data_7GUN
# 
_entry.id   7GUN 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7GUN         pdb_00007gun 10.2210/pdb7gun/pdb 
WWPDB D_1001406658 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.entry_id                        7GUN 
_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           Y 
_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-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' 260.679   1   ? ? ? ? 
4 non-polymer nat 'CHLORIDE ION'                                                35.453    1   ? ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                          78.133    1   ? ? ? ? 
6 water       nat water                                                         18.015    181 ? ? ? ? 
# 
_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-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' 7ZO 
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 
7ZO non-polymer         . '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' ? 'C12 H9 Cl N4 O' 260.679 
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 7ZO 1   201 1   7ZO 375 A . 
D 4 CL  1   202 1   CL  CL  A . 
E 5 DMS 1   101 1   DMS DMS D . 
F 6 HOH 1   301 42  HOH HOH A . 
F 6 HOH 2   302 81  HOH HOH A . 
F 6 HOH 3   303 15  HOH HOH A . 
F 6 HOH 4   304 166 HOH HOH A . 
F 6 HOH 5   305 84  HOH HOH A . 
F 6 HOH 6   306 88  HOH HOH A . 
F 6 HOH 7   307 159 HOH HOH A . 
F 6 HOH 8   308 130 HOH HOH A . 
F 6 HOH 9   309 33  HOH HOH A . 
F 6 HOH 10  310 114 HOH HOH A . 
F 6 HOH 11  311 87  HOH HOH A . 
F 6 HOH 12  312 85  HOH HOH A . 
F 6 HOH 13  313 189 HOH HOH A . 
F 6 HOH 14  314 32  HOH HOH A . 
F 6 HOH 15  315 149 HOH HOH A . 
F 6 HOH 16  316 14  HOH HOH A . 
F 6 HOH 17  317 23  HOH HOH A . 
F 6 HOH 18  318 92  HOH HOH A . 
F 6 HOH 19  319 24  HOH HOH A . 
F 6 HOH 20  320 5   HOH HOH A . 
F 6 HOH 21  321 143 HOH HOH A . 
F 6 HOH 22  322 230 HOH HOH A . 
F 6 HOH 23  323 196 HOH HOH A . 
F 6 HOH 24  324 187 HOH HOH A . 
F 6 HOH 25  325 83  HOH HOH A . 
F 6 HOH 26  326 103 HOH HOH A . 
F 6 HOH 27  327 134 HOH HOH A . 
F 6 HOH 28  328 109 HOH HOH A . 
F 6 HOH 29  329 63  HOH HOH A . 
F 6 HOH 30  330 50  HOH HOH A . 
F 6 HOH 31  331 165 HOH HOH A . 
F 6 HOH 32  332 113 HOH HOH A . 
F 6 HOH 33  333 3   HOH HOH A . 
F 6 HOH 34  334 90  HOH HOH A . 
F 6 HOH 35  335 100 HOH HOH A . 
F 6 HOH 36  336 97  HOH HOH A . 
F 6 HOH 37  337 141 HOH HOH A . 
F 6 HOH 38  338 94  HOH HOH A . 
F 6 HOH 39  339 110 HOH HOH A . 
F 6 HOH 40  340 213 HOH HOH A . 
F 6 HOH 41  341 11  HOH HOH A . 
F 6 HOH 42  342 112 HOH HOH A . 
F 6 HOH 43  343 35  HOH HOH A . 
F 6 HOH 44  344 26  HOH HOH A . 
F 6 HOH 45  345 151 HOH HOH A . 
F 6 HOH 46  346 13  HOH HOH A . 
F 6 HOH 47  347 135 HOH HOH A . 
F 6 HOH 48  348 117 HOH HOH A . 
F 6 HOH 49  349 180 HOH HOH A . 
F 6 HOH 50  350 51  HOH HOH A . 
F 6 HOH 51  351 25  HOH HOH A . 
F 6 HOH 52  352 184 HOH HOH A . 
F 6 HOH 53  353 115 HOH HOH A . 
F 6 HOH 54  354 116 HOH HOH A . 
F 6 HOH 55  355 6   HOH HOH A . 
F 6 HOH 56  356 49  HOH HOH A . 
F 6 HOH 57  357 136 HOH HOH A . 
F 6 HOH 58  358 102 HOH HOH A . 
F 6 HOH 59  359 74  HOH HOH A . 
F 6 HOH 60  360 95  HOH HOH A . 
F 6 HOH 61  361 123 HOH HOH A . 
F 6 HOH 62  362 44  HOH HOH A . 
F 6 HOH 63  363 231 HOH HOH A . 
F 6 HOH 64  364 119 HOH HOH A . 
F 6 HOH 65  365 150 HOH HOH A . 
F 6 HOH 66  366 121 HOH HOH A . 
F 6 HOH 67  367 20  HOH HOH A . 
F 6 HOH 68  368 18  HOH HOH A . 
F 6 HOH 69  369 62  HOH HOH A . 
F 6 HOH 70  370 28  HOH HOH A . 
F 6 HOH 71  371 86  HOH HOH A . 
F 6 HOH 72  372 147 HOH HOH A . 
F 6 HOH 73  373 66  HOH HOH A . 
F 6 HOH 74  374 107 HOH HOH A . 
F 6 HOH 75  375 244 HOH HOH A . 
F 6 HOH 76  376 89  HOH HOH A . 
F 6 HOH 77  377 22  HOH HOH A . 
F 6 HOH 78  378 57  HOH HOH A . 
F 6 HOH 79  379 178 HOH HOH A . 
F 6 HOH 80  380 246 HOH HOH A . 
F 6 HOH 81  381 164 HOH HOH A . 
F 6 HOH 82  382 10  HOH HOH A . 
F 6 HOH 83  383 40  HOH HOH A . 
F 6 HOH 84  384 238 HOH HOH A . 
F 6 HOH 85  385 168 HOH HOH A . 
F 6 HOH 86  386 104 HOH HOH A . 
F 6 HOH 87  387 29  HOH HOH A . 
F 6 HOH 88  388 105 HOH HOH A . 
F 6 HOH 89  389 56  HOH HOH A . 
F 6 HOH 90  390 192 HOH HOH A . 
F 6 HOH 91  391 101 HOH HOH A . 
F 6 HOH 92  392 99  HOH HOH A . 
F 6 HOH 93  393 21  HOH HOH A . 
F 6 HOH 94  394 39  HOH HOH A . 
F 6 HOH 95  395 60  HOH HOH A . 
F 6 HOH 96  396 30  HOH HOH A . 
F 6 HOH 97  397 96  HOH HOH A . 
F 6 HOH 98  398 82  HOH HOH A . 
F 6 HOH 99  399 242 HOH HOH A . 
F 6 HOH 100 400 38  HOH HOH A . 
F 6 HOH 101 401 36  HOH HOH A . 
F 6 HOH 102 402 75  HOH HOH A . 
F 6 HOH 103 403 17  HOH HOH A . 
F 6 HOH 104 404 45  HOH HOH A . 
F 6 HOH 105 405 52  HOH HOH A . 
F 6 HOH 106 406 193 HOH HOH A . 
F 6 HOH 107 407 203 HOH HOH A . 
F 6 HOH 108 408 27  HOH HOH A . 
F 6 HOH 109 409 237 HOH HOH A . 
F 6 HOH 110 410 167 HOH HOH A . 
F 6 HOH 111 411 209 HOH HOH A . 
F 6 HOH 112 412 53  HOH HOH A . 
F 6 HOH 113 413 37  HOH HOH A . 
F 6 HOH 114 414 69  HOH HOH A . 
F 6 HOH 115 415 241 HOH HOH A . 
F 6 HOH 116 416 93  HOH HOH A . 
F 6 HOH 117 417 54  HOH HOH A . 
F 6 HOH 118 418 176 HOH HOH A . 
F 6 HOH 119 419 171 HOH HOH A . 
F 6 HOH 120 420 146 HOH HOH A . 
F 6 HOH 121 421 239 HOH HOH A . 
F 6 HOH 122 422 55  HOH HOH A . 
F 6 HOH 123 423 79  HOH HOH A . 
F 6 HOH 124 424 200 HOH HOH A . 
F 6 HOH 125 425 153 HOH HOH A . 
F 6 HOH 126 426 186 HOH HOH A . 
F 6 HOH 127 427 148 HOH HOH A . 
F 6 HOH 128 428 98  HOH HOH A . 
F 6 HOH 129 429 43  HOH HOH A . 
F 6 HOH 130 430 31  HOH HOH A . 
F 6 HOH 131 431 185 HOH HOH A . 
F 6 HOH 132 432 188 HOH HOH A . 
F 6 HOH 133 433 145 HOH HOH A . 
F 6 HOH 134 434 191 HOH HOH A . 
F 6 HOH 135 435 139 HOH HOH A . 
F 6 HOH 136 436 106 HOH HOH A . 
F 6 HOH 137 437 158 HOH HOH A . 
F 6 HOH 138 438 80  HOH HOH A . 
F 6 HOH 139 439 232 HOH HOH A . 
F 6 HOH 140 440 76  HOH HOH A . 
F 6 HOH 141 441 137 HOH HOH A . 
F 6 HOH 142 442 111 HOH HOH A . 
F 6 HOH 143 443 204 HOH HOH A . 
F 6 HOH 144 444 221 HOH HOH A . 
F 6 HOH 145 445 140 HOH HOH A . 
F 6 HOH 146 446 206 HOH HOH A . 
F 6 HOH 147 447 108 HOH HOH A . 
F 6 HOH 148 448 169 HOH HOH A . 
F 6 HOH 149 449 131 HOH HOH A . 
F 6 HOH 150 450 247 HOH HOH A . 
F 6 HOH 151 451 70  HOH HOH A . 
F 6 HOH 152 452 243 HOH HOH A . 
F 6 HOH 153 453 161 HOH HOH A . 
F 6 HOH 154 454 212 HOH HOH A . 
F 6 HOH 155 455 228 HOH HOH A . 
F 6 HOH 156 456 183 HOH HOH A . 
F 6 HOH 157 457 215 HOH HOH A . 
F 6 HOH 158 458 73  HOH HOH A . 
F 6 HOH 159 459 142 HOH HOH A . 
F 6 HOH 160 460 179 HOH HOH A . 
F 6 HOH 161 461 59  HOH HOH A . 
F 6 HOH 162 462 245 HOH HOH A . 
F 6 HOH 163 463 175 HOH HOH A . 
F 6 HOH 164 464 65  HOH HOH A . 
F 6 HOH 165 465 195 HOH HOH A . 
F 6 HOH 166 466 170 HOH HOH A . 
F 6 HOH 167 467 181 HOH HOH A . 
F 6 HOH 168 468 152 HOH HOH A . 
F 6 HOH 169 469 61  HOH HOH A . 
F 6 HOH 170 470 208 HOH HOH A . 
F 6 HOH 171 471 233 HOH HOH A . 
F 6 HOH 172 472 225 HOH HOH A . 
F 6 HOH 173 473 144 HOH HOH A . 
G 6 HOH 1   201 77  HOH HOH D . 
G 6 HOH 2   202 71  HOH HOH D . 
G 6 HOH 3   203 68  HOH HOH D . 
G 6 HOH 4   204 47  HOH HOH D . 
G 6 HOH 5   205 58  HOH HOH D . 
G 6 HOH 6   206 240 HOH HOH D . 
G 6 HOH 7   207 220 HOH HOH D . 
G 6 HOH 8   208 210 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 D ALA 5   ? CA  ? B ALA 6   CA  
8  1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
9  1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
10 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           7GUN 
_cell.length_a           67.610 
_cell.length_b           67.610 
_cell.length_c           166.280 
_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                         7GUN 
_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          7GUN 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.62 
_exptl_crystal.density_percent_sol   66.03 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    '1.0 M K2HPO4, 0.7 M NaH2PO4, 75 mM sodium acetate pH 4.5, 2% DMSO' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2017-07-31 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9686 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I24' 
_diffrn_source.pdbx_wavelength_list        0.9686 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7GUN 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.900 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   21743 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.099 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.100 
_reflns.B_iso_Wilson_estimate        32.650 
_reflns.pdbx_redundancy              9.000 
_reflns.pdbx_Rrim_I_all              0.106 
_reflns.pdbx_Rpim_I_all              0.035 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     196096 
_reflns.pdbx_scaling_rejects         614 
_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 1.800 1.840  ? 11649 1252 ? 2.014 ? ? ? 9.300 ? 1.100  ? ? ? ? ? ? 100.000 2.131 0.688 0.659 ? 
1 2 9.000 33.900 ? 1521  226  ? 0.047 ? ? ? 6.700 ? 27.300 ? ? ? ? ? ? 98.700  0.050 0.019 0.998 ? 
# 
_refine.entry_id                                 7GUN 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8000 
_refine.ls_d_res_low                             33.9000 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.9000 
_refine.ls_number_reflns_obs                     21664 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1830 
_refine.ls_R_factor_R_work                       0.1810 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2080 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1900 
_refine.ls_number_reflns_R_free                  1125 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               38.8100 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.2274 
_refine.aniso_B[2][2]                            -0.2274 
_refine.aniso_B[3][3]                            0.4547 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9610 
_refine.correlation_coeff_Fo_to_Fc_free          0.9510 
_refine.overall_SU_R_Cruickshank_DPI             0.0950 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0940 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1090 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1030 
_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                                137.970 
_refine.B_iso_min                                19.760 
_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                        7GUN 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.200 
_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                       1.8000 
_refine_hist.d_res_low                        33.9000 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.number_atoms_solvent             181 
_refine_hist.number_atoms_total               1230 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           32.92 
_refine_hist.pdbx_B_iso_mean_solvent          56.90 
_refine_hist.pdbx_number_atoms_protein        1026 
_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        451  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              233  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1236 ?      ? 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        7    ?      ? 1.000  HARMONIC     
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1617 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1236 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1693 0.920  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.360  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    16.300 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.8000 
_refine_ls_shell.d_res_low                        1.8900 
_refine_ls_shell.pdbx_total_number_of_bins_used   11 
_refine_ls_shell.percent_reflns_obs               99.5700 
_refine_ls_shell.number_reflns_R_work             2673 
_refine_ls_shell.R_factor_all                     0.2763 
_refine_ls_shell.R_factor_R_work                  0.2773 
_refine_ls_shell.R_factor_R_free                  0.2551 
_refine_ls_shell.percent_reflns_R_free            4.6000 
_refine_ls_shell.number_reflns_R_free             129 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2802 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUN 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 16.61 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUN 
_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 7GUN       7GUN   ? 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 7GUN A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUN D 1 ? 6   ? 7GUN   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 7GUN GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUN PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUN 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)' 6370  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  13300 ? 
# 
_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 33.8050000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5519775499 0.0000000000 0.0000000000 -1.0000000000 27.7133333333 
# 
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 ? ? ? ? ? ? ? 1.328 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 40 ? O GLU A 41 N VAL A 37 ? N VAL A 38 
AA1 2 3 N VAL A 36 ? N VAL A 37 O ILE A 71 ? O ILE A 72 
# 
_pdbx_entry_details.entry_id                   7GUN 
_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 38.38 48.02   
2 1 SER A 39  ? B 61.62 -109.48 
3 1 SER A 93  ? ? 76.86 -1.45   
4 1 SER A 93  ? ? 76.86 -3.24   
5 1 GLN A 113 ? ? 62.85 61.75   
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             VAL 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              38 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.41 
# 
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 331 ? F HOH . 
2 1 A HOH 381 ? F HOH . 
3 1 A HOH 448 ? F HOH . 
4 1 A HOH 460 ? F HOH . 
5 1 A HOH 463 ? F HOH . 
6 1 A HOH 465 ? 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 29.2805 -16.6200 24.3685 0.0029  -0.0556 -0.0614 -0.0394 0.0262  -0.0173 1.0887 1.9007  2.2565 
0.4718 -0.3011 1.2423 0.1388 -0.0960 -0.0428 -0.0690 0.0992 0.0884 0.2596  0.0143 -0.0466 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.1107 0.1282  -0.0489 -0.0635 -0.0216 -0.0816 0.6493 -0.0099 0.0000 
0.1789 0.0020  0.2199 0.0052 0.0115  -0.0166 0.0080  0.0204 0.0487 -0.0081 0.0131 -0.0020 
# 
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 
7ZO C4   C  Y N 1   
7ZO C5   C  Y N 2   
7ZO C6   C  Y N 3   
7ZO C7   C  Y N 4   
7ZO C8   C  Y N 5   
7ZO C10  C  Y N 6   
7ZO C1   C  Y N 7   
7ZO C2   C  Y N 8   
7ZO C3   C  Y N 9   
7ZO C9   C  Y N 10  
7ZO C11  C  N N 11  
7ZO C12  C  N N 12  
7ZO N13  N  Y N 13  
7ZO N14  N  Y N 14  
7ZO N15  N  N N 15  
7ZO N16  N  N N 16  
7ZO O17  O  N N 17  
7ZO CL1  CL N N 18  
7ZO H1   H  N N 19  
7ZO H2   H  N N 20  
7ZO H3   H  N N 21  
7ZO H4   H  N N 22  
7ZO H5   H  N N 23  
7ZO H6   H  N N 24  
7ZO H7   H  N N 25  
7ZO H8   H  N N 26  
7ZO H9   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 
7ZO O17 C11  doub N N 1   
7ZO C11 C12  sing N N 2   
7ZO C11 N15  sing N N 3   
7ZO C12 C6   sing N N 4   
7ZO N15 C7   sing N N 5   
7ZO C6  C7   doub Y N 6   
7ZO C6  C3   sing Y N 7   
7ZO C7  C1   sing Y N 8   
7ZO C3  C8   doub Y N 9   
7ZO C1  C2   doub Y N 10  
7ZO C8  C2   sing Y N 11  
7ZO C8  N16  sing N N 12  
7ZO N16 C10  sing N N 13  
7ZO C10 N14  doub Y N 14  
7ZO C10 C9   sing Y N 15  
7ZO CL1 C9   sing N N 16  
7ZO N14 C5   sing Y N 17  
7ZO C9  C4   doub Y N 18  
7ZO C5  N13  doub Y N 19  
7ZO C4  N13  sing Y N 20  
7ZO C4  H1   sing N N 21  
7ZO C5  H2   sing N N 22  
7ZO C1  H3   sing N N 23  
7ZO C2  H4   sing N N 24  
7ZO C3  H5   sing N N 25  
7ZO C12 H6   sing N N 26  
7ZO C12 H7   sing N N 27  
7ZO N15 H8   sing N N 28  
7ZO N16 H9   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_1002059 
_pdbx_deposit_group.group_title         'X-ray dose series of B-cell lymphoma 6 protein BTB domain in complex with ligand 1' 
_pdbx_deposit_group.group_description   
;Crystal structures of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 solved at increasing X-ray dose using Many Structures One Crystal (MSOX) crystallography.
;
_pdbx_deposit_group.group_type          undefined 
# 
_atom_sites.entry_id                    7GUN 
_atom_sites.fract_transf_matrix[1][1]   0.014791 
_atom_sites.fract_transf_matrix[1][2]   0.008539 
_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]   0.017079 
_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]   0.006014 
_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 
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   ? 17.572 -21.150 -4.936 1.00 71.03  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.435 -22.061 -5.693 1.00 70.03  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.934 -23.525 -5.607 1.00 69.99  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.844 -23.777 -5.081 1.00 70.74  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.897 -21.945 -5.193 1.00 70.67  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.943 -22.014 -6.296 1.00 84.40  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 20.998 -23.049 -7.006 1.00 85.37  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.717 -21.040 -6.442 1.00 90.93  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.726 -24.477 -6.137 1.00 61.50  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.429 -25.909 -6.111 1.00 59.01  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.412 -26.669 -5.165 1.00 54.83  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.701 -27.848 -5.379 1.00 54.52  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.472 -26.475 -7.526 1.00 64.80  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.735 -26.259 -8.134 1.00 77.36  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.898 -25.991 -4.106 1.00 44.98  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.831 -26.574 -3.133 1.00 41.23  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.208 -27.739 -2.332 1.00 40.49  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.991 -27.808 -2.181 1.00 41.42  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.330 -25.489 -2.177 1.00 41.85  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.441 -24.258 -2.925 1.00 46.77  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.047 -28.631 -1.799 1.00 30.80  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.659 -29.629 -0.799 1.00 28.02  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.267 -29.093 0.497  1.00 30.15  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.218 -28.309 0.444  1.00 28.55  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 21.028 -31.107 -1.106 1.00 31.05  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.553 -31.275 -1.384 1.00 30.96  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.174 -31.638 -2.268 1.00 32.62  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.069 -32.728 -1.547 1.00 34.78  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.777 -29.525 1.654  0.57 25.62  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.677 -29.449 1.637  0.43 25.72  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.308 -29.006 2.913  0.57 24.43  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.109 -28.978 2.948  0.43 24.45  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.644 -30.127 3.895  0.57 27.55  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.565 -30.139 3.819  0.43 26.88  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.845 -31.051 4.051  0.57 27.20  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.935 -31.195 3.816  0.43 26.53  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.291 -28.010 3.520  0.57 25.96  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.959 -28.197 3.635  0.43 25.92  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.698 -27.390 4.860  0.57 24.66  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.174 -27.909 5.142  0.43 34.01  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.520 -26.723 5.531  0.57 51.53  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.097 -26.455 5.541  0.43 42.79  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.546 -27.366 5.939  0.57 43.27  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.779 -25.562 4.739  0.43 31.94  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.584 -25.410 5.661  0.57 54.76  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.389 -26.188 6.813  0.43 32.49  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.811 -30.042 4.564  0.78 25.07  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.639 -29.922 4.584  0.22 23.29  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.201 -31.044 5.558  0.78 24.84  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.162 -30.891 5.537  0.22 22.98  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.719 -30.545 6.916  0.78 26.97  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.649 -30.435 6.888  0.22 26.53  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.276 -29.587 7.463  0.78 25.76  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 23.087 -29.394 7.393  0.22 25.50  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.730 -31.331 5.537  0.78 26.11  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.697 -30.937 5.465  0.22 24.13  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.105 -32.549 6.359  0.78 27.39  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.188 -31.848 4.366  0.22 26.32  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.689 -33.825 5.981  0.78 31.58  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 25.063 -31.486 3.028  0.22 29.88  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.854 -32.418 7.525  0.78 29.52  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.738 -33.087 4.665  0.22 29.22  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 25.015 -34.947 6.761  0.78 32.30  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.504 -32.335 2.013  0.22 31.22  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.179 -33.534 8.300  0.78 32.12  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.172 -33.938 3.646  0.22 32.66  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.757 -34.789 7.917  0.78 30.55  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 26.064 -33.550 2.332  0.22 30.67  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.641 -31.156 7.423  1.00 23.90  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.965 -30.771 8.680  1.00 24.32  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.913 -30.540 9.883  1.00 27.05  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.773 -29.523 10.567 1.00 25.64  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.876 -31.795 9.023  1.00 32.71  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.957 -31.865 7.921  1.00 31.33  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.102 -31.431 10.307 1.00 36.61  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.861 -31.465 10.112 0.50 24.44  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.856 -31.468 10.118 0.50 24.67  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.782 -31.401 11.256 0.50 24.68  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.784 -31.404 11.257 0.50 25.00  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 25.031 -30.528 11.049 0.50 26.09  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 25.018 -30.509 11.059 0.50 26.18  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.849 -30.441 11.968 0.50 24.40  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.817 -30.393 11.993 0.50 24.44  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.199 -32.827 11.685 0.50 28.51  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.231 -32.827 11.640 0.50 29.49  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.054 -33.706 12.227 0.50 35.12  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.268 -33.545 12.591 0.50 40.27  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.497 -33.227 13.561 0.50 47.78  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 22.991 -34.988 12.209 0.50 48.87  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.431 -33.424 14.674 0.50 55.39  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.201 -35.760 11.906 0.50 50.73  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.394 -32.744 15.817 0.50 62.85  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.363 -36.491 10.807 0.50 60.09  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.485 -31.794 16.004 0.50 42.41  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.488 -37.166 10.612 0.50 52.99  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.271 -33.000 16.776 0.50 51.03  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.396 -36.565 9.901  0.50 36.27  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.187 -29.893 9.870  1.00 22.20  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.386 -29.086 9.558  1.00 22.09  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.666 -27.982 10.570 1.00 24.85  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.794 -27.916 11.075 1.00 23.58  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.366 -28.517 8.125  1.00 21.78  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.648 -27.783 7.804  1.00 23.37  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.830 -28.462 7.650  1.00 23.76  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.884 -26.454 7.671  1.00 23.98  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.755 -27.545 7.403  1.00 23.36  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.231 -26.319 7.395  1.00 23.36  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.671 -27.097 10.846 1.00 22.04  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.893 -25.975 11.776 1.00 21.59  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.313 -26.459 13.181 1.00 23.92  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.230 -25.887 13.763 1.00 21.92  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.652 -25.084 11.855 1.00 23.05  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.650 -27.503 13.700 0.38 21.89  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.654 -27.510 13.697 0.33 22.07  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.650 -27.508 13.706 0.29 21.58  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.946 -28.081 15.009 0.38 22.24  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.943 -28.099 15.006 0.33 22.52  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.954 -28.076 15.022 0.29 21.79  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.358 -28.678 15.040 0.38 26.53  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.353 -28.691 15.043 0.33 26.85  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.352 -28.705 15.056 0.29 26.65  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.081 -28.465 16.017 0.38 24.28  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.067 -28.491 16.028 0.33 24.99  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.059 -28.544 16.053 0.29 25.07  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.897 -29.127 15.382 0.38 26.35  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.903 -29.160 15.357 0.33 26.88  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.881 -29.076 15.450 0.29 25.19  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.124 -29.635 16.686 0.38 31.26  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.598 -28.608 15.362 0.33 33.25  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.840 -30.208 14.598 0.29 28.40  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.756 -29.389 13.961 1.00 24.75  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.097 -30.009 13.832 1.00 25.41  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.171 -28.910 13.794 1.00 25.23  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.221 -29.064 14.417 1.00 24.91  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.181 -30.865 12.556 1.00 27.45  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.423 -32.194 12.638 1.00 39.45  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.884 -32.510 13.729 1.00 39.41  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.360 -32.911 11.606 1.00 39.63  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.900 -27.793 13.066 1.00 21.26  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.835 -26.657 13.030 1.00 20.46  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 31.023 -26.098 14.463 1.00 22.98  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.148 -25.895 14.907 1.00 22.19  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.346 -25.549 12.055 1.00 22.56  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.099 -24.235 12.280 1.00 22.46  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.446 -26.009 10.599 1.00 21.97  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.920 -25.847 15.175 1.00 21.52  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 30.017 -25.271 16.519 1.00 21.68  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.758 -26.205 17.487 1.00 24.68  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.611 -25.734 18.258 1.00 22.58  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.635 -24.875 17.060 1.00 23.06  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.660 -23.925 18.290 1.00 25.91  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.212 -22.529 17.924 1.00 26.06  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.253 -23.794 18.881 1.00 29.93  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.482 -27.521 17.390 1.00 22.89  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.158 -28.554 18.196 1.00 24.41  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.681 -28.500 17.947 1.00 24.61  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.470 -28.485 18.904 1.00 23.22  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.595 -29.941 17.839 1.00 26.61  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.182 -31.116 18.600 1.00 35.00  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.777 -31.057 20.087 1.00 36.90  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.675 -32.424 18.013 1.00 40.22  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.088 -28.385 16.674 1.00 21.18  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.504 -28.278 16.322 1.00 21.48  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.137 -26.971 16.809 1.00 23.87  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.293 -26.977 17.236 1.00 23.47  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.700 -28.505 14.830 1.00 22.77  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.642 -29.971 14.485 1.00 34.03  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.799 -30.836 15.355 1.00 30.33  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.381 -30.284 13.220 1.00 26.30  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.392 -25.850 16.734 1.00 21.54  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.868 -24.559 17.259 1.00 21.23  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.079 -24.690 18.767 1.00 23.23  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.081 -24.194 19.293 1.00 21.05  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.887 -23.405 16.937 1.00 20.90  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.794 -23.043 15.436 1.00 24.18  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.736 -21.962 15.210 1.00 23.88  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.151 -22.567 14.881 1.00 26.95  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.150 -25.372 19.469 1.00 19.98  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.330 -25.578 20.920 1.00 21.13  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.565 -26.476 21.233 1.00 26.01  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.270 -26.227 22.218 1.00 26.89  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.077 -26.157 21.556 1.00 23.71  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.101 -26.009 23.063 1.00 29.25  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.594 -25.025 23.610 1.00 27.44  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.570 -26.979 23.744 1.00 30.41  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.839 -27.492 20.389 1.00 23.66  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 37.038 -28.352 20.555 1.00 24.90  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.312 -27.518 20.370 1.00 28.34  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.254 -27.695 21.117 1.00 28.42  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 37.050 -29.497 19.536 1.00 24.59  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 36.054 -30.601 19.858 1.00 31.51  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.803 -31.476 18.640 1.00 36.46  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.967 -32.622 18.978 1.00 41.18  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.487 -33.497 18.101 1.00 60.96  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.706 -33.335 16.798 1.00 45.55  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.774 -34.536 18.516 1.00 48.74  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.318 -26.567 19.409 1.00 25.05  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.465 -25.676 19.237 1.00 24.00  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.633 -24.796 20.483 1.00 27.52  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.760 -24.645 20.988 1.00 27.12  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.282 -24.797 18.012 1.00 23.20  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.269 -25.504 16.632 1.00 26.86  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.098 -24.466 15.534 1.00 26.66  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.563 -26.339 16.402 1.00 29.11  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.513 -24.263 21.016 1.00 23.88  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.577 -23.469 22.253 1.00 25.13  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.196 -24.283 23.427 1.00 30.50  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.087 -23.763 24.125 1.00 30.66  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.185 -22.942 22.652 1.00 26.02  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.266 -22.060 23.912 1.00 30.80  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.944 -21.432 24.257 1.00 31.07  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.933 -22.417 24.642 1.00 30.95  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.346 -22.465 25.832 1.00 44.75  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.727 -21.641 26.804 1.00 37.90  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.400 -23.361 26.074 1.00 32.09  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.709 -25.514 23.648 0.40 28.88  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.712 -25.521 23.646 0.35 28.72  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.713 -25.525 23.645 0.25 28.22  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.189 -26.407 24.709 0.40 30.51  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.173 -26.414 24.720 0.35 30.27  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.165 -26.436 24.709 0.25 29.57  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.699 -26.589 24.626 0.40 35.61  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.669 -26.737 24.628 0.35 35.62  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.661 -26.758 24.623 0.25 35.22  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.386 -26.524 25.649 0.40 36.51  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.313 -26.944 25.659 0.35 36.51  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.294 -26.996 25.654 0.25 36.03  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.536 -27.781 24.587 0.40 34.82  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.350 -27.700 24.747 0.35 34.25  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.349 -27.725 24.693 0.25 32.93  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.142 -27.749 24.827 0.40 42.90  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.620 -28.537 23.634 0.35 42.22  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.809 -28.661 25.656 0.25 40.31  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.213 -26.787 23.399 1.00 31.83  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.637 -27.063 23.151 1.00 33.63  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.450 -25.780 22.964 1.00 36.45  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.658 -25.850 22.732 1.00 37.09  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.776 -28.025 21.971 1.00 36.24  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 42.010 -29.330 22.191 1.00 44.93  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 41.996 -30.200 20.956 1.00 52.84  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.321 -30.764 20.701 1.00 71.08  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.841 -30.925 19.491 1.00 89.23  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.053 -31.441 19.347 1.00 80.90  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.156 -30.565 18.417 1.00 75.25  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.786 -24.610 23.097 1.00 30.60  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.378 -23.269 22.957 1.00 31.67  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 44.004 -23.069 21.549 1.00 36.01  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.080 -22.481 21.403 1.00 37.06  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.405 -22.990 24.095 1.00 35.30  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.737 -21.525 24.267 1.00 43.93  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.824 -20.680 24.077 1.00 42.13  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.903 -21.217 24.590 1.00 50.03  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.338 -23.594 20.523 1.00 29.61  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.839 -23.501 19.152 1.00 28.28  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.224 -22.311 18.447 1.00 31.00  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 41.983 -22.194 18.364 1.00 28.33  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.643 -24.822 18.358 1.00 31.13  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.446 -25.990 18.993 1.00 32.65  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.997 -24.642 16.857 1.00 30.52  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.912 -27.400 18.516 1.00 34.85  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.094 -21.426 17.927 0.54 28.75  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.100 -21.428 17.930 0.46 29.17  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.735 -20.228 17.164 0.54 28.13  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.768 -20.220 17.173 0.46 28.82  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.846 -19.235 17.928 0.54 30.64  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.858 -19.236 17.926 0.46 30.99  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.201 -18.390 17.303 0.54 29.29  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.212 -18.397 17.294 0.46 29.71  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.114 -20.584 15.798 0.54 28.09  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.207 -20.556 15.789 0.46 29.02  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 44.036 -21.222 14.732 0.54 33.83  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.244 -20.463 14.674 0.46 35.24  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.493 -20.960 13.370 0.54 32.46  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.490 -21.817 14.033 0.46 35.56  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.465 -20.676 14.787 0.54 37.25  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.835 -19.440 13.647 0.46 37.39  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.860 -19.291 19.274 1.00 27.19  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.133 -18.310 20.099 1.00 27.02  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.957 -17.017 19.906 1.00 33.59  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.188 -17.082 19.780 1.00 33.79  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.065 -18.723 21.571 1.00 33.11  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.374 -19.063 21.989 1.00 34.37  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.098 -19.887 21.809 1.00 31.37  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.284 -15.887 19.738 1.00 30.08  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.959 -14.639 19.394 1.00 30.27  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.635 -13.486 20.316 1.00 31.52  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.994 -12.341 20.025 1.00 31.39  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.645 -14.280 17.927 1.00 31.44  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.163 -14.292 17.565 1.00 40.90  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.319 -14.355 18.490 1.00 37.01  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.850 -14.251 16.361 1.00 49.78  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.967 -13.775 21.438 1.00 26.61  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.646 -12.734 22.417 1.00 26.07  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.469 -13.323 23.806 1.00 29.01  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.083 -14.494 23.950 1.00 28.72  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.386 -11.893 21.970 1.00 29.17  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 39.070 -12.675 22.126 1.00 27.38  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.314 -10.530 22.693 1.00 29.04  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.756 -12.502 24.827 0.53 26.35  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.771 -12.517 24.832 0.47 26.64  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.533 -12.816 26.232 0.53 25.94  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.503 -12.875 26.215 0.47 26.42  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.474 -11.825 26.721 0.53 29.14  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.513 -11.845 26.782 0.47 29.58  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.629 -10.613 26.528 0.53 29.29  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.721 -10.634 26.643 0.47 29.83  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.834 -12.726 27.077 0.53 30.52  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.752 -13.153 27.101 0.47 31.29  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.562 -12.971 28.563 0.53 30.79  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.578 -11.899 27.363 0.47 32.20  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.890 -13.689 26.562 0.53 30.89  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.356 -13.823 28.412 0.47 31.45  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.407 -12.335 27.342 1.00 25.57  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.359 -11.508 27.940 1.00 25.10  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.642 -11.550 29.438 1.00 30.60  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.642 -12.636 30.039 1.00 29.54  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.918 -11.993 27.609 1.00 26.64  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.675 -12.143 26.079 1.00 25.74  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.877 -11.101 28.258 1.00 28.30  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 37.018 -10.906 25.186 1.00 26.70  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.882 -10.371 30.027 1.00 27.57  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.196 -10.228 31.456 1.00 28.09  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.927 -9.788  32.186 1.00 31.88  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.326 -8.757  31.838 1.00 29.97  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.391 -9.259  31.700 1.00 32.58  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.731 -9.145  33.188 1.00 33.57  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.627 -9.695  30.922 1.00 33.19  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.531 -10.566 33.213 1.00 29.29  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.328 -10.329 34.009 1.00 29.25  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.797 -10.385 35.450 1.00 34.57  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 37.041 -11.473 35.971 1.00 32.50  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.202 -11.350 33.685 1.00 32.77  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.894 -10.947 34.353 1.00 32.82  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 35.005 -11.504 32.167 1.00 31.59  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.695 -9.267  36.203 0.50 34.39  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.297 -9.189  35.849 0.50 31.43  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 37.053 -9.245  37.637 0.50 36.45  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.967 -8.832  37.086 0.50 32.18  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.317 -10.114 37.953 0.50 41.91  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.260 -9.644  37.229 0.50 35.22  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.280 -10.952 38.857 0.50 42.31  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.172 -9.413  36.434 0.50 33.76  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.864 -9.685  38.501 0.50 42.00  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 37.017 -8.904  38.275 0.50 36.76  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.761 -8.789  38.449 0.50 52.95  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.069 -7.854  38.146 0.50 44.63  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.402 -9.940  37.151 0.50 38.44  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.344 -10.615 38.161 0.50 32.25  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.686 -10.665 37.243 0.50 38.99  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.578 -11.394 38.283 0.50 33.26  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.564 -12.204 37.003 0.50 41.15  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.709 -12.427 37.118 0.50 37.97  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.326 -13.009 37.570 0.50 41.72  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.738 -12.458 36.424 0.50 38.08  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.443 -10.362 38.554 0.50 41.46  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.729 -12.016 39.697 0.50 34.05  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 42.020 -8.956  38.656 0.50 53.20  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 41.025 -10.965 40.791 0.50 42.53  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.051 -8.908  39.766 0.50 60.23  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.346 -11.566 42.154 0.50 41.50  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.435 -7.542  40.125 0.50 66.56  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.518 -10.548 43.196 0.50 42.68  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.841 -6.816  41.068 0.50 78.80  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.684 -10.013 43.554 0.50 58.43  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.809 -7.307  41.744 0.50 63.58  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.805 -10.372 42.941 0.50 47.46  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.267 -5.588  41.333 0.50 65.54  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.736 -9.105  44.517 0.50 49.16  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.601 -12.596 36.160 0.50 34.23  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.620 -13.159 36.834 0.50 32.46  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.399 -13.970 35.695 0.50 33.53  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.562 -14.231 35.830 0.50 31.52  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.537 -13.862 34.184 0.50 34.49  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.805 -13.793 34.376 0.50 33.16  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.951 -12.956 33.580 0.50 31.68  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.477 -12.675 33.985 0.50 30.29  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 38.034 -14.542 36.119 0.50 34.84  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.235 -15.009 35.931 0.50 32.68  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.927 -14.771 37.620 0.50 48.25  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.743 -15.185 37.363 0.50 48.27  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.868 -16.220 38.064 0.50 83.69  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.907 -16.543 38.019 0.50 85.21  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.826 -16.622 38.630 0.50 86.46  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.969 -17.183 37.835 0.50 87.78  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.862 -16.952 37.852 0.50 84.10  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 36.974 -16.955 38.746 0.50 86.49  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.368 -14.720 33.579 1.00 30.75  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.681 -14.589 32.162 1.00 30.09  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 40.057 -15.710 31.358 1.00 33.05  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.105 -16.866 31.777 1.00 33.65  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.207 -14.573 31.974 1.00 32.96  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.879 -13.345 32.573 1.00 47.12  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.355 -13.231 32.268 1.00 68.72  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.930 -13.961 31.445 1.00 61.42  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 45.002 -12.291 32.933 1.00 72.61  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.466 -15.370 30.206 1.00 27.03  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.822 -16.360 29.331 1.00 26.47  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.333 -16.182 27.919 1.00 30.20  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.170 -15.106 27.346 1.00 29.84  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.288 -16.189 29.350 1.00 28.21  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.665 -16.277 30.721 1.00 30.11  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.536 -15.142 31.521 1.00 32.03  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.173 -17.487 31.201 1.00 32.30  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 35.966 -15.223 32.793 1.00 33.98  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.604 -17.568 32.476 1.00 35.25  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.499 -16.435 33.264 1.00 33.21  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.933 -17.233 27.345 1.00 26.59  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.449 -17.185 25.976 1.00 25.79  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.328 -17.596 25.026 1.00 29.72  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.537 -18.496 25.343 1.00 28.70  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.673 -18.110 25.809 1.00 27.18  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.905 -17.679 26.654 1.00 36.49  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.233 -18.076 26.004 1.00 47.62  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.250 -17.665 24.592 1.00 59.35  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.870 -16.592 24.110 1.00 70.85  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.628 -15.844 24.899 1.00 62.38  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.779 -16.291 22.822 1.00 52.45  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.221 -16.923 23.871 1.00 25.75  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.143 -17.250 22.918 1.00 25.37  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.536 -16.829 21.515 1.00 26.42  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.627 -16.282 21.300 1.00 25.69  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.842 -16.540 23.326 1.00 26.47  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.645 -17.097 20.556 1.00 22.34  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.807 -16.673 19.173 1.00 22.18  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.924 -15.425 18.986 1.00 26.09  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.708 -15.465 19.260 1.00 24.64  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.360 -17.798 18.210 1.00 22.05  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.113 -19.092 18.413 1.00 25.82  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.594 -20.123 19.185 1.00 27.88  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.346 -19.455 17.977 1.00 26.54  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.520 -21.078 19.191 1.00 26.88  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.585 -20.728 18.461 1.00 26.82  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.528 -14.332 18.529 1.00 24.35  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.807 -13.086 18.245 1.00 24.26  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.575 -13.320 17.377 1.00 26.42  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.522 -12.786 17.704 1.00 24.47  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.722 -12.091 17.520 1.00 27.09  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.721 -11.453 18.460 1.00 24.44  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.643 -10.509 17.679 1.00 26.80  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.800 -10.107 18.546 1.00 31.98  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.720 -9.193  17.826 1.00 34.58  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.688 -14.138 16.303 1.00 22.42  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.541 -14.340 15.403 1.00 22.20  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.357 -15.010 16.074 1.00 24.35  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.227 -14.640 15.779 1.00 23.29  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.934 -15.056 14.120 1.00 30.03  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.524 -16.289 14.480 1.00 30.94  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.859 -14.204 13.249 1.00 31.45  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.606 -15.972 16.961 1.00 21.72  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.513 -16.668 17.671 1.00 21.77  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.842 -15.671 18.626 1.00 24.15  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.600 -15.620 18.720 1.00 22.18  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 33.025 -17.934 18.415 1.00 24.05  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.920 -18.536 19.295 1.00 23.88  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.517 -18.981 17.408 1.00 23.71  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.668 -14.882 19.355 1.00 21.19  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.121 -13.860 20.275 1.00 21.44  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.236 -12.857 19.504 1.00 23.85  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.139 -12.538 19.951 1.00 22.19  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.269 -13.086 20.963 1.00 21.47  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.188 -13.877 21.923 1.00 24.93  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.241 -12.931 22.535 1.00 25.02  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.389 -14.563 23.029 1.00 26.49  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.692 -12.403 18.331 1.00 21.19  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.910 -11.470 17.501 1.00 22.16  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.619 -12.118 17.011 1.00 26.02  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.573 -11.465 17.024 1.00 26.25  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.714 -10.989 16.292 1.00 23.92  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.910 -10.156 16.667 1.00 26.72  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.940 -10.062 15.209 1.00 31.06  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.158 -8.726  14.381 1.00 27.52  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.677 -13.409 16.613 1.00 23.27  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.503 -14.128 16.105 1.00 23.16  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.394 -14.304 17.172 1.00 25.23  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.232 -14.490 16.823 1.00 25.98  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.920 -15.496 15.543 1.00 23.38  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.765 -14.253 18.459 1.00 22.22  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.863 -14.495 19.585 1.00 22.54  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.421 -13.272 20.362 1.00 26.19  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.458 -13.371 21.133 1.00 25.72  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.525 -15.486 20.539 1.00 23.02  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.838 -17.114 19.823 1.00 26.51  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.173 -12.171 20.271 1.00 22.87  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.964 -11.035 21.155 1.00 21.50  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 27.009 -9.708  20.429 1.00 26.95  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.977 -9.433  19.714 1.00 24.57  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.055 -11.102 22.223 1.00 23.53  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.440 -9.854  22.775 1.00 27.38  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.976 -8.888  20.635 1.00 25.23  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.915 -7.554  20.047 1.00 25.28  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 27.036 -6.667  20.551 1.00 28.64  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.546 -5.826  19.800 1.00 28.42  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.452 -6.867  21.828 1.00 26.36  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.548 -6.085  22.407 1.00 26.02  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.868 -6.434  21.715 1.00 27.30  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.548 -5.514  21.252 1.00 27.13  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.664 -6.284  23.933 1.00 25.74  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.693 -5.368  24.618 1.00 30.70  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.211 -3.888  24.646 1.00 31.68  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 30.010 -5.861  26.013 1.00 31.15  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.199 -7.747  21.587 1.00 23.13  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.459 -8.128  20.917 1.00 22.34  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.446 -7.789  19.449 1.00 26.92  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.487 -7.409  18.916 1.00 25.88  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.838 -9.581  21.174 1.00 22.56  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.246 -9.806  22.617 1.00 23.43  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.348 -9.143  23.161 1.00 26.00  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.579 -10.741 23.407 1.00 25.28  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.724 -9.346  24.502 1.00 26.96  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 31.998 -10.997 24.726 1.00 28.05  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 33.050 -10.277 25.272 1.00 25.87  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.267 -7.860  18.802 1.00 25.08  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.155 -7.453  17.402 1.00 25.95  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.586 -5.973  17.231 1.00 30.16  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.375 -5.668  16.336 1.00 28.35  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.727 -7.694  16.901 1.00 28.41  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.496 -7.166  15.507 1.00 32.27  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 29.041 -7.805  14.399 1.00 33.89  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.716 -6.036  15.295 1.00 36.42  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.822 -7.323  13.107 1.00 35.80  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.489 -5.548  14.013 1.00 39.47  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.041 -6.196  12.925 1.00 45.80  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.799 -5.695  11.680 1.00 51.49  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.076 -5.074  18.091 0.52 27.44  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 30.070 -5.081  18.097 0.48 27.79  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.396 -3.644  18.076 0.52 28.89  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.378 -3.650  18.113 0.48 29.36  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.879 -3.401  18.393 0.52 33.98  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.875 -3.429  18.375 0.48 34.02  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.513 -2.596  17.716 0.52 35.33  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.510 -2.676  17.644 0.48 35.10  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.494 -2.896  19.053 0.52 31.09  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.541 -2.951  19.184 0.48 32.19  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.150 -2.937  18.603 0.52 33.23  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.783 -1.554  19.191 0.48 38.82  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.435 -4.126  19.388 1.00 29.97  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.847 -4.023  19.793 1.00 29.20  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.791 -4.420  18.669 1.00 32.19  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.694 -3.647  18.335 1.00 33.87  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.163 -4.853  21.099 1.00 30.55  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.445 -4.276  22.332 1.00 31.20  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.691 -4.953  21.357 1.00 28.30  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.385 -5.266  23.553 1.00 34.56  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.606 -5.615  18.091 1.00 26.62  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.580 -6.066  17.101 1.00 26.81  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.334 -5.530  15.687 1.00 31.52  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.183 -5.752  14.828 1.00 32.34  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.755 -7.595  17.143 1.00 27.24  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.166 -8.091  18.516 1.00 27.63  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.355 -7.658  19.109 1.00 30.83  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.344 -8.944  19.235 1.00 28.08  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.730 -8.116  20.380 1.00 31.00  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.722 -9.410  20.503 1.00 31.00  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.903 -8.987  21.071 1.00 29.25  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.268 -4.739  15.460 1.00 29.10  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.106 -4.048  14.167 1.00 30.15  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.657 -2.618  14.293 1.00 37.42  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.720 -1.875  13.308 1.00 37.13  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.682 -4.080  13.613 1.00 36.91  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.791 -3.577  14.597 1.00 35.33  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.256 -5.477  13.113 1.00 33.44  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.086 -2.238  15.506 1.00 34.61  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.694 -0.932  15.719 1.00 36.00  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.132 -1.009  15.199 1.00 41.87  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.880 -1.890  15.617 1.00 39.94  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.671 -0.546  17.206 1.00 37.42  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.428 0.741   17.432 1.00 51.28  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.821 1.815   17.270 1.00 56.77  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.653 0.673   17.696 1.00 52.68  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.528 -0.053  14.331 1.00 43.05  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.844 -0.011  13.689 1.00 44.47  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 40.042 -0.066  14.652 1.00 49.08  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 41.086 -0.574  14.246 1.00 51.33  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.966 1.193   12.744 1.00 48.03  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 38.125 1.060   11.477 1.00 67.65  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.918 0.459   15.896 1.00 42.40  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 41.012 0.395   16.874 1.00 41.09  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.938 -0.853  17.731 1.00 44.12  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.967 -1.446  18.038 1.00 45.85  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 40.998 1.606   17.828 1.00 41.77  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.640 2.898   17.350 1.00 48.70  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.454 3.971   18.379 1.00 49.17  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.135 2.728   17.068 1.00 53.33  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.737 -1.197  18.205 1.00 37.44  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.563 -2.316  19.130 1.00 35.74  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.686 -3.677  18.468 1.00 39.93  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 40.044 -4.631  19.152 1.00 37.84  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.237 -2.212  19.901 1.00 36.72  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.116 -0.988  20.788 1.00 36.66  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.843 -1.074  21.613 1.00 32.85  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.528 0.236   22.308 1.00 38.83  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.929 1.240   21.396 1.00 38.38  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.409 -3.765  17.148 1.00 39.53  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.495 -5.018  16.377 1.00 39.82  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.887 -5.657  16.505 1.00 44.97  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 41.017 -6.870  16.326 1.00 44.82  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.122 -4.787  14.912 1.00 41.20  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.325 -3.793  13.970 1.00 47.36  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.915 -4.820  16.803 1.00 41.44  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.320 -5.204  16.925 1.00 42.17  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.804 -5.495  18.350 1.00 44.38  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.975 -5.834  18.544 1.00 44.40  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.216 -4.146  16.258 1.00 44.14  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 44.011 -4.089  14.756 1.00 59.86  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 43.973 -3.015  14.155 1.00 59.05  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.833 -5.243  14.117 1.00 50.43  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.920 -5.381  19.338 1.00 39.87  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.307 -5.642  20.720 1.00 39.05  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.292 -7.145  20.996 1.00 40.07  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.412 -7.838  20.480 1.00 38.18  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.330 -4.935  21.681 1.00 39.30  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.334 -3.398  21.653 1.00 44.48  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.283 -2.851  22.588 1.00 44.53  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.724 -2.819  22.012 1.00 45.86  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.253 -7.626  21.817 1.00 36.27  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.365 -9.037  22.206 0.42 35.58  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.330 -9.044  22.188 0.58 35.80  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.734 -9.248  23.585 1.00 36.86  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.536 -10.382 24.015 1.00 33.23  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.830 -9.471  22.228 0.42 40.38  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.772 -9.544  22.127 0.58 40.74  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.427 -9.356  20.947 0.42 46.77  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.603 -8.813  23.013 0.58 47.89  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.453 -8.143  24.299 1.00 33.37  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.851 -8.171  25.638 1.00 32.46  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.676 -7.188  25.676 1.00 34.41  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.832 -6.019  25.281 1.00 34.27  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.900 -7.831  26.749 1.00 38.09  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.276 -7.857  28.147 1.00 38.08  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 45.116 -8.756  26.686 1.00 38.84  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.514 -7.656  26.175 1.00 28.12  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.311 -6.846  26.387 1.00 27.38  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.922 -6.953  27.856 1.00 30.83  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.721 -8.058  28.355 1.00 30.74  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.141 -7.218  25.421 1.00 28.78  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.540 -7.083  23.918 1.00 29.66  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.844 -6.433  25.740 1.00 29.84  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.907 -5.634  23.401 1.00 34.20  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.787 -5.809  28.545 1.00 28.39  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.380 -5.815  29.941 1.00 28.79  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.900 -5.473  30.048 1.00 31.08  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.478 -4.387  29.618 1.00 29.44  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.199 -4.790  30.752 1.00 32.82  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.685 -4.979  30.672 1.00 51.84  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.223 -5.993  31.092 1.00 41.76  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.385 -3.997  30.151 1.00 49.63  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.125 -6.355  30.668 1.00 26.37  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.706 -6.091  30.859 1.00 25.96  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.467 -5.200  32.071 1.00 29.89  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.340 -5.066  32.940 1.00 31.13  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.886 -7.393  30.979 1.00 25.61  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.963 -8.402  29.805 1.00 29.22  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.831 -9.460  29.933 1.00 29.20  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.926 -7.700  28.436 1.00 29.65  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.274 -4.614  32.138 1.00 26.74  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.850 -3.722  33.225 1.00 28.66  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 33.015 -4.473  34.568 1.00 33.99  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.650 -5.646  34.642 1.00 32.50  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.379 -3.319  33.003 1.00 30.29  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.840 -2.287  33.981 1.00 40.85  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.686 -2.622  35.176 1.00 41.57  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.537 -1.161  33.545 1.00 44.37  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.600 -3.838  35.609 1.00 35.00  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.812 -4.559  36.886 1.00 35.47  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.570 -5.116  37.560 1.00 38.96  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.706 -5.971  38.429 1.00 40.65  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.501 -3.521  37.783 1.00 38.26  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.200 -2.186  37.151 1.00 43.63  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.130 -2.457  35.676 1.00 37.74  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.370 -4.667  37.169 1.00 34.89  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.135 -5.194  37.757 1.00 35.86  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.825 -6.598  37.205 1.00 36.15  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.981 -7.294  37.765 1.00 35.54  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.948 -4.246  37.498 1.00 38.61  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.911 -3.035  38.419 1.00 59.33  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.371 -3.315  39.808 1.00 92.94  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.142 -3.522  39.939 1.00 94.02  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.178 -3.333  40.766 1.00 93.20  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.495 -7.004  36.106 1.00 30.91  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.255 -8.315  35.502 1.00 30.16  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.854 -9.429  36.342 1.00 34.43  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 32.031 -9.404  36.684 1.00 33.38  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.690 -8.376  34.014 1.00 31.84  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.946 -7.292  33.179 1.00 33.30  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.497 -9.801  33.422 1.00 28.71  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.314 -7.318  33.257 1.00 39.13  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 30.025 -10.411 36.634 1.00 33.41  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.352 -11.586 37.418 1.00 33.97  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.076 -12.631 36.545 1.00 34.44  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.545 -13.013 35.503 1.00 31.93  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 29.040 -12.145 38.004 1.00 36.95  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.202 -13.439 38.750 1.00 54.43  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.880 -14.506 38.233 1.00 42.40  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.703 -13.370 39.977 1.00 46.93  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.278 -13.123 36.952 1.00 31.94  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.983 -14.132 36.130 1.00 31.08  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.191 -15.421 35.868 1.00 34.37  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.269 -15.954 34.759 1.00 33.05  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.248 -14.419 36.944 1.00 34.03  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.450 -13.175 37.771 1.00 39.06  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.067 -12.773 38.151 1.00 34.73  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.431 -15.920 36.864 1.00 31.23  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.657 -17.159 36.657 1.00 31.43  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.576 -16.944 35.586 1.00 32.70  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.466 -17.765 34.686 1.00 30.38  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.056 -17.682 37.971 1.00 34.15  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.403 -19.049 37.792 1.00 46.78  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.574 -19.582 38.947 1.00 74.69  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.585 -20.816 39.155 1.00 76.28  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 27.902 -18.777 39.634 1.00 70.74  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.856 -15.812 35.656 1.00 30.91  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.852 -15.458 34.653 1.00 30.08  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.474 -15.407 33.268 1.00 30.93  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.908 -15.934 32.299 1.00 29.00  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.679 -14.805 33.164 1.00 26.58  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.363 -14.753 31.873 1.00 25.22  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.729 -16.156 31.406 1.00 26.99  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.554 -16.464 30.238 1.00 24.95  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.638 -13.888 31.918 1.00 26.38  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.234 -13.763 30.532 1.00 26.36  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.667 -12.908 29.587 1.00 28.95  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.308 -14.559 30.143 1.00 26.46  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.169 -12.849 28.285 1.00 29.35  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.817 -14.487 28.843 1.00 28.49  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.230 -13.649 27.920 1.00 27.42  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.285 -16.976 32.296 1.00 27.40  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.708 -18.343 31.964 1.00 29.70  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.517 -19.167 31.396 1.00 29.99  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.655 -19.831 30.356 1.00 28.26  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.323 -19.017 33.189 1.00 33.85  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.966 -20.679 32.855 1.00 39.95  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.348 -19.084 32.061 1.00 26.16  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.113 -19.788 31.646 1.00 25.05  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.709 -19.321 30.233 1.00 26.22  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.337 -20.143 29.381 1.00 24.44  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.989 -19.559 32.696 1.00 28.30  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.259 -20.389 33.995 1.00 28.68  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.572 -19.821 32.114 1.00 28.33  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.574 -19.803 35.213 1.00 34.65  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.792 -18.020 29.985 1.00 23.80  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.437 -17.462 28.674 1.00 23.93  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.443 -17.816 27.607 1.00 26.13  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.046 -18.061 26.472 1.00 24.62  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.180 -15.954 28.746 1.00 25.09  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.867 -15.588 29.489 1.00 31.23  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.778 -14.129 29.706 1.00 32.92  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.623 -16.067 28.713 1.00 33.28  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.752 -17.823 27.948 1.00 23.79  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.790 -18.226 26.986 1.00 22.86  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.548 -19.700 26.585 1.00 25.56  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.620 -20.038 25.400 1.00 23.84  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.193 -18.037 27.598 1.00 22.91  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.369 -18.326 26.645 1.00 27.44  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.333 -17.410 25.405 1.00 26.41  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.725 -18.195 27.392 1.00 32.08  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.241 -20.568 27.566 1.00 24.17  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.917 -21.970 27.290 1.00 24.06  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.712 -22.068 26.360 1.00 26.40  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.749 -22.846 25.415 1.00 26.46  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.617 -22.707 28.600 1.00 27.36  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.860 -23.073 29.393 1.00 40.79  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.983 -22.990 28.821 1.00 40.48  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.717 -23.438 30.588 1.00 43.24  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.658 -21.265 26.610 1.00 24.14  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.456 -21.221 25.752 1.00 22.61  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.821 -20.844 24.305 1.00 23.56  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.339 -21.447 23.334 1.00 21.40  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.403 -20.248 26.335 1.00 23.35  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.286 -19.971 25.355 1.00 23.94  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.314 -20.935 25.094 1.00 25.84  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.269 -18.790 24.607 1.00 25.65  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.333 -20.714 24.131 1.00 26.35  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.277 -18.569 23.643 1.00 28.18  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.309 -19.525 23.421 1.00 26.91  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.656 -19.821 24.160 1.00 20.49  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.087 -19.372 22.817 1.00 19.76  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.656 -20.517 22.002 1.00 23.64  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.309 -20.657 20.835 1.00 23.62  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.161 -18.274 22.946 1.00 21.18  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.628 -16.982 23.496 1.00 23.30  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 29.994 -15.769 23.391 1.00 26.78  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.341 -14.478 24.501 1.00 26.34  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.513 -21.342 22.625 1.00 20.87  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.195 -22.443 21.945 1.00 20.93  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.426 -23.769 21.942 1.00 24.83  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.900 -24.734 21.325 1.00 23.91  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.568 -22.650 22.596 1.00 22.06  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.631 -21.687 22.104 1.00 23.36  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.801 -20.440 22.701 1.00 24.91  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.464 -22.025 21.037 1.00 24.05  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.787 -19.556 22.256 1.00 24.40  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.495 -21.180 20.629 1.00 24.60  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.625 -19.931 21.214 1.00 26.30  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.661 -19.122 20.828 1.00 25.82  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.272 -23.859 22.642 1.00 21.90  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.585 -25.162 22.699 1.00 23.20  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.077 -25.126 22.437 1.00 25.88  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.496 -26.203 22.283 1.00 25.71  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.777 -25.857 24.091 1.00 28.78  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.098 -25.095 25.097 1.00 27.22  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.248 -26.068 24.494 1.00 28.66  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.426 -23.941 22.535 1.00 21.31  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.945 -23.769 22.487 1.00 21.10  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.297 -24.183 23.840 1.00 25.05  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.085 -24.063 23.981 1.00 25.55  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.299 -24.617 21.378 1.00 22.93  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.915 -24.408 20.118 1.00 29.62  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.107 -24.646 24.812 0.60 23.57  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.089 -24.683 24.811 0.40 22.45  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.617 -25.105 26.112 0.60 24.74  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.539 -25.115 26.097 0.40 23.16  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.819 -24.047 27.181 0.60 28.20  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.809 -24.112 27.197 0.40 27.50  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.941 -23.556 27.374 0.60 26.90  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.956 -23.692 27.402 0.40 26.37  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.313 -26.410 26.533 0.60 27.94  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.994 -26.533 26.479 0.40 23.94  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.144 -27.558 25.530 0.60 36.75  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.357 -27.591 25.585 0.40 22.70  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.096 -28.703 25.835 0.60 43.31  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 24.054 -28.928 25.668 0.40 36.52  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.838 -29.281 27.158 0.60 47.54  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.468 -29.896 24.738 0.40 43.72  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 23.963 -30.252 27.392 0.60 58.05  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.349 -31.197 24.982 0.40 57.55  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.786 -30.710 28.622 0.60 43.05  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.810 -32.002 24.075 0.40 45.04  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.258 -30.776 26.395 0.60 46.30  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.765 -31.705 26.135 0.40 47.34  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.730 -23.711 27.884 1.00 25.03  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.758 -22.716 28.939 1.00 25.44  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.514 -23.342 30.306 1.00 31.16  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.433 -23.879 30.577 1.00 30.35  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.752 -21.603 28.620 1.00 25.57  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.785 -20.394 29.567 1.00 29.48  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 23.042 -19.550 29.321 1.00 28.38  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.525 -19.561 29.417 1.00 29.86  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.522 -23.248 31.185 1.00 30.76  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.431 -23.805 32.539 1.00 31.95  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.715 -22.801 33.458 1.00 36.27  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.347 -22.094 34.245 1.00 36.16  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.833 -24.197 33.068 1.00 34.58  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.814 -24.781 34.478 1.00 52.81  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.848 -25.404 34.909 1.00 43.72  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.872 -24.569 35.238 1.00 46.12  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.401 -22.699 33.297 1.00 32.96  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.598 -21.734 34.043 1.00 34.12  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.050 -22.366 35.310 1.00 38.35  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.405 -23.419 35.244 1.00 37.45  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.487 -21.228 33.117 1.00 34.85  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.771 -19.942 33.465 1.00 41.14  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.767 -18.743 33.552 1.00 40.94  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.677 -19.676 32.436 1.00 41.79  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.370 -21.763 36.478 1.00 35.74  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 19.975 -22.277 37.801 1.00 37.68  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.454 -21.157 38.690 1.00 40.43  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.790 -19.990 38.463 1.00 38.18  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.171 -22.966 38.492 1.00 39.16  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.794 -24.123 37.683 1.00 45.66  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.061 -24.693 38.314 1.00 63.73  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.839 -25.184 39.681 1.00 82.60  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.370 -26.392 39.991 1.00 101.75 ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.193 -26.735 41.261 1.00 88.75  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.069 -27.262 39.033 1.00 90.61  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.638 -21.492 39.712 1.00 38.68  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.118 -20.478 40.644 1.00 39.14  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.252 -19.592 41.207 1.00 43.88  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.095 -18.372 41.300 1.00 43.24  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.348 -21.160 41.799 1.00 42.71  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.647 -20.184 42.728 1.00 55.01  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.928 -20.818 43.904 1.00 90.04  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.510 -21.714 44.560 1.00 88.77  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.777 -20.407 44.174 1.00 94.51  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.386 -20.216 41.526 1.00 41.73  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.550 -19.543 42.096 1.00 41.64  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.357 -18.660 41.162 1.00 42.67  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.181 -17.870 41.624 1.00 42.29  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.141 -18.766 39.846 1.00 36.87  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.931 -17.960 38.915 1.00 34.69  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.105 -17.099 37.954 1.00 38.01  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.691 -16.313 37.209 1.00 36.59  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.899 -18.877 38.134 1.00 33.19  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.231 -19.798 37.130 1.00 39.25  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.181 -19.479 36.565 1.00 31.70  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.847 -20.941 36.837 1.00 32.84  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.764 -17.281 37.929 1.00 36.34  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.883 -16.629 36.947 1.00 35.63  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 20.024 -15.098 36.915 1.00 37.54  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 20.071 -14.522 35.816 1.00 34.91  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.399 -17.071 37.054 1.00 39.61  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.564 -16.482 35.881 1.00 40.18  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.775 -16.799 38.433 1.00 39.05  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.389 -17.316 35.440 1.00 41.25  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.119 -14.446 38.085 1.00 36.05  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.265 -12.990 38.126 1.00 36.82  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.566 -12.520 37.486 1.00 37.28  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.525 -11.589 36.684 1.00 35.69  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.091 -12.424 39.550 1.00 41.32  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.714 -12.706 40.164 1.00 48.14  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.279 -12.296 39.118 1.00 54.31  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.302 -10.485 39.233 1.00 51.65  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.708 -13.181 37.805 1.00 33.91  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 24.026 -12.841 37.228 1.00 32.88  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 24.030 -13.147 35.727 1.00 34.48  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.546 -12.350 34.940 1.00 32.14  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.128 -13.640 37.910 1.00 34.23  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.444 -14.300 35.328 1.00 29.21  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.377 -14.678 33.904 1.00 27.64  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.575 -13.646 33.103 1.00 30.91  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.060 -13.204 32.049 1.00 28.59  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.902 -16.140 33.676 1.00 30.82  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.630 -16.432 32.194 1.00 29.48  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.928 -17.125 34.223 1.00 30.48  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.378 -13.256 33.587 0.65 29.30  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.378 -13.252 33.585 0.35 29.68  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.556 -12.259 32.889 0.65 30.59  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.555 -12.258 32.887 0.35 30.77  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.274 -10.907 32.768 0.65 34.07  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.270 -10.907 32.768 0.35 34.31  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.251 -10.301 31.692 0.65 33.26  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.257 -10.310 31.687 0.35 33.48  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.192 -12.072 33.564 0.65 34.60  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.186 -12.079 33.553 0.35 34.87  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.263 -11.164 32.768 0.65 39.06  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.243 -11.229 32.724 0.35 39.47  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.572 -11.197 33.384 0.65 45.30  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.650 -10.998 33.518 0.35 46.09  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.705 -10.078 34.841 0.65 43.14  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.200 -9.425  32.844 0.35 43.75  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.891 -10.434 33.868 1.00 31.48  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.639 -9.151  33.886 1.00 31.36  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.805 -9.199  32.894 1.00 31.67  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.982 -8.251  32.124 1.00 30.37  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.142 -8.844  35.288 1.00 32.58  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.532 -10.336 32.836 1.00 28.27  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.634 -10.505 31.885 1.00 27.12  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.113 -10.550 30.429 1.00 30.31  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.699 -9.884  29.566 1.00 27.77  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.544 -11.698 32.251 1.00 32.01  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.835 -11.676 33.653 1.00 30.91  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.859 -11.691 31.459 1.00 29.20  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 24.003 -11.297 30.168 1.00 27.01  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.404 -11.396 28.826 1.00 26.14  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.900 -10.018 28.360 1.00 28.70  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.027 -9.692  27.182 1.00 27.02  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.269 -12.426 28.813 1.00 26.78  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.372 -9.191  29.285 1.00 26.54  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.923 -7.835  28.921 1.00 27.54  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.115 -6.962  28.468 1.00 30.51  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.062 -6.321  27.413 1.00 30.73  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.166 -7.191  30.089 1.00 31.20  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.747 -7.717  30.215 1.00 37.09  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 18.975 -7.167  31.756 1.00 45.02  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.726 -5.437  31.385 1.00 43.08  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.206 -7.012  29.228 1.00 27.92  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.450 -6.287  28.949 1.00 27.74  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.068 -6.769  27.619 1.00 29.87  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.465 -5.944  26.788 1.00 28.36  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.419 -6.516  30.114 1.00 28.39  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.839 -6.038  29.881 1.00 28.72  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.161 -4.685  29.951 1.00 31.57  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.876 -6.948  29.679 1.00 27.86  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.470 -4.242  29.740 1.00 28.66  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.193 -6.521  29.517 1.00 27.78  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.484 -5.167  29.559 1.00 29.91  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.780 -4.748  29.432 1.00 29.31  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.102 -8.095  27.404 1.00 26.34  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.686 -8.689  26.197 1.00 24.60  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.768 -8.560  24.981 1.00 27.71  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.210 -8.831  23.867 1.00 26.55  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.069 -10.164 26.443 1.00 23.33  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.209 -10.438 27.462 1.00 26.45  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.503 -11.964 27.534 1.00 25.60  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.521 -9.645  27.090 1.00 27.39  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.481 -8.197  25.199 1.00 26.39  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.474 -8.059  24.135 1.00 27.05  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.240 -9.417  23.450 1.00 29.07  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.522 -9.609  22.263 1.00 27.29  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.859 -6.959  23.124 1.00 28.60  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 24.026 -5.571  23.759 1.00 32.63  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.738 -4.633  22.816 1.00 42.02  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.616 -4.729  21.599 1.00 34.47  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.516 -3.719  23.353 1.00 38.02  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.770 -10.371 24.249 1.00 25.74  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.444 -11.742 23.814 1.00 25.19  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.943 -11.899 24.083 1.00 31.92  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.523 -12.380 25.144 1.00 30.63  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.303 -12.729 24.607 1.00 25.96  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.796 -12.590 24.295 1.00 27.75  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.802 -13.622 25.366 1.00 30.60  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.426 -15.293 24.638 1.00 27.36  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.138 -11.357 23.154 1.00 31.85  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.681 -11.216 23.276 1.00 34.32  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.912 -12.500 23.587 1.00 35.41  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.993 -12.442 24.399 1.00 35.68  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.084 -10.540 22.032 1.00 37.66  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.610 -9.128  21.817 1.00 52.28  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.275 -13.645 22.977 1.00 30.56  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.543 -14.885 23.263 1.00 32.20  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.761 -15.361 24.696 1.00 35.00  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.800 -15.804 25.333 1.00 36.19  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.846 -15.978 22.240 1.00 33.55  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.391 -15.638 20.859 1.00 38.24  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 16.056 -15.418 20.572 1.00 41.95  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 18.107 -15.539 19.716 1.00 39.64  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 16.007 -15.155 19.276 1.00 41.66  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.215 -15.229 18.719 1.00 40.83  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 18.993 -15.184 25.230 1.00 28.56  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.304 -15.522 26.629 1.00 27.93  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.517 -14.614 27.580 1.00 33.43  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.920 -15.106 28.545 1.00 31.49  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.818 -15.542 26.952 1.00 29.97  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.054 -15.814 28.441 1.00 30.02  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.542 -16.587 26.099 1.00 28.80  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.510 -13.288 27.312 1.00 30.03  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.757 -12.323 28.130 1.00 31.19  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.267 -12.738 28.203 1.00 37.83  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.708 -12.795 29.304 1.00 37.09  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.936 -10.862 27.623 1.00 34.42  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.089 -9.878  28.443 1.00 34.96  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.409 -10.446 27.646 1.00 33.44  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.616 -12.944 27.038 0.41 35.99  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.693 -13.138 27.050 0.59 35.35  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.189 -13.291 26.938 0.41 37.88  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.311 -13.605 26.913 0.59 36.95  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.776 -14.506 27.773 0.41 42.14  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 13.998 -14.820 27.800 0.59 39.17  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.711 -14.486 28.384 0.41 43.55  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.029 -14.761 28.555 0.59 39.42  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.772 -13.478 25.468 0.41 39.99  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 13.988 -13.904 25.437 0.59 38.98  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.627 -12.194 24.671 0.41 52.34  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.538 -14.265 25.167 0.59 53.97  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.135 -11.193 25.237 0.41 56.08  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.649 -13.456 25.515 0.59 56.91  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 13.994 -12.191 23.478 0.41 57.32  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.295 -15.347 24.592 0.59 58.89  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.623 -15.544 27.813 0.41 37.29  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.816 -15.901 27.741 0.59 33.96  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.369 -16.781 28.560 0.41 37.45  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.535 -17.088 28.571 0.59 34.14  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.545 -16.582 30.042 0.41 40.17  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.719 -16.814 30.072 0.59 38.04  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.713 -17.063 30.813 0.41 40.75  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 14.043 -17.455 30.876 0.59 37.60  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.215 -17.893 27.991 0.41 45.37  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.298 -18.346 28.112 0.59 34.57  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 14.877 -17.930 26.623 0.41 45.99  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.660 -19.475 28.713 0.59 35.89  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.921 -19.244 28.622 0.41 45.27  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.771 -18.343 28.509 0.59 27.76  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.627 -15.879 30.444 1.00 34.91  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.883 -15.529 31.855 1.00 35.43  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.679 -14.799 32.399 1.00 41.79  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.203 -15.142 33.488 1.00 42.44  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.136 -14.673 31.974 1.00 34.49  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.670 -15.594 31.757 1.00 36.85  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.144 -13.838 31.602 1.00 39.43  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.944 -13.065 31.937 1.00 41.91  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.744 -13.996 32.186 1.00 47.46  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.000 -13.799 33.154 1.00 47.74  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.604 -12.086 30.806 1.00 44.88  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.441 -10.825 30.818 1.00 58.57  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.609 -9.605  30.466 1.00 74.44  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 13.002 -9.031  29.177 1.00 83.52  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.927 -8.087  29.020 1.00 92.64  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.574 -7.599  30.073 1.00 72.90  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.215 -7.627  27.810 1.00 80.25  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.570 -15.005 31.313 1.00 44.51  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.475 -15.979 31.402 1.00 45.83  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.629 -16.888 32.621 1.00 49.09  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.641  -17.141 33.303 1.00 49.10  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.372 -16.812 30.110 1.00 47.76  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.850  -16.025 28.913 1.00 66.09  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.561  -16.932 27.716 1.00 77.46  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.614  -16.213 26.385 1.00 87.17  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.575  -15.154 26.254 1.00 96.59  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.862 -17.385 32.889 1.00 44.48  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.145 -18.247 34.041 1.00 45.04  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.945 -17.487 35.362 1.00 50.41  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.400 -18.058 36.312 1.00 50.38  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.546 -18.862 33.937 1.00 45.32  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.664 -20.165 33.162 1.00 47.05  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.118 -20.293 31.886 1.00 50.52  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.384 -21.237 33.679 1.00 49.81  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.239 -21.492 31.168 1.00 50.94  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.522 -22.429 32.951 1.00 51.45  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.944 -22.549 31.705 1.00 48.96  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.319 -16.186 35.398 1.00 46.18  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.120 -15.327 36.580 1.00 47.61  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.621 -15.073 36.824 1.00 54.64  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.171 -15.169 37.970 1.00 55.28  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.972 -14.025 36.512 1.00 49.61  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.462 -14.366 36.683 1.00 48.07  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.536 -12.981 37.581 1.00 52.40  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.416 -13.343 36.130 1.00 54.00  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.853  -14.794 35.744 1.00 53.22  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.403  -14.542 35.801 1.00 55.91  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.629  -15.770 36.325 1.00 61.31  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.650  -15.607 37.054 1.00 62.08  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.876  -14.115 34.421 1.00 59.17  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.522  -13.413 34.461 1.00 78.45  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.901  -13.319 33.073 1.00 91.28  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.472  -12.837 33.122 1.00 105.71 ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.819  -12.916 31.788 1.00 116.04 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.089  -16.987 35.982 1.00 56.93  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.472  -18.235 36.437 1.00 58.64  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.635  -18.446 37.955 1.00 64.72  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.763  -19.043 38.573 1.00 65.57  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.058  -19.416 35.674 1.00 57.67  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.745  -17.961 38.546 1.00 62.82  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 9.027  -18.104 39.979 1.00 65.50  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.307  -17.076 40.876 1.00 73.45  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.189  -17.319 42.081 1.00 75.56  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.531 -18.087 40.240 1.00 68.97  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 11.103 -19.366 40.014 1.00 79.18  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.818  -15.950 40.304 1.00 70.18  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.117  -14.909 41.066 1.00 94.96  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.661  -15.285 41.374 1.00 137.97 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.402  -16.279 42.050 1.00 105.59 ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.222  -13.532 40.374 1.00 95.51  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.238  -13.299 39.234 1.00 106.01 ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.428  -12.052 38.388 1.00 126.39 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.521  -11.442 38.438 1.00 119.19 ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.476  -11.693 37.658 1.00 120.43 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.275 -35.120 5.870  1.00 30.55  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.324 -33.967 6.334  1.00 31.06  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.487 -36.329 6.764  1.00 30.41  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.998 -35.381 4.598  0.78 29.26  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 21.036 -35.392 4.585  0.22 29.28  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.780 -34.335 3.610  0.78 28.79  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.765 -34.355 3.588  0.22 28.76  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.280 -34.185 3.316  0.78 32.74  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.262 -34.180 3.394  0.22 32.18  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.544 -35.179 3.294  0.78 32.49  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.512 -35.158 3.469  0.22 31.64  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.573 -34.658 2.328  0.78 27.69  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.468 -34.635 2.233  0.22 27.49  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.071 -34.617 2.526  0.78 28.18  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.820 -35.685 1.374  0.22 28.37  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.865 -35.619 3.001  0.78 30.97  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.140 -37.008 1.321  0.22 31.44  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.935 -33.497 2.292  0.78 27.53  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.755 -35.491 0.429  0.22 28.24  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.177 -35.191 3.072  0.78 30.09  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.315 -37.661 0.438  0.22 31.01  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.257 -33.918 2.575  0.78 31.11  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.464 -36.753 -0.137 0.22 32.30  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.726 -32.182 1.842  0.78 27.93  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 19.001 -34.377 0.020  0.22 29.26  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.359 -33.064 2.448  0.78 29.73  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.456 -36.931 -1.092 0.22 31.44  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.825 -31.356 1.662  0.78 28.80  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 17.996 -34.557 -0.918 0.22 30.97  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.118 -31.792 1.978  0.78 29.71  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.738 -35.819 -1.471 0.22 31.53  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.829 -32.940 3.122  1.00 28.21  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.418 -32.600 2.874  1.00 27.88  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.299 -31.544 1.772  1.00 29.50  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.276 -30.855 1.441  1.00 28.08  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.690 -32.087 4.176  1.00 30.56  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.693 -33.133 5.295  1.00 30.45  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.277 -30.748 4.675  1.00 29.99  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.072 -31.360 1.287  1.00 26.55  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.701 -30.273 0.394  1.00 27.66  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.309 -29.148 1.383  1.00 31.38  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.310 -29.292 2.094  1.00 29.75  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.491 -30.638 -0.505 1.00 30.19  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.757 -31.912 -1.373 1.00 30.13  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.063 -29.413 -1.356 1.00 31.37  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.066 -31.866 -2.337 1.00 31.37  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.085 -28.055 1.468  1.00 30.39  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.754 -26.992 2.439  1.00 30.91  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.498 -26.201 2.068  1.00 34.90  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.220 -26.014 0.884  1.00 33.29  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 17.008 -26.112 2.438  1.00 32.62  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.559 -26.267 1.028  1.00 36.14  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.285 -27.711 0.667  1.00 31.78  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.865 -25.579 3.074  1.00 32.43  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.340 -10.280 11.832 1.00 30.33  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.305 -9.380  12.188 1.00 32.12  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.983 -10.730 18.088 1.00 29.63  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.494 -9.429  18.147 1.00 30.93  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.543 -10.047 16.379 1.00 26.70  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.390 -10.214 14.015 1.00 28.55  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.974 -8.436  17.296 1.00 28.35  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.990 -8.761  16.402 1.00 27.44  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 25.006 -11.045 17.199 1.00 27.15  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.450 -10.584 13.178 1.00 28.55  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.271 -10.562 19.709 1.00 34.93  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.233 -11.555 19.092 1.00 32.48  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.270 -9.671  11.316 1.00 32.53  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.294 -9.612  13.506 1.00 31.38  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.492 -9.356  19.123 1.00 31.93  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.388 -10.516 15.345 1.00 26.07  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.412 -10.797 20.558 1.00 34.86  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.860 -11.393 13.759 0.99 28.35  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.325 -15.206 22.558 1.00 36.40  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.590 -35.393 -1.237 0.78 49.68  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.318 -35.172 -0.573 0.78 51.35  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.745 -34.506 -0.222 0.78 48.40  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 18.024 -37.035 -0.779 0.78 48.49  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 35.748 -25.668 25.612 1.00 45.87  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 25.911 -3.400  26.353 1.00 36.87  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 38.429 -14.903 15.480 1.00 36.88  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 22.740 -5.308  19.803 1.00 60.25  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 37.955 2.441   19.668 1.00 44.70  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 41.305 -21.635 25.173 1.00 46.53  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 44.570 -0.867  17.880 1.00 58.20  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 43.687 -6.578  31.959 1.00 49.26  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 17.971 -29.383 7.686  1.00 36.95  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 16.560 -27.572 -3.289 1.00 58.21  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 26.745 -31.972 16.102 1.00 50.26  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 31.825 -0.817  15.823 1.00 44.08  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 33.340 -20.813 29.622 1.00 55.40  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 37.638 -20.425 26.988 1.00 36.12  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 20.815 -5.831  26.017 1.00 44.79  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 41.364 -16.975 15.173 1.00 38.32  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 19.855 -9.497  36.982 1.00 43.18  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 45.031 -11.209 18.672 1.00 64.65  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 27.295 -10.148 35.841 1.00 42.32  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 22.957 -28.243 12.642 1.00 28.76  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 30.290 1.506   33.963 1.00 64.14  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 27.255 -35.381 11.782 1.00 61.74  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 13.463 -14.291 21.846 1.00 70.26  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 32.461 -24.705 32.234 1.00 67.50  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 23.487 -5.709  32.934 1.00 40.55  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 22.627 -27.632 17.702 1.00 56.19  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 19.012 -24.883 32.987 1.00 41.44  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 20.510 -13.357 20.393 1.00 52.46  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 29.950 -32.069 9.564  1.00 50.80  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 28.259 -8.750  39.951 1.00 51.57  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 34.922 -18.873 13.857 0.50 31.52  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 41.622 -12.900 14.121 1.00 94.53  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 21.937 -24.925 18.308 1.00 25.27  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 26.840 -16.469 38.631 1.00 52.71  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 15.479 -9.857  24.810 1.00 52.18  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 14.280 -16.790 23.390 1.00 48.09  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 29.587 -2.155  13.820 1.00 64.06  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 30.329 -0.466  36.825 1.00 56.92  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 43.959 -4.383  25.824 1.00 49.42  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 7.077  -16.847 32.389 1.00 57.63  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 26.143 -22.546 29.929 1.00 29.98  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 12.614 -20.435 42.493 1.00 63.90  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 28.198 -23.756 31.625 1.00 44.98  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 24.056 -15.742 21.148 1.00 33.98  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 21.467 -27.077 14.516 0.50 43.99  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 27.307 -28.096 18.670 1.00 33.31  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 32.325 -8.915  39.741 1.00 59.45  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 27.163 -2.441  16.069 1.00 67.20  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 29.049 -31.196 7.255  1.00 32.71  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 41.372 -6.972  35.889 1.00 48.07  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 39.148 -18.951 33.342 1.00 52.31  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 41.242 -7.731  46.413 1.00 59.01  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 21.437 -29.986 14.172 1.00 71.67  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 44.392 -12.441 41.176 1.00 54.50  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 29.355 -27.372 20.625 1.00 28.32  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 26.022 -21.812 38.692 1.00 41.17  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 25.717 -2.737  19.953 1.00 64.40  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 20.839 -7.174  19.677 1.00 61.73  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 46.108 -14.197 21.537 1.00 68.56  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 42.497 -10.396 15.425 1.00 50.75  ? 360 HOH A O   1 
HETATM 1263 O  O   . HOH F 6 .   ? 23.263 -17.055 44.300 1.00 67.64  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 43.556 -10.634 35.324 1.00 68.19  ? 362 HOH A O   1 
HETATM 1265 O  O   A HOH F 6 .   ? 19.112 -23.012 4.291  0.60 38.93  ? 363 HOH A O   1 
HETATM 1266 O  O   . HOH F 6 .   ? 26.095 -19.140 41.747 1.00 75.93  ? 364 HOH A O   1 
HETATM 1267 O  O   . HOH F 6 .   ? 46.228 -15.853 27.638 1.00 67.60  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 28.519 -24.281 34.344 1.00 59.01  ? 366 HOH A O   1 
HETATM 1269 O  O   . HOH F 6 .   ? 22.679 -34.055 8.857  1.00 37.49  ? 367 HOH A O   1 
HETATM 1270 O  O   . HOH F 6 .   ? 36.826 -5.511  12.097 1.00 42.44  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 22.275 -34.094 26.253 1.00 77.29  ? 369 HOH A O   1 
HETATM 1272 O  O   . HOH F 6 .   ? 37.424 -6.455  34.232 1.00 44.66  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 24.875 -26.812 19.000 1.00 37.85  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 46.327 -29.804 21.259 1.00 75.38  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 46.886 -21.877 17.843 1.00 46.31  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 25.881 -4.452  17.868 1.00 53.54  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 21.341 -31.206 29.949 1.00 70.98  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 30.729 -28.820 22.644 1.00 43.70  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 34.160 -7.833  35.610 1.00 38.68  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 26.226 -7.934  9.071  1.00 49.88  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 46.314 -18.992 19.718 1.00 55.62  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 11.345 -14.820 40.567 1.00 91.70  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 27.684 -23.051 13.857 0.50 28.85  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 20.150 -15.738 40.834 1.00 37.94  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 31.890 -31.852 14.664 1.00 46.09  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 42.258 -6.022  11.833 1.00 71.25  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 18.013 -24.306 39.799 1.00 46.03  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 44.944 -8.625  17.819 1.00 75.41  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 18.063 -34.581 8.314  1.00 35.32  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 4.250  -20.184 37.728 1.00 71.80  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 21.021 -22.988 42.067 1.00 52.04  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 47.276 -25.228 21.662 1.00 62.41  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 10.964 -11.237 34.511 1.00 57.33  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 33.067 -29.649 21.539 1.00 45.74  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 40.394 -19.610 28.987 1.00 38.56  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 45.326 -12.666 23.626 1.00 50.04  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 46.074 -8.870  44.081 1.00 56.90  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 23.738 -15.749 17.799 1.00 45.25  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 47.002 -20.192 22.025 1.00 66.32  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 37.955 -16.313 12.729 1.00 56.93  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 19.696 -27.406 10.129 1.00 60.81  ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 27.138 -1.597  21.980 1.00 54.85  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 41.215 -17.102 35.218 1.00 48.80  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 34.803 -33.305 21.909 1.00 63.31  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 30.290 -10.473 40.585 1.00 46.21  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 35.261 -29.765 23.540 1.00 51.74  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 33.720 -33.110 12.302 1.00 46.55  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 35.503 2.100   13.601 1.00 61.90  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 10.152 -11.745 39.941 1.00 66.37  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 22.852 -14.783 40.397 1.00 38.23  ? 408 HOH A O   1 
HETATM 1311 O  O   . HOH F 6 .   ? 41.907 -8.038  13.651 1.00 67.05  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 37.205 -2.547  11.648 1.00 60.49  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 29.653 -0.761  22.160 1.00 63.57  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 44.575 -16.476 29.707 1.00 53.28  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 32.131 -15.631 39.851 1.00 39.20  ? 413 HOH A O   1 
HETATM 1316 O  O   . HOH F 6 .   ? 39.979 -5.574  33.881 1.00 49.22  ? 414 HOH A O   1 
HETATM 1317 O  O   . HOH F 6 .   ? 28.810 -15.963 41.385 1.00 72.20  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 22.413 -10.220 14.431 1.00 45.45  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 33.597 -0.231  19.994 1.00 49.05  ? 417 HOH A O   1 
HETATM 1320 O  O   B HOH F 6 .   ? 37.283 -11.935 40.076 0.50 38.93  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 25.979 -29.262 22.553 1.00 60.49  ? 419 HOH A O   1 
HETATM 1322 O  O   . HOH F 6 .   ? 23.421 -30.443 19.217 1.00 71.33  ? 420 HOH A O   1 
HETATM 1323 O  O   . HOH F 6 .   ? 45.524 -10.540 30.335 1.00 57.20  ? 421 HOH A O   1 
HETATM 1324 O  O   . HOH F 6 .   ? 27.431 -25.595 28.217 1.00 58.09  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 45.970 -17.147 17.138 1.00 69.36  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 44.407 -26.022 26.565 1.00 63.97  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 44.846 -8.099  15.135 1.00 77.56  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 33.914 -17.671 39.506 1.00 70.07  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 28.357 -2.514  11.325 1.00 71.85  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 42.845 -18.310 30.756 1.00 51.48  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 25.717 -15.854 41.049 1.00 55.60  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 45.894 -5.504  23.737 1.00 55.33  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 32.404 -3.919  41.167 1.00 65.12  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 37.811 -27.064 28.445 1.00 69.21  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 29.907 -22.744 36.733 1.00 83.82  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 47.977 -23.290 19.890 1.00 67.80  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 32.014 0.135   13.275 1.00 63.77  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 31.874 -26.224 27.014 1.00 50.69  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 27.024 -34.647 17.971 1.00 80.24  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 35.131 -3.999  10.629 1.00 48.99  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 28.319 -29.306 26.714 1.00 78.52  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 20.051 -35.305 10.146 1.00 42.55  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 37.115 -24.312 27.539 1.00 60.31  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 24.312 -21.532 41.054 1.00 62.15  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 19.394 -31.753 13.872 1.00 74.97  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 47.133 -12.879 28.526 1.00 66.40  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 22.996 -2.704  26.151 1.00 68.41  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 46.597 -14.631 17.997 1.00 74.44  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 31.072 -34.445 14.789 1.00 65.25  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 33.805 -10.897 41.570 0.50 52.99  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 47.339 -28.729 17.718 1.00 70.02  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 11.965 -18.660 22.504 1.00 64.25  ? 450 HOH A O   1 
HETATM 1353 O  O   . HOH F 6 .   ? 34.616 -18.805 36.146 1.00 67.31  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 32.314 -1.049  22.241 1.00 64.58  ? 452 HOH A O   1 
HETATM 1355 O  O   . HOH F 6 .   ? 47.113 -11.883 25.527 1.00 69.82  ? 453 HOH A O   1 
HETATM 1356 O  O   . HOH F 6 .   ? 13.662 -16.110 39.880 1.00 76.90  ? 454 HOH A O   1 
HETATM 1357 O  O   A HOH F 6 .   ? 12.020 -20.613 27.824 0.78 55.59  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 19.262 -7.534  35.224 1.00 62.50  ? 456 HOH A O   1 
HETATM 1359 O  O   . HOH F 6 .   ? 43.163 -3.036  33.784 1.00 61.26  ? 457 HOH A O   1 
HETATM 1360 O  O   . HOH F 6 .   ? 25.346 -5.702  35.171 1.00 58.72  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 17.097 -28.117 9.891  1.00 58.16  ? 459 HOH A O   1 
HETATM 1362 O  O   . HOH F 6 .   ? 44.285 -13.467 13.857 0.50 78.90  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 15.916 -15.411 41.222 1.00 66.97  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 17.391 -7.999  24.780 1.00 63.27  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 33.805 -13.917 41.570 0.50 46.95  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 32.154 -23.900 34.846 1.00 70.48  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 19.002 -28.064 13.857 0.50 74.04  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 28.139 -29.904 24.063 1.00 76.15  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 32.645 -20.481 37.024 1.00 76.20  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 45.558 -12.820 16.193 1.00 76.96  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 21.145 -5.610  34.704 1.00 62.37  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 23.225 -4.585  17.110 1.00 77.06  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 34.965 -23.588 32.753 1.00 66.29  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 32.929 -0.677  42.862 1.00 60.17  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 16.733 -6.611  34.632 1.00 82.83  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.357 -24.267 -0.048 1.00 53.88  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 14.994 -25.861 -1.845 1.00 49.82  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 11.793 -23.575 2.926  1.00 55.31  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 21.076 -38.334 4.028  1.00 52.11  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 17.788 -36.424 6.098  1.00 42.52  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 20.910 -39.620 -2.179 1.00 68.07  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 18.700 -40.689 0.764  1.00 68.90  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.617 -24.831 5.546  1.00 60.55  ? 208 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   ? 0.8784 1.0627 0.7579 0.0319  -0.1379 -0.0234 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8742 1.0511 0.7354 0.0146  -0.1285 -0.0260 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8549 1.0632 0.7413 0.0018  -0.1237 -0.0432 6   ASP A C   
4    O O   . ASP A 5   ? 0.8450 1.0822 0.7606 0.0058  -0.1289 -0.0531 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8962 1.0417 0.7472 0.0057  -0.1102 -0.0186 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0892 1.2127 0.9048 -0.0047 -0.1050 -0.0139 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0984 1.2343 0.9108 -0.0163 -0.1026 -0.0232 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1903 1.2836 0.9809 -0.0023 -0.1020 -0.0020 6   ASP A OD2 
9    N N   . SER A 6   ? 0.7533 0.9553 0.6281 -0.0143 -0.1129 -0.0477 7   SER A N   
10   C CA  . SER A 6   ? 0.7082 0.9323 0.6017 -0.0283 -0.1058 -0.0635 7   SER A CA  
11   C C   . SER A 6   ? 0.6564 0.8651 0.5619 -0.0394 -0.0858 -0.0656 7   SER A C   
12   O O   . SER A 6   ? 0.6506 0.8624 0.5586 -0.0529 -0.0766 -0.0755 7   SER A O   
13   C CB  . SER A 6   ? 0.7875 1.0168 0.6578 -0.0372 -0.1105 -0.0688 7   SER A CB  
14   O OG  . SER A 6   ? 0.9664 1.1662 0.8066 -0.0428 -0.1025 -0.0604 7   SER A OG  
15   N N   . CYS A 7   ? 0.5349 0.7269 0.4474 -0.0330 -0.0799 -0.0568 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4889 0.6658 0.4116 -0.0406 -0.0638 -0.0576 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4658 0.6585 0.4140 -0.0486 -0.0572 -0.0701 8   CYS A C   
18   O O   . CYS A 7   ? 0.4644 0.6809 0.4284 -0.0465 -0.0640 -0.0772 8   CYS A O   
19   C CB  . CYS A 7   ? 0.5025 0.6610 0.4266 -0.0313 -0.0613 -0.0461 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5852 0.7153 0.4768 -0.0269 -0.0621 -0.0319 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3468 0.5251 0.2983 -0.0576 -0.0438 -0.0731 9   ILE A N   
22   C CA  . ILE A 8   ? 0.3040 0.4860 0.2744 -0.0650 -0.0354 -0.0818 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3354 0.4991 0.3112 -0.0592 -0.0297 -0.0730 9   ILE A C   
24   O O   . ILE A 8   ? 0.3241 0.4717 0.2888 -0.0533 -0.0296 -0.0632 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3448 0.5218 0.3133 -0.0786 -0.0258 -0.0923 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3560 0.5093 0.3109 -0.0796 -0.0185 -0.0877 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3579 0.5576 0.3240 -0.0856 -0.0317 -0.1032 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.4080 0.5514 0.3622 -0.0905 -0.0082 -0.0978 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2726 0.4374 0.2634 -0.0623 -0.0241 -0.0771 10  GLN A N   
30   N N   B GLN A 9   ? 0.2730 0.4398 0.2645 -0.0617 -0.0250 -0.0772 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2621 0.4099 0.2561 -0.0572 -0.0194 -0.0692 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2607 0.4116 0.2567 -0.0571 -0.0201 -0.0700 10  GLN A CA  
33   C C   A GLN A 9   ? 0.3058 0.4380 0.3028 -0.0657 -0.0086 -0.0734 10  GLN A C   
34   C C   B GLN A 9   ? 0.2966 0.4307 0.2940 -0.0659 -0.0090 -0.0740 10  GLN A C   
35   O O   A GLN A 9   ? 0.2966 0.4367 0.3002 -0.0750 -0.0046 -0.0832 10  GLN A O   
36   O O   B GLN A 9   ? 0.2887 0.4287 0.2906 -0.0760 -0.0046 -0.0841 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2726 0.4346 0.2791 -0.0491 -0.0251 -0.0676 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2690 0.4361 0.2798 -0.0510 -0.0245 -0.0707 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2604 0.4067 0.2701 -0.0445 -0.0203 -0.0604 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3743 0.5271 0.3909 -0.0495 -0.0176 -0.0664 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5899 0.7528 0.6154 -0.0395 -0.0231 -0.0633 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4849 0.6372 0.5039 -0.0371 -0.0228 -0.0581 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4757 0.6538 0.5146 -0.0467 -0.0195 -0.0738 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3451 0.5069 0.3616 -0.0279 -0.0326 -0.0547 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.6321 0.7920 0.6566 -0.0276 -0.0286 -0.0551 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3579 0.4968 0.3797 -0.0365 -0.0166 -0.0546 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2839 0.3935 0.2751 -0.0627 -0.0042 -0.0663 11  PHE A N   
48   N N   B PHE A 10  ? 0.2600 0.3724 0.2525 -0.0622 -0.0050 -0.0663 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2877 0.3782 0.2781 -0.0683 0.0041  -0.0685 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2634 0.3555 0.2542 -0.0674 0.0033  -0.0679 11  PHE A CA  
51   C C   A PHE A 10  ? 0.3138 0.4009 0.3099 -0.0663 0.0059  -0.0652 11  PHE A C   
52   C C   B PHE A 10  ? 0.3073 0.3964 0.3042 -0.0658 0.0053  -0.0650 11  PHE A C   
53   O O   A PHE A 10  ? 0.3012 0.3814 0.2963 -0.0584 0.0039  -0.0568 11  PHE A O   
54   O O   B PHE A 10  ? 0.2959 0.3803 0.2926 -0.0576 0.0028  -0.0568 11  PHE A O   
55   C CB  A PHE A 10  ? 0.3133 0.3832 0.2955 -0.0653 0.0065  -0.0647 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2869 0.3602 0.2696 -0.0632 0.0048  -0.0628 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.3378 0.3862 0.3165 -0.0697 0.0130  -0.0678 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3168 0.3890 0.2941 -0.0681 0.0069  -0.0694 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3929 0.4378 0.3690 -0.0791 0.0178  -0.0770 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3583 0.4454 0.3316 -0.0686 0.0028  -0.0711 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3721 0.4016 0.3480 -0.0646 0.0139  -0.0616 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3603 0.4149 0.3350 -0.0721 0.0128  -0.0743 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.4129 0.4322 0.3820 -0.0826 0.0236  -0.0789 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3775 0.4638 0.3450 -0.0744 0.0058  -0.0783 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.4153 0.4211 0.3840 -0.0673 0.0182  -0.0634 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.4055 0.4589 0.3764 -0.0766 0.0156  -0.0817 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3991 0.3982 0.3636 -0.0760 0.0231  -0.0715 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3758 0.4460 0.3436 -0.0783 0.0126  -0.0841 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2709 0.3642 0.2729 -0.0749 0.0105  -0.0728 12  THR A N   
70   C CA  . THR A 11  ? 0.2743 0.3675 0.2822 -0.0759 0.0141  -0.0726 12  THR A CA  
71   C C   . THR A 11  ? 0.3207 0.3879 0.3193 -0.0719 0.0169  -0.0637 12  THR A C   
72   O O   . THR A 11  ? 0.3005 0.3705 0.3033 -0.0663 0.0156  -0.0592 12  THR A O   
73   C CB  . THR A 11  ? 0.3776 0.4758 0.3894 -0.0899 0.0221  -0.0842 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3466 0.4741 0.3697 -0.0928 0.0179  -0.0935 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.4246 0.5241 0.4421 -0.0933 0.0279  -0.0860 12  THR A CG2 
76   N N   A ARG A 12  ? 0.2998 0.3427 0.2862 -0.0741 0.0200  -0.0620 13  ARG A N   
77   N N   B ARG A 12  ? 0.3027 0.3455 0.2891 -0.0742 0.0200  -0.0620 13  ARG A N   
78   C CA  A ARG A 12  ? 0.3144 0.3326 0.2908 -0.0701 0.0210  -0.0547 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.3185 0.3366 0.2949 -0.0701 0.0210  -0.0547 13  ARG A CA  
80   C C   A ARG A 12  ? 0.3329 0.3491 0.3094 -0.0588 0.0148  -0.0469 13  ARG A C   
81   C C   B ARG A 12  ? 0.3339 0.3503 0.3105 -0.0588 0.0148  -0.0469 13  ARG A C   
82   O O   A ARG A 12  ? 0.3195 0.3184 0.2893 -0.0550 0.0143  -0.0418 13  ARG A O   
83   O O   B ARG A 12  ? 0.3198 0.3191 0.2898 -0.0549 0.0143  -0.0417 13  ARG A O   
84   C CB  A ARG A 12  ? 0.3767 0.3675 0.3390 -0.0760 0.0258  -0.0567 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.3890 0.3800 0.3515 -0.0758 0.0256  -0.0567 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.4644 0.4487 0.4213 -0.0898 0.0346  -0.0638 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.5324 0.5111 0.4867 -0.0877 0.0341  -0.0610 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.6280 0.6065 0.5811 -0.0932 0.0389  -0.0616 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.6487 0.6138 0.5943 -0.0982 0.0402  -0.0686 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.7409 0.6878 0.6758 -0.0893 0.0382  -0.0535 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.6830 0.6257 0.6187 -0.0922 0.0374  -0.0660 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.8393 0.7798 0.7691 -0.0882 0.0390  -0.0488 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.7999 0.7455 0.7378 -0.0943 0.0379  -0.0723 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.5684 0.5316 0.5114 -0.0902 0.0415  -0.0517 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.7191 0.6443 0.6498 -0.0876 0.0357  -0.0710 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.7053 0.6169 0.6166 -0.0845 0.0368  -0.0418 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.4868 0.4567 0.4347 -0.1028 0.0404  -0.0810 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.2761 0.3090 0.2586 -0.0545 0.0103  -0.0466 14  HIS A N   
99   C CA  . HIS A 13  ? 0.2758 0.3065 0.2571 -0.0466 0.0066  -0.0408 14  HIS A CA  
100  C C   . HIS A 13  ? 0.3121 0.3381 0.2938 -0.0412 0.0055  -0.0342 14  HIS A C   
101  O O   . HIS A 13  ? 0.3012 0.3152 0.2796 -0.0377 0.0048  -0.0313 14  HIS A O   
102  C CB  . HIS A 13  ? 0.2661 0.3126 0.2489 -0.0448 0.0031  -0.0412 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.2889 0.3308 0.2685 -0.0397 0.0019  -0.0368 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.2971 0.3304 0.2754 -0.0397 0.0039  -0.0396 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.2963 0.3406 0.2743 -0.0350 -0.0002 -0.0309 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.2921 0.3259 0.2696 -0.0365 0.0036  -0.0365 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.2912 0.3296 0.2666 -0.0342 0.0015  -0.0307 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.2714 0.3079 0.2582 -0.0402 0.0050  -0.0329 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2672 0.2988 0.2542 -0.0354 0.0047  -0.0275 15  ALA A CA  
110  C C   . ALA A 14  ? 0.3049 0.3186 0.2852 -0.0379 0.0077  -0.0265 15  ALA A C   
111  O O   . ALA A 14  ? 0.2836 0.2887 0.2606 -0.0340 0.0064  -0.0224 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2785 0.3240 0.2734 -0.0333 0.0041  -0.0282 15  ALA A CB  
113  N N   A SER A 15  ? 0.2826 0.2899 0.2591 -0.0449 0.0118  -0.0306 16  SER A N   
114  N N   B SER A 15  ? 0.2849 0.2922 0.2614 -0.0449 0.0118  -0.0306 16  SER A N   
115  N N   C SER A 15  ? 0.2788 0.2860 0.2552 -0.0449 0.0118  -0.0306 16  SER A N   
116  C CA  A SER A 15  ? 0.2982 0.2842 0.2627 -0.0480 0.0144  -0.0291 16  SER A CA  
117  C CA  B SER A 15  ? 0.3018 0.2877 0.2663 -0.0481 0.0144  -0.0292 16  SER A CA  
118  C CA  C SER A 15  ? 0.2925 0.2783 0.2570 -0.0480 0.0144  -0.0291 16  SER A CA  
119  C C   A SER A 15  ? 0.3604 0.3305 0.3173 -0.0434 0.0102  -0.0266 16  SER A C   
120  C C   B SER A 15  ? 0.3645 0.3345 0.3213 -0.0435 0.0102  -0.0266 16  SER A C   
121  C C   C SER A 15  ? 0.3621 0.3318 0.3187 -0.0435 0.0103  -0.0267 16  SER A C   
122  O O   A SER A 15  ? 0.3387 0.2957 0.2882 -0.0401 0.0079  -0.0229 16  SER A O   
123  O O   B SER A 15  ? 0.3479 0.3046 0.2971 -0.0403 0.0080  -0.0229 16  SER A O   
124  O O   C SER A 15  ? 0.3493 0.3052 0.2980 -0.0405 0.0080  -0.0230 16  SER A O   
125  C CB  A SER A 15  ? 0.3539 0.3340 0.3130 -0.0585 0.0210  -0.0346 16  SER A CB  
126  C CB  B SER A 15  ? 0.3607 0.3407 0.3197 -0.0586 0.0210  -0.0347 16  SER A CB  
127  C CB  C SER A 15  ? 0.3394 0.3193 0.2984 -0.0585 0.0211  -0.0344 16  SER A CB  
128  O OG  A SER A 15  ? 0.4301 0.3853 0.3724 -0.0623 0.0238  -0.0322 16  SER A OG  
129  O OG  B SER A 15  ? 0.4314 0.4304 0.4014 -0.0626 0.0249  -0.0394 16  SER A OG  
130  O OG  C SER A 15  ? 0.3810 0.3593 0.3387 -0.0624 0.0219  -0.0389 16  SER A OG  
131  N N   . ASP A 16  ? 0.3359 0.3089 0.2956 -0.0426 0.0088  -0.0297 17  ASP A N   
132  C CA  . ASP A 16  ? 0.3490 0.3106 0.3057 -0.0370 0.0049  -0.0298 17  ASP A CA  
133  C C   . ASP A 16  ? 0.3417 0.3116 0.3052 -0.0298 0.0008  -0.0271 17  ASP A C   
134  O O   . ASP A 16  ? 0.3418 0.3019 0.3028 -0.0245 -0.0033 -0.0263 17  ASP A O   
135  C CB  . ASP A 16  ? 0.3720 0.3386 0.3325 -0.0386 0.0059  -0.0355 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.5313 0.4843 0.4832 -0.0461 0.0104  -0.0396 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.5398 0.4768 0.4806 -0.0504 0.0130  -0.0377 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.5314 0.4885 0.4858 -0.0489 0.0122  -0.0453 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.2831 0.2703 0.2545 -0.0298 0.0016  -0.0260 18  VAL A N   
140  C CA  . VAL A 17  ? 0.2697 0.2625 0.2453 -0.0255 -0.0002 -0.0238 18  VAL A CA  
141  C C   . VAL A 17  ? 0.3060 0.2897 0.2773 -0.0239 -0.0015 -0.0203 18  VAL A C   
142  O O   . VAL A 17  ? 0.2966 0.2775 0.2688 -0.0203 -0.0046 -0.0207 18  VAL A O   
143  C CB  . VAL A 17  ? 0.2905 0.2970 0.2696 -0.0262 0.0012  -0.0221 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.2889 0.2958 0.2686 -0.0238 0.0012  -0.0191 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.2799 0.2947 0.2602 -0.0279 0.0017  -0.0257 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.2898 0.2707 0.2572 -0.0271 0.0011  -0.0182 19  LEU A N   
147  C CA  . LEU A 18  ? 0.2967 0.2689 0.2582 -0.0269 0.0009  -0.0155 19  LEU A CA  
148  C C   . LEU A 18  ? 0.3441 0.2989 0.2948 -0.0256 -0.0030 -0.0153 19  LEU A C   
149  O O   . LEU A 18  ? 0.3197 0.2704 0.2677 -0.0224 -0.0068 -0.0142 19  LEU A O   
150  C CB  . LEU A 18  ? 0.3140 0.2878 0.2744 -0.0314 0.0059  -0.0152 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.3536 0.3215 0.3094 -0.0316 0.0073  -0.0133 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.3503 0.3264 0.3134 -0.0273 0.0064  -0.0117 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.4041 0.3736 0.3596 -0.0369 0.0136  -0.0153 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.3274 0.2712 0.2711 -0.0275 -0.0028 -0.0167 20  LEU A N   
155  C CA  . LEU A 19  ? 0.3584 0.2806 0.2884 -0.0245 -0.0078 -0.0158 20  LEU A CA  
156  C C   . LEU A 19  ? 0.3566 0.2838 0.2949 -0.0153 -0.0155 -0.0178 20  LEU A C   
157  O O   . LEU A 19  ? 0.3443 0.2622 0.2758 -0.0103 -0.0221 -0.0165 20  LEU A O   
158  C CB  . LEU A 19  ? 0.3933 0.3023 0.3154 -0.0284 -0.0049 -0.0178 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.5151 0.3957 0.4190 -0.0247 -0.0100 -0.0162 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.5534 0.4131 0.4356 -0.0291 -0.0094 -0.0114 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5877 0.4553 0.4853 -0.0290 -0.0059 -0.0192 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.3026 0.2464 0.2559 -0.0136 -0.0145 -0.0218 21  ASN A N   
163  C CA  . ASN A 20  ? 0.2994 0.2526 0.2641 -0.0065 -0.0196 -0.0263 21  ASN A CA  
164  C C   . ASN A 20  ? 0.3243 0.2882 0.2947 -0.0058 -0.0210 -0.0260 21  ASN A C   
165  O O   . ASN A 20  ? 0.3166 0.2831 0.2919 0.0001  -0.0275 -0.0296 21  ASN A O   
166  C CB  . ASN A 20  ? 0.3072 0.2742 0.2839 -0.0074 -0.0159 -0.0316 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.4551 0.4101 0.4280 -0.0054 -0.0167 -0.0348 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.4183 0.3534 0.3805 -0.0009 -0.0217 -0.0334 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.3520 0.3162 0.3309 -0.0090 -0.0118 -0.0389 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.2925 0.2630 0.2630 -0.0115 -0.0153 -0.0227 22  LEU A N   
171  C CA  . LEU A 21  ? 0.2856 0.2623 0.2588 -0.0123 -0.0151 -0.0224 22  LEU A CA  
172  C C   . LEU A 21  ? 0.3187 0.2828 0.2811 -0.0103 -0.0207 -0.0205 22  LEU A C   
173  O O   . LEU A 21  ? 0.2883 0.2574 0.2543 -0.0079 -0.0252 -0.0235 22  LEU A O   
174  C CB  . LEU A 21  ? 0.2800 0.2611 0.2530 -0.0173 -0.0082 -0.0188 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.3156 0.3078 0.2955 -0.0189 -0.0040 -0.0197 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.3123 0.3054 0.2897 -0.0211 0.0005  -0.0154 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.3448 0.3464 0.3327 -0.0191 -0.0035 -0.0248 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.2880 0.2355 0.2357 -0.0123 -0.0203 -0.0164 23  ASN A N   
179  C CA  . ASN A 22  ? 0.3133 0.2446 0.2449 -0.0113 -0.0256 -0.0141 23  ASN A CA  
180  C C   . ASN A 22  ? 0.3779 0.3028 0.3074 -0.0021 -0.0370 -0.0165 23  ASN A C   
181  O O   . ASN A 22  ? 0.3923 0.3138 0.3156 0.0013  -0.0445 -0.0168 23  ASN A O   
182  C CB  . ASN A 22  ? 0.3581 0.2711 0.2719 -0.0174 -0.0209 -0.0099 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.4402 0.3368 0.3344 -0.0193 -0.0237 -0.0072 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.4142 0.3178 0.3107 -0.0190 -0.0256 -0.0081 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4698 0.3430 0.3425 -0.0224 -0.0234 -0.0041 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.3464 0.2706 0.2818 0.0026  -0.0389 -0.0190 24  ARG A N   
187  C CA  . ARG A 23  ? 0.3630 0.2829 0.3003 0.0138  -0.0503 -0.0228 24  ARG A CA  
188  C C   . ARG A 23  ? 0.3914 0.3362 0.3493 0.0181  -0.0546 -0.0303 24  ARG A C   
189  O O   . ARG A 23  ? 0.3928 0.3369 0.3502 0.0263  -0.0657 -0.0331 24  ARG A O   
190  C CB  . ARG A 23  ? 0.3583 0.2748 0.3011 0.0174  -0.0492 -0.0259 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.4631 0.3508 0.3835 0.0143  -0.0469 -0.0203 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.5229 0.4115 0.4510 0.0136  -0.0418 -0.0242 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.6000 0.4588 0.5058 0.0100  -0.0394 -0.0203 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.8520 0.7055 0.7585 0.0066  -0.0336 -0.0232 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.6421 0.5190 0.5697 0.0064  -0.0297 -0.0297 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.7148 0.5383 0.5989 0.0020  -0.0307 -0.0202 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.3371 0.3030 0.3115 0.0119  -0.0458 -0.0338 25  LEU A N   
198  C CA  . LEU A 24  ? 0.3104 0.2989 0.3026 0.0124  -0.0470 -0.0417 25  LEU A CA  
199  C C   . LEU A 24  ? 0.3580 0.3450 0.3425 0.0104  -0.0506 -0.0402 25  LEU A C   
200  O O   . LEU A 24  ? 0.3465 0.3447 0.3394 0.0153  -0.0590 -0.0471 25  LEU A O   
201  C CB  . LEU A 24  ? 0.2914 0.2952 0.2950 0.0041  -0.0354 -0.0438 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.3329 0.3424 0.3452 0.0045  -0.0309 -0.0474 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.3246 0.3461 0.3423 -0.0045 -0.0201 -0.0483 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.3526 0.3728 0.3806 0.0133  -0.0377 -0.0580 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.3213 0.2956 0.2903 0.0033  -0.0447 -0.0324 26  ARG A N   
206  C CA  . ARG A 25  ? 0.3418 0.3122 0.3009 0.0004  -0.0472 -0.0312 26  ARG A CA  
207  C C   . ARG A 25  ? 0.4181 0.3765 0.3642 0.0086  -0.0614 -0.0312 26  ARG A C   
208  O O   . ARG A 25  ? 0.4160 0.3839 0.3651 0.0104  -0.0685 -0.0363 26  ARG A O   
209  C CB  . ARG A 25  ? 0.3622 0.3195 0.3068 -0.0077 -0.0381 -0.0239 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.4275 0.3809 0.3618 -0.0117 -0.0392 -0.0240 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.4375 0.3813 0.3616 -0.0194 -0.0289 -0.0192 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.4477 0.3731 0.3552 -0.0205 -0.0278 -0.0138 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.6347 0.5437 0.5218 -0.0252 -0.0266 -0.0111 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.5504 0.4590 0.4307 -0.0280 -0.0281 -0.0131 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.4849 0.3772 0.3570 -0.0284 -0.0232 -0.0073 26  ARG A NH2 
216  N N   A SER A 26  ? 0.4102 0.3469 0.3401 0.0131  -0.0654 -0.0256 27  SER A N   
217  N N   B SER A 26  ? 0.4082 0.3448 0.3381 0.0132  -0.0655 -0.0256 27  SER A N   
218  N N   C SER A 26  ? 0.4019 0.3385 0.3318 0.0132  -0.0655 -0.0256 27  SER A N   
219  C CA  A SER A 26  ? 0.4433 0.3612 0.3547 0.0220  -0.0795 -0.0235 27  SER A CA  
220  C CA  B SER A 26  ? 0.4405 0.3580 0.3514 0.0219  -0.0795 -0.0234 27  SER A CA  
221  C CA  C SER A 26  ? 0.4319 0.3490 0.3426 0.0220  -0.0795 -0.0233 27  SER A CA  
222  C C   A SER A 26  ? 0.4959 0.4319 0.4254 0.0339  -0.0927 -0.0327 27  SER A C   
223  C C   B SER A 26  ? 0.4973 0.4308 0.4252 0.0347  -0.0933 -0.0322 27  SER A C   
224  C C   C SER A 26  ? 0.4925 0.4256 0.4202 0.0348  -0.0934 -0.0321 27  SER A C   
225  O O   A SER A 26  ? 0.5105 0.4449 0.4318 0.0395  -0.1052 -0.0343 27  SER A O   
226  O O   B SER A 26  ? 0.5146 0.4413 0.4311 0.0422  -0.1072 -0.0326 27  SER A O   
227  O O   C SER A 26  ? 0.5091 0.4348 0.4250 0.0424  -0.1073 -0.0324 27  SER A O   
228  C CB  A SER A 26  ? 0.5126 0.4037 0.4066 0.0250  -0.0799 -0.0174 27  SER A CB  
229  C CB  B SER A 26  ? 0.5077 0.3959 0.3976 0.0231  -0.0788 -0.0162 27  SER A CB  
230  C CB  C SER A 26  ? 0.4907 0.3792 0.3814 0.0232  -0.0786 -0.0163 27  SER A CB  
231  O OG  A SER A 26  ? 0.6266 0.5007 0.5027 0.0136  -0.0685 -0.0105 27  SER A OG  
232  O OG  B SER A 26  ? 0.6023 0.4951 0.5069 0.0293  -0.0789 -0.0197 27  SER A OG  
233  O OG  C SER A 26  ? 0.5997 0.4639 0.4679 0.0326  -0.0926 -0.0131 27  SER A OG  
234  N N   . ARG A 27  ? 0.4331 0.3884 0.3879 0.0373  -0.0899 -0.0399 28  ARG A N   
235  C CA  . ARG A 27  ? 0.4413 0.4178 0.4188 0.0488  -0.1008 -0.0514 28  ARG A CA  
236  C C   . ARG A 27  ? 0.4584 0.4674 0.4591 0.0427  -0.0972 -0.0618 28  ARG A C   
237  O O   . ARG A 27  ? 0.4509 0.4837 0.4747 0.0499  -0.1044 -0.0741 28  ARG A O   
238  C CB  . ARG A 27  ? 0.4689 0.4477 0.4602 0.0548  -0.0984 -0.0554 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.5988 0.5427 0.5656 0.0599  -0.1015 -0.0460 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.6942 0.6395 0.6738 0.0631  -0.0963 -0.0501 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.9130 0.8735 0.9141 0.0780  -0.1074 -0.0618 28  ARG A NE  
242  C CZ  . ARG A 27  ? 1.1270 1.1090 1.1542 0.0791  -0.1015 -0.0725 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 1.0093 1.0066 1.0579 0.0933  -0.1117 -0.0848 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 0.9461 0.9352 0.9779 0.0662  -0.0857 -0.0718 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.3863 0.3958 0.3808 0.0292  -0.0858 -0.0579 29  ASP A N   
246  C CA  . ASP A 28  ? 0.3863 0.4200 0.3972 0.0203  -0.0795 -0.0663 29  ASP A CA  
247  C C   . ASP A 28  ? 0.4243 0.4820 0.4618 0.0174  -0.0707 -0.0763 29  ASP A C   
248  O O   . ASP A 28  ? 0.4225 0.5055 0.4802 0.0150  -0.0708 -0.0889 29  ASP A O   
249  C CB  . ASP A 28  ? 0.4275 0.4729 0.4408 0.0248  -0.0930 -0.0740 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.5285 0.5908 0.5499 0.0124  -0.0850 -0.0807 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.5124 0.5643 0.5242 0.0010  -0.0712 -0.0740 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.5925 0.6784 0.6303 0.0141  -0.0926 -0.0934 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.3462 0.3960 0.3828 0.0166  -0.0630 -0.0716 30  ILE A N   
254  C CA  . ILE A 29  ? 0.3163 0.3850 0.3732 0.0129  -0.0540 -0.0803 30  ILE A CA  
255  C C   . ILE A 29  ? 0.3523 0.4206 0.4051 -0.0011 -0.0385 -0.0765 30  ILE A C   
256  O O   . ILE A 29  ? 0.3302 0.3801 0.3662 -0.0046 -0.0332 -0.0650 30  ILE A O   
257  C CB  . ILE A 29  ? 0.3538 0.4159 0.4129 0.0208  -0.0555 -0.0796 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.3715 0.4331 0.4361 0.0369  -0.0718 -0.0850 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.3347 0.4142 0.4107 0.0142  -0.0436 -0.0879 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.4085 0.4505 0.4652 0.0448  -0.0737 -0.0803 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.3120 0.4004 0.3800 -0.0092 -0.0312 -0.0871 31  LEU A N   
262  N N   B LEU A 30  ? 0.3172 0.4057 0.3853 -0.0091 -0.0312 -0.0871 31  LEU A N   
263  C CA  A LEU A 30  ? 0.3064 0.3928 0.3694 -0.0226 -0.0163 -0.0849 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.3149 0.4018 0.3783 -0.0226 -0.0164 -0.0852 31  LEU A CA  
265  C C   A LEU A 30  ? 0.3500 0.4192 0.3949 -0.0279 -0.0133 -0.0749 31  LEU A C   
266  C C   B LEU A 30  ? 0.3544 0.4238 0.3995 -0.0279 -0.0133 -0.0750 31  LEU A C   
267  O O   A LEU A 30  ? 0.3393 0.3988 0.3748 -0.0358 -0.0025 -0.0692 31  LEU A O   
268  O O   B LEU A 30  ? 0.3445 0.4042 0.3802 -0.0358 -0.0026 -0.0694 31  LEU A O   
269  C CB  A LEU A 30  ? 0.3093 0.3898 0.3684 -0.0249 -0.0080 -0.0805 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.3201 0.4021 0.3805 -0.0252 -0.0079 -0.0815 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.3698 0.4687 0.4469 -0.0245 -0.0051 -0.0926 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.3868 0.4885 0.4636 -0.0313 0.0002  -0.0946 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.3574 0.4501 0.4257 -0.0328 0.0069  -0.0889 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.3849 0.4935 0.4725 -0.0229 -0.0038 -0.0997 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.3981 0.5219 0.4955 -0.0297 -0.0027 -0.1090 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.4207 0.5143 0.4854 -0.0442 0.0147  -0.0906 31  LEU A CD2 
277  N N   . THR A 31  ? 0.3097 0.3746 0.3489 -0.0235 -0.0227 -0.0735 32  THR A N   
278  C CA  . THR A 31  ? 0.3174 0.3679 0.3412 -0.0292 -0.0191 -0.0667 32  THR A CA  
279  C C   . THR A 31  ? 0.3940 0.4563 0.4260 -0.0404 -0.0104 -0.0760 32  THR A C   
280  O O   . THR A 31  ? 0.3835 0.4674 0.4329 -0.0416 -0.0125 -0.0889 32  THR A O   
281  C CB  . THR A 31  ? 0.4003 0.4437 0.4142 -0.0232 -0.0309 -0.0645 32  THR A CB  
282  O OG1 . THR A 31  ? 0.4052 0.4676 0.4332 -0.0185 -0.0413 -0.0759 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.3887 0.4142 0.3889 -0.0152 -0.0365 -0.0544 32  THR A CG2 
284  N N   . ASP A 32  ? 0.3580 0.4064 0.3784 -0.0487 0.0005  -0.0704 33  ASP A N   
285  C CA  . ASP A 32  ? 0.3577 0.4108 0.3815 -0.0610 0.0114  -0.0781 33  ASP A CA  
286  C C   . ASP A 32  ? 0.3816 0.4220 0.3938 -0.0673 0.0156  -0.0765 33  ASP A C   
287  O O   . ASP A 32  ? 0.3818 0.4189 0.3920 -0.0785 0.0266  -0.0811 33  ASP A O   
288  C CB  . ASP A 32  ? 0.3768 0.4220 0.3959 -0.0664 0.0232  -0.0743 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.5092 0.5328 0.5122 -0.0614 0.0248  -0.0596 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.4659 0.4793 0.4612 -0.0562 0.0199  -0.0529 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.6251 0.6431 0.6232 -0.0631 0.0307  -0.0557 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.3255 0.3570 0.3285 -0.0612 0.0080  -0.0706 34  VAL A N   
293  C CA  . VAL A 33  ? 0.3262 0.3460 0.3182 -0.0671 0.0119  -0.0703 34  VAL A CA  
294  C C   . VAL A 33  ? 0.3661 0.3850 0.3513 -0.0614 0.0005  -0.0692 34  VAL A C   
295  O O   . VAL A 33  ? 0.3639 0.3810 0.3465 -0.0520 -0.0085 -0.0636 34  VAL A O   
296  C CB  . VAL A 33  ? 0.3779 0.3741 0.3562 -0.0689 0.0229  -0.0600 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.3613 0.3469 0.3320 -0.0593 0.0184  -0.0491 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.3833 0.3673 0.3529 -0.0774 0.0310  -0.0630 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.3344 0.3523 0.3144 -0.0681 0.0014  -0.0748 35  VAL A N   
300  N N   B VAL A 34  ? 0.3379 0.3561 0.3180 -0.0681 0.0012  -0.0750 35  VAL A N   
301  C CA  A VAL A 34  ? 0.3349 0.3478 0.3027 -0.0654 -0.0076 -0.0739 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.3411 0.3538 0.3088 -0.0649 -0.0079 -0.0734 35  VAL A CA  
303  C C   A VAL A 34  ? 0.3873 0.3796 0.3404 -0.0711 0.0031  -0.0690 35  VAL A C   
304  C C   B VAL A 34  ? 0.3927 0.3855 0.3457 -0.0711 0.0025  -0.0694 35  VAL A C   
305  O O   A VAL A 34  ? 0.3901 0.3786 0.3443 -0.0799 0.0139  -0.0735 35  VAL A O   
306  O O   B VAL A 34  ? 0.3965 0.3863 0.3507 -0.0802 0.0129  -0.0744 35  VAL A O   
307  C CB  A VAL A 34  ? 0.3844 0.4164 0.3587 -0.0683 -0.0171 -0.0866 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.3947 0.4263 0.3680 -0.0645 -0.0208 -0.0845 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.3968 0.4201 0.3528 -0.0664 -0.0264 -0.0849 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.4006 0.4427 0.3803 -0.0770 -0.0142 -0.0969 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.3753 0.4302 0.3680 -0.0609 -0.0279 -0.0933 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.4064 0.4274 0.3610 -0.0589 -0.0324 -0.0797 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.3513 0.3295 0.2907 -0.0664 0.0010  -0.0608 36  ILE A N   
314  C CA  . ILE A 35  ? 0.3553 0.3160 0.2824 -0.0707 0.0106  -0.0580 36  ILE A CA  
315  C C   . ILE A 35  ? 0.4299 0.3893 0.3434 -0.0744 0.0042  -0.0627 36  ILE A C   
316  O O   . ILE A 35  ? 0.4199 0.3785 0.3240 -0.0693 -0.0067 -0.0596 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3805 0.3289 0.3029 -0.0648 0.0144  -0.0481 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.3641 0.3155 0.2983 -0.0600 0.0177  -0.0432 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.4094 0.3432 0.3228 -0.0686 0.0246  -0.0478 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.3748 0.3243 0.3154 -0.0647 0.0273  -0.0457 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.3936 0.3502 0.3036 -0.0836 0.0112  -0.0700 37  VAL A N   
322  C CA  . VAL A 36  ? 0.4054 0.3609 0.3009 -0.0891 0.0060  -0.0760 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4652 0.4010 0.3452 -0.0924 0.0159  -0.0727 37  VAL A C   
324  O O   . VAL A 36  ? 0.4429 0.3691 0.3266 -0.0957 0.0295  -0.0733 37  VAL A O   
325  C CB  . VAL A 36  ? 0.4557 0.4240 0.3583 -0.0987 0.0070  -0.0889 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4735 0.4422 0.3598 -0.1044 0.0001  -0.0957 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.4493 0.4409 0.3711 -0.0960 -0.0012 -0.0944 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.4411 0.3695 0.3024 -0.0915 0.0094  -0.0698 38  VAL A N   
329  C CA  . VAL A 37  ? 0.4515 0.3628 0.2971 -0.0957 0.0189  -0.0682 38  VAL A CA  
330  C C   . VAL A 37  ? 0.5275 0.4353 0.3508 -0.1025 0.0120  -0.0736 38  VAL A C   
331  O O   . VAL A 37  ? 0.5069 0.4127 0.3151 -0.0990 -0.0007 -0.0697 38  VAL A O   
332  C CB  . VAL A 37  ? 0.4999 0.4031 0.3421 -0.0893 0.0199  -0.0587 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.5085 0.3980 0.3404 -0.0946 0.0330  -0.0597 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.4753 0.3860 0.3392 -0.0814 0.0219  -0.0535 38  VAL A CG2 
335  N N   A SER A 38  ? 0.5294 0.4316 0.3458 -0.1124 0.0215  -0.0818 39  SER A N   
336  N N   B SER A 38  ? 0.4861 0.3968 0.3111 -0.1113 0.0177  -0.0835 39  SER A N   
337  C CA  A SER A 38  ? 0.5651 0.4629 0.3571 -0.1204 0.0158  -0.0877 39  SER A CA  
338  C CA  B SER A 38  ? 0.5007 0.4127 0.3093 -0.1200 0.0126  -0.0923 39  SER A CA  
339  C C   A SER A 38  ? 0.6321 0.5425 0.4180 -0.1161 -0.0054 -0.0882 39  SER A C   
340  C C   B SER A 38  ? 0.5337 0.4623 0.3422 -0.1152 -0.0077 -0.0941 39  SER A C   
341  O O   A SER A 38  ? 0.6487 0.5497 0.4093 -0.1153 -0.0157 -0.0847 39  SER A O   
342  O O   B SER A 38  ? 0.5019 0.4486 0.3323 -0.1133 -0.0108 -0.0988 39  SER A O   
343  C CB  A SER A 38  ? 0.6496 0.5283 0.4178 -0.1239 0.0221  -0.0837 39  SER A CB  
344  C CB  B SER A 38  ? 0.5738 0.4673 0.3558 -0.1261 0.0183  -0.0917 39  SER A CB  
345  O OG  A SER A 38  ? 0.7893 0.6591 0.5635 -0.1282 0.0409  -0.0868 39  SER A OG  
346  O OG  B SER A 38  ? 0.6746 0.5582 0.4630 -0.1309 0.0372  -0.0949 39  SER A OG  
347  N N   A ARG A 39  ? 0.5735 0.5045 0.3827 -0.1126 -0.0117 -0.0928 40  ARG A N   
348  N N   B ARG A 39  ? 0.5063 0.4285 0.2907 -0.1124 -0.0214 -0.0904 40  ARG A N   
349  C CA  A ARG A 39  ? 0.5732 0.5224 0.3859 -0.1064 -0.0318 -0.0959 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.5133 0.4513 0.2989 -0.1049 -0.0427 -0.0924 40  ARG A CA  
351  C C   A ARG A 39  ? 0.6044 0.5486 0.4105 -0.0931 -0.0453 -0.0848 40  ARG A C   
352  C C   B ARG A 39  ? 0.5648 0.5095 0.3682 -0.0914 -0.0496 -0.0844 40  ARG A C   
353  O O   A ARG A 39  ? 0.6137 0.5625 0.4090 -0.0867 -0.0641 -0.0852 40  ARG A O   
354  O O   B ARG A 39  ? 0.5508 0.5182 0.3779 -0.0866 -0.0570 -0.0901 40  ARG A O   
355  C CB  A ARG A 39  ? 0.6087 0.5629 0.4037 -0.1135 -0.0419 -0.1057 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.5391 0.4652 0.2893 -0.1056 -0.0570 -0.0914 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.7493 0.7158 0.5563 -0.1261 -0.0325 -0.1199 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.6505 0.5782 0.3871 -0.1191 -0.0540 -0.1030 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.8378 0.8178 0.6327 -0.1305 -0.0480 -0.1308 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.6531 0.5708 0.3530 -0.1195 -0.0709 -0.1026 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.9142 0.9012 0.7137 -0.1457 -0.0373 -0.1453 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.6729 0.5909 0.3578 -0.1338 -0.0664 -0.1141 40  ARG A NE  
363  C CZ  A ARG A 39  ? 1.0821 1.0520 0.8600 -0.1572 -0.0269 -0.1489 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.8623 0.8031 0.5548 -0.1373 -0.0771 -0.1272 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.9063 0.8524 0.6570 -0.1559 -0.0249 -0.1394 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.7061 0.6736 0.4237 -0.1273 -0.0927 -0.1313 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.9103 0.8864 0.6935 -0.1712 -0.0170 -0.1631 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.7508 0.6896 0.4274 -0.1516 -0.0716 -0.1378 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.5181 0.4522 0.3304 -0.0887 -0.0361 -0.0753 41  GLU A N   
370  N N   B GLU A 40  ? 0.5041 0.4306 0.2987 -0.0872 -0.0442 -0.0729 41  GLU A N   
371  C CA  A GLU A 40  ? 0.5119 0.4404 0.3217 -0.0773 -0.0450 -0.0654 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.4877 0.4160 0.2941 -0.0755 -0.0496 -0.0649 41  GLU A CA  
373  C C   A GLU A 40  ? 0.5089 0.4519 0.3497 -0.0725 -0.0394 -0.0650 41  GLU A C   
374  C C   B GLU A 40  ? 0.4914 0.4371 0.3313 -0.0730 -0.0420 -0.0671 41  GLU A C   
375  O O   A GLU A 40  ? 0.4697 0.4119 0.3222 -0.0776 -0.0239 -0.0657 41  GLU A O   
376  O O   B GLU A 40  ? 0.4508 0.3982 0.3018 -0.0803 -0.0273 -0.0707 41  GLU A O   
377  C CB  A GLU A 40  ? 0.5448 0.4477 0.3314 -0.0793 -0.0375 -0.0560 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.5166 0.4207 0.3043 -0.0748 -0.0430 -0.0539 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.7325 0.6177 0.4831 -0.0851 -0.0431 -0.0558 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.7336 0.6158 0.4847 -0.0820 -0.0438 -0.0522 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.1965 1.0629 0.9203 -0.0783 -0.0563 -0.0466 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.2174 1.0814 0.9388 -0.0759 -0.0593 -0.0446 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.2480 1.0908 0.9464 -0.0844 -0.0483 -0.0410 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.2451 1.1185 0.9717 -0.0648 -0.0774 -0.0447 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.1977 1.0721 0.9257 -0.0671 -0.0741 -0.0457 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.2517 1.0909 0.9437 -0.0823 -0.0532 -0.0393 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.4529 0.4089 0.3064 -0.0624 -0.0521 -0.0648 42  GLN A N   
388  C CA  . GLN A 41  ? 0.4299 0.4017 0.3118 -0.0593 -0.0470 -0.0664 42  GLN A CA  
389  C C   . GLN A 41  ? 0.4695 0.4332 0.3529 -0.0504 -0.0479 -0.0566 42  GLN A C   
390  O O   . GLN A 41  ? 0.4847 0.4394 0.3543 -0.0428 -0.0599 -0.0517 42  GLN A O   
391  C CB  . GLN A 41  ? 0.4510 0.4493 0.3520 -0.0564 -0.0584 -0.0776 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.6253 0.6355 0.5294 -0.0675 -0.0553 -0.0897 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.8807 0.9217 0.8086 -0.0667 -0.0639 -0.1035 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.7771 0.8330 0.7235 -0.0579 -0.0704 -0.1050 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.9256 0.9783 0.8548 -0.0768 -0.0632 -0.1154 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.3880 0.3529 0.2860 -0.0516 -0.0354 -0.0537 43  PHE A N   
397  C CA  . PHE A 42  ? 0.3819 0.3410 0.2829 -0.0445 -0.0348 -0.0456 43  PHE A CA  
398  C C   . PHE A 42  ? 0.4155 0.3911 0.3408 -0.0425 -0.0312 -0.0486 43  PHE A C   
399  O O   . PHE A 42  ? 0.4070 0.3856 0.3410 -0.0487 -0.0197 -0.0507 43  PHE A O   
400  C CB  . PHE A 42  ? 0.4130 0.3552 0.3038 -0.0485 -0.0225 -0.0385 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.4510 0.3760 0.3168 -0.0533 -0.0222 -0.0367 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.4784 0.4007 0.3378 -0.0617 -0.0152 -0.0416 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.4905 0.3996 0.3370 -0.0506 -0.0275 -0.0304 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.5167 0.4230 0.3513 -0.0675 -0.0139 -0.0409 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.5429 0.4339 0.3626 -0.0570 -0.0259 -0.0290 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.5191 0.4097 0.3332 -0.0655 -0.0190 -0.0345 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.3641 0.3480 0.2984 -0.0340 -0.0405 -0.0490 44  ARG A N   
408  C CA  . ARG A 43  ? 0.3413 0.3410 0.2974 -0.0328 -0.0366 -0.0527 44  ARG A CA  
409  C C   . ARG A 43  ? 0.3949 0.3844 0.3499 -0.0311 -0.0289 -0.0440 44  ARG A C   
410  O O   . ARG A 43  ? 0.3909 0.3664 0.3332 -0.0272 -0.0319 -0.0370 44  ARG A O   
411  C CB  . ARG A 43  ? 0.3491 0.3652 0.3182 -0.0240 -0.0499 -0.0596 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.4595 0.4924 0.4346 -0.0250 -0.0591 -0.0710 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.5830 0.6428 0.5836 -0.0195 -0.0662 -0.0828 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.7231 0.7918 0.7400 -0.0254 -0.0524 -0.0853 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.8591 0.9432 0.8897 -0.0362 -0.0422 -0.0950 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.7463 0.8431 0.7808 -0.0424 -0.0447 -0.1051 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.6225 0.7088 0.6614 -0.0418 -0.0296 -0.0952 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.3389 0.3343 0.3052 -0.0349 -0.0188 -0.0447 45  ALA A N   
419  C CA  . ALA A 44  ? 0.3370 0.3248 0.3024 -0.0331 -0.0127 -0.0371 45  ALA A CA  
420  C C   . ALA A 44  ? 0.3427 0.3404 0.3208 -0.0354 -0.0061 -0.0397 45  ALA A C   
421  O O   . ALA A 44  ? 0.3263 0.3360 0.3139 -0.0396 -0.0048 -0.0478 45  ALA A O   
422  C CB  . ALA A 44  ? 0.3593 0.3329 0.3137 -0.0367 -0.0046 -0.0313 45  ALA A CB  
423  N N   . HIS A 45  ? 0.2930 0.2858 0.2700 -0.0336 -0.0018 -0.0336 46  HIS A N   
424  C CA  . HIS A 45  ? 0.2874 0.2849 0.2705 -0.0363 0.0049  -0.0342 46  HIS A CA  
425  C C   . HIS A 45  ? 0.3439 0.3289 0.3185 -0.0398 0.0135  -0.0290 46  HIS A C   
426  O O   . HIS A 45  ? 0.3305 0.3066 0.2990 -0.0366 0.0140  -0.0229 46  HIS A O   
427  C CB  . HIS A 45  ? 0.2843 0.2839 0.2698 -0.0315 0.0027  -0.0311 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.3270 0.3346 0.3195 -0.0261 -0.0060 -0.0357 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.3584 0.3573 0.3437 -0.0207 -0.0129 -0.0320 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.3270 0.3491 0.3324 -0.0252 -0.0084 -0.0444 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.3410 0.3467 0.3336 -0.0152 -0.0205 -0.0374 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.3301 0.3520 0.3371 -0.0171 -0.0183 -0.0456 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.3223 0.3060 0.2967 -0.0464 0.0207  -0.0322 47  LYS A N   
434  C CA  . LYS A 46  ? 0.3298 0.2977 0.2944 -0.0487 0.0287  -0.0272 47  LYS A CA  
435  C C   . LYS A 46  ? 0.3608 0.3222 0.3208 -0.0423 0.0284  -0.0189 47  LYS A C   
436  O O   . LYS A 46  ? 0.3412 0.2924 0.2962 -0.0387 0.0298  -0.0143 47  LYS A O   
437  C CB  . LYS A 46  ? 0.3676 0.3323 0.3296 -0.0576 0.0371  -0.0315 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.3315 0.3004 0.2968 -0.0654 0.0395  -0.0406 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.3634 0.3289 0.3258 -0.0768 0.0499  -0.0463 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.4224 0.3998 0.3930 -0.0857 0.0514  -0.0585 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.4571 0.4317 0.4250 -0.0994 0.0634  -0.0659 47  LYS A NZ  
442  N N   . THR A 47  ? 0.3066 0.2757 0.2696 -0.0407 0.0262  -0.0181 48  THR A N   
443  C CA  . THR A 47  ? 0.3067 0.2718 0.2651 -0.0352 0.0252  -0.0112 48  THR A CA  
444  C C   . THR A 47  ? 0.3322 0.2993 0.2937 -0.0290 0.0204  -0.0084 48  THR A C   
445  O O   . THR A 47  ? 0.3213 0.2836 0.2800 -0.0244 0.0207  -0.0039 48  THR A O   
446  C CB  . THR A 47  ? 0.4030 0.3757 0.3624 -0.0363 0.0246  -0.0121 48  THR A CB  
447  O OG1 . THR A 47  ? 0.4064 0.3924 0.3766 -0.0355 0.0198  -0.0175 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.4252 0.3925 0.3774 -0.0441 0.0320  -0.0142 48  THR A CG2 
449  N N   . VAL A 48  ? 0.2951 0.2686 0.2616 -0.0289 0.0162  -0.0115 49  VAL A N   
450  C CA  . VAL A 48  ? 0.2959 0.2689 0.2625 -0.0257 0.0136  -0.0098 49  VAL A CA  
451  C C   . VAL A 48  ? 0.3298 0.2947 0.2930 -0.0259 0.0175  -0.0091 49  VAL A C   
452  O O   . VAL A 48  ? 0.3047 0.2690 0.2690 -0.0229 0.0188  -0.0074 49  VAL A O   
453  C CB  . VAL A 48  ? 0.3236 0.2994 0.2908 -0.0260 0.0082  -0.0125 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.3247 0.2954 0.2873 -0.0257 0.0079  -0.0110 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.3153 0.2985 0.2873 -0.0245 0.0050  -0.0140 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.2949 0.2549 0.2552 -0.0298 0.0197  -0.0120 50  LEU A N   
457  C CA  . LEU A 49  ? 0.3024 0.2533 0.2588 -0.0308 0.0245  -0.0126 50  LEU A CA  
458  C C   . LEU A 49  ? 0.3353 0.2793 0.2915 -0.0263 0.0287  -0.0090 50  LEU A C   
459  O O   . LEU A 49  ? 0.3146 0.2560 0.2724 -0.0227 0.0309  -0.0089 50  LEU A O   
460  C CB  . LEU A 49  ? 0.3051 0.2523 0.2582 -0.0369 0.0267  -0.0172 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.3470 0.3007 0.2995 -0.0399 0.0207  -0.0216 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.3490 0.3018 0.2998 -0.0465 0.0230  -0.0278 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.3703 0.3201 0.3163 -0.0391 0.0184  -0.0206 50  LEU A CD2 
464  N N   . MET A 50  ? 0.3038 0.2443 0.2572 -0.0260 0.0296  -0.0064 51  MET A N   
465  C CA  . MET A 50  ? 0.3209 0.2511 0.2698 -0.0202 0.0316  -0.0017 51  MET A CA  
466  C C   . MET A 50  ? 0.3647 0.3040 0.3198 -0.0122 0.0267  0.0008  51  MET A C   
467  O O   . MET A 50  ? 0.3686 0.3036 0.3254 -0.0050 0.0270  0.0020  51  MET A O   
468  C CB  . MET A 50  ? 0.3490 0.2711 0.2887 -0.0231 0.0335  0.0010  51  MET A CB  
469  C CG  . MET A 50  ? 0.3895 0.3023 0.3234 -0.0323 0.0401  -0.0030 51  MET A CG  
470  S SD  . MET A 50  ? 0.4487 0.3580 0.3734 -0.0390 0.0433  -0.0022 51  MET A SD  
471  C CE  . MET A 50  ? 0.4195 0.3010 0.3253 -0.0338 0.0466  0.0062  51  MET A CE  
472  N N   . ALA A 51  ? 0.3238 0.2765 0.2837 -0.0133 0.0223  0.0003  52  ALA A N   
473  C CA  . ALA A 51  ? 0.3167 0.2804 0.2831 -0.0078 0.0180  0.0010  52  ALA A CA  
474  C C   . ALA A 51  ? 0.3382 0.3075 0.3129 -0.0062 0.0196  -0.0028 52  ALA A C   
475  O O   . ALA A 51  ? 0.3420 0.3208 0.3244 -0.0010 0.0175  -0.0039 52  ALA A O   
476  C CB  . ALA A 51  ? 0.3153 0.2896 0.2836 -0.0112 0.0145  0.0001  52  ALA A CB  
477  N N   . CYS A 52  ? 0.3023 0.2668 0.2751 -0.0115 0.0234  -0.0059 53  CYS A N   
478  C CA  . CYS A 52  ? 0.3037 0.2716 0.2810 -0.0131 0.0268  -0.0105 53  CYS A CA  
479  C C   . CYS A 52  ? 0.3522 0.3125 0.3304 -0.0111 0.0324  -0.0131 53  CYS A C   
480  O O   . CYS A 52  ? 0.3427 0.3080 0.3267 -0.0117 0.0364  -0.0182 53  CYS A O   
481  C CB  . CYS A 52  ? 0.3128 0.2787 0.2832 -0.0210 0.0267  -0.0122 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.3548 0.3276 0.3248 -0.0227 0.0210  -0.0108 53  CYS A SG  
483  N N   . SER A 53  ? 0.3166 0.2640 0.2882 -0.0105 0.0342  -0.0110 54  SER A N   
484  C CA  . SER A 53  ? 0.3032 0.2400 0.2735 -0.0104 0.0405  -0.0144 54  SER A CA  
485  C C   . SER A 53  ? 0.3783 0.3009 0.3450 -0.0037 0.0417  -0.0111 54  SER A C   
486  O O   . SER A 53  ? 0.3539 0.2681 0.3117 -0.0061 0.0406  -0.0069 54  SER A O   
487  C CB  . SER A 53  ? 0.3340 0.2650 0.2952 -0.0203 0.0429  -0.0170 54  SER A CB  
488  O OG  . SER A 53  ? 0.3891 0.3063 0.3448 -0.0225 0.0487  -0.0194 54  SER A OG  
489  N N   . GLY A 54  ? 0.3557 0.2745 0.3285 0.0043  0.0444  -0.0136 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3646 0.2645 0.3314 0.0123  0.0455  -0.0102 55  GLY A CA  
491  C C   . GLY A 54  ? 0.4182 0.2982 0.3718 0.0038  0.0522  -0.0107 55  GLY A C   
492  O O   . GLY A 54  ? 0.4258 0.2868 0.3673 0.0051  0.0531  -0.0059 55  GLY A O   
493  N N   . LEU A 55  ? 0.3880 0.2716 0.3418 -0.0061 0.0572  -0.0171 56  LEU A N   
494  C CA  . LEU A 55  ? 0.3924 0.2611 0.3351 -0.0157 0.0633  -0.0197 56  LEU A CA  
495  C C   . LEU A 55  ? 0.4108 0.2804 0.3461 -0.0233 0.0605  -0.0163 56  LEU A C   
496  O O   . LEU A 55  ? 0.4177 0.2703 0.3429 -0.0266 0.0648  -0.0151 56  LEU A O   
497  C CB  . LEU A 55  ? 0.3870 0.2609 0.3300 -0.0245 0.0677  -0.0276 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.4580 0.3179 0.3905 -0.0345 0.0741  -0.0323 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.4791 0.3163 0.4081 -0.0299 0.0823  -0.0342 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.4618 0.3302 0.3917 -0.0441 0.0750  -0.0390 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.3501 0.2384 0.2903 -0.0259 0.0541  -0.0155 57  PHE A N   
502  C CA  . PHE A 56  ? 0.3400 0.2323 0.2766 -0.0323 0.0517  -0.0143 57  PHE A CA  
503  C C   . PHE A 56  ? 0.4027 0.2865 0.3338 -0.0281 0.0511  -0.0080 57  PHE A C   
504  O O   . PHE A 56  ? 0.3941 0.2714 0.3179 -0.0353 0.0543  -0.0084 57  PHE A O   
505  C CB  . PHE A 56  ? 0.3344 0.2458 0.2771 -0.0348 0.0449  -0.0157 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.3446 0.2596 0.2859 -0.0411 0.0449  -0.0217 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.3799 0.2913 0.3168 -0.0495 0.0478  -0.0272 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.3653 0.2873 0.3080 -0.0398 0.0417  -0.0222 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.3920 0.3069 0.3256 -0.0550 0.0462  -0.0328 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.4023 0.3248 0.3388 -0.0459 0.0407  -0.0269 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.3772 0.2965 0.3091 -0.0527 0.0422  -0.0320 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.3785 0.2621 0.3123 -0.0172 0.0474  -0.0030 58  TYR A N   
513  C CA  . TYR A 57  ? 0.3965 0.2687 0.3208 -0.0121 0.0456  0.0038  58  TYR A CA  
514  C C   . TYR A 57  ? 0.4648 0.3083 0.3730 -0.0146 0.0532  0.0054  58  TYR A C   
515  O O   . TYR A 57  ? 0.4501 0.2820 0.3449 -0.0203 0.0558  0.0084  58  TYR A O   
516  C CB  . TYR A 57  ? 0.4234 0.3018 0.3543 0.0014  0.0389  0.0074  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.4816 0.3454 0.3993 0.0086  0.0354  0.0152  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.5029 0.3714 0.4135 0.0047  0.0322  0.0188  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.5431 0.3870 0.4538 0.0198  0.0348  0.0187  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.5378 0.3906 0.4317 0.0105  0.0287  0.0264  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.5930 0.4198 0.4870 0.0274  0.0299  0.0270  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6749 0.5060 0.5593 0.0221  0.0269  0.0311  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.7602 0.5721 0.6241 0.0290  0.0220  0.0395  58  TYR A OH  
524  N N   A SER A 58  ? 0.4344 0.2653 0.3429 -0.0113 0.0577  0.0027  59  SER A N   
525  N N   B SER A 58  ? 0.4388 0.2699 0.3474 -0.0112 0.0576  0.0027  59  SER A N   
526  C CA  A SER A 58  ? 0.4683 0.2684 0.3609 -0.0135 0.0658  0.0033  59  SER A CA  
527  C CA  B SER A 58  ? 0.4740 0.2746 0.3671 -0.0135 0.0658  0.0031  59  SER A CA  
528  C C   A SER A 58  ? 0.5363 0.3329 0.4219 -0.0308 0.0738  -0.0022 59  SER A C   
529  C C   B SER A 58  ? 0.5366 0.3337 0.4224 -0.0307 0.0736  -0.0021 59  SER A C   
530  O O   A SER A 58  ? 0.5667 0.3406 0.4351 -0.0370 0.0800  0.0001  59  SER A O   
531  O O   B SER A 58  ? 0.5632 0.3384 0.4319 -0.0367 0.0794  0.0005  59  SER A O   
532  C CB  A SER A 58  ? 0.4972 0.2887 0.3954 -0.0062 0.0691  -0.0007 59  SER A CB  
533  C CB  B SER A 58  ? 0.5101 0.3035 0.4095 -0.0073 0.0694  -0.0016 59  SER A CB  
534  O OG  A SER A 58  ? 0.5211 0.3150 0.4264 0.0107  0.0620  0.0032  59  SER A OG  
535  O OG  B SER A 58  ? 0.6103 0.3708 0.4937 -0.0086 0.0777  -0.0013 59  SER A OG  
536  N N   . ILE A 59  ? 0.4738 0.2929 0.3719 -0.0389 0.0732  -0.0098 60  ILE A N   
537  C CA  . ILE A 59  ? 0.4633 0.2866 0.3596 -0.0544 0.0785  -0.0173 60  ILE A CA  
538  C C   . ILE A 59  ? 0.5007 0.3293 0.3932 -0.0611 0.0784  -0.0161 60  ILE A C   
539  O O   . ILE A 59  ? 0.5301 0.3449 0.4118 -0.0724 0.0870  -0.0193 60  ILE A O   
540  C CB  . ILE A 59  ? 0.4679 0.3155 0.3775 -0.0587 0.0745  -0.0251 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.4786 0.3185 0.3884 -0.0568 0.0780  -0.0289 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.4349 0.2940 0.3463 -0.0727 0.0764  -0.0337 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.5112 0.3722 0.4297 -0.0583 0.0724  -0.0338 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.4208 0.2689 0.3219 -0.0556 0.0700  -0.0127 61  PHE A N   
545  C CA  . PHE A 60  ? 0.4210 0.2770 0.3206 -0.0630 0.0708  -0.0138 61  PHE A CA  
546  C C   . PHE A 60  ? 0.4940 0.3283 0.3753 -0.0613 0.0738  -0.0056 61  PHE A C   
547  O O   . PHE A 60  ? 0.5048 0.3424 0.3815 -0.0698 0.0771  -0.0074 61  PHE A O   
548  C CB  . PHE A 60  ? 0.4113 0.2967 0.3272 -0.0602 0.0616  -0.0159 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.4064 0.3087 0.3347 -0.0627 0.0581  -0.0236 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.4445 0.3516 0.3751 -0.0740 0.0625  -0.0332 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.4063 0.3185 0.3421 -0.0545 0.0505  -0.0216 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.4388 0.3608 0.3783 -0.0753 0.0572  -0.0400 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.4375 0.3612 0.3793 -0.0570 0.0467  -0.0276 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.4133 0.3416 0.3564 -0.0665 0.0491  -0.0363 61  PHE A CZ  
555  N N   . THR A 61  ? 0.4753 0.2860 0.3445 -0.0512 0.0734  0.0024  62  THR A N   
556  C CA  . THR A 61  ? 0.5056 0.2888 0.3511 -0.0496 0.0760  0.0108  62  THR A CA  
557  C C   . THR A 61  ? 0.6154 0.3654 0.4411 -0.0592 0.0882  0.0095  62  THR A C   
558  O O   . THR A 61  ? 0.6304 0.3501 0.4304 -0.0612 0.0929  0.0161  62  THR A O   
559  C CB  . THR A 61  ? 0.5948 0.3709 0.4366 -0.0317 0.0663  0.0206  62  THR A CB  
560  O OG1 . THR A 61  ? 0.5735 0.3451 0.4236 -0.0219 0.0650  0.0196  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.5365 0.3418 0.3923 -0.0256 0.0560  0.0220  62  THR A CG2 
562  N N   . ASP A 62  ? 0.5755 0.3292 0.4105 -0.0664 0.0939  0.0006  63  ASP A N   
563  C CA  . ASP A 62  ? 0.6086 0.3327 0.4264 -0.0780 0.1068  -0.0030 63  ASP A CA  
564  C C   . ASP A 62  ? 0.6827 0.4126 0.4958 -0.0976 0.1158  -0.0103 63  ASP A C   
565  O O   . ASP A 62  ? 0.6396 0.4040 0.4738 -0.1041 0.1133  -0.0195 63  ASP A O   
566  C CB  . ASP A 62  ? 0.6210 0.3499 0.4509 -0.0801 0.1097  -0.0116 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.8117 0.5121 0.6246 -0.0950 0.1241  -0.0174 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.9001 0.5631 0.6940 -0.0893 0.1289  -0.0116 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.8228 0.5377 0.6412 -0.1123 0.1308  -0.0283 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.7184 0.4136 0.5036 -0.1072 0.1268  -0.0072 64  GLN A N   
571  C CA  . GLN A 63  ? 0.7383 0.4355 0.5159 -0.1277 0.1381  -0.0149 64  GLN A CA  
572  C C   . GLN A 63  ? 0.7810 0.5048 0.5791 -0.1442 0.1449  -0.0322 64  GLN A C   
573  O O   . GLN A 63  ? 0.7991 0.5453 0.6061 -0.1571 0.1491  -0.0415 64  GLN A O   
574  C CB  . GLN A 63  ? 0.8130 0.4604 0.5516 -0.1364 0.1507  -0.0084 64  GLN A CB  
575  C CG  . GLN A 63  ? 1.0762 0.7022 0.7919 -0.1236 0.1434  0.0072  64  GLN A CG  
576  N N   . LEU A 64  ? 0.6943 0.4168 0.5001 -0.1441 0.1460  -0.0377 65  LEU A N   
577  C CA  . LEU A 64  ? 0.6621 0.4118 0.4872 -0.1588 0.1501  -0.0546 65  LEU A CA  
578  C C   . LEU A 64  ? 0.6762 0.4689 0.5313 -0.1488 0.1352  -0.0586 65  LEU A C   
579  O O   . LEU A 64  ? 0.6808 0.5063 0.5549 -0.1576 0.1337  -0.0710 65  LEU A O   
580  C CB  . LEU A 64  ? 0.6817 0.4078 0.4976 -0.1658 0.1593  -0.0600 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.7905 0.4796 0.5803 -0.1848 0.1780  -0.0641 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.8064 0.4729 0.5892 -0.1888 0.1853  -0.0690 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.8381 0.5512 0.6370 -0.2075 0.1875  -0.0800 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.5907 0.3823 0.4495 -0.1309 0.1247  -0.0494 66  LYS A N   
585  C CA  . LYS A 65  ? 0.5503 0.3756 0.4319 -0.1222 0.1117  -0.0523 66  LYS A CA  
586  C C   . LYS A 65  ? 0.5903 0.4420 0.4850 -0.1159 0.1019  -0.0498 66  LYS A C   
587  O O   . LYS A 65  ? 0.5479 0.4290 0.4609 -0.1137 0.0929  -0.0557 66  LYS A O   
588  C CB  . LYS A 65  ? 0.5664 0.3816 0.4473 -0.1079 0.1062  -0.0452 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.5761 0.3691 0.4477 -0.1134 0.1151  -0.0499 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.5275 0.3178 0.4030 -0.0994 0.1095  -0.0454 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.6162 0.3786 0.4805 -0.1024 0.1196  -0.0490 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.6295 0.3539 0.4751 -0.0965 0.1261  -0.0403 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.5928 0.4326 0.4764 -0.1129 0.1033  -0.0413 67  CYS A N   
594  C CA  . CYS A 66  ? 0.5858 0.4477 0.4796 -0.1077 0.0955  -0.0392 67  CYS A CA  
595  C C   . CYS A 66  ? 0.6345 0.5275 0.5467 -0.1183 0.0959  -0.0532 67  CYS A C   
596  O O   . CYS A 66  ? 0.6195 0.5369 0.5467 -0.1120 0.0869  -0.0544 67  CYS A O   
597  C CB  . CYS A 66  ? 0.6169 0.4576 0.4911 -0.1064 0.0993  -0.0296 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.7079 0.5290 0.5624 -0.1277 0.1168  -0.0359 67  CYS A SG  
599  N N   . ASN A 67  ? 0.5904 0.4822 0.5018 -0.1343 0.1064  -0.0649 68  ASN A N   
600  C CA  . ASN A 67  ? 0.5831 0.5056 0.5135 -0.1460 0.1082  -0.0812 68  ASN A CA  
601  C C   . ASN A 67  ? 0.5964 0.5440 0.5459 -0.1452 0.0999  -0.0917 68  ASN A C   
602  O O   . ASN A 67  ? 0.5807 0.5573 0.5488 -0.1529 0.0989  -0.1066 68  ASN A O   
603  C CB  . ASN A 67  ? 0.6168 0.5254 0.5349 -0.1663 0.1259  -0.0897 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.8288 0.7177 0.7279 -0.1688 0.1333  -0.0815 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.8387 0.6936 0.7116 -0.1792 0.1465  -0.0778 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.7003 0.6068 0.6089 -0.1591 0.1247  -0.0778 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.5441 0.4818 0.4891 -0.1360 0.0935  -0.0850 69  LEU A N   
608  C CA  . LEU A 68  ? 0.5228 0.4805 0.4805 -0.1354 0.0850  -0.0938 69  LEU A CA  
609  C C   . LEU A 68  ? 0.5219 0.5053 0.4953 -0.1222 0.0688  -0.0925 69  LEU A C   
610  O O   . LEU A 68  ? 0.5014 0.4782 0.4712 -0.1106 0.0639  -0.0808 69  LEU A O   
611  C CB  . LEU A 68  ? 0.5380 0.4731 0.4823 -0.1318 0.0860  -0.0876 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.6186 0.5249 0.5464 -0.1440 0.1015  -0.0899 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.6295 0.5155 0.5469 -0.1378 0.1015  -0.0842 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.6289 0.5496 0.5640 -0.1626 0.1088  -0.1077 69  LEU A CD2 
615  N N   . SER A 69  ? 0.4592 0.4702 0.4487 -0.1237 0.0601  -0.1048 70  SER A N   
616  C CA  A SER A 69  ? 0.4391 0.4715 0.4412 -0.1107 0.0437  -0.1045 70  SER A CA  
617  C CA  B SER A 69  ? 0.4422 0.4740 0.4440 -0.1105 0.0437  -0.1040 70  SER A CA  
618  C C   . SER A 69  ? 0.4601 0.4866 0.4538 -0.1036 0.0339  -0.0999 70  SER A C   
619  O O   . SER A 69  ? 0.4108 0.4448 0.4070 -0.0921 0.0207  -0.0960 70  SER A O   
620  C CB  A SER A 69  ? 0.4812 0.5473 0.5056 -0.1146 0.0384  -0.1213 70  SER A CB  
621  C CB  B SER A 69  ? 0.4860 0.5515 0.5103 -0.1138 0.0383  -0.1203 70  SER A CB  
622  O OG  A SER A 69  ? 0.5571 0.6303 0.5897 -0.1224 0.0486  -0.1270 70  SER A OG  
623  O OG  B SER A 69  ? 0.5708 0.6485 0.6003 -0.1243 0.0392  -0.1340 70  SER A OG  
624  N N   . VAL A 70  ? 0.4250 0.4361 0.4069 -0.1115 0.0413  -0.1012 71  VAL A N   
625  C CA  . VAL A 70  ? 0.4195 0.4230 0.3907 -0.1078 0.0350  -0.0983 71  VAL A CA  
626  C C   . VAL A 70  ? 0.4596 0.4332 0.4146 -0.1096 0.0468  -0.0900 71  VAL A C   
627  O O   . VAL A 70  ? 0.4637 0.4241 0.4142 -0.1195 0.0598  -0.0933 71  VAL A O   
628  C CB  . VAL A 70  ? 0.4836 0.5044 0.4593 -0.1162 0.0301  -0.1130 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.4917 0.5027 0.4523 -0.1136 0.0240  -0.1101 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.4758 0.5290 0.4709 -0.1127 0.0171  -0.1231 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.3867 0.3490 0.3328 -0.1002 0.0426  -0.0802 72  ILE A N   
632  C CA  . ILE A 71  ? 0.3895 0.3272 0.3234 -0.0993 0.0518  -0.0739 72  ILE A CA  
633  C C   . ILE A 71  ? 0.4370 0.3727 0.3619 -0.0996 0.0478  -0.0761 72  ILE A C   
634  O O   . ILE A 71  ? 0.4338 0.3773 0.3571 -0.0931 0.0371  -0.0728 72  ILE A O   
635  C CB  . ILE A 71  ? 0.4112 0.3381 0.3442 -0.0886 0.0531  -0.0615 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.4210 0.3475 0.3585 -0.0894 0.0573  -0.0591 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.4350 0.3401 0.3588 -0.0854 0.0610  -0.0567 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.4870 0.3954 0.4170 -0.0994 0.0709  -0.0625 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.4132 0.3357 0.3299 -0.1076 0.0570  -0.0816 73  ASN A N   
640  C CA  . ASN A 72  ? 0.4232 0.3420 0.3289 -0.1095 0.0550  -0.0845 73  ASN A CA  
641  C C   . ASN A 72  ? 0.4608 0.3600 0.3599 -0.1041 0.0634  -0.0780 73  ASN A C   
642  O O   . ASN A 72  ? 0.4460 0.3283 0.3444 -0.1052 0.0749  -0.0780 73  ASN A O   
643  C CB  . ASN A 72  ? 0.4756 0.3945 0.3768 -0.1229 0.0600  -0.0973 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.7056 0.6474 0.6166 -0.1294 0.0527  -0.1070 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.5707 0.5313 0.4845 -0.1252 0.0383  -0.1084 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.6763 0.6169 0.5924 -0.1398 0.0627  -0.1149 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.4027 0.3030 0.2963 -0.0987 0.0580  -0.0736 74  LEU A N   
648  C CA  . LEU A 73  ? 0.4032 0.2896 0.2935 -0.0943 0.0662  -0.0701 74  LEU A CA  
649  C C   . LEU A 73  ? 0.4602 0.3357 0.3397 -0.1025 0.0747  -0.0786 74  LEU A C   
650  O O   . LEU A 73  ? 0.4771 0.3572 0.3483 -0.1117 0.0715  -0.0861 74  LEU A O   
651  C CB  . LEU A 73  ? 0.3976 0.2891 0.2864 -0.0873 0.0598  -0.0633 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.4366 0.3382 0.3354 -0.0789 0.0519  -0.0552 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.4370 0.3387 0.3336 -0.0736 0.0500  -0.0497 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.4394 0.3376 0.3494 -0.0747 0.0570  -0.0520 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.4244 0.2868 0.3047 -0.0989 0.0850  -0.0784 75  ASP A N   
656  C CA  . ASP A 74  ? 0.4557 0.3061 0.3272 -0.1057 0.0954  -0.0872 75  ASP A CA  
657  C C   . ASP A 74  ? 0.5262 0.3830 0.3822 -0.1134 0.0900  -0.0911 75  ASP A C   
658  O O   . ASP A 74  ? 0.5060 0.3697 0.3590 -0.1095 0.0828  -0.0853 75  ASP A O   
659  C CB  . ASP A 74  ? 0.4771 0.3176 0.3562 -0.0970 0.1050  -0.0860 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.6174 0.4441 0.4906 -0.1023 0.1178  -0.0962 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.6295 0.4588 0.4910 -0.1103 0.1192  -0.1021 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.6652 0.4767 0.5441 -0.0982 0.1266  -0.0984 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.5445 0.3974 0.3881 -0.1249 0.0929  -0.1009 76  PRO A N   
664  C CA  . PRO A 75  ? 0.5556 0.4124 0.3797 -0.1322 0.0861  -0.1040 76  PRO A CA  
665  C C   . PRO A 75  ? 0.6053 0.4556 0.4193 -0.1317 0.0912  -0.1026 76  PRO A C   
666  O O   . PRO A 75  ? 0.6329 0.4839 0.4277 -0.1364 0.0840  -0.1018 76  PRO A O   
667  C CB  . PRO A 75  ? 0.5958 0.4482 0.4097 -0.1448 0.0911  -0.1162 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.6638 0.5036 0.4902 -0.1442 0.1055  -0.1200 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.5822 0.4254 0.4262 -0.1325 0.1022  -0.1098 76  PRO A CD  
670  N N   . GLU A 76  ? 0.5519 0.3957 0.3780 -0.1262 0.1034  -0.1027 77  GLU A N   
671  C CA  . GLU A 76  ? 0.5671 0.4080 0.3872 -0.1269 0.1102  -0.1037 77  GLU A CA  
672  C C   . GLU A 76  ? 0.5674 0.4166 0.3897 -0.1203 0.1010  -0.0933 77  GLU A C   
673  O O   . GLU A 76  ? 0.5634 0.4106 0.3762 -0.1236 0.1050  -0.0938 77  GLU A O   
674  C CB  . GLU A 76  ? 0.5984 0.4335 0.4351 -0.1217 0.1255  -0.1094 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.8672 0.6904 0.6966 -0.1304 0.1381  -0.1219 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.3007 1.1203 1.1104 -0.1421 0.1456  -0.1302 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.3114 1.1327 1.1282 -0.1399 0.1551  -0.1336 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.3128 1.1287 1.0997 -0.1541 0.1420  -0.1341 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.4943 0.3519 0.3282 -0.1121 0.0902  -0.0851 78  ILE A N   
680  C CA  . ILE A 77  ? 0.4817 0.3462 0.3183 -0.1057 0.0817  -0.0759 78  ILE A CA  
681  C C   . ILE A 77  ? 0.5445 0.4066 0.3572 -0.1113 0.0708  -0.0730 78  ILE A C   
682  O O   . ILE A 77  ? 0.5335 0.3975 0.3373 -0.1140 0.0611  -0.0740 78  ILE A O   
683  C CB  . ILE A 77  ? 0.4933 0.3667 0.3498 -0.0953 0.0750  -0.0688 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.5062 0.3772 0.3818 -0.0884 0.0851  -0.0703 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.4509 0.3311 0.3090 -0.0896 0.0662  -0.0602 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.5772 0.4483 0.4613 -0.0845 0.0952  -0.0729 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.5364 0.3941 0.3390 -0.1127 0.0724  -0.0699 79  ASN A N   
688  C CA  . ASN A 78  ? 0.5555 0.4044 0.3308 -0.1174 0.0631  -0.0656 79  ASN A CA  
689  C C   . ASN A 78  ? 0.5577 0.4125 0.3384 -0.1080 0.0480  -0.0563 79  ASN A C   
690  O O   . ASN A 78  ? 0.5177 0.3792 0.3165 -0.1010 0.0496  -0.0520 79  ASN A O   
691  C CB  . ASN A 78  ? 0.6008 0.4400 0.3632 -0.1245 0.0746  -0.0671 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.8382 0.6620 0.5678 -0.1299 0.0669  -0.0614 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.6867 0.5082 0.4160 -0.1264 0.0636  -0.0547 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.7577 0.5685 0.4569 -0.1387 0.0636  -0.0639 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.5314 0.3849 0.2972 -0.1070 0.0327  -0.0540 80  PRO A N   
696  C CA  . PRO A 79  ? 0.5162 0.3757 0.2889 -0.0970 0.0185  -0.0467 80  PRO A CA  
697  C C   . PRO A 79  ? 0.5640 0.4135 0.3285 -0.0948 0.0186  -0.0392 80  PRO A C   
698  O O   . PRO A 79  ? 0.5386 0.3964 0.3207 -0.0864 0.0146  -0.0347 80  PRO A O   
699  C CB  . PRO A 79  ? 0.5604 0.4181 0.3144 -0.0970 0.0025  -0.0476 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.6254 0.4844 0.3744 -0.1063 0.0087  -0.0569 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.5761 0.4240 0.3195 -0.1142 0.0268  -0.0591 80  PRO A CD  
702  N N   . GLU A 80  ? 0.5396 0.3705 0.2765 -0.1036 0.0243  -0.0387 81  GLU A N   
703  C CA  . GLU A 80  ? 0.5495 0.3686 0.2763 -0.1040 0.0262  -0.0327 81  GLU A CA  
704  C C   . GLU A 80  ? 0.5511 0.3840 0.3074 -0.1019 0.0387  -0.0344 81  GLU A C   
705  O O   . GLU A 80  ? 0.5174 0.3535 0.2835 -0.0959 0.0349  -0.0294 81  GLU A O   
706  C CB  . GLU A 80  ? 0.6051 0.3992 0.2931 -0.1165 0.0319  -0.0327 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.7755 0.5533 0.4486 -0.1184 0.0335  -0.0264 81  GLU A CG  
708  C CD  . GLU A 80  ? 1.1506 0.9019 0.7854 -0.1336 0.0439  -0.0271 81  GLU A CD  
709  O OE1 . GLU A 80  ? 1.1880 0.9154 0.7948 -0.1351 0.0386  -0.0198 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 1.1010 0.8538 0.7329 -0.1445 0.0582  -0.0355 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.5206 0.3622 0.2916 -0.1058 0.0521  -0.0419 82  GLY A N   
712  C CA  . GLY A 81  ? 0.4953 0.3518 0.2958 -0.1016 0.0619  -0.0445 82  GLY A CA  
713  C C   . GLY A 81  ? 0.4932 0.3640 0.3180 -0.0895 0.0529  -0.0397 82  GLY A C   
714  O O   . GLY A 81  ? 0.4611 0.3399 0.3008 -0.0846 0.0536  -0.0371 82  GLY A O   
715  N N   . PHE A 82  ? 0.4358 0.3104 0.2637 -0.0856 0.0446  -0.0392 83  PHE A N   
716  C CA  . PHE A 82  ? 0.4075 0.2947 0.2560 -0.0760 0.0372  -0.0356 83  PHE A CA  
717  C C   . PHE A 82  ? 0.4319 0.3177 0.2759 -0.0715 0.0268  -0.0291 83  PHE A C   
718  O O   . PHE A 82  ? 0.3974 0.2925 0.2583 -0.0653 0.0259  -0.0263 83  PHE A O   
719  C CB  . PHE A 82  ? 0.4194 0.3116 0.2715 -0.0753 0.0316  -0.0384 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.4079 0.3126 0.2810 -0.0675 0.0273  -0.0359 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.4333 0.3427 0.3238 -0.0642 0.0354  -0.0362 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.4068 0.3175 0.2811 -0.0631 0.0152  -0.0335 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.4307 0.3486 0.3358 -0.0584 0.0321  -0.0333 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.4225 0.3449 0.3153 -0.0576 0.0130  -0.0323 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.4036 0.3285 0.3099 -0.0560 0.0219  -0.0318 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.4492 0.3224 0.2695 -0.0739 0.0184  -0.0269 84  CYS A N   
727  C CA  . CYS A 83  ? 0.4828 0.3501 0.2956 -0.0685 0.0076  -0.0210 84  CYS A CA  
728  C C   . CYS A 83  ? 0.4868 0.3506 0.3022 -0.0699 0.0152  -0.0183 84  CYS A C   
729  O O   . CYS A 83  ? 0.4586 0.3287 0.2865 -0.0634 0.0108  -0.0152 84  CYS A O   
730  C CB  . CYS A 83  ? 0.5520 0.4007 0.3333 -0.0708 -0.0024 -0.0188 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.6370 0.4739 0.4069 -0.0616 -0.0175 -0.0115 84  CYS A SG  
732  N N   . ILE A 84  ? 0.4443 0.3001 0.2496 -0.0793 0.0274  -0.0212 85  ILE A N   
733  C CA  . ILE A 84  ? 0.4293 0.2845 0.2381 -0.0833 0.0366  -0.0216 85  ILE A CA  
734  C C   . ILE A 84  ? 0.4253 0.3034 0.2677 -0.0759 0.0392  -0.0230 85  ILE A C   
735  O O   . ILE A 84  ? 0.3988 0.2810 0.2490 -0.0736 0.0384  -0.0211 85  ILE A O   
736  C CB  . ILE A 84  ? 0.4778 0.3246 0.2728 -0.0960 0.0510  -0.0275 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.5060 0.3239 0.2597 -0.1050 0.0485  -0.0243 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.4690 0.3269 0.2807 -0.1000 0.0633  -0.0325 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.5900 0.3995 0.3271 -0.1178 0.0613  -0.0311 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.3846 0.2753 0.2443 -0.0723 0.0418  -0.0263 86  LEU A N   
741  C CA  . LEU A 85  ? 0.3713 0.2797 0.2581 -0.0645 0.0432  -0.0268 86  LEU A CA  
742  C C   . LEU A 85  ? 0.3946 0.3087 0.2894 -0.0567 0.0327  -0.0217 86  LEU A C   
743  O O   . LEU A 85  ? 0.3671 0.2916 0.2766 -0.0520 0.0324  -0.0204 86  LEU A O   
744  C CB  . LEU A 85  ? 0.3799 0.2945 0.2790 -0.0628 0.0498  -0.0314 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.4572 0.3722 0.3573 -0.0688 0.0625  -0.0389 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.4751 0.3917 0.3841 -0.0665 0.0682  -0.0437 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.4730 0.4016 0.3900 -0.0667 0.0669  -0.0415 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.3695 0.2788 0.2556 -0.0553 0.0241  -0.0199 87  LEU A N   
749  C CA  . LEU A 86  ? 0.3525 0.2689 0.2474 -0.0484 0.0147  -0.0171 87  LEU A CA  
750  C C   . LEU A 86  ? 0.3898 0.3015 0.2799 -0.0470 0.0109  -0.0138 87  LEU A C   
751  O O   . LEU A 86  ? 0.3603 0.2815 0.2639 -0.0422 0.0089  -0.0126 87  LEU A O   
752  C CB  . LEU A 86  ? 0.3561 0.2707 0.2438 -0.0477 0.0060  -0.0184 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.4055 0.3313 0.3059 -0.0411 -0.0025 -0.0184 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.3819 0.3202 0.3015 -0.0395 0.0032  -0.0194 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.4654 0.3929 0.3605 -0.0404 -0.0120 -0.0220 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.3849 0.2799 0.2536 -0.0520 0.0107  -0.0125 88  ASP A N   
757  C CA  . ASP A 87  ? 0.3895 0.2748 0.2498 -0.0523 0.0089  -0.0097 88  ASP A CA  
758  C C   . ASP A 87  ? 0.4100 0.3069 0.2861 -0.0542 0.0176  -0.0117 88  ASP A C   
759  O O   . ASP A 87  ? 0.4073 0.3077 0.2903 -0.0509 0.0147  -0.0104 88  ASP A O   
760  C CB  . ASP A 87  ? 0.4497 0.3103 0.2795 -0.0598 0.0100  -0.0081 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.6313 0.4773 0.4414 -0.0554 -0.0029 -0.0048 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.6191 0.4763 0.4427 -0.0460 -0.0132 -0.0048 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.6794 0.5032 0.4603 -0.0616 -0.0030 -0.0030 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.3767 0.2807 0.2596 -0.0591 0.0277  -0.0158 89  PHE A N   
765  C CA  . PHE A 88  ? 0.3462 0.2657 0.2473 -0.0596 0.0348  -0.0194 89  PHE A CA  
766  C C   . PHE A 88  ? 0.3460 0.2818 0.2674 -0.0503 0.0294  -0.0177 89  PHE A C   
767  O O   . PHE A 88  ? 0.3126 0.2573 0.2434 -0.0490 0.0291  -0.0182 89  PHE A O   
768  C CB  . PHE A 88  ? 0.3510 0.2774 0.2588 -0.0638 0.0452  -0.0256 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.3437 0.2908 0.2751 -0.0606 0.0495  -0.0302 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.3650 0.3175 0.2993 -0.0664 0.0542  -0.0343 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.3548 0.3151 0.3045 -0.0512 0.0476  -0.0302 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.3563 0.3312 0.3138 -0.0625 0.0558  -0.0393 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.3739 0.3529 0.3439 -0.0461 0.0486  -0.0338 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.3530 0.3413 0.3281 -0.0514 0.0521  -0.0388 89  PHE A CZ  
775  N N   . MET A 89  ? 0.3042 0.2434 0.2310 -0.0450 0.0259  -0.0162 90  MET A N   
776  C CA  . MET A 89  ? 0.2860 0.2371 0.2276 -0.0378 0.0220  -0.0144 90  MET A CA  
777  C C   . MET A 89  ? 0.3349 0.2868 0.2764 -0.0358 0.0158  -0.0123 90  MET A C   
778  O O   . MET A 89  ? 0.3277 0.2900 0.2796 -0.0329 0.0154  -0.0121 90  MET A O   
779  C CB  . MET A 89  ? 0.3043 0.2540 0.2463 -0.0355 0.0199  -0.0137 90  MET A CB  
780  C CG  . MET A 89  ? 0.3309 0.2793 0.2750 -0.0363 0.0265  -0.0161 90  MET A CG  
781  S SD  . MET A 89  ? 0.3756 0.3217 0.3200 -0.0352 0.0247  -0.0160 90  MET A SD  
782  C CE  . MET A 89  ? 0.3737 0.3123 0.3150 -0.0383 0.0334  -0.0201 90  MET A CE  
783  N N   . TYR A 90  ? 0.3079 0.2483 0.2368 -0.0366 0.0105  -0.0110 91  TYR A N   
784  C CA  . TYR A 90  ? 0.3091 0.2483 0.2380 -0.0333 0.0043  -0.0100 91  TYR A CA  
785  C C   . TYR A 90  ? 0.3641 0.2944 0.2849 -0.0371 0.0061  -0.0100 91  TYR A C   
786  O O   . TYR A 90  ? 0.3533 0.2810 0.2741 -0.0342 0.0018  -0.0098 91  TYR A O   
787  C CB  . TYR A 90  ? 0.3284 0.2601 0.2495 -0.0299 -0.0040 -0.0096 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.3364 0.2810 0.2701 -0.0264 -0.0065 -0.0117 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.3554 0.3018 0.2892 -0.0287 -0.0039 -0.0129 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.3382 0.2925 0.2832 -0.0220 -0.0102 -0.0136 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.3422 0.2988 0.2861 -0.0277 -0.0046 -0.0158 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.3379 0.3037 0.2933 -0.0211 -0.0110 -0.0170 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.3594 0.3259 0.3139 -0.0244 -0.0078 -0.0179 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.3470 0.3235 0.3106 -0.0255 -0.0072 -0.0223 91  TYR A OH  
795  N N   . THR A 91  ? 0.3313 0.2560 0.2447 -0.0444 0.0135  -0.0114 92  THR A N   
796  C CA  . THR A 91  ? 0.3550 0.2685 0.2579 -0.0505 0.0168  -0.0124 92  THR A CA  
797  C C   . THR A 91  ? 0.3820 0.3072 0.2940 -0.0576 0.0265  -0.0176 92  THR A C   
798  O O   . THR A 91  ? 0.3839 0.3028 0.2900 -0.0640 0.0302  -0.0199 92  THR A O   
799  C CB  . THR A 91  ? 0.4441 0.3301 0.3192 -0.0558 0.0165  -0.0100 92  THR A CB  
800  O OG1 . THR A 91  ? 0.4268 0.3115 0.2960 -0.0626 0.0240  -0.0120 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.4503 0.3239 0.3147 -0.0477 0.0047  -0.0058 92  THR A CG2 
802  N N   . SER A 92  ? 0.3149 0.2551 0.2397 -0.0572 0.0311  -0.0205 93  SER A N   
803  C CA  . SER A 92  ? 0.3036 0.2583 0.2399 -0.0630 0.0401  -0.0276 93  SER A CA  
804  C C   . SER A 92  ? 0.3642 0.3040 0.2835 -0.0751 0.0496  -0.0314 93  SER A C   
805  O O   . SER A 92  ? 0.3633 0.3155 0.2922 -0.0817 0.0588  -0.0394 93  SER A O   
806  C CB  . SER A 92  ? 0.3192 0.2860 0.2659 -0.0647 0.0404  -0.0313 93  SER A CB  
807  O OG  . SER A 92  ? 0.3968 0.3742 0.3544 -0.0553 0.0322  -0.0279 93  SER A OG  
808  N N   A ARG A 93  ? 0.3627 0.2766 0.2564 -0.0781 0.0473  -0.0263 94  ARG A N   
809  N N   B ARG A 93  ? 0.3487 0.2623 0.2421 -0.0784 0.0475  -0.0263 94  ARG A N   
810  C CA  A ARG A 93  ? 0.3921 0.2857 0.2620 -0.0907 0.0560  -0.0284 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.3717 0.2661 0.2423 -0.0911 0.0567  -0.0289 94  ARG A CA  
812  C C   A ARG A 93  ? 0.4394 0.3294 0.3027 -0.0912 0.0580  -0.0285 94  ARG A C   
813  C C   B ARG A 93  ? 0.4313 0.3202 0.2934 -0.0916 0.0582  -0.0285 94  ARG A C   
814  O O   A ARG A 93  ? 0.4263 0.3108 0.2848 -0.0834 0.0489  -0.0230 94  ARG A O   
815  O O   B ARG A 93  ? 0.4211 0.3035 0.2773 -0.0840 0.0487  -0.0227 94  ARG A O   
816  C CB  A ARG A 93  ? 0.4532 0.3153 0.2933 -0.0936 0.0514  -0.0221 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.4015 0.2653 0.2429 -0.0963 0.0543  -0.0239 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.5636 0.4251 0.4075 -0.0942 0.0505  -0.0227 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.3827 0.2498 0.2300 -0.1011 0.0580  -0.0275 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.6667 0.4958 0.4832 -0.0920 0.0427  -0.0154 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.5766 0.4126 0.3982 -0.1015 0.0527  -0.0214 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.7431 0.5393 0.5240 -0.1034 0.0486  -0.0137 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.6642 0.5040 0.4928 -0.1065 0.0569  -0.0258 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.8878 0.6663 0.6514 -0.1176 0.0596  -0.0170 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.8575 0.6679 0.6611 -0.1152 0.0609  -0.0251 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.7211 0.4663 0.4481 -0.1288 0.0654  -0.0148 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.6944 0.5105 0.5065 -0.1204 0.0652  -0.0304 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.7284 0.5213 0.5093 -0.1219 0.0653  -0.0231 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.7527 0.5257 0.5204 -0.1191 0.0603  -0.0190 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.3979 0.2919 0.2614 -0.1013 0.0708  -0.0364 95  LEU A N   
831  C CA  . LEU A 94  ? 0.4063 0.2969 0.2634 -0.1037 0.0752  -0.0387 95  LEU A CA  
832  C C   . LEU A 94  ? 0.4991 0.3628 0.3220 -0.1187 0.0836  -0.0398 95  LEU A C   
833  O O   . LEU A 94  ? 0.4905 0.3533 0.3095 -0.1317 0.0964  -0.0471 95  LEU A O   
834  C CB  . LEU A 94  ? 0.3886 0.3071 0.2760 -0.1013 0.0830  -0.0481 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.4390 0.3563 0.3246 -0.1019 0.0880  -0.0516 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.4252 0.3405 0.3127 -0.0900 0.0763  -0.0441 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.4266 0.3683 0.3398 -0.1014 0.0984  -0.0634 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.5099 0.3518 0.3069 -0.1177 0.0765  -0.0331 96  ASN A N   
839  C CA  . ASN A 95  ? 0.5484 0.3597 0.3059 -0.1313 0.0824  -0.0324 96  ASN A CA  
840  C C   . ASN A 95  ? 0.6005 0.4186 0.3590 -0.1405 0.0957  -0.0416 96  ASN A C   
841  O O   . ASN A 95  ? 0.6058 0.4163 0.3516 -0.1393 0.0922  -0.0401 96  ASN A O   
842  C CB  . ASN A 95  ? 0.6001 0.3856 0.3283 -0.1249 0.0667  -0.0216 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.8587 0.6080 0.5399 -0.1378 0.0704  -0.0191 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.7541 0.4891 0.4178 -0.1530 0.0842  -0.0231 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.7865 0.5203 0.4454 -0.1329 0.0583  -0.0132 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.5467 0.3821 0.3235 -0.1489 0.1109  -0.0527 97  LEU A N   
847  C CA  . LEU A 96  ? 0.5552 0.4017 0.3397 -0.1565 0.1250  -0.0642 97  LEU A CA  
848  C C   . LEU A 96  ? 0.6295 0.4505 0.3772 -0.1773 0.1392  -0.0686 97  LEU A C   
849  O O   . LEU A 96  ? 0.6247 0.4368 0.3616 -0.1889 0.1474  -0.0711 97  LEU A O   
850  C CB  . LEU A 96  ? 0.5376 0.4206 0.3661 -0.1521 0.1323  -0.0753 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.6025 0.5063 0.4542 -0.1512 0.1426  -0.0875 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.5995 0.5018 0.4544 -0.1384 0.1326  -0.0816 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.5848 0.5241 0.4791 -0.1447 0.1465  -0.0978 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.6092 0.4151 0.3336 -0.1831 0.1423  -0.0694 98  ARG A N   
855  C CA  . ARG A 97  ? 0.6577 0.4345 0.3396 -0.2038 0.1555  -0.0727 98  ARG A CA  
856  C C   . ARG A 97  ? 0.6879 0.4743 0.3740 -0.2116 0.1693  -0.0850 98  ARG A C   
857  O O   . ARG A 97  ? 0.6443 0.4502 0.3562 -0.1990 0.1640  -0.0869 98  ARG A O   
858  C CB  . ARG A 97  ? 0.7059 0.4428 0.3392 -0.2036 0.1412  -0.0580 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.7950 0.5184 0.4214 -0.1945 0.1267  -0.0458 98  ARG A CG  
860  C CD  . ARG A 97  ? 1.0502 0.7375 0.6336 -0.1896 0.1093  -0.0318 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.3199 0.9685 0.8499 -0.2076 0.1177  -0.0309 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.5855 1.2009 1.0796 -0.2214 0.1255  -0.0281 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.4508 1.0287 0.8928 -0.2385 0.1336  -0.0271 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.4391 1.0566 0.9472 -0.2193 0.1260  -0.0267 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.6797 0.4507 0.3392 -0.2332 0.1882  -0.0941 99  GLU A N   
866  C CA  . GLU A 98  ? 0.6825 0.4610 0.3435 -0.2426 0.2035  -0.1076 99  GLU A CA  
867  C C   . GLU A 98  ? 0.7507 0.5191 0.3975 -0.2338 0.1909  -0.1006 99  GLU A C   
868  O O   . GLU A 98  ? 0.7273 0.5160 0.3995 -0.2287 0.1955  -0.1098 99  GLU A O   
869  C CB  . GLU A 98  ? 0.7497 0.5029 0.3700 -0.2698 0.2242  -0.1156 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.9007 0.6644 0.5252 -0.2818 0.2436  -0.1327 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.3676 1.1049 0.9487 -0.3107 0.2656  -0.1413 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.3849 1.0786 0.9095 -0.3209 0.2606  -0.1286 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.4095 1.1691 1.0125 -0.3231 0.2881  -0.1615 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.7464 0.4844 0.3547 -0.2312 0.1744  -0.0853 100 GLY A N   
875  C CA  . GLY A 99  ? 0.7543 0.4821 0.3456 -0.2241 0.1605  -0.0788 100 GLY A CA  
876  C C   . GLY A 99  ? 0.7461 0.4992 0.3760 -0.2026 0.1451  -0.0751 100 GLY A C   
877  O O   . GLY A 99  ? 0.7442 0.4953 0.3674 -0.1985 0.1374  -0.0741 100 GLY A O   
878  N N   . ASN A 100 ? 0.6520 0.4282 0.3206 -0.1900 0.1411  -0.0737 101 ASN A N   
879  C CA  . ASN A 100 ? 0.6067 0.4034 0.3078 -0.1711 0.1272  -0.0696 101 ASN A CA  
880  C C   . ASN A 100 ? 0.6217 0.4509 0.3714 -0.1624 0.1350  -0.0785 101 ASN A C   
881  O O   . ASN A 100 ? 0.5909 0.4342 0.3650 -0.1480 0.1256  -0.0757 101 ASN A O   
882  C CB  . ASN A 100 ? 0.5914 0.3813 0.2882 -0.1597 0.1082  -0.0558 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.6601 0.4580 0.3733 -0.1579 0.1103  -0.0544 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.5468 0.3672 0.2905 -0.1583 0.1217  -0.0634 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.5905 0.3715 0.2858 -0.1545 0.0984  -0.0439 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.5922 0.4330 0.3556 -0.1708 0.1514  -0.0895 102 ILE A N   
887  C CA  . ILE A 101 ? 0.5569 0.4298 0.3670 -0.1608 0.1566  -0.0982 102 ILE A CA  
888  C C   . ILE A 101 ? 0.5694 0.4547 0.4021 -0.1505 0.1572  -0.1036 102 ILE A C   
889  O O   . ILE A 101 ? 0.5198 0.4228 0.3839 -0.1345 0.1498  -0.1016 102 ILE A O   
890  C CB  . ILE A 101 ? 0.5988 0.4852 0.4210 -0.1726 0.1746  -0.1120 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.5774 0.4994 0.4499 -0.1585 0.1752  -0.1200 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.6014 0.4784 0.4040 -0.1908 0.1936  -0.1248 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.5794 0.5194 0.4685 -0.1656 0.1845  -0.1292 102 ILE A CD1 
894  N N   . MET A 102 ? 0.5606 0.4342 0.3751 -0.1597 0.1657  -0.1100 103 MET A N   
895  C CA  . MET A 102 ? 0.5614 0.4428 0.3946 -0.1512 0.1676  -0.1160 103 MET A CA  
896  C C   . MET A 102 ? 0.5678 0.4455 0.4033 -0.1379 0.1503  -0.1041 103 MET A C   
897  O O   . MET A 102 ? 0.5338 0.4242 0.3979 -0.1245 0.1480  -0.1053 103 MET A O   
898  C CB  . MET A 102 ? 0.6298 0.4988 0.4414 -0.1657 0.1815  -0.1267 103 MET A CB  
899  C CG  . MET A 102 ? 0.7129 0.5891 0.5270 -0.1798 0.2021  -0.1421 103 MET A CG  
900  S SD  . MET A 102 ? 0.7601 0.6732 0.6303 -0.1677 0.2108  -0.1555 103 MET A SD  
901  C CE  . MET A 102 ? 0.7162 0.6358 0.6104 -0.1552 0.2147  -0.1649 103 MET A CE  
902  N N   . ALA A 103 ? 0.5408 0.4010 0.3464 -0.1413 0.1379  -0.0931 104 ALA A N   
903  C CA  . ALA A 103 ? 0.5274 0.3863 0.3354 -0.1304 0.1217  -0.0834 104 ALA A CA  
904  C C   . ALA A 103 ? 0.5338 0.4076 0.3686 -0.1166 0.1129  -0.0764 104 ALA A C   
905  O O   . ALA A 103 ? 0.4956 0.3767 0.3488 -0.1056 0.1070  -0.0739 104 ALA A O   
906  C CB  . ALA A 103 ? 0.5627 0.4029 0.3350 -0.1363 0.1098  -0.0750 104 ALA A CB  
907  N N   . VAL A 104 ? 0.4661 0.3428 0.3011 -0.1183 0.1130  -0.0737 105 VAL A N   
908  C CA  . VAL A 104 ? 0.4335 0.3246 0.2922 -0.1065 0.1051  -0.0680 105 VAL A CA  
909  C C   . VAL A 104 ? 0.4569 0.3675 0.3500 -0.0962 0.1104  -0.0744 105 VAL A C   
910  O O   . VAL A 104 ? 0.4200 0.3373 0.3289 -0.0839 0.1015  -0.0687 105 VAL A O   
911  C CB  . VAL A 104 ? 0.4772 0.3662 0.3277 -0.1119 0.1049  -0.0650 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.4451 0.3522 0.3227 -0.1007 0.0989  -0.0618 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.4917 0.3581 0.3084 -0.1168 0.0949  -0.0557 105 VAL A CG2 
914  N N   A MET A 105 ? 0.4302 0.3491 0.3341 -0.1007 0.1245  -0.0866 106 MET A N   
915  N N   B MET A 105 ? 0.4350 0.3539 0.3390 -0.1007 0.1245  -0.0866 106 MET A N   
916  C CA  A MET A 105 ? 0.4295 0.3663 0.3665 -0.0887 0.1284  -0.0937 106 MET A CA  
917  C CA  B MET A 105 ? 0.4317 0.3687 0.3688 -0.0887 0.1284  -0.0937 106 MET A CA  
918  C C   A MET A 105 ? 0.4746 0.4042 0.4156 -0.0797 0.1251  -0.0918 106 MET A C   
919  C C   B MET A 105 ? 0.4776 0.4072 0.4187 -0.0797 0.1251  -0.0918 106 MET A C   
920  O O   A MET A 105 ? 0.4554 0.3921 0.4162 -0.0656 0.1191  -0.0886 106 MET A O   
921  O O   B MET A 105 ? 0.4582 0.3949 0.4189 -0.0656 0.1190  -0.0885 106 MET A O   
922  C CB  A MET A 105 ? 0.4724 0.4208 0.4214 -0.0954 0.1448  -0.1095 106 MET A CB  
923  C CB  B MET A 105 ? 0.4757 0.4243 0.4249 -0.0953 0.1447  -0.1095 106 MET A CB  
924  C CG  A MET A 105 ? 0.5095 0.4790 0.4955 -0.0801 0.1465  -0.1175 106 MET A CG  
925  C CG  B MET A 105 ? 0.5144 0.4845 0.5007 -0.0801 0.1462  -0.1173 106 MET A CG  
926  S SD  A MET A 105 ? 0.5741 0.5656 0.5816 -0.0872 0.1649  -0.1387 106 MET A SD  
927  S SD  B MET A 105 ? 0.5855 0.5743 0.5915 -0.0871 0.1657  -0.1391 106 MET A SD  
928  C CE  A MET A 105 ? 0.5567 0.5320 0.5506 -0.0954 0.1790  -0.1489 106 MET A CE  
929  C CE  B MET A 105 ? 0.5408 0.5408 0.5808 -0.0647 0.1634  -0.1450 106 MET A CE  
930  N N   . ALA A 106 ? 0.4539 0.3678 0.3742 -0.0886 0.1292  -0.0941 107 ALA A N   
931  C CA  . ALA A 106 ? 0.4555 0.3599 0.3763 -0.0833 0.1278  -0.0937 107 ALA A CA  
932  C C   . ALA A 106 ? 0.4606 0.3621 0.3806 -0.0756 0.1135  -0.0814 107 ALA A C   
933  O O   . ALA A 106 ? 0.4400 0.3405 0.3733 -0.0653 0.1115  -0.0797 107 ALA A O   
934  C CB  . ALA A 106 ? 0.4842 0.3736 0.3799 -0.0968 0.1340  -0.0989 107 ALA A CB  
935  N N   . THR A 107 ? 0.4232 0.3227 0.3281 -0.0800 0.1039  -0.0731 108 THR A N   
936  C CA  . THR A 107 ? 0.4083 0.3079 0.3142 -0.0735 0.0912  -0.0632 108 THR A CA  
937  C C   . THR A 107 ? 0.4372 0.3488 0.3656 -0.0611 0.0874  -0.0590 108 THR A C   
938  O O   . THR A 107 ? 0.4032 0.3133 0.3386 -0.0536 0.0826  -0.0546 108 THR A O   
939  C CB  . THR A 107 ? 0.4789 0.3733 0.3641 -0.0797 0.0816  -0.0570 108 THR A CB  
940  O OG1 . THR A 107 ? 0.4767 0.3593 0.3384 -0.0909 0.0847  -0.0612 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.4422 0.3381 0.3294 -0.0742 0.0696  -0.0500 108 THR A CG2 
942  N N   . ALA A 108 ? 0.3882 0.3114 0.3267 -0.0600 0.0901  -0.0612 109 ALA A N   
943  C CA  . ALA A 108 ? 0.3657 0.3025 0.3251 -0.0486 0.0857  -0.0585 109 ALA A CA  
944  C C   . ALA A 108 ? 0.3921 0.3299 0.3683 -0.0373 0.0888  -0.0620 109 ALA A C   
945  O O   . ALA A 108 ? 0.3672 0.3070 0.3523 -0.0266 0.0818  -0.0561 109 ALA A O   
946  C CB  . ALA A 108 ? 0.3666 0.3172 0.3336 -0.0520 0.0893  -0.0631 109 ALA A CB  
947  N N   . MET A 109 ? 0.3655 0.2994 0.3437 -0.0396 0.0992  -0.0715 110 MET A N   
948  C CA  . MET A 109 ? 0.3743 0.3049 0.3670 -0.0276 0.1022  -0.0752 110 MET A CA  
949  C C   . MET A 109 ? 0.4216 0.3338 0.4037 -0.0245 0.0974  -0.0674 110 MET A C   
950  O O   . MET A 109 ? 0.4233 0.3314 0.4128 -0.0124 0.0927  -0.0626 110 MET A O   
951  C CB  . MET A 109 ? 0.4198 0.3494 0.4164 -0.0318 0.1155  -0.0885 110 MET A CB  
952  C CG  . MET A 109 ? 0.4807 0.4319 0.4966 -0.0309 0.1215  -0.0989 110 MET A CG  
953  S SD  . MET A 109 ? 0.5809 0.5316 0.5979 -0.0406 0.1397  -0.1164 110 MET A SD  
954  C CE  . MET A 109 ? 0.5537 0.4955 0.5875 -0.0228 0.1412  -0.1207 110 MET A CE  
955  N N   . TYR A 110 ? 0.3988 0.3002 0.3620 -0.0362 0.0981  -0.0663 111 TYR A N   
956  C CA  . TYR A 110 ? 0.4049 0.2914 0.3575 -0.0375 0.0952  -0.0613 111 TYR A CA  
957  C C   . TYR A 110 ? 0.4304 0.3204 0.3842 -0.0321 0.0846  -0.0509 111 TYR A C   
958  O O   . TYR A 110 ? 0.4149 0.2941 0.3685 -0.0264 0.0833  -0.0467 111 TYR A O   
959  C CB  . TYR A 110 ? 0.4212 0.3023 0.3552 -0.0518 0.0963  -0.0641 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.4317 0.3037 0.3561 -0.0559 0.0923  -0.0608 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.4736 0.3302 0.3957 -0.0566 0.0989  -0.0646 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.4207 0.2996 0.3383 -0.0602 0.0826  -0.0555 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.4418 0.2914 0.3557 -0.0627 0.0968  -0.0634 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.4229 0.2977 0.3347 -0.0651 0.0796  -0.0552 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.4551 0.3161 0.3651 -0.0674 0.0872  -0.0596 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.4501 0.3086 0.3548 -0.0746 0.0858  -0.0612 111 TYR A OH  
967  N N   . LEU A 111 ? 0.3812 0.2844 0.3350 -0.0344 0.0780  -0.0470 112 LEU A N   
968  C CA  . LEU A 111 ? 0.3572 0.2653 0.3122 -0.0305 0.0687  -0.0385 112 LEU A CA  
969  C C   . LEU A 111 ? 0.3900 0.3042 0.3586 -0.0180 0.0658  -0.0353 112 LEU A C   
970  O O   . LEU A 111 ? 0.3750 0.2906 0.3432 -0.0144 0.0591  -0.0285 112 LEU A O   
971  C CB  . LEU A 111 ? 0.3400 0.2574 0.2891 -0.0369 0.0629  -0.0363 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.3867 0.2984 0.3201 -0.0471 0.0611  -0.0377 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.3760 0.2937 0.3029 -0.0500 0.0535  -0.0342 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.4017 0.3073 0.3319 -0.0485 0.0589  -0.0365 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.3674 0.2868 0.3484 -0.0116 0.0704  -0.0412 113 GLN A N   
976  C CA  . GLN A 112 ? 0.3680 0.2962 0.3638 0.0020  0.0661  -0.0399 113 GLN A CA  
977  C C   . GLN A 112 ? 0.3859 0.3320 0.3867 0.0013  0.0591  -0.0368 113 GLN A C   
978  O O   . GLN A 112 ? 0.3632 0.3105 0.3631 0.0066  0.0514  -0.0296 113 GLN A O   
979  C CB  . GLN A 112 ? 0.3949 0.3060 0.3857 0.0117  0.0626  -0.0331 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.4548 0.3448 0.4400 0.0125  0.0705  -0.0368 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.5857 0.4529 0.5580 0.0171  0.0682  -0.0289 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.4906 0.3572 0.4617 0.0254  0.0605  -0.0215 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.5459 0.3925 0.5060 0.0102  0.0754  -0.0306 113 GLN A NE2 
984  N N   . MET A 113 ? 0.3390 0.2967 0.3424 -0.0071 0.0630  -0.0426 114 MET A N   
985  C CA  . MET A 113 ? 0.3257 0.2987 0.3328 -0.0103 0.0588  -0.0417 114 MET A CA  
986  C C   . MET A 113 ? 0.3988 0.3899 0.4240 -0.0084 0.0641  -0.0521 114 MET A C   
987  O O   . MET A 113 ? 0.3821 0.3762 0.4054 -0.0187 0.0725  -0.0595 114 MET A O   
988  C CB  . MET A 113 ? 0.3434 0.3095 0.3335 -0.0233 0.0595  -0.0398 114 MET A CB  
989  C CG  . MET A 113 ? 0.3745 0.3283 0.3515 -0.0243 0.0536  -0.0320 114 MET A CG  
990  S SD  . MET A 113 ? 0.4198 0.3653 0.3776 -0.0364 0.0523  -0.0309 114 MET A SD  
991  C CE  . MET A 113 ? 0.3746 0.3303 0.3347 -0.0373 0.0472  -0.0283 114 MET A CE  
992  N N   . GLU A 114 ? 0.3884 0.3907 0.4309 0.0053  0.0594  -0.0535 115 GLU A N   
993  C CA  . GLU A 114 ? 0.4051 0.4283 0.4708 0.0110  0.0631  -0.0654 115 GLU A CA  
994  C C   . GLU A 114 ? 0.4095 0.4529 0.4831 0.0001  0.0678  -0.0737 115 GLU A C   
995  O O   . GLU A 114 ? 0.4049 0.4600 0.4908 -0.0040 0.0776  -0.0863 115 GLU A O   
996  C CB  . GLU A 114 ? 0.4396 0.4713 0.5202 0.0296  0.0530  -0.0637 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.6354 0.6434 0.7075 0.0406  0.0507  -0.0573 115 GLU A CG  
998  N N   . HIS A 115 ? 0.3495 0.3959 0.4156 -0.0056 0.0623  -0.0679 116 HIS A N   
999  C CA  . HIS A 115 ? 0.3634 0.4254 0.4346 -0.0174 0.0680  -0.0761 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.4092 0.4576 0.4632 -0.0341 0.0798  -0.0796 116 HIS A C   
1001 O O   . HIS A 115 ? 0.4176 0.4781 0.4792 -0.0435 0.0901  -0.0915 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.3805 0.4469 0.4473 -0.0192 0.0597  -0.0698 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.4289 0.5120 0.5121 -0.0048 0.0488  -0.0687 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.4581 0.5683 0.5673 0.0022  0.0485  -0.0804 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.4513 0.5278 0.5269 0.0031  0.0378  -0.0579 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.4501 0.5677 0.5649 0.0153  0.0358  -0.0752 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.4537 0.5504 0.5473 0.0154  0.0298  -0.0615 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.3437 0.3673 0.3743 -0.0377 0.0786  -0.0704 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.3481 0.3554 0.3577 -0.0522 0.0878  -0.0725 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.4134 0.4249 0.4319 -0.0539 0.0994  -0.0842 117 VAL A C   
1011 O O   . VAL A 116 ? 0.3908 0.4025 0.4032 -0.0673 0.1110  -0.0930 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.3902 0.3736 0.3748 -0.0544 0.0817  -0.0612 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.4044 0.3708 0.3655 -0.0683 0.0897  -0.0638 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.3789 0.3594 0.3560 -0.0537 0.0717  -0.0521 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.3657 0.3783 0.3971 -0.0409 0.0973  -0.0848 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.3752 0.3919 0.4180 -0.0400 0.1082  -0.0970 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.4425 0.4860 0.5089 -0.0428 0.1167  -0.1122 118 VAL A C   
1018 O O   . VAL A 117 ? 0.4332 0.4784 0.4978 -0.0548 0.1306  -0.1239 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.4142 0.4258 0.4678 -0.0231 0.1033  -0.0946 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.4148 0.4308 0.4826 -0.0208 0.1149  -0.1087 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.4180 0.4043 0.4484 -0.0240 0.0976  -0.0822 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.4041 0.4699 0.4934 -0.0319 0.1086  -0.1135 119 ASP A N   
1023 N N   B ASP A 118 ? 0.3975 0.4621 0.4837 -0.0340 0.1086  -0.1126 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.4083 0.5055 0.5255 -0.0328 0.1148  -0.1297 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.3988 0.4942 0.5111 -0.0361 0.1144  -0.1279 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.4647 0.5649 0.5715 -0.0552 0.1280  -0.1380 119 ASP A C   
1027 C C   B ASP A 118 ? 0.4316 0.5264 0.5303 -0.0590 0.1276  -0.1350 119 ASP A C   
1028 O O   A ASP A 118 ? 0.4709 0.5895 0.5944 -0.0622 0.1410  -0.1552 119 ASP A O   
1029 O O   B ASP A 118 ? 0.4258 0.5350 0.5371 -0.0673 0.1416  -0.1514 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.4210 0.5396 0.5587 -0.0186 0.1010  -0.1275 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.4119 0.5271 0.5421 -0.0234 0.1006  -0.1246 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.5706 0.6928 0.7252 0.0048  0.0901  -0.1251 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.5788 0.7310 0.7409 -0.0231 0.1044  -0.1420 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.6128 0.7372 0.7807 0.0119  0.0962  -0.1345 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.6020 0.7716 0.7887 -0.0157 0.1099  -0.1561 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.6348 0.7557 0.7876 0.0160  0.0759  -0.1142 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.6362 0.8012 0.8002 -0.0301 0.1017  -0.1428 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.4194 0.4998 0.4978 -0.0666 0.1252  -0.1265 120 THR A N   
1039 N N   B THR A 119 ? 0.3807 0.4572 0.4525 -0.0694 0.1239  -0.1234 120 THR A N   
1040 C CA  A THR A 119 ? 0.4295 0.5037 0.4899 -0.0881 0.1367  -0.1313 120 THR A CA  
1041 C CA  B THR A 119 ? 0.3915 0.4608 0.4449 -0.0912 0.1362  -0.1288 120 THR A CA  
1042 C C   A THR A 119 ? 0.4784 0.5322 0.5157 -0.1021 0.1501  -0.1350 120 THR A C   
1043 C C   B THR A 119 ? 0.4554 0.5041 0.4859 -0.1045 0.1494  -0.1325 120 THR A C   
1044 O O   A THR A 119 ? 0.4845 0.5438 0.5202 -0.1184 0.1656  -0.1482 120 THR A O   
1045 O O   B THR A 119 ? 0.4525 0.5013 0.4748 -0.1223 0.1641  -0.1432 120 THR A O   
1046 C CB  A THR A 119 ? 0.5422 0.6006 0.5812 -0.0918 0.1272  -0.1174 120 THR A CB  
1047 C CB  B THR A 119 ? 0.4102 0.4630 0.4405 -0.0974 0.1286  -0.1162 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.5343 0.6155 0.5977 -0.0790 0.1165  -0.1169 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.4314 0.4820 0.4501 -0.1174 0.1416  -0.1247 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.5512 0.5993 0.5695 -0.1131 0.1382  -0.1214 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.3457 0.3655 0.3437 -0.0971 0.1212  -0.1002 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.4258 0.4563 0.4442 -0.0972 0.1447  -0.1244 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.4470 0.4574 0.4419 -0.1092 0.1557  -0.1277 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.5128 0.5433 0.5316 -0.1111 0.1707  -0.1469 121 CYS A C   
1055 O O   . CYS A 120 ? 0.5276 0.5528 0.5323 -0.1292 0.1866  -0.1571 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.4466 0.4369 0.4271 -0.1003 0.1461  -0.1159 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.4960 0.4606 0.4437 -0.1022 0.1314  -0.0965 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.4632 0.5169 0.5180 -0.0924 0.1658  -0.1524 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.4763 0.5540 0.5618 -0.0891 0.1778  -0.1722 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.5345 0.6357 0.6328 -0.1045 0.1916  -0.1889 122 ARG A C   
1061 O O   . ARG A 121 ? 0.5341 0.6426 0.6373 -0.1163 0.2093  -0.2059 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.4959 0.5931 0.6162 -0.0635 0.1657  -0.1728 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.6789 0.7547 0.7919 -0.0500 0.1591  -0.1637 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.8625 0.9558 1.0101 -0.0301 0.1586  -0.1750 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.9762 1.0660 1.1313 -0.0083 0.1405  -0.1621 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.1053 1.1686 1.2458 0.0010  0.1341  -0.1505 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8701 0.9102 0.9897 -0.0090 0.1434  -0.1505 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.9484 1.0074 1.0932 0.0191  0.1189  -0.1392 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.4918 0.6044 0.5950 -0.1057 0.1845  -0.1851 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.4969 0.6321 0.6122 -0.1216 0.1970  -0.2009 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.5600 0.6691 0.6363 -0.1493 0.2133  -0.2021 123 LYS A C   
1072 O O   . LYS A 122 ? 0.5529 0.6761 0.6367 -0.1658 0.2321  -0.2209 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.5123 0.6630 0.6396 -0.1160 0.1842  -0.1954 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.7198 0.9029 0.8885 -0.0910 0.1703  -0.1993 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.8532 1.0558 1.0342 -0.0890 0.1601  -0.1978 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.9632 1.1815 1.1674 -0.0623 0.1398  -0.1911 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 1.0583 1.3089 1.3028 -0.0457 0.1393  -0.2075 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.5285 0.5993 0.5624 -0.1544 0.2059  -0.1825 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.5610 0.5997 0.5505 -0.1785 0.2181  -0.1802 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.6356 0.6657 0.6140 -0.1884 0.2337  -0.1907 124 PHE A C   
1081 O O   . PHE A 123 ? 0.6449 0.6661 0.6032 -0.2114 0.2522  -0.2012 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.5895 0.5920 0.5404 -0.1767 0.2030  -0.1572 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.6158 0.6135 0.5584 -0.1804 0.1964  -0.1495 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.6373 0.6663 0.6159 -0.1695 0.1895  -0.1535 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.6784 0.6383 0.5758 -0.1932 0.1955  -0.1376 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.6470 0.6709 0.6175 -0.1738 0.1841  -0.1473 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.7042 0.6570 0.5937 -0.1958 0.1896  -0.1308 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.6495 0.6348 0.5760 -0.1869 0.1847  -0.1362 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.5768 0.6095 0.5684 -0.1721 0.2277  -0.1893 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.5990 0.6257 0.5840 -0.1795 0.2422  -0.2006 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.6649 0.7259 0.6852 -0.1860 0.2615  -0.2269 125 ILE A C   
1092 O O   . ILE A 124 ? 0.6810 0.7348 0.6846 -0.2064 0.2814  -0.2399 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.6262 0.6440 0.6147 -0.1610 0.2308  -0.1922 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.6325 0.6147 0.5794 -0.1621 0.2169  -0.1705 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.6599 0.6788 0.6524 -0.1660 0.2471  -0.2083 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.7067 0.6839 0.6612 -0.1422 0.2013  -0.1592 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.6185 0.7170 0.6866 -0.1691 0.2554  -0.2354 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.6250 0.7639 0.7354 -0.1712 0.2706  -0.2621 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.6954 0.8396 0.7943 -0.1998 0.2899  -0.2754 126 LYS A C   
1100 O O   . LYS A 125 ? 0.6939 0.8569 0.8078 -0.2133 0.3110  -0.2987 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.6375 0.8134 0.7971 -0.1452 0.2551  -0.2653 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.8506 1.0697 1.0605 -0.1381 0.2660  -0.2928 126 LYS A CG  
1103 C CD  . LYS A 125 ? 0.9855 1.2426 1.2402 -0.1156 0.2498  -0.2966 126 LYS A CD  
1104 C CE  . LYS A 125 ? 1.1349 1.4398 1.4417 -0.1100 0.2604  -0.3265 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.2390 1.5830 1.5871 -0.0902 0.2436  -0.3312 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.6557 0.7810 0.7265 -0.2100 0.2838  -0.2612 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.6846 0.8065 0.7370 -0.2385 0.3017  -0.2710 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.7890 0.8757 0.7942 -0.2646 0.3214  -0.2737 127 ALA A C   
1109 O O   . ALA A 126 ? 0.7998 0.8921 0.7996 -0.2895 0.3439  -0.2913 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.6855 0.7896 0.7162 -0.2403 0.2885  -0.2531 127 ALA A CB  
1111 N N   . SER A 127 ? 0.7886 0.8396 0.7588 -0.2599 0.3133  -0.2569 128 SER A N   
1112 C CA  . SER A 127 ? 0.8513 0.8657 0.7716 -0.2828 0.3287  -0.2571 128 SER A CA  
1113 C C   . SER A 127 ? 0.9407 0.9718 0.8781 -0.2887 0.3483  -0.2794 128 SER A C   
1114 O O   . SER A 127 ? 0.9880 0.9955 0.8876 -0.3132 0.3670  -0.2860 128 SER A O   
1115 C CB  . SER A 127 ? 0.9247 0.8959 0.8000 -0.2758 0.3105  -0.2310 128 SER A CB  
1116 O OG  . SER A 127 ? 1.0757 1.0179 0.9148 -0.2834 0.3021  -0.2142 128 SER A OG  
1117 N N   . GLU A 128 ? 0.8684 0.9379 0.8603 -0.2665 0.3443  -0.2913 129 GLU A N   
1118 C CA  . GLU A 128 ? 1.1688 1.2565 1.1829 -0.2685 0.3621  -0.3139 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.6933 1.8149 1.7342 -0.2878 0.3877  -0.3437 129 GLU A C   
1120 O O   . GLU A 128 ? 1.3003 1.4048 1.3068 -0.3171 0.4050  -0.3482 129 GLU A O   
1121 C CB  . GLU A 128 ? 1.1539 1.2634 1.2118 -0.2360 0.3472  -0.3142 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.2496 1.4085 1.3697 -0.2166 0.3415  -0.3279 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.4907 1.6640 1.6475 -0.1824 0.3229  -0.3236 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.4175 1.5604 1.5509 -0.1717 0.3104  -0.3051 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.3840 1.5989 1.5928 -0.1662 0.3206  -0.3392 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.2723 0.5102 0.3293 -0.0629 -0.0210 -0.0823 1   TRP D N   
1130 N N   B TRP B 2   ? 0.2726 0.5105 0.3296 -0.0629 -0.0210 -0.0824 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.2661 0.5042 0.3237 -0.0629 -0.0210 -0.0828 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.2657 0.5038 0.3234 -0.0630 -0.0210 -0.0828 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.3153 0.5535 0.3753 -0.0635 -0.0212 -0.0820 1   TRP D C   
1134 C C   B TRP B 2   ? 0.3082 0.5464 0.3682 -0.0635 -0.0211 -0.0820 1   TRP D C   
1135 O O   A TRP B 2   ? 0.3121 0.5497 0.3727 -0.0637 -0.0216 -0.0815 1   TRP D O   
1136 O O   B TRP B 2   ? 0.3013 0.5390 0.3620 -0.0638 -0.0215 -0.0815 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.2527 0.4904 0.3091 -0.0629 -0.0221 -0.0835 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.2501 0.4878 0.3066 -0.0629 -0.0222 -0.0835 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.2597 0.4972 0.3138 -0.0624 -0.0220 -0.0849 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.2609 0.4985 0.3187 -0.0633 -0.0233 -0.0834 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.2956 0.5325 0.3488 -0.0621 -0.0224 -0.0854 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.2998 0.5369 0.3580 -0.0633 -0.0241 -0.0840 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.2516 0.4897 0.3045 -0.0622 -0.0213 -0.0858 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.2584 0.4969 0.3177 -0.0638 -0.0238 -0.0829 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.2850 0.5221 0.3363 -0.0616 -0.0221 -0.0870 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.2933 0.5312 0.3536 -0.0638 -0.0247 -0.0842 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.2978 0.5356 0.3486 -0.0618 -0.0214 -0.0874 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.3093 0.5481 0.3698 -0.0641 -0.0246 -0.0835 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.2562 0.4949 0.3100 -0.0624 -0.0208 -0.0854 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.2707 0.5099 0.3310 -0.0640 -0.0237 -0.0820 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.2808 0.5190 0.3299 -0.0615 -0.0206 -0.0889 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.2973 0.5377 0.3595 -0.0645 -0.0250 -0.0835 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.2676 0.5067 0.3201 -0.0622 -0.0201 -0.0866 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.2916 0.5319 0.3533 -0.0644 -0.0244 -0.0815 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.2801 0.5188 0.3300 -0.0618 -0.0199 -0.0885 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.2982 0.5393 0.3606 -0.0646 -0.0250 -0.0824 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.2570 0.4960 0.3188 -0.0635 -0.0208 -0.0820 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.2519 0.4911 0.3164 -0.0639 -0.0210 -0.0815 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.2718 0.5113 0.3378 -0.0639 -0.0217 -0.0808 2   VAL D C   
1160 O O   . VAL B 3   ? 0.2540 0.4937 0.3193 -0.0637 -0.0216 -0.0808 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2845 0.5250 0.3515 -0.0644 -0.0199 -0.0821 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2835 0.5244 0.3489 -0.0649 -0.0193 -0.0821 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2761 0.5182 0.3450 -0.0643 -0.0188 -0.0830 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.2336 0.4732 0.3019 -0.0641 -0.0223 -0.0802 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.2467 0.4868 0.3174 -0.0642 -0.0231 -0.0791 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.2923 0.5328 0.3672 -0.0642 -0.0222 -0.0797 3   ILE D C   
1167 O O   . ILE B 4   ? 0.2709 0.5117 0.3479 -0.0646 -0.0218 -0.0807 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.2783 0.5189 0.3500 -0.0644 -0.0243 -0.0783 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.2783 0.5196 0.3470 -0.0645 -0.0249 -0.0785 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.2919 0.5333 0.3667 -0.0644 -0.0253 -0.0766 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.2944 0.5370 0.3606 -0.0648 -0.0256 -0.0781 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.2791 0.5201 0.3557 -0.0640 -0.0216 -0.0797 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.2835 0.5257 0.3654 -0.0642 -0.0205 -0.0810 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.3321 0.5744 0.4196 -0.0644 -0.0215 -0.0804 4   PRO D C   
1175 O O   . PRO B 5   ? 0.3120 0.5535 0.3995 -0.0643 -0.0230 -0.0782 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.3048 0.5474 0.3872 -0.0638 -0.0196 -0.0811 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.3510 0.5924 0.4299 -0.0637 -0.0210 -0.0789 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.2974 0.5382 0.3717 -0.0638 -0.0219 -0.0787 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.2984 0.5423 0.3913 -0.0648 -0.0206 -0.0824 5   ALA D N   
# 
