 -0.0701 -0.0628 -0.0575 0.1080 0.0884 0.2516  -0.0160 -0.0093 
'X-RAY DIFFRACTION' 2 ? refined 18.9076 -32.4261 1.8469  -0.1048 0.1260  -0.0471 -0.0224 -0.0239 -0.0992 0.8803 -0.2576 0.0000 
0.0311 -0.1493 0.2327 0.0242 -0.0141 -0.0102 -0.0096 0.0004 0.0242 -0.0193 -0.0022 -0.0178 
# 
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                    7GUZ 
_atom_sites.fract_transf_matrix[1][1]   0.014784 
_atom_sites.fract_transf_matrix[1][2]   0.008536 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017071 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006003 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
BR 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP   A 1 5   ? 17.300 -21.239 -4.817 1.00 67.39  ? 6   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 5   ? 18.220 -22.122 -5.537 1.00 66.27  ? 6   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 5   ? 17.765 -23.601 -5.477 1.00 65.68  ? 6   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 5   ? 16.720 -23.912 -4.895 1.00 66.55  ? 6   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 5   ? 19.654 -21.965 -4.972 1.00 67.12  ? 6   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 5   ? 20.748 -22.016 -6.030 1.00 81.38  ? 6   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 5   ? 20.894 -23.077 -6.690 1.00 81.64  ? 6   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 5   ? 21.465 -21.002 -6.191 1.00 88.60  ? 6   ASP   A OD2 1 
ATOM   9    N  N   . SER   A 1 6   ? 18.548 -24.502 -6.091 1.00 56.58  ? 7   SER   A N   1 
ATOM   10   C  CA  . SER   A 1 6   ? 18.298 -25.940 -6.093 1.00 53.81  ? 7   SER   A CA  1 
ATOM   11   C  C   . SER   A 1 6   ? 19.287 -26.659 -5.124 1.00 49.33  ? 7   SER   A C   1 
ATOM   12   O  O   . SER   A 1 6   ? 19.598 -27.834 -5.313 1.00 48.12  ? 7   SER   A O   1 
ATOM   13   C  CB  . SER   A 1 6   ? 18.411 -26.487 -7.513 1.00 59.70  ? 7   SER   A CB  1 
ATOM   14   O  OG  . SER   A 1 6   ? 19.696 -26.246 -8.063 1.00 71.46  ? 7   SER   A OG  1 
ATOM   15   N  N   . CYS   A 1 7   ? 19.745 -25.956 -4.072 1.00 40.67  ? 8   CYS   A N   1 
ATOM   16   C  CA  . CYS   A 1 7   ? 20.684 -26.512 -3.095 1.00 37.47  ? 8   CYS   A CA  1 
ATOM   17   C  C   . CYS   A 1 7   ? 20.069 -27.664 -2.292 1.00 37.94  ? 8   CYS   A C   1 
ATOM   18   O  O   . CYS   A 1 7   ? 18.851 -27.707 -2.105 1.00 37.76  ? 8   CYS   A O   1 
ATOM   19   C  CB  . CYS   A 1 7   ? 21.165 -25.411 -2.147 1.00 38.58  ? 8   CYS   A CB  1 
ATOM   20   S  SG  . CYS   A 1 7   ? 22.341 -24.233 -2.875 1.00 43.91  ? 8   CYS   A SG  1 
ATOM   21   N  N   . ILE   A 1 8   ? 20.909 -28.569 -1.788 1.00 29.42  ? 9   ILE   A N   1 
ATOM   22   C  CA  . ILE   A 1 8   ? 20.526 -29.557 -0.775 1.00 26.81  ? 9   ILE   A CA  1 
ATOM   23   C  C   . ILE   A 1 8   ? 21.143 -29.025 0.520  1.00 28.48  ? 9   ILE   A C   1 
ATOM   24   O  O   . ILE   A 1 8   ? 22.091 -28.230 0.466  1.00 26.34  ? 9   ILE   A O   1 
ATOM   25   C  CB  . ILE   A 1 8   ? 20.872 -31.037 -1.081 1.00 30.00  ? 9   ILE   A CB  1 
ATOM   26   C  CG1 . ILE   A 1 8   ? 22.390 -31.222 -1.332 1.00 29.52  ? 9   ILE   A CG1 1 
ATOM   27   C  CG2 . ILE   A 1 8   ? 20.050 -31.541 -2.263 1.00 28.91  ? 9   ILE   A CG2 1 
ATOM   28   C  CD1 . ILE   A 1 8   ? 22.901 -32.671 -1.510 1.00 35.16  ? 9   ILE   A CD1 1 
ATOM   29   N  N   A GLN   A 1 9   ? 20.672 -29.466 1.688  0.66 23.21  ? 10  GLN   A N   1 
ATOM   30   N  N   B GLN   A 1 9   ? 20.552 -29.386 1.657  0.34 24.24  ? 10  GLN   A N   1 
ATOM   31   C  CA  A GLN   A 1 9   ? 21.225 -28.966 2.951  0.66 22.40  ? 10  GLN   A CA  1 
ATOM   32   C  CA  B GLN   A 1 9   ? 20.980 -28.891 2.952  0.34 23.25  ? 10  GLN   A CA  1 
ATOM   33   C  C   A GLN   A 1 9   ? 21.591 -30.111 3.880  0.66 24.94  ? 10  GLN   A C   1 
ATOM   34   C  C   B GLN   A 1 9   ? 21.387 -30.021 3.875  0.34 26.96  ? 10  GLN   A C   1 
ATOM   35   O  O   A GLN   A 1 9   ? 20.846 -31.088 3.949  0.66 25.88  ? 10  GLN   A O   1 
ATOM   36   O  O   B GLN   A 1 9   ? 20.684 -31.027 3.963  0.34 27.44  ? 10  GLN   A O   1 
ATOM   37   C  CB  A GLN   A 1 9   ? 20.218 -28.008 3.632  0.66 24.41  ? 10  GLN   A CB  1 
ATOM   38   C  CB  B GLN   A 1 9   ? 19.855 -28.063 3.581  0.34 24.59  ? 10  GLN   A CB  1 
ATOM   39   C  CG  A GLN   A 1 9   ? 20.578 -27.665 5.094  0.66 27.68  ? 10  GLN   A CG  1 
ATOM   40   C  CG  B GLN   A 1 9   ? 20.356 -27.067 4.622  0.34 27.37  ? 10  GLN   A CG  1 
ATOM   41   C  CD  A GLN   A 1 9   ? 20.045 -26.352 5.596  0.66 47.84  ? 10  GLN   A CD  1 
ATOM   42   C  CD  B GLN   A 1 9   ? 19.636 -27.197 5.941  0.34 40.51  ? 10  GLN   A CD  1 
ATOM   43   O  OE1 A GLN   A 1 9   ? 19.436 -25.568 4.864  0.66 41.83  ? 10  GLN   A OE1 1 
ATOM   44   O  OE1 B GLN   A 1 9   ? 18.415 -27.382 6.000  0.34 34.38  ? 10  GLN   A OE1 1 
ATOM   45   N  NE2 A GLN   A 1 9   ? 20.299 -26.068 6.870  0.66 41.70  ? 10  GLN   A NE2 1 
ATOM   46   N  NE2 B GLN   A 1 9   ? 20.380 -27.072 7.033  0.34 37.49  ? 10  GLN   A NE2 1 
ATOM   47   N  N   A PHE   A 1 10  ? 22.727 -30.004 4.585  0.66 22.60  ? 11  PHE   A N   1 
ATOM   48   N  N   B PHE   A 1 10  ? 22.514 -29.849 4.565  0.34 23.94  ? 11  PHE   A N   1 
ATOM   49   C  CA  A PHE   A 1 10  ? 23.112 -31.026 5.555  0.66 21.93  ? 11  PHE   A CA  1 
ATOM   50   C  CA  B PHE   A 1 10  ? 23.030 -30.825 5.520  0.34 23.53  ? 11  PHE   A CA  1 
ATOM   51   C  C   A PHE   A 1 10  ? 22.642 -30.544 6.923  0.66 24.84  ? 11  PHE   A C   1 
ATOM   52   C  C   B PHE   A 1 10  ? 22.526 -30.393 6.882  0.34 25.88  ? 11  PHE   A C   1 
ATOM   53   O  O   A PHE   A 1 10  ? 23.225 -29.601 7.483  0.66 24.07  ? 11  PHE   A O   1 
ATOM   54   O  O   B PHE   A 1 10  ? 22.943 -29.342 7.393  0.34 25.15  ? 11  PHE   A O   1 
ATOM   55   C  CB  A PHE   A 1 10  ? 24.631 -31.316 5.514  0.66 23.08  ? 11  PHE   A CB  1 
ATOM   56   C  CB  B PHE   A 1 10  ? 24.567 -30.902 5.425  0.34 25.09  ? 11  PHE   A CB  1 
ATOM   57   C  CG  A PHE   A 1 10  ? 25.003 -32.520 6.347  0.66 23.58  ? 11  PHE   A CG  1 
ATOM   58   C  CG  B PHE   A 1 10  ? 25.041 -31.684 4.218  0.34 27.30  ? 11  PHE   A CG  1 
ATOM   59   C  CD1 A PHE   A 1 10  ? 24.633 -33.803 5.952  0.66 26.36  ? 11  PHE   A CD1 1 
ATOM   60   C  CD1 B PHE   A 1 10  ? 24.805 -31.217 2.926  0.34 31.20  ? 11  PHE   A CD1 1 
ATOM   61   C  CD2 A PHE   A 1 10  ? 25.775 -32.379 7.497  0.66 24.82  ? 11  PHE   A CD2 1 
ATOM   62   C  CD2 B PHE   A 1 10  ? 25.714 -32.888 4.370  0.34 30.52  ? 11  PHE   A CD2 1 
ATOM   63   C  CE1 A PHE   A 1 10  ? 24.971 -34.917 6.732  0.66 27.38  ? 11  PHE   A CE1 1 
ATOM   64   C  CE1 B PHE   A 1 10  ? 25.234 -31.942 1.811  0.34 32.40  ? 11  PHE   A CE1 1 
ATOM   65   C  CE2 A PHE   A 1 10  ? 26.098 -33.487 8.284  0.66 26.53  ? 11  PHE   A CE2 1 
ATOM   66   C  CE2 B PHE   A 1 10  ? 26.144 -33.614 3.249  0.34 34.12  ? 11  PHE   A CE2 1 
ATOM   67   C  CZ  A PHE   A 1 10  ? 25.703 -34.748 7.895  0.66 24.83  ? 11  PHE   A CZ  1 
ATOM   68   C  CZ  B PHE   A 1 10  ? 25.901 -33.135 1.980  0.34 32.03  ? 11  PHE   A CZ  1 
ATOM   69   N  N   . THR   A 1 11  ? 21.553 -31.153 7.429  1.00 22.22  ? 12  THR   A N   1 
ATOM   70   C  CA  . THR   A 1 11  ? 20.891 -30.776 8.695  1.00 22.87  ? 12  THR   A CA  1 
ATOM   71   C  C   . THR   A 1 11  ? 21.856 -30.533 9.872  1.00 24.73  ? 12  THR   A C   1 
ATOM   72   O  O   . THR   A 1 11  ? 21.737 -29.514 10.566 1.00 24.48  ? 12  THR   A O   1 
ATOM   73   C  CB  . THR   A 1 11  ? 19.815 -31.798 9.069  1.00 28.58  ? 12  THR   A CB  1 
ATOM   74   O  OG1 . THR   A 1 11  ? 18.919 -31.953 7.946  1.00 29.04  ? 12  THR   A OG1 1 
ATOM   75   C  CG2 . THR   A 1 11  ? 19.002 -31.371 10.313 1.00 33.38  ? 12  THR   A CG2 1 
ATOM   76   N  N   . ARG   A 1 12  ? 22.783 -31.472 10.092 1.00 22.53  ? 13  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 12  ? 23.690 -31.369 11.245 1.00 22.96  ? 13  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 12  ? 24.935 -30.468 11.038 1.00 23.93  ? 13  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 12  ? 25.773 -30.398 11.950 1.00 22.81  ? 13  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 12  ? 24.148 -32.781 11.669 1.00 28.23  ? 13  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 12  ? 23.048 -33.726 12.197 1.00 39.66  ? 13  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 12  ? 22.471 -33.287 13.531 1.00 60.93  ? 13  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 12  ? 23.434 -33.389 14.631 1.00 73.17  ? 13  ARG   A NE  1 
ATOM   84   C  CZ  . ARG   A 1 12  ? 23.304 -32.771 15.801 1.00 83.77  ? 13  ARG   A CZ  1 
ATOM   85   N  NH1 . ARG   A 1 12  ? 24.223 -32.926 16.744 1.00 73.00  ? 13  ARG   A NH1 1 
ATOM   86   N  NH2 . ARG   A 1 12  ? 22.264 -31.978 16.031 1.00 65.47  ? 13  ARG   A NH2 1 
ATOM   87   N  N   . HIS   A 1 13  ? 25.077 -29.811 9.875  1.00 19.96  ? 14  HIS   A N   1 
ATOM   88   C  CA  . HIS   A 1 13  ? 26.309 -29.077 9.578  1.00 20.58  ? 14  HIS   A CA  1 
ATOM   89   C  C   . HIS   A 1 13  ? 26.612 -27.990 10.599 1.00 23.24  ? 14  HIS   A C   1 
ATOM   90   O  O   . HIS   A 1 13  ? 27.752 -27.929 11.102 1.00 22.44  ? 14  HIS   A O   1 
ATOM   91   C  CB  . HIS   A 1 13  ? 26.295 -28.502 8.149  1.00 20.50  ? 14  HIS   A CB  1 
ATOM   92   C  CG  . HIS   A 1 13  ? 27.558 -27.761 7.843  1.00 22.73  ? 14  HIS   A CG  1 
ATOM   93   N  ND1 . HIS   A 1 13  ? 28.738 -28.437 7.641  1.00 23.54  ? 14  HIS   A ND1 1 
ATOM   94   C  CD2 . HIS   A 1 13  ? 27.780 -26.431 7.706  1.00 23.53  ? 14  HIS   A CD2 1 
ATOM   95   C  CE1 . HIS   A 1 13  ? 29.650 -27.509 7.388  1.00 23.15  ? 14  HIS   A CE1 1 
ATOM   96   N  NE2 . HIS   A 1 13  ? 29.115 -26.286 7.392  1.00 22.79  ? 14  HIS   A NE2 1 
ATOM   97   N  N   . ALA   A 1 14  ? 25.619 -27.108 10.877 1.00 20.60  ? 15  ALA   A N   1 
ATOM   98   C  CA  . ALA   A 1 14  ? 25.851 -25.984 11.815 1.00 20.85  ? 15  ALA   A CA  1 
ATOM   99   C  C   . ALA   A 1 14  ? 26.269 -26.485 13.204 1.00 22.47  ? 15  ALA   A C   1 
ATOM   100  O  O   . ALA   A 1 14  ? 27.192 -25.923 13.802 1.00 20.03  ? 15  ALA   A O   1 
ATOM   101  C  CB  . ALA   A 1 14  ? 24.620 -25.084 11.897 1.00 22.44  ? 15  ALA   A CB  1 
ATOM   102  N  N   A SER   A 1 15  ? 25.599 -27.534 13.706 0.42 21.33  ? 16  SER   A N   1 
ATOM   103  N  N   B SER   A 1 15  ? 25.601 -27.542 13.704 0.30 20.87  ? 16  SER   A N   1 
ATOM   104  N  N   C SER   A 1 15  ? 25.600 -27.534 13.717 0.28 20.28  ? 16  SER   A N   1 
ATOM   105  C  CA  A SER   A 1 15  ? 25.902 -28.127 15.007 0.42 21.62  ? 16  SER   A CA  1 
ATOM   106  C  CA  B SER   A 1 15  ? 25.893 -28.149 15.005 0.30 21.07  ? 16  SER   A CA  1 
ATOM   107  C  CA  C SER   A 1 15  ? 25.921 -28.103 15.029 0.28 20.15  ? 16  SER   A CA  1 
ATOM   108  C  C   A SER   A 1 15  ? 27.311 -28.715 15.024 0.42 25.07  ? 16  SER   A C   1 
ATOM   109  C  C   B SER   A 1 15  ? 27.298 -28.740 15.033 0.30 25.25  ? 16  SER   A C   1 
ATOM   110  C  C   C SER   A 1 15  ? 27.309 -28.744 15.045 0.28 24.89  ? 16  SER   A C   1 
ATOM   111  O  O   A SER   A 1 15  ? 28.052 -28.500 15.992 0.42 22.32  ? 16  SER   A O   1 
ATOM   112  O  O   B SER   A 1 15  ? 28.018 -28.563 16.022 0.30 23.40  ? 16  SER   A O   1 
ATOM   113  O  O   C SER   A 1 15  ? 28.033 -28.594 16.034 0.28 23.11  ? 16  SER   A O   1 
ATOM   114  C  CB  A SER   A 1 15  ? 24.861 -29.186 15.363 0.42 25.40  ? 16  SER   A CB  1 
ATOM   115  C  CB  B SER   A 1 15  ? 24.861 -29.223 15.338 0.30 24.30  ? 16  SER   A CB  1 
ATOM   116  C  CB  C SER   A 1 15  ? 24.845 -29.087 15.479 0.28 22.21  ? 16  SER   A CB  1 
ATOM   117  O  OG  A SER   A 1 15  ? 25.078 -29.717 16.660 0.42 30.39  ? 16  SER   A OG  1 
ATOM   118  O  OG  B SER   A 1 15  ? 23.556 -28.675 15.413 0.30 27.84  ? 16  SER   A OG  1 
ATOM   119  O  OG  C SER   A 1 15  ? 24.790 -30.226 14.637 0.28 21.18  ? 16  SER   A OG  1 
ATOM   120  N  N   . ASP   A 1 16  ? 27.694 -29.425 13.940 1.00 23.13  ? 17  ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 16  ? 29.022 -30.040 13.814 1.00 23.75  ? 17  ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 16  ? 30.102 -28.941 13.771 1.00 23.66  ? 17  ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 16  ? 31.160 -29.090 14.383 1.00 23.30  ? 17  ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 16  ? 29.090 -30.912 12.558 1.00 25.66  ? 17  ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 16  ? 28.297 -32.218 12.639 1.00 34.59  ? 17  ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 16  ? 27.776 -32.540 13.741 1.00 32.71  ? 17  ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 16  ? 28.192 -32.912 11.604 1.00 37.38  ? 17  ASP   A OD2 1 
ATOM   128  N  N   . VAL   A 1 17  ? 29.826 -27.822 13.065 1.00 19.73  ? 18  VAL   A N   1 
ATOM   129  C  CA  . VAL   A 1 17  ? 30.791 -26.714 13.034 1.00 19.44  ? 18  VAL   A CA  1 
ATOM   130  C  C   . VAL   A 1 17  ? 31.012 -26.170 14.460 1.00 22.56  ? 18  VAL   A C   1 
ATOM   131  O  O   . VAL   A 1 17  ? 32.150 -26.000 14.895 1.00 20.51  ? 18  VAL   A O   1 
ATOM   132  C  CB  . VAL   A 1 17  ? 30.311 -25.596 12.062 1.00 21.46  ? 18  VAL   A CB  1 
ATOM   133  C  CG1 . VAL   A 1 17  ? 31.076 -24.294 12.276 1.00 21.60  ? 18  VAL   A CG1 1 
ATOM   134  C  CG2 . VAL   A 1 17  ? 30.381 -26.053 10.603 1.00 21.06  ? 18  VAL   A CG2 1 
ATOM   135  N  N   . LEU   A 1 18  ? 29.924 -25.921 15.182 1.00 20.13  ? 19  LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 18  ? 30.014 -25.349 16.525 1.00 21.08  ? 19  LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 18  ? 30.748 -26.309 17.484 1.00 21.99  ? 19  LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 18  ? 31.617 -25.858 18.259 1.00 20.98  ? 19  LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 18  ? 28.624 -24.995 17.052 1.00 21.80  ? 19  LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 18  ? 28.635 -24.073 18.303 1.00 24.89  ? 19  LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 18  ? 29.282 -22.706 17.994 1.00 25.10  ? 19  LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 18  ? 27.227 -23.883 18.826 1.00 30.05  ? 19  LEU   A CD2 1 
ATOM   143  N  N   . LEU   A 1 19  ? 30.458 -27.611 17.366 1.00 20.95  ? 20  LEU   A N   1 
ATOM   144  C  CA  . LEU   A 1 19  ? 31.129 -28.645 18.165 1.00 21.67  ? 20  LEU   A CA  1 
ATOM   145  C  C   . LEU   A 1 19  ? 32.649 -28.567 17.916 1.00 24.08  ? 20  LEU   A C   1 
ATOM   146  O  O   . LEU   A 1 19  ? 33.435 -28.560 18.878 1.00 23.05  ? 20  LEU   A O   1 
ATOM   147  C  CB  . LEU   A 1 19  ? 30.589 -30.036 17.784 1.00 23.48  ? 20  LEU   A CB  1 
ATOM   148  C  CG  . LEU   A 1 19  ? 31.169 -31.223 18.556 1.00 31.56  ? 20  LEU   A CG  1 
ATOM   149  C  CD1 . LEU   A 1 19  ? 30.787 -31.139 20.042 1.00 34.39  ? 20  LEU   A CD1 1 
ATOM   150  C  CD2 . LEU   A 1 19  ? 30.602 -32.530 18.004 1.00 36.50  ? 20  LEU   A CD2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 33.057 -28.450 16.635 1.00 21.48  ? 21  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 34.475 -28.322 16.282 1.00 21.28  ? 21  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 35.097 -27.017 16.787 1.00 23.45  ? 21  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 36.224 -27.031 17.266 1.00 23.28  ? 21  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 34.682 -28.522 14.805 1.00 23.32  ? 21  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.671 -29.988 14.433 1.00 33.52  ? 21  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.921 -30.874 15.264 1.00 29.43  ? 21  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.375 -30.284 13.178 1.00 27.03  ? 21  ASN   A ND2 1 
ATOM   159  N  N   . LEU   A 1 21  ? 34.355 -25.900 16.704 1.00 21.16  ? 22  LEU   A N   1 
ATOM   160  C  CA  . LEU   A 1 21  ? 34.831 -24.624 17.252 1.00 20.69  ? 22  LEU   A CA  1 
ATOM   161  C  C   . LEU   A 1 21  ? 35.058 -24.781 18.764 1.00 23.37  ? 22  LEU   A C   1 
ATOM   162  O  O   . LEU   A 1 21  ? 36.040 -24.257 19.291 1.00 22.72  ? 22  LEU   A O   1 
ATOM   163  C  CB  . LEU   A 1 21  ? 33.835 -23.479 16.962 1.00 20.83  ? 22  LEU   A CB  1 
ATOM   164  C  CG  . LEU   A 1 21  ? 33.742 -23.096 15.466 1.00 23.50  ? 22  LEU   A CG  1 
ATOM   165  C  CD1 . LEU   A 1 21  ? 32.605 -22.088 15.224 1.00 23.73  ? 22  LEU   A CD1 1 
ATOM   166  C  CD2 . LEU   A 1 21  ? 35.088 -22.576 14.906 1.00 26.30  ? 22  LEU   A CD2 1 
ATOM   167  N  N   . ASN   A 1 22  ? 34.137 -25.483 19.464 1.00 21.34  ? 23  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 22  ? 34.303 -25.704 20.911 1.00 21.93  ? 23  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 22  ? 35.539 -26.577 21.217 1.00 25.26  ? 23  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 22  ? 36.227 -26.339 22.212 1.00 26.17  ? 23  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 22  ? 33.050 -26.312 21.538 1.00 23.32  ? 23  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 22  ? 33.072 -26.184 23.048 1.00 30.55  ? 23  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 22  ? 33.615 -25.223 23.612 1.00 27.40  ? 23  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 22  ? 32.493 -27.149 23.724 1.00 30.49  ? 23  ASN   A ND2 1 
ATOM   175  N  N   . ARG   A 1 23  ? 35.821 -27.586 20.354 1.00 23.30  ? 24  ARG   A N   1 
ATOM   176  C  CA  . ARG   A 1 23  ? 37.013 -28.441 20.484 1.00 24.66  ? 24  ARG   A CA  1 
ATOM   177  C  C   . ARG   A 1 23  ? 38.278 -27.587 20.347 1.00 28.38  ? 24  ARG   A C   1 
ATOM   178  O  O   . ARG   A 1 23  ? 39.232 -27.769 21.106 1.00 27.89  ? 24  ARG   A O   1 
ATOM   179  C  CB  . ARG   A 1 23  ? 37.004 -29.528 19.410 1.00 23.80  ? 24  ARG   A CB  1 
ATOM   180  C  CG  . ARG   A 1 23  ? 36.016 -30.644 19.731 1.00 26.98  ? 24  ARG   A CG  1 
ATOM   181  C  CD  . ARG   A 1 23  ? 35.848 -31.597 18.552 1.00 30.46  ? 24  ARG   A CD  1 
ATOM   182  N  NE  . ARG   A 1 23  ? 34.982 -32.710 18.927 1.00 37.60  ? 24  ARG   A NE  1 
ATOM   183  C  CZ  . ARG   A 1 23  ? 34.304 -33.470 18.074 1.00 52.06  ? 24  ARG   A CZ  1 
ATOM   184  N  NH1 . ARG   A 1 23  ? 34.335 -33.211 16.770 1.00 40.04  ? 24  ARG   A NH1 1 
ATOM   185  N  NH2 . ARG   A 1 23  ? 33.569 -34.477 18.518 1.00 45.27  ? 24  ARG   A NH2 1 
ATOM   186  N  N   . LEU   A 1 24  ? 38.273 -26.628 19.398 1.00 24.96  ? 25  LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 24  ? 39.400 -25.712 19.236 1.00 24.52  ? 25  LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 24  ? 39.566 -24.853 20.485 1.00 27.58  ? 25  LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 24  ? 40.695 -24.703 20.976 1.00 27.08  ? 25  LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 24  ? 39.203 -24.804 18.034 1.00 23.94  ? 25  LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 24  ? 39.220 -25.481 16.658 1.00 27.00  ? 25  LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 24  ? 39.061 -24.431 15.556 1.00 27.15  ? 25  LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 24  ? 40.518 -26.320 16.450 1.00 27.46  ? 25  LEU   A CD2 1 
ATOM   194  N  N   . ARG   A 1 25  ? 38.440 -24.328 21.028 1.00 23.43  ? 26  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 25  ? 38.493 -23.548 22.267 1.00 23.95  ? 26  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 25  ? 39.117 -24.380 23.434 1.00 29.50  ? 26  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 25  ? 40.002 -23.866 24.140 1.00 29.36  ? 26  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 25  ? 37.097 -23.052 22.672 1.00 25.14  ? 26  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 25  ? 37.234 -22.118 23.884 1.00 28.37  ? 26  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 25  ? 35.942 -21.497 24.295 1.00 32.95  ? 26  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 25  ? 34.938 -22.494 24.653 1.00 28.54  ? 26  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 25  ? 34.319 -22.553 25.828 1.00 40.94  ? 26  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 25  ? 34.650 -21.716 26.806 1.00 34.48  ? 26  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 25  ? 33.378 -23.456 26.040 1.00 29.75  ? 26  ARG   A NH2 1 
ATOM   205  N  N   A SER   A 1 26  ? 38.643 -25.623 23.635 0.39 27.39  ? 27  SER   A N   1 
ATOM   206  N  N   B SER   A 1 26  ? 38.646 -25.634 23.613 0.28 27.38  ? 27  SER   A N   1 
ATOM   207  N  N   C SER   A 1 26  ? 38.643 -25.623 23.634 0.33 27.73  ? 27  SER   A N   1 
ATOM   208  C  CA  A SER   A 1 26  ? 39.114 -26.522 24.698 0.39 28.67  ? 27  SER   A CA  1 
ATOM   209  C  CA  B SER   A 1 26  ? 39.095 -26.590 24.638 0.28 28.68  ? 27  SER   A CA  1 
ATOM   210  C  CA  C SER   A 1 26  ? 39.111 -26.533 24.690 0.33 29.21  ? 27  SER   A CA  1 
ATOM   211  C  C   A SER   A 1 26  ? 40.627 -26.786 24.623 0.39 34.52  ? 27  SER   A C   1 
ATOM   212  C  C   B SER   A 1 26  ? 40.610 -26.790 24.609 0.28 34.39  ? 27  SER   A C   1 
ATOM   213  C  C   C SER   A 1 26  ? 40.625 -26.786 24.620 0.33 34.69  ? 27  SER   A C   1 
ATOM   214  O  O   A SER   A 1 26  ? 41.276 -26.897 25.666 0.39 35.60  ? 27  SER   A O   1 
ATOM   215  O  O   B SER   A 1 26  ? 41.239 -26.885 25.665 0.28 35.36  ? 27  SER   A O   1 
ATOM   216  O  O   C SER   A 1 26  ? 41.270 -26.899 25.664 0.33 35.70  ? 27  SER   A O   1 
ATOM   217  C  CB  A SER   A 1 26  ? 38.331 -27.832 24.689 0.39 32.22  ? 27  SER   A CB  1 
ATOM   218  C  CB  B SER   A 1 26  ? 38.423 -27.945 24.430 0.28 32.51  ? 27  SER   A CB  1 
ATOM   219  C  CB  C SER   A 1 26  ? 38.346 -27.851 24.637 0.33 33.59  ? 27  SER   A CB  1 
ATOM   220  O  OG  A SER   A 1 26  ? 38.708 -28.689 23.623 0.39 36.46  ? 27  SER   A OG  1 
ATOM   221  O  OG  B SER   A 1 26  ? 37.054 -27.941 24.792 0.28 38.61  ? 27  SER   A OG  1 
ATOM   222  O  OG  C SER   A 1 26  ? 38.802 -28.761 25.626 0.33 43.08  ? 27  SER   A OG  1 
ATOM   223  N  N   . ARG   A 1 27  ? 41.185 -26.859 23.398 1.00 30.76  ? 28  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 27  ? 42.620 -27.092 23.181 1.00 32.12  ? 28  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 27  ? 43.411 -25.797 22.980 1.00 35.02  ? 28  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 27  ? 44.618 -25.840 22.710 1.00 36.16  ? 28  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 27  ? 42.803 -28.067 22.015 1.00 33.48  ? 28  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 27  ? 42.055 -29.382 22.220 1.00 40.04  ? 28  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 27  ? 42.018 -30.204 20.954 1.00 46.15  ? 28  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 27  ? 43.367 -30.597 20.546 1.00 60.08  ? 28  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 27  ? 43.732 -30.804 19.287 1.00 74.37  ? 28  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 27  ? 44.982 -31.139 18.999 1.00 63.51  ? 28  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 27  ? 42.858 -30.649 18.305 1.00 56.58  ? 28  ARG   A NH2 1 
ATOM   234  N  N   . ASP   A 1 28  ? 42.732 -24.644 23.139 1.00 29.42  ? 29  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 28  ? 43.290 -23.302 22.993 1.00 29.90  ? 29  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 28  ? 43.896 -23.082 21.585 1.00 34.27  ? 29  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 28  ? 44.941 -22.444 21.440 1.00 35.71  ? 29  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 28  ? 44.317 -23.010 24.121 1.00 33.31  ? 29  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 28  ? 44.613 -21.536 24.292 1.00 43.64  ? 29  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 28  ? 43.686 -20.716 24.087 1.00 42.90  ? 29  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 28  ? 45.769 -21.199 24.628 1.00 48.46  ? 29  ASP   A OD2 1 
ATOM   242  N  N   . ILE   A 1 29  ? 43.245 -23.625 20.553 1.00 28.16  ? 30  ILE   A N   1 
ATOM   243  C  CA  . ILE   A 1 29  ? 43.758 -23.515 19.190 1.00 27.91  ? 30  ILE   A CA  1 
ATOM   244  C  C   . ILE   A 1 29  ? 43.156 -22.312 18.478 1.00 30.87  ? 30  ILE   A C   1 
ATOM   245  O  O   . ILE   A 1 29  ? 41.927 -22.183 18.389 1.00 27.44  ? 30  ILE   A O   1 
ATOM   246  C  CB  . ILE   A 1 29  ? 43.559 -24.828 18.389 1.00 30.81  ? 30  ILE   A CB  1 
ATOM   247  C  CG1 . ILE   A 1 29  ? 44.363 -26.002 19.022 1.00 32.95  ? 30  ILE   A CG1 1 
ATOM   248  C  CG2 . ILE   A 1 29  ? 43.904 -24.624 16.893 1.00 29.69  ? 30  ILE   A CG2 1 
ATOM   249  C  CD1 . ILE   A 1 29  ? 43.901 -27.387 18.522 1.00 35.97  ? 30  ILE   A CD1 1 
ATOM   250  N  N   . LEU   A 1 30  ? 44.043 -21.428 17.974 1.00 29.59  ? 31  LEU   A N   1 
ATOM   251  C  CA  . LEU   A 1 30  ? 43.680 -20.225 17.221 1.00 29.28  ? 31  LEU   A CA  1 
ATOM   252  C  C   . LEU   A 1 30  ? 42.769 -19.237 17.979 1.00 30.08  ? 31  LEU   A C   1 
ATOM   253  O  O   . LEU   A 1 30  ? 42.172 -18.369 17.347 1.00 28.33  ? 31  LEU   A O   1 
ATOM   254  C  CB  . LEU   A 1 30  ? 43.099 -20.549 15.842 1.00 29.65  ? 31  LEU   A CB  1 
ATOM   255  C  CG  . LEU   A 1 30  ? 44.125 -21.093 14.806 1.00 37.12  ? 31  LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A 1 30  ? 43.514 -21.148 13.460 1.00 37.88  ? 31  LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A 1 30  ? 45.369 -20.244 14.730 1.00 43.94  ? 31  LEU   A CD2 1 
ATOM   258  N  N   . THR   A 1 31  ? 42.746 -19.309 19.320 1.00 27.25  ? 32  THR   A N   1 
ATOM   259  C  CA  . THR   A 1 31  ? 42.071 -18.306 20.144 1.00 26.60  ? 32  THR   A CA  1 
ATOM   260  C  C   . THR   A 1 31  ? 42.887 -17.015 19.948 1.00 32.70  ? 32  THR   A C   1 
ATOM   261  O  O   . THR   A 1 31  ? 44.117 -17.068 19.830 1.00 32.31  ? 32  THR   A O   1 
ATOM   262  C  CB  . THR   A 1 31  ? 41.996 -18.748 21.599 1.00 30.93  ? 32  THR   A CB  1 
ATOM   263  O  OG1 . THR   A 1 31  ? 43.320 -19.073 22.029 1.00 33.20  ? 32  THR   A OG1 1 
ATOM   264  C  CG2 . THR   A 1 31  ? 41.036 -19.958 21.786 1.00 29.23  ? 32  THR   A CG2 1 
ATOM   265  N  N   . ASP   A 1 32  ? 42.210 -15.885 19.797 1.00 30.13  ? 33  ASP   A N   1 
ATOM   266  C  CA  . ASP   A 1 32  ? 42.885 -14.639 19.449 1.00 30.85  ? 33  ASP   A CA  1 
ATOM   267  C  C   . ASP   A 1 32  ? 42.555 -13.482 20.361 1.00 31.39  ? 33  ASP   A C   1 
ATOM   268  O  O   . ASP   A 1 32  ? 42.894 -12.339 20.060 1.00 31.38  ? 33  ASP   A O   1 
ATOM   269  C  CB  . ASP   A 1 32  ? 42.580 -14.289 17.979 1.00 32.38  ? 33  ASP   A CB  1 
ATOM   270  C  CG  . ASP   A 1 32  ? 41.101 -14.249 17.599 1.00 39.66  ? 33  ASP   A CG  1 
ATOM   271  O  OD1 . ASP   A 1 32  ? 40.241 -14.434 18.497 1.00 33.41  ? 33  ASP   A OD1 1 
ATOM   272  O  OD2 . ASP   A 1 32  ? 40.804 -14.043 16.407 1.00 49.72  ? 33  ASP   A OD2 1 
ATOM   273  N  N   . VAL   A 1 33  ? 41.892 -13.768 21.481 1.00 25.76  ? 34  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 33  ? 41.567 -12.723 22.448 1.00 25.16  ? 34  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 33  ? 41.405 -13.324 23.837 1.00 28.39  ? 34  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 33  ? 41.004 -14.496 23.977 1.00 28.07  ? 34  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 33  ? 40.288 -11.910 22.005 1.00 27.92  ? 34  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 33  ? 38.995 -12.716 22.177 1.00 26.18  ? 34  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 33  ? 40.179 -10.558 22.733 1.00 28.00  ? 34  VAL   A CG2 1 
ATOM   280  N  N   A VAL   A 1 34  ? 41.702 -12.513 24.854 0.60 25.62  ? 35  VAL   A N   1 
ATOM   281  N  N   B VAL   A 1 34  ? 41.701 -12.524 24.869 0.40 24.75  ? 35  VAL   A N   1 
ATOM   282  C  CA  A VAL   A 1 34  ? 41.480 -12.833 26.256 0.60 25.22  ? 35  VAL   A CA  1 
ATOM   283  C  CA  B VAL   A 1 34  ? 41.448 -12.896 26.253 0.40 24.00  ? 35  VAL   A CA  1 
ATOM   284  C  C   A VAL   A 1 34  ? 40.406 -11.844 26.721 0.60 28.45  ? 35  VAL   A C   1 
ATOM   285  C  C   B VAL   A 1 34  ? 40.481 -11.863 26.849 0.40 28.36  ? 35  VAL   A C   1 
ATOM   286  O  O   A VAL   A 1 34  ? 40.518 -10.642 26.444 0.60 28.04  ? 35  VAL   A O   1 
ATOM   287  O  O   B VAL   A 1 34  ? 40.715 -10.654 26.748 0.40 28.78  ? 35  VAL   A O   1 
ATOM   288  C  CB  A VAL   A 1 34  ? 42.775 -12.711 27.115 0.60 30.63  ? 35  VAL   A CB  1 
ATOM   289  C  CB  B VAL   A 1 34  ? 42.703 -13.203 27.122 0.40 28.36  ? 35  VAL   A CB  1 
ATOM   290  C  CG1 A VAL   A 1 34  ? 42.505 -13.002 28.593 0.60 31.12  ? 35  VAL   A CG1 1 
ATOM   291  C  CG1 B VAL   A 1 34  ? 43.564 -11.969 27.362 0.40 28.84  ? 35  VAL   A CG1 1 
ATOM   292  C  CG2 A VAL   A 1 34  ? 43.873 -13.623 26.589 0.60 31.11  ? 35  VAL   A CG2 1 
ATOM   293  C  CG2 B VAL   A 1 34  ? 42.313 -13.861 28.443 0.40 28.33  ? 35  VAL   A CG2 1 
ATOM   294  N  N   . ILE   A 1 35  ? 39.360 -12.349 27.384 1.00 24.03  ? 36  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 35  ? 38.300 -11.529 27.984 1.00 24.72  ? 36  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 35  ? 38.583 -11.567 29.472 1.00 29.48  ? 36  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 35  ? 38.584 -12.656 30.074 1.00 28.56  ? 36  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 35  ? 36.866 -12.055 27.665 1.00 26.58  ? 36  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 35  ? 36.609 -12.221 26.140 1.00 25.63  ? 36  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 35  ? 35.801 -11.169 28.315 1.00 27.89  ? 36  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 35  ? 36.902 -10.956 25.230 1.00 26.94  ? 36  ILE   A CD1 1 
ATOM   302  N  N   . VAL   A 1 36  ? 38.820 -10.383 30.058 1.00 26.62  ? 37  VAL   A N   1 
ATOM   303  C  CA  . VAL   A 1 36  ? 39.128 -10.251 31.483 1.00 27.26  ? 37  VAL   A CA  1 
ATOM   304  C  C   . VAL   A 1 36  ? 37.867 -9.823  32.218 1.00 32.23  ? 37  VAL   A C   1 
ATOM   305  O  O   . VAL   A 1 36  ? 37.247 -8.816  31.862 1.00 30.73  ? 37  VAL   A O   1 
ATOM   306  C  CB  . VAL   A 1 36  ? 40.322 -9.284  31.725 1.00 31.87  ? 37  VAL   A CB  1 
ATOM   307  C  CG1 . VAL   A 1 36  ? 40.627 -9.127  33.221 1.00 32.74  ? 37  VAL   A CG1 1 
ATOM   308  C  CG2 . VAL   A 1 36  ? 41.570 -9.756  30.981 1.00 32.76  ? 37  VAL   A CG2 1 
ATOM   309  N  N   . VAL   A 1 37  ? 37.475 -10.613 33.229 1.00 29.12  ? 38  VAL   A N   1 
ATOM   310  C  CA  . VAL   A 1 37  ? 36.277 -10.383 34.030 1.00 29.67  ? 38  VAL   A CA  1 
ATOM   311  C  C   . VAL   A 1 37  ? 36.780 -10.429 35.456 1.00 36.53  ? 38  VAL   A C   1 
ATOM   312  O  O   . VAL   A 1 37  ? 36.950 -11.511 36.024 1.00 33.26  ? 38  VAL   A O   1 
ATOM   313  C  CB  . VAL   A 1 37  ? 35.163 -11.425 33.734 1.00 33.18  ? 38  VAL   A CB  1 
ATOM   314  C  CG1 . VAL   A 1 37  ? 33.845 -11.000 34.371 1.00 33.26  ? 38  VAL   A CG1 1 
ATOM   315  C  CG2 . VAL   A 1 37  ? 34.988 -11.633 32.228 1.00 31.98  ? 38  VAL   A CG2 1 
ATOM   316  N  N   A SER   A 1 38  ? 37.153 -9.252  35.989 0.54 36.66  ? 39  SER   A N   1 
ATOM   317  N  N   B SER   A 1 38  ? 37.010 -9.230  36.022 0.46 36.06  ? 39  SER   A N   1 
ATOM   318  C  CA  A SER   A 1 38  ? 37.753 -9.084  37.317 0.54 38.22  ? 39  SER   A CA  1 
ATOM   319  C  CA  B SER   A 1 38  ? 37.538 -8.990  37.364 0.46 37.46  ? 39  SER   A CA  1 
ATOM   320  C  C   A SER   A 1 38  ? 39.104 -9.846  37.380 0.54 39.96  ? 39  SER   A C   1 
ATOM   321  C  C   B SER   A 1 38  ? 38.643 -9.996  37.721 0.46 40.08  ? 39  SER   A C   1 
ATOM   322  O  O   A SER   A 1 38  ? 39.994 -9.551  36.580 0.54 38.86  ? 39  SER   A O   1 
ATOM   323  O  O   B SER   A 1 38  ? 38.466 -10.886 38.560 0.46 39.81  ? 39  SER   A O   1 
ATOM   324  C  CB  A SER   A 1 38  ? 36.786 -9.512  38.426 0.54 44.06  ? 39  SER   A CB  1 
ATOM   325  C  CB  B SER   A 1 38  ? 36.417 -8.922  38.394 0.46 42.34  ? 39  SER   A CB  1 
ATOM   326  O  OG  A SER   A 1 38  ? 35.535 -8.853  38.323 0.54 59.26  ? 39  SER   A OG  1 
ATOM   327  O  OG  B SER   A 1 38  ? 35.718 -7.695  38.249 0.46 51.07  ? 39  SER   A OG  1 
ATOM   328  N  N   A ARG   A 1 39  ? 39.231 -10.841 38.285 0.54 36.03  ? 40  ARG   A N   1 
ATOM   329  N  N   B ARG   A 1 39  ? 39.750 -9.884  36.965 0.46 34.97  ? 40  ARG   A N   1 
ATOM   330  C  CA  A ARG   A 1 39  ? 40.443 -11.642 38.479 0.54 36.20  ? 40  ARG   A CA  1 
ATOM   331  C  CA  B ARG   A 1 39  ? 40.997 -10.651 37.021 0.46 35.14  ? 40  ARG   A CA  1 
ATOM   332  C  C   A ARG   A 1 39  ? 40.544 -12.831 37.523 0.54 38.35  ? 40  ARG   A C   1 
ATOM   333  C  C   B ARG   A 1 39  ? 40.873 -12.075 36.443 0.46 37.10  ? 40  ARG   A C   1 
ATOM   334  O  O   A ARG   A 1 39  ? 41.561 -13.533 37.538 0.54 38.18  ? 40  ARG   A O   1 
ATOM   335  O  O   B ARG   A 1 39  ? 41.897 -12.608 36.013 0.46 37.22  ? 40  ARG   A O   1 
ATOM   336  C  CB  A ARG   A 1 39  ? 40.544 -12.132 39.938 0.54 36.33  ? 40  ARG   A CB  1 
ATOM   337  C  CB  B ARG   A 1 39  ? 41.654 -10.649 38.416 0.46 36.10  ? 40  ARG   A CB  1 
ATOM   338  C  CG  A ARG   A 1 39  ? 40.997 -11.067 40.924 0.54 43.06  ? 40  ARG   A CG  1 
ATOM   339  C  CG  B ARG   A 1 39  ? 42.188 -9.270  38.803 0.46 47.64  ? 40  ARG   A CG  1 
ATOM   340  C  CD  A ARG   A 1 39  ? 41.351 -11.696 42.256 0.54 42.40  ? 40  ARG   A CD  1 
ATOM   341  C  CD  B ARG   A 1 39  ? 43.181 -9.323  39.944 0.46 54.24  ? 40  ARG   A CD  1 
ATOM   342  N  NE  A ARG   A 1 39  ? 41.548 -10.696 43.302 0.54 45.45  ? 40  ARG   A NE  1 
ATOM   343  N  NE  B ARG   A 1 39  ? 43.620 -7.985  40.349 0.46 61.42  ? 40  ARG   A NE  1 
ATOM   344  C  CZ  A ARG   A 1 39  ? 42.719 -10.158 43.629 0.54 60.75  ? 40  ARG   A CZ  1 
ATOM   345  C  CZ  B ARG   A 1 39  ? 43.024 -7.247  41.281 0.46 72.65  ? 40  ARG   A CZ  1 
ATOM   346  N  NH1 A ARG   A 1 39  ? 42.794 -9.264  44.603 0.54 48.68  ? 40  ARG   A NH1 1 
ATOM   347  N  NH1 B ARG   A 1 39  ? 41.946 -7.702  41.910 0.46 56.10  ? 40  ARG   A NH1 1 
ATOM   348  N  NH2 A ARG   A 1 39  ? 43.823 -10.503 42.977 0.54 48.52  ? 40  ARG   A NH2 1 
ATOM   349  N  NH2 B ARG   A 1 39  ? 43.495 -6.046  41.587 0.46 60.79  ? 40  ARG   A NH2 1 
ATOM   350  N  N   A GLU   A 1 40  ? 39.490 -13.078 36.715 0.54 32.84  ? 41  GLU   A N   1 
ATOM   351  N  N   B GLU   A 1 40  ? 39.642 -12.659 36.356 0.46 32.65  ? 41  GLU   A N   1 
ATOM   352  C  CA  A GLU   A 1 40  ? 39.468 -14.213 35.788 0.54 31.96  ? 41  GLU   A CA  1 
ATOM   353  C  CA  B GLU   A 1 40  ? 39.417 -13.984 35.742 0.46 31.96  ? 41  GLU   A CA  1 
ATOM   354  C  C   A GLU   A 1 40  ? 39.733 -13.809 34.343 0.54 34.44  ? 41  GLU   A C   1 
ATOM   355  C  C   B GLU   A 1 40  ? 39.565 -13.836 34.224 0.46 34.34  ? 41  GLU   A C   1 
ATOM   356  O  O   A GLU   A 1 40  ? 39.384 -12.706 33.923 0.54 32.72  ? 41  GLU   A O   1 
ATOM   357  O  O   B GLU   A 1 40  ? 38.992 -12.912 33.644 0.46 32.20  ? 41  GLU   A O   1 
ATOM   358  C  CB  A GLU   A 1 40  ? 38.146 -15.001 35.898 0.54 33.01  ? 41  GLU   A CB  1 
ATOM   359  C  CB  B GLU   A 1 40  ? 38.033 -14.552 36.108 0.46 33.16  ? 41  GLU   A CB  1 
ATOM   360  C  CG  A GLU   A 1 40  ? 37.871 -15.567 37.286 0.54 47.87  ? 41  GLU   A CG  1 
ATOM   361  C  CG  B GLU   A 1 40  ? 37.943 -15.089 37.528 0.46 47.00  ? 41  GLU   A CG  1 
ATOM   362  C  CD  A GLU   A 1 40  ? 38.178 -17.042 37.452 0.54 85.23  ? 41  GLU   A CD  1 
ATOM   363  C  CD  B GLU   A 1 40  ? 38.167 -16.583 37.649 0.46 82.52  ? 41  GLU   A CD  1 
ATOM   364  O  OE1 A GLU   A 1 40  ? 37.433 -17.875 36.884 0.54 86.65  ? 41  GLU   A OE1 1 
ATOM   365  O  OE1 B GLU   A 1 40  ? 39.217 -16.982 38.203 0.46 84.83  ? 41  GLU   A OE1 1 
ATOM   366  O  OE2 A GLU   A 1 40  ? 39.158 -17.367 38.160 0.54 86.18  ? 41  GLU   A OE2 1 
ATOM   367  O  OE2 B GLU   A 1 40  ? 37.294 -17.356 37.189 0.46 83.59  ? 41  GLU   A OE2 1 
ATOM   368  N  N   . GLN   A 1 41  ? 40.334 -14.734 33.581 1.00 30.87  ? 42  GLN   A N   1 
ATOM   369  C  CA  . GLN   A 1 41  ? 40.656 -14.604 32.165 1.00 30.41  ? 42  GLN   A CA  1 
ATOM   370  C  C   . GLN   A 1 41  ? 40.013 -15.724 31.375 1.00 32.59  ? 42  GLN   A C   1 
ATOM   371  O  O   . GLN   A 1 41  ? 40.061 -16.875 31.813 1.00 32.71  ? 42  GLN   A O   1 
ATOM   372  C  CB  . GLN   A 1 41  ? 42.180 -14.646 31.983 1.00 33.25  ? 42  GLN   A CB  1 
ATOM   373  C  CG  . GLN   A 1 41  ? 42.897 -13.421 32.545 1.00 48.17  ? 42  GLN   A CG  1 
ATOM   374  C  CD  . GLN   A 1 41  ? 44.365 -13.341 32.192 1.00 68.23  ? 42  GLN   A CD  1 
ATOM   375  O  OE1 . GLN   A 1 41  ? 44.930 -14.174 31.466 1.00 61.01  ? 42  GLN   A OE1 1 
ATOM   376  N  NE2 . GLN   A 1 41  ? 45.019 -12.314 32.708 1.00 71.16  ? 42  GLN   A NE2 1 
ATOM   377  N  N   . PHE   A 1 42  ? 39.418 -15.399 30.207 1.00 26.48  ? 43  PHE   A N   1 
ATOM   378  C  CA  . PHE   A 1 42  ? 38.766 -16.405 29.347 1.00 26.09  ? 43  PHE   A CA  1 
ATOM   379  C  C   . PHE   A 1 42  ? 39.284 -16.214 27.945 1.00 29.81  ? 43  PHE   A C   1 
ATOM   380  O  O   . PHE   A 1 42  ? 39.132 -15.121 27.388 1.00 29.59  ? 43  PHE   A O   1 
ATOM   381  C  CB  . PHE   A 1 42  ? 37.234 -16.237 29.350 1.00 27.07  ? 43  PHE   A CB  1 
ATOM   382  C  CG  . PHE   A 1 42  ? 36.613 -16.327 30.723 1.00 29.10  ? 43  PHE   A CG  1 
ATOM   383  C  CD1 . PHE   A 1 42  ? 36.509 -15.197 31.535 1.00 31.57  ? 43  PHE   A CD1 1 
ATOM   384  C  CD2 . PHE   A 1 42  ? 36.160 -17.543 31.219 1.00 32.34  ? 43  PHE   A CD2 1 
ATOM   385  C  CE1 . PHE   A 1 42  ? 35.950 -15.283 32.812 1.00 33.49  ? 43  PHE   A CE1 1 
ATOM   386  C  CE2 . PHE   A 1 42  ? 35.613 -17.630 32.505 1.00 35.45  ? 43  PHE   A CE2 1 
ATOM   387  C  CZ  . PHE   A 1 42  ? 35.510 -16.500 33.291 1.00 33.07  ? 43  PHE   A CZ  1 
ATOM   388  N  N   . ARG   A 1 43  ? 39.891 -17.260 27.370 1.00 27.11  ? 44  ARG   A N   1 
ATOM   389  C  CA  . ARG   A 1 43  ? 40.411 -17.201 26.011 1.00 25.46  ? 44  ARG   A CA  1 
ATOM   390  C  C   . ARG   A 1 43  ? 39.286 -17.598 25.054 1.00 27.59  ? 44  ARG   A C   1 
ATOM   391  O  O   . ARG   A 1 43  ? 38.474 -18.480 25.369 1.00 26.71  ? 44  ARG   A O   1 
ATOM   392  C  CB  . ARG   A 1 43  ? 41.622 -18.138 25.829 1.00 27.11  ? 44  ARG   A CB  1 
ATOM   393  C  CG  . ARG   A 1 43  ? 42.859 -17.703 26.668 1.00 34.00  ? 44  ARG   A CG  1 
ATOM   394  C  CD  . ARG   A 1 43  ? 44.175 -18.115 26.022 1.00 42.91  ? 44  ARG   A CD  1 
ATOM   395  N  NE  . ARG   A 1 43  ? 44.192 -17.732 24.607 1.00 55.02  ? 44  ARG   A NE  1 
ATOM   396  C  CZ  . ARG   A 1 43  ? 44.769 -16.642 24.112 1.00 68.31  ? 44  ARG   A CZ  1 
ATOM   397  N  NH1 . ARG   A 1 43  ? 45.482 -15.845 24.896 1.00 60.77  ? 44  ARG   A NH1 1 
ATOM   398  N  NH2 . ARG   A 1 43  ? 44.680 -16.369 22.818 1.00 49.93  ? 44  ARG   A NH2 1 
ATOM   399  N  N   . ALA   A 1 44  ? 39.203 -16.932 23.903 1.00 23.99  ? 45  ALA   A N   1 
ATOM   400  C  CA  . ALA   A 1 44  ? 38.125 -17.244 22.944 1.00 23.95  ? 45  ALA   A CA  1 
ATOM   401  C  C   . ALA   A 1 44  ? 38.504 -16.827 21.533 1.00 26.08  ? 45  ALA   A C   1 
ATOM   402  O  O   . ALA   A 1 44  ? 39.597 -16.295 21.306 1.00 24.79  ? 45  ALA   A O   1 
ATOM   403  C  CB  . ALA   A 1 44  ? 36.817 -16.547 23.363 1.00 25.04  ? 45  ALA   A CB  1 
ATOM   404  N  N   . HIS   A 1 45  ? 37.607 -17.118 20.577 1.00 22.97  ? 46  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 45  ? 37.754 -16.703 19.193 1.00 22.32  ? 46  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 45  ? 36.874 -15.456 19.015 1.00 25.33  ? 46  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 45  ? 35.663 -15.498 19.306 1.00 23.73  ? 46  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 45  ? 37.290 -17.822 18.238 1.00 21.73  ? 46  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 45  ? 38.057 -19.099 18.422 1.00 24.85  ? 46  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 45  ? 37.580 -20.122 19.246 1.00 26.70  ? 46  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 45  ? 39.282 -19.450 17.957 1.00 26.05  ? 46  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 45  ? 38.502 -21.078 19.204 1.00 26.82  ? 46  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 45  ? 39.558 -20.707 18.463 1.00 26.57  ? 46  HIS   A NE2 1 
ATOM   414  N  N   . LYS   A 1 46  ? 37.477 -14.359 18.547 1.00 24.20  ? 47  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 46  ? 36.747 -13.097 18.294 1.00 23.38  ? 47  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 46  ? 35.506 -13.355 17.415 1.00 25.36  ? 47  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 46  ? 34.439 -12.841 17.727 1.00 22.68  ? 47  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 46  ? 37.661 -12.089 17.574 1.00 25.65  ? 47  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 46  ? 38.640 -11.454 18.531 1.00 25.98  ? 47  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 46  ? 39.595 -10.565 17.726 1.00 25.11  ? 47  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 46  ? 40.631 -10.014 18.652 1.00 30.74  ? 47  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 46  ? 41.644 -9.272  17.880 1.00 31.12  ? 47  LYS   A NZ  1 
ATOM   423  N  N   . THR   A 1 47  ? 35.632 -14.170 16.364 1.00 22.39  ? 48  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 47  ? 34.504 -14.407 15.456 1.00 22.00  ? 48  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 47  ? 33.319 -15.052 16.144 1.00 23.26  ? 48  THR   A C   1 
ATOM   426  O  O   . THR   A 1 47  ? 32.179 -14.680 15.866 1.00 23.61  ? 48  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 47  ? 34.935 -15.182 14.213 1.00 29.51  ? 48  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 47  ? 35.552 -16.392 14.644 1.00 30.30  ? 48  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 47  ? 35.839 -14.355 13.313 1.00 30.67  ? 48  THR   A CG2 1 
ATOM   430  N  N   . VAL   A 1 48  ? 33.577 -16.017 17.028 1.00 20.17  ? 49  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 48  ? 32.493 -16.706 17.739 1.00 19.91  ? 49  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 48  ? 31.828 -15.724 18.695 1.00 22.77  ? 49  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 48  ? 30.586 -15.686 18.787 1.00 20.68  ? 49  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 48  ? 33.005 -17.971 18.469 1.00 21.64  ? 49  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 48  ? 31.888 -18.595 19.326 1.00 22.48  ? 49  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 48  ? 33.519 -19.005 17.444 1.00 21.47  ? 49  VAL   A CG2 1 
ATOM   437  N  N   . LEU   A 1 49  ? 32.643 -14.935 19.423 1.00 20.80  ? 50  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 49  ? 32.065 -13.927 20.325 1.00 20.88  ? 50  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 49  ? 31.153 -12.939 19.568 1.00 23.10  ? 50  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 49  ? 30.045 -12.638 20.032 1.00 22.44  ? 50  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 49  ? 33.173 -13.145 21.067 1.00 20.74  ? 50  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 49  ? 34.153 -13.946 21.973 1.00 23.97  ? 50  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 49  ? 35.186 -13.011 22.610 1.00 24.33  ? 50  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 49  ? 33.397 -14.709 23.069 1.00 25.07  ? 50  LEU   A CD2 1 
ATOM   445  N  N   . MET   A 1 50  ? 31.604 -12.462 18.402 1.00 20.53  ? 51  MET   A N   1 
ATOM   446  C  CA  . MET   A 1 50  ? 30.817 -11.537 17.581 1.00 21.88  ? 51  MET   A CA  1 
ATOM   447  C  C   . MET   A 1 50  ? 29.523 -12.178 17.087 1.00 26.16  ? 51  MET   A C   1 
ATOM   448  O  O   . MET   A 1 50  ? 28.469 -11.537 17.105 1.00 25.86  ? 51  MET   A O   1 
ATOM   449  C  CB  . MET   A 1 50  ? 31.630 -11.051 16.389 1.00 23.51  ? 51  MET   A CB  1 
ATOM   450  C  CG  . MET   A 1 50  ? 32.849 -10.249 16.778 1.00 25.79  ? 51  MET   A CG  1 
ATOM   451  S  SD  . MET   A 1 50  ? 33.897 -10.167 15.318 1.00 30.33  ? 51  MET   A SD  1 
ATOM   452  C  CE  . MET   A 1 50  ? 33.104 -8.862  14.466 1.00 27.07  ? 51  MET   A CE  1 
ATOM   453  N  N   . ALA   A 1 51  ? 29.593 -13.465 16.702 1.00 22.79  ? 52  ALA   A N   1 
ATOM   454  C  CA  . ALA   A 1 51  ? 28.436 -14.206 16.187 1.00 22.55  ? 52  ALA   A CA  1 
ATOM   455  C  C   . ALA   A 1 51  ? 27.332 -14.400 17.259 1.00 24.64  ? 52  ALA   A C   1 
ATOM   456  O  O   . ALA   A 1 51  ? 26.179 -14.639 16.898 1.00 26.61  ? 52  ALA   A O   1 
ATOM   457  C  CB  . ALA   A 1 51  ? 28.882 -15.561 15.626 1.00 22.96  ? 52  ALA   A CB  1 
ATOM   458  N  N   . CYS   A 1 52  ? 27.700 -14.326 18.561 1.00 20.96  ? 53  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 52  ? 26.797 -14.591 19.687 1.00 21.19  ? 53  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 52  ? 26.344 -13.377 20.474 1.00 25.37  ? 53  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 52  ? 25.397 -13.513 21.251 1.00 23.96  ? 53  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 52  ? 27.457 -15.596 20.633 1.00 21.44  ? 53  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 52  ? 27.827 -17.190 19.878 1.00 24.83  ? 53  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 53  ? 27.102 -12.273 20.401 1.00 22.29  ? 54  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 53  ? 26.913 -11.120 21.286 1.00 21.25  ? 54  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 53  ? 26.909 -9.817  20.531 1.00 25.32  ? 54  SER   A C   1 
ATOM   467  O  O   . SER   A 1 53  ? 27.879 -9.523  19.821 1.00 23.62  ? 54  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 53  ? 28.038 -11.148 22.321 1.00 22.72  ? 54  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 53  ? 28.365 -9.906  22.927 1.00 25.59  ? 54  SER   A OG  1 
ATOM   470  N  N   . GLY   A 1 54  ? 25.866 -9.004  20.747 1.00 23.29  ? 55  GLY   A N   1 
ATOM   471  C  CA  . GLY   A 1 54  ? 25.798 -7.668  20.154 1.00 22.91  ? 55  GLY   A CA  1 
ATOM   472  C  C   . GLY   A 1 54  ? 26.922 -6.778  20.658 1.00 26.40  ? 55  GLY   A C   1 
ATOM   473  O  O   . GLY   A 1 54  ? 27.475 -5.980  19.887 1.00 26.48  ? 55  GLY   A O   1 
ATOM   474  N  N   . LEU   A 1 55  ? 27.327 -6.963  21.941 1.00 24.27  ? 56  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 55  ? 28.442 -6.184  22.501 1.00 25.72  ? 56  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 55  ? 29.774 -6.527  21.801 1.00 27.21  ? 56  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 55  ? 30.460 -5.609  21.342 1.00 25.35  ? 56  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 55  ? 28.553 -6.377  24.028 1.00 25.98  ? 56  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 55  ? 29.605 -5.497  24.720 1.00 30.72  ? 56  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 55  ? 29.180 -4.016  24.735 1.00 31.67  ? 56  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 55  ? 29.874 -5.983  26.123 1.00 28.63  ? 56  LEU   A CD2 1 
ATOM   482  N  N   . PHE   A 1 56  ? 30.110 -7.837  21.672 1.00 22.54  ? 57  PHE   A N   1 
ATOM   483  C  CA  . PHE   A 1 56  ? 31.369 -8.219  21.001 1.00 22.04  ? 57  PHE   A CA  1 
ATOM   484  C  C   . PHE   A 1 56  ? 31.350 -7.872  19.535 1.00 26.04  ? 57  PHE   A C   1 
ATOM   485  O  O   . PHE   A 1 56  ? 32.389 -7.499  18.993 1.00 24.44  ? 57  PHE   A O   1 
ATOM   486  C  CB  . PHE   A 1 56  ? 31.740 -9.685  21.248 1.00 22.90  ? 57  PHE   A CB  1 
ATOM   487  C  CG  . PHE   A 1 56  ? 32.138 -9.910  22.691 1.00 24.00  ? 57  PHE   A CG  1 
ATOM   488  C  CD1 . PHE   A 1 56  ? 33.208 -9.215  23.255 1.00 26.29  ? 57  PHE   A CD1 1 
ATOM   489  C  CD2 . PHE   A 1 56  ? 31.492 -10.874 23.464 1.00 25.57  ? 57  PHE   A CD2 1 
ATOM   490  C  CE1 . PHE   A 1 56  ? 33.566 -9.412  24.605 1.00 27.30  ? 57  PHE   A CE1 1 
ATOM   491  C  CE2 . PHE   A 1 56  ? 31.899 -11.122 24.783 1.00 28.17  ? 57  PHE   A CE2 1 
ATOM   492  C  CZ  . PHE   A 1 56  ? 32.918 -10.380 25.349 1.00 25.74  ? 57  PHE   A CZ  1 
ATOM   493  N  N   . TYR   A 1 57  ? 30.162 -7.941  18.898 1.00 23.15  ? 58  TYR   A N   1 
ATOM   494  C  CA  . TYR   A 1 57  ? 30.038 -7.536  17.487 1.00 24.50  ? 58  TYR   A CA  1 
ATOM   495  C  C   . TYR   A 1 57  ? 30.464 -6.068  17.327 1.00 28.65  ? 58  TYR   A C   1 
ATOM   496  O  O   . TYR   A 1 57  ? 31.263 -5.764  16.441 1.00 26.42  ? 58  TYR   A O   1 
ATOM   497  C  CB  . TYR   A 1 57  ? 28.598 -7.772  17.007 1.00 26.46  ? 58  TYR   A CB  1 
ATOM   498  C  CG  . TYR   A 1 57  ? 28.334 -7.241  15.622 1.00 30.36  ? 58  TYR   A CG  1 
ATOM   499  C  CD1 . TYR   A 1 57  ? 28.941 -7.813  14.506 1.00 32.24  ? 58  TYR   A CD1 1 
ATOM   500  C  CD2 . TYR   A 1 57  ? 27.493 -6.151  15.425 1.00 34.56  ? 58  TYR   A CD2 1 
ATOM   501  C  CE1 . TYR   A 1 57  ? 28.700 -7.319  13.222 1.00 34.89  ? 58  TYR   A CE1 1 
ATOM   502  C  CE2 . TYR   A 1 57  ? 27.237 -5.659  14.151 1.00 37.76  ? 58  TYR   A CE2 1 
ATOM   503  C  CZ  . TYR   A 1 57  ? 27.831 -6.256  13.053 1.00 44.29  ? 58  TYR   A CZ  1 
ATOM   504  O  OH  . TYR   A 1 57  ? 27.557 -5.761  11.812 1.00 50.54  ? 58  TYR   A OH  1 
ATOM   505  N  N   A SER   A 1 58  ? 29.940 -5.172  18.187 0.53 26.17  ? 59  SER   A N   1 
ATOM   506  N  N   B SER   A 1 58  ? 29.936 -5.180  18.192 0.47 26.06  ? 59  SER   A N   1 
ATOM   507  C  CA  A SER   A 1 58  ? 30.264 -3.742  18.174 0.53 27.12  ? 59  SER   A CA  1 
ATOM   508  C  CA  B SER   A 1 58  ? 30.252 -3.752  18.202 0.47 27.00  ? 59  SER   A CA  1 
ATOM   509  C  C   A SER   A 1 58  ? 31.752 -3.510  18.490 0.53 31.80  ? 59  SER   A C   1 
ATOM   510  C  C   B SER   A 1 58  ? 31.751 -3.538  18.472 0.47 31.60  ? 59  SER   A C   1 
ATOM   511  O  O   A SER   A 1 58  ? 32.401 -2.719  17.807 0.53 33.50  ? 59  SER   A O   1 
ATOM   512  O  O   B SER   A 1 58  ? 32.399 -2.787  17.745 0.47 33.06  ? 59  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 58  ? 29.367 -2.996  19.157 0.53 30.22  ? 59  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 58  ? 29.416 -3.041  19.264 0.47 29.98  ? 59  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 58  ? 28.020 -3.044  18.714 0.53 33.89  ? 59  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 58  ? 29.721 -1.658  19.288 0.47 35.47  ? 59  SER   A OG  1 
ATOM   517  N  N   . ILE   A 1 59  ? 32.299 -4.228  19.493 1.00 27.58  ? 60  ILE   A N   1 
ATOM   518  C  CA  . ILE   A 1 59  ? 33.718 -4.114  19.890 1.00 27.26  ? 60  ILE   A CA  1 
ATOM   519  C  C   . ILE   A 1 59  ? 34.663 -4.507  18.759 1.00 29.98  ? 60  ILE   A C   1 
ATOM   520  O  O   . ILE   A 1 59  ? 35.543 -3.721  18.389 1.00 30.73  ? 60  ILE   A O   1 
ATOM   521  C  CB  . ILE   A 1 59  ? 34.047 -4.936  21.193 1.00 28.94  ? 60  ILE   A CB  1 
ATOM   522  C  CG1 . ILE   A 1 59  ? 33.311 -4.379  22.437 1.00 29.49  ? 60  ILE   A CG1 1 
ATOM   523  C  CG2 . ILE   A 1 59  ? 35.579 -4.997  21.451 1.00 27.86  ? 60  ILE   A CG2 1 
ATOM   524  C  CD1 . ILE   A 1 59  ? 33.365 -5.403  23.648 1.00 31.19  ? 60  ILE   A CD1 1 
ATOM   525  N  N   . PHE   A 1 60  ? 34.477 -5.699  18.190 1.00 24.78  ? 61  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 60  ? 35.452 -6.144  17.213 1.00 25.70  ? 61  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 60  ? 35.230 -5.608  15.795 1.00 30.02  ? 61  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 60  ? 36.075 -5.867  14.937 1.00 31.42  ? 61  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 60  ? 35.630 -7.666  17.246 1.00 25.99  ? 61  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 60  ? 36.045 -8.164  18.622 1.00 26.89  ? 61  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 60  ? 37.249 -7.759  19.197 1.00 30.73  ? 61  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 60  ? 35.228 -9.027  19.341 1.00 27.67  ? 61  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 60  ? 37.624 -8.213  20.470 1.00 31.19  ? 61  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 60  ? 35.623 -9.513  20.595 1.00 30.05  ? 61  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 60  ? 36.811 -9.097  21.155 1.00 28.91  ? 61  PHE   A CZ  1 
ATOM   536  N  N   . THR   A 1 61  ? 34.151 -4.838  15.549 1.00 27.91  ? 62  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 61  ? 33.997 -4.137  14.252 1.00 28.63  ? 62  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 61  ? 34.551 -2.713  14.392 1.00 35.95  ? 62  THR   A C   1 
ATOM   539  O  O   . THR   A 1 61  ? 34.644 -1.975  13.400 1.00 35.31  ? 62  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 61  ? 32.572 -4.166  13.689 1.00 34.85  ? 62  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 61  ? 31.666 -3.659  14.664 1.00 32.50  ? 62  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 61  ? 32.143 -5.565  13.215 1.00 31.95  ? 62  THR   A CG2 1 
ATOM   543  N  N   . ASP   A 1 62  ? 34.958 -2.327  15.619 1.00 32.79  ? 63  ASP   A N   1 
ATOM   544  C  CA  . ASP   A 1 62  ? 35.571 -1.014  15.823 1.00 34.33  ? 63  ASP   A CA  1 
ATOM   545  C  C   . ASP   A 1 62  ? 36.998 -1.069  15.262 1.00 39.12  ? 63  ASP   A C   1 
ATOM   546  O  O   . ASP   A 1 62  ? 37.759 -1.964  15.623 1.00 36.22  ? 63  ASP   A O   1 
ATOM   547  C  CB  . ASP   A 1 62  ? 35.575 -0.621  17.309 1.00 36.16  ? 63  ASP   A CB  1 
ATOM   548  C  CG  . ASP   A 1 62  ? 36.300 0.685   17.533 1.00 48.10  ? 63  ASP   A CG  1 
ATOM   549  O  OD1 . ASP   A 1 62  ? 35.662 1.743   17.395 1.00 52.98  ? 63  ASP   A OD1 1 
ATOM   550  O  OD2 . ASP   A 1 62  ? 37.524 0.648   17.786 1.00 47.51  ? 63  ASP   A OD2 1 
ATOM   551  N  N   . GLN   A 1 63  ? 37.363 -0.095  14.406 1.00 40.52  ? 64  GLN   A N   1 
ATOM   552  C  CA  . GLN   A 1 63  ? 38.666 -0.033  13.736 1.00 41.85  ? 64  GLN   A CA  1 
ATOM   553  C  C   . GLN   A 1 63  ? 39.878 -0.065  14.682 1.00 45.36  ? 64  GLN   A C   1 
ATOM   554  O  O   . GLN   A 1 63  ? 40.941 -0.515  14.252 1.00 47.76  ? 64  GLN   A O   1 
ATOM   555  C  CB  . GLN   A 1 63  ? 38.745 1.166   12.777 1.00 45.45  ? 64  GLN   A CB  1 
ATOM   556  C  CG  . GLN   A 1 63  ? 37.901 0.983   11.518 1.00 62.15  ? 64  GLN   A CG  1 
ATOM   557  N  N   . LEU   A 1 64  ? 39.738 0.403   15.946 1.00 38.04  ? 65  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 64  ? 40.827 0.334   16.922 1.00 37.14  ? 65  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 64  ? 40.735 -0.918  17.781 1.00 40.84  ? 65  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 64  ? 41.753 -1.553  18.048 1.00 42.54  ? 65  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 64  ? 40.821 1.552   17.871 1.00 37.97  ? 65  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 64  ? 41.442 2.829   17.349 1.00 44.46  ? 65  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 64  ? 41.335 3.928   18.387 1.00 45.25  ? 65  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 64  ? 42.909 2.638   16.956 1.00 49.61  ? 65  LEU   A CD2 1 
ATOM   565  N  N   . LYS   A 1 65  ? 39.535 -1.232  18.287 1.00 34.20  ? 66  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 65  ? 39.367 -2.354  19.216 1.00 32.59  ? 66  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 65  ? 39.518 -3.718  18.551 1.00 37.80  ? 66  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 65  ? 39.923 -4.662  19.227 1.00 36.93  ? 66  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 65  ? 38.047 -2.265  20.001 1.00 32.88  ? 66  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 65  ? 37.942 -1.035  20.898 1.00 32.06  ? 66  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 65  ? 36.650 -1.078  21.701 1.00 30.19  ? 66  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 65  ? 36.361 0.242   22.384 1.00 34.54  ? 66  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 65  ? 35.819 1.259   21.452 1.00 37.55  ? 66  LYS   A NZ  1 
ATOM   574  N  N   . CYS   A 1 66  ? 39.253 -3.806  17.230 1.00 37.21  ? 67  CYS   A N   1 
ATOM   575  C  CA  . CYS   A 1 66  ? 39.389 -5.055  16.455 1.00 38.01  ? 67  CYS   A CA  1 
ATOM   576  C  C   . CYS   A 1 66  ? 40.782 -5.684  16.606 1.00 42.00  ? 67  CYS   A C   1 
ATOM   577  O  O   . CYS   A 1 66  ? 40.917 -6.899  16.431 1.00 42.17  ? 67  CYS   A O   1 
ATOM   578  C  CB  . CYS   A 1 66  ? 39.035 -4.835  14.985 1.00 40.29  ? 67  CYS   A CB  1 
ATOM   579  S  SG  . CYS   A 1 66  ? 40.188 -3.757  14.080 1.00 46.86  ? 67  CYS   A SG  1 
ATOM   580  N  N   . ASN   A 1 67  ? 41.810 -4.845  16.894 1.00 37.89  ? 68  ASN   A N   1 
ATOM   581  C  CA  . ASN   A 1 67  ? 43.215 -5.237  17.015 1.00 38.75  ? 68  ASN   A CA  1 
ATOM   582  C  C   . ASN   A 1 67  ? 43.692 -5.523  18.439 1.00 41.04  ? 68  ASN   A C   1 
ATOM   583  O  O   . ASN   A 1 67  ? 44.862 -5.870  18.639 1.00 40.15  ? 68  ASN   A O   1 
ATOM   584  C  CB  . ASN   A 1 67  ? 44.116 -4.188  16.340 1.00 40.86  ? 68  ASN   A CB  1 
ATOM   585  C  CG  . ASN   A 1 67  ? 43.871 -4.096  14.843 1.00 54.36  ? 68  ASN   A CG  1 
ATOM   586  O  OD1 . ASN   A 1 67  ? 43.773 -3.007  14.276 1.00 55.54  ? 68  ASN   A OD1 1 
ATOM   587  N  ND2 . ASN   A 1 67  ? 43.713 -5.236  14.173 1.00 43.98  ? 68  ASN   A ND2 1 
ATOM   588  N  N   . LEU   A 1 68  ? 42.810 -5.362  19.433 1.00 37.02  ? 69  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 68  ? 43.202 -5.625  20.809 1.00 36.23  ? 69  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 68  ? 43.196 -7.124  21.079 1.00 38.71  ? 69  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 68  ? 42.311 -7.835  20.581 1.00 37.22  ? 69  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 68  ? 42.258 -4.913  21.798 1.00 36.17  ? 69  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 68  ? 42.227 -3.379  21.717 1.00 41.40  ? 69  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 68  ? 41.161 -2.826  22.643 1.00 41.34  ? 69  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 68  ? 43.596 -2.763  22.051 1.00 43.50  ? 69  LEU   A CD2 1 
ATOM   596  N  N   A SER   A 1 69  ? 44.172 -7.602  21.867 0.51 35.77  ? 70  SER   A N   1 
ATOM   597  N  N   B SER   A 1 69  ? 44.176 -7.591  21.870 0.49 35.57  ? 70  SER   A N   1 
ATOM   598  C  CA  A SER   A 1 69  ? 44.264 -9.017  22.238 0.51 35.19  ? 70  SER   A CA  1 
ATOM   599  C  CA  B SER   A 1 69  ? 44.315 -8.997  22.260 0.49 34.95  ? 70  SER   A CA  1 
ATOM   600  C  C   A SER   A 1 69  ? 43.652 -9.246  23.627 0.51 35.95  ? 70  SER   A C   1 
ATOM   601  C  C   B SER   A 1 69  ? 43.679 -9.239  23.634 0.49 35.89  ? 70  SER   A C   1 
ATOM   602  O  O   A SER   A 1 69  ? 43.450 -10.392 24.028 0.51 33.77  ? 70  SER   A O   1 
ATOM   603  O  O   B SER   A 1 69  ? 43.490 -10.389 24.031 0.49 33.72  ? 70  SER   A O   1 
ATOM   604  C  CB  A SER   A 1 69  ? 45.713 -9.495  22.195 0.51 40.44  ? 70  SER   A CB  1 
ATOM   605  C  CB  B SER   A 1 69  ? 45.787 -9.400  22.277 0.49 39.82  ? 70  SER   A CB  1 
ATOM   606  O  OG  A SER   A 1 69  ? 46.525 -8.758  23.093 0.51 49.01  ? 70  SER   A OG  1 
ATOM   607  O  OG  B SER   A 1 69  ? 46.327 -9.395  20.967 0.49 46.29  ? 70  SER   A OG  1 
ATOM   608  N  N   . VAL   A 1 70  ? 43.376 -8.147  24.367 1.00 32.77  ? 71  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 70  ? 42.768 -8.184  25.702 1.00 32.48  ? 71  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 70  ? 41.586 -7.198  25.737 1.00 33.46  ? 71  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 70  ? 41.744 -6.027  25.344 1.00 32.17  ? 71  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 70  ? 43.802 -7.842  26.827 1.00 38.11  ? 71  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 70  ? 43.146 -7.839  28.212 1.00 38.07  ? 71  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 70  ? 45.001 -8.792  26.805 1.00 38.79  ? 71  VAL   A CG2 1 
ATOM   615  N  N   . ILE   A 1 71  ? 40.423 -7.673  26.223 1.00 26.58  ? 72  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 71  ? 39.219 -6.860  26.427 1.00 25.89  ? 72  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 71  ? 38.829 -6.979  27.891 1.00 29.66  ? 72  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 71  ? 38.603 -8.093  28.374 1.00 30.04  ? 72  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 71  ? 38.057 -7.253  25.468 1.00 27.97  ? 72  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 71  ? 38.457 -7.085  23.965 1.00 28.77  ? 72  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 71  ? 36.750 -6.516  25.815 1.00 28.97  ? 72  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 71  ? 38.796 -5.634  23.474 1.00 33.77  ? 72  ILE   A CD1 1 
ATOM   623  N  N   . ASN   A 1 72  ? 38.724 -5.828  28.591 1.00 27.66  ? 73  ASN   A N   1 
ATOM   624  C  CA  . ASN   A 1 72  ? 38.329 -5.808  29.985 1.00 28.27  ? 73  ASN   A CA  1 
ATOM   625  C  C   . ASN   A 1 72  ? 36.852 -5.484  30.094 1.00 30.52  ? 73  ASN   A C   1 
ATOM   626  O  O   . ASN   A 1 72  ? 36.428 -4.406  29.663 1.00 28.74  ? 73  ASN   A O   1 
ATOM   627  C  CB  . ASN   A 1 72  ? 39.145 -4.772  30.779 1.00 32.19  ? 73  ASN   A CB  1 
ATOM   628  C  CG  . ASN   A 1 72  ? 40.626 -4.985  30.719 1.00 50.96  ? 73  ASN   A CG  1 
ATOM   629  O  OD1 . ASN   A 1 72  ? 41.143 -6.019  31.127 1.00 41.41  ? 73  ASN   A OD1 1 
ATOM   630  N  ND2 . ASN   A 1 72  ? 41.344 -3.994  30.231 1.00 47.46  ? 73  ASN   A ND2 1 
ATOM   631  N  N   . LEU   A 1 73  ? 36.082 -6.386  30.704 1.00 25.85  ? 74  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 73  ? 34.655 -6.160  30.906 1.00 25.81  ? 74  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 73  ? 34.416 -5.274  32.123 1.00 29.53  ? 74  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 73  ? 35.300 -5.127  32.985 1.00 30.22  ? 74  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 73  ? 33.852 -7.478  31.044 1.00 25.07  ? 74  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 73  ? 33.897 -8.504  29.874 1.00 27.89  ? 74  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 73  ? 32.745 -9.539  30.018 1.00 28.61  ? 74  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 73  ? 33.863 -7.820  28.493 1.00 27.79  ? 74  LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 74  ? 33.215 -4.695  32.202 1.00 26.57  ? 75  ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 74  ? 32.789 -3.826  33.308 1.00 28.14  ? 75  ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 74  ? 32.986 -4.593  34.641 1.00 32.24  ? 75  ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 74  ? 32.666 -5.786  34.702 1.00 31.27  ? 75  ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 74  ? 31.313 -3.452  33.105 1.00 29.90  ? 75  ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 74  ? 30.755 -2.441  34.089 1.00 39.92  ? 75  ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 74  ? 30.648 -2.773  35.292 1.00 40.79  ? 75  ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 74  ? 30.385 -1.338  33.653 1.00 40.91  ? 75  ASP   A OD2 1 
ATOM   647  N  N   . PRO   A 1 75  ? 33.539 -3.945  35.687 1.00 33.59  ? 76  PRO   A N   1 
ATOM   648  C  CA  . PRO   A 1 75  ? 33.777 -4.664  36.962 1.00 33.69  ? 76  PRO   A CA  1 
ATOM   649  C  C   . PRO   A 1 75  ? 32.549 -5.247  37.642 1.00 37.11  ? 76  PRO   A C   1 
ATOM   650  O  O   . PRO   A 1 75  ? 32.710 -6.107  38.501 1.00 38.61  ? 76  PRO   A O   1 
ATOM   651  C  CB  . PRO   A 1 75  ? 34.460 -3.618  37.861 1.00 36.75  ? 76  PRO   A CB  1 
ATOM   652  C  CG  . PRO   A 1 75  ? 34.169 -2.299  37.230 1.00 42.06  ? 76  PRO   A CG  1 
ATOM   653  C  CD  . PRO   A 1 75  ? 34.006 -2.543  35.760 1.00 36.25  ? 76  PRO   A CD  1 
ATOM   654  N  N   . GLU   A 1 76  ? 31.335 -4.810  37.262 1.00 33.70  ? 77  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 76  ? 30.087 -5.325  37.830 1.00 34.78  ? 77  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 76  ? 29.793 -6.740  37.275 1.00 34.17  ? 77  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 76  ? 28.970 -7.457  37.840 1.00 33.42  ? 77  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 76  ? 28.914 -4.386  37.472 1.00 37.59  ? 77  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 76  ? 27.769 -4.394  38.470 1.00 58.75  ? 77  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 76  ? 27.993 -3.532  39.699 1.00 89.49  ? 77  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 76  ? 28.064 -2.290  39.551 1.00 90.49  ? 77  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 76  ? 28.095 -4.099  40.811 1.00 84.76  ? 77  GLU   A OE2 1 
ATOM   663  N  N   . ILE   A 1 77  ? 30.446 -7.124  36.172 1.00 29.26  ? 78  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 77  ? 30.203 -8.432  35.550 1.00 29.03  ? 78  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 77  ? 30.786 -9.563  36.376 1.00 33.76  ? 78  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 77  ? 31.954 -9.535  36.766 1.00 32.83  ? 78  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 77  ? 30.665 -8.457  34.068 1.00 31.25  ? 78  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 77  ? 29.932 -7.350  33.256 1.00 31.90  ? 78  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 77  ? 30.447 -9.852  33.447 1.00 28.70  ? 78  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 77  ? 28.311 -7.393  33.288 1.00 36.85  ? 78  ILE   A CD1 1 
ATOM   671  N  N   . ASN   A 1 78  ? 29.950 -10.551 36.629 1.00 33.51  ? 79  ASN   A N   1 
ATOM   672  C  CA  . ASN   A 1 78  ? 30.280 -11.726 37.414 1.00 33.82  ? 79  ASN   A CA  1 
ATOM   673  C  C   . ASN   A 1 78  ? 31.033 -12.756 36.553 1.00 33.59  ? 79  ASN   A C   1 
ATOM   674  O  O   . ASN   A 1 78  ? 30.507 -13.166 35.521 1.00 31.43  ? 79  ASN   A O   1 
ATOM   675  C  CB  . ASN   A 1 78  ? 28.988 -12.301 37.997 1.00 36.29  ? 79  ASN   A CB  1 
ATOM   676  C  CG  . ASN   A 1 78  ? 29.188 -13.578 38.755 1.00 50.92  ? 79  ASN   A CG  1 
ATOM   677  O  OD1 . ASN   A 1 78  ? 28.874 -14.648 38.253 1.00 40.21  ? 79  ASN   A OD1 1 
ATOM   678  N  ND2 . ASN   A 1 78  ? 29.727 -13.491 39.970 1.00 42.75  ? 79  ASN   A ND2 1 
ATOM   679  N  N   . PRO   A 1 79  ? 32.246 -13.206 36.970 1.00 30.82  ? 80  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 79  ? 32.993 -14.197 36.162 1.00 30.19  ? 80  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 79  ? 32.240 -15.511 35.903 1.00 33.21  ? 80  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 79  ? 32.351 -16.067 34.802 1.00 32.42  ? 80  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 79  ? 34.268 -14.428 36.980 1.00 33.75  ? 80  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 79  ? 34.405 -13.203 37.837 1.00 38.49  ? 80  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 79  ? 33.006 -12.819 38.179 1.00 34.25  ? 80  PRO   A CD  1 
ATOM   686  N  N   . GLU   A 1 80  ? 31.459 -16.006 36.898 1.00 30.07  ? 81  GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 80  ? 30.705 -17.250 36.700 1.00 30.14  ? 81  GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 80  ? 29.615 -17.066 35.627 1.00 31.50  ? 81  GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 80  ? 29.479 -17.926 34.760 1.00 28.98  ? 81  GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 80  ? 30.108 -17.775 38.016 1.00 33.12  ? 81  GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 80  ? 29.505 -19.159 37.807 1.00 39.92  ? 81  GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 80  ? 28.714 -19.775 38.947 1.00 66.32  ? 81  GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 80  ? 28.733 -21.021 39.056 1.00 67.07  ? 81  GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 80  ? 28.065 -19.028 39.716 1.00 58.60  ? 81  GLU   A OE2 1 
ATOM   695  N  N   . GLY   A 1 81  ? 28.888 -15.939 35.685 1.00 29.67  ? 82  GLY   A N   1 
ATOM   696  C  CA  . GLY   A 1 81  ? 27.862 -15.600 34.703 1.00 29.23  ? 82  GLY   A CA  1 
ATOM   697  C  C   . GLY   A 1 81  ? 28.468 -15.547 33.311 1.00 29.29  ? 82  GLY   A C   1 
ATOM   698  O  O   . GLY   A 1 81  ? 27.902 -16.088 32.342 1.00 26.52  ? 82  GLY   A O   1 
ATOM   699  N  N   . PHE   A 1 82  ? 29.656 -14.926 33.210 1.00 25.81  ? 83  PHE   A N   1 
ATOM   700  C  CA  . PHE   A 1 82  ? 30.349 -14.858 31.921 1.00 24.21  ? 83  PHE   A CA  1 
ATOM   701  C  C   . PHE   A 1 82  ? 30.738 -16.264 31.450 1.00 25.64  ? 83  PHE   A C   1 
ATOM   702  O  O   . PHE   A 1 82  ? 30.558 -16.593 30.277 1.00 25.42  ? 83  PHE   A O   1 
ATOM   703  C  CB  . PHE   A 1 82  ? 31.605 -13.956 31.983 1.00 25.66  ? 83  PHE   A CB  1 
ATOM   704  C  CG  . PHE   A 1 82  ? 32.214 -13.828 30.603 1.00 26.22  ? 83  PHE   A CG  1 
ATOM   705  C  CD1 . PHE   A 1 82  ? 31.647 -12.982 29.651 1.00 29.64  ? 83  PHE   A CD1 1 
ATOM   706  C  CD2 . PHE   A 1 82  ? 33.274 -14.640 30.215 1.00 27.17  ? 83  PHE   A CD2 1 
ATOM   707  C  CE1 . PHE   A 1 82  ? 32.146 -12.935 28.347 1.00 30.35  ? 83  PHE   A CE1 1 
ATOM   708  C  CE2 . PHE   A 1 82  ? 33.783 -14.582 28.916 1.00 29.40  ? 83  PHE   A CE2 1 
ATOM   709  C  CZ  . PHE   A 1 82  ? 33.192 -13.758 27.979 1.00 27.99  ? 83  PHE   A CZ  1 
ATOM   710  N  N   . CYS   A 1 83  ? 31.314 -17.074 32.349 1.00 25.70  ? 84  CYS   A N   1 
ATOM   711  C  CA  . CYS   A 1 83  ? 31.715 -18.446 32.012 1.00 28.51  ? 84  CYS   A CA  1 
ATOM   712  C  C   . CYS   A 1 83  ? 30.533 -19.268 31.440 1.00 28.72  ? 84  CYS   A C   1 
ATOM   713  O  O   . CYS   A 1 83  ? 30.685 -19.958 30.420 1.00 26.65  ? 84  CYS   A O   1 
ATOM   714  C  CB  . CYS   A 1 83  ? 32.321 -19.131 33.232 1.00 32.47  ? 84  CYS   A CB  1 
ATOM   715  S  SG  . CYS   A 1 83  ? 33.027 -20.756 32.861 1.00 38.19  ? 84  CYS   A SG  1 
ATOM   716  N  N   . ILE   A 1 84  ? 29.354 -19.179 32.105 1.00 25.89  ? 85  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 84  ? 28.133 -19.883 31.705 1.00 24.54  ? 85  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 84  ? 27.727 -19.438 30.299 1.00 25.74  ? 85  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 84  ? 27.381 -20.281 29.454 1.00 23.70  ? 85  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 84  ? 27.010 -19.646 32.759 1.00 26.98  ? 85  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 84  ? 27.296 -20.458 34.078 1.00 27.58  ? 85  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 84  ? 25.604 -19.945 32.179 1.00 27.17  ? 85  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 84  ? 26.583 -19.958 35.259 1.00 34.37  ? 85  ILE   A CD1 1 
ATOM   724  N  N   . LEU   A 1 85  ? 27.809 -18.134 30.042 1.00 22.76  ? 86  LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 85  ? 27.446 -17.600 28.721 1.00 22.57  ? 86  LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 85  ? 28.454 -17.949 27.649 1.00 24.15  ? 86  LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 85  ? 28.056 -18.212 26.514 1.00 22.66  ? 86  LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 85  ? 27.168 -16.109 28.780 1.00 23.49  ? 86  LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 85  ? 25.892 -15.739 29.565 1.00 28.72  ? 86  LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 85  ? 25.810 -14.274 29.752 1.00 30.10  ? 86  LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 85  ? 24.615 -16.221 28.857 1.00 29.87  ? 86  LEU   A CD2 1 
ATOM   732  N  N   . LEU   A 1 86  ? 29.755 -17.930 27.984 1.00 22.43  ? 87  LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 86  ? 30.799 -18.337 27.032 1.00 21.45  ? 87  LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 86  ? 30.558 -19.817 26.636 1.00 24.75  ? 87  LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 86  ? 30.615 -20.160 25.456 1.00 23.35  ? 87  LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 86  ? 32.188 -18.139 27.652 1.00 21.49  ? 87  LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 86  ? 33.351 -18.440 26.680 1.00 25.65  ? 87  LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 86  ? 33.286 -17.539 25.425 1.00 25.50  ? 87  LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 86  ? 34.723 -18.306 27.401 1.00 28.23  ? 87  LEU   A CD2 1 
ATOM   740  N  N   . ASP   A 1 87  ? 30.280 -20.693 27.621 1.00 22.35  ? 88  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 87  ? 29.945 -22.091 27.332 1.00 22.43  ? 88  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 87  ? 28.738 -22.175 26.399 1.00 24.01  ? 88  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 87  ? 28.769 -22.949 25.451 1.00 24.25  ? 88  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 87  ? 29.644 -22.838 28.633 1.00 25.42  ? 88  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 87  ? 30.878 -23.173 29.455 1.00 39.00  ? 88  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 87  ? 32.006 -23.081 28.907 1.00 39.21  ? 88  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 87  ? 30.717 -23.541 30.641 1.00 39.88  ? 88  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 88  ? 27.678 -21.404 26.676 1.00 22.40  ? 89  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 88  ? 26.487 -21.338 25.813 1.00 20.86  ? 89  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 88  ? 26.862 -20.954 24.372 1.00 22.06  ? 89  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 88  ? 26.393 -21.577 23.401 1.00 20.24  ? 89  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 88  ? 25.440 -20.360 26.388 1.00 21.61  ? 89  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 88  ? 24.322 -20.088 25.400 1.00 22.23  ? 89  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 88  ? 23.370 -21.063 25.117 1.00 24.34  ? 89  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 88  ? 24.296 -18.904 24.659 1.00 24.68  ? 89  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 88  ? 22.378 -20.842 24.157 1.00 23.53  ? 89  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 88  ? 23.290 -18.682 23.700 1.00 27.27  ? 89  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 88  ? 22.342 -19.651 23.458 1.00 25.52  ? 89  PHE   A CZ  1 
ATOM   759  N  N   . MET   A 1 89  ? 27.669 -19.908 24.220 1.00 19.13  ? 90  MET   A N   1 
ATOM   760  C  CA  . MET   A 1 89  ? 28.063 -19.476 22.868 1.00 18.82  ? 90  MET   A CA  1 
ATOM   761  C  C   . MET   A 1 89  ? 28.639 -20.615 22.048 1.00 22.22  ? 90  MET   A C   1 
ATOM   762  O  O   . MET   A 1 89  ? 28.314 -20.748 20.871 1.00 22.00  ? 90  MET   A O   1 
ATOM   763  C  CB  . MET   A 1 89  ? 29.139 -18.379 22.961 1.00 19.84  ? 90  MET   A CB  1 
ATOM   764  C  CG  . MET   A 1 89  ? 28.637 -17.105 23.581 1.00 22.03  ? 90  MET   A CG  1 
ATOM   765  S  SD  . MET   A 1 89  ? 29.982 -15.878 23.480 1.00 25.65  ? 90  MET   A SD  1 
ATOM   766  C  CE  . MET   A 1 89  ? 29.303 -14.611 24.600 1.00 25.88  ? 90  MET   A CE  1 
ATOM   767  N  N   . TYR   A 1 90  ? 29.506 -21.430 22.675 1.00 19.57  ? 91  TYR   A N   1 
ATOM   768  C  CA  . TYR   A 1 90  ? 30.191 -22.532 21.990 1.00 19.98  ? 91  TYR   A CA  1 
ATOM   769  C  C   . TYR   A 1 90  ? 29.439 -23.863 21.960 1.00 24.03  ? 91  TYR   A C   1 
ATOM   770  O  O   . TYR   A 1 90  ? 29.920 -24.824 21.341 1.00 23.48  ? 91  TYR   A O   1 
ATOM   771  C  CB  . TYR   A 1 90  ? 31.571 -22.758 22.624 1.00 21.15  ? 91  TYR   A CB  1 
ATOM   772  C  CG  . TYR   A 1 90  ? 32.620 -21.779 22.134 1.00 22.11  ? 91  TYR   A CG  1 
ATOM   773  C  CD1 . TYR   A 1 90  ? 32.771 -20.529 22.732 1.00 23.44  ? 91  TYR   A CD1 1 
ATOM   774  C  CD2 . TYR   A 1 90  ? 33.471 -22.111 21.074 1.00 23.48  ? 91  TYR   A CD2 1 
ATOM   775  C  CE1 . TYR   A 1 90  ? 33.747 -19.623 22.285 1.00 23.48  ? 91  TYR   A CE1 1 
ATOM   776  C  CE2 . TYR   A 1 90  ? 34.480 -21.238 20.655 1.00 24.00  ? 91  TYR   A CE2 1 
ATOM   777  C  CZ  . TYR   A 1 90  ? 34.588 -19.984 21.237 1.00 25.76  ? 91  TYR   A CZ  1 
ATOM   778  O  OH  . TYR   A 1 90  ? 35.617 -19.173 20.842 1.00 24.24  ? 91  TYR   A OH  1 
ATOM   779  N  N   . THR   A 1 91  ? 28.288 -23.960 22.652 1.00 20.96  ? 92  THR   A N   1 
ATOM   780  C  CA  . THR   A 1 91  ? 27.596 -25.265 22.709 1.00 22.33  ? 92  THR   A CA  1 
ATOM   781  C  C   . THR   A 1 91  ? 26.075 -25.253 22.483 1.00 24.33  ? 92  THR   A C   1 
ATOM   782  O  O   . THR   A 1 91  ? 25.514 -26.347 22.300 1.00 23.36  ? 92  THR   A O   1 
ATOM   783  C  CB  . THR   A 1 91  ? 27.778 -25.937 24.114 1.00 25.17  ? 92  THR   A CB  1 
ATOM   784  O  OG1 . THR   A 1 91  ? 27.092 -25.177 25.124 1.00 25.15  ? 92  THR   A OG1 1 
ATOM   785  C  CG2 . THR   A 1 91  ? 29.240 -26.156 24.526 1.00 26.30  ? 92  THR   A CG2 1 
ATOM   786  N  N   A SER   A 1 92  ? 25.417 -24.067 22.564 0.67 20.19  ? 93  SER   A N   1 
ATOM   787  N  N   B SER   A 1 92  ? 25.423 -24.070 22.593 0.33 20.49  ? 93  SER   A N   1 
ATOM   788  C  CA  A SER   A 1 92  ? 23.940 -23.875 22.520 0.67 19.97  ? 93  SER   A CA  1 
ATOM   789  C  CA  B SER   A 1 92  ? 23.960 -23.859 22.537 0.33 20.44  ? 93  SER   A CA  1 
ATOM   790  C  C   A SER   A 1 92  ? 23.286 -24.263 23.861 0.67 23.06  ? 93  SER   A C   1 
ATOM   791  C  C   B SER   A 1 92  ? 23.272 -24.370 23.825 0.33 24.47  ? 93  SER   A C   1 
ATOM   792  O  O   A SER   A 1 92  ? 22.093 -24.034 24.035 0.67 23.15  ? 93  SER   A O   1 
ATOM   793  O  O   B SER   A 1 92  ? 22.043 -24.410 23.887 0.33 24.76  ? 93  SER   A O   1 
ATOM   794  C  CB  A SER   A 1 92  ? 23.279 -24.678 21.396 0.67 21.34  ? 93  SER   A CB  1 
ATOM   795  C  CB  B SER   A 1 92  ? 23.338 -24.493 21.289 0.33 22.61  ? 93  SER   A CB  1 
ATOM   796  O  OG  A SER   A 1 92  ? 23.915 -24.503 20.145 0.67 20.32  ? 93  SER   A OG  1 
ATOM   797  O  OG  B SER   A 1 92  ? 23.039 -25.869 21.470 0.33 26.28  ? 93  SER   A OG  1 
ATOM   798  N  N   A ARG   A 1 93  ? 24.071 -24.801 24.825 0.67 21.30  ? 94  ARG   A N   1 
ATOM   799  N  N   B ARG   A 1 93  ? 24.073 -24.736 24.855 0.33 21.96  ? 94  ARG   A N   1 
ATOM   800  C  CA  A ARG   A 1 93  ? 23.539 -25.220 26.129 0.67 21.52  ? 94  ARG   A CA  1 
ATOM   801  C  CA  B ARG   A 1 93  ? 23.593 -25.261 26.139 0.33 22.50  ? 94  ARG   A CA  1 
ATOM   802  C  C   A ARG   A 1 93  ? 23.780 -24.173 27.194 0.67 25.84  ? 94  ARG   A C   1 
ATOM   803  C  C   B ARG   A 1 93  ? 23.805 -24.223 27.239 0.33 26.30  ? 94  ARG   A C   1 
ATOM   804  O  O   A ARG   A 1 93  ? 24.913 -23.722 27.387 0.67 23.73  ? 94  ARG   A O   1 
ATOM   805  O  O   B ARG   A 1 93  ? 24.937 -23.785 27.465 0.33 24.85  ? 94  ARG   A O   1 
ATOM   806  C  CB  A ARG   A 1 93  ? 24.134 -26.566 26.577 0.67 24.83  ? 94  ARG   A CB  1 
ATOM   807  C  CB  B ARG   A 1 93  ? 24.303 -26.590 26.495 0.33 24.67  ? 94  ARG   A CB  1 
ATOM   808  C  CG  A ARG   A 1 93  ? 23.819 -27.727 25.631 0.67 29.52  ? 94  ARG   A CG  1 
ATOM   809  C  CG  B ARG   A 1 93  ? 24.191 -27.683 25.422 0.33 32.96  ? 94  ARG   A CG  1 
ATOM   810  C  CD  A ARG   A 1 93  ? 24.830 -28.857 25.816 0.67 36.83  ? 94  ARG   A CD  1 
ATOM   811  C  CD  B ARG   A 1 93  ? 23.061 -28.655 25.696 0.33 36.68  ? 94  ARG   A CD  1 
ATOM   812  N  NE  A ARG   A 1 93  ? 24.791 -29.396 27.178 0.67 48.05  ? 94  ARG   A NE  1 
ATOM   813  N  NE  B ARG   A 1 93  ? 22.926 -29.671 24.648 0.33 39.55  ? 94  ARG   A NE  1 
ATOM   814  C  CZ  A ARG   A 1 93  ? 24.003 -30.394 27.565 0.67 61.01  ? 94  ARG   A CZ  1 
ATOM   815  C  CZ  B ARG   A 1 93  ? 23.209 -30.961 24.808 0.33 51.21  ? 94  ARG   A CZ  1 
ATOM   816  N  NH1 A ARG   A 1 93  ? 23.199 -30.990 26.693 0.67 49.38  ? 94  ARG   A NH1 1 
ATOM   817  N  NH1 B ARG   A 1 93  ? 23.037 -31.814 23.807 0.33 40.35  ? 94  ARG   A NH1 1 
ATOM   818  N  NH2 A ARG   A 1 93  ? 24.021 -30.811 28.823 0.67 46.40  ? 94  ARG   A NH2 1 
ATOM   819  N  NH2 B ARG   A 1 93  ? 23.644 -31.412 25.977 0.33 34.29  ? 94  ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 94  ? 22.716 -23.834 27.918 1.00 23.31  ? 95  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 94  ? 22.761 -22.827 28.979 1.00 22.72  ? 95  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 94  ? 22.546 -23.476 30.333 1.00 28.58  ? 95  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 94  ? 21.484 -24.063 30.575 1.00 28.07  ? 95  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 94  ? 21.687 -21.771 28.699 1.00 23.16  ? 95  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 94  ? 21.727 -20.548 29.640 1.00 26.49  ? 95  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 94  ? 23.009 -19.728 29.390 1.00 24.88  ? 95  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 94  ? 20.485 -19.683 29.447 1.00 29.37  ? 95  LEU   A CD2 1 
ATOM   828  N  N   . ASN   A 1 95  ? 23.543 -23.355 31.231 1.00 27.72  ? 96  ASN   A N   1 
ATOM   829  C  CA  . ASN   A 1 95  ? 23.446 -23.940 32.579 1.00 28.65  ? 96  ASN   A CA  1 
ATOM   830  C  C   . ASN   A 1 95  ? 22.748 -22.935 33.513 1.00 33.84  ? 96  ASN   A C   1 
ATOM   831  O  O   . ASN   A 1 95  ? 23.398 -22.238 34.290 1.00 33.49  ? 96  ASN   A O   1 
ATOM   832  C  CB  . ASN   A 1 95  ? 24.843 -24.335 33.097 1.00 32.32  ? 96  ASN   A CB  1 
ATOM   833  C  CG  . ASN   A 1 95  ? 24.823 -24.964 34.480 1.00 50.98  ? 96  ASN   A CG  1 
ATOM   834  O  OD1 . ASN   A 1 95  ? 23.830 -25.553 34.907 1.00 39.63  ? 96  ASN   A OD1 1 
ATOM   835  N  ND2 . ASN   A 1 95  ? 25.916 -24.837 35.215 1.00 45.26  ? 96  ASN   A ND2 1 
ATOM   836  N  N   . LEU   A 1 96  ? 21.435 -22.817 33.361 1.00 31.12  ? 97  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 96  ? 20.613 -21.874 34.110 1.00 32.57  ? 97  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 96  ? 20.091 -22.536 35.378 1.00 36.51  ? 97  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 96  ? 19.464 -23.602 35.317 1.00 36.29  ? 97  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 96  ? 19.488 -21.401 33.177 1.00 33.27  ? 97  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 96  ? 18.725 -20.146 33.522 1.00 39.61  ? 97  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 96  ? 19.684 -18.928 33.635 1.00 39.94  ? 97  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 96  ? 17.642 -19.900 32.470 1.00 39.63  ? 97  LEU   A CD2 1 
ATOM   844  N  N   . ARG   A 1 97  ? 20.439 -21.946 36.544 1.00 33.47  ? 98  ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 97  ? 20.076 -22.461 37.874 1.00 35.45  ? 98  ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 97  ? 19.552 -21.329 38.748 1.00 36.60  ? 98  ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 97  ? 19.876 -20.159 38.516 1.00 34.34  ? 98  ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 97  ? 21.290 -23.125 38.562 1.00 37.97  ? 98  ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 97  ? 21.909 -24.290 37.780 1.00 45.89  ? 98  ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 97  ? 23.157 -24.861 38.442 1.00 64.24  ? 98  ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 97  ? 22.879 -25.483 39.743 1.00 83.87  ? 98  ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 97  ? 22.483 -26.742 39.915 1.00 104.30 ? 98  ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 97  ? 22.250 -27.209 41.136 1.00 92.08  ? 98  ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 97  ? 22.304 -27.540 38.868 1.00 94.31  ? 98  ARG   A NH2 1 
ATOM   855  N  N   . GLU   A 1 98  ? 18.731 -21.664 39.748 1.00 35.53  ? 99  GLU   A N   1 
ATOM   856  C  CA  . GLU   A 1 98  ? 18.187 -20.655 40.661 1.00 35.39  ? 99  GLU   A CA  1 
ATOM   857  C  C   . GLU   A 1 98  ? 19.299 -19.767 41.253 1.00 40.72  ? 99  GLU   A C   1 
ATOM   858  O  O   . GLU   A 1 98  ? 19.120 -18.552 41.345 1.00 40.41  ? 99  GLU   A O   1 
ATOM   859  C  CB  . GLU   A 1 98  ? 17.376 -21.336 41.787 1.00 38.68  ? 99  GLU   A CB  1 
ATOM   860  C  CG  . GLU   A 1 98  ? 16.746 -20.361 42.765 1.00 49.35  ? 99  GLU   A CG  1 
ATOM   861  C  CD  . GLU   A 1 98  ? 16.032 -21.004 43.941 1.00 82.17  ? 99  GLU   A CD  1 
ATOM   862  O  OE1 . GLU   A 1 98  ? 16.617 -21.904 44.591 1.00 79.12  ? 99  GLU   A OE1 1 
ATOM   863  O  OE2 . GLU   A 1 98  ? 14.883 -20.594 44.221 1.00 82.77  ? 99  GLU   A OE2 1 
ATOM   864  N  N   . GLY   A 1 99  ? 20.436 -20.376 41.593 1.00 38.79  ? 100 GLY   A N   1 
ATOM   865  C  CA  . GLY   A 1 99  ? 21.572 -19.673 42.191 1.00 39.24  ? 100 GLY   A CA  1 
ATOM   866  C  C   . GLY   A 1 99  ? 22.364 -18.774 41.257 1.00 39.27  ? 100 GLY   A C   1 
ATOM   867  O  O   . GLY   A 1 99  ? 23.097 -17.895 41.717 1.00 39.40  ? 100 GLY   A O   1 
ATOM   868  N  N   . ASN   A 1 100 ? 22.215 -18.957 39.940 1.00 34.56  ? 101 ASN   A N   1 
ATOM   869  C  CA  . ASN   A 1 100 ? 22.993 -18.162 38.993 1.00 32.22  ? 101 ASN   A CA  1 
ATOM   870  C  C   . ASN   A 1 100 ? 22.150 -17.310 38.029 1.00 36.23  ? 101 ASN   A C   1 
ATOM   871  O  O   . ASN   A 1 100 ? 22.728 -16.498 37.295 1.00 34.73  ? 101 ASN   A O   1 
ATOM   872  C  CB  . ASN   A 1 100 ? 23.967 -19.075 38.228 1.00 31.05  ? 101 ASN   A CB  1 
ATOM   873  C  CG  . ASN   A 1 100 ? 23.324 -20.001 37.205 1.00 37.32  ? 101 ASN   A CG  1 
ATOM   874  O  OD1 . ASN   A 1 100 ? 22.273 -19.701 36.630 1.00 31.32  ? 101 ASN   A OD1 1 
ATOM   875  N  ND2 . ASN   A 1 100 ? 23.965 -21.132 36.915 1.00 33.10  ? 101 ASN   A ND2 1 
ATOM   876  N  N   . ILE   A 1 101 ? 20.804 -17.511 37.999 1.00 33.28  ? 102 ILE   A N   1 
ATOM   877  C  CA  . ILE   A 1 101 ? 19.930 -16.838 37.018 1.00 32.93  ? 102 ILE   A CA  1 
ATOM   878  C  C   . ILE   A 1 101 ? 20.058 -15.305 37.010 1.00 33.81  ? 102 ILE   A C   1 
ATOM   879  O  O   . ILE   A 1 101 ? 20.079 -14.706 35.925 1.00 31.23  ? 102 ILE   A O   1 
ATOM   880  C  CB  . ILE   A 1 101 ? 18.447 -17.274 37.095 1.00 36.88  ? 102 ILE   A CB  1 
ATOM   881  C  CG1 . ILE   A 1 101 ? 17.642 -16.710 35.882 1.00 36.94  ? 102 ILE   A CG1 1 
ATOM   882  C  CG2 . ILE   A 1 101 ? 17.797 -16.962 38.458 1.00 36.55  ? 102 ILE   A CG2 1 
ATOM   883  C  CD1 . ILE   A 1 101 ? 16.476 -17.535 35.440 1.00 40.38  ? 102 ILE   A CD1 1 
ATOM   884  N  N   . MET   A 1 102 ? 20.157 -14.673 38.181 1.00 32.66  ? 103 MET   A N   1 
ATOM   885  C  CA  . MET   A 1 102 ? 20.287 -13.218 38.218 1.00 33.36  ? 103 MET   A CA  1 
ATOM   886  C  C   . MET   A 1 102 ? 21.589 -12.730 37.571 1.00 35.00  ? 103 MET   A C   1 
ATOM   887  O  O   . MET   A 1 102 ? 21.551 -11.786 36.778 1.00 34.00  ? 103 MET   A O   1 
ATOM   888  C  CB  . MET   A 1 102 ? 20.119 -12.667 39.646 1.00 37.62  ? 103 MET   A CB  1 
ATOM   889  C  CG  . MET   A 1 102 ? 18.739 -12.956 40.244 1.00 44.82  ? 103 MET   A CG  1 
ATOM   890  S  SD  . MET   A 1 102 ? 17.335 -12.503 39.181 1.00 51.26  ? 103 MET   A SD  1 
ATOM   891  C  CE  . MET   A 1 102 ? 17.300 -10.727 39.414 1.00 49.63  ? 103 MET   A CE  1 
ATOM   892  N  N   . ALA   A 1 103 ? 22.729 -13.398 37.876 1.00 32.86  ? 104 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 103 ? 24.043 -13.054 37.301 1.00 32.37  ? 104 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 103 ? 24.054 -13.346 35.804 1.00 32.94  ? 104 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 103 ? 24.569 -12.545 35.022 1.00 30.51  ? 104 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 103 ? 25.153 -13.841 37.987 1.00 33.71  ? 104 ALA   A CB  1 
ATOM   897  N  N   . VAL   A 1 104 ? 23.480 -14.488 35.397 1.00 28.15  ? 105 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 104 ? 23.413 -14.849 33.971 1.00 25.64  ? 105 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 104 ? 22.607 -13.811 33.192 1.00 28.97  ? 105 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 104 ? 23.094 -13.343 32.153 1.00 26.90  ? 105 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 104 ? 22.914 -16.305 33.760 1.00 28.43  ? 105 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 104 ? 22.592 -16.597 32.282 1.00 26.39  ? 105 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 104 ? 23.952 -17.290 34.276 1.00 28.78  ? 105 VAL   A CG2 1 
ATOM   904  N  N   A MET   A 1 105 ? 21.404 -13.440 33.683 0.20 27.50  ? 106 MET   A N   1 
ATOM   905  N  N   B MET   A 1 105 ? 21.398 -13.447 33.678 0.80 28.22  ? 106 MET   A N   1 
ATOM   906  C  CA  A MET   A 1 105 ? 20.552 -12.444 33.024 0.20 28.32  ? 106 MET   A CA  1 
ATOM   907  C  CA  B MET   A 1 105 ? 20.579 -12.444 32.980 0.80 29.93  ? 106 MET   A CA  1 
ATOM   908  C  C   A MET   A 1 105 ? 21.256 -11.093 32.884 0.20 32.04  ? 106 MET   A C   1 
ATOM   909  C  C   B MET   A 1 105 ? 21.280 -11.084 32.870 0.80 32.37  ? 106 MET   A C   1 
ATOM   910  O  O   A MET   A 1 105 ? 21.223 -10.505 31.802 0.20 31.21  ? 106 MET   A O   1 
ATOM   911  O  O   B MET   A 1 105 ? 21.244 -10.462 31.805 0.80 31.26  ? 106 MET   A O   1 
ATOM   912  C  CB  A MET   A 1 105 ? 19.215 -12.274 33.754 0.20 31.97  ? 106 MET   A CB  1 
ATOM   913  C  CB  B MET   A 1 105 ? 19.207 -12.271 33.635 0.80 33.45  ? 106 MET   A CB  1 
ATOM   914  C  CG  A MET   A 1 105 ? 18.236 -11.415 32.989 0.20 36.12  ? 106 MET   A CG  1 
ATOM   915  C  CG  B MET   A 1 105 ? 18.281 -11.372 32.824 0.80 37.29  ? 106 MET   A CG  1 
ATOM   916  S  SD  A MET   A 1 105 ? 16.734 -11.086 33.914 0.20 41.93  ? 106 MET   A SD  1 
ATOM   917  S  SD  B MET   A 1 105 ? 16.595 -11.363 33.460 0.80 42.82  ? 106 MET   A SD  1 
ATOM   918  C  CE  A MET   A 1 105 ? 16.178 -9.654  33.075 0.20 39.33  ? 106 MET   A CE  1 
ATOM   919  C  CE  B MET   A 1 105 ? 16.791 -10.353 35.011 0.80 41.24  ? 106 MET   A CE  1 
ATOM   920  N  N   . ALA   A 1 106 ? 21.888 -10.610 33.973 1.00 29.17  ? 107 ALA   A N   1 
ATOM   921  C  CA  . ALA   A 1 106 ? 22.619 -9.325  33.987 1.00 30.12  ? 107 ALA   A CA  1 
ATOM   922  C  C   . ALA   A 1 106 ? 23.783 -9.361  32.981 1.00 30.54  ? 107 ALA   A C   1 
ATOM   923  O  O   . ALA   A 1 106 ? 23.950 -8.416  32.193 1.00 28.70  ? 107 ALA   A O   1 
ATOM   924  C  CB  . ALA   A 1 106 ? 23.127 -9.032  35.389 1.00 31.53  ? 107 ALA   A CB  1 
ATOM   925  N  N   . THR   A 1 107 ? 24.525 -10.489 32.939 1.00 26.92  ? 108 THR   A N   1 
ATOM   926  C  CA  . THR   A 1 107 ? 25.626 -10.651 31.982 1.00 26.42  ? 108 THR   A CA  1 
ATOM   927  C  C   . THR   A 1 107 ? 25.084 -10.698 30.532 1.00 28.49  ? 108 THR   A C   1 
ATOM   928  O  O   . THR   A 1 107 ? 25.666 -10.053 29.654 1.00 25.25  ? 108 THR   A O   1 
ATOM   929  C  CB  . THR   A 1 107 ? 26.547 -11.838 32.354 1.00 29.86  ? 108 THR   A CB  1 
ATOM   930  O  OG1 . THR   A 1 107 ? 26.853 -11.807 33.755 1.00 29.68  ? 108 THR   A OG1 1 
ATOM   931  C  CG2 . THR   A 1 107 ? 27.857 -11.842 31.547 1.00 29.17  ? 108 THR   A CG2 1 
ATOM   932  N  N   . ALA   A 1 108 ? 23.970 -11.448 30.281 1.00 25.78  ? 109 ALA   A N   1 
ATOM   933  C  CA  . ALA   A 1 108 ? 23.384 -11.537 28.936 1.00 24.11  ? 109 ALA   A CA  1 
ATOM   934  C  C   . ALA   A 1 108 ? 22.864 -10.164 28.466 1.00 27.20  ? 109 ALA   A C   1 
ATOM   935  O  O   . ALA   A 1 108 ? 23.039 -9.818  27.300 1.00 26.26  ? 109 ALA   A O   1 
ATOM   936  C  CB  . ALA   A 1 108 ? 22.284 -12.603 28.888 1.00 24.88  ? 109 ALA   A CB  1 
ATOM   937  N  N   . MET   A 1 109 ? 22.309 -9.339  29.385 1.00 25.02  ? 110 MET   A N   1 
ATOM   938  C  CA  . MET   A 1 109 ? 21.864 -7.988  28.997 1.00 25.66  ? 110 MET   A CA  1 
ATOM   939  C  C   . MET   A 1 109 ? 23.062 -7.121  28.560 1.00 28.87  ? 110 MET   A C   1 
ATOM   940  O  O   . MET   A 1 109 ? 23.021 -6.469  27.517 1.00 28.93  ? 110 MET   A O   1 
ATOM   941  C  CB  . MET   A 1 109 ? 21.097 -7.334  30.152 1.00 28.87  ? 110 MET   A CB  1 
ATOM   942  C  CG  . MET   A 1 109 ? 19.716 -7.943  30.357 1.00 34.04  ? 110 MET   A CG  1 
ATOM   943  S  SD  . MET   A 1 109 ? 18.995 -7.384  31.923 1.00 42.35  ? 110 MET   A SD  1 
ATOM   944  C  CE  . MET   A 1 109 ? 18.706 -5.646  31.522 1.00 40.43  ? 110 MET   A CE  1 
ATOM   945  N  N   . TYR   A 1 110 ? 24.141 -7.173  29.331 1.00 26.56  ? 111 TYR   A N   1 
ATOM   946  C  CA  . TYR   A 1 110 ? 25.378 -6.435  29.051 1.00 25.68  ? 111 TYR   A CA  1 
ATOM   947  C  C   . TYR   A 1 110 ? 25.994 -6.910  27.723 1.00 27.79  ? 111 TYR   A C   1 
ATOM   948  O  O   . TYR   A 1 110 ? 26.394 -6.084  26.894 1.00 26.81  ? 111 TYR   A O   1 
ATOM   949  C  CB  . TYR   A 1 110 ? 26.357 -6.690  30.194 1.00 26.14  ? 111 TYR   A CB  1 
ATOM   950  C  CG  . TYR   A 1 110 ? 27.763 -6.177  29.961 1.00 26.42  ? 111 TYR   A CG  1 
ATOM   951  C  CD1 . TYR   A 1 110 ? 28.059 -4.817  30.064 1.00 29.94  ? 111 TYR   A CD1 1 
ATOM   952  C  CD2 . TYR   A 1 110 ? 28.815 -7.062  29.718 1.00 25.89  ? 111 TYR   A CD2 1 
ATOM   953  C  CE1 . TYR   A 1 110 ? 29.362 -4.344  29.873 1.00 27.26  ? 111 TYR   A CE1 1 
ATOM   954  C  CE2 . TYR   A 1 110 ? 30.123 -6.606  29.568 1.00 25.82  ? 111 TYR   A CE2 1 
ATOM   955  C  CZ  . TYR   A 1 110 ? 30.387 -5.246  29.637 1.00 29.14  ? 111 TYR   A CZ  1 
ATOM   956  O  OH  . TYR   A 1 110 ? 31.682 -4.839  29.540 1.00 27.68  ? 111 TYR   A OH  1 
ATOM   957  N  N   . LEU   A 1 111 ? 26.033 -8.237  27.512 1.00 25.14  ? 112 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 111 ? 26.614 -8.824  26.295 1.00 23.16  ? 112 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 111 ? 25.691 -8.698  25.086 1.00 26.50  ? 112 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 111 ? 26.121 -8.948  23.957 1.00 25.36  ? 112 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 111 ? 27.024 -10.287 26.532 1.00 22.45  ? 112 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 111 ? 28.165 -10.550 27.544 1.00 24.73  ? 112 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 111 ? 28.454 -12.080 27.630 1.00 24.40  ? 112 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 111 ? 29.470 -9.808  27.141 1.00 26.86  ? 112 LEU   A CD2 1 
ATOM   965  N  N   . GLN   A 1 112 ? 24.420 -8.322  25.315 1.00 24.62  ? 113 GLN   A N   1 
ATOM   966  C  CA  . GLN   A 1 112 ? 23.423 -8.186  24.241 1.00 24.47  ? 113 GLN   A CA  1 
ATOM   967  C  C   . GLN   A 1 112 ? 23.176 -9.540  23.562 1.00 27.96  ? 113 GLN   A C   1 
ATOM   968  O  O   . GLN   A 1 112 ? 23.432 -9.730  22.372 1.00 27.12  ? 113 GLN   A O   1 
ATOM   969  C  CB  . GLN   A 1 112 ? 23.800 -7.080  23.238 1.00 25.10  ? 113 GLN   A CB  1 
ATOM   970  C  CG  . GLN   A 1 112 ? 23.923 -5.690  23.882 1.00 27.75  ? 113 GLN   A CG  1 
ATOM   971  C  CD  . GLN   A 1 112 ? 24.640 -4.731  22.966 1.00 40.14  ? 113 GLN   A CD  1 
ATOM   972  O  OE1 . GLN   A 1 112 ? 24.549 -4.824  21.751 1.00 32.79  ? 113 GLN   A OE1 1 
ATOM   973  N  NE2 . GLN   A 1 112 ? 25.377 -3.793  23.528 1.00 36.97  ? 113 GLN   A NE2 1 
ATOM   974  N  N   . MET   A 1 113 ? 22.716 -10.494 24.370 1.00 24.90  ? 114 MET   A N   1 
ATOM   975  C  CA  . MET   A 1 113 ? 22.387 -11.866 23.942 1.00 24.29  ? 114 MET   A CA  1 
ATOM   976  C  C   . MET   A 1 113 ? 20.890 -12.030 24.205 1.00 30.61  ? 114 MET   A C   1 
ATOM   977  O  O   . MET   A 1 113 ? 20.466 -12.522 25.260 1.00 28.50  ? 114 MET   A O   1 
ATOM   978  C  CB  . MET   A 1 113 ? 23.256 -12.848 24.740 1.00 25.14  ? 114 MET   A CB  1 
ATOM   979  C  CG  . MET   A 1 113 ? 24.744 -12.716 24.404 1.00 27.02  ? 114 MET   A CG  1 
ATOM   980  S  SD  . MET   A 1 113 ? 25.764 -13.755 25.446 1.00 29.83  ? 114 MET   A SD  1 
ATOM   981  C  CE  . MET   A 1 113 ? 25.433 -15.416 24.653 1.00 27.13  ? 114 MET   A CE  1 
ATOM   982  N  N   . GLU   A 1 114 ? 20.086 -11.489 23.274 1.00 30.39  ? 115 GLU   A N   1 
ATOM   983  C  CA  . GLU   A 1 114 ? 18.621 -11.368 23.385 1.00 32.25  ? 115 GLU   A CA  1 
ATOM   984  C  C   . GLU   A 1 114 ? 17.871 -12.650 23.737 1.00 32.80  ? 115 GLU   A C   1 
ATOM   985  O  O   . GLU   A 1 114 ? 16.971 -12.596 24.570 1.00 32.16  ? 115 GLU   A O   1 
ATOM   986  C  CB  . GLU   A 1 114 ? 18.012 -10.745 22.119 1.00 35.23  ? 115 GLU   A CB  1 
ATOM   987  C  CG  . GLU   A 1 114 ? 18.527 -9.342  21.842 1.00 49.38  ? 115 GLU   A CG  1 
ATOM   988  N  N   . HIS   A 1 115 ? 18.223 -13.790 23.115 1.00 29.05  ? 116 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 115 ? 17.501 -15.035 23.405 1.00 30.95  ? 116 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 115 ? 17.731 -15.516 24.832 1.00 31.79  ? 116 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 115 ? 16.782 -15.991 25.474 1.00 32.49  ? 116 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 115 ? 17.819 -16.117 22.377 1.00 32.96  ? 116 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 115 ? 17.383 -15.758 20.990 1.00 38.35  ? 116 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 115 ? 16.053 -15.511 20.695 1.00 42.31  ? 116 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 115 ? 18.108 -15.665 19.852 1.00 40.31  ? 116 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 115 ? 16.017 -15.235 19.401 1.00 42.11  ? 116 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 115 ? 17.226 -15.326 18.850 1.00 41.36  ? 116 HIS   A NE2 1 
ATOM   998  N  N   . VAL   A 1 116 ? 18.972 -15.350 25.345 1.00 25.88  ? 117 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 116 ? 19.305 -15.715 26.728 1.00 25.52  ? 117 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 116 ? 18.517 -14.807 27.685 1.00 31.58  ? 117 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 116 ? 17.897 -15.304 28.630 1.00 30.30  ? 117 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 116 ? 20.826 -15.699 27.033 1.00 28.41  ? 117 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 116 ? 21.077 -15.958 28.523 1.00 28.95  ? 117 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 116 ? 21.566 -16.723 26.178 1.00 27.24  ? 117 VAL   A CG2 1 
ATOM   1005 N  N   . VAL   A 1 117 ? 18.514 -13.483 27.421 1.00 28.30  ? 118 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 117 ? 17.760 -12.521 28.252 1.00 28.92  ? 118 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 117 ? 16.271 -12.942 28.333 1.00 34.78  ? 118 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 117 ? 15.727 -13.015 29.431 1.00 33.85  ? 118 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 117 ? 17.944 -11.046 27.784 1.00 31.25  ? 118 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 117 ? 17.093 -10.078 28.632 1.00 32.10  ? 118 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 117 ? 19.413 -10.629 27.834 1.00 30.09  ? 118 VAL   A CG2 1 
ATOM   1012 N  N   A ASP   A 1 118 ? 15.667 -13.286 27.182 0.61 33.24  ? 119 ASP   A N   1 
ATOM   1013 N  N   B ASP   A 1 118 ? 15.638 -13.201 27.170 0.39 33.10  ? 119 ASP   A N   1 
ATOM   1014 C  CA  A ASP   A 1 118 ? 14.279 -13.739 27.063 0.61 34.91  ? 119 ASP   A CA  1 
ATOM   1015 C  CA  B ASP   A 1 118 ? 14.233 -13.606 27.035 0.39 34.77  ? 119 ASP   A CA  1 
ATOM   1016 C  C   A ASP   A 1 118 ? 13.974 -14.971 27.932 0.61 37.42  ? 119 ASP   A C   1 
ATOM   1017 C  C   B ASP   A 1 118 ? 13.870 -14.818 27.896 0.39 38.44  ? 119 ASP   A C   1 
ATOM   1018 O  O   A ASP   A 1 118 ? 12.988 -14.939 28.669 0.61 38.12  ? 119 ASP   A O   1 
ATOM   1019 O  O   B ASP   A 1 118 ? 12.849 -14.786 28.582 0.39 39.52  ? 119 ASP   A O   1 
ATOM   1020 C  CB  A ASP   A 1 118 ? 13.927 -14.007 25.587 0.61 37.31  ? 119 ASP   A CB  1 
ATOM   1021 C  CB  B ASP   A 1 118 ? 13.899 -13.894 25.556 0.39 36.98  ? 119 ASP   A CB  1 
ATOM   1022 C  CG  A ASP   A 1 118 ? 12.479 -14.408 25.361 0.61 50.77  ? 119 ASP   A CG  1 
ATOM   1023 C  CG  B ASP   A 1 118 ? 13.664 -12.676 24.681 0.39 49.34  ? 119 ASP   A CG  1 
ATOM   1024 O  OD1 A ASP   A 1 118 ? 11.581 -13.602 25.692 0.61 54.48  ? 119 ASP   A OD1 1 
ATOM   1025 O  OD1 B ASP   A 1 118 ? 13.233 -11.632 25.216 0.39 52.65  ? 119 ASP   A OD1 1 
ATOM   1026 O  OD2 A ASP   A 1 118 ? 12.246 -15.523 24.851 0.61 55.57  ? 119 ASP   A OD2 1 
ATOM   1027 O  OD2 B ASP   A 1 118 ? 13.884 -12.776 23.454 0.39 55.59  ? 119 ASP   A OD2 1 
ATOM   1028 N  N   A THR   A 1 119 ? 14.805 -16.044 27.864 0.61 32.32  ? 120 THR   A N   1 
ATOM   1029 N  N   B THR   A 1 119 ? 14.706 -15.874 27.869 0.39 33.56  ? 120 THR   A N   1 
ATOM   1030 C  CA  A THR   A 1 119 ? 14.531 -17.245 28.679 0.61 32.85  ? 120 THR   A CA  1 
ATOM   1031 C  CA  B THR   A 1 119 ? 14.457 -17.106 28.627 0.39 33.96  ? 120 THR   A CA  1 
ATOM   1032 C  C   A THR   A 1 119 ? 14.717 -16.966 30.171 0.61 36.24  ? 120 THR   A C   1 
ATOM   1033 C  C   B THR   A 1 119 ? 14.651 -16.881 30.132 0.39 37.05  ? 120 THR   A C   1 
ATOM   1034 O  O   A THR   A 1 119 ? 13.993 -17.545 30.983 0.61 36.37  ? 120 THR   A O   1 
ATOM   1035 O  O   B THR   A 1 119 ? 13.863 -17.408 30.919 0.39 37.42  ? 120 THR   A O   1 
ATOM   1036 C  CB  A THR   A 1 119 ? 15.284 -18.507 28.209 0.61 33.79  ? 120 THR   A CB  1 
ATOM   1037 C  CB  B THR   A 1 119 ? 15.261 -18.280 28.059 0.39 39.47  ? 120 THR   A CB  1 
ATOM   1038 O  OG1 A THR   A 1 119 ? 14.684 -19.637 28.849 0.61 34.71  ? 120 THR   A OG1 1 
ATOM   1039 O  OG1 B THR   A 1 119 ? 15.217 -18.218 26.633 0.39 38.77  ? 120 THR   A OG1 1 
ATOM   1040 C  CG2 A THR   A 1 119 ? 16.777 -18.485 28.532 0.61 28.80  ? 120 THR   A CG2 1 
ATOM   1041 C  CG2 B THR   A 1 119 ? 14.708 -19.622 28.501 0.39 39.38  ? 120 THR   A CG2 1 
ATOM   1042 N  N   . CYS   A 1 120 ? 15.673 -16.081 30.526 1.00 32.87  ? 121 CYS   A N   1 
ATOM   1043 C  CA  . CYS   A 1 120 ? 15.927 -15.711 31.934 1.00 33.41  ? 121 CYS   A CA  1 
ATOM   1044 C  C   . CYS   A 1 120 ? 14.707 -15.008 32.488 1.00 38.57  ? 121 CYS   A C   1 
ATOM   1045 O  O   . CYS   A 1 120 ? 14.252 -15.369 33.583 1.00 37.38  ? 121 CYS   A O   1 
ATOM   1046 C  CB  . CYS   A 1 120 ? 17.166 -14.834 32.061 1.00 33.08  ? 121 CYS   A CB  1 
ATOM   1047 S  SG  . CYS   A 1 120 ? 18.719 -15.729 31.860 1.00 35.43  ? 121 CYS   A SG  1 
ATOM   1048 N  N   A ARG   A 1 121 ? 14.152 -14.039 31.719 0.48 36.30  ? 122 ARG   A N   1 
ATOM   1049 N  N   B ARG   A 1 121 ? 14.158 -14.025 31.736 0.52 36.58  ? 122 ARG   A N   1 
ATOM   1050 C  CA  A ARG   A 1 121 ? 12.951 -13.272 32.077 0.48 38.20  ? 122 ARG   A CA  1 
ATOM   1051 C  CA  B ARG   A 1 121 ? 12.960 -13.279 32.138 0.52 38.59  ? 122 ARG   A CA  1 
ATOM   1052 C  C   A ARG   A 1 121 ? 11.760 -14.202 32.332 0.48 42.47  ? 122 ARG   A C   1 
ATOM   1053 C  C   B ARG   A 1 121 ? 11.752 -14.207 32.345 0.52 42.58  ? 122 ARG   A C   1 
ATOM   1054 O  O   A ARG   A 1 121 ? 11.014 -14.004 33.295 0.48 42.88  ? 122 ARG   A O   1 
ATOM   1055 O  O   B ARG   A 1 121 ? 10.992 -14.016 33.297 0.52 42.90  ? 122 ARG   A O   1 
ATOM   1056 C  CB  A ARG   A 1 121 ? 12.588 -12.274 30.962 0.48 39.60  ? 122 ARG   A CB  1 
ATOM   1057 C  CB  B ARG   A 1 121 ? 12.632 -12.177 31.124 0.52 40.63  ? 122 ARG   A CB  1 
ATOM   1058 C  CG  A ARG   A 1 121 ? 13.535 -11.092 30.851 0.48 52.46  ? 122 ARG   A CG  1 
ATOM   1059 C  CG  B ARG   A 1 121 ? 13.407 -10.885 31.357 0.52 55.30  ? 122 ARG   A CG  1 
ATOM   1060 C  CD  A ARG   A 1 121 ? 12.933 -9.952  30.050 0.48 64.73  ? 122 ARG   A CD  1 
ATOM   1061 C  CD  B ARG   A 1 121 ? 12.711 -9.690  30.723 0.52 67.08  ? 122 ARG   A CD  1 
ATOM   1062 N  NE  A ARG   A 1 121 ? 13.942 -8.954  29.690 0.48 68.72  ? 122 ARG   A NE  1 
ATOM   1063 N  NE  B ARG   A 1 121 ? 12.846 -9.681  29.264 0.52 72.23  ? 122 ARG   A NE  1 
ATOM   1064 C  CZ  A ARG   A 1 121 ? 14.299 -7.925  30.454 0.48 78.65  ? 122 ARG   A CZ  1 
ATOM   1065 C  CZ  B ARG   A 1 121 ? 13.626 -8.847  28.583 0.52 82.14  ? 122 ARG   A CZ  1 
ATOM   1066 N  NH1 A ARG   A 1 121 ? 13.724 -7.735  31.635 0.48 69.03  ? 122 ARG   A NH1 1 
ATOM   1067 N  NH1 B ARG   A 1 121 ? 14.347 -7.931  29.220 0.52 66.70  ? 122 ARG   A NH1 1 
ATOM   1068 N  NH2 A ARG   A 1 121 ? 15.233 -7.079  30.042 0.48 59.27  ? 122 ARG   A NH2 1 
ATOM   1069 N  NH2 B ARG   A 1 121 ? 13.687 -8.917  27.260 0.52 66.69  ? 122 ARG   A NH2 1 
ATOM   1070 N  N   . LYS   A 1 122 ? 11.603 -15.223 31.472 1.00 38.78  ? 123 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 122 ? 10.517 -16.214 31.549 1.00 40.39  ? 123 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 122 ? 10.667 -17.117 32.767 1.00 43.74  ? 123 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 122 ? 9.687  -17.318 33.486 1.00 43.94  ? 123 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 122 ? 10.417 -17.025 30.246 1.00 42.31  ? 123 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 122 ? 9.854  -16.185 29.106 1.00 61.31  ? 123 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 122 ? 9.734  -16.934 27.799 1.00 73.46  ? 123 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 122 ? 9.309  -15.988 26.702 1.00 87.49  ? 123 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 122 ? 8.439  -16.655 25.700 1.00 100.26 ? 123 LYS   A NZ  1 
ATOM   1079 N  N   . PHE   A 1 123 ? 11.900 -17.613 33.032 1.00 38.73  ? 124 PHE   A N   1 
ATOM   1080 C  CA  . PHE   A 1 123 ? 12.176 -18.470 34.193 1.00 39.22  ? 124 PHE   A CA  1 
ATOM   1081 C  C   . PHE   A 1 123 ? 11.985 -17.703 35.497 1.00 43.73  ? 124 PHE   A C   1 
ATOM   1082 O  O   . PHE   A 1 123 ? 11.455 -18.270 36.460 1.00 43.24  ? 124 PHE   A O   1 
ATOM   1083 C  CB  . PHE   A 1 123 ? 13.581 -19.083 34.103 1.00 39.36  ? 124 PHE   A CB  1 
ATOM   1084 C  CG  . PHE   A 1 123 ? 13.698 -20.362 33.291 1.00 40.27  ? 124 PHE   A CG  1 
ATOM   1085 C  CD1 . PHE   A 1 123 ? 13.163 -20.449 32.008 1.00 42.85  ? 124 PHE   A CD1 1 
ATOM   1086 C  CD2 . PHE   A 1 123 ? 14.418 -21.450 33.777 1.00 42.82  ? 124 PHE   A CD2 1 
ATOM   1087 C  CE1 . PHE   A 1 123 ? 13.279 -21.631 31.258 1.00 43.71  ? 124 PHE   A CE1 1 
ATOM   1088 C  CE2 . PHE   A 1 123 ? 14.546 -22.626 33.020 1.00 44.14  ? 124 PHE   A CE2 1 
ATOM   1089 C  CZ  . PHE   A 1 123 ? 13.978 -22.707 31.767 1.00 41.65  ? 124 PHE   A CZ  1 
ATOM   1090 N  N   . ILE   A 1 124 ? 12.364 -16.404 35.518 1.00 40.06  ? 125 ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 124 ? 12.168 -15.546 36.701 1.00 41.41  ? 125 ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 124 ? 10.666 -15.298 36.955 1.00 48.73  ? 125 ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 124 ? 10.211 -15.445 38.100 1.00 49.66  ? 125 ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 124 ? 13.020 -14.247 36.608 1.00 43.54  ? 125 ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 124 ? 14.514 -14.592 36.775 1.00 42.49  ? 125 ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 124 ? 12.585 -13.189 37.662 1.00 45.90  ? 125 ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 124 ? 15.475 -13.583 36.219 1.00 47.34  ? 125 ILE   A CD1 1 
ATOM   1098 N  N   . LYS   A 1 125 ? 9.892  -14.980 35.885 1.00 46.66  ? 126 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 125 ? 8.447  -14.729 35.986 1.00 49.47  ? 126 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 125 ? 7.687  -15.955 36.517 1.00 54.09  ? 126 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 125 ? 6.717  -15.794 37.251 1.00 54.37  ? 126 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 125 ? 7.862  -14.270 34.643 1.00 52.90  ? 126 LYS   A CB  1 
ATOM   1103 N  N   . ALA   A 1 126 ? 8.151  -17.173 36.170 1.00 49.44  ? 127 ALA   A N   1 
ATOM   1104 C  CA  . ALA   A 1 126 ? 7.533  -18.418 36.637 1.00 50.83  ? 127 ALA   A CA  1 
ATOM   1105 C  C   . ALA   A 1 126 ? 7.701  -18.648 38.151 1.00 57.19  ? 127 ALA   A C   1 
ATOM   1106 O  O   . ALA   A 1 126 ? 6.815  -19.228 38.766 1.00 58.08  ? 127 ALA   A O   1 
ATOM   1107 C  CB  . ALA   A 1 126 ? 8.097  -19.601 35.863 1.00 49.93  ? 127 ALA   A CB  1 
ATOM   1108 N  N   . SER   A 1 127 ? 8.833  -18.222 38.737 1.00 55.51  ? 128 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 127 ? 9.137  -18.427 40.156 1.00 58.16  ? 128 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 127 ? 8.550  -17.366 41.101 1.00 66.84  ? 128 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 127 ? 8.536  -17.592 42.316 1.00 69.21  ? 128 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 127 ? 10.643 -18.562 40.371 1.00 61.54  ? 128 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 127 ? 11.065 -19.908 40.209 1.00 72.37  ? 128 SER   A OG  1 
ATOM   1114 N  N   . GLU   A 1 128 ? 8.039  -16.235 40.562 1.00 63.63  ? 129 GLU   A N   1 
ATOM   1115 C  CA  . GLU   A 1 128 ? 7.455  -15.161 41.381 1.00 84.03  ? 129 GLU   A CA  1 
ATOM   1116 C  C   . GLU   A 1 128 ? 6.025  -15.466 41.861 1.00 128.23 ? 129 GLU   A C   1 
ATOM   1117 O  O   . GLU   A 1 128 ? 5.620  -16.623 41.958 1.00 96.37  ? 129 GLU   A O   1 
ATOM   1118 C  CB  . GLU   A 1 128 ? 7.530  -13.797 40.665 1.00 84.57  ? 129 GLU   A CB  1 
ATOM   1119 C  CG  . GLU   A 1 128 ? 6.492  -13.581 39.573 1.00 94.58  ? 129 GLU   A CG  1 
ATOM   1120 C  CD  . GLU   A 1 128 ? 6.652  -12.348 38.701 1.00 115.73 ? 129 GLU   A CD  1 
ATOM   1121 O  OE1 . GLU   A 1 128 ? 7.784  -11.823 38.590 1.00 109.46 ? 129 GLU   A OE1 1 
ATOM   1122 O  OE2 . GLU   A 1 128 ? 5.635  -11.916 38.110 1.00 109.16 ? 129 GLU   A OE2 1 
HETATM 1123 C  C   . ACE   B 2 1   ? 21.218 -35.068 5.838  1.00 29.19  ? 0   ACE   D C   1 
HETATM 1124 O  O   . ACE   B 2 1   ? 21.289 -33.931 6.326  1.00 30.76  ? 0   ACE   D O   1 
HETATM 1125 C  CH3 . ACE   B 2 1   ? 21.426 -36.299 6.706  1.00 29.13  ? 0   ACE   D CH3 1 
ATOM   1126 N  N   A TRP   B 2 2   ? 20.957 -35.301 4.553  0.66 27.52  ? 1   TRP   D N   1 
ATOM   1127 N  N   B TRP   B 2 2   ? 20.960 -35.301 4.551  0.34 28.39  ? 1   TRP   D N   1 
ATOM   1128 C  CA  A TRP   B 2 2   ? 20.738 -34.248 3.564  0.66 26.64  ? 1   TRP   D CA  1 
ATOM   1129 C  CA  B TRP   B 2 2   ? 20.676 -34.228 3.603  0.34 28.05  ? 1   TRP   D CA  1 
ATOM   1130 C  C   A TRP   B 2 2   ? 19.227 -34.102 3.265  0.66 30.94  ? 1   TRP   D C   1 
ATOM   1131 C  C   B TRP   B 2 2   ? 19.171 -34.075 3.447  0.34 30.79  ? 1   TRP   D C   1 
ATOM   1132 O  O   A TRP   B 2 2   ? 18.526 -35.113 3.146  0.66 30.67  ? 1   TRP   D O   1 
ATOM   1133 O  O   B TRP   B 2 2   ? 18.424 -35.054 3.564  0.34 29.98  ? 1   TRP   D O   1 
ATOM   1134 C  CB  A TRP   B 2 2   ? 21.537 -34.569 2.281  0.66 25.68  ? 1   TRP   D CB  1 
ATOM   1135 C  CB  B TRP   B 2 2   ? 21.337 -34.463 2.223  0.34 27.42  ? 1   TRP   D CB  1 
ATOM   1136 C  CG  A TRP   B 2 2   ? 23.035 -34.555 2.473  0.66 25.76  ? 1   TRP   D CG  1 
ATOM   1137 C  CG  B TRP   B 2 2   ? 20.714 -35.549 1.395  0.34 28.60  ? 1   TRP   D CG  1 
ATOM   1138 C  CD1 A TRP   B 2 2   ? 23.824 -35.591 2.886  0.66 28.23  ? 1   TRP   D CD1 1 
ATOM   1139 C  CD1 B TRP   B 2 2   ? 21.096 -36.855 1.346  0.34 31.71  ? 1   TRP   D CD1 1 
ATOM   1140 C  CD2 A TRP   B 2 2   ? 23.915 -33.439 2.266  0.66 25.17  ? 1   TRP   D CD2 1 
ATOM   1141 C  CD2 B TRP   B 2 2   ? 19.623 -35.414 0.466  0.34 28.66  ? 1   TRP   D CD2 1 
ATOM   1142 N  NE1 A TRP   B 2 2   ? 25.140 -35.185 2.960  0.66 27.51  ? 1   TRP   D NE1 1 
ATOM   1143 N  NE1 B TRP   B 2 2   ? 20.287 -37.555 0.484  0.34 31.18  ? 1   TRP   D NE1 1 
ATOM   1144 C  CE2 A TRP   B 2 2   ? 25.226 -33.875 2.569  0.66 28.39  ? 1   TRP   D CE2 1 
ATOM   1145 C  CE2 B TRP   B 2 2   ? 19.383 -36.692 -0.083 0.34 32.69  ? 1   TRP   D CE2 1 
ATOM   1146 C  CE3 A TRP   B 2 2   ? 23.722 -32.105 1.869  0.66 25.73  ? 1   TRP   D CE3 1 
ATOM   1147 C  CE3 B TRP   B 2 2   ? 18.799 -34.343 0.073  0.34 29.54  ? 1   TRP   D CE3 1 
ATOM   1148 C  CZ2 A TRP   B 2 2   ? 26.340 -33.033 2.456  0.66 27.83  ? 1   TRP   D CZ2 1 
ATOM   1149 C  CZ2 B TRP   B 2 2   ? 18.357 -36.931 -1.005 0.34 31.99  ? 1   TRP   D CZ2 1 
ATOM   1150 C  CZ3 A TRP   B 2 2   ? 24.828 -31.280 1.739  0.66 26.86  ? 1   TRP   D CZ3 1 
ATOM   1151 C  CZ3 B TRP   B 2 2   ? 17.792 -34.578 -0.849 0.34 31.18  ? 1   TRP   D CZ3 1 
ATOM   1152 C  CH2 A TRP   B 2 2   ? 26.115 -31.742 2.038  0.66 27.48  ? 1   TRP   D CH2 1 
ATOM   1153 C  CH2 B TRP   B 2 2   ? 17.583 -35.857 -1.383 0.34 31.74  ? 1   TRP   D CH2 1 
ATOM   1154 N  N   . VAL   B 2 3   ? 18.729 -32.854 3.153  1.00 26.48  ? 2   VAL   D N   1 
ATOM   1155 C  CA  . VAL   B 2 3   ? 17.303 -32.548 2.911  1.00 26.60  ? 2   VAL   D CA  1 
ATOM   1156 C  C   . VAL   B 2 3   ? 17.162 -31.496 1.808  1.00 28.45  ? 2   VAL   D C   1 
ATOM   1157 O  O   . VAL   B 2 3   ? 18.142 -30.827 1.456  1.00 26.47  ? 2   VAL   D O   1 
ATOM   1158 C  CB  . VAL   B 2 3   ? 16.588 -32.042 4.205  1.00 29.96  ? 2   VAL   D CB  1 
ATOM   1159 C  CG1 . VAL   B 2 3   ? 16.617 -33.092 5.322  1.00 29.66  ? 2   VAL   D CG1 1 
ATOM   1160 C  CG2 . VAL   B 2 3   ? 17.171 -30.697 4.692  1.00 29.50  ? 2   VAL   D CG2 1 
ATOM   1161 N  N   . ILE   B 2 4   ? 15.925 -31.321 1.329  1.00 25.80  ? 3   ILE   D N   1 
ATOM   1162 C  CA  . ILE   B 2 4   ? 15.546 -30.242 0.435  1.00 25.48  ? 3   ILE   D CA  1 
ATOM   1163 C  C   . ILE   B 2 4   ? 15.170 -29.109 1.419  1.00 30.33  ? 3   ILE   D C   1 
ATOM   1164 O  O   . ILE   B 2 4   ? 14.162 -29.244 2.131  1.00 29.68  ? 3   ILE   D O   1 
ATOM   1165 C  CB  . ILE   B 2 4   ? 14.339 -30.607 -0.466 1.00 27.27  ? 3   ILE   D CB  1 
ATOM   1166 C  CG1 . ILE   B 2 4   ? 14.623 -31.869 -1.360 1.00 25.61  ? 3   ILE   D CG1 1 
ATOM   1167 C  CG2 . ILE   B 2 4   ? 13.913 -29.363 -1.304 1.00 29.51  ? 3   ILE   D CG2 1 
ATOM   1168 C  CD1 . ILE   B 2 4   ? 15.953 -31.770 -2.293 1.00 31.73  ? 3   ILE   D CD1 1 
ATOM   1169 N  N   . PRO   B 2 5   ? 15.958 -28.010 1.500  1.00 30.03  ? 4   PRO   D N   1 
ATOM   1170 C  CA  . PRO   B 2 5   ? 15.635 -26.947 2.475  1.00 30.50  ? 4   PRO   D CA  1 
ATOM   1171 C  C   . PRO   B 2 5   ? 14.400 -26.127 2.101  1.00 33.93  ? 4   PRO   D C   1 
ATOM   1172 O  O   . PRO   B 2 5   ? 14.079 -26.003 0.924  1.00 32.36  ? 4   PRO   D O   1 
ATOM   1173 C  CB  . PRO   B 2 5   ? 16.901 -26.083 2.491  1.00 32.64  ? 4   PRO   D CB  1 
ATOM   1174 C  CG  . PRO   B 2 5   ? 17.471 -26.248 1.098  1.00 36.89  ? 4   PRO   D CG  1 
ATOM   1175 C  CD  . PRO   B 2 5   ? 17.186 -27.689 0.737  1.00 32.67  ? 4   PRO   D CD  1 
ATOM   1176 N  N   . ALA   B 2 6   ? 13.698 -25.590 3.109  1.00 33.34  ? 5   ALA   D N   1 
HETATM 1177 C  C4  . A1ACA C 3 .   ? 25.471 -10.143 16.473 1.00 26.11  ? 201 A1ACA A C4  1 
HETATM 1178 C  C5  . A1ACA C 3 .   ? 24.879 -8.875  16.509 1.00 26.68  ? 201 A1ACA A C5  1 
HETATM 1179 C  C6  . A1ACA C 3 .   ? 23.862 -8.592  17.411 1.00 27.88  ? 201 A1ACA A C6  1 
HETATM 1180 C  C7  . A1ACA C 3 .   ? 23.425 -9.604  18.261 1.00 28.93  ? 201 A1ACA A C7  1 
HETATM 1181 C  C8  . A1ACA C 3 .   ? 22.255 -10.787 19.828 1.00 33.18  ? 201 A1ACA A C8  1 
HETATM 1182 C  C10 . A1ACA C 3 .   ? 23.966 -10.885 18.200 1.00 27.93  ? 201 A1ACA A C10 1 
HETATM 1183 C  C1  . A1ACA C 3 .   ? 27.254 -10.257 11.921 1.00 31.36  ? 201 A1ACA A C1  1 
HETATM 1184 C  C2  . A1ACA C 3 .   ? 27.390 -10.590 13.255 1.00 29.63  ? 201 A1ACA A C2  1 
HETATM 1185 C  C3  . A1ACA C 3 .   ? 26.353 -10.245 14.147 1.00 28.95  ? 201 A1ACA A C3  1 
HETATM 1186 C  C9  . A1ACA C 3 .   ? 23.253 -11.740 19.206 1.00 30.55  ? 201 A1ACA A C9  1 
HETATM 1187 O  O   . A1ACA C 3 .   ? 21.426 -11.049 20.698 1.00 33.90  ? 201 A1ACA A O   1 
HETATM 1188 N  N2  . A1ACA C 3 .   ? 22.425 -9.571  19.241 1.00 31.16  ? 201 A1ACA A N2  1 
HETATM 1189 C  C11 . A1ACA C 3 .   ? 24.991 -11.160 17.303 1.00 27.72  ? 201 A1ACA A C11 1 
HETATM 1190 N  N1  . A1ACA C 3 .   ? 26.361 -10.566 15.470 1.00 26.27  ? 201 A1ACA A N1  1 
HETATM 1191 N  N3  . A1ACA C 3 .   ? 25.262 -9.630  13.662 1.00 31.77  ? 201 A1ACA A N3  1 
HETATM 1192 C  C   . A1ACA C 3 .   ? 25.255 -9.373  12.367 1.00 34.15  ? 201 A1ACA A C   1 
HETATM 1193 CL CL  . A1ACA C 3 .   ? 23.814 -8.604  11.783 0.49 33.26  ? 201 A1ACA A CL  1 
HETATM 1194 BR BR  . A1ACA C 3 .   ? 28.939 -11.489 13.837 0.70 26.88  ? 201 A1ACA A BR  1 
HETATM 1195 N  N   . A1ACA C 3 .   ? 26.171 -9.628  11.449 1.00 32.74  ? 201 A1ACA A N   1 
HETATM 1196 CL CL  . CL    D 4 .   ? 21.334 -15.372 22.687 1.00 38.47  ? 202 CL    A CL  1 
HETATM 1197 S  S   A DMS   E 5 .   ? 17.557 -35.356 -1.308 0.66 46.38  ? 101 DMS   D S   1 
HETATM 1198 O  O   A DMS   E 5 .   ? 16.251 -35.150 -0.690 0.66 47.21  ? 101 DMS   D O   1 
HETATM 1199 C  C1  A DMS   E 5 .   ? 18.637 -34.417 -0.260 0.66 45.51  ? 101 DMS   D C1  1 
HETATM 1200 C  C2  A DMS   E 5 .   ? 18.002 -36.970 -0.767 0.66 45.45  ? 101 DMS   D C2  1 
HETATM 1201 O  O   . HOH   F 6 .   ? 35.670 -25.819 25.549 1.00 39.80  ? 301 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 6 .   ? 25.775 -3.546  26.474 1.00 35.10  ? 302 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 6 .   ? 26.780 -32.044 16.155 1.00 46.09  ? 303 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 6 .   ? 22.694 -5.460  19.945 1.00 55.08  ? 304 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 6 .   ? 20.784 -5.887  26.185 1.00 41.86  ? 305 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 6 .   ? 41.079 -21.653 25.174 1.00 43.36  ? 306 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 6 .   ? 37.830 2.348   19.827 1.00 41.35  ? 307 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 6 .   ? 16.437 -27.477 -3.234 1.00 51.52  ? 308 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 6 .   ? 44.347 -0.915  17.891 1.00 50.63  ? 309 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 6 .   ? 33.273 -20.828 29.607 1.00 48.35  ? 310 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 6 .   ? 19.940 -9.663  37.103 1.00 39.56  ? 311 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 6 .   ? 38.452 -14.985 15.507 1.00 36.82  ? 312 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 6 .   ? 29.783 -32.237 9.542  1.00 49.92  ? 313 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 6 .   ? 37.187 -12.491 40.303 1.00 60.87  ? 314 HOH   A O   1 
HETATM 1215 O  O   A HOH   F 6 .   ? 19.046 -22.949 4.372  0.67 43.95  ? 315 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 6 .   ? 37.694 -20.501 26.977 1.00 36.73  ? 316 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 6 .   ? 22.665 -27.664 17.752 1.00 50.37  ? 317 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 6 .   ? 45.081 -11.320 18.847 1.00 69.37  ? 318 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 6 .   ? 15.419 -10.061 24.999 1.00 48.82  ? 319 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 6 .   ? 30.348 1.358   33.851 1.00 65.40  ? 320 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 6 .   ? 28.280 -8.947  39.989 1.00 48.41  ? 321 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 6 .   ? 43.625 -6.630  32.014 1.00 51.78  ? 322 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 6 .   ? 23.359 -5.881  32.939 1.00 38.86  ? 323 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 6 .   ? 31.663 -0.946  15.896 1.00 44.64  ? 324 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 6 .   ? 21.707 -29.533 -5.231 1.00 39.07  ? 325 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 6 .   ? 20.364 -13.542 20.619 1.00 45.39  ? 326 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 6 .   ? 21.445 -27.153 14.648 0.50 35.79  ? 327 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 6 .   ? 32.657 -24.643 32.189 1.00 62.20  ? 328 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 6 .   ? 27.194 -10.217 35.930 1.00 39.97  ? 329 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 6 .   ? 17.898 -29.446 7.688  1.00 35.45  ? 330 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 6 .   ? 25.665 -2.986  20.088 1.00 59.36  ? 331 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 6 .   ? 28.753 -21.887 41.634 1.00 74.16  ? 332 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 6 .   ? 21.935 -25.009 18.345 1.00 24.33  ? 333 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 6 .   ? 23.297 -17.066 44.310 1.00 67.84  ? 334 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 6 .   ? 29.374 -27.409 20.649 1.00 24.82  ? 335 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 6 .   ? 28.218 -23.774 31.720 1.00 40.14  ? 336 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 6 .   ? 22.963 -28.263 12.664 1.00 25.01  ? 337 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 6 .   ? 30.374 -0.706  37.059 1.00 51.85  ? 338 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 6 .   ? 27.314 -28.235 18.647 1.00 28.11  ? 339 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 6 .   ? 41.246 -16.928 15.213 1.00 41.47  ? 340 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 6 .   ? 34.431 -23.889 29.886 1.00 75.72  ? 341 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 6 .   ? 36.874 -5.741  12.322 1.00 39.97  ? 342 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 6 .   ? 23.966 -15.846 21.306 1.00 32.49  ? 343 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 6 .   ? 26.099 -22.650 29.943 1.00 28.56  ? 344 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 6 .   ? 41.376 -12.746 14.063 1.00 109.63 ? 345 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 6 .   ? 24.883 -26.821 19.044 1.00 35.47  ? 346 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 6 .   ? 21.477 -30.005 14.210 1.00 75.55  ? 347 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 6 .   ? 43.927 -4.408  25.821 1.00 46.87  ? 348 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 6 .   ? 18.012 -34.528 8.353  1.00 34.28  ? 349 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 6 .   ? 41.138 -1.487  11.674 1.00 64.94  ? 350 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 6 .   ? 28.980 -31.167 7.254  1.00 36.74  ? 351 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 6 .   ? 10.783 -11.565 34.591 1.00 49.38  ? 352 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 6 .   ? 20.843 -7.371  19.824 1.00 50.03  ? 353 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 6 .   ? 37.307 -6.452  34.373 1.00 41.44  ? 354 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 6 .   ? 44.415 -12.694 41.374 1.00 55.58  ? 355 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 6 .   ? 46.811 -21.655 18.099 1.00 49.25  ? 356 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 6 .   ? 28.857 -0.461  16.931 1.00 76.16  ? 357 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 6 .   ? 26.861 -35.358 11.628 1.00 57.21  ? 358 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 6 .   ? 45.971 -14.233 21.578 1.00 56.80  ? 359 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 6 .   ? 42.467 -10.519 15.526 1.00 53.45  ? 360 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 6 .   ? 28.534 -24.296 34.394 1.00 53.54  ? 361 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 6 .   ? 34.779 -18.972 13.882 0.50 24.75  ? 362 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 6 .   ? 47.149 -25.295 21.630 1.00 54.46  ? 363 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 6 .   ? 30.612 -28.935 22.654 1.00 43.09  ? 364 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 6 .   ? 46.206 -15.841 27.607 1.00 68.54  ? 365 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 6 .   ? 26.106 -21.934 38.671 1.00 40.18  ? 366 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 6 .   ? 41.303 -7.777  46.465 1.00 56.81  ? 367 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 6 .   ? 14.332 -16.869 23.528 1.00 44.82  ? 368 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 6 .   ? 26.894 -16.671 38.716 1.00 54.38  ? 369 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 6 .   ? 34.116 -7.986  35.696 1.00 37.48  ? 370 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 6 .   ? 38.974 -18.926 33.411 1.00 46.02  ? 371 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 6 .   ? 12.671 -20.672 42.475 1.00 58.64  ? 372 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 6 .   ? 27.579 -23.129 13.883 0.50 26.74  ? 373 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 6 .   ? 24.062 -28.660 21.588 1.00 54.64  ? 374 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 6 .   ? 20.294 -16.013 40.944 1.00 36.95  ? 375 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 6 .   ? 44.613 -16.391 29.740 1.00 54.31  ? 376 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 6 .   ? 12.227 -18.162 25.888 1.00 58.35  ? 377 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 6 .   ? 26.078 -19.261 41.726 1.00 64.99  ? 378 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 6 .   ? 37.949 -16.668 13.139 0.50 29.51  ? 379 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 6 .   ? 27.081 -2.393  16.105 1.00 63.79  ? 380 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 6 .   ? 43.803 -10.678 35.125 1.00 73.86  ? 381 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 6 .   ? 42.154 -6.049  11.916 1.00 70.29  ? 382 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 6 .   ? 11.633 -15.348 40.583 1.00 80.27  ? 383 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 6 .   ? 26.134 -8.105  9.024  1.00 46.60  ? 384 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 6 .   ? 45.478 -10.873 30.269 1.00 56.52  ? 385 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 6 .   ? 46.284 -18.940 19.633 1.00 54.26  ? 386 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 6 .   ? 45.219 -12.653 23.625 1.00 48.81  ? 387 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 6 .   ? 37.455 3.344   15.806 1.00 41.62  ? 388 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 6 .   ? 19.905 -25.545 41.328 1.00 78.71  ? 389 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 6 .   ? 34.762 -29.179 26.039 1.00 66.20  ? 390 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 6 .   ? 41.266 -7.030  35.966 1.00 45.25  ? 391 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 6 .   ? 31.878 -31.892 14.560 1.00 38.15  ? 392 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 6 .   ? 17.319 -24.558 -2.130 1.00 67.44  ? 393 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 6 .   ? 23.650 -15.745 17.806 1.00 43.19  ? 394 HOH   A O   1 
HETATM 1295 O  O   A HOH   F 6 .   ? 12.164 -20.735 27.894 0.66 45.94  ? 395 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 6 .   ? 33.062 -29.815 21.482 1.00 42.20  ? 396 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 6 .   ? 16.755 -6.515  27.619 1.00 64.00  ? 397 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 6 .   ? 26.442 -30.786 19.020 1.00 57.16  ? 398 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 6 .   ? 40.329 -19.639 29.026 1.00 36.88  ? 399 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 6 .   ? 29.653 -22.720 36.844 1.00 67.74  ? 400 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 6 .   ? 47.423 -6.745  20.318 1.00 69.74  ? 401 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 6 .   ? 46.060 -8.970  44.121 1.00 52.04  ? 402 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 6 .   ? 35.162 -29.746 23.414 1.00 45.62  ? 403 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 6 .   ? 36.976 -2.266  11.589 1.00 60.58  ? 404 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 6 .   ? 4.227  -20.407 37.897 1.00 65.15  ? 405 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 6 .   ? 30.369 -10.657 40.625 1.00 45.11  ? 406 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 6 .   ? 10.404 -11.744 40.007 1.00 65.27  ? 407 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 6 .   ? 44.631 -8.790  17.954 1.00 69.40  ? 408 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 6 .   ? 25.578 -4.630  17.949 1.00 52.35  ? 409 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 6 .   ? 22.949 -14.996 40.422 1.00 33.95  ? 410 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 6 .   ? 41.265 -17.102 35.214 1.00 46.09  ? 411 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 6 .   ? 45.797 -17.119 17.306 1.00 69.43  ? 412 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 6 .   ? 46.927 -20.194 21.936 1.00 68.66  ? 413 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 6 .   ? 21.220 -23.290 42.093 1.00 50.25  ? 414 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 6 .   ? 33.524 -33.011 12.067 1.00 50.21  ? 415 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 6 .   ? 32.387 -9.047  39.769 1.00 60.10  ? 416 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 6 .   ? 32.136 -15.689 39.879 1.00 37.00  ? 417 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 6 .   ? 19.632 -27.311 10.083 1.00 54.51  ? 418 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 6 .   ? 35.158 1.900   13.579 1.00 57.60  ? 419 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 6 .   ? 27.320 -25.560 28.322 1.00 58.77  ? 420 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 6 .   ? 26.992 -1.613  22.027 1.00 55.37  ? 421 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 6 .   ? 42.025 -8.071  13.764 1.00 61.39  ? 422 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 6 .   ? 29.529 -0.908  22.316 1.00 58.25  ? 423 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 6 .   ? 39.872 -5.594  33.958 1.00 42.94  ? 424 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 6 .   ? 25.615 -16.121 41.128 1.00 50.70  ? 425 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 6 .   ? 33.456 -0.375  20.105 1.00 44.06  ? 426 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 6 .   ? 34.465 -18.894 36.272 1.00 65.81  ? 427 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 6 .   ? 45.826 -5.527  23.690 1.00 51.59  ? 428 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 6 .   ? 23.454 -30.492 19.325 1.00 65.63  ? 429 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 6 .   ? 33.980 -32.796 21.999 1.00 69.43  ? 430 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 6 .   ? 42.835 -18.236 30.733 1.00 48.33  ? 431 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 6 .   ? 22.270 -10.545 14.645 1.00 43.36  ? 432 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 6 .   ? 26.420 -29.502 22.668 1.00 61.25  ? 433 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 6 .   ? 37.127 -31.611 23.373 1.00 78.87  ? 434 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 6 .   ? 44.390 -4.249  28.903 1.00 66.41  ? 435 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 6 .   ? 31.752 -26.183 27.100 1.00 56.24  ? 436 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 6 .   ? 31.893 -0.050  13.324 1.00 63.92  ? 437 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 6 .   ? 23.055 -3.151  26.842 1.00 64.37  ? 438 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 6 .   ? 26.984 -34.458 18.039 1.00 65.09  ? 439 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 6 .   ? 28.777 -2.597  13.153 1.00 76.12  ? 440 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 6 .   ? 19.443 -31.794 13.909 1.00 70.36  ? 441 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 6 .   ? 47.918 -23.477 19.777 1.00 63.77  ? 442 HOH   A O   1 
HETATM 1343 O  O   . HOH   F 6 .   ? 30.660 -34.316 14.879 1.00 60.97  ? 443 HOH   A O   1 
HETATM 1344 O  O   . HOH   F 6 .   ? 19.710 -8.180  24.634 1.00 53.07  ? 444 HOH   A O   1 
HETATM 1345 O  O   . HOH   F 6 .   ? 36.795 -24.491 27.637 1.00 56.90  ? 445 HOH   A O   1 
HETATM 1346 O  O   . HOH   F 6 .   ? 35.417 -4.257  10.668 1.00 47.57  ? 446 HOH   A O   1 
HETATM 1347 O  O   . HOH   F 6 .   ? 46.638 -14.708 18.300 1.00 70.67  ? 447 HOH   A O   1 
HETATM 1348 O  O   . HOH   F 6 .   ? 24.518 -21.814 41.097 1.00 59.11  ? 448 HOH   A O   1 
HETATM 1349 O  O   . HOH   F 6 .   ? 47.416 -28.393 17.641 1.00 60.34  ? 449 HOH   A O   1 
HETATM 1350 O  O   . HOH   F 6 .   ? 11.953 -18.816 22.710 1.00 68.43  ? 450 HOH   A O   1 
HETATM 1351 O  O   . HOH   F 6 .   ? 35.867 -21.248 30.547 1.00 63.40  ? 451 HOH   A O   1 
HETATM 1352 O  O   . HOH   F 6 .   ? 47.137 -11.927 25.426 1.00 66.67  ? 452 HOH   A O   1 
HETATM 1353 O  O   . HOH   F 6 .   ? 47.030 -12.599 28.462 1.00 62.24  ? 453 HOH   A O   1 
HETATM 1354 O  O   . HOH   F 6 .   ? 32.191 -1.125  22.376 1.00 56.80  ? 454 HOH   A O   1 
HETATM 1355 O  O   . HOH   F 6 .   ? 34.073 -17.652 39.533 1.00 67.91  ? 455 HOH   A O   1 
HETATM 1356 O  O   . HOH   F 6 .   ? 19.418 -7.734  35.287 1.00 57.02  ? 456 HOH   A O   1 
HETATM 1357 O  O   . HOH   F 6 .   ? 43.945 -13.681 13.882 0.50 96.31  ? 457 HOH   A O   1 
HETATM 1358 O  O   . HOH   F 6 .   ? 25.344 -5.746  34.981 1.00 62.51  ? 458 HOH   A O   1 
HETATM 1359 O  O   . HOH   F 6 .   ? 45.545 -8.451  31.406 1.00 62.99  ? 459 HOH   A O   1 
HETATM 1360 O  O   . HOH   F 6 .   ? 17.045 -7.934  25.058 1.00 68.29  ? 460 HOH   A O   1 
HETATM 1361 O  O   . HOH   F 6 .   ? 20.112 -35.265 10.116 1.00 39.84  ? 461 HOH   A O   1 
HETATM 1362 O  O   . HOH   F 6 .   ? 17.079 -28.171 9.923  1.00 51.20  ? 462 HOH   A O   1 
HETATM 1363 O  O   . HOH   F 6 .   ? 19.923 -14.955 43.406 1.00 54.91  ? 463 HOH   A O   1 
HETATM 1364 O  O   . HOH   F 6 .   ? 43.112 -3.044  33.963 1.00 58.73  ? 464 HOH   A O   1 
HETATM 1365 O  O   . HOH   F 6 .   ? 32.509 -20.667 36.985 1.00 77.36  ? 465 HOH   A O   1 
HETATM 1366 O  O   . HOH   F 6 .   ? 28.274 -29.868 24.637 1.00 70.00  ? 466 HOH   A O   1 
HETATM 1367 O  O   . HOH   F 6 .   ? 19.090 -28.247 13.789 0.50 68.02  ? 467 HOH   A O   1 
HETATM 1368 O  O   . HOH   F 6 .   ? 33.820 -11.098 41.648 0.50 63.21  ? 468 HOH   A O   1 
HETATM 1369 O  O   . HOH   F 6 .   ? 33.820 -14.066 41.648 0.50 43.49  ? 469 HOH   A O   1 
HETATM 1370 O  O   . HOH   F 6 .   ? 32.012 -23.898 34.993 1.00 72.17  ? 470 HOH   A O   1 
HETATM 1371 O  O   . HOH   F 6 .   ? 16.752 -6.894  34.937 1.00 74.11  ? 471 HOH   A O   1 
HETATM 1372 O  O   . HOH   F 6 .   ? 12.511 -18.292 19.943 1.00 63.33  ? 472 HOH   A O   1 
HETATM 1373 O  O   . HOH   F 6 .   ? 21.179 -5.741  34.676 1.00 52.91  ? 473 HOH   A O   1 
HETATM 1374 O  O   . HOH   F 6 .   ? 45.144 -12.334 15.934 1.00 74.06  ? 474 HOH   A O   1 
HETATM 1375 O  O   . HOH   F 6 .   ? 39.482 -5.604  11.587 1.00 74.35  ? 475 HOH   A O   1 
HETATM 1376 O  O   . HOH   F 6 .   ? 16.695 -30.040 12.406 1.00 58.98  ? 476 HOH   A O   1 
HETATM 1377 O  O   . HOH   G 6 .   ? 12.171 -24.283 0.026  1.00 54.20  ? 201 HOH   D O   1 
HETATM 1378 O  O   . HOH   G 6 .   ? 17.712 -36.219 6.041  1.00 42.10  ? 202 HOH   D O   1 
HETATM 1379 O  O   . HOH   G 6 .   ? 22.612 -34.024 8.836  1.00 36.13  ? 203 HOH   D O   1 
HETATM 1380 O  O   . HOH   G 6 .   ? 14.898 -25.784 -1.792 1.00 46.47  ? 204 HOH   D O   1 
HETATM 1381 O  O   . HOH   G 6 .   ? 11.457 -23.597 3.138  1.00 57.66  ? 205 HOH   D O   1 
HETATM 1382 O  O   . HOH   G 6 .   ? 20.802 -38.315 4.047  1.00 50.50  ? 206 HOH   D O   1 
HETATM 1383 O  O   . HOH   G 6 .   ? 20.792 -39.435 -2.116 1.00 61.71  ? 207 HOH   D O   1 
HETATM 1384 O  O   . HOH   G 6 .   ? 10.608 -24.700 5.524  1.00 57.84  ? 208 HOH   D O   1 
HETATM 1385 O  O   . HOH   G 6 .   ? 23.620 -36.502 9.967  1.00 51.11  ? 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   ? 0.8482 1.0083 0.7043 0.0326  -0.1325 -0.0189 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8419 0.9955 0.6805 0.0165  -0.1235 -0.0211 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8165 0.9998 0.6791 0.0053  -0.1195 -0.0366 6   ASP A C   
4    O O   . ASP A 5   ? 0.8091 1.0183 0.7010 0.0090  -0.1233 -0.0458 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8648 0.9912 0.6944 0.0078  -0.1062 -0.0148 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0635 1.1692 0.8594 -0.0024 -0.1009 -0.0103 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0636 1.1808 0.8575 -0.0135 -0.0980 -0.0187 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1726 1.2499 0.9439 -0.0005 -0.0984 0.0006  6   ASP A OD2 
9    N N   . SER A 6   ? 0.7070 0.8860 0.5569 -0.0091 -0.1109 -0.0405 7   SER A N   
10   C CA  . SER A 6   ? 0.6588 0.8592 0.5265 -0.0214 -0.1047 -0.0548 7   SER A CA  
11   C C   . SER A 6   ? 0.6020 0.7908 0.4816 -0.0317 -0.0860 -0.0571 7   SER A C   
12   O O   . SER A 6   ? 0.5839 0.7774 0.4671 -0.0437 -0.0777 -0.0662 7   SER A O   
13   C CB  . SER A 6   ? 0.7398 0.9438 0.5848 -0.0295 -0.1092 -0.0588 7   SER A CB  
14   O OG  . SER A 6   ? 0.9073 1.0841 0.7237 -0.0358 -0.1011 -0.0512 7   SER A OG  
15   N N   . CYS A 7   ? 0.4954 0.6689 0.3810 -0.0261 -0.0802 -0.0494 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4555 0.6173 0.3509 -0.0334 -0.0650 -0.0506 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4476 0.6255 0.3685 -0.0395 -0.0593 -0.0620 8   CYS A C   
18   O O   . CYS A 7   ? 0.4330 0.6316 0.3700 -0.0362 -0.0659 -0.0679 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4753 0.6194 0.3710 -0.0256 -0.0621 -0.0405 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5629 0.6790 0.4264 -0.0239 -0.0613 -0.0279 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3418 0.5095 0.2664 -0.0483 -0.0470 -0.0655 9   ILE A N   
22   C CA  . ILE A 8   ? 0.3005 0.4735 0.2446 -0.0540 -0.0393 -0.0737 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3259 0.4820 0.2745 -0.0494 -0.0332 -0.0663 9   ILE A C   
24   O O   . ILE A 8   ? 0.3078 0.4486 0.2446 -0.0453 -0.0327 -0.0576 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3414 0.5132 0.2854 -0.0661 -0.0311 -0.0836 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3464 0.4981 0.2771 -0.0686 -0.0240 -0.0800 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3215 0.5135 0.2633 -0.0714 -0.0375 -0.0926 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.4194 0.5656 0.3509 -0.0785 -0.0149 -0.0896 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2535 0.4110 0.2173 -0.0515 -0.0278 -0.0703 10  GLN A N   
30   N N   B GLN A 9   ? 0.2658 0.4252 0.2302 -0.0508 -0.0288 -0.0703 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2478 0.3892 0.2140 -0.0476 -0.0226 -0.0637 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2567 0.4016 0.2249 -0.0469 -0.0237 -0.0642 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2826 0.4124 0.2526 -0.0551 -0.0127 -0.0682 10  GLN A C   
34   C C   B GLN A 9   ? 0.3067 0.4395 0.2783 -0.0546 -0.0135 -0.0685 10  GLN A C   
35   O O   A GLN A 9   ? 0.2895 0.4272 0.2666 -0.0626 -0.0094 -0.0771 10  GLN A O   
36   O O   B GLN A 9   ? 0.3080 0.4481 0.2865 -0.0624 -0.0099 -0.0775 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2662 0.4173 0.2440 -0.0400 -0.0269 -0.0619 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2653 0.4224 0.2466 -0.0402 -0.0280 -0.0640 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.3112 0.4476 0.2930 -0.0383 -0.0201 -0.0576 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3059 0.4477 0.2864 -0.0335 -0.0255 -0.0554 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5635 0.7029 0.5512 -0.0287 -0.0243 -0.0529 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4666 0.6113 0.4615 -0.0352 -0.0199 -0.0596 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4834 0.6340 0.4718 -0.0210 -0.0334 -0.0514 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3776 0.5417 0.3869 -0.0364 -0.0213 -0.0678 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.4888 0.6164 0.4794 -0.0282 -0.0181 -0.0503 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.4359 0.5619 0.4269 -0.0357 -0.0133 -0.0550 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2613 0.3717 0.2258 -0.0532 -0.0082 -0.0625 11  PHE A N   
48   N N   B PHE A 10  ? 0.2768 0.3902 0.2426 -0.0525 -0.0092 -0.0623 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2575 0.3530 0.2226 -0.0581 -0.0005 -0.0653 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2770 0.3744 0.2426 -0.0571 -0.0015 -0.0646 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2941 0.3850 0.2646 -0.0559 0.0017  -0.0624 11  PHE A C   
52   C C   B PHE A 10  ? 0.3063 0.3995 0.2777 -0.0553 0.0009  -0.0621 11  PHE A C   
53   O O   A PHE A 10  ? 0.2878 0.3708 0.2559 -0.0496 0.0005  -0.0551 11  PHE A O   
54   O O   B PHE A 10  ? 0.2994 0.3869 0.2694 -0.0486 -0.0008 -0.0549 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2803 0.3594 0.2374 -0.0567 0.0019  -0.0626 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.3048 0.3867 0.2619 -0.0550 0.0002  -0.0608 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2928 0.3549 0.2482 -0.0604 0.0077  -0.0660 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3336 0.4180 0.2859 -0.0594 0.0010  -0.0663 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3287 0.3895 0.2834 -0.0679 0.0116  -0.0742 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3801 0.4777 0.3277 -0.0597 -0.0037 -0.0667 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3150 0.3605 0.2677 -0.0561 0.0090  -0.0611 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3789 0.4509 0.3297 -0.0630 0.0062  -0.0714 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3501 0.3902 0.2999 -0.0706 0.0169  -0.0765 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3966 0.4963 0.3383 -0.0650 -0.0021 -0.0727 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3446 0.3710 0.2922 -0.0581 0.0129  -0.0632 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.4248 0.4993 0.3721 -0.0673 0.0079  -0.0778 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3253 0.3475 0.2707 -0.0651 0.0169  -0.0705 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3950 0.4840 0.3378 -0.0690 0.0042  -0.0787 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2567 0.3534 0.2343 -0.0623 0.0057  -0.0692 12  THR A N   
70   C CA  . THR A 11  ? 0.2637 0.3583 0.2468 -0.0626 0.0096  -0.0689 12  THR A CA  
71   C C   . THR A 11  ? 0.2980 0.3695 0.2719 -0.0595 0.0125  -0.0616 12  THR A C   
72   O O   . THR A 11  ? 0.2939 0.3655 0.2705 -0.0546 0.0118  -0.0572 12  THR A O   
73   C CB  . THR A 11  ? 0.3328 0.4320 0.3212 -0.0736 0.0168  -0.0792 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3267 0.4512 0.3256 -0.0762 0.0127  -0.0872 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3911 0.4912 0.3860 -0.0756 0.0221  -0.0809 12  THR A CG2 
76   N N   . ARG A 12  ? 0.2801 0.3323 0.2435 -0.0619 0.0153  -0.0609 13  ARG A N   
77   C CA  . ARG A 12  ? 0.2959 0.3266 0.2499 -0.0587 0.0166  -0.0549 13  ARG A CA  
78   C C   . ARG A 12  ? 0.3093 0.3381 0.2618 -0.0500 0.0112  -0.0482 13  ARG A C   
79   O O   . ARG A 12  ? 0.3025 0.3158 0.2483 -0.0470 0.0110  -0.0443 13  ARG A O   
80   C CB  . ARG A 12  ? 0.3738 0.3824 0.3164 -0.0634 0.0207  -0.0572 13  ARG A CB  
81   C CG  . ARG A 12  ? 0.5221 0.5240 0.4610 -0.0743 0.0286  -0.0635 13  ARG A CG  
82   C CD  . ARG A 12  ? 0.7952 0.7897 0.7303 -0.0771 0.0333  -0.0617 13  ARG A CD  
83   N NE  . ARG A 12  ? 0.9644 0.9322 0.8834 -0.0732 0.0324  -0.0549 13  ARG A NE  
84   C CZ  . ARG A 12  ? 1.1033 1.0631 1.0164 -0.0732 0.0343  -0.0514 13  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.9804 0.9162 0.8773 -0.0693 0.0320  -0.0455 13  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.8624 0.8389 0.7863 -0.0763 0.0382  -0.0543 13  ARG A NH2 
87   N N   . HIS A 13  ? 0.2529 0.2960 0.2097 -0.0468 0.0070  -0.0473 14  HIS A N   
88   C CA  . HIS A 13  ? 0.2625 0.3027 0.2165 -0.0413 0.0040  -0.0427 14  HIS A CA  
89   C C   . HIS A 13  ? 0.2987 0.3326 0.2517 -0.0369 0.0036  -0.0370 14  HIS A C   
90   O O   . HIS A 13  ? 0.2931 0.3169 0.2426 -0.0345 0.0032  -0.0352 14  HIS A O   
91   C CB  . HIS A 13  ? 0.2571 0.3106 0.2114 -0.0402 0.0006  -0.0424 14  HIS A CB  
92   C CG  . HIS A 13  ? 0.2881 0.3373 0.2381 -0.0370 -0.0001 -0.0389 14  HIS A CG  
93   N ND1 . HIS A 13  ? 0.3005 0.3444 0.2495 -0.0380 0.0016  -0.0422 14  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2992 0.3487 0.2463 -0.0336 -0.0016 -0.0334 14  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2965 0.3400 0.2432 -0.0362 0.0017  -0.0397 14  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2924 0.3375 0.2361 -0.0341 0.0001  -0.0340 14  HIS A NE2 
97   N N   . ALA A 14  ? 0.2615 0.3025 0.2188 -0.0355 0.0034  -0.0353 15  ALA A N   
98   C CA  . ALA A 14  ? 0.2671 0.3017 0.2234 -0.0317 0.0038  -0.0305 15  ALA A CA  
99   C C   . ALA A 14  ? 0.2946 0.3139 0.2452 -0.0337 0.0067  -0.0305 15  ALA A C   
100  O O   . ALA A 14  ? 0.2677 0.2788 0.2144 -0.0310 0.0058  -0.0274 15  ALA A O   
101  C CB  . ALA A 14  ? 0.2816 0.3261 0.2449 -0.0293 0.0035  -0.0303 15  ALA A CB  
102  N N   A SER A 15  ? 0.2824 0.2970 0.2311 -0.0389 0.0101  -0.0342 16  SER A N   
103  N N   B SER A 15  ? 0.2766 0.2911 0.2252 -0.0389 0.0101  -0.0342 16  SER A N   
104  N N   C SER A 15  ? 0.2691 0.2835 0.2177 -0.0389 0.0102  -0.0341 16  SER A N   
105  C CA  A SER A 15  ? 0.2959 0.2917 0.2340 -0.0414 0.0126  -0.0335 16  SER A CA  
106  C CA  B SER A 15  ? 0.2889 0.2847 0.2270 -0.0415 0.0127  -0.0336 16  SER A CA  
107  C CA  C SER A 15  ? 0.2773 0.2730 0.2154 -0.0413 0.0126  -0.0334 16  SER A CA  
108  C C   A SER A 15  ? 0.3457 0.3297 0.2770 -0.0379 0.0086  -0.0322 16  SER A C   
109  C C   B SER A 15  ? 0.3482 0.3319 0.2793 -0.0380 0.0087  -0.0323 16  SER A C   
110  C C   C SER A 15  ? 0.3437 0.3273 0.2747 -0.0380 0.0087  -0.0322 16  SER A C   
111  O O   A SER A 15  ? 0.3173 0.2895 0.2413 -0.0353 0.0067  -0.0295 16  SER A O   
112  O O   B SER A 15  ? 0.3314 0.3029 0.2549 -0.0355 0.0068  -0.0296 16  SER A O   
113  O O   C SER A 15  ? 0.3279 0.2989 0.2511 -0.0355 0.0068  -0.0296 16  SER A O   
114  C CB  A SER A 15  ? 0.3465 0.3374 0.2812 -0.0493 0.0184  -0.0382 16  SER A CB  
115  C CB  B SER A 15  ? 0.3326 0.3235 0.2673 -0.0494 0.0184  -0.0384 16  SER A CB  
116  C CB  C SER A 15  ? 0.3063 0.2968 0.2408 -0.0492 0.0186  -0.0379 16  SER A CB  
117  O OG  A SER A 15  ? 0.4222 0.3908 0.3418 -0.0523 0.0212  -0.0368 16  SER A OG  
118  O OG  B SER A 15  ? 0.3695 0.3745 0.3139 -0.0525 0.0224  -0.0417 16  SER A OG  
119  O OG  C SER A 15  ? 0.2931 0.2841 0.2275 -0.0525 0.0189  -0.0419 16  SER A OG  
120  N N   . ASP A 16  ? 0.3185 0.3072 0.2530 -0.0376 0.0070  -0.0351 17  ASP A N   
121  C CA  . ASP A 16  ? 0.3299 0.3107 0.2618 -0.0333 0.0032  -0.0360 17  ASP A CA  
122  C C   . ASP A 16  ? 0.3250 0.3124 0.2617 -0.0282 -0.0002 -0.0340 17  ASP A C   
123  O O   . ASP A 16  ? 0.3238 0.3035 0.2581 -0.0240 -0.0039 -0.0342 17  ASP A O   
124  C CB  . ASP A 16  ? 0.3507 0.3375 0.2867 -0.0350 0.0038  -0.0409 17  ASP A CB  
125  C CG  . ASP A 16  ? 0.4694 0.4457 0.3992 -0.0407 0.0076  -0.0444 17  ASP A CG  
126  O OD1 . ASP A 16  ? 0.4537 0.4151 0.3740 -0.0436 0.0102  -0.0428 17  ASP A OD1 
127  O OD2 . ASP A 16  ? 0.5018 0.4838 0.4349 -0.0434 0.0089  -0.0493 17  ASP A OD2 
128  N N   . VAL A 17  ? 0.2686 0.2697 0.2112 -0.0287 0.0008  -0.0324 18  VAL A N   
129  C CA  . VAL A 17  ? 0.2628 0.2678 0.2079 -0.0260 -0.0005 -0.0309 18  VAL A CA  
130  C C   . VAL A 17  ? 0.3068 0.3026 0.2476 -0.0245 -0.0014 -0.0283 18  VAL A C   
131  O O   . VAL A 17  ? 0.2814 0.2751 0.2226 -0.0219 -0.0042 -0.0297 18  VAL A O   
132  C CB  . VAL A 17  ? 0.2842 0.2996 0.2315 -0.0270 0.0011  -0.0286 18  VAL A CB  
133  C CG1 . VAL A 17  ? 0.2864 0.3011 0.2331 -0.0259 0.0017  -0.0264 18  VAL A CG1 
134  C CG2 . VAL A 17  ? 0.2759 0.2999 0.2244 -0.0289 0.0012  -0.0315 18  VAL A CG2 
135  N N   . LEU A 18  ? 0.2788 0.2703 0.2159 -0.0264 0.0011  -0.0259 19  LEU A N   
136  C CA  . LEU A 18  ? 0.2958 0.2781 0.2269 -0.0262 0.0013  -0.0238 19  LEU A CA  
137  C C   . LEU A 18  ? 0.3152 0.2832 0.2370 -0.0247 -0.0026 -0.0245 19  LEU A C   
138  O O   . LEU A 18  ? 0.3048 0.2689 0.2234 -0.0223 -0.0059 -0.0243 19  LEU A O   
139  C CB  . LEU A 18  ? 0.3056 0.2871 0.2357 -0.0293 0.0061  -0.0227 19  LEU A CB  
140  C CG  . LEU A 18  ? 0.3490 0.3231 0.2738 -0.0298 0.0079  -0.0212 19  LEU A CG  
141  C CD1 . LEU A 18  ? 0.3480 0.3278 0.2777 -0.0271 0.0073  -0.0198 19  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.4141 0.3884 0.3394 -0.0333 0.0139  -0.0222 19  LEU A CD2 
143  N N   . LEU A 19  ? 0.3063 0.2664 0.2232 -0.0256 -0.0027 -0.0258 20  LEU A N   
144  C CA  . LEU A 19  ? 0.3252 0.2676 0.2304 -0.0227 -0.0075 -0.0259 20  LEU A CA  
145  C C   . LEU A 19  ? 0.3514 0.2999 0.2638 -0.0156 -0.0146 -0.0286 20  LEU A C   
146  O O   . LEU A 19  ? 0.3432 0.2835 0.2491 -0.0113 -0.0206 -0.0283 20  LEU A O   
147  C CB  . LEU A 19  ? 0.3534 0.2858 0.2530 -0.0251 -0.0054 -0.0275 20  LEU A CB  
148  C CG  . LEU A 19  ? 0.4690 0.3773 0.3527 -0.0214 -0.0103 -0.0268 20  LEU A CG  
149  C CD1 . LEU A 19  ? 0.5181 0.4064 0.3820 -0.0243 -0.0097 -0.0226 20  LEU A CD1 
150  C CD2 . LEU A 19  ? 0.5366 0.4345 0.4155 -0.0249 -0.0065 -0.0291 20  LEU A CD2 
151  N N   . ASN A 20  ? 0.3085 0.2730 0.2347 -0.0149 -0.0137 -0.0321 21  ASN A N   
152  C CA  . ASN A 20  ? 0.2993 0.2737 0.2358 -0.0098 -0.0184 -0.0371 21  ASN A CA  
153  C C   . ASN A 20  ? 0.3228 0.3050 0.2630 -0.0100 -0.0192 -0.0372 21  ASN A C   
154  O O   . ASN A 20  ? 0.3186 0.3033 0.2625 -0.0054 -0.0252 -0.0412 21  ASN A O   
155  C CB  . ASN A 20  ? 0.3169 0.3048 0.2645 -0.0112 -0.0152 -0.0415 21  ASN A CB  
156  C CG  . ASN A 20  ? 0.4492 0.4292 0.3953 -0.0087 -0.0165 -0.0446 21  ASN A CG  
157  O OD1 . ASN A 20  ? 0.4054 0.3694 0.3435 -0.0037 -0.0216 -0.0444 21  ASN A OD1 
158  N ND2 . ASN A 20  ? 0.3623 0.3510 0.3138 -0.0123 -0.0121 -0.0476 21  ASN A ND2 
159  N N   . LEU A 21  ? 0.2929 0.2788 0.2323 -0.0151 -0.0136 -0.0335 22  LEU A N   
160  C CA  . LEU A 21  ? 0.2852 0.2749 0.2258 -0.0165 -0.0130 -0.0336 22  LEU A CA  
161  C C   . LEU A 21  ? 0.3264 0.3045 0.2571 -0.0141 -0.0183 -0.0326 22  LEU A C   
162  O O   . LEU A 21  ? 0.3157 0.2983 0.2492 -0.0128 -0.0220 -0.0361 22  LEU A O   
163  C CB  . LEU A 21  ? 0.2870 0.2781 0.2264 -0.0209 -0.0062 -0.0293 22  LEU A CB  
164  C CG  . LEU A 21  ? 0.3154 0.3164 0.2609 -0.0230 -0.0023 -0.0296 22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.3199 0.3194 0.2623 -0.0247 0.0022  -0.0245 22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.3456 0.3557 0.2979 -0.0245 -0.0015 -0.0348 22  LEU A CD2 
167  N N   . ASN A 22  ? 0.3101 0.2728 0.2278 -0.0147 -0.0182 -0.0285 23  ASN A N   
168  C CA  . ASN A 22  ? 0.3276 0.2752 0.2303 -0.0132 -0.0231 -0.0269 23  ASN A CA  
169  C C   . ASN A 22  ? 0.3713 0.3154 0.2729 -0.0053 -0.0338 -0.0303 23  ASN A C   
170  O O   . ASN A 22  ? 0.3862 0.3266 0.2813 -0.0024 -0.0406 -0.0313 23  ASN A O   
171  C CB  . ASN A 22  ? 0.3564 0.2863 0.2432 -0.0174 -0.0188 -0.0225 23  ASN A CB  
172  C CG  . ASN A 22  ? 0.4596 0.3733 0.3278 -0.0186 -0.0213 -0.0204 23  ASN A CG  
173  O OD1 . ASN A 22  ? 0.4178 0.3364 0.2868 -0.0186 -0.0232 -0.0217 23  ASN A OD1 
174  N ND2 . ASN A 22  ? 0.4724 0.3648 0.3214 -0.0206 -0.0208 -0.0175 23  ASN A ND2 
175  N N   . ARG A 23  ? 0.3437 0.2897 0.2520 -0.0011 -0.0359 -0.0327 24  ARG A N   
176  C CA  . ARG A 23  ? 0.3603 0.3050 0.2715 0.0086  -0.0465 -0.0373 24  ARG A CA  
177  C C   . ARG A 23  ? 0.3943 0.3610 0.3230 0.0110  -0.0504 -0.0448 24  ARG A C   
178  O O   . ARG A 23  ? 0.3883 0.3550 0.3165 0.0183  -0.0608 -0.0484 24  ARG A O   
179  C CB  . ARG A 23  ? 0.3470 0.2920 0.2652 0.0114  -0.0453 -0.0400 24  ARG A CB  
180  C CG  . ARG A 23  ? 0.4022 0.3219 0.3012 0.0101  -0.0436 -0.0345 24  ARG A CG  
181  C CD  . ARG A 23  ? 0.4433 0.3644 0.3497 0.0103  -0.0401 -0.0377 24  ARG A CD  
182  N NE  . ARG A 23  ? 0.5490 0.4438 0.4358 0.0082  -0.0379 -0.0335 24  ARG A NE  
183  C CZ  . ARG A 23  ? 0.7328 0.6247 0.6205 0.0037  -0.0314 -0.0350 24  ARG A CZ  
184  N NH1 . ARG A 23  ? 0.5669 0.4811 0.4732 0.0012  -0.0269 -0.0398 24  ARG A NH1 
185  N NH2 . ARG A 23  ? 0.6619 0.5278 0.5302 0.0005  -0.0288 -0.0319 24  ARG A NH2 
186  N N   . LEU A 24  ? 0.3402 0.3250 0.2832 0.0046  -0.0419 -0.0474 25  LEU A N   
187  C CA  . LEU A 24  ? 0.3228 0.3276 0.2813 0.0036  -0.0426 -0.0553 25  LEU A CA  
188  C C   . LEU A 24  ? 0.3652 0.3669 0.3157 0.0019  -0.0458 -0.0544 25  LEU A C   
189  O O   . LEU A 24  ? 0.3527 0.3650 0.3110 0.0058  -0.0534 -0.0617 25  LEU A O   
190  C CB  . LEU A 24  ? 0.3079 0.3255 0.2760 -0.0047 -0.0315 -0.0565 25  LEU A CB  
191  C CG  . LEU A 24  ? 0.3415 0.3660 0.3184 -0.0047 -0.0276 -0.0594 25  LEU A CG  
192  C CD1 . LEU A 24  ? 0.3388 0.3728 0.3199 -0.0135 -0.0173 -0.0597 25  LEU A CD1 
193  C CD2 . LEU A 24  ? 0.3384 0.3746 0.3304 0.0027  -0.0344 -0.0700 25  LEU A CD2 
194  N N   . ARG A 25  ? 0.3222 0.3104 0.2578 -0.0037 -0.0401 -0.0465 26  ARG A N   
195  C CA  . ARG A 25  ? 0.3339 0.3167 0.2594 -0.0061 -0.0421 -0.0457 26  ARG A CA  
196  C C   . ARG A 25  ? 0.4114 0.3843 0.3253 0.0018  -0.0556 -0.0466 26  ARG A C   
197  O O   . ARG A 25  ? 0.4063 0.3871 0.3223 0.0030  -0.0621 -0.0521 26  ARG A O   
198  C CB  . ARG A 25  ? 0.3582 0.3270 0.2699 -0.0125 -0.0336 -0.0380 26  ARG A CB  
199  C CG  . ARG A 25  ? 0.4037 0.3683 0.3061 -0.0162 -0.0341 -0.0388 26  ARG A CG  
200  C CD  . ARG A 25  ? 0.4688 0.4222 0.3608 -0.0225 -0.0247 -0.0335 26  ARG A CD  
201  N NE  . ARG A 25  ? 0.4233 0.3602 0.3009 -0.0222 -0.0239 -0.0280 26  ARG A NE  
202  C CZ  . ARG A 25  ? 0.5921 0.5126 0.4507 -0.0256 -0.0226 -0.0254 26  ARG A CZ  
203  N NH1 . ARG A 25  ? 0.5135 0.4319 0.3647 -0.0286 -0.0233 -0.0275 26  ARG A NH1 
204  N NH2 . ARG A 25  ? 0.4598 0.3652 0.3055 -0.0273 -0.0197 -0.0214 26  ARG A NH2 
205  N N   A SER A 26  ? 0.3954 0.3498 0.2956 0.0069  -0.0597 -0.0415 27  SER A N   
206  N N   B SER A 26  ? 0.3951 0.3496 0.2955 0.0069  -0.0597 -0.0415 27  SER A N   
207  N N   C SER A 26  ? 0.3997 0.3541 0.2999 0.0069  -0.0597 -0.0415 27  SER A N   
208  C CA  A SER A 26  ? 0.4226 0.3606 0.3060 0.0154  -0.0730 -0.0403 27  SER A CA  
209  C CA  B SER A 26  ? 0.4229 0.3605 0.3065 0.0156  -0.0728 -0.0402 27  SER A CA  
210  C CA  C SER A 26  ? 0.4295 0.3675 0.3129 0.0154  -0.0729 -0.0403 27  SER A CA  
211  C C   A SER A 26  ? 0.4857 0.4406 0.3853 0.0259  -0.0859 -0.0497 27  SER A C   
212  C C   B SER A 26  ? 0.4841 0.4389 0.3837 0.0258  -0.0857 -0.0496 27  SER A C   
213  C C   C SER A 26  ? 0.4878 0.4427 0.3874 0.0258  -0.0859 -0.0497 27  SER A C   
214  O O   A SER A 26  ? 0.5043 0.4544 0.3940 0.0321  -0.0984 -0.0513 27  SER A O   
215  O O   B SER A 26  ? 0.5015 0.4512 0.3908 0.0318  -0.0980 -0.0511 27  SER A O   
216  O O   C SER A 26  ? 0.5057 0.4556 0.3952 0.0321  -0.0983 -0.0512 27  SER A O   
217  C CB  A SER A 26  ? 0.4818 0.3948 0.3477 0.0179  -0.0728 -0.0335 27  SER A CB  
218  C CB  B SER A 26  ? 0.4830 0.3989 0.3533 0.0189  -0.0728 -0.0345 27  SER A CB  
219  C CB  C SER A 26  ? 0.4986 0.4122 0.3654 0.0181  -0.0728 -0.0337 27  SER A CB  
220  O OG  A SER A 26  ? 0.5284 0.4479 0.4089 0.0241  -0.0744 -0.0371 27  SER A OG  
221  O OG  B SER A 26  ? 0.5726 0.4701 0.4243 0.0100  -0.0631 -0.0270 27  SER A OG  
222  O OG  C SER A 26  ? 0.6326 0.5252 0.4791 0.0271  -0.0860 -0.0316 27  SER A OG  
223  N N   . ARG A 27  ? 0.4227 0.3985 0.3474 0.0275  -0.0830 -0.0569 28  ARG A N   
224  C CA  . ARG A 27  ? 0.4258 0.4228 0.3717 0.0368  -0.0934 -0.0685 28  ARG A CA  
225  C C   . ARG A 27  ? 0.4463 0.4716 0.4126 0.0299  -0.0894 -0.0784 28  ARG A C   
226  O O   . ARG A 27  ? 0.4457 0.4941 0.4341 0.0352  -0.0956 -0.0907 28  ARG A O   
227  C CB  . ARG A 27  ? 0.4368 0.4384 0.3969 0.0423  -0.0919 -0.0722 28  ARG A CB  
228  C CG  . ARG A 27  ? 0.5371 0.5084 0.4760 0.0483  -0.0952 -0.0633 28  ARG A CG  
229  C CD  . ARG A 27  ? 0.6088 0.5839 0.5608 0.0504  -0.0900 -0.0666 28  ARG A CD  
230  N NE  . ARG A 27  ? 0.7704 0.7658 0.7464 0.0611  -0.0985 -0.0794 28  ARG A NE  
231  C CZ  . ARG A 27  ? 0.9382 0.9515 0.9361 0.0602  -0.0919 -0.0878 28  ARG A CZ  
232  N NH1 . ARG A 27  ? 0.7860 0.8195 0.8075 0.0700  -0.0992 -0.1011 28  ARG A NH1 
233  N NH2 . ARG A 27  ? 0.7136 0.7261 0.7102 0.0493  -0.0779 -0.0839 28  ARG A NH2 
234  N N   . ASP A 28  ? 0.3786 0.4016 0.3377 0.0179  -0.0786 -0.0740 29  ASP A N   
235  C CA  . ASP A 28  ? 0.3733 0.4164 0.3463 0.0087  -0.0720 -0.0818 29  ASP A CA  
236  C C   . ASP A 28  ? 0.4132 0.4785 0.4106 0.0048  -0.0637 -0.0907 29  ASP A C   
237  O O   . ASP A 28  ? 0.4180 0.5057 0.4332 0.0013  -0.0630 -0.1027 29  ASP A O   
238  C CB  . ASP A 28  ? 0.4123 0.4659 0.3873 0.0124  -0.0844 -0.0901 29  ASP A CB  
239  C CG  . ASP A 28  ? 0.5368 0.6034 0.5179 0.0004  -0.0762 -0.0961 29  ASP A CG  
240  O OD1 . ASP A 28  ? 0.5343 0.5897 0.5060 -0.0095 -0.0631 -0.0890 29  ASP A OD1 
241  O OD2 . ASP A 28  ? 0.5858 0.6738 0.5817 0.0010  -0.0830 -0.1087 29  ASP A OD2 
242  N N   . ILE A 29  ? 0.3379 0.3970 0.3352 0.0045  -0.0568 -0.0857 30  ILE A N   
243  C CA  . ILE A 29  ? 0.3225 0.3994 0.3387 0.0002  -0.0485 -0.0936 30  ILE A CA  
244  C C   . ILE A 29  ? 0.3621 0.4371 0.3739 -0.0128 -0.0336 -0.0895 30  ILE A C   
245  O O   . ILE A 29  ? 0.3295 0.3871 0.3258 -0.0153 -0.0285 -0.0780 30  ILE A O   
246  C CB  . ILE A 29  ? 0.3595 0.4324 0.3787 0.0074  -0.0501 -0.0926 30  ILE A CB  
247  C CG1 . ILE A 29  ? 0.3841 0.4586 0.4093 0.0221  -0.0657 -0.0984 30  ILE A CG1 
248  C CG2 . ILE A 29  ? 0.3349 0.4238 0.3694 0.0004  -0.0389 -0.0998 30  ILE A CG2 
249  C CD1 . ILE A 29  ? 0.4287 0.4889 0.4490 0.0298  -0.0679 -0.0944 30  ILE A CD1 
250  N N   . LEU A 30  ? 0.3354 0.4282 0.3609 -0.0211 -0.0265 -0.0998 31  LEU A N   
251  C CA  . LEU A 30  ? 0.3344 0.4236 0.3545 -0.0336 -0.0123 -0.0972 31  LEU A CA  
252  C C   . LEU A 30  ? 0.3563 0.4277 0.3588 -0.0379 -0.0090 -0.0873 31  LEU A C   
253  O O   . LEU A 30  ? 0.3403 0.4021 0.3340 -0.0454 0.0015  -0.0818 31  LEU A O   
254  C CB  . LEU A 30  ? 0.3417 0.4263 0.3587 -0.0360 -0.0044 -0.0925 31  LEU A CB  
255  C CG  . LEU A 30  ? 0.4238 0.5279 0.4589 -0.0372 -0.0016 -0.1051 31  LEU A CG  
256  C CD1 . LEU A 30  ? 0.4383 0.5356 0.4655 -0.0424 0.0077  -0.1002 31  LEU A CD1 
257  C CD2 . LEU A 30  ? 0.4990 0.6220 0.5484 -0.0462 0.0042  -0.1193 31  LEU A CD2 
258  N N   . THR A 31  ? 0.3239 0.3908 0.3208 -0.0333 -0.0178 -0.0862 32  THR A N   
259  C CA  . THR A 31  ? 0.3251 0.3778 0.3076 -0.0382 -0.0140 -0.0801 32  THR A CA  
260  C C   . THR A 31  ? 0.3969 0.4592 0.3864 -0.0494 -0.0053 -0.0891 32  THR A C   
261  O O   . THR A 31  ? 0.3798 0.4625 0.3855 -0.0513 -0.0074 -0.1019 32  THR A O   
262  C CB  . THR A 31  ? 0.3851 0.4315 0.3587 -0.0319 -0.0252 -0.0785 32  THR A CB  
263  O OG1 . THR A 31  ? 0.4033 0.4681 0.3901 -0.0283 -0.0351 -0.0903 32  THR A OG1 
264  C CG2 . THR A 31  ? 0.3726 0.4035 0.3344 -0.0234 -0.0310 -0.0686 32  THR A CG2 
265  N N   . ASP A 32  ? 0.3730 0.4208 0.3511 -0.0568 0.0052  -0.0833 33  ASP A N   
266  C CA  . ASP A 32  ? 0.3801 0.4312 0.3608 -0.0689 0.0160  -0.0907 33  ASP A CA  
267  C C   . ASP A 32  ? 0.3950 0.4330 0.3646 -0.0746 0.0205  -0.0892 33  ASP A C   
268  O O   . ASP A 32  ? 0.3971 0.4309 0.3643 -0.0853 0.0313  -0.0934 33  ASP A O   
269  C CB  . ASP A 32  ? 0.4033 0.4471 0.3798 -0.0741 0.0270  -0.0866 33  ASP A CB  
270  C CG  . ASP A 32  ? 0.5076 0.5304 0.4687 -0.0693 0.0290  -0.0717 33  ASP A CG  
271  O OD1 . ASP A 32  ? 0.4337 0.4475 0.3882 -0.0630 0.0237  -0.0650 33  ASP A OD1 
272  O OD2 . ASP A 32  ? 0.6392 0.6554 0.5946 -0.0720 0.0357  -0.0676 33  ASP A OD2 
273  N N   . VAL A 33  ? 0.3293 0.3589 0.2904 -0.0683 0.0132  -0.0837 34  VAL A N   
274  C CA  . VAL A 33  ? 0.3294 0.3467 0.2798 -0.0736 0.0175  -0.0833 34  VAL A CA  
275  C C   . VAL A 33  ? 0.3726 0.3894 0.3169 -0.0677 0.0064  -0.0827 34  VAL A C   
276  O O   . VAL A 33  ? 0.3696 0.3855 0.3117 -0.0584 -0.0025 -0.0772 34  VAL A O   
277  C CB  . VAL A 33  ? 0.3764 0.3707 0.3138 -0.0747 0.0279  -0.0724 34  VAL A CB  
278  C CG1 . VAL A 33  ? 0.3598 0.3446 0.2903 -0.0649 0.0231  -0.0615 34  VAL A CG1 
279  C CG2 . VAL A 33  ? 0.3847 0.3659 0.3132 -0.0825 0.0361  -0.0748 34  VAL A CG2 
280  N N   A VAL A 34  ? 0.3397 0.3548 0.2789 -0.0738 0.0075  -0.0884 35  VAL A N   
281  N N   B VAL A 34  ? 0.3287 0.3438 0.2679 -0.0737 0.0073  -0.0884 35  VAL A N   
282  C CA  A VAL A 34  ? 0.3401 0.3502 0.2679 -0.0706 -0.0012 -0.0877 35  VAL A CA  
283  C CA  B VAL A 34  ? 0.3248 0.3348 0.2524 -0.0701 -0.0016 -0.0873 35  VAL A CA  
284  C C   A VAL A 34  ? 0.3927 0.3820 0.3064 -0.0754 0.0094  -0.0822 35  VAL A C   
285  C C   B VAL A 34  ? 0.3914 0.3814 0.3048 -0.0756 0.0085  -0.0830 35  VAL A C   
286  O O   A VAL A 34  ? 0.3888 0.3732 0.3034 -0.0838 0.0205  -0.0857 35  VAL A O   
287  O O   B VAL A 34  ? 0.3974 0.3843 0.3116 -0.0846 0.0185  -0.0879 35  VAL A O   
288  C CB  A VAL A 34  ? 0.4007 0.4285 0.3344 -0.0739 -0.0098 -0.1009 35  VAL A CB  
289  C CB  B VAL A 34  ? 0.3721 0.4002 0.3053 -0.0697 -0.0140 -0.0988 35  VAL A CB  
290  C CG1 A VAL A 34  ? 0.4155 0.4347 0.3320 -0.0711 -0.0191 -0.0994 35  VAL A CG1 
291  C CG1 B VAL A 34  ? 0.3729 0.4107 0.3123 -0.0817 -0.0076 -0.1112 35  VAL A CG1 
292  C CG2 A VAL A 34  ? 0.3931 0.4442 0.3448 -0.0680 -0.0201 -0.1084 35  VAL A CG2 
293  C CG2 B VAL A 34  ? 0.3809 0.3990 0.2965 -0.0638 -0.0251 -0.0946 35  VAL A CG2 
294  N N   . ILE A 35  ? 0.3455 0.3213 0.2463 -0.0704 0.0071  -0.0743 36  ILE A N   
295  C CA  . ILE A 35  ? 0.3642 0.3220 0.2530 -0.0740 0.0165  -0.0707 36  ILE A CA  
296  C C   . ILE A 35  ? 0.4294 0.3854 0.3054 -0.0770 0.0105  -0.0757 36  ILE A C   
297  O O   . ILE A 35  ? 0.4206 0.3765 0.2880 -0.0716 -0.0002 -0.0732 36  ILE A O   
298  C CB  . ILE A 35  ? 0.3931 0.3393 0.2776 -0.0676 0.0196  -0.0603 36  ILE A CB  
299  C CG1 . ILE A 35  ? 0.3761 0.3258 0.2720 -0.0634 0.0225  -0.0551 36  ILE A CG1 
300  C CG2 . ILE A 35  ? 0.4179 0.3484 0.2935 -0.0709 0.0297  -0.0590 36  ILE A CG2 
301  C CD1 . ILE A 35  ? 0.3916 0.3388 0.2931 -0.0686 0.0324  -0.0571 36  ILE A CD1 
302  N N   . VAL A 36  ? 0.3957 0.3479 0.2680 -0.0858 0.0175  -0.0826 37  VAL A N   
303  C CA  . VAL A 36  ? 0.4090 0.3594 0.2675 -0.0904 0.0127  -0.0886 37  VAL A CA  
304  C C   . VAL A 36  ? 0.4835 0.4139 0.3272 -0.0929 0.0221  -0.0846 37  VAL A C   
305  O O   . VAL A 36  ? 0.4667 0.3873 0.3136 -0.0961 0.0351  -0.0842 37  VAL A O   
306  C CB  . VAL A 36  ? 0.4612 0.4234 0.3261 -0.1000 0.0139  -0.1015 37  VAL A CB  
307  C CG1 . VAL A 36  ? 0.4780 0.4388 0.3271 -0.1051 0.0081  -0.1084 37  VAL A CG1 
308  C CG2 . VAL A 36  ? 0.4588 0.4442 0.3416 -0.0979 0.0053  -0.1076 37  VAL A CG2 
309  N N   . VAL A 37  ? 0.4523 0.3755 0.2787 -0.0910 0.0156  -0.0819 38  VAL A N   
310  C CA  . VAL A 37  ? 0.4702 0.3757 0.2814 -0.0942 0.0246  -0.0795 38  VAL A CA  
311  C C   . VAL A 37  ? 0.5651 0.4672 0.3557 -0.1001 0.0179  -0.0854 38  VAL A C   
312  O O   . VAL A 37  ? 0.5295 0.4290 0.3051 -0.0965 0.0061  -0.0822 38  VAL A O   
313  C CB  . VAL A 37  ? 0.5182 0.4162 0.3263 -0.0876 0.0250  -0.0700 38  VAL A CB  
314  C CG1 . VAL A 37  ? 0.5273 0.4105 0.3260 -0.0919 0.0378  -0.0698 38  VAL A CG1 
315  C CG2 . VAL A 37  ? 0.4934 0.3997 0.3218 -0.0806 0.0263  -0.0646 38  VAL A CG2 
316  N N   A SER A 38  ? 0.5673 0.4691 0.3564 -0.1091 0.0242  -0.0946 39  SER A N   
317  N N   B SER A 38  ? 0.5607 0.4606 0.3488 -0.1093 0.0255  -0.0941 39  SER A N   
318  C CA  A SER A 38  ? 0.5938 0.4945 0.3640 -0.1163 0.0180  -0.1024 39  SER A CA  
319  C CA  B SER A 38  ? 0.5856 0.4832 0.3544 -0.1170 0.0207  -0.1020 39  SER A CA  
320  C C   A SER A 38  ? 0.6093 0.5277 0.3813 -0.1117 -0.0014 -0.1055 39  SER A C   
321  C C   B SER A 38  ? 0.6171 0.5267 0.3793 -0.1121 0.0004  -0.1030 39  SER A C   
322  O O   A SER A 38  ? 0.5823 0.5186 0.3755 -0.1110 -0.0037 -0.1106 39  SER A O   
323  O O   B SER A 38  ? 0.6245 0.5241 0.3638 -0.1098 -0.0087 -0.0989 39  SER A O   
324  C CB  A SER A 38  ? 0.6829 0.5646 0.4266 -0.1189 0.0207  -0.0990 39  SER A CB  
325  C CB  B SER A 38  ? 0.6614 0.5392 0.4083 -0.1221 0.0295  -0.1008 39  SER A CB  
326  O OG  A SER A 38  ? 0.8786 0.7478 0.6252 -0.1220 0.0384  -0.0978 39  SER A OG  
327  O OG  B SER A 38  ? 0.7718 0.6419 0.5269 -0.1274 0.0471  -0.1046 39  SER A OG  
328  N N   A ARG A 39  ? 0.5689 0.4815 0.3186 -0.1082 -0.0151 -0.1027 40  ARG A N   
329  N N   B ARG A 39  ? 0.5383 0.4687 0.3216 -0.1099 -0.0062 -0.1082 40  ARG A N   
330  C CA  A ARG A 39  ? 0.5664 0.4937 0.3154 -0.1012 -0.0358 -0.1056 40  ARG A CA  
331  C CA  B ARG A 39  ? 0.5328 0.4818 0.3205 -0.1038 -0.0252 -0.1123 40  ARG A CA  
332  C C   A ARG A 39  ? 0.5878 0.5205 0.3488 -0.0884 -0.0447 -0.0974 40  ARG A C   
333  C C   B ARG A 39  ? 0.5570 0.5059 0.3466 -0.0907 -0.0359 -0.1023 40  ARG A C   
334  O O   A ARG A 39  ? 0.5798 0.5260 0.3446 -0.0804 -0.0621 -0.1003 40  ARG A O   
335  O O   B ARG A 39  ? 0.5475 0.5153 0.3515 -0.0839 -0.0487 -0.1061 40  ARG A O   
336  C CB  A ARG A 39  ? 0.5838 0.4981 0.2986 -0.1025 -0.0477 -0.1058 40  ARG A CB  
337  C CB  B ARG A 39  ? 0.5514 0.5019 0.3185 -0.1078 -0.0375 -0.1200 40  ARG A CB  
338  C CG  A ARG A 39  ? 0.6711 0.5888 0.3763 -0.1143 -0.0459 -0.1178 40  ARG A CG  
339  C CG  B ARG A 39  ? 0.6930 0.6520 0.4653 -0.1209 -0.0295 -0.1337 40  ARG A CG  
340  C CD  A ARG A 39  ? 0.6772 0.5854 0.3484 -0.1134 -0.0626 -0.1182 40  ARG A CD  
341  C CD  B ARG A 39  ? 0.7772 0.7473 0.5363 -0.1237 -0.0455 -0.1441 40  ARG A CD  
342  N NE  A ARG A 39  ? 0.7212 0.6282 0.3776 -0.1264 -0.0588 -0.1290 40  ARG A NE  
343  N NE  B ARG A 39  ? 0.8646 0.8417 0.6275 -0.1381 -0.0362 -0.1580 40  ARG A NE  
344  C CZ  A ARG A 39  ? 0.9051 0.8339 0.5694 -0.1299 -0.0688 -0.1422 40  ARG A CZ  
345  C CZ  B ARG A 39  ? 1.0196 0.9792 0.7617 -0.1486 -0.0260 -0.1608 40  ARG A CZ  
346  N NH1 A ARG A 39  ? 0.7585 0.6841 0.4071 -0.1428 -0.0640 -0.1521 40  ARG A NH1 
347  N NH1 B ARG A 39  ? 0.8267 0.7617 0.5430 -0.1470 -0.0230 -0.1508 40  ARG A NH1 
348  N NH2 A ARG A 39  ? 0.7330 0.6884 0.4223 -0.1211 -0.0831 -0.1470 40  ARG A NH2 
349  N NH2 B ARG A 39  ? 0.8656 0.8318 0.6124 -0.1619 -0.0175 -0.1744 40  ARG A NH2 
350  N N   A GLU A 40  ? 0.5193 0.4420 0.2864 -0.0859 -0.0334 -0.0882 41  GLU A N   
351  N N   B GLU A 40  ? 0.5111 0.4403 0.2890 -0.0875 -0.0297 -0.0909 41  GLU A N   
352  C CA  A GLU A 40  ? 0.5038 0.4296 0.2809 -0.0749 -0.0400 -0.0807 41  GLU A CA  
353  C CA  B GLU A 40  ? 0.5029 0.4294 0.2821 -0.0765 -0.0373 -0.0815 41  GLU A CA  
354  C C   A GLU A 40  ? 0.5191 0.4621 0.3274 -0.0733 -0.0333 -0.0824 41  GLU A C   
355  C C   B GLU A 40  ? 0.5181 0.4596 0.3270 -0.0730 -0.0316 -0.0811 41  GLU A C   
356  O O   A GLU A 40  ? 0.4938 0.4372 0.3122 -0.0803 -0.0190 -0.0848 41  GLU A O   
357  O O   B GLU A 40  ? 0.4881 0.4279 0.3073 -0.0784 -0.0167 -0.0810 41  GLU A O   
358  C CB  A GLU A 40  ? 0.5304 0.4336 0.2904 -0.0732 -0.0341 -0.0696 41  GLU A CB  
359  C CB  B GLU A 40  ? 0.5331 0.4352 0.2917 -0.0771 -0.0299 -0.0717 41  GLU A CB  
360  C CG  A GLU A 40  ? 0.7375 0.6196 0.4619 -0.0755 -0.0402 -0.0669 41  GLU A CG  
361  C CG  B GLU A 40  ? 0.7261 0.6097 0.4500 -0.0792 -0.0378 -0.0702 41  GLU A CG  
362  C CD  A GLU A 40  ? 1.2193 1.0915 0.9275 -0.0655 -0.0562 -0.0601 41  GLU A CD  
363  C CD  B GLU A 40  ? 1.1844 1.0582 0.8928 -0.0692 -0.0530 -0.0628 41  GLU A CD  
364  O OE1 A GLU A 40  ? 1.2409 1.1027 0.9485 -0.0618 -0.0523 -0.0521 41  GLU A OE1 
365  O OE1 B GLU A 40  ? 1.2154 1.0933 0.9144 -0.0637 -0.0708 -0.0659 41  GLU A OE1 
366  O OE2 A GLU A 40  ? 1.2351 1.1090 0.9305 -0.0612 -0.0732 -0.0633 41  GLU A OE2 
367  O OE2 B GLU A 40  ? 1.2031 1.0646 0.9085 -0.0666 -0.0476 -0.0545 41  GLU A OE2 
368  N N   . GLN A 41  ? 0.4656 0.4204 0.2868 -0.0638 -0.0435 -0.0810 42  GLN A N   
369  C CA  . GLN A 41  ? 0.4457 0.4163 0.2937 -0.0617 -0.0388 -0.0824 42  GLN A CA  
370  C C   . GLN A 41  ? 0.4750 0.4389 0.3246 -0.0532 -0.0398 -0.0726 42  GLN A C   
371  O O   . GLN A 41  ? 0.4831 0.4396 0.3201 -0.0457 -0.0515 -0.0685 42  GLN A O   
372  C CB  . GLN A 41  ? 0.4673 0.4632 0.3328 -0.0594 -0.0501 -0.0937 42  GLN A CB  
373  C CG  . GLN A 41  ? 0.6514 0.6583 0.5205 -0.0700 -0.0470 -0.1058 42  GLN A CG  
374  C CD  . GLN A 41  ? 0.8880 0.9243 0.7801 -0.0698 -0.0551 -0.1195 42  GLN A CD  
375  O OE1 . GLN A 41  ? 0.7865 0.8371 0.6944 -0.0611 -0.0631 -0.1208 42  GLN A OE1 
376  N NE2 . GLN A 41  ? 0.9204 0.9675 0.8159 -0.0801 -0.0524 -0.1315 42  GLN A NE2 
377  N N   . PHE A 42  ? 0.3926 0.3577 0.2560 -0.0544 -0.0281 -0.0689 43  PHE A N   
378  C CA  . PHE A 42  ? 0.3880 0.3487 0.2546 -0.0476 -0.0279 -0.0607 43  PHE A CA  
379  C C   . PHE A 42  ? 0.4222 0.3991 0.3115 -0.0467 -0.0246 -0.0636 43  PHE A C   
380  O O   . PHE A 42  ? 0.4162 0.3949 0.3130 -0.0530 -0.0134 -0.0652 43  PHE A O   
381  C CB  . PHE A 42  ? 0.4092 0.3530 0.2664 -0.0504 -0.0163 -0.0529 43  PHE A CB  
382  C CG  . PHE A 42  ? 0.4485 0.3751 0.2822 -0.0539 -0.0160 -0.0511 43  PHE A CG  
383  C CD1 . PHE A 42  ? 0.4834 0.4058 0.3103 -0.0618 -0.0093 -0.0557 43  PHE A CD1 
384  C CD2 . PHE A 42  ? 0.5000 0.4125 0.3162 -0.0503 -0.0217 -0.0454 43  PHE A CD2 
385  C CE1 . PHE A 42  ? 0.5209 0.4270 0.3244 -0.0662 -0.0081 -0.0549 43  PHE A CE1 
386  C CE2 . PHE A 42  ? 0.5539 0.4483 0.3447 -0.0553 -0.0204 -0.0441 43  PHE A CE2 
387  C CZ  . PHE A 42  ? 0.5266 0.4187 0.3114 -0.0633 -0.0136 -0.0490 43  PHE A CZ  
388  N N   . ARG A 43  ? 0.3816 0.3682 0.2800 -0.0390 -0.0336 -0.0644 44  ARG A N   
389  C CA  . ARG A 43  ? 0.3488 0.3510 0.2676 -0.0388 -0.0300 -0.0679 44  ARG A CA  
390  C C   . ARG A 43  ? 0.3790 0.3720 0.2972 -0.0369 -0.0228 -0.0587 44  ARG A C   
391  O O   . ARG A 43  ? 0.3761 0.3562 0.2827 -0.0325 -0.0257 -0.0518 44  ARG A O   
392  C CB  . ARG A 43  ? 0.3598 0.3788 0.2912 -0.0312 -0.0427 -0.0752 44  ARG A CB  
393  C CG  . ARG A 43  ? 0.4403 0.4746 0.3771 -0.0326 -0.0512 -0.0869 44  ARG A CG  
394  C CD  . ARG A 43  ? 0.5366 0.5967 0.4972 -0.0283 -0.0581 -0.0986 44  ARG A CD  
395  N NE  . ARG A 43  ? 0.6820 0.7506 0.6579 -0.0341 -0.0453 -0.1003 44  ARG A NE  
396  C CZ  . ARG A 43  ? 0.8422 0.9234 0.8300 -0.0450 -0.0350 -0.1091 44  ARG A CZ  
397  N NH1 . ARG A 43  ? 0.7425 0.8336 0.7329 -0.0513 -0.0364 -0.1189 44  ARG A NH1 
398  N NH2 . ARG A 43  ? 0.6059 0.6894 0.6017 -0.0502 -0.0234 -0.1088 44  ARG A NH2 
399  N N   . ALA A 44  ? 0.3282 0.3264 0.2568 -0.0410 -0.0133 -0.0590 45  ALA A N   
400  C CA  . ALA A 44  ? 0.3303 0.3215 0.2583 -0.0390 -0.0076 -0.0509 45  ALA A CA  
401  C C   . ALA A 44  ? 0.3503 0.3507 0.2898 -0.0419 -0.0013 -0.0530 45  ALA A C   
402  O O   . ALA A 44  ? 0.3273 0.3390 0.2756 -0.0465 0.0002  -0.0612 45  ALA A O   
403  C CB  . ALA A 44  ? 0.3527 0.3288 0.2699 -0.0415 0.0002  -0.0444 45  ALA A CB  
404  N N   . HIS A 45  ? 0.3128 0.3086 0.2515 -0.0398 0.0025  -0.0463 46  HIS A N   
405  C CA  . HIS A 45  ? 0.3013 0.3013 0.2453 -0.0429 0.0089  -0.0464 46  HIS A CA  
406  C C   . HIS A 45  ? 0.3467 0.3332 0.2823 -0.0461 0.0175  -0.0408 46  HIS A C   
407  O O   . HIS A 45  ? 0.3315 0.3089 0.2614 -0.0424 0.0178  -0.0344 46  HIS A O   
408  C CB  . HIS A 45  ? 0.2920 0.2949 0.2388 -0.0380 0.0064  -0.0429 46  HIS A CB  
409  C CG  . HIS A 45  ? 0.3259 0.3384 0.2800 -0.0332 -0.0021 -0.0480 46  HIS A CG  
410  N ND1 . HIS A 45  ? 0.3536 0.3590 0.3017 -0.0273 -0.0092 -0.0448 46  HIS A ND1 
411  C CD2 . HIS A 45  ? 0.3322 0.3592 0.2984 -0.0333 -0.0043 -0.0568 46  HIS A CD2 
412  C CE1 . HIS A 45  ? 0.3498 0.3636 0.3055 -0.0226 -0.0165 -0.0506 46  HIS A CE1 
413  N NE2 . HIS A 45  ? 0.3372 0.3662 0.3060 -0.0256 -0.0141 -0.0586 46  HIS A NE2 
414  N N   . LYS A 46  ? 0.3332 0.3180 0.2682 -0.0529 0.0247  -0.0440 47  LYS A N   
415  C CA  . LYS A 46  ? 0.3316 0.2999 0.2567 -0.0551 0.0327  -0.0387 47  LYS A CA  
416  C C   . LYS A 46  ? 0.3601 0.3221 0.2812 -0.0487 0.0323  -0.0297 47  LYS A C   
417  O O   . LYS A 46  ? 0.3314 0.2827 0.2477 -0.0449 0.0338  -0.0246 47  LYS A O   
418  C CB  . LYS A 46  ? 0.3625 0.3274 0.2848 -0.0643 0.0412  -0.0431 47  LYS A CB  
419  C CG  . LYS A 46  ? 0.3644 0.3330 0.2896 -0.0719 0.0437  -0.0523 47  LYS A CG  
420  C CD  . LYS A 46  ? 0.3549 0.3212 0.2779 -0.0831 0.0536  -0.0582 47  LYS A CD  
421  C CE  . LYS A 46  ? 0.4218 0.3959 0.3504 -0.0917 0.0558  -0.0697 47  LYS A CE  
422  N NZ  . LYS A 46  ? 0.4266 0.4012 0.3547 -0.1047 0.0666  -0.0778 47  LYS A NZ  
423  N N   . THR A 47  ? 0.3187 0.2889 0.2430 -0.0473 0.0298  -0.0290 48  THR A N   
424  C CA  . THR A 47  ? 0.3164 0.2827 0.2368 -0.0418 0.0286  -0.0216 48  THR A CA  
425  C C   . THR A 47  ? 0.3309 0.2984 0.2544 -0.0351 0.0240  -0.0183 48  THR A C   
426  O O   . THR A 47  ? 0.3381 0.2999 0.2589 -0.0305 0.0244  -0.0132 48  THR A O   
427  C CB  . THR A 47  ? 0.4079 0.3831 0.3301 -0.0430 0.0274  -0.0228 48  THR A CB  
428  O OG1 . THR A 47  ? 0.4099 0.3988 0.3427 -0.0421 0.0223  -0.0286 48  THR A OG1 
429  C CG2 . THR A 47  ? 0.4266 0.3969 0.3419 -0.0510 0.0346  -0.0251 48  THR A CG2 
430  N N   . VAL A 48  ? 0.2878 0.2623 0.2163 -0.0346 0.0196  -0.0218 49  VAL A N   
431  C CA  . VAL A 48  ? 0.2845 0.2583 0.2136 -0.0306 0.0169  -0.0196 49  VAL A CA  
432  C C   . VAL A 48  ? 0.3251 0.2894 0.2505 -0.0306 0.0210  -0.0187 49  VAL A C   
433  O O   . VAL A 48  ? 0.2988 0.2614 0.2254 -0.0272 0.0222  -0.0162 49  VAL A O   
434  C CB  . VAL A 48  ? 0.3047 0.2827 0.2350 -0.0303 0.0113  -0.0229 49  VAL A CB  
435  C CG1 . VAL A 48  ? 0.3183 0.2912 0.2448 -0.0288 0.0108  -0.0209 49  VAL A CG1 
436  C CG2 . VAL A 48  ? 0.2978 0.2847 0.2332 -0.0291 0.0078  -0.0245 49  VAL A CG2 
437  N N   . LEU A 49  ? 0.3029 0.2625 0.2251 -0.0348 0.0235  -0.0220 50  LEU A N   
438  C CA  . LEU A 49  ? 0.3086 0.2580 0.2267 -0.0356 0.0284  -0.0221 50  LEU A CA  
439  C C   . LEU A 49  ? 0.3394 0.2810 0.2572 -0.0316 0.0328  -0.0178 50  LEU A C   
440  O O   . LEU A 49  ? 0.3319 0.2697 0.2512 -0.0279 0.0350  -0.0170 50  LEU A O   
441  C CB  . LEU A 49  ? 0.3093 0.2551 0.2238 -0.0419 0.0309  -0.0274 50  LEU A CB  
442  C CG  . LEU A 49  ? 0.3477 0.3010 0.2619 -0.0445 0.0247  -0.0326 50  LEU A CG  
443  C CD1 . LEU A 49  ? 0.3532 0.3056 0.2654 -0.0512 0.0272  -0.0391 50  LEU A CD1 
444  C CD2 . LEU A 49  ? 0.3647 0.3146 0.2733 -0.0426 0.0219  -0.0315 50  LEU A CD2 
445  N N   . MET A 50  ? 0.3087 0.2475 0.2237 -0.0320 0.0338  -0.0155 51  MET A N   
446  C CA  . MET A 50  ? 0.3308 0.2588 0.2416 -0.0269 0.0361  -0.0103 51  MET A CA  
447  C C   . MET A 50  ? 0.3804 0.3161 0.2973 -0.0187 0.0313  -0.0069 51  MET A C   
448  O O   . MET A 50  ? 0.3778 0.3083 0.2964 -0.0120 0.0319  -0.0050 51  MET A O   
449  C CB  . MET A 50  ? 0.3567 0.2779 0.2588 -0.0304 0.0381  -0.0082 51  MET A CB  
450  C CG  . MET A 50  ? 0.3900 0.3034 0.2866 -0.0397 0.0446  -0.0129 51  MET A CG  
451  S SD  . MET A 50  ? 0.4508 0.3623 0.3391 -0.0467 0.0476  -0.0127 51  MET A SD  
452  C CE  . MET A 50  ? 0.4243 0.3092 0.2949 -0.0422 0.0513  -0.0040 51  MET A CE  
453  N N   . ALA A 51  ? 0.3316 0.2809 0.2534 -0.0193 0.0265  -0.0076 52  ALA A N   
454  C CA  . ALA A 51  ? 0.3231 0.2824 0.2515 -0.0136 0.0221  -0.0060 52  ALA A CA  
455  C C   . ALA A 51  ? 0.3455 0.3088 0.2819 -0.0113 0.0236  -0.0091 52  ALA A C   
456  O O   . ALA A 51  ? 0.3652 0.3366 0.3091 -0.0061 0.0214  -0.0092 52  ALA A O   
457  C CB  . ALA A 51  ? 0.3237 0.2944 0.2543 -0.0163 0.0182  -0.0072 52  ALA A CB  
458  N N   . CYS A 52  ? 0.3011 0.2596 0.2355 -0.0161 0.0274  -0.0125 53  CYS A N   
459  C CA  . CYS A 52  ? 0.3020 0.2624 0.2406 -0.0168 0.0305  -0.0163 53  CYS A CA  
460  C C   . CYS A 52  ? 0.3578 0.3093 0.2967 -0.0154 0.0365  -0.0185 53  CYS A C   
461  O O   . CYS A 52  ? 0.3370 0.2919 0.2813 -0.0155 0.0402  -0.0227 53  CYS A O   
462  C CB  . CYS A 52  ? 0.3074 0.2674 0.2399 -0.0236 0.0299  -0.0188 53  CYS A CB  
463  S SG  . CYS A 52  ? 0.3473 0.3158 0.2803 -0.0245 0.0237  -0.0176 53  CYS A SG  
464  N N   . SER A 53  ? 0.3249 0.2646 0.2572 -0.0159 0.0386  -0.0170 54  SER A N   
465  C CA  . SER A 53  ? 0.3163 0.2445 0.2466 -0.0162 0.0452  -0.0199 54  SER A CA  
466  C C   . SER A 53  ? 0.3732 0.2884 0.3004 -0.0107 0.0468  -0.0165 54  SER A C   
467  O O   . SER A 53  ? 0.3567 0.2652 0.2755 -0.0135 0.0458  -0.0132 54  SER A O   
468  C CB  . SER A 53  ? 0.3396 0.2628 0.2609 -0.0255 0.0474  -0.0232 54  SER A CB  
469  O OG  . SER A 53  ? 0.3822 0.2921 0.2981 -0.0282 0.0536  -0.0259 54  SER A OG  
470  N N   . GLY A 54  ? 0.3474 0.2573 0.2803 -0.0035 0.0499  -0.0180 55  GLY A N   
471  C CA  . GLY A 54  ? 0.3504 0.2424 0.2776 0.0031  0.0515  -0.0145 55  GLY A CA  
472  C C   . GLY A 54  ? 0.4048 0.2790 0.3193 -0.0054 0.0582  -0.0157 55  GLY A C   
473  O O   . GLY A 54  ? 0.4151 0.2729 0.3182 -0.0053 0.0593  -0.0113 55  GLY A O   
474  N N   . LEU A 55  ? 0.3768 0.2540 0.2912 -0.0142 0.0629  -0.0221 56  LEU A N   
475  C CA  . LEU A 55  ? 0.4033 0.2673 0.3068 -0.0238 0.0688  -0.0253 56  LEU A CA  
476  C C   . LEU A 55  ? 0.4235 0.2902 0.3202 -0.0311 0.0659  -0.0231 56  LEU A C   
477  O O   . LEU A 55  ? 0.4081 0.2596 0.2953 -0.0349 0.0703  -0.0223 56  LEU A O   
478  C CB  . LEU A 55  ? 0.4051 0.2733 0.3087 -0.0314 0.0728  -0.0329 56  LEU A CB  
479  C CG  . LEU A 55  ? 0.4725 0.3286 0.3660 -0.0415 0.0790  -0.0380 56  LEU A CG  
480  C CD1 . LEU A 55  ? 0.4931 0.3272 0.3830 -0.0383 0.0876  -0.0392 56  LEU A CD1 
481  C CD2 . LEU A 55  ? 0.4445 0.3078 0.3353 -0.0495 0.0797  -0.0448 56  LEU A CD2 
482  N N   . PHE A 56  ? 0.3567 0.2415 0.2580 -0.0330 0.0592  -0.0228 57  PHE A N   
483  C CA  . PHE A 56  ? 0.3497 0.2400 0.2478 -0.0392 0.0566  -0.0227 57  PHE A CA  
484  C C   . PHE A 56  ? 0.4044 0.2872 0.2977 -0.0357 0.0562  -0.0165 57  PHE A C   
485  O O   . PHE A 56  ? 0.3882 0.2660 0.2746 -0.0428 0.0593  -0.0174 57  PHE A O   
486  C CB  . PHE A 56  ? 0.3522 0.2615 0.2563 -0.0407 0.0494  -0.0244 57  PHE A CB  
487  C CG  . PHE A 56  ? 0.3656 0.2781 0.2683 -0.0462 0.0493  -0.0305 57  PHE A CG  
488  C CD1 . PHE A 56  ? 0.3973 0.3062 0.2954 -0.0544 0.0525  -0.0364 57  PHE A CD1 
489  C CD2 . PHE A 56  ? 0.3829 0.3017 0.2869 -0.0442 0.0457  -0.0308 57  PHE A CD2 
490  C CE1 . PHE A 56  ? 0.4103 0.3221 0.3050 -0.0591 0.0510  -0.0422 57  PHE A CE1 
491  C CE2 . PHE A 56  ? 0.4178 0.3367 0.3158 -0.0494 0.0447  -0.0356 57  PHE A CE2 
492  C CZ  . PHE A 56  ? 0.3896 0.3055 0.2830 -0.0562 0.0466  -0.0411 57  PHE A CZ  
493  N N   . TYR A 57  ? 0.3673 0.2490 0.2632 -0.0253 0.0528  -0.0109 58  TYR A N   
494  C CA  . TYR A 57  ? 0.3907 0.2622 0.2779 -0.0208 0.0513  -0.0041 58  TYR A CA  
495  C C   . TYR A 57  ? 0.4571 0.3020 0.3294 -0.0239 0.0590  -0.0028 58  TYR A C   
496  O O   . TYR A 57  ? 0.4364 0.2714 0.2962 -0.0298 0.0617  -0.0006 58  TYR A O   
497  C CB  . TYR A 57  ? 0.4118 0.2879 0.3057 -0.0079 0.0450  0.0003  58  TYR A CB  
498  C CG  . TYR A 57  ? 0.4697 0.3322 0.3515 -0.0014 0.0418  0.0079  58  TYR A CG  
499  C CD1 . TYR A 57  ? 0.4947 0.3612 0.3690 -0.0053 0.0388  0.0111  58  TYR A CD1 
500  C CD2 . TYR A 57  ? 0.5309 0.3748 0.4072 0.0091  0.0416  0.0117  58  TYR A CD2 
501  C CE1 . TYR A 57  ? 0.5385 0.3900 0.3973 -0.0001 0.0357  0.0185  58  TYR A CE1 
502  C CE2 . TYR A 57  ? 0.5818 0.4100 0.4431 0.0162  0.0371  0.0197  58  TYR A CE2 
503  C CZ  . TYR A 57  ? 0.6666 0.4984 0.5179 0.0111  0.0341  0.0234  58  TYR A CZ  
504  O OH  . TYR A 57  ? 0.7579 0.5719 0.5906 0.0176  0.0295  0.0316  58  TYR A OH  
505  N N   A SER A 58  ? 0.4298 0.2621 0.3024 -0.0209 0.0638  -0.0050 59  SER A N   
506  N N   B SER A 58  ? 0.4284 0.2608 0.3011 -0.0209 0.0637  -0.0050 59  SER A N   
507  C CA  A SER A 58  ? 0.4564 0.2600 0.3141 -0.0238 0.0722  -0.0045 59  SER A CA  
508  C CA  B SER A 58  ? 0.4545 0.2586 0.3127 -0.0238 0.0721  -0.0046 59  SER A CA  
509  C C   A SER A 58  ? 0.5185 0.3201 0.3697 -0.0401 0.0796  -0.0107 59  SER A C   
510  C C   B SER A 58  ? 0.5157 0.3178 0.3671 -0.0400 0.0794  -0.0106 59  SER A C   
511  O O   A SER A 58  ? 0.5520 0.3335 0.3873 -0.0465 0.0857  -0.0090 59  SER A O   
512  O O   B SER A 58  ? 0.5459 0.3285 0.3815 -0.0462 0.0852  -0.0086 59  SER A O   
513  C CB  A SER A 58  ? 0.4971 0.2913 0.3600 -0.0171 0.0758  -0.0075 59  SER A CB  
514  C CB  B SER A 58  ? 0.4932 0.2889 0.3569 -0.0180 0.0761  -0.0083 59  SER A CB  
515  O OG  A SER A 58  ? 0.5408 0.3364 0.4106 -0.0015 0.0692  -0.0029 59  SER A OG  
516  O OG  B SER A 58  ? 0.5779 0.3434 0.4266 -0.0208 0.0848  -0.0083 59  SER A OG  
517  N N   . ILE A 59  ? 0.4542 0.2769 0.3168 -0.0471 0.0786  -0.0184 60  ILE A N   
518  C CA  . ILE A 59  ? 0.4493 0.2766 0.3100 -0.0617 0.0836  -0.0265 60  ILE A CA  
519  C C   . ILE A 59  ? 0.4828 0.3160 0.3401 -0.0681 0.0832  -0.0259 60  ILE A C   
520  O O   . ILE A 59  ? 0.5001 0.3204 0.3470 -0.0788 0.0916  -0.0291 60  ILE A O   
521  C CB  . ILE A 59  ? 0.4591 0.3087 0.3318 -0.0654 0.0794  -0.0343 60  ILE A CB  
522  C CG1 . ILE A 59  ? 0.4687 0.3102 0.3416 -0.0633 0.0829  -0.0373 60  ILE A CG1 
523  C CG2 . ILE A 59  ? 0.4412 0.3020 0.3153 -0.0787 0.0812  -0.0435 60  ILE A CG2 
524  C CD1 . ILE A 59  ? 0.4809 0.3425 0.3615 -0.0648 0.0769  -0.0425 60  ILE A CD1 
525  N N   . PHE A 60  ? 0.4082 0.2599 0.2736 -0.0627 0.0747  -0.0227 61  PHE A N   
526  C CA  . PHE A 60  ? 0.4174 0.2775 0.2815 -0.0698 0.0751  -0.0243 61  PHE A CA  
527  C C   . PHE A 60  ? 0.4845 0.3245 0.3317 -0.0687 0.0784  -0.0164 61  PHE A C   
528  O O   . PHE A 60  ? 0.5019 0.3464 0.3455 -0.0766 0.0811  -0.0186 61  PHE A O   
529  C CB  . PHE A 60  ? 0.4068 0.2948 0.2859 -0.0668 0.0658  -0.0265 61  PHE A CB  
530  C CG  . PHE A 60  ? 0.4091 0.3129 0.2997 -0.0688 0.0622  -0.0342 61  PHE A CG  
531  C CD1 . PHE A 60  ? 0.4552 0.3643 0.3481 -0.0796 0.0663  -0.0442 61  PHE A CD1 
532  C CD2 . PHE A 60  ? 0.4135 0.3265 0.3112 -0.0606 0.0547  -0.0320 61  PHE A CD2 
533  C CE1 . PHE A 60  ? 0.4537 0.3766 0.3547 -0.0806 0.0611  -0.0510 61  PHE A CE1 
534  C CE2 . PHE A 60  ? 0.4383 0.3622 0.3415 -0.0627 0.0508  -0.0382 61  PHE A CE2 
535  C CZ  . PHE A 60  ? 0.4218 0.3505 0.3262 -0.0718 0.0531  -0.0472 61  PHE A CZ  
536  N N   . THR A 61  ? 0.4691 0.2864 0.3051 -0.0593 0.0784  -0.0080 62  THR A N   
537  C CA  . THR A 61  ? 0.4941 0.2857 0.3081 -0.0583 0.0813  0.0002  62  THR A CA  
538  C C   . THR A 61  ? 0.6030 0.3641 0.3989 -0.0677 0.0936  -0.0015 62  THR A C   
539  O O   . THR A 61  ? 0.6121 0.3453 0.3843 -0.0703 0.0986  0.0045  62  THR A O   
540  C CB  . THR A 61  ? 0.5765 0.3605 0.3869 -0.0414 0.0723  0.0104  62  THR A CB  
541  O OG1 . THR A 61  ? 0.5461 0.3247 0.3640 -0.0322 0.0714  0.0102  62  THR A OG1 
542  C CG2 . THR A 61  ? 0.5262 0.3377 0.3500 -0.0353 0.0619  0.0119  62  THR A CG2 
543  N N   . ASP A 62  ? 0.5589 0.3234 0.3636 -0.0741 0.0989  -0.0101 63  ASP A N   
544  C CA  . ASP A 62  ? 0.5930 0.3299 0.3816 -0.0854 0.1118  -0.0139 63  ASP A CA  
545  C C   . ASP A 62  ? 0.6536 0.3957 0.4372 -0.1036 0.1202  -0.0214 63  ASP A C   
546  O O   . ASP A 62  ? 0.5997 0.3741 0.4024 -0.1096 0.1174  -0.0304 63  ASP A O   
547  C CB  . ASP A 62  ? 0.6111 0.3521 0.4108 -0.0877 0.1149  -0.0221 63  ASP A CB  
548  C CG  . ASP A 62  ? 0.7764 0.4906 0.5604 -0.1015 0.1291  -0.0279 63  ASP A CG  
549  O OD1 . ASP A 62  ? 0.8554 0.5350 0.6224 -0.0962 0.1340  -0.0219 63  ASP A OD1 
550  O OD2 . ASP A 62  ? 0.7632 0.4904 0.5517 -0.1177 0.1354  -0.0389 63  ASP A OD2 
551  N N   . GLN A 63  ? 0.6909 0.4003 0.4485 -0.1125 0.1310  -0.0184 64  GLN A N   
552  C CA  . GLN A 63  ? 0.7097 0.4206 0.4598 -0.1315 0.1417  -0.0262 64  GLN A CA  
553  C C   . GLN A 63  ? 0.7399 0.4751 0.5086 -0.1473 0.1483  -0.0433 64  GLN A C   
554  O O   . GLN A 63  ? 0.7614 0.5160 0.5371 -0.1600 0.1527  -0.0526 64  GLN A O   
555  C CB  . GLN A 63  ? 0.7830 0.4472 0.4968 -0.1392 0.1539  -0.0196 64  GLN A CB  
556  C CG  . GLN A 63  ? 1.0075 0.6530 0.7009 -0.1270 0.1466  -0.0044 64  GLN A CG  
557  N N   . LEU A 64  ? 0.6443 0.3797 0.4213 -0.1466 0.1489  -0.0484 65  LEU A N   
558  C CA  . LEU A 64  ? 0.6184 0.3793 0.4135 -0.1600 0.1526  -0.0650 65  LEU A CA  
559  C C   . LEU A 64  ? 0.6428 0.4435 0.4654 -0.1503 0.1378  -0.0687 65  LEU A C   
560  O O   . LEU A 64  ? 0.6482 0.4799 0.4885 -0.1581 0.1357  -0.0807 65  LEU A O   
561  C CB  . LEU A 64  ? 0.6391 0.3777 0.4258 -0.1668 0.1620  -0.0702 65  LEU A CB  
562  C CG  . LEU A 64  ? 0.7409 0.4449 0.5034 -0.1842 0.1801  -0.0738 65  LEU A CG  
563  C CD1 . LEU A 64  ? 0.7598 0.4432 0.5162 -0.1893 0.1883  -0.0792 65  LEU A CD1 
564  C CD2 . LEU A 64  ? 0.7967 0.5218 0.5665 -0.2048 0.1888  -0.0886 65  LEU A CD2 
565  N N   . LYS A 65  ? 0.5583 0.3571 0.3840 -0.1337 0.1280  -0.0595 66  LYS A N   
566  C CA  . LYS A 65  ? 0.5204 0.3506 0.3671 -0.1254 0.1153  -0.0624 66  LYS A CA  
567  C C   . LYS A 65  ? 0.5739 0.4296 0.4329 -0.1197 0.1054  -0.0604 66  LYS A C   
568  O O   . LYS A 65  ? 0.5479 0.4314 0.4238 -0.1180 0.0967  -0.0667 66  LYS A O   
569  C CB  . LYS A 65  ? 0.5275 0.3481 0.3736 -0.1119 0.1101  -0.0551 66  LYS A CB  
570  C CG  . LYS A 65  ? 0.5269 0.3265 0.3646 -0.1174 0.1193  -0.0596 66  LYS A CG  
571  C CD  . LYS A 65  ? 0.5039 0.2988 0.3443 -0.1041 0.1144  -0.0544 66  LYS A CD  
572  C CE  . LYS A 65  ? 0.5713 0.3397 0.4013 -0.1075 0.1247  -0.0575 66  LYS A CE  
573  N NZ  . LYS A 65  ? 0.6271 0.3600 0.4397 -0.1030 0.1318  -0.0490 66  LYS A NZ  
574  N N   . CYS A 66  ? 0.5734 0.4183 0.4221 -0.1172 0.1068  -0.0522 67  CYS A N   
575  C CA  . CYS A 66  ? 0.5731 0.4396 0.4315 -0.1127 0.0990  -0.0507 67  CYS A CA  
576  C C   . CYS A 66  ? 0.6081 0.5041 0.4837 -0.1228 0.0990  -0.0648 67  CYS A C   
577  O O   . CYS A 66  ? 0.5977 0.5170 0.4874 -0.1168 0.0899  -0.0660 67  CYS A O   
578  C CB  . CYS A 66  ? 0.6145 0.4615 0.4549 -0.1119 0.1028  -0.0413 67  CYS A CB  
579  S SG  . CYS A 66  ? 0.7110 0.5375 0.5320 -0.1319 0.1201  -0.0474 67  CYS A SG  
580  N N   . ASN A 67  ? 0.5567 0.4514 0.4316 -0.1379 0.1093  -0.0764 68  ASN A N   
581  C CA  . ASN A 67  ? 0.5519 0.4757 0.4448 -0.1489 0.1106  -0.0927 68  ASN A CA  
582  C C   . ASN A 67  ? 0.5673 0.5143 0.4779 -0.1481 0.1026  -0.1031 68  ASN A C   
583  O O   . ASN A 67  ? 0.5409 0.5153 0.4691 -0.1552 0.1013  -0.1178 68  ASN A O   
584  C CB  . ASN A 67  ? 0.5866 0.4975 0.4685 -0.1681 0.1277  -0.1011 68  ASN A CB  
585  C CG  . ASN A 67  ? 0.7703 0.6615 0.6337 -0.1704 0.1348  -0.0925 68  ASN A CG  
586  O OD1 . ASN A 67  ? 0.8043 0.6627 0.6432 -0.1794 0.1475  -0.0883 68  ASN A OD1 
587  N ND2 . ASN A 67  ? 0.6306 0.5383 0.5023 -0.1618 0.1266  -0.0889 68  ASN A ND2 
588  N N   . LEU A 68  ? 0.5215 0.4581 0.4271 -0.1395 0.0971  -0.0964 69  LEU A N   
589  C CA  . LEU A 68  ? 0.5013 0.4566 0.4187 -0.1389 0.0889  -0.1052 69  LEU A CA  
590  C C   . LEU A 68  ? 0.5197 0.4995 0.4517 -0.1265 0.0731  -0.1042 69  LEU A C   
591  O O   . LEU A 68  ? 0.5036 0.4779 0.4325 -0.1153 0.0680  -0.0926 69  LEU A O   
592  C CB  . LEU A 68  ? 0.5117 0.4458 0.4168 -0.1356 0.0902  -0.0994 69  LEU A CB  
593  C CG  . LEU A 68  ? 0.5926 0.4985 0.4820 -0.1468 0.1057  -0.1008 69  LEU A CG  
594  C CD1 . LEU A 68  ? 0.6018 0.4878 0.4811 -0.1406 0.1060  -0.0947 69  LEU A CD1 
595  C CD2 . LEU A 68  ? 0.6130 0.5311 0.5087 -0.1644 0.1132  -0.1182 69  LEU A CD2 
596  N N   A SER A 69  ? 0.4686 0.4746 0.4158 -0.1281 0.0649  -0.1168 70  SER A N   
597  N N   B SER A 69  ? 0.4662 0.4721 0.4133 -0.1282 0.0649  -0.1169 70  SER A N   
598  C CA  A SER A 69  ? 0.4506 0.4769 0.4095 -0.1157 0.0488  -0.1165 70  SER A CA  
599  C CA  B SER A 69  ? 0.4473 0.4743 0.4066 -0.1161 0.0489  -0.1171 70  SER A CA  
600  C C   A SER A 69  ? 0.4646 0.4856 0.4158 -0.1085 0.0393  -0.1123 70  SER A C   
601  C C   B SER A 69  ? 0.4636 0.4850 0.4150 -0.1087 0.0393  -0.1126 70  SER A C   
602  O O   A SER A 69  ? 0.4336 0.4623 0.3873 -0.0974 0.0265  -0.1086 70  SER A O   
603  O O   B SER A 69  ? 0.4326 0.4619 0.3867 -0.0976 0.0264  -0.1091 70  SER A O   
604  C CB  A SER A 69  ? 0.4994 0.5576 0.4796 -0.1195 0.0436  -0.1328 70  SER A CB  
605  C CB  B SER A 69  ? 0.4913 0.5501 0.4716 -0.1206 0.0440  -0.1341 70  SER A CB  
606  O OG  A SER A 69  ? 0.6030 0.6716 0.5877 -0.1293 0.0447  -0.1463 70  SER A OG  
607  O OG  B SER A 69  ? 0.5684 0.6340 0.5565 -0.1270 0.0528  -0.1385 70  SER A OG  
608  N N   . VAL A 70  ? 0.4331 0.4390 0.3731 -0.1157 0.0465  -0.1135 71  VAL A N   
609  C CA  . VAL A 70  ? 0.4354 0.4336 0.3652 -0.1116 0.0405  -0.1106 71  VAL A CA  
610  C C   . VAL A 70  ? 0.4625 0.4318 0.3769 -0.1130 0.0521  -0.1018 71  VAL A C   
611  O O   . VAL A 70  ? 0.4518 0.4084 0.3620 -0.1226 0.0649  -0.1048 71  VAL A O   
612  C CB  . VAL A 70  ? 0.5003 0.5139 0.4339 -0.1194 0.0359  -0.1252 71  VAL A CB  
613  C CG1 . VAL A 70  ? 0.5083 0.5111 0.4271 -0.1165 0.0307  -0.1221 71  VAL A CG1 
614  C CG2 . VAL A 70  ? 0.4927 0.5372 0.4442 -0.1160 0.0228  -0.1355 71  VAL A CG2 
615  N N   . ILE A 71  ? 0.3820 0.3403 0.2879 -0.1036 0.0480  -0.0918 72  ILE A N   
616  C CA  . ILE A 71  ? 0.3851 0.3193 0.2794 -0.1026 0.0572  -0.0849 72  ILE A CA  
617  C C   . ILE A 71  ? 0.4366 0.3681 0.3223 -0.1022 0.0533  -0.0869 72  ILE A C   
618  O O   . ILE A 71  ? 0.4394 0.3782 0.3237 -0.0955 0.0429  -0.0837 72  ILE A O   
619  C CB  . ILE A 71  ? 0.4149 0.3394 0.3086 -0.0925 0.0582  -0.0723 72  ILE A CB  
620  C CG1 . ILE A 71  ? 0.4235 0.3480 0.3215 -0.0939 0.0625  -0.0701 72  ILE A CG1 
621  C CG2 . ILE A 71  ? 0.4374 0.3408 0.3225 -0.0891 0.0656  -0.0668 72  ILE A CG2 
622  C CD1 . ILE A 71  ? 0.4950 0.4022 0.3859 -0.1037 0.0758  -0.0732 72  ILE A CD1 
623  N N   . ASN A 72  ? 0.4182 0.3368 0.2961 -0.1100 0.0624  -0.0921 73  ASN A N   
624  C CA  . ASN A 72  ? 0.4309 0.3448 0.2982 -0.1115 0.0607  -0.0949 73  ASN A CA  
625  C C   . ASN A 72  ? 0.4680 0.3625 0.3290 -0.1061 0.0686  -0.0875 73  ASN A C   
626  O O   . ASN A 72  ? 0.4511 0.3295 0.3115 -0.1075 0.0799  -0.0867 73  ASN A O   
627  C CB  . ASN A 72  ? 0.4822 0.3956 0.3452 -0.1242 0.0659  -0.1074 73  ASN A CB  
628  C CG  . ASN A 72  ? 0.7093 0.6453 0.5816 -0.1304 0.0586  -0.1177 73  ASN A CG  
629  O OD1 . ASN A 72  ? 0.5815 0.5352 0.4565 -0.1259 0.0445  -0.1195 73  ASN A OD1 
630  N ND2 . ASN A 72  ? 0.6636 0.5988 0.5408 -0.1409 0.0683  -0.1257 73  ASN A ND2 
631  N N   . LEU A 73  ? 0.4104 0.3056 0.2662 -0.1002 0.0631  -0.0830 74  LEU A N   
632  C CA  . LEU A 73  ? 0.4157 0.2967 0.2683 -0.0957 0.0708  -0.0783 74  LEU A CA  
633  C C   . LEU A 73  ? 0.4703 0.3396 0.3122 -0.1033 0.0791  -0.0860 74  LEU A C   
634  O O   . LEU A 73  ? 0.4801 0.3538 0.3142 -0.1118 0.0760  -0.0939 74  LEU A O   
635  C CB  . LEU A 73  ? 0.4052 0.2909 0.2562 -0.0885 0.0641  -0.0717 74  LEU A CB  
636  C CG  . LEU A 73  ? 0.4341 0.3305 0.2950 -0.0804 0.0562  -0.0641 74  LEU A CG  
637  C CD1 . LEU A 73  ? 0.4442 0.3398 0.3032 -0.0747 0.0545  -0.0584 74  LEU A CD1 
638  C CD2 . LEU A 73  ? 0.4300 0.3241 0.3017 -0.0771 0.0612  -0.0606 74  LEU A CD2 
639  N N   . ASP A 74  ? 0.4371 0.2929 0.2796 -0.0999 0.0891  -0.0846 75  ASP A N   
640  C CA  . ASP A 74  ? 0.4642 0.3073 0.2978 -0.1063 0.0991  -0.0923 75  ASP A CA  
641  C C   . ASP A 74  ? 0.5193 0.3678 0.3379 -0.1126 0.0933  -0.0964 75  ASP A C   
642  O O   . ASP A 74  ? 0.5057 0.3609 0.3216 -0.1083 0.0857  -0.0909 75  ASP A O   
643  C CB  . ASP A 74  ? 0.4877 0.3203 0.3281 -0.0984 0.1084  -0.0897 75  ASP A CB  
644  C CG  . ASP A 74  ? 0.6212 0.4395 0.4559 -0.1035 0.1210  -0.0985 75  ASP A CG  
645  O OD1 . ASP A 74  ? 0.6359 0.4553 0.4587 -0.1106 0.1219  -0.1041 75  ASP A OD1 
646  O OD2 . ASP A 74  ? 0.6365 0.4408 0.4770 -0.1000 0.1300  -0.0998 75  ASP A OD2 
647  N N   . PRO A 75  ? 0.5419 0.3859 0.3486 -0.1232 0.0965  -0.1060 76  PRO A N   
648  C CA  . PRO A 75  ? 0.5484 0.3953 0.3364 -0.1292 0.0896  -0.1094 76  PRO A CA  
649  C C   . PRO A 75  ? 0.5977 0.4367 0.3757 -0.1280 0.0940  -0.1072 76  PRO A C   
650  O O   . PRO A 75  ? 0.6226 0.4620 0.3824 -0.1315 0.0865  -0.1069 76  PRO A O   
651  C CB  . PRO A 75  ? 0.5920 0.4342 0.3701 -0.1413 0.0946  -0.1213 76  PRO A CB  
652  C CG  . PRO A 75  ? 0.6591 0.4899 0.4491 -0.1416 0.1086  -0.1241 76  PRO A CG  
653  C CD  . PRO A 75  ? 0.5785 0.4130 0.3857 -0.1308 0.1063  -0.1143 76  PRO A CD  
654  N N   . GLU A 76  ? 0.5532 0.3850 0.3423 -0.1232 0.1059  -0.1060 77  GLU A N   
655  C CA  . GLU A 76  ? 0.5702 0.3973 0.3539 -0.1229 0.1125  -0.1059 77  GLU A CA  
656  C C   . GLU A 76  ? 0.5590 0.3945 0.3450 -0.1160 0.1031  -0.0963 77  GLU A C   
657  O O   . GLU A 76  ? 0.5536 0.3858 0.3303 -0.1182 0.1064  -0.0961 77  GLU A O   
658  C CB  . GLU A 76  ? 0.6024 0.4230 0.4028 -0.1179 0.1270  -0.1092 77  GLU A CB  
659  C CG  . GLU A 76  ? 0.8746 0.6891 0.6684 -0.1227 0.1390  -0.1162 77  GLU A CG  
660  C CD  . GLU A 76  ? 1.2732 1.0762 1.0509 -0.1345 0.1481  -0.1274 77  GLU A CD  
661  O OE1 . GLU A 76  ? 1.2854 1.0809 1.0718 -0.1340 0.1562  -0.1331 77  GLU A OE1 
662  O OE2 . GLU A 76  ? 1.2221 1.0217 0.9766 -0.1446 0.1473  -0.1306 77  GLU A OE2 
663  N N   . ILE A 77  ? 0.4896 0.3350 0.2873 -0.1088 0.0929  -0.0893 78  ILE A N   
664  C CA  . ILE A 77  ? 0.4830 0.3359 0.2841 -0.1021 0.0845  -0.0808 78  ILE A CA  
665  C C   . ILE A 77  ? 0.5508 0.4021 0.3298 -0.1063 0.0738  -0.0791 78  ILE A C   
666  O O   . ILE A 77  ? 0.5414 0.3950 0.3110 -0.1093 0.0646  -0.0812 78  ILE A O   
667  C CB  . ILE A 77  ? 0.5013 0.3645 0.3215 -0.0933 0.0782  -0.0747 78  ILE A CB  
668  C CG1 . ILE A 77  ? 0.5048 0.3648 0.3425 -0.0879 0.0884  -0.0751 78  ILE A CG1 
669  C CG2 . ILE A 77  ? 0.4657 0.3363 0.2886 -0.0871 0.0697  -0.0668 78  ILE A CG2 
670  C CD1 . ILE A 77  ? 0.5653 0.4235 0.4114 -0.0835 0.0977  -0.0758 78  ILE A CD1 
671  N N   . ASN A 78  ? 0.5520 0.3987 0.3225 -0.1063 0.0750  -0.0756 79  ASN A N   
672  C CA  . ASN A 78  ? 0.5670 0.4059 0.3121 -0.1096 0.0659  -0.0725 79  ASN A CA  
673  C C   . ASN A 78  ? 0.5594 0.4065 0.3101 -0.1010 0.0511  -0.0647 79  ASN A C   
674  O O   . ASN A 78  ? 0.5242 0.3780 0.2919 -0.0946 0.0523  -0.0601 79  ASN A O   
675  C CB  . ASN A 78  ? 0.6060 0.4340 0.3390 -0.1150 0.0763  -0.0729 79  ASN A CB  
676  C CG  . ASN A 78  ? 0.8061 0.6201 0.5086 -0.1188 0.0684  -0.0683 79  ASN A CG  
677  O OD1 . ASN A 78  ? 0.6708 0.4836 0.3734 -0.1151 0.0650  -0.0621 79  ASN A OD1 
678  N ND2 . ASN A 78  ? 0.7163 0.5177 0.3902 -0.1264 0.0650  -0.0713 79  ASN A ND2 
679  N N   . PRO A 79  ? 0.5289 0.3762 0.2659 -0.1003 0.0366  -0.0641 80  PRO A N   
680  C CA  . PRO A 79  ? 0.5158 0.3714 0.2599 -0.0912 0.0226  -0.0582 80  PRO A CA  
681  C C   . PRO A 79  ? 0.5593 0.4063 0.2963 -0.0879 0.0218  -0.0508 80  PRO A C   
682  O O   . PRO A 79  ? 0.5406 0.3970 0.2943 -0.0803 0.0174  -0.0465 80  PRO A O   
683  C CB  . PRO A 79  ? 0.5667 0.4220 0.2936 -0.0914 0.0076  -0.0608 80  PRO A CB  
684  C CG  . PRO A 79  ? 0.6294 0.4831 0.3499 -0.1006 0.0144  -0.0693 80  PRO A CG  
685  C CD  . PRO A 79  ? 0.5814 0.4227 0.2970 -0.1071 0.0317  -0.0699 80  PRO A CD  
686  N N   . GLU A 80  ? 0.5344 0.3625 0.2456 -0.0949 0.0273  -0.0500 81  GLU A N   
687  C CA  . GLU A 80  ? 0.5419 0.3593 0.2442 -0.0941 0.0285  -0.0440 81  GLU A CA  
688  C C   . GLU A 80  ? 0.5459 0.3754 0.2757 -0.0924 0.0403  -0.0442 81  GLU A C   
689  O O   . GLU A 80  ? 0.5097 0.3430 0.2485 -0.0868 0.0366  -0.0394 81  GLU A O   
690  C CB  . GLU A 80  ? 0.6000 0.3925 0.2660 -0.1043 0.0337  -0.0439 81  GLU A CB  
691  C CG  . GLU A 80  ? 0.6949 0.4734 0.3484 -0.1043 0.0341  -0.0377 81  GLU A CG  
692  C CD  . GLU A 80  ? 1.0506 0.8018 0.6676 -0.1164 0.0429  -0.0375 81  GLU A CD  
693  O OE1 . GLU A 80  ? 1.0741 0.8060 0.6685 -0.1159 0.0373  -0.0310 81  GLU A OE1 
694  O OE2 . GLU A 80  ? 0.9562 0.7039 0.5662 -0.1268 0.0561  -0.0442 81  GLU A OE2 
695  N N   . GLY A 81  ? 0.5163 0.3517 0.2594 -0.0963 0.0534  -0.0502 82  GLY A N   
696  C CA  . GLY A 81  ? 0.4973 0.3456 0.2676 -0.0929 0.0630  -0.0514 82  GLY A CA  
697  C C   . GLY A 81  ? 0.4852 0.3490 0.2788 -0.0826 0.0546  -0.0472 82  GLY A C   
698  O O   . GLY A 81  ? 0.4426 0.3144 0.2506 -0.0780 0.0550  -0.0443 82  GLY A O   
699  N N   . PHE A 82  ? 0.4386 0.3071 0.2349 -0.0801 0.0471  -0.0478 83  PHE A N   
700  C CA  . PHE A 82  ? 0.4073 0.2896 0.2232 -0.0721 0.0401  -0.0448 83  PHE A CA  
701  C C   . PHE A 82  ? 0.4262 0.3095 0.2387 -0.0674 0.0296  -0.0393 83  PHE A C   
702  O O   . PHE A 82  ? 0.4148 0.3076 0.2434 -0.0618 0.0286  -0.0363 83  PHE A O   
703  C CB  . PHE A 82  ? 0.4229 0.3104 0.2416 -0.0726 0.0354  -0.0484 83  PHE A CB  
704  C CG  . PHE A 82  ? 0.4190 0.3198 0.2574 -0.0664 0.0313  -0.0463 83  PHE A CG  
705  C CD1 . PHE A 82  ? 0.4556 0.3601 0.3103 -0.0639 0.0391  -0.0456 83  PHE A CD1 
706  C CD2 . PHE A 82  ? 0.4280 0.3365 0.2679 -0.0625 0.0195  -0.0450 83  PHE A CD2 
707  C CE1 . PHE A 82  ? 0.4569 0.3709 0.3255 -0.0592 0.0360  -0.0431 83  PHE A CE1 
708  C CE2 . PHE A 82  ? 0.4463 0.3670 0.3037 -0.0581 0.0173  -0.0439 83  PHE A CE2 
709  C CZ  . PHE A 82  ? 0.4237 0.3461 0.2936 -0.0571 0.0259  -0.0425 83  PHE A CZ  
710  N N   . CYS A 83  ? 0.4379 0.3102 0.2284 -0.0690 0.0212  -0.0382 84  CYS A N   
711  C CA  . CYS A 83  ? 0.4766 0.3456 0.2611 -0.0636 0.0108  -0.0332 84  CYS A CA  
712  C C   . CYS A 83  ? 0.4791 0.3449 0.2670 -0.0639 0.0177  -0.0299 84  CYS A C   
713  O O   . CYS A 83  ? 0.4467 0.3197 0.2462 -0.0580 0.0131  -0.0270 84  CYS A O   
714  C CB  . CYS A 83  ? 0.5422 0.3942 0.2973 -0.0650 0.0013  -0.0322 84  CYS A CB  
715  S SG  . CYS A 83  ? 0.6196 0.4650 0.3667 -0.0557 -0.0138 -0.0265 84  CYS A SG  
716  N N   . ILE A 84  ? 0.4497 0.3060 0.2281 -0.0717 0.0294  -0.0317 85  ILE A N   
717  C CA  . ILE A 84  ? 0.4318 0.2868 0.2139 -0.0745 0.0378  -0.0311 85  ILE A CA  
718  C C   . ILE A 84  ? 0.4296 0.3057 0.2428 -0.0684 0.0402  -0.0316 85  ILE A C   
719  O O   . ILE A 84  ? 0.3996 0.2804 0.2205 -0.0658 0.0390  -0.0294 85  ILE A O   
720  C CB  . ILE A 84  ? 0.4706 0.3149 0.2396 -0.0853 0.0515  -0.0359 85  ILE A CB  
721  C CG1 . ILE A 84  ? 0.4999 0.3175 0.2304 -0.0925 0.0489  -0.0337 85  ILE A CG1 
722  C CG2 . ILE A 84  ? 0.4650 0.3179 0.2495 -0.0882 0.0629  -0.0391 85  ILE A CG2 
723  C CD1 . ILE A 84  ? 0.5951 0.4016 0.3091 -0.1038 0.0613  -0.0393 85  ILE A CD1 
724  N N   . LEU A 85  ? 0.3831 0.2699 0.2117 -0.0661 0.0432  -0.0343 86  LEU A N   
725  C CA  . LEU A 85  ? 0.3667 0.2700 0.2207 -0.0596 0.0446  -0.0340 86  LEU A CA  
726  C C   . LEU A 85  ? 0.3814 0.2927 0.2434 -0.0530 0.0345  -0.0300 86  LEU A C   
727  O O   . LEU A 85  ? 0.3546 0.2759 0.2305 -0.0488 0.0341  -0.0283 86  LEU A O   
728  C CB  . LEU A 85  ? 0.3735 0.2808 0.2382 -0.0589 0.0514  -0.0378 86  LEU A CB  
729  C CG  . LEU A 85  ? 0.4408 0.3451 0.3053 -0.0640 0.0635  -0.0436 86  LEU A CG  
730  C CD1 . LEU A 85  ? 0.4556 0.3601 0.3280 -0.0627 0.0693  -0.0476 86  LEU A CD1 
731  C CD2 . LEU A 85  ? 0.4464 0.3619 0.3265 -0.0620 0.0680  -0.0452 86  LEU A CD2 
732  N N   . LEU A 86  ? 0.3634 0.2717 0.2172 -0.0523 0.0264  -0.0296 87  LEU A N   
733  C CA  . LEU A 86  ? 0.3453 0.2624 0.2075 -0.0467 0.0174  -0.0277 87  LEU A CA  
734  C C   . LEU A 86  ? 0.3891 0.3036 0.2479 -0.0445 0.0132  -0.0246 87  LEU A C   
735  O O   . LEU A 86  ? 0.3637 0.2881 0.2354 -0.0404 0.0113  -0.0233 87  LEU A O   
736  C CB  . LEU A 86  ? 0.3483 0.2647 0.2034 -0.0467 0.0093  -0.0301 87  LEU A CB  
737  C CG  . LEU A 86  ? 0.3927 0.3217 0.2601 -0.0414 0.0011  -0.0308 87  LEU A CG  
738  C CD1 . LEU A 86  ? 0.3812 0.3214 0.2662 -0.0408 0.0069  -0.0311 87  LEU A CD1 
739  C CD2 . LEU A 86  ? 0.4262 0.3578 0.2887 -0.0412 -0.0078 -0.0354 87  LEU A CD2 
740  N N   . ASP A 87  ? 0.3705 0.2693 0.2096 -0.0479 0.0126  -0.0236 88  ASP A N   
741  C CA  . ASP A 87  ? 0.3760 0.2675 0.2087 -0.0472 0.0105  -0.0209 88  ASP A CA  
742  C C   . ASP A 87  ? 0.3876 0.2891 0.2355 -0.0486 0.0187  -0.0216 88  ASP A C   
743  O O   . ASP A 87  ? 0.3864 0.2931 0.2417 -0.0455 0.0157  -0.0203 88  ASP A O   
744  C CB  . ASP A 87  ? 0.4309 0.2992 0.2356 -0.0529 0.0114  -0.0196 88  ASP A CB  
745  C CG  . ASP A 87  ? 0.6133 0.4693 0.3993 -0.0493 -0.0007 -0.0180 88  ASP A CG  
746  O OD1 . ASP A 87  ? 0.6079 0.4758 0.4060 -0.0417 -0.0104 -0.0187 88  ASP A OD1 
747  O OD2 . ASP A 87  ? 0.6405 0.4753 0.3994 -0.0542 -0.0006 -0.0167 88  ASP A OD2 
748  N N   . PHE A 88  ? 0.3643 0.2694 0.2174 -0.0530 0.0286  -0.0244 89  PHE A N   
749  C CA  . PHE A 88  ? 0.3346 0.2530 0.2051 -0.0531 0.0352  -0.0266 89  PHE A CA  
750  C C   . PHE A 88  ? 0.3380 0.2726 0.2274 -0.0455 0.0301  -0.0248 89  PHE A C   
751  O O   . PHE A 88  ? 0.3091 0.2523 0.2077 -0.0440 0.0295  -0.0248 89  PHE A O   
752  C CB  . PHE A 88  ? 0.3410 0.2628 0.2173 -0.0567 0.0454  -0.0314 89  PHE A CB  
753  C CG  . PHE A 88  ? 0.3355 0.2752 0.2340 -0.0537 0.0494  -0.0344 89  PHE A CG  
754  C CD1 . PHE A 88  ? 0.3593 0.3039 0.2615 -0.0578 0.0533  -0.0375 89  PHE A CD1 
755  C CD2 . PHE A 88  ? 0.3573 0.3084 0.2721 -0.0463 0.0481  -0.0341 89  PHE A CD2 
756  C CE1 . PHE A 88  ? 0.3353 0.2995 0.2594 -0.0541 0.0549  -0.0412 89  PHE A CE1 
757  C CE2 . PHE A 88  ? 0.3784 0.3457 0.3123 -0.0415 0.0492  -0.0364 89  PHE A CE2 
758  C CZ  . PHE A 88  ? 0.3515 0.3271 0.2911 -0.0452 0.0520  -0.0404 89  PHE A CZ  
759  N N   . MET A 89  ? 0.2984 0.2363 0.1922 -0.0419 0.0274  -0.0240 90  MET A N   
760  C CA  . MET A 89  ? 0.2860 0.2358 0.1935 -0.0363 0.0239  -0.0222 90  MET A CA  
761  C C   . MET A 89  ? 0.3276 0.2808 0.2360 -0.0343 0.0176  -0.0207 90  MET A C   
762  O O   . MET A 89  ? 0.3182 0.2813 0.2365 -0.0317 0.0169  -0.0200 90  MET A O   
763  C CB  . MET A 89  ? 0.2992 0.2480 0.2065 -0.0352 0.0222  -0.0222 90  MET A CB  
764  C CG  . MET A 89  ? 0.3281 0.2730 0.2359 -0.0365 0.0289  -0.0240 90  MET A CG  
765  S SD  . MET A 89  ? 0.3746 0.3178 0.2820 -0.0370 0.0278  -0.0248 90  MET A SD  
766  C CE  . MET A 89  ? 0.3820 0.3157 0.2857 -0.0399 0.0366  -0.0281 90  MET A CE  
767  N N   . TYR A 90  ? 0.3008 0.2450 0.1979 -0.0349 0.0123  -0.0205 91  TYR A N   
768  C CA  . TYR A 90  ? 0.3052 0.2509 0.2031 -0.0318 0.0060  -0.0201 91  TYR A CA  
769  C C   . TYR A 90  ? 0.3609 0.2995 0.2527 -0.0339 0.0072  -0.0197 91  TYR A C   
770  O O   . TYR A 90  ? 0.3537 0.2922 0.2463 -0.0313 0.0026  -0.0198 91  TYR A O   
771  C CB  . TYR A 90  ? 0.3243 0.2645 0.2149 -0.0292 -0.0019 -0.0210 91  TYR A CB  
772  C CG  . TYR A 90  ? 0.3288 0.2811 0.2304 -0.0274 -0.0039 -0.0234 91  TYR A CG  
773  C CD1 . TYR A 90  ? 0.3460 0.2982 0.2466 -0.0301 -0.0008 -0.0246 91  TYR A CD1 
774  C CD2 . TYR A 90  ? 0.3390 0.3019 0.2512 -0.0241 -0.0076 -0.0255 91  TYR A CD2 
775  C CE1 . TYR A 90  ? 0.3403 0.3019 0.2497 -0.0304 -0.0011 -0.0277 91  TYR A CE1 
776  C CE2 . TYR A 90  ? 0.3390 0.3126 0.2603 -0.0245 -0.0078 -0.0291 91  TYR A CE2 
777  C CZ  . TYR A 90  ? 0.3622 0.3347 0.2818 -0.0281 -0.0043 -0.0300 91  TYR A CZ  
778  O OH  . TYR A 90  ? 0.3373 0.3190 0.2647 -0.0302 -0.0034 -0.0346 91  TYR A OH  
779  N N   . THR A 91  ? 0.3265 0.2582 0.2116 -0.0395 0.0141  -0.0204 92  THR A N   
780  C CA  . THR A 91  ? 0.3497 0.2721 0.2265 -0.0439 0.0168  -0.0210 92  THR A CA  
781  C C   . THR A 91  ? 0.3696 0.3003 0.2546 -0.0497 0.0260  -0.0246 92  THR A C   
782  O O   . THR A 91  ? 0.3603 0.2862 0.2412 -0.0543 0.0289  -0.0265 92  THR A O   
783  C CB  . THR A 91  ? 0.4024 0.3000 0.2538 -0.0479 0.0165  -0.0195 92  THR A CB  
784  O OG1 . THR A 91  ? 0.4056 0.2993 0.2508 -0.0539 0.0239  -0.0210 92  THR A OG1 
785  C CG2 . THR A 91  ? 0.4234 0.3113 0.2646 -0.0413 0.0055  -0.0168 92  THR A CG2 
786  N N   A SER A 92  ? 0.3095 0.2518 0.2058 -0.0496 0.0306  -0.0267 93  SER A N   
787  N N   B SER A 92  ? 0.3136 0.2555 0.2095 -0.0497 0.0307  -0.0267 93  SER A N   
788  C CA  A SER A 92  ? 0.2994 0.2528 0.2067 -0.0540 0.0391  -0.0322 93  SER A CA  
789  C CA  B SER A 92  ? 0.3055 0.2586 0.2126 -0.0539 0.0391  -0.0321 93  SER A CA  
790  C C   A SER A 92  ? 0.3484 0.2872 0.2407 -0.0638 0.0481  -0.0356 93  SER A C   
791  C C   B SER A 92  ? 0.3665 0.3050 0.2584 -0.0642 0.0481  -0.0356 93  SER A C   
792  O O   A SER A 92  ? 0.3431 0.2915 0.2450 -0.0686 0.0567  -0.0420 93  SER A O   
793  O O   B SER A 92  ? 0.3640 0.3117 0.2648 -0.0698 0.0567  -0.0422 93  SER A O   
794  C CB  A SER A 92  ? 0.3087 0.2749 0.2273 -0.0547 0.0390  -0.0350 93  SER A CB  
795  C CB  B SER A 92  ? 0.3234 0.2916 0.2441 -0.0534 0.0382  -0.0346 93  SER A CB  
796  O OG  A SER A 92  ? 0.2892 0.2659 0.2171 -0.0473 0.0312  -0.0319 93  SER A OG  
797  O OG  B SER A 92  ? 0.3767 0.3348 0.2870 -0.0609 0.0415  -0.0368 93  SER A OG  
798  N N   A ARG A 93  ? 0.3418 0.2575 0.2099 -0.0667 0.0461  -0.0319 94  ARG A N   
799  N N   B ARG A 93  ? 0.3501 0.2660 0.2184 -0.0667 0.0462  -0.0319 94  ARG A N   
800  C CA  A ARG A 93  ? 0.3580 0.2546 0.2052 -0.0772 0.0547  -0.0342 94  ARG A CA  
801  C CA  B ARG A 93  ? 0.3711 0.2666 0.2172 -0.0771 0.0543  -0.0339 94  ARG A CA  
802  C C   A ARG A 93  ? 0.4173 0.3080 0.2566 -0.0780 0.0567  -0.0343 94  ARG A C   
803  C C   B ARG A 93  ? 0.4240 0.3134 0.2618 -0.0783 0.0566  -0.0341 94  ARG A C   
804  O O   A ARG A 93  ? 0.3941 0.2802 0.2276 -0.0719 0.0481  -0.0298 94  ARG A O   
805  O O   B ARG A 93  ? 0.4095 0.2937 0.2409 -0.0723 0.0481  -0.0297 94  ARG A O   
806  C CB  A ARG A 93  ? 0.4180 0.2877 0.2379 -0.0804 0.0511  -0.0298 94  ARG A CB  
807  C CB  B ARG A 93  ? 0.4159 0.2855 0.2359 -0.0789 0.0493  -0.0290 94  ARG A CB  
808  C CG  A ARG A 93  ? 0.4753 0.3465 0.2998 -0.0817 0.0512  -0.0309 94  ARG A CG  
809  C CG  B ARG A 93  ? 0.5176 0.3904 0.3441 -0.0781 0.0473  -0.0292 94  ARG A CG  
810  C CD  A ARG A 93  ? 0.5841 0.4298 0.3856 -0.0786 0.0429  -0.0249 94  ARG A CD  
811  C CD  B ARG A 93  ? 0.5716 0.4340 0.3882 -0.0907 0.0588  -0.0342 94  ARG A CD  
812  N NE  A ARG A 93  ? 0.7480 0.5617 0.5158 -0.0864 0.0466  -0.0227 94  ARG A NE  
813  N NE  B ARG A 93  ? 0.6045 0.4703 0.4278 -0.0908 0.0575  -0.0355 94  ARG A NE  
814  C CZ  A ARG A 93  ? 0.9253 0.7188 0.6742 -0.0980 0.0563  -0.0248 94  ARG A CZ  
815  C CZ  B ARG A 93  ? 0.7682 0.6080 0.5694 -0.0943 0.0571  -0.0331 94  ARG A CZ  
816  N NH1 A ARG A 93  ? 0.7695 0.5740 0.5326 -0.1031 0.0629  -0.0300 94  ARG A NH1 
817  N NH1 B ARG A 93  ? 0.6263 0.4710 0.4357 -0.0948 0.0569  -0.0355 94  ARG A NH1 
818  N NH2 A ARG A 93  ? 0.7626 0.5237 0.4766 -0.1053 0.0596  -0.0220 94  ARG A NH2 
819  N NH2 B ARG A 93  ? 0.5755 0.3826 0.3446 -0.0972 0.0567  -0.0283 94  ARG A NH2 
820  N N   . LEU A 94  ? 0.3852 0.2764 0.2241 -0.0865 0.0688  -0.0408 95  LEU A N   
821  C CA  . LEU A 94  ? 0.3819 0.2677 0.2135 -0.0891 0.0732  -0.0428 95  LEU A CA  
822  C C   . LEU A 94  ? 0.4755 0.3353 0.2752 -0.1014 0.0807  -0.0439 95  LEU A C   
823  O O   . LEU A 94  ? 0.4709 0.3282 0.2675 -0.1120 0.0923  -0.0498 95  LEU A O   
824  C CB  . LEU A 94  ? 0.3711 0.2794 0.2296 -0.0880 0.0817  -0.0507 95  LEU A CB  
825  C CG  . LEU A 94  ? 0.4151 0.3203 0.2709 -0.0890 0.0868  -0.0539 95  LEU A CG  
826  C CD1 . LEU A 94  ? 0.3950 0.2993 0.2512 -0.0795 0.0757  -0.0474 95  LEU A CD1 
827  C CD2 . LEU A 94  ? 0.4360 0.3616 0.3183 -0.0881 0.0965  -0.0634 95  LEU A CD2 
828  N N   . ASN A 95  ? 0.4792 0.3197 0.2544 -0.1010 0.0743  -0.0389 96  ASN A N   
829  C CA  . ASN A 95  ? 0.5131 0.3243 0.2514 -0.1124 0.0799  -0.0386 96  ASN A CA  
830  C C   . ASN A 95  ? 0.5781 0.3917 0.3158 -0.1208 0.0926  -0.0464 96  ASN A C   
831  O O   . ASN A 95  ? 0.5807 0.3864 0.3055 -0.1202 0.0893  -0.0452 96  ASN A O   
832  C CB  . ASN A 95  ? 0.5758 0.3655 0.2869 -0.1068 0.0650  -0.0300 96  ASN A CB  
833  C CG  . ASN A 95  ? 0.8380 0.5933 0.5056 -0.1174 0.0683  -0.0280 96  ASN A CG  
834  O OD1 . ASN A 95  ? 0.7038 0.4454 0.3565 -0.1302 0.0817  -0.0315 96  ASN A OD1 
835  N ND2 . ASN A 95  ? 0.7781 0.5185 0.4231 -0.1130 0.0564  -0.0231 96  ASN A ND2 
836  N N   . LEU A 96  ? 0.5333 0.3607 0.2885 -0.1279 0.1070  -0.0555 97  LEU A N   
837  C CA  . LEU A 96  ? 0.5474 0.3814 0.3086 -0.1352 0.1210  -0.0654 97  LEU A CA  
838  C C   . LEU A 96  ? 0.6177 0.4256 0.3440 -0.1528 0.1340  -0.0692 97  LEU A C   
839  O O   . LEU A 96  ? 0.6209 0.4202 0.3378 -0.1622 0.1412  -0.0711 97  LEU A O   
840  C CB  . LEU A 96  ? 0.5319 0.3980 0.3342 -0.1316 0.1281  -0.0745 97  LEU A CB  
841  C CG  . LEU A 96  ? 0.5998 0.4822 0.4229 -0.1318 0.1387  -0.0851 97  LEU A CG  
842  C CD1 . LEU A 96  ? 0.6037 0.4853 0.4286 -0.1217 0.1301  -0.0805 97  LEU A CD1 
843  C CD2 . LEU A 96  ? 0.5761 0.4903 0.4395 -0.1258 0.1422  -0.0934 97  LEU A CD2 
844  N N   . ARG A 97  ? 0.5922 0.3843 0.2953 -0.1581 0.1367  -0.0700 98  ARG A N   
845  C CA  . ARG A 97  ? 0.6405 0.4032 0.3033 -0.1756 0.1487  -0.0728 98  ARG A CA  
846  C C   . ARG A 97  ? 0.6520 0.4205 0.3181 -0.1830 0.1621  -0.0835 98  ARG A C   
847  O O   . ARG A 97  ? 0.6097 0.3961 0.2991 -0.1729 0.1575  -0.0852 98  ARG A O   
848  C CB  . ARG A 97  ? 0.6988 0.4272 0.3168 -0.1748 0.1347  -0.0606 98  ARG A CB  
849  C CG  . ARG A 97  ? 0.8042 0.5231 0.4163 -0.1665 0.1209  -0.0501 98  ARG A CG  
850  C CD  . ARG A 97  ? 1.0608 0.7481 0.6321 -0.1623 0.1047  -0.0388 98  ARG A CD  
851  N NE  . ARG A 97  ? 1.3389 0.9877 0.8599 -0.1778 0.1130  -0.0380 98  ARG A NE  
852  C CZ  . ARG A 97  ? 1.6173 1.2370 1.1088 -0.1871 0.1184  -0.0347 98  ARG A CZ  
853  N NH1 . ARG A 97  ? 1.4916 1.0734 0.9336 -0.2022 0.1267  -0.0338 98  ARG A NH1 
854  N NH2 . ARG A 97  ? 1.4825 1.1091 0.9919 -0.1824 0.1165  -0.0328 98  ARG A NH2 
855  N N   . GLU A 98  ? 0.6520 0.4039 0.2940 -0.2014 0.1798  -0.0916 99  GLU A N   
856  C CA  . GLU A 98  ? 0.6487 0.4045 0.2916 -0.2103 0.1948  -0.1034 99  GLU A CA  
857  C C   . GLU A 98  ? 0.7242 0.4709 0.3521 -0.2039 0.1836  -0.0981 99  GLU A C   
858  O O   . GLU A 98  ? 0.7068 0.4708 0.3576 -0.2004 0.1886  -0.1061 99  GLU A O   
859  C CB  . GLU A 98  ? 0.7107 0.4415 0.3176 -0.2336 0.2146  -0.1111 99  GLU A CB  
860  C CG  . GLU A 98  ? 0.8446 0.5790 0.4514 -0.2448 0.2324  -0.1252 99  GLU A CG  
861  C CD  . GLU A 98  ? 1.2830 0.9899 0.8493 -0.2697 0.2530  -0.1329 99  GLU A CD  
862  O OE1 . GLU A 98  ? 1.2747 0.9426 0.7888 -0.2779 0.2479  -0.1221 99  GLU A OE1 
863  O OE2 . GLU A 98  ? 1.2783 1.0021 0.8644 -0.2810 0.2745  -0.1504 99  GLU A OE2 
864  N N   . GLY A 99  ? 0.7204 0.4412 0.3121 -0.2014 0.1679  -0.0853 100 GLY A N   
865  C CA  . GLY A 99  ? 0.7346 0.4468 0.3094 -0.1962 0.1557  -0.0806 100 GLY A CA  
866  C C   . GLY A 99  ? 0.7145 0.4524 0.3253 -0.1782 0.1415  -0.0776 100 GLY A C   
867  O O   . GLY A 99  ? 0.7177 0.4554 0.3238 -0.1756 0.1359  -0.0782 100 GLY A O   
868  N N   . ASN A 100 ? 0.6360 0.3954 0.2816 -0.1668 0.1364  -0.0750 101 ASN A N   
869  C CA  . ASN A 100 ? 0.5890 0.3698 0.2652 -0.1509 0.1236  -0.0714 101 ASN A CA  
870  C C   . ASN A 100 ? 0.6150 0.4249 0.3366 -0.1439 0.1314  -0.0786 101 ASN A C   
871  O O   . ASN A 100 ? 0.5837 0.4081 0.3278 -0.1320 0.1230  -0.0763 101 ASN A O   
872  C CB  . ASN A 100 ? 0.5764 0.3543 0.2492 -0.1405 0.1052  -0.0597 101 ASN A CB  
873  C CG  . ASN A 100 ? 0.6473 0.4337 0.3368 -0.1378 0.1066  -0.0578 101 ASN A CG  
874  O OD1 . ASN A 100 ? 0.5556 0.3612 0.2734 -0.1384 0.1175  -0.0648 101 ASN A OD1 
875  N ND2 . ASN A 100 ? 0.6036 0.3770 0.2772 -0.1340 0.0948  -0.0488 101 ASN A ND2 
876  N N   . ILE A 101 ? 0.5705 0.3888 0.3051 -0.1509 0.1469  -0.0875 102 ILE A N   
877  C CA  . ILE A 101 ? 0.5418 0.3889 0.3203 -0.1423 0.1522  -0.0945 102 ILE A CA  
878  C C   . ILE A 101 ? 0.5430 0.4005 0.3412 -0.1347 0.1535  -0.0993 102 ILE A C   
879  O O   . ILE A 101 ? 0.4944 0.3696 0.3224 -0.1211 0.1472  -0.0975 102 ILE A O   
880  C CB  . ILE A 101 ? 0.5843 0.4416 0.3752 -0.1518 0.1689  -0.1061 102 ILE A CB  
881  C CG1 . ILE A 101 ? 0.5586 0.4483 0.3968 -0.1392 0.1691  -0.1119 102 ILE A CG1 
882  C CG2 . ILE A 101 ? 0.5897 0.4359 0.3633 -0.1677 0.1872  -0.1178 102 ILE A CG2 
883  C CD1 . ILE A 101 ? 0.5915 0.4966 0.4462 -0.1445 0.1775  -0.1196 102 ILE A CD1 
884  N N   . MET A 102 ? 0.5388 0.3834 0.3188 -0.1434 0.1617  -0.1051 103 MET A N   
885  C CA  . MET A 102 ? 0.5398 0.3912 0.3367 -0.1370 0.1641  -0.1104 103 MET A CA  
886  C C   . MET A 102 ? 0.5598 0.4109 0.3591 -0.1257 0.1478  -0.1003 103 MET A C   
887  O O   . MET A 102 ? 0.5343 0.3976 0.3601 -0.1145 0.1461  -0.1011 103 MET A O   
888  C CB  . MET A 102 ? 0.6057 0.4426 0.3809 -0.1502 0.1774  -0.1200 103 MET A CB  
889  C CG  . MET A 102 ? 0.6950 0.5352 0.4728 -0.1622 0.1968  -0.1330 103 MET A CG  
890  S SD  . MET A 102 ? 0.7479 0.6207 0.5790 -0.1510 0.2049  -0.1437 103 MET A SD  
891  C CE  . MET A 102 ? 0.7194 0.5962 0.5700 -0.1431 0.2109  -0.1527 103 MET A CE  
892  N N   . ALA A 103 ? 0.5467 0.3837 0.3183 -0.1283 0.1356  -0.0913 104 ALA A N   
893  C CA  . ALA A 103 ? 0.5391 0.3779 0.3130 -0.1192 0.1204  -0.0834 104 ALA A CA  
894  C C   . ALA A 103 ? 0.5324 0.3870 0.3321 -0.1069 0.1120  -0.0769 104 ALA A C   
895  O O   . ALA A 103 ? 0.4933 0.3559 0.3100 -0.0980 0.1067  -0.0747 104 ALA A O   
896  C CB  . ALA A 103 ? 0.5724 0.3953 0.3130 -0.1240 0.1087  -0.0770 104 ALA A CB  
897  N N   . VAL A 104 ? 0.4703 0.3280 0.2712 -0.1074 0.1116  -0.0742 105 VAL A N   
898  C CA  . VAL A 104 ? 0.4258 0.2988 0.2498 -0.0967 0.1041  -0.0688 105 VAL A CA  
899  C C   . VAL A 104 ? 0.4519 0.3414 0.3076 -0.0883 0.1097  -0.0737 105 VAL A C   
900  O O   . VAL A 104 ? 0.4182 0.3154 0.2886 -0.0780 0.1016  -0.0687 105 VAL A O   
901  C CB  . VAL A 104 ? 0.4638 0.3354 0.2812 -0.1005 0.1037  -0.0662 105 VAL A CB  
902  C CG1 . VAL A 104 ? 0.4229 0.3130 0.2669 -0.0906 0.0984  -0.0632 105 VAL A CG1 
903  C CG2 . VAL A 104 ? 0.4847 0.3377 0.2712 -0.1041 0.0937  -0.0587 105 VAL A CG2 
904  N N   A MET A 105 ? 0.4285 0.3227 0.2938 -0.0923 0.1233  -0.0838 106 MET A N   
905  N N   B MET A 105 ? 0.4375 0.3317 0.3029 -0.0923 0.1234  -0.0838 106 MET A N   
906  C CA  A MET A 105 ? 0.4236 0.3330 0.3195 -0.0825 0.1281  -0.0897 106 MET A CA  
907  C CA  B MET A 105 ? 0.4438 0.3534 0.3399 -0.0821 0.1275  -0.0893 106 MET A CA  
908  C C   A MET A 105 ? 0.4714 0.3750 0.3709 -0.0754 0.1253  -0.0881 106 MET A C   
909  C C   B MET A 105 ? 0.4757 0.3792 0.3751 -0.0753 0.1251  -0.0879 106 MET A C   
910  O O   A MET A 105 ? 0.4521 0.3634 0.3704 -0.0633 0.1199  -0.0848 106 MET A O   
911  O O   B MET A 105 ? 0.4529 0.3638 0.3710 -0.0632 0.1199  -0.0848 106 MET A O   
912  C CB  A MET A 105 ? 0.4646 0.3803 0.3699 -0.0888 0.1439  -0.1032 106 MET A CB  
913  C CB  B MET A 105 ? 0.4822 0.3993 0.3896 -0.0876 0.1431  -0.1027 106 MET A CB  
914  C CG  A MET A 105 ? 0.4994 0.4336 0.4394 -0.0762 0.1467  -0.1099 106 MET A CG  
915  C CG  B MET A 105 ? 0.5131 0.4484 0.4552 -0.0743 0.1451  -0.1089 106 MET A CG  
916  S SD  A MET A 105 ? 0.5644 0.5090 0.5197 -0.0831 0.1662  -0.1288 106 MET A SD  
917  S SD  B MET A 105 ? 0.5711 0.5224 0.5333 -0.0800 0.1628  -0.1272 106 MET A SD  
918  C CE  A MET A 105 ? 0.5156 0.4732 0.5058 -0.0633 0.1640  -0.1332 106 MET A CE  
919  C CE  B MET A 105 ? 0.5634 0.4958 0.5079 -0.0900 0.1767  -0.1360 106 MET A CE  
920  N N   . ALA A 106 ? 0.4468 0.3354 0.3262 -0.0837 0.1292  -0.0906 107 ALA A N   
921  C CA  . ALA A 106 ? 0.4614 0.3420 0.3410 -0.0800 0.1284  -0.0906 107 ALA A CA  
922  C C   . ALA A 106 ? 0.4667 0.3476 0.3461 -0.0733 0.1147  -0.0801 107 ALA A C   
923  O O   . ALA A 106 ? 0.4391 0.3201 0.3313 -0.0648 0.1131  -0.0783 107 ALA A O   
924  C CB  . ALA A 106 ? 0.4923 0.3581 0.3476 -0.0923 0.1341  -0.0959 107 ALA A CB  
925  N N   . THR A 107 ? 0.4256 0.3064 0.2910 -0.0768 0.1051  -0.0735 108 THR A N   
926  C CA  . THR A 107 ? 0.4177 0.3014 0.2846 -0.0713 0.0929  -0.0652 108 THR A CA  
927  C C   . THR A 107 ? 0.4328 0.3284 0.3214 -0.0602 0.0895  -0.0608 108 THR A C   
928  O O   . THR A 107 ? 0.3895 0.2852 0.2847 -0.0542 0.0851  -0.0568 108 THR A O   
929  C CB  . THR A 107 ? 0.4688 0.3494 0.3165 -0.0764 0.0832  -0.0606 108 THR A CB  
930  O OG1 . THR A 107 ? 0.4780 0.3466 0.3032 -0.0862 0.0860  -0.0649 108 THR A OG1 
931  C CG2 . THR A 107 ? 0.4579 0.3426 0.3078 -0.0719 0.0717  -0.0550 108 THR A CG2 
932  N N   . ALA A 108 ? 0.3920 0.2972 0.2903 -0.0585 0.0919  -0.0621 109 ALA A N   
933  C CA  . ALA A 108 ? 0.3599 0.2780 0.2782 -0.0482 0.0878  -0.0589 109 ALA A CA  
934  C C   . ALA A 108 ? 0.3938 0.3120 0.3278 -0.0387 0.0914  -0.0613 109 ALA A C   
935  O O   . ALA A 108 ? 0.3784 0.2989 0.3204 -0.0297 0.0849  -0.0556 109 ALA A O   
936  C CB  . ALA A 108 ? 0.3632 0.2930 0.2891 -0.0500 0.0905  -0.0621 109 ALA A CB  
937  N N   . MET A 109 ? 0.3674 0.2801 0.3032 -0.0409 0.1017  -0.0697 110 MET A N   
938  C CA  . MET A 109 ? 0.3724 0.2811 0.3215 -0.0307 0.1050  -0.0722 110 MET A CA  
939  C C   . MET A 109 ? 0.4215 0.3150 0.3603 -0.0291 0.1009  -0.0657 110 MET A C   
940  O O   . MET A 109 ? 0.4212 0.3112 0.3670 -0.0188 0.0968  -0.0610 110 MET A O   
941  C CB  . MET A 109 ? 0.4131 0.3183 0.3657 -0.0344 0.1180  -0.0838 110 MET A CB  
942  C CG  . MET A 109 ? 0.4672 0.3898 0.4365 -0.0341 0.1238  -0.0924 110 MET A CG  
943  S SD  . MET A 109 ? 0.5742 0.4923 0.5427 -0.0433 0.1413  -0.1076 110 MET A SD  
944  C CE  . MET A 109 ? 0.5471 0.4569 0.5321 -0.0281 0.1437  -0.1110 110 MET A CE  
945  N N   . TYR A 110 ? 0.4012 0.2857 0.3221 -0.0399 0.1015  -0.0658 111 TYR A N   
946  C CA  . TYR A 110 ? 0.3975 0.2699 0.3084 -0.0418 0.0989  -0.0621 111 TYR A CA  
947  C C   . TYR A 110 ? 0.4218 0.2996 0.3344 -0.0371 0.0886  -0.0529 111 TYR A C   
948  O O   . TYR A 110 ? 0.4125 0.2812 0.3250 -0.0327 0.0878  -0.0491 111 TYR A O   
949  C CB  . TYR A 110 ? 0.4107 0.2787 0.3039 -0.0547 0.0995  -0.0654 111 TYR A CB  
950  C CG  . TYR A 110 ? 0.4194 0.2807 0.3038 -0.0591 0.0959  -0.0635 111 TYR A CG  
951  C CD1 . TYR A 110 ? 0.4696 0.3164 0.3516 -0.0606 0.1029  -0.0672 111 TYR A CD1 
952  C CD2 . TYR A 110 ? 0.4120 0.2814 0.2904 -0.0626 0.0862  -0.0596 111 TYR A CD2 
953  C CE1 . TYR A 110 ? 0.4399 0.2816 0.3141 -0.0669 0.1012  -0.0673 111 TYR A CE1 
954  C CE2 . TYR A 110 ? 0.4138 0.2806 0.2867 -0.0678 0.0837  -0.0604 111 TYR A CE2 
955  C CZ  . TYR A 110 ? 0.4609 0.3145 0.3318 -0.0707 0.0916  -0.0645 111 TYR A CZ  
956  O OH  . TYR A 110 ? 0.4444 0.2972 0.3103 -0.0780 0.0902  -0.0671 111 TYR A OH  
957  N N   . LEU A 111 ? 0.3838 0.2746 0.2967 -0.0384 0.0819  -0.0497 112 LEU A N   
958  C CA  . LEU A 111 ? 0.3560 0.2533 0.2705 -0.0348 0.0728  -0.0422 112 LEU A CA  
959  C C   . LEU A 111 ? 0.3923 0.2949 0.3199 -0.0235 0.0702  -0.0384 112 LEU A C   
960  O O   . LEU A 111 ? 0.3768 0.2821 0.3045 -0.0201 0.0637  -0.0323 112 LEU A O   
961  C CB  . LEU A 111 ? 0.3456 0.2525 0.2547 -0.0398 0.0665  -0.0408 112 LEU A CB  
962  C CG  . LEU A 111 ? 0.3809 0.2834 0.2752 -0.0491 0.0646  -0.0432 112 LEU A CG  
963  C CD1 . LEU A 111 ? 0.3764 0.2856 0.2650 -0.0509 0.0568  -0.0406 112 LEU A CD1 
964  C CD2 . LEU A 111 ? 0.4102 0.3089 0.3015 -0.0512 0.0624  -0.0428 112 LEU A CD2 
965  N N   . GLN A 112 ? 0.3638 0.2688 0.3028 -0.0175 0.0750  -0.0428 113 GLN A N   
966  C CA  . GLN A 112 ? 0.3548 0.2672 0.3079 -0.0051 0.0710  -0.0405 113 GLN A CA  
967  C C   . GLN A 112 ? 0.3913 0.3213 0.3499 -0.0049 0.0638  -0.0377 113 GLN A C   
968  O O   . GLN A 112 ? 0.3799 0.3123 0.3381 0.0000  0.0564  -0.0313 113 GLN A O   
969  C CB  . GLN A 112 ? 0.3693 0.2667 0.3178 0.0028  0.0683  -0.0343 113 GLN A CB  
970  C CG  . GLN A 112 ? 0.4112 0.2886 0.3545 0.0029  0.0765  -0.0378 113 GLN A CG  
971  C CD  . GLN A 112 ? 0.5788 0.4361 0.5102 0.0061  0.0749  -0.0309 113 GLN A CD  
972  O OE1 . GLN A 112 ? 0.4862 0.3433 0.4164 0.0134  0.0677  -0.0238 113 GLN A OE1 
973  N NE2 . GLN A 112 ? 0.5488 0.3873 0.4688 -0.0005 0.0823  -0.0332 113 GLN A NE2 
974  N N   . MET A 113 ? 0.3485 0.2883 0.3094 -0.0116 0.0671  -0.0430 114 MET A N   
975  C CA  . MET A 113 ? 0.3344 0.2890 0.2994 -0.0136 0.0626  -0.0422 114 MET A CA  
976  C C   . MET A 113 ? 0.4040 0.3729 0.3862 -0.0111 0.0676  -0.0507 114 MET A C   
977  O O   . MET A 113 ? 0.3772 0.3479 0.3577 -0.0199 0.0754  -0.0575 114 MET A O   
978  C CB  . MET A 113 ? 0.3523 0.3018 0.3013 -0.0250 0.0627  -0.0414 114 MET A CB  
979  C CG  . MET A 113 ? 0.3831 0.3236 0.3199 -0.0265 0.0569  -0.0352 114 MET A CG  
980  S SD  . MET A 113 ? 0.4267 0.3610 0.3456 -0.0370 0.0550  -0.0353 114 MET A SD  
981  C CE  . MET A 113 ? 0.3877 0.3330 0.3101 -0.0364 0.0491  -0.0325 114 MET A CE  
982  N N   . GLU A 114 ? 0.3927 0.3710 0.3911 0.0011  0.0635  -0.0511 115 GLU A N   
983  C CA  . GLU A 114 ? 0.4031 0.3985 0.4236 0.0067  0.0671  -0.0610 115 GLU A CA  
984  C C   . GLU A 114 ? 0.4017 0.4145 0.4298 -0.0023 0.0713  -0.0685 115 GLU A C   
985  O O   . GLU A 114 ? 0.3873 0.4083 0.4264 -0.0058 0.0808  -0.0795 115 GLU A O   
986  C CB  . GLU A 114 ? 0.4334 0.4369 0.4681 0.0230  0.0578  -0.0587 115 GLU A CB  
987  C CG  . GLU A 114 ? 0.6223 0.6048 0.6489 0.0323  0.0558  -0.0526 115 GLU A CG  
988  N N   . HIS A 115 ? 0.3547 0.3724 0.3767 -0.0067 0.0654  -0.0636 116 HIS A N   
989  C CA  . HIS A 115 ? 0.3724 0.4038 0.3997 -0.0163 0.0703  -0.0709 116 HIS A CA  
990  C C   . HIS A 115 ? 0.3929 0.4112 0.4037 -0.0309 0.0812  -0.0745 116 HIS A C   
991  O O   . HIS A 115 ? 0.3964 0.4237 0.4143 -0.0389 0.0908  -0.0849 116 HIS A O   
992  C CB  . HIS A 115 ? 0.3970 0.4345 0.4209 -0.0173 0.0618  -0.0653 116 HIS A CB  
993  C CG  . HIS A 115 ? 0.4552 0.5077 0.4944 -0.0042 0.0515  -0.0635 116 HIS A CG  
994  N ND1 . HIS A 115 ? 0.4896 0.5646 0.5533 0.0028  0.0513  -0.0731 116 HIS A ND1 
995  C CD2 . HIS A 115 ? 0.4838 0.5320 0.5158 0.0023  0.0411  -0.0538 116 HIS A CD2 
996  C CE1 . HIS A 115 ? 0.4831 0.5651 0.5519 0.0144  0.0394  -0.0680 116 HIS A CE1 
997  N NE2 . HIS A 115 ? 0.4857 0.5511 0.5346 0.0137  0.0337  -0.0561 116 HIS A NE2 
998  N N   . VAL A 116 ? 0.3326 0.3297 0.3211 -0.0347 0.0798  -0.0669 117 VAL A N   
999  C CA  . VAL A 116 ? 0.3400 0.3213 0.3082 -0.0475 0.0881  -0.0691 117 VAL A CA  
1000 C C   . VAL A 116 ? 0.4140 0.3961 0.3898 -0.0493 0.0997  -0.0792 117 VAL A C   
1001 O O   . VAL A 116 ? 0.3998 0.3811 0.3706 -0.0605 0.1104  -0.0872 117 VAL A O   
1002 C CB  . VAL A 116 ? 0.3910 0.3527 0.3357 -0.0497 0.0821  -0.0598 117 VAL A CB  
1003 C CG1 . VAL A 116 ? 0.4108 0.3560 0.3333 -0.0617 0.0895  -0.0626 117 VAL A CG1 
1004 C CG2 . VAL A 116 ? 0.3782 0.3401 0.3167 -0.0487 0.0721  -0.0520 117 VAL A CG2 
1005 N N   . VAL A 117 ? 0.3686 0.3511 0.3557 -0.0386 0.0983  -0.0793 118 VAL A N   
1006 C CA  . VAL A 117 ? 0.3728 0.3561 0.3698 -0.0383 0.1092  -0.0898 118 VAL A CA  
1007 C C   . VAL A 117 ? 0.4322 0.4376 0.4515 -0.0401 0.1173  -0.1029 118 VAL A C   
1008 O O   . VAL A 117 ? 0.4216 0.4260 0.4386 -0.0506 0.1304  -0.1131 118 VAL A O   
1009 C CB  . VAL A 117 ? 0.4009 0.3792 0.4071 -0.0245 0.1055  -0.0875 118 VAL A CB  
1010 C CG1 . VAL A 117 ? 0.4072 0.3867 0.4259 -0.0232 0.1173  -0.0998 118 VAL A CG1 
1011 C CG2 . VAL A 117 ? 0.4006 0.3579 0.3847 -0.0263 0.1004  -0.0773 118 VAL A CG2 
1012 N N   A ASP A 118 ? 0.3993 0.4248 0.4387 -0.0314 0.1096  -0.1031 119 ASP A N   
1013 N N   B ASP A 118 ? 0.3971 0.4229 0.4377 -0.0305 0.1096  -0.1033 119 ASP A N   
1014 C CA  A ASP A 118 ? 0.4035 0.4550 0.4680 -0.0324 0.1153  -0.1164 119 ASP A CA  
1015 C CA  B ASP A 118 ? 0.4008 0.4531 0.4674 -0.0309 0.1151  -0.1168 119 ASP A CA  
1016 C C   A ASP A 118 ? 0.4396 0.4901 0.4919 -0.0519 0.1270  -0.1231 119 ASP A C   
1017 C C   B ASP A 118 ? 0.4506 0.5033 0.5066 -0.0501 0.1270  -0.1241 119 ASP A C   
1018 O O   A ASP A 118 ? 0.4409 0.5023 0.5053 -0.0591 0.1403  -0.1376 119 ASP A O   
1019 O O   B ASP A 118 ? 0.4556 0.5206 0.5254 -0.0567 0.1400  -0.1390 119 ASP A O   
1020 C CB  A ASP A 118 ? 0.4211 0.4924 0.5039 -0.0204 0.1021  -0.1134 119 ASP A CB  
1021 C CB  B ASP A 118 ? 0.4164 0.4882 0.5007 -0.0190 0.1018  -0.1135 119 ASP A CB  
1022 C CG  A ASP A 118 ? 0.5712 0.6741 0.6839 -0.0201 0.1062  -0.1287 119 ASP A CG  
1023 C CG  B ASP A 118 ? 0.5650 0.6427 0.6669 0.0013  0.0919  -0.1115 119 ASP A CG  
1024 O OD1 A ASP A 118 ? 0.6059 0.7225 0.7416 -0.0135 0.1118  -0.1408 119 ASP A OD1 
1025 O OD1 B ASP A 118 ? 0.6037 0.6802 0.7165 0.0076  0.0975  -0.1185 119 ASP A OD1 
1026 O OD2 A ASP A 118 ? 0.6274 0.7422 0.7418 -0.0265 0.1040  -0.1296 119 ASP A OD2 
1027 O OD2 B ASP A 118 ? 0.6422 0.7243 0.7456 0.0110  0.0785  -0.1031 119 ASP A OD2 
1028 N N   A THR A 119 ? 0.3881 0.4241 0.4157 -0.0606 0.1228  -0.1131 120 THR A N   
1029 N N   B THR A 119 ? 0.4022 0.4400 0.4331 -0.0592 0.1232  -0.1143 120 THR A N   
1030 C CA  A THR A 119 ? 0.4026 0.4317 0.4137 -0.0791 0.1338  -0.1182 120 THR A CA  
1031 C CA  B THR A 119 ? 0.4149 0.4462 0.4294 -0.0775 0.1336  -0.1190 120 THR A CA  
1032 C C   A THR A 119 ? 0.4598 0.4684 0.4488 -0.0910 0.1462  -0.1218 120 THR A C   
1033 C C   B THR A 119 ? 0.4686 0.4790 0.4603 -0.0900 0.1463  -0.1225 120 THR A C   
1034 O O   A THR A 119 ? 0.4635 0.4715 0.4470 -0.1059 0.1604  -0.1322 120 THR A O   
1035 O O   B THR A 119 ? 0.4738 0.4857 0.4625 -0.1044 0.1607  -0.1337 120 THR A O   
1036 C CB  A THR A 119 ? 0.4253 0.4425 0.4159 -0.0840 0.1259  -0.1076 120 THR A CB  
1037 C CB  B THR A 119 ? 0.4946 0.5150 0.4900 -0.0809 0.1245  -0.1075 120 THR A CB  
1038 O OG1 A THR A 119 ? 0.4420 0.4552 0.4215 -0.1011 0.1379  -0.1150 120 THR A OG1 
1039 O OG1 B THR A 119 ? 0.4732 0.5115 0.4884 -0.0676 0.1119  -0.1035 120 THR A OG1 
1040 C CG2 A THR A 119 ? 0.3812 0.3710 0.3420 -0.0835 0.1181  -0.0936 120 THR A CG2 
1041 C CG2 B THR A 119 ? 0.4980 0.5157 0.4826 -0.0977 0.1346  -0.1138 120 THR A CG2 
1042 N N   . CYS A 120 ? 0.4273 0.4189 0.4028 -0.0857 0.1417  -0.1141 121 CYS A N   
1043 C CA  . CYS A 120 ? 0.4481 0.4199 0.4013 -0.0965 0.1522  -0.1175 121 CYS A CA  
1044 C C   . CYS A 120 ? 0.5014 0.4881 0.4762 -0.0987 0.1671  -0.1342 121 CYS A C   
1045 O O   . CYS A 120 ? 0.4935 0.4725 0.4543 -0.1145 0.1818  -0.1432 121 CYS A O   
1046 C CB  . CYS A 120 ? 0.4543 0.4093 0.3933 -0.0896 0.1436  -0.1076 121 CYS A CB  
1047 S SG  . CYS A 120 ? 0.5009 0.4359 0.4094 -0.0910 0.1291  -0.0912 121 CYS A SG  
1048 N N   A ARG A 121 ? 0.4546 0.4619 0.4629 -0.0827 0.1633  -0.1389 122 ARG A N   
1049 N N   B ARG A 121 ? 0.4583 0.4653 0.4663 -0.0828 0.1634  -0.1389 122 ARG A N   
1050 C CA  A ARG A 121 ? 0.4631 0.4888 0.4994 -0.0804 0.1754  -0.1560 122 ARG A CA  
1051 C CA  B ARG A 121 ? 0.4687 0.4936 0.5038 -0.0812 0.1760  -0.1562 122 ARG A CA  
1052 C C   A ARG A 121 ? 0.5067 0.5515 0.5554 -0.0932 0.1881  -0.1708 122 ARG A C   
1053 C C   B ARG A 121 ? 0.5081 0.5529 0.5568 -0.0934 0.1883  -0.1709 122 ARG A C   
1054 O O   A ARG A 121 ? 0.5092 0.5578 0.5622 -0.1036 0.2050  -0.1858 122 ARG A O   
1055 O O   B ARG A 121 ? 0.5092 0.5582 0.5626 -0.1038 0.2052  -0.1861 122 ARG A O   
1056 C CB  A ARG A 121 ? 0.4637 0.5078 0.5330 -0.0581 0.1648  -0.1563 122 ARG A CB  
1057 C CB  B ARG A 121 ? 0.4784 0.5199 0.5455 -0.0590 0.1662  -0.1567 122 ARG A CB  
1058 C CG  A ARG A 121 ? 0.6362 0.6610 0.6963 -0.0467 0.1571  -0.1461 122 ARG A CG  
1059 C CG  B ARG A 121 ? 0.6736 0.6956 0.7321 -0.0503 0.1633  -0.1507 122 ARG A CG  
1060 C CD  A ARG A 121 ? 0.7767 0.8151 0.8675 -0.0259 0.1511  -0.1499 122 ARG A CD  
1061 C CD  B ARG A 121 ? 0.8074 0.8434 0.8980 -0.0305 0.1598  -0.1568 122 ARG A CD  
1062 N NE  A ARG A 121 ? 0.8387 0.8555 0.9169 -0.0154 0.1422  -0.1375 122 ARG A NE  
1063 N NE  B ARG A 121 ? 0.8660 0.9105 0.9678 -0.0143 0.1425  -0.1465 122 ARG A NE  
1064 C CZ  A ARG A 121 ? 0.9734 0.9719 1.0429 -0.0159 0.1492  -0.1397 122 ARG A CZ  
1065 C CZ  B ARG A 121 ? 0.9991 1.0279 1.0939 -0.0015 0.1314  -0.1342 122 ARG A CZ  
1066 N NH1 A ARG A 121 ? 0.8505 0.8500 0.9222 -0.0257 0.1650  -0.1537 122 ARG A NH1 
1067 N NH1 B ARG A 121 ? 0.8168 0.8219 0.8954 -0.0028 0.1357  -0.1314 122 ARG A NH1 
1068 N NH2 A ARG A 121 ? 0.7386 0.7173 0.7962 -0.0078 0.1414  -0.1287 122 ARG A NH2 
1069 N NH2 B ARG A 121 ? 0.7985 0.8346 0.9009 0.0116  0.1166  -0.1254 122 ARG A NH2 
1070 N N   . LYS A 122 ? 0.4545 0.5107 0.5081 -0.0937 0.1811  -0.1672 123 LYS A N   
1071 C CA  . LYS A 122 ? 0.4646 0.5396 0.5302 -0.1068 0.1924  -0.1810 123 LYS A CA  
1072 C C   . LYS A 122 ? 0.5274 0.5778 0.5568 -0.1308 0.2074  -0.1827 123 LYS A C   
1073 O O   . LYS A 122 ? 0.5244 0.5843 0.5609 -0.1449 0.2254  -0.1996 123 LYS A O   
1074 C CB  . LYS A 122 ? 0.4793 0.5708 0.5576 -0.1007 0.1797  -0.1760 123 LYS A CB  
1075 C CG  . LYS A 122 ? 0.6967 0.8181 0.8145 -0.0790 0.1679  -0.1797 123 LYS A CG  
1076 C CD  . LYS A 122 ? 0.8410 0.9796 0.9706 -0.0730 0.1549  -0.1755 123 LYS A CD  
1077 C CE  . LYS A 122 ? 0.9999 1.1624 1.1620 -0.0498 0.1408  -0.1766 123 LYS A CE  
1078 N NZ  . LYS A 122 ? 1.1420 1.3372 1.3304 -0.0471 0.1349  -0.1851 123 LYS A NZ  
1079 N N   . PHE A 123 ? 0.4880 0.5059 0.4778 -0.1353 0.2000  -0.1658 124 PHE A N   
1080 C CA  . PHE A 123 ? 0.5178 0.5059 0.4662 -0.1562 0.2113  -0.1645 124 PHE A CA  
1081 C C   . PHE A 123 ? 0.5824 0.5597 0.5196 -0.1652 0.2261  -0.1737 124 PHE A C   
1082 O O   . PHE A 123 ? 0.5860 0.5525 0.5042 -0.1851 0.2433  -0.1831 124 PHE A O   
1083 C CB  . PHE A 123 ? 0.5417 0.4999 0.4539 -0.1546 0.1967  -0.1445 124 PHE A CB  
1084 C CG  . PHE A 123 ? 0.5553 0.5124 0.4623 -0.1564 0.1896  -0.1378 124 PHE A CG  
1085 C CD1 . PHE A 123 ? 0.5664 0.5533 0.5085 -0.1460 0.1827  -0.1409 124 PHE A CD1 
1086 C CD2 . PHE A 123 ? 0.6121 0.5367 0.4780 -0.1670 0.1880  -0.1278 124 PHE A CD2 
1087 C CE1 . PHE A 123 ? 0.5796 0.5650 0.5164 -0.1485 0.1768  -0.1356 124 PHE A CE1 
1088 C CE2 . PHE A 123 ? 0.6316 0.5530 0.4926 -0.1682 0.1818  -0.1220 124 PHE A CE2 
1089 C CZ  . PHE A 123 ? 0.5778 0.5301 0.4746 -0.1596 0.1769  -0.1263 124 PHE A CZ  
1090 N N   . ILE A 124 ? 0.5313 0.5109 0.4799 -0.1516 0.2206  -0.1721 125 ILE A N   
1091 C CA  . ILE A 124 ? 0.5538 0.5249 0.4949 -0.1589 0.2347  -0.1821 125 ILE A CA  
1092 C C   . ILE A 124 ? 0.6264 0.6249 0.6003 -0.1647 0.2534  -0.2051 125 ILE A C   
1093 O O   . ILE A 124 ? 0.6470 0.6358 0.6042 -0.1833 0.2723  -0.2167 125 ILE A O   
1094 C CB  . ILE A 124 ? 0.5821 0.5464 0.5258 -0.1433 0.2242  -0.1744 125 ILE A CB  
1095 C CG1 . ILE A 124 ? 0.5915 0.5265 0.4963 -0.1444 0.2106  -0.1557 125 ILE A CG1 
1096 C CG2 . ILE A 124 ? 0.6115 0.5739 0.5584 -0.1483 0.2398  -0.1885 125 ILE A CG2 
1097 C CD1 . ILE A 124 ? 0.6518 0.5841 0.5628 -0.1278 0.1961  -0.1456 125 ILE A CD1 
1098 N N   . LYS A 125 ? 0.5734 0.6065 0.5931 -0.1494 0.2480  -0.2124 126 LYS A N   
1099 C CA  . LYS A 125 ? 0.5853 0.6509 0.6435 -0.1517 0.2632  -0.2358 126 LYS A CA  
1100 C C   . LYS A 125 ? 0.6464 0.7145 0.6943 -0.1762 0.2809  -0.2478 126 LYS A C   
1101 O O   . LYS A 125 ? 0.6411 0.7224 0.7024 -0.1882 0.3010  -0.2684 126 LYS A O   
1102 C CB  . LYS A 125 ? 0.6008 0.7021 0.7069 -0.1289 0.2498  -0.2393 126 LYS A CB  
1103 N N   . ALA A 126 ? 0.6008 0.6542 0.6235 -0.1842 0.2744  -0.2355 127 ALA A N   
1104 C CA  . ALA A 126 ? 0.6253 0.6741 0.6318 -0.2086 0.2910  -0.2447 127 ALA A CA  
1105 C C   . ALA A 126 ? 0.7325 0.7467 0.6937 -0.2320 0.3095  -0.2473 127 ALA A C   
1106 O O   . ALA A 126 ? 0.7440 0.7612 0.7016 -0.2534 0.3308  -0.2635 127 ALA A O   
1107 C CB  . ALA A 126 ? 0.6241 0.6609 0.6123 -0.2093 0.2781  -0.2293 127 ALA A CB  
1108 N N   . SER A 127 ? 0.7339 0.7155 0.6596 -0.2289 0.3017  -0.2320 128 SER A N   
1109 C CA  . SER A 127 ? 0.7958 0.7411 0.6728 -0.2496 0.3158  -0.2319 128 SER A CA  
1110 C C   . SER A 127 ? 0.8997 0.8527 0.7874 -0.2552 0.3335  -0.2496 128 SER A C   
1111 O O   . SER A 127 ? 0.9514 0.8778 0.8006 -0.2761 0.3496  -0.2540 128 SER A O   
1112 C CB  . SER A 127 ? 0.8661 0.7737 0.6986 -0.2445 0.2981  -0.2083 128 SER A CB  
1113 O OG  . SER A 127 ? 1.0219 0.9060 0.8218 -0.2527 0.2924  -0.1960 128 SER A OG  
1114 N N   . GLU A 128 ? 0.8308 0.8181 0.7688 -0.2371 0.3312  -0.2602 129 GLU A N   
1115 C CA  . GLU A 128 ? 1.0810 1.0776 1.0343 -0.2399 0.3477  -0.2784 129 GLU A CA  
1116 C C   . GLU A 128 ? 1.6259 1.6458 1.6005 -0.2582 0.3740  -0.3053 129 GLU A C   
1117 O O   . GLU A 128 ? 1.2287 1.2447 1.1883 -0.2767 0.3838  -0.3087 129 GLU A O   
1118 C CB  . GLU A 128 ? 1.0665 1.0853 1.0616 -0.2122 0.3346  -0.2786 129 GLU A CB  
1119 C CG  . GLU A 128 ? 1.1585 1.2224 1.2125 -0.1961 0.3311  -0.2913 129 GLU A CG  
1120 C CD  . GLU A 128 ? 1.4092 1.4891 1.4987 -0.1666 0.3143  -0.2874 129 GLU A CD  
1121 O OE1 . GLU A 128 ? 1.3450 1.4007 1.4131 -0.1563 0.2999  -0.2692 129 GLU A OE1 
1122 O OE2 . GLU A 128 ? 1.2974 1.4140 1.4360 -0.1538 0.3152  -0.3030 129 GLU A OE2 
1126 N N   A TRP B 2   ? 0.2506 0.4850 0.3101 -0.0245 -0.0235 -0.0964 1   TRP D N   
1127 N N   B TRP B 2   ? 0.2616 0.4960 0.3211 -0.0245 -0.0235 -0.0964 1   TRP D N   
1128 C CA  A TRP B 2   ? 0.2406 0.4730 0.2985 -0.0238 -0.0236 -0.0980 1   TRP D CA  
1129 C CA  B TRP B 2   ? 0.2584 0.4909 0.3164 -0.0239 -0.0235 -0.0979 1   TRP D CA  
1130 C C   A TRP B 2   ? 0.2946 0.5272 0.3537 -0.0237 -0.0241 -0.0982 1   TRP D C   
1131 C C   B TRP B 2   ? 0.2925 0.5254 0.3518 -0.0238 -0.0241 -0.0981 1   TRP D C   
1132 O O   A TRP B 2   ? 0.2906 0.5232 0.3513 -0.0240 -0.0248 -0.0979 1   TRP D O   
1133 O O   B TRP B 2   ? 0.2817 0.5150 0.3426 -0.0242 -0.0247 -0.0976 1   TRP D O   
1134 C CB  A TRP B 2   ? 0.2298 0.4596 0.2864 -0.0233 -0.0243 -0.0986 1   TRP D CB  
1135 C CB  B TRP B 2   ? 0.2518 0.4816 0.3085 -0.0233 -0.0243 -0.0986 1   TRP D CB  
1136 C CG  A TRP B 2   ? 0.2316 0.4608 0.2863 -0.0234 -0.0238 -0.0989 1   TRP D CG  
1137 C CG  B TRP B 2   ? 0.2660 0.4957 0.3248 -0.0232 -0.0254 -0.0989 1   TRP D CG  
1138 C CD1 A TRP B 2   ? 0.2627 0.4921 0.3179 -0.0237 -0.0240 -0.0984 1   TRP D CD1 
1139 C CD1 B TRP B 2   ? 0.3047 0.5343 0.3660 -0.0237 -0.0259 -0.0988 1   TRP D CD1 
1140 C CD2 A TRP B 2   ? 0.2253 0.4537 0.2775 -0.0230 -0.0228 -0.1001 1   TRP D CD2 
1141 C CD2 B TRP B 2   ? 0.2664 0.4967 0.3259 -0.0227 -0.0259 -0.0996 1   TRP D CD2 
1142 N NE1 A TRP B 2   ? 0.2546 0.4835 0.3070 -0.0236 -0.0234 -0.0994 1   TRP D NE1 
1143 N NE1 B TRP B 2   ? 0.2968 0.5272 0.3609 -0.0236 -0.0265 -0.0999 1   TRP D NE1 
1144 C CE2 A TRP B 2   ? 0.2667 0.4949 0.3172 -0.0232 -0.0226 -0.1006 1   TRP D CE2 
1145 C CE2 B TRP B 2   ? 0.3160 0.5472 0.3787 -0.0229 -0.0265 -0.1005 1   TRP D CE2 
1146 C CE3 A TRP B 2   ? 0.2327 0.4605 0.2845 -0.0225 -0.0220 -0.1006 1   TRP D CE3 
1147 C CE3 B TRP B 2   ? 0.2777 0.5085 0.3362 -0.0220 -0.0256 -0.0997 1   TRP D CE3 
1148 C CZ2 A TRP B 2   ? 0.2608 0.4881 0.3085 -0.0229 -0.0215 -0.1021 1   TRP D CZ2 
1149 C CZ2 B TRP B 2   ? 0.3059 0.5393 0.3703 -0.0224 -0.0267 -0.1020 1   TRP D CZ2 
1150 C CZ3 A TRP B 2   ? 0.2479 0.4747 0.2980 -0.0222 -0.0208 -0.1017 1   TRP D CZ3 
1151 C CZ3 B TRP B 2   ? 0.2976 0.5301 0.3571 -0.0213 -0.0261 -0.1006 1   TRP D CZ3 
1152 C CH2 A TRP B 2   ? 0.2566 0.4832 0.3043 -0.0225 -0.0205 -0.1027 1   TRP D CH2 
1153 C CH2 B TRP B 2   ? 0.3032 0.5374 0.3654 -0.0215 -0.0265 -0.1019 1   TRP D CH2 
1154 N N   . VAL B 3   ? 0.2381 0.4708 0.2970 -0.0234 -0.0237 -0.0990 2   VAL D N   
1155 C CA  . VAL B 3   ? 0.2393 0.4724 0.2990 -0.0232 -0.0242 -0.0994 2   VAL D CA  
1156 C C   . VAL B 3   ? 0.2633 0.4951 0.3225 -0.0220 -0.0241 -0.0996 2   VAL D C   
1157 O O   . VAL B 3   ? 0.2388 0.4696 0.2974 -0.0215 -0.0234 -0.0993 2   VAL D O   
1158 C CB  . VAL B 3   ? 0.2802 0.5164 0.3417 -0.0242 -0.0240 -0.1000 2   VAL D CB  
1159 C CG1 . VAL B 3   ? 0.2752 0.5141 0.3376 -0.0254 -0.0242 -0.0991 2   VAL D CG1 
1160 C CG2 . VAL B 3   ? 0.2735 0.5111 0.3364 -0.0243 -0.0227 -0.1010 2   VAL D CG2 
1161 N N   . ILE B 4   ? 0.2295 0.4617 0.2890 -0.0214 -0.0246 -0.0998 3   ILE D N   
1162 C CA  . ILE B 4   ? 0.2255 0.4574 0.2852 -0.0202 -0.0243 -0.0993 3   ILE D CA  
1163 C C   . ILE B 4   ? 0.2859 0.5183 0.3482 -0.0208 -0.0237 -0.1000 3   ILE D C   
1164 O O   . ILE B 4   ? 0.2769 0.5107 0.3401 -0.0215 -0.0242 -0.1012 3   ILE D O   
1165 C CB  . ILE B 4   ? 0.2478 0.4812 0.3070 -0.0192 -0.0250 -0.0996 3   ILE D CB  
1166 C CG1 . ILE B 4   ? 0.2267 0.4614 0.2851 -0.0189 -0.0255 -0.1001 3   ILE D CG1 
1167 C CG2 . ILE B 4   ? 0.2758 0.5098 0.3357 -0.0177 -0.0246 -0.0983 3   ILE D CG2 
1168 C CD1 . ILE B 4   ? 0.3043 0.5393 0.3621 -0.0185 -0.0255 -0.0991 3   ILE D CD1 
1169 N N   . PRO B 5   ? 0.2816 0.5134 0.3459 -0.0205 -0.0224 -0.0997 4   PRO D N   
1170 C CA  . PRO B 5   ? 0.2856 0.5191 0.3543 -0.0213 -0.0215 -0.1012 4   PRO D CA  
1171 C C   . PRO B 5   ? 0.3282 0.5617 0.3994 -0.0206 -0.0219 -0.1011 4   PRO D C   
1172 O O   . PRO B 5   ? 0.3092 0.5414 0.3791 -0.0190 -0.0221 -0.0992 4   PRO D O   
1173 C CB  . PRO B 5   ? 0.3122 0.5450 0.3830 -0.0211 -0.0197 -0.1012 4   PRO D CB  
1174 C CG  . PRO B 5   ? 0.3680 0.5981 0.4357 -0.0196 -0.0199 -0.0988 4   PRO D CG  
1175 C CD  . PRO B 5   ? 0.3159 0.5461 0.3793 -0.0197 -0.0216 -0.0985 4   PRO D CD  
1176 N N   . ALA B 6   ? 0.3186 0.5545 0.3936 -0.0218 -0.0219 -0.1033 5   ALA D N   
# 
