data_7GUJ
# 
_entry.id   7GUJ 
# 
_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   7GUJ         pdb_00007guj 10.2210/pdb7guj/pdb 
WWPDB D_1001406654 ?            ?                   
# 
_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                        7GUJ 
_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 81  HOH HOH A . 
F 6 HOH 2   302 42  HOH HOH A . 
F 6 HOH 3   303 166 HOH HOH A . 
F 6 HOH 4   304 15  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   307 189 HOH HOH A . 
F 6 HOH 8   308 159 HOH HOH A . 
F 6 HOH 9   309 114 HOH HOH A . 
F 6 HOH 10  310 23  HOH HOH A . 
F 6 HOH 11  311 149 HOH HOH A . 
F 6 HOH 12  312 130 HOH HOH A . 
F 6 HOH 13  313 92  HOH HOH A . 
F 6 HOH 14  314 32  HOH HOH A . 
F 6 HOH 15  315 87  HOH HOH A . 
F 6 HOH 16  316 85  HOH HOH A . 
F 6 HOH 17  317 83  HOH HOH A . 
F 6 HOH 18  318 63  HOH HOH A . 
F 6 HOH 19  319 187 HOH HOH A . 
F 6 HOH 20  320 230 HOH HOH A . 
F 6 HOH 21  321 14  HOH HOH A . 
F 6 HOH 22  322 33  HOH HOH A . 
F 6 HOH 23  323 196 HOH HOH A . 
F 6 HOH 24  324 5   HOH HOH A . 
F 6 HOH 25  325 3   HOH HOH A . 
F 6 HOH 26  326 24  HOH HOH A . 
F 6 HOH 27  327 143 HOH HOH A . 
F 6 HOH 28  328 97  HOH HOH A . 
F 6 HOH 29  329 103 HOH HOH A . 
F 6 HOH 30  330 11  HOH HOH A . 
F 6 HOH 31  331 165 HOH HOH A . 
F 6 HOH 32  332 135 HOH HOH A . 
F 6 HOH 33  333 113 HOH HOH A . 
F 6 HOH 34  334 50  HOH HOH A . 
F 6 HOH 35  335 134 HOH HOH A . 
F 6 HOH 36  336 213 HOH HOH A . 
F 6 HOH 37  337 109 HOH HOH A . 
F 6 HOH 38  338 141 HOH HOH A . 
F 6 HOH 39  339 100 HOH HOH A . 
F 6 HOH 40  340 13  HOH HOH A . 
F 6 HOH 41  341 35  HOH HOH A . 
F 6 HOH 42  342 110 HOH HOH A . 
F 6 HOH 43  343 112 HOH HOH A . 
F 6 HOH 44  344 49  HOH HOH A . 
F 6 HOH 45  345 184 HOH HOH A . 
F 6 HOH 46  346 105 HOH HOH A . 
F 6 HOH 47  347 117 HOH HOH A . 
F 6 HOH 48  348 90  HOH HOH A . 
F 6 HOH 49  349 86  HOH HOH A . 
F 6 HOH 50  350 51  HOH HOH A . 
F 6 HOH 51  351 94  HOH HOH A . 
F 6 HOH 52  352 115 HOH HOH A . 
F 6 HOH 53  353 180 HOH HOH A . 
F 6 HOH 54  354 18  HOH HOH A . 
F 6 HOH 55  355 20  HOH HOH A . 
F 6 HOH 56  356 44  HOH HOH A . 
F 6 HOH 57  357 136 HOH HOH A . 
F 6 HOH 58  358 116 HOH HOH A . 
F 6 HOH 59  359 74  HOH HOH A . 
F 6 HOH 60  360 22  HOH HOH A . 
F 6 HOH 61  361 102 HOH HOH A . 
F 6 HOH 62  362 95  HOH HOH A . 
F 6 HOH 63  363 123 HOH HOH A . 
F 6 HOH 64  364 26  HOH HOH A . 
F 6 HOH 65  365 6   HOH HOH A . 
F 6 HOH 66  366 150 HOH HOH A . 
F 6 HOH 67  367 151 HOH HOH A . 
F 6 HOH 68  368 231 HOH HOH A . 
F 6 HOH 69  369 121 HOH HOH A . 
F 6 HOH 70  370 25  HOH HOH A . 
F 6 HOH 71  371 62  HOH HOH A . 
F 6 HOH 72  372 101 HOH HOH A . 
F 6 HOH 73  373 147 HOH HOH A . 
F 6 HOH 74  374 89  HOH HOH A . 
F 6 HOH 75  375 119 HOH HOH A . 
F 6 HOH 76  376 66  HOH HOH A . 
F 6 HOH 77  377 28  HOH HOH A . 
F 6 HOH 78  378 10  HOH HOH A . 
F 6 HOH 79  379 164 HOH HOH A . 
F 6 HOH 80  380 192 HOH HOH A . 
F 6 HOH 81  381 29  HOH HOH A . 
F 6 HOH 82  382 107 HOH HOH A . 
F 6 HOH 83  383 57  HOH HOH A . 
F 6 HOH 84  384 246 HOH HOH A . 
F 6 HOH 85  385 178 HOH HOH A . 
F 6 HOH 86  386 168 HOH HOH A . 
F 6 HOH 87  387 244 HOH HOH A . 
F 6 HOH 88  388 104 HOH HOH A . 
F 6 HOH 89  389 99  HOH HOH A . 
F 6 HOH 90  390 40  HOH HOH A . 
F 6 HOH 91  391 238 HOH HOH A . 
F 6 HOH 92  392 60  HOH HOH A . 
F 6 HOH 93  393 21  HOH HOH A . 
F 6 HOH 94  394 56  HOH HOH A . 
F 6 HOH 95  395 39  HOH HOH A . 
F 6 HOH 96  396 38  HOH HOH A . 
F 6 HOH 97  397 82  HOH HOH A . 
F 6 HOH 98  398 96  HOH HOH A . 
F 6 HOH 99  399 36  HOH HOH A . 
F 6 HOH 100 400 242 HOH HOH A . 
F 6 HOH 101 401 30  HOH HOH A . 
F 6 HOH 102 402 193 HOH HOH A . 
F 6 HOH 103 403 52  HOH HOH A . 
F 6 HOH 104 404 45  HOH HOH A . 
F 6 HOH 105 405 75  HOH HOH A . 
F 6 HOH 106 406 27  HOH HOH A . 
F 6 HOH 107 407 17  HOH HOH A . 
F 6 HOH 108 408 37  HOH HOH A . 
F 6 HOH 109 409 93  HOH HOH A . 
F 6 HOH 110 410 69  HOH HOH A . 
F 6 HOH 111 411 239 HOH HOH A . 
F 6 HOH 112 412 167 HOH HOH A . 
F 6 HOH 113 413 53  HOH HOH A . 
F 6 HOH 114 414 203 HOH HOH A . 
F 6 HOH 115 415 171 HOH HOH A . 
F 6 HOH 116 416 237 HOH HOH A . 
F 6 HOH 117 417 209 HOH HOH A . 
F 6 HOH 118 418 176 HOH HOH A . 
F 6 HOH 119 419 55  HOH HOH A . 
F 6 HOH 120 420 54  HOH HOH A . 
F 6 HOH 121 421 241 HOH HOH A . 
F 6 HOH 122 422 79  HOH HOH A . 
F 6 HOH 123 423 186 HOH HOH A . 
F 6 HOH 124 424 200 HOH HOH A . 
F 6 HOH 125 425 146 HOH HOH A . 
F 6 HOH 126 426 153 HOH HOH A . 
F 6 HOH 127 427 31  HOH HOH A . 
F 6 HOH 128 428 145 HOH HOH A . 
F 6 HOH 129 429 148 HOH HOH A . 
F 6 HOH 130 430 43  HOH HOH A . 
F 6 HOH 131 431 98  HOH HOH A . 
F 6 HOH 132 432 106 HOH HOH A . 
F 6 HOH 133 433 185 HOH HOH A . 
F 6 HOH 134 434 188 HOH HOH A . 
F 6 HOH 135 435 191 HOH HOH A . 
F 6 HOH 136 436 139 HOH HOH A . 
F 6 HOH 137 437 232 HOH HOH A . 
F 6 HOH 138 438 76  HOH HOH A . 
F 6 HOH 139 439 80  HOH HOH A . 
F 6 HOH 140 440 158 HOH HOH A . 
F 6 HOH 141 441 137 HOH HOH A . 
F 6 HOH 142 442 204 HOH HOH A . 
F 6 HOH 143 443 111 HOH HOH A . 
F 6 HOH 144 444 221 HOH HOH A . 
F 6 HOH 145 445 140 HOH HOH A . 
F 6 HOH 146 446 169 HOH HOH A . 
F 6 HOH 147 447 206 HOH HOH A . 
F 6 HOH 148 448 108 HOH HOH A . 
F 6 HOH 149 449 70  HOH HOH A . 
F 6 HOH 150 450 247 HOH HOH A . 
F 6 HOH 151 451 161 HOH HOH A . 
F 6 HOH 152 452 243 HOH HOH A . 
F 6 HOH 153 453 228 HOH HOH A . 
F 6 HOH 154 454 131 HOH HOH A . 
F 6 HOH 155 455 212 HOH HOH A . 
F 6 HOH 156 456 215 HOH HOH A . 
F 6 HOH 157 457 183 HOH HOH A . 
F 6 HOH 158 458 142 HOH HOH A . 
F 6 HOH 159 459 59  HOH HOH A . 
F 6 HOH 160 460 73  HOH HOH A . 
F 6 HOH 161 461 245 HOH HOH A . 
F 6 HOH 162 462 170 HOH HOH A . 
F 6 HOH 163 463 179 HOH HOH A . 
F 6 HOH 164 464 175 HOH HOH A . 
F 6 HOH 165 465 65  HOH HOH A . 
F 6 HOH 166 466 181 HOH HOH A . 
F 6 HOH 167 467 195 HOH HOH A . 
F 6 HOH 168 468 152 HOH HOH A . 
F 6 HOH 169 469 208 HOH HOH A . 
F 6 HOH 170 470 61  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 47  HOH HOH D . 
G 6 HOH 4   204 68  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           7GUJ 
_cell.length_a           67.590 
_cell.length_b           67.590 
_cell.length_c           166.260 
_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                         7GUJ 
_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          7GUJ 
_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   66.01 
_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                     7GUJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.890 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   21723 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.089 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.800 
_reflns.B_iso_Wilson_estimate        30.370 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.094 
_reflns.pdbx_Rpim_I_all              0.031 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     196620 
_reflns.pdbx_scaling_rejects         699 
_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  ? 11588 1243 ? 1.200 ? ? ? 9.300 ? 1.900  ? ? ? ? ? ? 100.000 1.269 0.409 0.833 ? 
1 2 9.000 33.890 ? 1525  226  ? 0.058 ? ? ? 6.700 ? 25.900 ? ? ? ? ? ? 98.700  0.063 0.023 0.996 ? 
# 
_refine.entry_id                                 7GUJ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8000 
_refine.ls_d_res_low                             33.8900 
_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                          0.1820 
_refine.ls_R_factor_R_work                       0.1810 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2060 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.2000 
_refine.ls_number_reflns_R_free                  1126 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               35.8400 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.2734 
_refine.aniso_B[2][2]                            -0.2734 
_refine.aniso_B[3][3]                            0.5467 
_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               0.9600 
_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   0.0930 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1090 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1020 
_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                                130.840 
_refine.B_iso_min                                17.360 
_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                        7GUJ 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.230 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.8000 
_refine_hist.d_res_low                        33.8900 
_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           30.52 
_refine_hist.pdbx_B_iso_mean_solvent          53.36 
_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      1629 ?      ? 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           ?    3.400  ? ?      ?            
'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               99.7500 
_refine_ls_shell.number_reflns_R_work             2680 
_refine_ls_shell.R_factor_all                     0.2740 
_refine_ls_shell.R_factor_R_work                  0.2732 
_refine_ls_shell.R_factor_R_free                  0.2896 
_refine_ls_shell.percent_reflns_R_free            4.6300 
_refine_ls_shell.number_reflns_R_free             130 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2810 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUJ 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 10.57 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUJ 
_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 7GUJ       7GUJ   ? 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 7GUJ A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUJ D 1 ? 6   ? 7GUJ   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 7GUJ GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUJ PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUJ 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)' 6360  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  13280 ? 
# 
_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 33.7950000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5346570418 0.0000000000 0.0000000000 -1.0000000000 27.7100000000 
# 
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 ? ? ? ? ? ? ? 1.329 ? ? 
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                   7GUJ 
_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 37.62 48.60   
2 1 SER A 39  ? B 61.71 -109.23 
3 1 SER A 93  ? ? 76.80 -0.77   
4 1 SER A 93  ? ? 76.80 -2.74   
5 1 GLN A 113 ? ? 63.11 61.34   
# 
_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   11.09 
# 
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 379 ? F HOH . 
3 1 A HOH 446 ? F HOH . 
4 1 A HOH 463 ? F HOH . 
5 1 A HOH 464 ? F HOH . 
6 1 A HOH 467 ? 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 0.0058  -0.0539 -0.0665 -0.0400 0.0260  -0.0170 1.0289 1.8565 2.2017 
0.4132 -0.2780 1.2453 0.1352 -0.0906 -0.0446 -0.0583 0.0960 0.0820 0.2596  0.0148 -0.0557 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.1055 0.1229  -0.0431 -0.0564 -0.0167 -0.0825 0.5968 0.0710 0.0000 
0.2338 0.0471  0.3260 0.0105 0.0111  -0.0216 -0.0003 0.0231 0.0421 -0.0074 0.0116 0.0136  
# 
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                    7GUJ 
_atom_sites.fract_transf_matrix[1][1]   0.014795 
_atom_sites.fract_transf_matrix[1][2]   0.008542 
_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]   0.017084 
_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]   0.006015 
_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   ? 17.544 -21.144 -4.904 1.00 67.25  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.399 -22.058 -5.664 1.00 66.22  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.891 -23.518 -5.581 1.00 66.18  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.788 -23.764 -5.078 1.00 66.88  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.864 -21.949 -5.170 1.00 66.92  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.906 -22.033 -6.276 1.00 80.74  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 20.991 -23.097 -6.940 1.00 81.39  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.647 -21.042 -6.470 1.00 87.84  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.689 -24.473 -6.097 1.00 57.61  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.392 -25.904 -6.074 1.00 55.05  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.390 -26.661 -5.140 1.00 50.86  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.684 -27.838 -5.366 1.00 50.41  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.424 -26.465 -7.491 1.00 60.61  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.697 -26.291 -8.094 1.00 72.73  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.884 -25.984 -4.082 1.00 41.19  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.836 -26.569 -3.125 1.00 37.54  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.210 -27.723 -2.322 1.00 37.50  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.998 -27.752 -2.130 1.00 37.94  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.348 -25.489 -2.169 1.00 38.14  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.451 -24.252 -2.917 1.00 42.97  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.038 -28.637 -1.813 1.00 28.72  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.646 -29.627 -0.806 1.00 25.77  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.260 -29.095 0.494  1.00 27.81  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.214 -28.314 0.441  1.00 26.32  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 21.017 -31.104 -1.119 1.00 28.46  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.542 -31.277 -1.359 1.00 28.25  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.184 -31.628 -2.300 1.00 29.83  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.050 -32.727 -1.566 1.00 30.92  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.770 -29.528 1.655  0.57 23.25  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.669 -29.446 1.636  0.43 22.99  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.310 -29.017 2.918  0.57 22.10  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.107 -28.970 2.944  0.43 21.57  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.635 -30.142 3.895  0.57 25.34  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.574 -30.126 3.815  0.43 23.70  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.820 -31.049 4.066  0.57 25.00  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.958 -31.191 3.805  0.43 23.09  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.303 -28.015 3.536  0.57 23.48  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.950 -28.203 3.632  0.43 22.79  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.744 -27.380 4.862  0.57 23.32  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.167 -27.903 5.136  0.43 30.32  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.588 -26.692 5.546  0.57 50.76  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.089 -26.445 5.519  0.43 39.86  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.626 -27.323 5.993  0.57 42.33  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.755 -25.563 4.710  0.43 29.47  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.660 -25.377 5.645  0.57 54.19  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.395 -26.163 6.784  0.43 27.26  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.812 -30.076 4.546  0.78 22.71  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.638 -29.899 4.590  0.22 20.13  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.200 -31.073 5.546  0.78 22.28  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.155 -30.869 5.543  0.22 19.75  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.713 -30.567 6.910  0.78 23.87  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.625 -30.425 6.890  0.22 23.33  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.282 -29.619 7.465  0.78 22.82  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 23.040 -29.377 7.400  0.22 22.37  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.725 -31.358 5.518  0.78 23.46  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.690 -30.918 5.482  0.22 20.77  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.105 -32.557 6.358  0.78 24.70  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.175 -31.826 4.379  0.22 22.65  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.709 -33.843 5.990  0.78 28.73  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 25.032 -31.465 3.042  0.22 26.13  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.843 -32.402 7.527  0.78 26.61  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.731 -33.063 4.671  0.22 25.58  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 25.041 -34.951 6.786  0.78 29.92  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.466 -32.312 2.022  0.22 27.53  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.165 -33.504 8.324  0.78 28.74  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.157 -33.912 3.647  0.22 29.02  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.762 -34.767 7.952  0.78 27.11  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 26.034 -33.524 2.334  0.22 27.10  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.626 -31.165 7.414  1.00 20.88  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.943 -30.784 8.673  1.00 21.40  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.892 -30.537 9.881  1.00 24.78  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.749 -29.520 10.573 1.00 23.01  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.865 -31.826 9.016  1.00 29.59  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.931 -31.895 7.924  1.00 28.40  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.104 -31.487 10.311 1.00 34.17  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.843 -31.455 10.109 0.50 22.30  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.835 -31.460 10.117 0.50 22.57  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.759 -31.386 11.256 0.50 22.41  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.757 -31.391 11.260 0.50 22.79  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 25.008 -30.506 11.057 0.50 24.10  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 24.999 -30.498 11.063 0.50 24.24  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.816 -30.405 11.986 0.50 22.58  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.797 -30.382 12.000 0.50 22.71  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.180 -32.810 11.684 0.50 25.80  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.190 -32.813 11.656 0.50 26.90  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.042 -33.695 12.219 0.50 32.57  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.221 -33.516 12.610 0.50 37.38  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.488 -33.225 13.557 0.50 43.88  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 22.928 -34.961 12.240 0.50 45.38  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.441 -33.402 14.657 0.50 51.15  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.130 -35.749 11.951 0.50 48.38  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.398 -32.733 15.805 0.50 59.67  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.300 -36.475 10.849 0.50 57.61  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.465 -31.811 16.013 0.50 39.97  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.419 -37.164 10.667 0.50 49.99  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.297 -32.970 16.750 0.50 49.18  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.346 -36.529 9.927  0.50 34.14  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.176 -29.888 9.870  1.00 20.34  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.380 -29.081 9.560  1.00 20.00  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.666 -27.975 10.575 1.00 22.48  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.802 -27.896 11.062 1.00 20.76  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.351 -28.507 8.130  1.00 20.00  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.618 -27.766 7.806  1.00 21.70  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.806 -28.434 7.635  1.00 22.10  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.840 -26.437 7.683  1.00 22.47  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.716 -27.507 7.378  1.00 21.64  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.180 -26.287 7.391  1.00 21.46  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.671 -27.104 10.858 1.00 19.69  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.882 -25.974 11.786 1.00 19.27  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.298 -26.455 13.186 1.00 21.49  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.207 -25.876 13.778 1.00 19.66  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.642 -25.082 11.850 1.00 20.65  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.640 -27.505 13.696 0.38 19.14  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.644 -27.513 13.694 0.33 19.42  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.640 -27.509 13.706 0.29 19.05  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.937 -28.088 15.003 0.38 19.21  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.935 -28.105 15.002 0.33 19.65  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.952 -28.073 15.023 0.29 19.11  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.355 -28.674 15.031 0.38 23.28  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.349 -28.689 15.037 0.33 23.71  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.351 -28.703 15.051 0.29 23.66  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.078 -28.454 16.007 0.38 20.82  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.063 -28.488 16.023 0.33 21.68  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.059 -28.543 16.048 0.29 21.97  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.898 -29.150 15.360 0.38 22.86  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.906 -29.180 15.343 0.33 23.72  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.881 -29.072 15.460 0.29 22.53  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.174 -29.730 16.624 0.38 26.40  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.598 -28.637 15.386 0.33 29.36  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.821 -30.191 14.593 0.29 25.79  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.756 -29.384 13.952 1.00 21.78  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.096 -29.999 13.825 1.00 22.74  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.159 -28.901 13.785 1.00 22.56  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.214 -29.048 14.408 1.00 22.56  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.188 -30.865 12.560 1.00 24.59  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.418 -32.183 12.641 1.00 33.87  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.852 -32.485 13.724 1.00 33.94  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.368 -32.902 11.623 1.00 33.76  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.880 -27.788 13.059 1.00 18.81  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.818 -26.655 13.035 1.00 18.18  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 31.003 -26.092 14.458 1.00 20.43  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.126 -25.904 14.906 1.00 19.37  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.342 -25.542 12.062 1.00 20.26  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.092 -24.227 12.294 1.00 20.07  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.437 -26.001 10.605 1.00 19.85  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.898 -25.845 15.171 1.00 18.33  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 29.995 -25.262 16.511 1.00 19.07  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.748 -26.191 17.476 1.00 22.33  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.599 -25.714 18.248 1.00 19.78  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.606 -24.900 17.055 1.00 20.21  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.629 -23.937 18.281 1.00 23.24  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.184 -22.543 17.909 1.00 23.53  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.233 -23.796 18.859 1.00 27.55  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.475 -27.511 17.381 1.00 20.82  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.151 -28.547 18.183 1.00 22.28  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.667 -28.489 17.938 1.00 22.49  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.452 -28.480 18.901 1.00 21.36  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.598 -29.936 17.835 1.00 24.39  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.203 -31.098 18.608 1.00 32.87  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.748 -31.065 20.075 1.00 35.13  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.790 -32.416 17.981 1.00 38.06  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.077 -28.388 16.658 1.00 19.31  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.493 -28.276 16.307 1.00 19.36  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.125 -26.965 16.795 1.00 21.41  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.278 -26.970 17.230 1.00 21.09  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.694 -28.499 14.817 1.00 20.88  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.636 -29.971 14.479 1.00 32.21  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.807 -30.831 15.351 1.00 27.36  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.354 -30.300 13.224 1.00 23.56  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.377 -25.840 16.714 1.00 18.87  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.853 -24.551 17.245 1.00 18.84  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.069 -24.687 18.756 1.00 21.10  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.060 -24.180 19.290 1.00 18.80  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.863 -23.397 16.929 1.00 18.48  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.770 -23.027 15.430 1.00 21.24  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.694 -21.953 15.210 1.00 20.98  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.125 -22.562 14.861 1.00 24.20  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.139 -25.372 19.457 1.00 18.49  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.323 -25.572 20.905 1.00 19.39  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.559 -26.472 21.212 1.00 23.56  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.264 -26.232 22.196 1.00 24.54  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.061 -26.138 21.539 1.00 21.42  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.089 -26.010 23.047 1.00 27.86  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.585 -25.028 23.600 1.00 24.72  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.561 -26.999 23.719 1.00 28.12  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.834 -27.487 20.361 1.00 21.11  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 37.023 -28.350 20.527 1.00 22.39  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.296 -27.514 20.353 1.00 26.50  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.239 -27.692 21.109 1.00 26.42  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 37.023 -29.489 19.506 1.00 21.21  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 35.999 -30.567 19.825 1.00 28.11  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.788 -31.468 18.620 1.00 32.74  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.929 -32.598 18.954 1.00 40.17  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.444 -33.471 18.076 1.00 59.17  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.678 -33.318 16.775 1.00 43.55  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.707 -34.493 18.489 1.00 47.83  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.300 -26.559 19.396 1.00 23.02  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.448 -25.669 19.231 1.00 21.87  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.607 -24.792 20.477 1.00 25.27  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.734 -24.633 20.972 1.00 25.96  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.278 -24.782 18.011 1.00 20.89  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.242 -25.488 16.633 1.00 24.33  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.074 -24.435 15.522 1.00 24.54  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.519 -26.333 16.399 1.00 26.82  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.485 -24.255 21.007 1.00 21.43  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.550 -23.460 22.246 1.00 22.30  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.167 -24.286 23.414 1.00 27.97  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.054 -23.773 24.122 1.00 28.04  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.153 -22.959 22.658 1.00 22.29  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.255 -22.047 23.896 1.00 28.12  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.937 -21.436 24.273 1.00 29.23  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.928 -22.425 24.649 1.00 28.05  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.313 -22.462 25.827 1.00 40.58  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.672 -21.629 26.801 1.00 35.84  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.360 -23.354 26.053 1.00 30.04  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.677 -25.519 23.619 0.40 26.24  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.683 -25.526 23.624 0.35 25.99  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.684 -25.531 23.618 0.25 25.80  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.154 -26.420 24.675 0.40 27.92  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.150 -26.416 24.701 0.35 27.53  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.136 -26.447 24.679 0.25 27.27  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.667 -26.599 24.601 0.40 32.83  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.646 -26.741 24.607 0.35 32.97  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.635 -26.762 24.600 0.25 32.73  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.350 -26.514 25.624 0.40 33.58  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.293 -26.936 25.638 0.35 33.99  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.269 -26.982 25.634 0.25 33.64  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.493 -27.789 24.543 0.40 32.04  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.321 -27.696 24.747 0.35 31.01  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.326 -27.740 24.650 0.25 30.78  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.122 -27.767 24.901 0.40 39.93  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.580 -28.548 23.643 0.35 37.05  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.759 -28.661 25.640 0.25 38.89  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.186 -26.803 23.377 1.00 29.06  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.612 -27.077 23.126 1.00 30.70  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.438 -25.795 22.941 1.00 33.52  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.649 -25.866 22.699 1.00 34.38  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.745 -28.042 21.946 1.00 33.79  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 41.976 -29.344 22.171 1.00 43.00  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 41.981 -30.220 20.945 1.00 49.59  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.311 -30.786 20.718 1.00 68.12  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.861 -30.934 19.521 1.00 85.82  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.076 -31.451 19.403 1.00 77.15  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.204 -30.565 18.434 1.00 71.93  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.783 -24.626 23.092 1.00 27.73  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.373 -23.288 22.955 1.00 28.44  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 43.981 -23.085 21.544 1.00 32.77  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.044 -22.479 21.389 1.00 33.83  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.411 -23.008 24.081 1.00 31.53  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.719 -21.537 24.258 1.00 39.72  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.799 -20.708 24.054 1.00 37.97  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.878 -21.212 24.594 1.00 45.13  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.313 -23.620 20.523 1.00 26.84  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.813 -23.520 19.153 1.00 25.99  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.209 -22.328 18.443 1.00 28.97  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 41.971 -22.202 18.364 1.00 25.89  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.603 -24.837 18.354 1.00 28.52  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.383 -26.018 18.989 1.00 30.43  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.970 -24.653 16.859 1.00 27.24  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.895 -27.404 18.467 1.00 33.09  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.087 -21.446 17.924 0.54 26.64  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.092 -21.448 17.926 0.46 27.56  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.735 -20.244 17.160 0.54 25.75  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.770 -20.234 17.171 0.46 27.21  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.849 -19.241 17.919 0.54 27.98  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.858 -19.243 17.917 0.46 28.77  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.225 -18.384 17.289 0.54 26.23  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.230 -18.393 17.281 0.46 27.14  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.118 -20.593 15.794 0.54 25.60  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.216 -20.557 15.783 0.46 27.52  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 44.024 -21.276 14.738 0.54 30.68  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.257 -20.457 14.673 0.46 33.79  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.525 -20.976 13.373 0.54 29.19  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.532 -21.812 14.053 0.46 34.62  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.476 -20.807 14.813 0.54 33.44  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.833 -19.461 13.629 0.46 35.68  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.849 -19.300 19.264 1.00 25.08  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.131 -18.316 20.093 1.00 24.99  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.953 -17.021 19.897 1.00 30.30  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.184 -17.077 19.756 1.00 31.05  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.069 -18.739 21.568 1.00 31.02  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.380 -19.095 21.976 1.00 32.74  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.089 -19.909 21.802 1.00 28.84  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.275 -15.891 19.748 1.00 26.46  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.931 -14.637 19.395 1.00 26.62  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.603 -13.486 20.315 1.00 28.52  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.948 -12.341 20.019 1.00 29.14  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.601 -14.289 17.930 1.00 27.77  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.114 -14.302 17.604 1.00 35.89  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.293 -14.352 18.551 1.00 31.48  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.773 -14.284 16.410 1.00 44.66  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.939 -13.775 21.437 1.00 23.78  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.628 -12.728 22.414 1.00 23.09  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.450 -13.325 23.799 1.00 26.59  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.052 -14.493 23.936 1.00 26.48  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.367 -11.882 21.978 1.00 26.05  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 39.052 -12.663 22.137 1.00 24.35  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.297 -10.528 22.719 1.00 26.16  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.737 -12.510 24.821 0.53 23.75  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.751 -12.525 24.826 0.47 23.93  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.511 -12.821 26.225 0.53 23.21  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.478 -12.884 26.206 0.47 23.51  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.453 -11.829 26.705 0.53 26.67  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.498 -11.851 26.775 0.47 27.01  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.603 -10.618 26.501 0.53 26.68  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.715 -10.642 26.649 0.47 27.22  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.810 -12.721 27.074 0.53 27.81  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.722 -13.173 27.095 0.47 28.25  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.532 -12.962 28.559 0.53 28.11  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.551 -11.922 27.366 0.47 29.13  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.870 -13.682 26.572 0.53 28.09  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.313 -13.847 28.402 0.47 28.24  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.387 -12.340 27.327 1.00 22.62  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.338 -11.521 27.929 1.00 22.03  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.631 -11.555 29.432 1.00 27.44  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.651 -12.637 30.040 1.00 26.77  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.900 -12.012 27.596 1.00 23.80  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.663 -12.158 26.061 1.00 23.01  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.851 -11.125 28.236 1.00 25.13  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 37.000 -10.892 25.171 1.00 23.43  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.863 -10.374 30.013 1.00 24.32  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.188 -10.228 31.437 1.00 24.92  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.923 -9.796  32.182 1.00 29.50  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.317 -8.770  31.840 1.00 27.91  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.382 -9.253  31.666 1.00 29.62  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.685 -9.081  33.155 1.00 30.53  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.634 -9.733  30.937 1.00 30.32  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.531 -10.582 33.207 1.00 26.45  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.326 -10.358 34.011 1.00 26.58  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.790 -10.404 35.455 1.00 31.49  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 37.038 -11.487 35.980 1.00 29.37  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.201 -11.381 33.680 1.00 30.59  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.878 -10.964 34.317 1.00 30.71  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 35.036 -11.551 32.161 1.00 29.51  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.674 -9.287  36.209 0.50 31.00  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.308 -9.207  35.838 0.50 28.08  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 37.035 -9.268  37.644 0.50 33.13  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.987 -8.837  37.068 0.50 28.84  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.298 -10.139 37.954 0.50 38.13  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.275 -9.660  37.222 0.50 32.04  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.258 -10.995 38.843 0.50 38.07  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.188 -9.446  36.427 0.50 30.53  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.848 -9.698  38.514 0.50 38.80  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 37.045 -8.875  38.265 0.50 33.25  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.783 -8.759  38.519 0.50 49.98  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.087 -7.840  38.106 0.50 39.59  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.383 -9.953  37.155 0.50 34.75  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.355 -10.620 38.165 0.50 29.69  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.672 -10.674 37.235 0.50 35.64  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.587 -11.405 38.287 0.50 30.55  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.558 -12.210 36.983 0.50 38.53  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.712 -12.442 37.122 0.50 35.75  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.342 -13.013 37.527 0.50 39.68  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.742 -12.478 36.429 0.50 35.95  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.433 -10.380 38.543 0.50 37.76  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.736 -12.022 39.705 0.50 31.34  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 41.982 -8.963  38.660 0.50 48.29  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 41.059 -10.972 40.788 0.50 39.06  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.075 -8.913  39.710 0.50 54.34  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.371 -11.566 42.159 0.50 38.05  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.435 -7.545  40.086 0.50 61.10  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.549 -10.539 43.190 0.50 40.27  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.850 -6.853  41.060 0.50 73.13  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.721 -10.028 43.564 0.50 54.90  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.848 -7.383  41.752 0.50 59.09  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.845 -10.428 42.983 0.50 42.96  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.251 -5.620  41.339 0.50 58.72  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.777 -9.108  44.516 0.50 46.36  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.584 -12.604 36.159 0.50 31.20  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.619 -13.170 36.834 0.50 30.36  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.391 -13.978 35.689 0.50 30.46  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.555 -14.245 35.831 0.50 29.35  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.533 -13.855 34.179 0.50 31.19  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.788 -13.802 34.372 0.50 30.61  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.973 -12.928 33.586 0.50 28.09  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.462 -12.682 33.988 0.50 27.58  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 38.030 -14.559 36.108 0.50 31.81  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.231 -15.027 35.947 0.50 30.57  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.923 -14.790 37.610 0.50 45.54  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.756 -15.207 37.385 0.50 45.57  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.861 -16.239 38.053 0.50 80.15  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.908 -16.571 38.032 0.50 81.94  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.821 -16.636 38.628 0.50 82.66  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.958 -17.225 37.832 0.50 83.90  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.852 -16.974 37.839 0.50 80.50  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 36.978 -16.974 38.769 0.50 82.76  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.345 -14.725 33.564 1.00 27.74  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.658 -14.577 32.151 1.00 27.25  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 40.040 -15.691 31.348 1.00 30.20  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.095 -16.845 31.770 1.00 30.64  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.185 -14.572 31.964 1.00 29.71  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.861 -13.359 32.596 1.00 43.95  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.320 -13.206 32.248 1.00 65.04  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.897 -13.947 31.437 1.00 57.51  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 44.951 -12.220 32.861 1.00 69.24  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.441 -15.350 30.197 1.00 24.47  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.806 -16.344 29.322 1.00 24.06  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.320 -16.177 27.912 1.00 28.31  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.145 -15.107 27.330 1.00 28.17  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.270 -16.172 29.330 1.00 25.20  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.647 -16.271 30.700 1.00 27.09  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.536 -15.146 31.517 1.00 28.81  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.144 -17.481 31.166 1.00 29.20  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 35.970 -15.238 32.792 1.00 31.19  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.572 -17.571 32.439 1.00 31.92  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.489 -16.448 33.244 1.00 29.86  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.922 -17.235 27.345 1.00 24.40  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.433 -17.191 25.971 1.00 23.45  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.306 -17.594 25.020 1.00 26.78  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.508 -18.487 25.334 1.00 25.57  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.661 -18.113 25.791 1.00 25.17  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.889 -17.711 26.652 1.00 34.05  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.221 -18.100 26.000 1.00 43.76  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.246 -17.691 24.587 1.00 54.76  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.839 -16.601 24.111 1.00 67.57  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.567 -15.831 24.907 1.00 59.89  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.755 -16.303 22.822 1.00 49.97  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.203 -16.918 23.872 1.00 23.10  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.128 -17.229 22.911 1.00 23.10  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.539 -16.819 21.502 1.00 24.05  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.632 -16.270 21.294 1.00 23.16  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.837 -16.495 23.309 1.00 24.32  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.649 -17.075 20.541 1.00 20.32  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.808 -16.656 19.155 1.00 19.79  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.914 -15.414 18.963 1.00 23.90  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.696 -15.458 19.236 1.00 22.89  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.368 -17.785 18.197 1.00 19.33  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.113 -19.079 18.414 1.00 22.93  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.580 -20.106 19.185 1.00 24.68  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.350 -19.446 17.994 1.00 23.93  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.501 -21.067 19.201 1.00 23.93  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.579 -20.721 18.484 1.00 24.09  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.516 -14.312 18.516 1.00 22.02  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.785 -13.068 18.243 1.00 21.43  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.553 -13.313 17.369 1.00 23.92  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.490 -12.805 17.705 1.00 21.89  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.692 -12.053 17.531 1.00 23.67  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.709 -11.433 18.470 1.00 23.03  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.646 -10.510 17.678 1.00 23.56  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.784 -10.094 18.561 1.00 27.78  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.721 -9.202  17.835 1.00 29.59  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.675 -14.139 16.303 1.00 20.59  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.529 -14.335 15.402 1.00 20.16  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.349 -15.008 16.068 1.00 21.39  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.209 -14.631 15.786 1.00 19.80  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.927 -15.042 14.117 1.00 27.31  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.526 -16.273 14.464 1.00 27.69  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.838 -14.173 13.240 1.00 29.19  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.608 -15.970 16.957 1.00 18.49  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.515 -16.663 17.667 1.00 18.95  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.839 -15.663 18.631 1.00 21.48  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.596 -15.618 18.728 1.00 19.40  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 33.022 -17.931 18.415 1.00 21.83  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.908 -18.538 19.287 1.00 21.73  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.521 -18.977 17.411 1.00 21.68  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.660 -14.874 19.362 1.00 18.24  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.101 -13.864 20.290 1.00 18.72  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.209 -12.866 19.515 1.00 21.55  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.105 -12.550 19.956 1.00 20.08  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.239 -13.082 20.984 1.00 19.06  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.185 -13.870 21.918 1.00 21.91  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.225 -12.906 22.540 1.00 22.29  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.405 -14.572 23.030 1.00 23.63  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.670 -12.409 18.345 1.00 18.83  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.889 -11.480 17.509 1.00 19.37  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.597 -12.125 17.019 1.00 22.43  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.557 -11.467 17.034 1.00 22.75  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.688 -10.990 16.300 1.00 20.94  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.915 -10.179 16.686 1.00 23.49  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.940 -10.098 15.221 1.00 27.94  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.149 -8.769  14.388 1.00 24.93  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.650 -13.416 16.635 1.00 20.28  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.480 -14.141 16.109 1.00 20.55  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.367 -14.320 17.174 1.00 22.87  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.201 -14.500 16.822 1.00 24.39  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.914 -15.507 15.561 1.00 21.04  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.743 -14.267 18.463 1.00 19.54  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.854 -14.501 19.598 1.00 19.70  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.412 -13.273 20.370 1.00 23.54  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.445 -13.370 21.142 1.00 23.33  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.531 -15.483 20.550 1.00 19.89  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.830 -17.116 19.836 1.00 23.22  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.174 -12.180 20.284 1.00 20.63  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.959 -11.036 21.168 1.00 18.85  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 26.997 -9.710  20.431 1.00 24.34  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.975 -9.430  19.727 1.00 22.07  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.050 -11.094 22.238 1.00 20.52  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.440 -9.841  22.784 1.00 23.94  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.959 -8.890  20.624 1.00 23.05  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.896 -7.553  20.038 1.00 23.35  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 27.020 -6.667  20.540 1.00 26.24  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.548 -5.840  19.786 1.00 26.15  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.423 -6.859  21.821 1.00 23.88  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.526 -6.084  22.399 1.00 23.77  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.848 -6.427  21.704 1.00 25.29  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.528 -5.508  21.239 1.00 24.40  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.647 -6.290  23.926 1.00 23.79  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.675 -5.371  24.612 1.00 28.28  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.200 -3.898  24.628 1.00 29.68  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 29.990 -5.858  26.015 1.00 27.55  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.183 -7.736  21.594 1.00 21.16  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.435 -8.138  20.925 1.00 20.61  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.420 -7.804  19.449 1.00 24.99  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.457 -7.423  18.911 1.00 23.40  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.795 -9.597  21.192 1.00 21.18  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.227 -9.825  22.625 1.00 21.90  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.321 -9.137  23.160 1.00 23.76  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.569 -10.756 23.428 1.00 23.51  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.717 -9.339  24.494 1.00 24.90  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 32.005 -11.004 24.742 1.00 26.09  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 33.051 -10.264 25.278 1.00 24.00  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.240 -7.884  18.806 1.00 22.79  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.133 -7.475  17.403 1.00 23.74  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.569 -5.997  17.245 1.00 28.05  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.374 -5.687  16.362 1.00 26.21  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.700 -7.698  16.905 1.00 25.54  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.480 -7.180  15.505 1.00 28.87  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 29.040 -7.826  14.405 1.00 30.55  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.725 -6.036  15.280 1.00 33.27  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.833 -7.351  13.109 1.00 32.56  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.516 -5.552  13.995 1.00 36.37  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.065 -6.216  12.916 1.00 42.90  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.829 -5.715  11.669 1.00 49.30  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.047 -5.102  18.103 0.52 25.32  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 30.043 -5.108  18.107 0.48 25.66  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.373 -3.673  18.091 0.52 26.47  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.358 -3.679  18.118 0.48 26.96  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.857 -3.434  18.392 0.52 31.05  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.852 -3.455  18.381 0.48 31.15  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.493 -2.645  17.699 0.52 32.48  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.486 -2.699  17.651 0.48 32.35  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.486 -2.924  19.082 0.52 29.07  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.518 -2.967  19.177 0.48 30.25  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.145 -2.915  18.623 0.52 30.59  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.777 -1.573  19.171 0.48 36.61  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.410 -4.142  19.398 1.00 27.30  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.819 -4.035  19.804 1.00 26.31  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.768 -4.424  18.678 1.00 28.91  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.669 -3.644  18.347 1.00 30.10  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.124 -4.873  21.108 1.00 27.48  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.411 -4.295  22.344 1.00 27.77  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.653 -4.986  21.375 1.00 25.98  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.398 -5.274  23.577 1.00 29.47  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.578 -5.615  18.092 1.00 24.31  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.547 -6.068  17.106 1.00 24.85  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.303 -5.535  15.690 1.00 29.03  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.147 -5.769  14.829 1.00 30.15  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.715 -7.593  17.151 1.00 24.96  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.132 -8.091  18.525 1.00 25.29  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.323 -7.658  19.113 1.00 28.37  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.321 -8.961  19.240 1.00 26.02  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.705 -8.118  20.382 1.00 28.79  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.709 -9.436  20.501 1.00 28.88  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.894 -9.013  21.064 1.00 27.26  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.235 -4.753  15.462 1.00 26.36  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.075 -4.058  14.171 1.00 27.47  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.634 -2.633  14.301 1.00 34.73  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.717 -1.893  13.312 1.00 34.39  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.656 -4.087  13.611 1.00 34.00  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.758 -3.577  14.585 1.00 31.03  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.234 -5.485  13.110 1.00 29.84  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.057 -2.257  15.520 1.00 31.28  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.666 -0.948  15.732 1.00 32.30  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.095 -1.010  15.198 1.00 38.34  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.844 -1.907  15.577 1.00 36.23  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.655 -0.559  17.218 1.00 33.09  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.398 0.737   17.432 1.00 45.86  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.776 1.802   17.281 1.00 51.22  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.628 0.684   17.676 1.00 46.26  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.479 -0.036  14.346 1.00 39.40  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.788 0.004   13.694 1.00 41.11  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 39.984 -0.057  14.652 1.00 45.52  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 41.010 -0.601  14.250 1.00 47.60  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.910 1.201   12.741 1.00 44.72  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 38.102 1.035   11.457 1.00 63.99  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.876 0.491   15.894 1.00 38.73  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 40.980 0.412   16.861 1.00 37.74  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.899 -0.836  17.715 1.00 40.65  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.927 -1.427  18.027 1.00 42.61  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 40.995 1.619   17.820 1.00 38.72  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.635 2.902   17.327 1.00 46.07  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.476 3.986   18.356 1.00 46.84  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.122 2.718   16.999 1.00 51.06  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.698 -1.177  18.192 1.00 33.57  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.530 -2.301  19.115 1.00 31.50  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.659 -3.662  18.454 1.00 36.00  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 40.029 -4.607  19.143 1.00 33.50  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.206 -2.215  19.894 1.00 32.55  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.099 -1.018  20.818 1.00 32.25  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.806 -1.106  21.614 1.00 28.93  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.509 0.202   22.318 1.00 36.56  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.925 1.213   21.408 1.00 35.72  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.374 -3.761  17.132 1.00 35.90  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.467 -5.023  16.372 1.00 36.21  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.860 -5.661  16.507 1.00 41.31  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 40.997 -6.877  16.344 1.00 41.48  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.097 -4.807  14.905 1.00 37.73  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.274 -3.780  13.974 1.00 43.94  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.882 -4.819  16.791 1.00 37.68  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.288 -5.201  16.918 1.00 38.53  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.762 -5.486  18.350 1.00 40.86  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.931 -5.823  18.555 1.00 40.95  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.182 -4.151  16.244 1.00 41.70  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 43.981 -4.108  14.740 1.00 56.57  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 43.948 -3.038  14.130 1.00 55.44  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.804 -5.267  14.106 1.00 46.49  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.869 -5.377  19.333 1.00 36.98  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.261 -5.639  20.714 1.00 36.22  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.237 -7.142  20.988 1.00 37.63  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.348 -7.831  20.477 1.00 35.62  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.304 -4.921  21.688 1.00 36.32  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.316 -3.383  21.661 1.00 41.38  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.246 -2.828  22.575 1.00 41.37  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.696 -2.814  22.058 1.00 42.40  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.205 -7.626  21.802 1.00 33.95  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.335 -9.033  22.206 0.42 32.99  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.277 -9.043  22.179 0.58 33.19  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.703 -9.239  23.588 1.00 33.84  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.512 -10.372 24.028 1.00 29.63  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.808 -9.435  22.251 0.42 37.76  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.714 -9.556  22.094 0.58 38.36  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.414 -9.346  20.973 0.42 43.60  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.559 -8.842  22.980 0.58 45.06  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.429 -8.128  24.301 1.00 30.02  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.833 -8.163  25.641 1.00 29.21  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.655 -7.188  25.681 1.00 30.80  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.804 -6.022  25.278 1.00 30.51  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.883 -7.822  26.747 1.00 34.43  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.259 -7.824  28.145 1.00 34.52  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 45.085 -8.765  26.692 1.00 35.23  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.498 -7.662  26.175 1.00 25.04  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.291 -6.849  26.386 1.00 24.54  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.895 -6.959  27.854 1.00 27.87  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.677 -8.068  28.351 1.00 27.83  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.120 -7.215  25.419 1.00 26.10  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.519 -7.068  23.914 1.00 27.07  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.828 -6.433  25.750 1.00 26.95  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.910 -5.635  23.418 1.00 30.89  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.763 -5.814  28.535 1.00 26.06  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.364 -5.788  29.936 1.00 26.29  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.890 -5.456  30.046 1.00 28.70  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.454 -4.385  29.596 1.00 26.54  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.187 -4.749  30.722 1.00 29.60  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.663 -4.978  30.676 1.00 47.88  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.163 -6.009  31.102 1.00 37.98  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.398 -4.013  30.173 1.00 44.36  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.126 -6.343  30.674 1.00 23.65  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.703 -6.093  30.861 1.00 23.38  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.461 -5.207  32.071 1.00 27.08  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.339 -5.054  32.933 1.00 28.83  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.889 -7.395  30.987 1.00 23.36  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.957 -8.404  29.812 1.00 26.14  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.834 -9.456  29.946 1.00 26.46  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.924 -7.709  28.424 1.00 26.93  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.268 -4.627  32.129 1.00 23.69  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.850 -3.731  33.216 1.00 25.94  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 33.011 -4.487  34.560 1.00 31.28  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.647 -5.661  34.637 1.00 29.81  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.381 -3.316  32.999 1.00 27.96  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.851 -2.294  33.993 1.00 36.97  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.717 -2.638  35.188 1.00 38.14  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.543 -1.164  33.573 1.00 40.55  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.591 -3.846  35.598 1.00 32.56  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.795 -4.556  36.886 1.00 32.70  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.552 -5.117  37.557 1.00 35.70  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.692 -5.967  38.430 1.00 36.84  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.478 -3.512  37.776 1.00 35.66  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.189 -2.182  37.128 1.00 40.98  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.114 -2.463  35.657 1.00 35.04  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.348 -4.675  37.165 1.00 31.99  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.112 -5.199  37.750 1.00 33.09  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.799 -6.605  37.191 1.00 32.45  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.957 -7.304  37.754 1.00 32.00  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.928 -4.247  37.493 1.00 35.85  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.900 -3.030  38.404 1.00 56.46  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.378 -3.310  39.800 1.00 89.44  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.150 -3.508  39.948 1.00 90.12  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.200 -3.342  40.745 1.00 89.44  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.473 -7.012  36.097 1.00 27.56  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.229 -8.324  35.496 1.00 26.88  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.831 -9.437  36.334 1.00 31.33  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 32.009 -9.404  36.681 1.00 29.84  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.665 -8.380  34.011 1.00 28.71  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.917 -7.296  33.177 1.00 29.72  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.472 -9.804  33.432 1.00 24.69  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.299 -7.359  33.205 1.00 33.95  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 30.006 -10.431 36.615 1.00 30.72  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.338 -11.605 37.400 1.00 31.30  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.060 -12.647 36.524 1.00 31.16  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.522 -13.038 35.489 1.00 29.40  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 29.033 -12.165 37.999 1.00 35.02  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.199 -13.461 38.741 1.00 49.84  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.875 -14.525 38.225 1.00 39.30  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.702 -13.396 39.968 1.00 44.28  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.265 -13.130 36.933 1.00 28.52  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.976 -14.137 36.120 1.00 28.04  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.185 -15.426 35.878 1.00 31.12  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.258 -15.968 34.774 1.00 30.48  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.244 -14.412 36.934 1.00 30.91  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.434 -13.175 37.761 1.00 35.76  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.054 -12.757 38.126 1.00 31.60  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.415 -15.911 36.883 1.00 28.31  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.640 -17.144 36.670 1.00 28.67  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.558 -16.932 35.595 1.00 30.01  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.430 -17.775 34.719 1.00 27.79  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.037 -17.683 37.975 1.00 31.41  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.446 -19.074 37.772 1.00 41.10  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.582 -19.645 38.883 1.00 68.28  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.592 -20.885 39.049 1.00 68.08  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 27.880 -18.867 39.570 1.00 62.15  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.848 -15.791 35.649 1.00 28.32  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.839 -15.434 34.653 1.00 27.61  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.460 -15.393 33.266 1.00 28.27  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.901 -15.940 32.300 1.00 25.86  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.663 -14.799 33.169 1.00 24.05  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.355 -14.749 31.881 1.00 22.86  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.710 -16.156 31.407 1.00 24.60  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.537 -16.459 30.235 1.00 23.69  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.632 -13.891 31.928 1.00 23.92  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.228 -13.762 30.540 1.00 23.75  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.660 -12.904 29.599 1.00 26.86  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.300 -14.555 30.149 1.00 24.12  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.159 -12.844 28.293 1.00 27.16  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.804 -14.488 28.848 1.00 26.14  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.222 -13.644 27.925 1.00 25.24  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.285 -16.971 32.291 1.00 24.45  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.694 -18.346 31.954 1.00 26.41  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.502 -19.168 31.387 1.00 27.25  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.638 -19.858 30.359 1.00 24.88  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.312 -19.019 33.176 1.00 30.46  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.959 -20.679 32.844 1.00 36.47  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.333 -19.074 32.056 1.00 24.05  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.103 -19.782 31.644 1.00 22.95  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.696 -19.327 30.230 1.00 24.20  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.320 -20.155 29.381 1.00 21.95  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.984 -19.556 32.697 1.00 26.05  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.269 -20.388 33.996 1.00 26.16  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.567 -19.847 32.120 1.00 26.13  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.526 -19.859 35.199 1.00 31.97  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.780 -18.029 29.976 1.00 21.92  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.426 -17.478 28.661 1.00 21.65  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.430 -17.828 27.589 1.00 23.77  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.034 -18.068 26.449 1.00 22.07  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.179 -15.976 28.738 1.00 22.82  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.882 -15.601 29.496 1.00 28.54  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.812 -14.137 29.715 1.00 30.04  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.628 -16.075 28.732 1.00 30.30  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.736 -17.829 27.933 1.00 21.38  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.778 -18.230 26.971 1.00 20.76  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.542 -19.706 26.584 1.00 23.46  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.626 -20.057 25.406 1.00 22.21  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.178 -18.030 27.581 1.00 20.65  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.346 -18.328 26.619 1.00 25.38  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.332 -17.374 25.395 1.00 24.44  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.700 -18.241 27.369 1.00 29.34  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.235 -20.568 27.571 1.00 22.10  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.909 -21.972 27.300 1.00 21.48  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.706 -22.076 26.371 1.00 23.65  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.753 -22.842 25.416 1.00 23.60  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.609 -22.697 28.618 1.00 24.30  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.855 -23.052 29.408 1.00 37.71  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.972 -22.969 28.832 1.00 37.63  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.719 -23.415 30.600 1.00 38.63  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.652 -21.278 26.617 1.00 21.76  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.455 -21.232 25.757 1.00 20.46  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.824 -20.845 24.316 1.00 21.95  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.340 -21.443 23.345 1.00 19.38  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.402 -20.262 26.342 1.00 21.08  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.286 -19.981 25.364 1.00 21.33  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.322 -20.951 25.088 1.00 23.44  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.265 -18.796 24.626 1.00 23.25  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.333 -20.722 24.134 1.00 23.76  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.271 -18.569 23.664 1.00 26.11  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.311 -19.531 23.428 1.00 25.02  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.656 -19.816 24.175 1.00 17.93  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.083 -19.374 22.826 1.00 17.36  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.642 -20.514 22.002 1.00 21.34  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.293 -20.643 20.831 1.00 20.92  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.162 -18.279 22.941 1.00 18.46  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.636 -16.979 23.509 1.00 20.31  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 30.006 -15.767 23.401 1.00 23.75  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.348 -14.474 24.513 1.00 23.77  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.506 -21.341 22.622 1.00 18.51  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.187 -22.436 21.945 1.00 18.75  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.428 -23.761 21.937 1.00 22.85  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.921 -24.714 21.323 1.00 21.87  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.556 -22.654 22.591 1.00 19.88  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.619 -21.688 22.104 1.00 20.93  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.782 -20.439 22.702 1.00 22.11  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.455 -22.022 21.036 1.00 21.74  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.778 -19.558 22.269 1.00 20.85  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.479 -21.172 20.625 1.00 22.28  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.615 -19.930 21.222 1.00 23.92  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.644 -19.120 20.819 1.00 22.21  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.270 -23.864 22.638 1.00 19.63  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.575 -25.168 22.692 1.00 20.96  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.061 -25.137 22.435 1.00 23.12  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.478 -26.221 22.283 1.00 22.71  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.760 -25.855 24.092 1.00 25.66  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.080 -25.087 25.090 1.00 25.19  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.233 -26.050 24.501 1.00 25.78  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.413 -23.952 22.537 1.00 19.44  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.935 -23.764 22.487 1.00 19.32  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.279 -24.177 23.828 1.00 22.59  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.065 -24.054 23.956 1.00 23.43  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.275 -24.585 21.365 1.00 20.70  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.902 -24.415 20.106 1.00 25.80  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.085 -24.644 24.809 0.60 21.04  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.064 -24.684 24.806 0.40 19.81  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.600 -25.117 26.110 0.60 21.91  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.510 -25.117 26.094 0.40 20.21  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.805 -24.057 27.180 0.60 25.13  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.788 -24.108 27.187 0.40 24.48  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.926 -23.560 27.362 0.60 23.69  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.932 -23.676 27.374 0.40 23.28  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.316 -26.420 26.518 0.60 25.82  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.965 -26.534 26.480 0.40 21.42  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.169 -27.561 25.498 0.60 33.18  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.313 -27.601 25.608 0.40 18.90  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.099 -28.728 25.811 0.60 37.48  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 24.061 -28.912 25.629 0.40 32.15  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.854 -29.276 27.148 0.60 40.60  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.456 -29.884 24.716 0.40 40.08  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 23.967 -30.230 27.414 0.60 53.46  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.337 -31.183 24.970 0.40 53.77  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.805 -30.663 28.655 0.60 40.00  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.781 -31.991 24.077 0.40 40.91  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.239 -30.761 26.438 0.60 42.27  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.771 -31.685 26.118 0.40 43.61  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.717 -23.712 27.882 1.00 22.26  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.754 -22.708 28.932 1.00 22.23  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.507 -23.341 30.295 1.00 28.25  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.431 -23.897 30.549 1.00 28.42  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.724 -21.609 28.607 1.00 22.34  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.737 -20.405 29.564 1.00 26.73  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 23.000 -19.554 29.339 1.00 25.52  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.480 -19.572 29.399 1.00 27.84  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.515 -23.259 31.180 1.00 27.34  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.426 -23.817 32.542 1.00 28.48  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.709 -22.805 33.456 1.00 33.17  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.342 -22.105 34.248 1.00 33.16  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.837 -24.182 33.080 1.00 31.21  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.819 -24.797 34.480 1.00 49.97  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.836 -25.389 34.916 1.00 41.60  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.901 -24.655 35.223 1.00 44.28  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.393 -22.702 33.298 1.00 30.09  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.580 -21.742 34.038 1.00 31.39  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.043 -22.376 35.304 1.00 36.01  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.408 -23.437 35.242 1.00 35.32  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.464 -21.248 33.109 1.00 32.16  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.732 -19.972 33.461 1.00 38.60  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.710 -18.767 33.558 1.00 38.73  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.637 -19.709 32.433 1.00 39.17  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.370 -21.767 36.469 1.00 33.40  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 19.986 -22.280 37.794 1.00 35.22  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.460 -21.157 38.679 1.00 37.24  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.798 -19.987 38.455 1.00 34.78  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.187 -22.966 38.482 1.00 36.63  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.810 -24.123 37.678 1.00 44.20  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.067 -24.703 38.319 1.00 61.34  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.830 -25.202 39.680 1.00 79.25  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.367 -26.415 39.977 1.00 98.84  ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.175 -26.767 41.242 1.00 86.44  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.087 -27.283 39.010 1.00 87.64  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.644 -21.496 39.703 1.00 35.34  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.119 -20.481 40.627 1.00 36.04  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.246 -19.588 41.194 1.00 41.06  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.075 -18.370 41.299 1.00 40.43  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.348 -21.159 41.788 1.00 39.49  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.611 -20.183 42.690 1.00 51.61  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.927 -20.807 43.892 1.00 85.21  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.528 -21.697 44.539 1.00 82.17  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.784 -20.394 44.193 1.00 88.74  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.381 -20.206 41.523 1.00 39.00  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.532 -19.522 42.111 1.00 39.12  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.346 -18.652 41.170 1.00 39.91  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.176 -17.864 41.625 1.00 39.19  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.124 -18.766 39.854 1.00 34.31  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.913 -17.966 38.919 1.00 31.99  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.087 -17.106 37.956 1.00 35.06  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.673 -16.301 37.224 1.00 32.76  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.892 -18.877 38.142 1.00 30.46  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.250 -19.818 37.134 1.00 37.55  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.211 -19.517 36.549 1.00 29.51  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.878 -20.963 36.864 1.00 31.02  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.746 -17.292 37.925 1.00 33.06  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.873 -16.638 36.937 1.00 32.56  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 20.017 -15.110 36.914 1.00 34.00  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 20.050 -14.530 35.821 1.00 31.55  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.390 -17.076 37.028 1.00 36.94  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.562 -16.489 35.846 1.00 37.22  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.759 -16.798 38.400 1.00 36.64  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.387 -17.321 35.398 1.00 38.35  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.109 -14.463 38.088 1.00 32.36  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.266 -13.009 38.129 1.00 33.08  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.571 -12.545 37.489 1.00 34.32  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.536 -11.611 36.689 1.00 32.52  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.094 -12.447 39.557 1.00 37.47  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.710 -12.711 40.154 1.00 44.49  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.288 -12.281 39.099 1.00 51.00  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.352 -10.470 39.183 1.00 48.34  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.712 -13.213 37.802 1.00 31.35  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 24.029 -12.867 37.223 1.00 30.70  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 24.023 -13.160 35.720 1.00 31.97  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.510 -12.345 34.929 1.00 29.45  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.137 -13.675 37.890 1.00 32.07  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.451 -14.315 35.329 1.00 27.10  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.372 -14.689 33.906 1.00 25.16  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.566 -13.652 33.113 1.00 28.01  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.056 -13.205 32.072 1.00 26.40  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.888 -16.150 33.680 1.00 28.74  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.631 -16.441 32.197 1.00 27.31  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.906 -17.142 34.237 1.00 28.56  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.365 -13.261 33.593 0.65 27.14  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.364 -13.262 33.591 0.35 27.15  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.547 -12.268 32.882 0.65 28.23  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.545 -12.269 32.884 0.35 28.14  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.263 -10.916 32.763 0.65 31.39  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.259 -10.920 32.764 0.35 31.63  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.243 -10.304 31.688 0.65 29.87  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.244 -10.320 31.684 0.35 30.46  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.183 -12.079 33.553 0.65 32.08  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.172 -12.089 33.541 0.35 32.11  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.254 -11.182 32.749 0.65 36.22  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.235 -11.244 32.702 0.35 36.50  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.579 -11.181 33.405 0.65 42.17  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.624 -11.037 33.463 0.35 42.84  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.768 -10.058 34.849 0.65 39.88  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.200 -9.440  32.835 0.35 40.39  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.887 -10.452 33.860 1.00 28.90  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.628 -9.168  33.876 1.00 28.76  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.786 -9.203  32.874 1.00 29.06  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.949 -8.254  32.096 1.00 27.37  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.128 -8.855  35.280 1.00 30.12  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.521 -10.332 32.819 1.00 25.28  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.622 -10.504 31.874 1.00 24.39  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.093 -10.552 30.427 1.00 27.76  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.673 -9.889  29.557 1.00 25.81  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.529 -11.694 32.256 1.00 29.60  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.809 -11.656 33.665 1.00 29.50  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.844 -11.704 31.464 1.00 28.93  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 23.981 -11.288 30.178 1.00 24.47  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.393 -11.386 28.832 1.00 23.03  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.886 -10.015 28.360 1.00 25.81  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.028 -9.688  27.186 1.00 24.43  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.283 -12.440 28.800 1.00 23.98  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.358 -9.184  29.279 1.00 24.32  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.905 -7.831  28.909 1.00 24.82  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.100 -6.964  28.459 1.00 27.75  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.048 -6.322  27.407 1.00 27.69  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.161 -7.188  30.087 1.00 28.44  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.755 -7.739  30.236 1.00 33.98  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 19.005 -7.182  31.779 1.00 41.78  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.685 -5.474  31.366 1.00 39.86  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.185 -7.009  29.227 1.00 25.12  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.431 -6.286  28.939 1.00 24.88  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.050 -6.774  27.608 1.00 26.77  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.439 -5.949  26.769 1.00 24.94  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.399 -6.514  30.103 1.00 25.68  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.818 -6.039  29.872 1.00 26.34  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.140 -4.685  29.940 1.00 29.03  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.852 -6.949  29.651 1.00 25.66  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.449 -4.244  29.744 1.00 26.44  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.170 -6.523  29.489 1.00 25.39  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.463 -5.169  29.559 1.00 26.01  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.756 -4.748  29.438 1.00 25.97  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.094 -8.104  27.400 1.00 23.66  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.671 -8.701  26.189 1.00 22.12  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.753 -8.571  24.975 1.00 25.44  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.193 -8.839  23.860 1.00 24.13  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.036 -10.181 26.433 1.00 21.05  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.171 -10.455 27.456 1.00 23.83  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.446 -11.978 27.545 1.00 22.87  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.480 -9.673  27.089 1.00 24.76  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.469 -8.209  25.197 1.00 23.81  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.463 -8.067  24.134 1.00 24.25  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.227 -9.422  23.452 1.00 26.23  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.491 -9.606  22.261 1.00 24.85  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.849 -6.963  23.127 1.00 25.65  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 24.021 -5.569  23.767 1.00 29.29  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.728 -4.632  22.821 1.00 40.76  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.585 -4.727  21.611 1.00 31.64  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.525 -3.720  23.346 1.00 35.53  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.761 -10.382 24.255 1.00 23.39  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.438 -11.752 23.818 1.00 22.31  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.933 -11.909 24.080 1.00 28.81  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.511 -12.388 25.142 1.00 27.32  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.291 -12.732 24.629 1.00 22.89  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.784 -12.600 24.314 1.00 24.45  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.802 -13.630 25.373 1.00 27.77  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.427 -15.305 24.635 1.00 24.79  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.123 -11.366 23.149 1.00 28.82  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.668 -11.223 23.288 1.00 31.44  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.907 -12.508 23.596 1.00 32.14  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.991 -12.461 24.413 1.00 32.50  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.054 -10.530 22.062 1.00 34.85  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.624 -9.139  21.825 1.00 48.09  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.271 -13.644 22.979 1.00 27.80  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.534 -14.882 23.269 1.00 29.47  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.754 -15.354 24.705 1.00 31.60  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.795 -15.792 25.343 1.00 32.20  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.827 -15.979 22.250 1.00 31.08  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.371 -15.642 20.867 1.00 35.92  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 16.034 -15.442 20.580 1.00 39.74  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 18.086 -15.525 19.725 1.00 37.34  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 15.982 -15.172 19.286 1.00 39.26  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.188 -15.227 18.729 1.00 38.39  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 18.990 -15.197 25.232 1.00 25.54  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.298 -15.545 26.627 1.00 25.37  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.510 -14.642 27.582 1.00 31.19  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.899 -15.136 28.540 1.00 29.67  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.812 -15.554 26.948 1.00 27.43  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.047 -15.820 28.437 1.00 27.38  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.541 -16.597 26.100 1.00 26.35  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.507 -13.317 27.312 1.00 28.18  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.758 -12.351 28.135 1.00 29.27  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.270 -12.759 28.195 1.00 35.15  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.704 -12.817 29.291 1.00 34.41  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.944 -10.882 27.654 1.00 31.94  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.093 -9.909  28.486 1.00 32.51  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.416 -10.465 27.704 1.00 30.85  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.631 -12.961 27.022 0.41 33.40  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.701 -13.163 27.040 0.59 32.62  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.206 -13.308 26.896 0.41 35.20  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.318 -13.630 26.905 0.59 34.00  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.776 -14.514 27.734 0.41 39.53  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 14.002 -14.838 27.803 0.59 36.28  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.699 -14.485 28.324 0.41 41.00  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.052 -14.758 28.581 0.59 36.59  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.820 -13.509 25.418 0.41 37.34  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 13.994 -13.938 25.429 0.59 36.07  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.614 -12.230 24.627 0.41 50.28  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.543 -14.292 25.166 0.59 50.03  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.096 -11.248 25.203 0.41 54.15  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.660 -13.479 25.513 0.59 53.01  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 13.959 -12.212 23.428 0.41 55.60  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.292 -15.374 24.596 0.59 55.02  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.619 -15.556 27.800 0.41 34.83  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.800 -15.935 27.733 0.59 31.26  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.355 -16.782 28.561 0.41 35.05  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.531 -17.116 28.576 0.59 31.58  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.534 -16.563 30.037 0.41 37.58  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.735 -16.834 30.075 0.59 35.53  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.689 -17.009 30.816 0.41 38.22  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 14.088 -17.487 30.893 0.59 35.32  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.199 -17.909 28.014 0.41 43.42  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.294 -18.375 28.116 0.59 31.76  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 14.856 -17.981 26.650 0.41 44.26  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.663 -19.508 28.723 0.59 32.88  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.905 -19.245 28.679 0.41 43.48  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.773 -18.358 28.497 0.59 25.45  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.637 -15.887 30.430 1.00 32.24  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.896 -15.531 31.840 1.00 32.75  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.684 -14.803 32.385 1.00 39.24  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.197 -15.152 33.469 1.00 39.52  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.147 -14.674 31.954 1.00 31.66  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.682 -15.600 31.768 1.00 34.03  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.154 -13.835 31.591 1.00 37.04  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.950 -13.069 31.933 1.00 39.05  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.758 -14.010 32.194 1.00 43.88  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.042 -13.837 33.187 1.00 43.51  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.595 -12.092 30.806 1.00 41.68  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.444 -10.835 30.798 1.00 56.25  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.623 -9.607  30.453 1.00 71.62  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 13.012 -9.035  29.161 1.00 80.83  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.938 -8.093  29.001 1.00 90.93  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.592 -7.607  30.050 1.00 71.76  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.221 -7.633  27.789 1.00 79.11  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.567 -15.008 31.310 1.00 41.30  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.473 -15.984 31.414 1.00 42.57  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.626 -16.890 32.633 1.00 45.93  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.638  -17.133 33.322 1.00 45.96  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.355 -16.827 30.128 1.00 44.27  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.876  -16.034 28.917 1.00 61.76  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.558  -16.939 27.728 1.00 72.64  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.613  -16.225 26.393 1.00 82.76  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.590  -15.150 26.263 1.00 91.95  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.856 -17.392 32.899 1.00 41.34  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.140 -18.256 34.051 1.00 41.94  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.944 -17.499 35.370 1.00 46.98  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.399 -18.068 36.325 1.00 46.96  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.544 -18.864 33.943 1.00 42.24  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.659 -20.173 33.179 1.00 43.85  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.126 -20.305 31.898 1.00 46.90  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.370 -21.246 33.708 1.00 46.56  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.245 -21.510 31.190 1.00 47.36  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.498 -22.447 32.994 1.00 48.08  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.937 -22.569 31.742 1.00 45.55  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.327 -16.205 35.405 1.00 42.58  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.127 -15.351 36.589 1.00 43.97  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.628 -15.109 36.839 1.00 50.83  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.174 -15.235 37.982 1.00 51.80  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.967 -14.045 36.517 1.00 45.68  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.462 -14.374 36.675 1.00 43.93  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.529 -13.011 37.593 1.00 48.09  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.404 -13.328 36.120 1.00 49.95  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.862  -14.807 35.764 1.00 49.09  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.412  -14.559 35.820 1.00 51.79  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.637  -15.785 36.350 1.00 57.56  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.676  -15.619 37.098 1.00 58.24  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.882  -14.135 34.440 1.00 55.13  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.516  -13.454 34.480 1.00 74.74  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.906  -13.350 33.089 1.00 87.48  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.479  -12.859 33.130 1.00 102.34 ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.842  -12.912 31.788 1.00 112.64 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.080  -17.003 35.985 1.00 53.13  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.466  -18.256 36.435 1.00 54.76  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.619  -18.474 37.953 1.00 60.90  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.744  -19.078 38.561 1.00 61.73  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.063  -19.431 35.669 1.00 53.78  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.719  -17.984 38.554 1.00 58.96  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 8.998  -18.127 39.989 1.00 61.62  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.298  -17.084 40.885 1.00 69.79  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.192  -17.313 42.095 1.00 72.15  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.503 -18.130 40.249 1.00 65.15  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 11.059 -19.417 40.026 1.00 76.31  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.807  -15.962 40.306 1.00 66.29  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.124  -14.907 41.064 1.00 88.87  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.667  -15.263 41.392 1.00 130.84 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.398  -16.295 42.002 1.00 97.78  ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.239  -13.538 40.359 1.00 89.37  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.227  -13.288 39.248 1.00 99.55  ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.436  -12.063 38.374 1.00 120.27 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.545  -11.479 38.397 1.00 113.26 ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.483  -11.695 37.649 1.00 114.37 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.264 -35.132 5.860  1.00 28.16  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.336 -33.980 6.315  1.00 28.78  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.455 -36.330 6.759  1.00 28.11  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.985 -35.392 4.587  0.78 27.04  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 21.014 -35.408 4.578  0.22 27.18  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.776 -34.338 3.605  0.78 26.14  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.756 -34.369 3.579  0.22 26.58  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.277 -34.184 3.313  0.78 29.88  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.256 -34.182 3.385  0.22 29.67  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.540 -35.179 3.290  0.78 29.60  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.499 -35.155 3.458  0.22 29.16  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.563 -34.652 2.320  0.78 25.05  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.458 -34.658 2.227  0.22 25.40  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.060 -34.617 2.510  0.78 25.40  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.805 -35.701 1.363  0.22 26.33  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.852 -35.622 2.984  0.78 28.12  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.127 -37.023 1.296  0.22 29.37  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.928 -33.497 2.281  0.78 24.90  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.749 -35.497 0.409  0.22 26.19  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.163 -35.194 3.068  0.78 27.09  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.305 -37.667 0.403  0.22 28.83  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.247 -33.919 2.573  0.78 28.21  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.460 -36.752 -0.170 0.22 30.19  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.723 -32.178 1.841  0.78 25.40  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 18.998 -34.378 0.005  0.22 27.24  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.355 -33.070 2.441  0.78 27.05  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.460 -36.920 -1.137 0.22 29.38  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.826 -31.351 1.673  0.78 26.37  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 18.002 -34.548 -0.944 0.22 28.88  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.120 -31.798 1.972  0.78 27.27  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.747 -35.804 -1.511 0.22 29.42  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.831 -32.939 3.118  1.00 25.55  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.424 -32.593 2.874  1.00 25.18  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.291 -31.546 1.769  1.00 27.43  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.258 -30.851 1.426  1.00 25.57  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.697 -32.078 4.173  1.00 28.11  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.682 -33.128 5.286  1.00 28.12  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.284 -30.742 4.675  1.00 27.91  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.058 -31.369 1.302  1.00 24.82  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.686 -30.282 0.409  1.00 25.16  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.294 -29.154 1.396  1.00 28.63  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.280 -29.289 2.097  1.00 27.65  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.488 -30.647 -0.502 1.00 26.89  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.770 -31.911 -1.391 1.00 26.14  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.057 -29.411 -1.345 1.00 27.68  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.082 -31.832 -2.317 1.00 29.52  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.077 -28.062 1.490  1.00 27.96  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.741 -26.997 2.457  1.00 28.69  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.480 -26.210 2.088  1.00 32.69  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.198 -26.012 0.904  1.00 32.09  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 16.992 -26.105 2.451  1.00 30.15  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.557 -26.280 1.053  1.00 33.98  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.304 -27.735 0.726  1.00 29.60  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.862 -25.583 3.096  1.00 30.34  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.312 -10.297 11.839 1.00 28.87  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.291 -9.366  12.200 1.00 30.71  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.978 -10.744 18.111 1.00 27.14  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.480 -9.446  18.158 1.00 28.37  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.526 -10.068 16.390 1.00 24.84  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.365 -10.223 14.022 1.00 26.55  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.949 -8.460  17.296 1.00 26.64  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.965 -8.785  16.402 1.00 25.73  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 25.001 -11.061 17.221 1.00 25.26  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.419 -10.606 13.185 1.00 26.61  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.260 -10.576 19.725 1.00 32.10  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.233 -11.567 19.121 1.00 29.29  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.250 -9.672  11.327 1.00 30.97  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.276 -9.601  13.518 1.00 29.62  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.474 -9.372  19.131 1.00 29.37  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.367 -10.530 15.351 1.00 25.00  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.406 -10.808 20.581 1.00 31.87  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.835 -11.396 13.774 0.99 25.98  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.312 -15.224 22.569 1.00 33.11  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.589 -35.390 -1.241 0.78 45.47  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.314 -35.175 -0.578 0.78 46.81  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.729 -34.482 -0.226 0.78 43.96  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 18.029 -37.025 -0.763 0.78 44.87  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 25.869 -3.403  26.378 1.00 33.85  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 35.691 -25.656 25.586 1.00 42.07  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 22.767 -5.362  19.794 1.00 57.18  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 38.384 -14.920 15.444 1.00 33.36  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 37.935 2.445   19.652 1.00 40.54  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 41.275 -21.649 25.170 1.00 43.06  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 33.372 -20.816 29.577 1.00 48.11  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 44.543 -0.890  17.882 1.00 52.79  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 16.594 -27.593 -3.292 1.00 53.38  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 19.872 -9.523  36.968 1.00 40.18  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 20.808 -5.884  25.987 1.00 43.14  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 43.645 -6.586  31.959 1.00 47.61  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 44.989 -11.249 18.651 1.00 59.35  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 37.625 -20.421 26.987 1.00 33.43  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 26.821 -31.982 16.161 1.00 45.35  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 31.784 -0.813  15.847 1.00 40.25  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 23.449 -5.735  32.934 1.00 37.97  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 29.915 -32.068 9.568  1.00 46.81  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 32.501 -24.712 32.167 1.00 64.09  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 27.144 -35.308 11.791 1.00 59.09  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 41.338 -16.947 15.176 1.00 36.66  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 17.974 -29.374 7.668  1.00 34.33  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 13.483 -14.348 21.828 1.00 64.68  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 22.971 -28.246 12.632 1.00 25.94  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 21.932 -24.962 18.321 1.00 23.63  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 27.273 -10.111 35.850 1.00 38.91  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 30.304 1.518   33.930 1.00 62.59  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 14.260 -16.833 23.416 1.00 42.95  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 22.606 -27.652 17.718 1.00 50.59  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 26.100 -22.522 29.932 1.00 26.95  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 34.928 -18.857 13.855 0.50 27.68  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 32.336 -8.909  39.702 1.00 57.14  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 41.653 -12.823 14.287 1.00 85.04  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 28.264 -8.819  39.918 1.00 47.72  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 19.020 -24.842 32.931 1.00 39.34  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 7.058  -16.989 32.431 1.00 55.07  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 20.507 -13.383 20.399 1.00 51.49  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 29.557 -2.171  13.777 1.00 64.22  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 15.429 -9.868  24.842 1.00 50.54  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 27.330 -28.125 18.651 1.00 31.49  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 28.208 -23.708 31.645 1.00 41.04  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 43.918 -4.349  25.742 1.00 47.13  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 12.638 -20.381 42.491 1.00 59.67  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 26.051 -21.818 38.626 1.00 38.12  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 26.410 -7.712  36.829 1.00 53.54  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 4.339  -20.200 37.860 1.00 61.12  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 27.192 -2.440  16.093 1.00 64.98  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 26.817 -16.514 38.626 1.00 50.68  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 24.840 -26.758 19.006 1.00 33.02  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 41.283 -6.966  35.916 1.00 46.35  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 30.396 -0.465  36.873 1.00 55.16  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 21.461 -29.941 14.203 1.00 73.76  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 29.024 -31.171 7.259  1.00 30.83  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 36.845 -5.582  12.147 1.00 38.18  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 22.651 -34.052 8.853  1.00 33.37  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 43.533 -10.650 35.322 1.00 63.64  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 25.634 -2.785  19.904 1.00 60.89  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 44.429 -12.460 41.159 1.00 56.59  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 46.074 -14.211 21.522 1.00 60.30  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 34.137 -7.817  35.611 1.00 34.25  ? 360 HOH A O   1 
HETATM 1263 O  O   . HOH F 6 .   ? 20.819 -7.167  19.597 1.00 54.57  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 42.467 -10.365 15.404 1.00 48.12  ? 362 HOH A O   1 
HETATM 1265 O  O   . HOH F 6 .   ? 23.143 -17.011 44.288 1.00 61.91  ? 363 HOH A O   1 
HETATM 1266 O  O   . HOH F 6 .   ? 24.045 -15.792 21.148 1.00 30.38  ? 364 HOH A O   1 
HETATM 1267 O  O   . HOH F 6 .   ? 29.362 -27.370 20.641 1.00 25.53  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 46.203 -15.854 27.636 1.00 61.45  ? 366 HOH A O   1 
HETATM 1269 O  O   . HOH F 6 .   ? 21.436 -27.077 14.516 0.50 44.04  ? 367 HOH A O   1 
HETATM 1270 O  O   A HOH F 6 .   ? 19.102 -22.989 4.284  0.60 35.18  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 28.520 -24.246 34.306 1.00 55.91  ? 369 HOH A O   1 
HETATM 1272 O  O   . HOH F 6 .   ? 39.057 -18.966 33.287 1.00 51.85  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 22.225 -34.023 26.346 1.00 72.41  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 10.847 -11.347 34.489 1.00 51.89  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 46.359 -29.723 21.222 1.00 71.65  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 30.705 -28.820 22.631 1.00 39.31  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 26.066 -19.112 41.717 1.00 71.39  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 46.894 -21.846 17.891 1.00 43.00  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 37.409 -6.458  34.264 1.00 40.78  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 20.167 -15.782 40.856 1.00 34.68  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 27.639 -23.066 13.855 0.50 25.81  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 47.255 -25.297 21.712 1.00 56.24  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 18.078 -34.578 8.336  1.00 33.99  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 25.894 -4.539  17.863 1.00 50.89  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 26.323 -7.907  9.075  1.00 47.56  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 11.359 -14.891 40.568 1.00 84.84  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 46.264 -19.060 19.751 1.00 50.85  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 18.038 -24.307 39.764 1.00 43.18  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 21.322 -31.116 30.051 1.00 64.66  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 44.898 -8.637  17.897 1.00 63.99  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 33.057 -29.633 21.526 1.00 41.64  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 31.836 -31.866 14.645 1.00 43.10  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 42.200 -6.097  11.824 1.00 62.89  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 46.058 -8.865  44.068 1.00 52.83  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 40.353 -19.613 28.989 1.00 35.63  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 20.914 -23.041 42.033 1.00 49.03  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 45.280 -12.672 23.607 1.00 48.50  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 27.119 -1.714  21.906 1.00 53.08  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 37.934 -16.265 12.764 1.00 50.29  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 47.024 -20.184 22.066 1.00 65.39  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 41.198 -17.086 35.179 1.00 43.66  ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 19.684 -27.410 10.090 1.00 57.72  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 23.671 -15.712 17.865 1.00 42.63  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 35.537 2.107   13.567 1.00 57.44  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 33.767 -33.083 12.282 1.00 41.15  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 35.245 -29.725 23.569 1.00 48.69  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 34.896 -33.321 21.890 1.00 60.80  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 22.863 -14.812 40.371 1.00 34.65  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 30.334 -10.480 40.544 1.00 42.32  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 32.152 -15.619 39.824 1.00 35.91  ? 408 HOH A O   1 
HETATM 1311 O  O   . HOH F 6 .   ? 22.416 -10.150 14.411 1.00 42.54  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 39.956 -5.581  33.868 1.00 46.05  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 45.513 -10.497 30.403 1.00 59.48  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 37.181 -2.435  11.591 1.00 60.04  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 44.578 -16.450 29.714 1.00 49.11  ? 413 HOH A O   1 
HETATM 1316 O  O   . HOH F 6 .   ? 10.202 -11.766 39.906 1.00 64.29  ? 414 HOH A O   1 
HETATM 1317 O  O   . HOH F 6 .   ? 25.973 -29.256 22.545 1.00 57.10  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 42.000 -8.103  13.675 1.00 61.59  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 29.593 -0.803  22.183 1.00 56.19  ? 417 HOH A O   1 
HETATM 1320 O  O   B HOH F 6 .   ? 37.264 -11.903 40.092 0.50 34.32  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 27.466 -25.688 28.158 1.00 56.02  ? 419 HOH A O   1 
HETATM 1322 O  O   . HOH F 6 .   ? 33.547 -0.295  19.985 1.00 47.81  ? 420 HOH A O   1 
HETATM 1323 O  O   . HOH F 6 .   ? 28.782 -16.070 41.371 1.00 69.52  ? 421 HOH A O   1 
HETATM 1324 O  O   . HOH F 6 .   ? 45.856 -17.150 17.063 1.00 67.04  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 33.913 -17.664 39.363 1.00 64.28  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 44.348 -25.951 26.549 1.00 59.19  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 23.451 -30.474 19.252 1.00 68.28  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 44.847 -8.126  15.204 1.00 75.68  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 45.735 -5.492  23.696 1.00 47.42  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 29.971 -22.617 36.684 1.00 77.80  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 28.294 -2.498  11.335 1.00 70.33  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 25.723 -15.858 41.049 1.00 53.96  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 42.874 -18.312 30.749 1.00 47.15  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 31.948 -26.236 27.000 1.00 45.30  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 32.466 -4.086  41.239 1.00 61.41  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 37.718 -27.065 28.455 1.00 63.71  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 47.915 -23.457 19.834 1.00 64.68  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 31.958 0.138   13.302 1.00 58.23  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 28.307 -29.252 26.833 1.00 80.70  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 20.097 -35.329 10.173 1.00 39.41  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 35.229 -4.075  10.630 1.00 48.47  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 27.170 -34.630 17.969 1.00 74.82  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 37.057 -24.334 27.535 1.00 58.12  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 19.435 -31.734 13.924 1.00 69.33  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 24.363 -21.490 40.995 1.00 58.46  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 47.151 -13.033 28.591 1.00 63.85  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 23.030 -2.720  26.177 1.00 63.66  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 33.795 -10.863 41.565 0.50 52.67  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 46.602 -14.682 17.942 1.00 72.25  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 31.014 -34.456 14.780 1.00 63.37  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 34.569 -18.820 36.076 1.00 63.05  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 11.962 -18.626 22.435 1.00 59.10  ? 450 HOH A O   1 
HETATM 1353 O  O   . HOH F 6 .   ? 47.063 -11.880 25.499 1.00 67.28  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 32.264 -1.054  22.257 1.00 61.24  ? 452 HOH A O   1 
HETATM 1355 O  O   A HOH F 6 .   ? 11.999 -20.536 27.810 0.78 50.33  ? 453 HOH A O   1 
HETATM 1356 O  O   . HOH F 6 .   ? 47.362 -28.587 17.714 1.00 66.24  ? 454 HOH A O   1 
HETATM 1357 O  O   . HOH F 6 .   ? 13.660 -16.181 39.824 1.00 76.00  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 43.106 -3.100  33.804 1.00 62.08  ? 456 HOH A O   1 
HETATM 1359 O  O   . HOH F 6 .   ? 19.258 -7.540  35.243 1.00 60.71  ? 457 HOH A O   1 
HETATM 1360 O  O   . HOH F 6 .   ? 17.084 -28.102 9.865  1.00 55.02  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 15.896 -15.469 41.190 1.00 63.71  ? 459 HOH A O   1 
HETATM 1362 O  O   . HOH F 6 .   ? 25.358 -5.711  35.284 1.00 55.50  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 17.346 -8.027  24.790 1.00 56.19  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 28.057 -29.864 24.190 1.00 66.87  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 44.279 -13.459 13.855 0.50 73.30  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 33.795 -13.973 41.565 0.50 42.81  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 32.132 -23.874 34.780 1.00 67.80  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 32.632 -20.473 37.060 1.00 69.45  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 18.977 -28.068 13.855 0.50 71.42  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 45.465 -12.822 16.238 1.00 70.59  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 23.238 -4.601  17.205 1.00 77.16  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 21.118 -5.615  34.666 1.00 59.53  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 34.982 -23.690 32.721 1.00 61.11  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 32.964 -0.648  42.877 1.00 55.46  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 16.745 -6.611  34.614 1.00 82.64  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.344 -24.239 -0.039 1.00 49.25  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 15.070 -25.905 -1.784 1.00 44.57  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 21.024 -38.309 4.031  1.00 49.06  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 11.720 -23.534 3.031  1.00 54.24  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 17.791 -36.369 6.104  1.00 39.87  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 20.974 -39.589 -2.179 1.00 65.22  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 18.698 -40.712 0.669  1.00 70.04  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.661 -24.814 5.538  1.00 57.21  ? 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   ? 0.8284 1.0161 0.7105 0.0436  -0.1327 -0.0278 6   ASP A N   
2    C CA  . ASP A 5   ? 0.8232 1.0042 0.6884 0.0272  -0.1241 -0.0299 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8036 1.0163 0.6946 0.0147  -0.1200 -0.0466 6   ASP A C   
4    O O   . ASP A 5   ? 0.7935 1.0349 0.7128 0.0186  -0.1254 -0.0568 6   ASP A O   
5    C CB  . ASP A 5   ? 0.8458 0.9961 0.7008 0.0175  -0.1064 -0.0219 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.0394 1.1683 0.8603 0.0080  -0.1015 -0.0170 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.0436 1.1852 0.8635 -0.0032 -0.0989 -0.0261 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.1479 1.2469 0.9428 0.0106  -0.0989 -0.0051 6   ASP A OD2 
9    N N   . SER A 6   ? 0.7005 0.9073 0.5812 -0.0008 -0.1099 -0.0504 7   SER A N   
10   C CA  . SER A 6   ? 0.6541 0.8833 0.5540 -0.0145 -0.1037 -0.0657 7   SER A CA  
11   C C   . SER A 6   ? 0.6024 0.8166 0.5135 -0.0266 -0.0845 -0.0669 7   SER A C   
12   O O   . SER A 6   ? 0.5945 0.8123 0.5087 -0.0397 -0.0762 -0.0761 7   SER A O   
13   C CB  . SER A 6   ? 0.7299 0.9647 0.6082 -0.0216 -0.1088 -0.0709 7   SER A CB  
14   O OG  . SER A 6   ? 0.9027 1.1087 0.7520 -0.0273 -0.1008 -0.0624 7   SER A OG  
15   N N   . CYS A 7   ? 0.4835 0.6808 0.4005 -0.0215 -0.0784 -0.0581 8   CYS A N   
16   C CA  . CYS A 7   ? 0.4392 0.6216 0.3655 -0.0301 -0.0630 -0.0583 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4249 0.6234 0.3766 -0.0384 -0.0570 -0.0704 8   CYS A C   
18   O O   . CYS A 7   ? 0.4175 0.6389 0.3850 -0.0358 -0.0633 -0.0775 8   CYS A O   
19   C CB  . CYS A 7   ? 0.4529 0.6166 0.3796 -0.0220 -0.0600 -0.0470 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.5343 0.6697 0.4287 -0.0173 -0.0605 -0.0329 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3170 0.5022 0.2720 -0.0481 -0.0445 -0.0731 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2721 0.4612 0.2457 -0.0560 -0.0366 -0.0816 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3027 0.4733 0.2806 -0.0516 -0.0307 -0.0729 9   ILE A C   
24   O O   . ILE A 8   ? 0.2931 0.4475 0.2596 -0.0460 -0.0304 -0.0631 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3080 0.4930 0.2805 -0.0692 -0.0280 -0.0914 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3175 0.4790 0.2767 -0.0703 -0.0212 -0.0863 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3184 0.5258 0.2891 -0.0748 -0.0340 -0.1022 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3543 0.5073 0.3131 -0.0811 -0.0122 -0.0960 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2398 0.4115 0.2322 -0.0554 -0.0251 -0.0770 10  GLN A N   
30   N N   B GLN A 9   ? 0.2356 0.4092 0.2286 -0.0547 -0.0260 -0.0770 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2303 0.3846 0.2249 -0.0514 -0.0203 -0.0692 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2218 0.3793 0.2183 -0.0512 -0.0210 -0.0699 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2753 0.4147 0.2728 -0.0606 -0.0101 -0.0731 10  GLN A C   
34   C C   B GLN A 9   ? 0.2539 0.3950 0.2516 -0.0605 -0.0106 -0.0734 10  GLN A C   
35   O O   A GLN A 9   ? 0.2659 0.4136 0.2705 -0.0696 -0.0064 -0.0828 10  GLN A O   
36   O O   B GLN A 9   ? 0.2426 0.3898 0.2451 -0.0703 -0.0066 -0.0833 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2395 0.4070 0.2457 -0.0437 -0.0250 -0.0678 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2275 0.4006 0.2381 -0.0455 -0.0246 -0.0711 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2423 0.3933 0.2503 -0.0399 -0.0202 -0.0605 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.3260 0.4847 0.3415 -0.0450 -0.0177 -0.0668 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5798 0.7463 0.6026 -0.0351 -0.0224 -0.0634 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4467 0.6044 0.4636 -0.0329 -0.0225 -0.0588 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4638 0.6449 0.4999 -0.0421 -0.0187 -0.0736 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3126 0.4798 0.3272 -0.0233 -0.0318 -0.0558 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.6250 0.7881 0.6458 -0.0234 -0.0275 -0.0554 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.2910 0.4349 0.3098 -0.0330 -0.0163 -0.0550 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2518 0.3686 0.2427 -0.0584 -0.0059 -0.0660 11  PHE A N   
48   N N   B PHE A 10  ? 0.2177 0.3372 0.2100 -0.0575 -0.0068 -0.0657 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2529 0.3509 0.2428 -0.0646 0.0018  -0.0680 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2200 0.3198 0.2105 -0.0634 0.0009  -0.0671 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2726 0.3668 0.2675 -0.0634 0.0040  -0.0648 11  PHE A C   
52   C C   B PHE A 10  ? 0.2647 0.3612 0.2605 -0.0627 0.0033  -0.0646 11  PHE A C   
53   O O   A PHE A 10  ? 0.2625 0.3491 0.2556 -0.0560 0.0023  -0.0566 11  PHE A O   
54   O O   B PHE A 10  ? 0.2544 0.3460 0.2496 -0.0550 0.0012  -0.0566 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2774 0.3553 0.2589 -0.0619 0.0036  -0.0639 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2419 0.3231 0.2241 -0.0596 0.0020  -0.0618 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.3014 0.3581 0.2792 -0.0668 0.0094  -0.0667 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2674 0.3482 0.2450 -0.0639 0.0033  -0.0680 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3540 0.4077 0.3298 -0.0758 0.0136  -0.0756 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3076 0.4035 0.2819 -0.0635 -0.0007 -0.0696 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3330 0.3709 0.3073 -0.0625 0.0103  -0.0606 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3110 0.3749 0.2859 -0.0682 0.0085  -0.0726 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3799 0.4084 0.3484 -0.0797 0.0188  -0.0773 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3270 0.4227 0.2962 -0.0685 0.0015  -0.0764 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3701 0.3849 0.3371 -0.0657 0.0140  -0.0622 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3558 0.4194 0.3274 -0.0720 0.0105  -0.0797 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3529 0.3612 0.3160 -0.0739 0.0184  -0.0701 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3266 0.4070 0.2959 -0.0728 0.0075  -0.0819 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2305 0.3313 0.2315 -0.0718 0.0085  -0.0726 12  THR A N   
70   C CA  . THR A 11  ? 0.2356 0.3358 0.2418 -0.0735 0.0126  -0.0726 12  THR A CA  
71   C C   . THR A 11  ? 0.2904 0.3645 0.2867 -0.0702 0.0153  -0.0636 12  THR A C   
72   O O   . THR A 11  ? 0.2660 0.3422 0.2659 -0.0649 0.0144  -0.0593 12  THR A O   
73   C CB  . THR A 11  ? 0.3363 0.4414 0.3465 -0.0874 0.0204  -0.0841 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3074 0.4420 0.3297 -0.0895 0.0165  -0.0936 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3927 0.4980 0.4077 -0.0915 0.0268  -0.0861 12  THR A CG2 
76   N N   A ARG A 12  ? 0.2710 0.3213 0.2552 -0.0726 0.0177  -0.0617 13  ARG A N   
77   N N   B ARG A 12  ? 0.2743 0.3245 0.2585 -0.0727 0.0178  -0.0618 13  ARG A N   
78   C CA  A ARG A 12  ? 0.2841 0.3096 0.2578 -0.0694 0.0187  -0.0545 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.2889 0.3143 0.2625 -0.0694 0.0187  -0.0545 13  ARG A CA  
80   C C   A ARG A 12  ? 0.3064 0.3295 0.2797 -0.0583 0.0126  -0.0467 13  ARG A C   
81   C C   B ARG A 12  ? 0.3082 0.3313 0.2816 -0.0583 0.0126  -0.0467 13  ARG A C   
82   O O   A ARG A 12  ? 0.2955 0.3011 0.2616 -0.0550 0.0121  -0.0417 13  ARG A O   
83   O O   B ARG A 12  ? 0.2969 0.3028 0.2632 -0.0550 0.0121  -0.0417 13  ARG A O   
84   C CB  A ARG A 12  ? 0.3406 0.3394 0.3003 -0.0756 0.0229  -0.0565 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.3544 0.3534 0.3142 -0.0755 0.0228  -0.0565 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.4301 0.4227 0.3846 -0.0892 0.0316  -0.0636 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.4938 0.4808 0.4456 -0.0875 0.0313  -0.0609 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.5770 0.5630 0.5271 -0.0930 0.0363  -0.0615 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.6020 0.5765 0.5457 -0.0979 0.0369  -0.0683 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.6857 0.6403 0.6175 -0.0895 0.0353  -0.0535 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.6509 0.6031 0.5843 -0.0923 0.0336  -0.0657 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.7980 0.7454 0.7240 -0.0888 0.0366  -0.0490 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.7656 0.7215 0.7018 -0.0938 0.0335  -0.0716 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.5370 0.5061 0.4757 -0.0910 0.0398  -0.0520 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.6785 0.6140 0.6069 -0.0876 0.0307  -0.0702 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.6808 0.5995 0.5882 -0.0853 0.0341  -0.0422 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.4564 0.4372 0.4037 -0.1013 0.0358  -0.0800 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.2513 0.2908 0.2307 -0.0535 0.0083  -0.0463 14  HIS A N   
99   C CA  . HIS A 13  ? 0.2483 0.2853 0.2265 -0.0457 0.0046  -0.0405 14  HIS A CA  
100  C C   . HIS A 13  ? 0.2816 0.3131 0.2594 -0.0408 0.0039  -0.0341 14  HIS A C   
101  O O   . HIS A 13  ? 0.2651 0.2846 0.2393 -0.0376 0.0031  -0.0312 14  HIS A O   
102  C CB  . HIS A 13  ? 0.2423 0.2952 0.2224 -0.0432 0.0013  -0.0408 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.2665 0.3146 0.2433 -0.0382 0.0000  -0.0363 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.2747 0.3146 0.2502 -0.0384 0.0014  -0.0389 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.2762 0.3263 0.2512 -0.0334 -0.0017 -0.0305 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.2693 0.3094 0.2436 -0.0352 0.0012  -0.0357 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.2663 0.3105 0.2386 -0.0327 -0.0002 -0.0301 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.2414 0.2829 0.2240 -0.0398 0.0040  -0.0330 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2380 0.2741 0.2202 -0.0354 0.0041  -0.0277 15  ALA A CA  
110  C C   . ALA A 14  ? 0.2744 0.2925 0.2496 -0.0384 0.0069  -0.0268 15  ALA A C   
111  O O   . ALA A 14  ? 0.2553 0.2645 0.2270 -0.0348 0.0056  -0.0227 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2482 0.2982 0.2383 -0.0331 0.0039  -0.0285 15  ALA A CB  
113  N N   A SER A 15  ? 0.2478 0.2599 0.2194 -0.0455 0.0107  -0.0309 16  SER A N   
114  N N   B SER A 15  ? 0.2514 0.2635 0.2230 -0.0455 0.0107  -0.0309 16  SER A N   
115  N N   C SER A 15  ? 0.2468 0.2588 0.2184 -0.0455 0.0107  -0.0309 16  SER A N   
116  C CA  A SER A 15  ? 0.2600 0.2506 0.2193 -0.0491 0.0132  -0.0296 16  SER A CA  
117  C CA  B SER A 15  ? 0.2656 0.2561 0.2248 -0.0492 0.0132  -0.0296 16  SER A CA  
118  C CA  C SER A 15  ? 0.2588 0.2492 0.2180 -0.0490 0.0132  -0.0294 16  SER A CA  
119  C C   A SER A 15  ? 0.3194 0.2943 0.2710 -0.0447 0.0086  -0.0270 16  SER A C   
120  C C   B SER A 15  ? 0.3249 0.2996 0.2764 -0.0448 0.0086  -0.0271 16  SER A C   
121  C C   C SER A 15  ? 0.3244 0.2988 0.2757 -0.0448 0.0086  -0.0271 16  SER A C   
122  O O   A SER A 15  ? 0.2953 0.2567 0.2391 -0.0418 0.0063  -0.0234 16  SER A O   
123  O O   B SER A 15  ? 0.3065 0.2675 0.2500 -0.0420 0.0064  -0.0235 16  SER A O   
124  O O   C SER A 15  ? 0.3105 0.2706 0.2535 -0.0421 0.0064  -0.0235 16  SER A O   
125  C CB  A SER A 15  ? 0.3099 0.2949 0.2639 -0.0595 0.0196  -0.0350 16  SER A CB  
126  C CB  B SER A 15  ? 0.3208 0.3057 0.2747 -0.0595 0.0196  -0.0351 16  SER A CB  
127  C CB  C SER A 15  ? 0.3057 0.2905 0.2596 -0.0594 0.0198  -0.0348 16  SER A CB  
128  O OG  A SER A 15  ? 0.3691 0.3283 0.3057 -0.0635 0.0221  -0.0328 16  SER A OG  
129  O OG  B SER A 15  ? 0.3826 0.3858 0.3472 -0.0635 0.0240  -0.0397 16  SER A OG  
130  O OG  C SER A 15  ? 0.3474 0.3318 0.3008 -0.0632 0.0202  -0.0392 16  SER A OG  
131  N N   . ASP A 16  ? 0.2981 0.2764 0.2529 -0.0437 0.0068  -0.0300 17  ASP A N   
132  C CA  . ASP A 16  ? 0.3151 0.2822 0.2667 -0.0384 0.0025  -0.0301 17  ASP A CA  
133  C C   . ASP A 16  ? 0.3081 0.2829 0.2662 -0.0314 -0.0014 -0.0274 17  ASP A C   
134  O O   . ASP A 16  ? 0.3124 0.2771 0.2676 -0.0265 -0.0056 -0.0267 17  ASP A O   
135  C CB  . ASP A 16  ? 0.3354 0.3079 0.2911 -0.0396 0.0030  -0.0355 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.4599 0.4197 0.4073 -0.0471 0.0071  -0.0396 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.4696 0.4139 0.4060 -0.0518 0.0100  -0.0379 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.4560 0.4204 0.4064 -0.0494 0.0084  -0.0450 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.2523 0.2441 0.2184 -0.0310 -0.0002 -0.0262 18  VAL A N   
140  C CA  . VAL A 17  ? 0.2413 0.2380 0.2114 -0.0268 -0.0019 -0.0240 18  VAL A CA  
141  C C   . VAL A 17  ? 0.2747 0.2617 0.2400 -0.0256 -0.0029 -0.0207 18  VAL A C   
142  O O   . VAL A 17  ? 0.2622 0.2457 0.2280 -0.0222 -0.0061 -0.0212 18  VAL A O   
143  C CB  . VAL A 17  ? 0.2619 0.2723 0.2358 -0.0269 -0.0001 -0.0222 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.2593 0.2696 0.2337 -0.0245 0.0002  -0.0192 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.2531 0.2724 0.2288 -0.0281 0.0002  -0.0255 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.2503 0.2345 0.2117 -0.0287 0.0000  -0.0187 19  LEU A N   
147  C CA  . LEU A 18  ? 0.2648 0.2397 0.2200 -0.0288 0.0000  -0.0162 19  LEU A CA  
148  C C   . LEU A 18  ? 0.3158 0.2730 0.2599 -0.0278 -0.0042 -0.0161 19  LEU A C   
149  O O   . LEU A 18  ? 0.2859 0.2385 0.2271 -0.0248 -0.0078 -0.0151 19  LEU A O   
150  C CB  . LEU A 18  ? 0.2792 0.2555 0.2331 -0.0331 0.0053  -0.0159 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.3213 0.2913 0.2705 -0.0334 0.0069  -0.0139 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.3199 0.2978 0.2762 -0.0290 0.0062  -0.0122 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.3754 0.3471 0.3242 -0.0386 0.0134  -0.0159 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.3023 0.2492 0.2396 -0.0298 -0.0042 -0.0176 20  LEU A N   
155  C CA  . LEU A 19  ? 0.3326 0.2578 0.2560 -0.0272 -0.0094 -0.0170 20  LEU A CA  
156  C C   . LEU A 19  ? 0.3312 0.2610 0.2624 -0.0183 -0.0172 -0.0191 20  LEU A C   
157  O O   . LEU A 19  ? 0.3227 0.2423 0.2465 -0.0136 -0.0238 -0.0181 20  LEU A O   
158  C CB  . LEU A 19  ? 0.3661 0.2789 0.2817 -0.0311 -0.0070 -0.0190 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.4891 0.3736 0.3862 -0.0276 -0.0125 -0.0177 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.5322 0.3952 0.4074 -0.0325 -0.0112 -0.0132 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5605 0.4334 0.4523 -0.0311 -0.0094 -0.0207 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.2802 0.2269 0.2265 -0.0164 -0.0165 -0.0229 21  ASN A N   
163  C CA  . ASN A 20  ? 0.2741 0.2298 0.2315 -0.0096 -0.0217 -0.0274 21  ASN A CA  
164  C C   . ASN A 20  ? 0.2950 0.2604 0.2579 -0.0088 -0.0228 -0.0271 21  ASN A C   
165  O O   . ASN A 20  ? 0.2890 0.2562 0.2562 -0.0032 -0.0293 -0.0308 21  ASN A O   
166  C CB  . ASN A 20  ? 0.2845 0.2546 0.2541 -0.0101 -0.0184 -0.0323 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.4332 0.3919 0.3989 -0.0083 -0.0198 -0.0354 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.3820 0.3209 0.3367 -0.0042 -0.0250 -0.0344 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.3185 0.2866 0.2903 -0.0115 -0.0152 -0.0391 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.2606 0.2325 0.2239 -0.0141 -0.0167 -0.0236 22  LEU A N   
171  C CA  . LEU A 21  ? 0.2575 0.2349 0.2235 -0.0148 -0.0163 -0.0233 22  LEU A CA  
172  C C   . LEU A 21  ? 0.2943 0.2583 0.2490 -0.0131 -0.0218 -0.0218 22  LEU A C   
173  O O   . LEU A 21  ? 0.2627 0.2308 0.2208 -0.0108 -0.0261 -0.0248 22  LEU A O   
174  C CB  . LEU A 21  ? 0.2515 0.2334 0.2175 -0.0194 -0.0090 -0.0194 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.2801 0.2736 0.2533 -0.0207 -0.0048 -0.0201 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.2772 0.2718 0.2481 -0.0226 0.0000  -0.0156 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.3119 0.3145 0.2932 -0.0208 -0.0044 -0.0251 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.2716 0.2194 0.2117 -0.0151 -0.0213 -0.0178 23  ASN A N   
179  C CA  . ASN A 22  ? 0.2939 0.2249 0.2178 -0.0143 -0.0265 -0.0158 23  ASN A CA  
180  C C   . ASN A 22  ? 0.3498 0.2740 0.2712 -0.0055 -0.0381 -0.0186 23  ASN A C   
181  O O   . ASN A 22  ? 0.3658 0.2857 0.2807 -0.0021 -0.0454 -0.0193 23  ASN A O   
182  C CB  . ASN A 22  ? 0.3314 0.2447 0.2377 -0.0204 -0.0216 -0.0117 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.4253 0.3213 0.3118 -0.0221 -0.0244 -0.0092 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.3828 0.2850 0.2715 -0.0216 -0.0261 -0.0101 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4435 0.3163 0.3087 -0.0253 -0.0242 -0.0063 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.3168 0.2411 0.2440 -0.0010 -0.0403 -0.0212 24  ARG A N   
187  C CA  . ARG A 23  ? 0.3342 0.2537 0.2626 0.0097  -0.0517 -0.0254 24  ARG A CA  
188  C C   . ARG A 23  ? 0.3717 0.3149 0.3202 0.0139  -0.0560 -0.0328 24  ARG A C   
189  O O   . ARG A 23  ? 0.3717 0.3133 0.3190 0.0219  -0.0671 -0.0360 24  ARG A O   
190  C CB  . ARG A 23  ? 0.3184 0.2353 0.2521 0.0129  -0.0511 -0.0282 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.4223 0.3117 0.3340 0.0094  -0.0486 -0.0227 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.4779 0.3689 0.3972 0.0091  -0.0444 -0.0264 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.5889 0.4512 0.4863 0.0052  -0.0420 -0.0226 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.8306 0.6887 0.7289 0.0018  -0.0366 -0.0253 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.6177 0.4996 0.5374 0.0020  -0.0332 -0.0313 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.7039 0.5332 0.5801 -0.0031 -0.0336 -0.0224 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.3150 0.2795 0.2803 0.0081  -0.0473 -0.0358 25  LEU A N   
198  C CA  . LEU A 24  ? 0.2874 0.2735 0.2702 0.0087  -0.0485 -0.0436 25  LEU A CA  
199  C C   . LEU A 24  ? 0.3339 0.3174 0.3089 0.0068  -0.0517 -0.0422 25  LEU A C   
200  O O   . LEU A 24  ? 0.3365 0.3303 0.3197 0.0116  -0.0599 -0.0494 25  LEU A O   
201  C CB  . LEU A 24  ? 0.2656 0.2676 0.2604 0.0008  -0.0369 -0.0453 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.3042 0.3125 0.3076 0.0011  -0.0327 -0.0484 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.3007 0.3215 0.3102 -0.0074 -0.0218 -0.0489 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.3275 0.3459 0.3457 0.0096  -0.0399 -0.0590 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.2943 0.2655 0.2544 0.0000  -0.0455 -0.0344 26  ARG A N   
206  C CA  . ARG A 25  ? 0.3103 0.2767 0.2605 -0.0027 -0.0477 -0.0333 26  ARG A CA  
207  C C   . ARG A 25  ? 0.3908 0.3444 0.3275 0.0054  -0.0618 -0.0338 26  ARG A C   
208  O O   . ARG A 25  ? 0.3880 0.3498 0.3275 0.0073  -0.0688 -0.0391 26  ARG A O   
209  C CB  . ARG A 25  ? 0.3191 0.2726 0.2551 -0.0103 -0.0386 -0.0258 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.3976 0.3470 0.3238 -0.0140 -0.0394 -0.0260 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.4182 0.3581 0.3343 -0.0214 -0.0292 -0.0209 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.4147 0.3368 0.3142 -0.0226 -0.0281 -0.0157 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.5857 0.4913 0.4650 -0.0272 -0.0266 -0.0130 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.5283 0.4326 0.4009 -0.0297 -0.0278 -0.0149 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.4623 0.3520 0.3270 -0.0305 -0.0231 -0.0093 26  ARG A NH2 
216  N N   A SER A 26  ? 0.3813 0.3138 0.3019 0.0095  -0.0658 -0.0286 27  SER A N   
217  N N   B SER A 26  ? 0.3782 0.3106 0.2987 0.0096  -0.0659 -0.0286 27  SER A N   
218  N N   C SER A 26  ? 0.3758 0.3082 0.2964 0.0096  -0.0659 -0.0286 27  SER A N   
219  C CA  A SER A 26  ? 0.4154 0.3285 0.3170 0.0181  -0.0798 -0.0271 27  SER A CA  
220  C CA  B SER A 26  ? 0.4108 0.3235 0.3119 0.0180  -0.0798 -0.0270 27  SER A CA  
221  C CA  C SER A 26  ? 0.4075 0.3199 0.3086 0.0181  -0.0798 -0.0269 27  SER A CA  
222  C C   A SER A 26  ? 0.4661 0.3963 0.3850 0.0297  -0.0931 -0.0366 27  SER A C   
223  C C   B SER A 26  ? 0.4691 0.3969 0.3865 0.0305  -0.0938 -0.0362 27  SER A C   
224  C C   C SER A 26  ? 0.4663 0.3937 0.3835 0.0306  -0.0938 -0.0361 27  SER A C   
225  O O   A SER A 26  ? 0.4792 0.4069 0.3899 0.0352  -0.1051 -0.0387 27  SER A O   
226  O O   B SER A 26  ? 0.4885 0.4088 0.3943 0.0378  -0.1073 -0.0373 27  SER A O   
227  O O   C SER A 26  ? 0.4845 0.4038 0.3897 0.0380  -0.1073 -0.0370 27  SER A O   
228  C CB  A SER A 26  ? 0.4819 0.3693 0.3663 0.0206  -0.0802 -0.0212 27  SER A CB  
229  C CB  B SER A 26  ? 0.4714 0.3556 0.3513 0.0188  -0.0793 -0.0199 27  SER A CB  
230  C CB  C SER A 26  ? 0.4678 0.3527 0.3490 0.0191  -0.0791 -0.0201 27  SER A CB  
231  O OG  A SER A 26  ? 0.5942 0.4638 0.4592 0.0098  -0.0696 -0.0138 27  SER A OG  
232  O OG  B SER A 26  ? 0.5417 0.4307 0.4355 0.0247  -0.0798 -0.0232 27  SER A OG  
233  O OG  C SER A 26  ? 0.5867 0.4464 0.4444 0.0279  -0.0927 -0.0174 27  SER A OG  
234  N N   . ARG A 27  ? 0.4035 0.3533 0.3474 0.0329  -0.0906 -0.0436 28  ARG A N   
235  C CA  . ARG A 27  ? 0.4101 0.3803 0.3760 0.0441  -0.1017 -0.0554 28  ARG A CA  
236  C C   . ARG A 27  ? 0.4275 0.4295 0.4168 0.0384  -0.0981 -0.0656 28  ARG A C   
237  O O   . ARG A 27  ? 0.4231 0.4482 0.4351 0.0455  -0.1053 -0.0781 28  ARG A O   
238  C CB  . ARG A 27  ? 0.4437 0.4170 0.4230 0.0496  -0.0997 -0.0591 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.5801 0.5193 0.5346 0.0543  -0.1029 -0.0499 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.6585 0.6003 0.6256 0.0575  -0.0986 -0.0539 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.8817 0.8377 0.8689 0.0720  -0.1102 -0.0657 28  ARG A NE  
242  C CZ  . ARG A 27  ? 1.0896 1.0681 1.1030 0.0732  -0.1051 -0.0762 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 0.9682 0.9612 1.0018 0.0872  -0.1158 -0.0887 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 0.9088 0.8960 0.9283 0.0608  -0.0894 -0.0751 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.3558 0.3583 0.3397 0.0256  -0.0867 -0.0613 29  ASP A N   
246  C CA  . ASP A 28  ? 0.3514 0.3774 0.3519 0.0171  -0.0803 -0.0694 29  ASP A CA  
247  C C   . ASP A 28  ? 0.3894 0.4394 0.4162 0.0141  -0.0717 -0.0788 29  ASP A C   
248  O O   . ASP A 28  ? 0.3882 0.4624 0.4349 0.0116  -0.0715 -0.0913 29  ASP A O   
249  C CB  . ASP A 28  ? 0.3862 0.4227 0.3891 0.0218  -0.0936 -0.0777 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.4819 0.5342 0.4931 0.0098  -0.0853 -0.0838 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.4660 0.5084 0.4682 -0.0010 -0.0715 -0.0766 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.5378 0.6123 0.5648 0.0115  -0.0927 -0.0967 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.3169 0.3601 0.3429 0.0132  -0.0643 -0.0738 30  ILE A N   
254  C CA  . ILE A 29  ? 0.2929 0.3554 0.3392 0.0096  -0.0556 -0.0821 30  ILE A CA  
255  C C   . ILE A 29  ? 0.3314 0.3944 0.3747 -0.0039 -0.0400 -0.0780 30  ILE A C   
256  O O   . ILE A 29  ? 0.3037 0.3492 0.3307 -0.0073 -0.0346 -0.0663 30  ILE A O   
257  C CB  . ILE A 29  ? 0.3263 0.3829 0.3743 0.0169  -0.0573 -0.0813 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.3497 0.4046 0.4018 0.0324  -0.0737 -0.0869 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.2985 0.3731 0.3636 0.0106  -0.0459 -0.0891 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.3914 0.4292 0.4365 0.0397  -0.0757 -0.0829 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.2903 0.3729 0.3491 -0.0116 -0.0328 -0.0883 31  LEU A N   
262  N N   B LEU A 30  ? 0.3018 0.3846 0.3607 -0.0116 -0.0328 -0.0884 31  LEU A N   
263  C CA  A LEU A 30  ? 0.2808 0.3622 0.3355 -0.0245 -0.0178 -0.0858 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.2990 0.3808 0.3541 -0.0246 -0.0178 -0.0862 31  LEU A CA  
265  C C   A LEU A 30  ? 0.3206 0.3848 0.3576 -0.0296 -0.0143 -0.0758 31  LEU A C   
266  C C   B LEU A 30  ? 0.3305 0.3948 0.3676 -0.0296 -0.0143 -0.0759 31  LEU A C   
267  O O   A LEU A 30  ? 0.3042 0.3597 0.3327 -0.0373 -0.0034 -0.0701 31  LEU A O   
268  O O   B LEU A 30  ? 0.3156 0.3713 0.3442 -0.0373 -0.0034 -0.0701 31  LEU A O   
269  C CB  A LEU A 30  ? 0.2817 0.3583 0.3328 -0.0268 -0.0096 -0.0811 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.3050 0.3831 0.3574 -0.0271 -0.0094 -0.0821 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.3341 0.4288 0.4029 -0.0261 -0.0075 -0.0929 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.3724 0.4701 0.4413 -0.0332 -0.0016 -0.0950 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.3192 0.4095 0.3804 -0.0343 0.0047  -0.0892 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.3767 0.4822 0.4564 -0.0250 -0.0063 -0.1003 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.3540 0.4730 0.4435 -0.0304 -0.0059 -0.1095 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.4027 0.4928 0.4602 -0.0454 0.0130  -0.0905 31  LEU A CD2 
277  N N   . THR A 31  ? 0.2875 0.3466 0.3186 -0.0253 -0.0235 -0.0746 32  THR A N   
278  C CA  . THR A 31  ? 0.2962 0.3410 0.3122 -0.0306 -0.0198 -0.0678 32  THR A CA  
279  C C   . THR A 31  ? 0.3569 0.4130 0.3815 -0.0414 -0.0109 -0.0769 32  THR A C   
280  O O   . THR A 31  ? 0.3536 0.4305 0.3955 -0.0428 -0.0130 -0.0899 32  THR A O   
281  C CB  . THR A 31  ? 0.3784 0.4156 0.3845 -0.0247 -0.0315 -0.0660 32  THR A CB  
282  O OG1 . THR A 31  ? 0.3898 0.4447 0.4095 -0.0200 -0.0420 -0.0778 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.3614 0.3810 0.3533 -0.0170 -0.0372 -0.0560 32  THR A CG2 
284  N N   . ASP A 32  ? 0.3165 0.3591 0.3299 -0.0493 -0.0001 -0.0710 33  ASP A N   
285  C CA  . ASP A 32  ? 0.3158 0.3627 0.3329 -0.0611 0.0110  -0.0782 33  ASP A CA  
286  C C   . ASP A 32  ? 0.3480 0.3820 0.3538 -0.0670 0.0152  -0.0764 33  ASP A C   
287  O O   . ASP A 32  ? 0.3575 0.3880 0.3616 -0.0778 0.0262  -0.0806 33  ASP A O   
288  C CB  . ASP A 32  ? 0.3343 0.3741 0.3469 -0.0662 0.0226  -0.0740 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.4492 0.4685 0.4458 -0.0613 0.0241  -0.0592 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.3992 0.4086 0.3882 -0.0562 0.0193  -0.0528 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.5635 0.5779 0.5555 -0.0625 0.0299  -0.0549 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.2940 0.3190 0.2905 -0.0610 0.0076  -0.0707 34  VAL A N   
293  C CA  . VAL A 33  ? 0.2927 0.3060 0.2786 -0.0666 0.0116  -0.0704 34  VAL A CA  
294  C C   . VAL A 33  ? 0.3398 0.3515 0.3188 -0.0608 0.0002  -0.0695 34  VAL A C   
295  O O   . VAL A 33  ? 0.3402 0.3500 0.3160 -0.0519 -0.0087 -0.0641 34  VAL A O   
296  C CB  . VAL A 33  ? 0.3422 0.3330 0.3146 -0.0682 0.0226  -0.0598 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.3267 0.3075 0.2910 -0.0589 0.0181  -0.0489 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.3504 0.3291 0.3144 -0.0762 0.0304  -0.0625 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.3062 0.3162 0.2801 -0.0670 0.0010  -0.0751 35  VAL A N   
300  N N   B VAL A 34  ? 0.3082 0.3186 0.2823 -0.0669 0.0008  -0.0752 35  VAL A N   
301  C CA  A VAL A 34  ? 0.3053 0.3097 0.2670 -0.0641 -0.0080 -0.0742 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.3092 0.3134 0.2708 -0.0636 -0.0083 -0.0738 35  VAL A CA  
303  C C   A VAL A 34  ? 0.3605 0.3450 0.3079 -0.0693 0.0026  -0.0690 35  VAL A C   
304  C C   B VAL A 34  ? 0.3647 0.3497 0.3119 -0.0693 0.0019  -0.0694 35  VAL A C   
305  O O   A VAL A 34  ? 0.3613 0.3422 0.3101 -0.0777 0.0133  -0.0730 35  VAL A O   
306  O O   B VAL A 34  ? 0.3677 0.3500 0.3165 -0.0780 0.0121  -0.0741 35  VAL A O   
307  C CB  A VAL A 34  ? 0.3555 0.3774 0.3237 -0.0667 -0.0173 -0.0873 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.3616 0.3830 0.3286 -0.0628 -0.0212 -0.0851 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.3686 0.3809 0.3185 -0.0645 -0.0266 -0.0857 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.3672 0.3986 0.3411 -0.0746 -0.0148 -0.0973 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.3458 0.3898 0.3318 -0.0598 -0.0281 -0.0944 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.3716 0.3817 0.3197 -0.0572 -0.0326 -0.0805 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.3183 0.2891 0.2519 -0.0647 0.0005  -0.0608 36  ILE A N   
314  C CA  . ILE A 35  ? 0.3206 0.2746 0.2420 -0.0686 0.0098  -0.0576 36  ILE A CA  
315  C C   . ILE A 35  ? 0.3943 0.3459 0.3023 -0.0718 0.0033  -0.0624 36  ILE A C   
316  O O   . ILE A 35  ? 0.3894 0.3400 0.2878 -0.0669 -0.0076 -0.0599 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3485 0.2912 0.2647 -0.0631 0.0136  -0.0476 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.3332 0.2798 0.2612 -0.0588 0.0170  -0.0427 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.3730 0.3015 0.2803 -0.0665 0.0235  -0.0467 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.3370 0.2819 0.2714 -0.0634 0.0267  -0.0450 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.3569 0.3054 0.2618 -0.0803 0.0101  -0.0693 37  VAL A N   
322  C CA  . VAL A 36  ? 0.3698 0.3164 0.2608 -0.0851 0.0048  -0.0754 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4393 0.3668 0.3145 -0.0881 0.0142  -0.0717 37  VAL A C   
324  O O   . VAL A 36  ? 0.4210 0.3398 0.2998 -0.0913 0.0275  -0.0718 37  VAL A O   
325  C CB  . VAL A 36  ? 0.4228 0.3813 0.3214 -0.0941 0.0058  -0.0882 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4400 0.3972 0.3228 -0.0994 -0.0004 -0.0950 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.4178 0.3992 0.3351 -0.0916 -0.0029 -0.0942 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.4096 0.3292 0.2661 -0.0870 0.0077  -0.0690 38  VAL A N   
329  C CA  . VAL A 37  ? 0.4222 0.3251 0.2627 -0.0908 0.0167  -0.0669 38  VAL A CA  
330  C C   . VAL A 37  ? 0.4931 0.3914 0.3120 -0.0968 0.0099  -0.0724 38  VAL A C   
331  O O   . VAL A 37  ? 0.4723 0.3677 0.2759 -0.0934 -0.0025 -0.0690 38  VAL A O   
332  C CB  . VAL A 37  ? 0.4766 0.3723 0.3134 -0.0850 0.0179  -0.0575 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.4858 0.3684 0.3127 -0.0899 0.0309  -0.0579 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.4530 0.3572 0.3111 -0.0779 0.0198  -0.0524 38  VAL A CG2 
335  N N   A SER A 38  ? 0.4911 0.3835 0.3033 -0.1058 0.0190  -0.0799 39  SER A N   
336  N N   B SER A 38  ? 0.4481 0.3493 0.2694 -0.1047 0.0151  -0.0819 39  SER A N   
337  C CA  A SER A 38  ? 0.5279 0.4148 0.3163 -0.1128 0.0132  -0.0858 39  SER A CA  
338  C CA  B SER A 38  ? 0.4629 0.3644 0.2687 -0.1124 0.0098  -0.0908 39  SER A CA  
339  C C   A SER A 38  ? 0.5893 0.4874 0.3719 -0.1083 -0.0076 -0.0871 39  SER A C   
340  C C   B SER A 38  ? 0.4983 0.4150 0.3040 -0.1076 -0.0100 -0.0933 39  SER A C   
341  O O   A SER A 38  ? 0.6003 0.4882 0.3578 -0.1071 -0.0177 -0.0838 39  SER A O   
342  O O   B SER A 38  ? 0.4659 0.4005 0.2934 -0.1060 -0.0132 -0.0982 39  SER A O   
343  C CB  A SER A 38  ? 0.6139 0.4821 0.3784 -0.1161 0.0192  -0.0817 39  SER A CB  
344  C CB  B SER A 38  ? 0.5335 0.4166 0.3131 -0.1181 0.0154  -0.0901 39  SER A CB  
345  O OG  A SER A 38  ? 0.7565 0.6167 0.5259 -0.1208 0.0375  -0.0845 39  SER A OG  
346  O OG  B SER A 38  ? 0.6145 0.4888 0.4008 -0.1224 0.0338  -0.0922 39  SER A OG  
347  N N   A ARG A 39  ? 0.5321 0.4504 0.3379 -0.1053 -0.0136 -0.0920 40  ARG A N   
348  N N   B ARG A 39  ? 0.4791 0.3883 0.2607 -0.1047 -0.0233 -0.0903 40  ARG A N   
349  C CA  A ARG A 39  ? 0.5363 0.4717 0.3461 -0.0992 -0.0331 -0.0960 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.4849 0.4085 0.2675 -0.0973 -0.0442 -0.0930 40  ARG A CA  
351  C C   A ARG A 39  ? 0.5768 0.5074 0.3798 -0.0867 -0.0462 -0.0856 40  ARG A C   
352  C C   B ARG A 39  ? 0.5427 0.4733 0.3423 -0.0850 -0.0507 -0.0854 40  ARG A C   
353  O O   A ARG A 39  ? 0.5934 0.5279 0.3863 -0.0800 -0.0647 -0.0869 40  ARG A O   
354  O O   B ARG A 39  ? 0.5300 0.4828 0.3530 -0.0804 -0.0580 -0.0915 40  ARG A O   
355  C CB  A ARG A 39  ? 0.5677 0.5066 0.3604 -0.1050 -0.0434 -0.1059 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.5110 0.4213 0.2584 -0.0973 -0.0582 -0.0924 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.6932 0.6435 0.4980 -0.1170 -0.0341 -0.1195 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.6124 0.5242 0.3476 -0.1093 -0.0560 -0.1038 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.7686 0.7322 0.5638 -0.1201 -0.0498 -0.1311 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.6157 0.5158 0.3144 -0.1090 -0.0725 -0.1040 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.8506 0.8205 0.6505 -0.1344 -0.0394 -0.1448 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.6483 0.5484 0.3334 -0.1219 -0.0684 -0.1151 40  ARG A NE  
363  C CZ  A ARG A 39  ? 1.0158 0.9688 0.7939 -0.1447 -0.0302 -0.1477 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.8240 0.7455 0.5166 -0.1245 -0.0795 -0.1283 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.8549 0.7847 0.6054 -0.1429 -0.0292 -0.1380 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.6564 0.6034 0.3727 -0.1146 -0.0954 -0.1330 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.8296 0.7882 0.6133 -0.1578 -0.0206 -0.1612 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.7213 0.6406 0.3995 -0.1374 -0.0743 -0.1385 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.4853 0.4067 0.2934 -0.0831 -0.0369 -0.0759 41  GLU A N   
370  N N   B GLU A 40  ? 0.4832 0.3966 0.2737 -0.0814 -0.0451 -0.0739 41  GLU A N   
371  C CA  A GLU A 40  ? 0.4787 0.3949 0.2839 -0.0726 -0.0456 -0.0666 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.4661 0.3816 0.2676 -0.0708 -0.0502 -0.0662 41  GLU A CA  
373  C C   A GLU A 40  ? 0.4725 0.4041 0.3084 -0.0686 -0.0399 -0.0662 41  GLU A C   
374  C C   B GLU A 40  ? 0.4648 0.3985 0.2996 -0.0690 -0.0425 -0.0682 41  GLU A C   
375  O O   A GLU A 40  ? 0.4292 0.3611 0.2769 -0.0739 -0.0247 -0.0665 41  GLU A O   
376  O O   B GLU A 40  ? 0.4219 0.3580 0.2679 -0.0761 -0.0282 -0.0713 41  GLU A O   
377  C CB  A GLU A 40  ? 0.5119 0.4032 0.2937 -0.0745 -0.0383 -0.0570 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.4957 0.3878 0.2780 -0.0704 -0.0438 -0.0552 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.7037 0.5765 0.4500 -0.0795 -0.0439 -0.0570 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.7051 0.5750 0.4511 -0.0768 -0.0448 -0.0536 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.1574 1.0110 0.8768 -0.0730 -0.0567 -0.0485 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.1820 1.0329 0.8983 -0.0707 -0.0598 -0.0467 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.2055 1.0359 0.8994 -0.0790 -0.0487 -0.0428 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.2025 1.0618 0.9237 -0.0600 -0.0774 -0.0473 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.1583 1.0189 0.8815 -0.0622 -0.0740 -0.0483 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.2104 1.0367 0.8973 -0.0770 -0.0537 -0.0414 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.4207 0.3647 0.2688 -0.0591 -0.0522 -0.0664 42  GLN A N   
388  C CA  . GLN A 41  ? 0.3996 0.3599 0.2757 -0.0567 -0.0469 -0.0679 42  GLN A CA  
389  C C   . GLN A 41  ? 0.4390 0.3922 0.3162 -0.0487 -0.0477 -0.0584 42  GLN A C   
390  O O   . GLN A 41  ? 0.4523 0.3963 0.3156 -0.0414 -0.0595 -0.0541 42  GLN A O   
391  C CB  . GLN A 41  ? 0.4162 0.4017 0.3111 -0.0538 -0.0583 -0.0794 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.5918 0.5882 0.4900 -0.0639 -0.0556 -0.0913 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.8409 0.8670 0.7634 -0.0634 -0.0633 -0.1053 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.7347 0.7756 0.6750 -0.0553 -0.0699 -0.1071 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.8896 0.9264 0.8146 -0.0732 -0.0618 -0.1171 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.3608 0.3163 0.2525 -0.0502 -0.0353 -0.0551 43  PHE A N   
397  C CA  . PHE A 42  ? 0.3564 0.3071 0.2507 -0.0439 -0.0348 -0.0471 43  PHE A CA  
398  C C   . PHE A 42  ? 0.3966 0.3642 0.3150 -0.0422 -0.0313 -0.0500 43  PHE A C   
399  O O   . PHE A 42  ? 0.3906 0.3616 0.3180 -0.0481 -0.0198 -0.0515 43  PHE A O   
400  C CB  . PHE A 42  ? 0.3793 0.3143 0.2638 -0.0477 -0.0225 -0.0396 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.4175 0.3349 0.2771 -0.0520 -0.0224 -0.0377 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.4424 0.3568 0.2956 -0.0597 -0.0158 -0.0423 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.4558 0.3575 0.2962 -0.0495 -0.0274 -0.0317 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.4861 0.3841 0.3147 -0.0649 -0.0147 -0.0415 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.5053 0.3885 0.3191 -0.0554 -0.0259 -0.0302 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.4813 0.3637 0.2896 -0.0631 -0.0195 -0.0353 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.3414 0.3172 0.2685 -0.0342 -0.0405 -0.0507 44  ARG A N   
408  C CA  . ARG A 43  ? 0.3168 0.3088 0.2656 -0.0332 -0.0367 -0.0543 44  ARG A CA  
409  C C   . ARG A 43  ? 0.3623 0.3453 0.3098 -0.0319 -0.0290 -0.0454 44  ARG A C   
410  O O   . ARG A 43  ? 0.3559 0.3251 0.2905 -0.0283 -0.0318 -0.0385 44  ARG A O   
411  C CB  . ARG A 43  ? 0.3291 0.3367 0.2905 -0.0249 -0.0498 -0.0617 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.4346 0.4574 0.4017 -0.0253 -0.0593 -0.0731 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.5405 0.5894 0.5326 -0.0201 -0.0664 -0.0853 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.6710 0.7299 0.6798 -0.0261 -0.0528 -0.0874 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.8238 0.8973 0.8462 -0.0367 -0.0425 -0.0965 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.7218 0.8062 0.7477 -0.0425 -0.0446 -0.1064 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.5969 0.6737 0.6280 -0.0422 -0.0300 -0.0964 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.3097 0.2992 0.2687 -0.0357 -0.0189 -0.0457 45  ALA A N   
419  C CA  . ALA A 44  ? 0.3121 0.2953 0.2703 -0.0342 -0.0127 -0.0380 45  ALA A CA  
420  C C   . ALA A 44  ? 0.3163 0.3100 0.2874 -0.0364 -0.0063 -0.0405 45  ALA A C   
421  O O   . ALA A 44  ? 0.2980 0.3032 0.2788 -0.0405 -0.0050 -0.0486 45  ALA A O   
422  C CB  . ALA A 44  ? 0.3357 0.3053 0.2831 -0.0376 -0.0045 -0.0320 45  ALA A CB  
423  N N   . HIS A 45  ? 0.2708 0.2605 0.2409 -0.0348 -0.0020 -0.0343 46  HIS A N   
424  C CA  . HIS A 45  ? 0.2602 0.2551 0.2366 -0.0374 0.0048  -0.0346 46  HIS A CA  
425  C C   . HIS A 45  ? 0.3191 0.3019 0.2872 -0.0405 0.0135  -0.0291 46  HIS A C   
426  O O   . HIS A 45  ? 0.3111 0.2856 0.2729 -0.0373 0.0140  -0.0230 46  HIS A O   
427  C CB  . HIS A 45  ? 0.2527 0.2504 0.2314 -0.0328 0.0025  -0.0316 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.2935 0.2987 0.2789 -0.0278 -0.0064 -0.0364 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.3212 0.3176 0.2990 -0.0227 -0.0133 -0.0329 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.2974 0.3166 0.2954 -0.0270 -0.0092 -0.0452 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.3073 0.3101 0.2919 -0.0175 -0.0212 -0.0384 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.2992 0.3179 0.2982 -0.0192 -0.0193 -0.0466 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.2957 0.2771 0.2638 -0.0468 0.0207  -0.0321 47  LYS A N   
434  C CA  . LYS A 46  ? 0.2966 0.2627 0.2550 -0.0487 0.0288  -0.0269 47  LYS A CA  
435  C C   . LYS A 46  ? 0.3315 0.2922 0.2853 -0.0424 0.0286  -0.0186 47  LYS A C   
436  O O   . LYS A 46  ? 0.3107 0.2617 0.2593 -0.0386 0.0300  -0.0140 47  LYS A O   
437  C CB  . LYS A 46  ? 0.3270 0.2895 0.2829 -0.0573 0.0373  -0.0310 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.3163 0.2826 0.2760 -0.0650 0.0395  -0.0401 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.3248 0.2881 0.2823 -0.0760 0.0498  -0.0458 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.3721 0.3458 0.3376 -0.0846 0.0511  -0.0578 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.3964 0.3679 0.3601 -0.0978 0.0631  -0.0652 47  LYS A NZ  
442  N N   . THR A 47  ? 0.2855 0.2542 0.2425 -0.0409 0.0264  -0.0180 48  THR A N   
443  C CA  . THR A 47  ? 0.2828 0.2482 0.2352 -0.0354 0.0255  -0.0111 48  THR A CA  
444  C C   . THR A 47  ? 0.2966 0.2642 0.2517 -0.0294 0.0208  -0.0084 48  THR A C   
445  O O   . THR A 47  ? 0.2791 0.2423 0.2312 -0.0248 0.0213  -0.0039 48  THR A O   
446  C CB  . THR A 47  ? 0.3703 0.3435 0.3240 -0.0364 0.0250  -0.0120 48  THR A CB  
447  O OG1 . THR A 47  ? 0.3672 0.3533 0.3314 -0.0360 0.0199  -0.0175 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.3983 0.3659 0.3450 -0.0438 0.0325  -0.0139 48  THR A CG2 
449  N N   . VAL A 48  ? 0.2563 0.2299 0.2163 -0.0296 0.0164  -0.0117 49  VAL A N   
450  C CA  . VAL A 48  ? 0.2624 0.2356 0.2221 -0.0266 0.0138  -0.0099 49  VAL A CA  
451  C C   . VAL A 48  ? 0.2984 0.2633 0.2544 -0.0267 0.0178  -0.0092 49  VAL A C   
452  O O   . VAL A 48  ? 0.2718 0.2366 0.2287 -0.0237 0.0191  -0.0075 49  VAL A O   
453  C CB  . VAL A 48  ? 0.2979 0.2735 0.2582 -0.0271 0.0082  -0.0129 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.2999 0.2705 0.2553 -0.0269 0.0079  -0.0114 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.2917 0.2750 0.2570 -0.0258 0.0048  -0.0144 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.2601 0.2197 0.2133 -0.0305 0.0199  -0.0119 50  LEU A N   
457  C CA  . LEU A 49  ? 0.2706 0.2210 0.2197 -0.0313 0.0247  -0.0123 50  LEU A CA  
458  C C   . LEU A 49  ? 0.3086 0.2528 0.2573 -0.0266 0.0290  -0.0087 50  LEU A C   
459  O O   . LEU A 49  ? 0.2903 0.2322 0.2403 -0.0230 0.0312  -0.0085 50  LEU A O   
460  C CB  . LEU A 49  ? 0.2773 0.2234 0.2233 -0.0371 0.0267  -0.0168 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.3118 0.2636 0.2573 -0.0402 0.0206  -0.0215 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.3176 0.2676 0.2616 -0.0464 0.0229  -0.0275 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.3371 0.2849 0.2759 -0.0394 0.0181  -0.0206 50  LEU A CD2 
464  N N   . MET A 50  ? 0.2759 0.2172 0.2222 -0.0262 0.0300  -0.0062 51  MET A N   
465  C CA  . MET A 50  ? 0.2876 0.2191 0.2293 -0.0202 0.0322  -0.0015 51  MET A CA  
466  C C   . MET A 50  ? 0.3212 0.2623 0.2688 -0.0124 0.0275  0.0009  51  MET A C   
467  O O   . MET A 50  ? 0.3261 0.2632 0.2749 -0.0053 0.0280  0.0021  51  MET A O   
468  C CB  . MET A 50  ? 0.3130 0.2366 0.2459 -0.0229 0.0343  0.0012  51  MET A CB  
469  C CG  . MET A 50  ? 0.3501 0.2645 0.2778 -0.0321 0.0407  -0.0028 51  MET A CG  
470  S SD  . MET A 50  ? 0.4103 0.3216 0.3296 -0.0384 0.0439  -0.0021 51  MET A SD  
471  C CE  . MET A 50  ? 0.3874 0.2719 0.2878 -0.0330 0.0475  0.0062  51  MET A CE  
472  N N   . ALA A 51  ? 0.2878 0.2422 0.2404 -0.0136 0.0231  0.0002  52  ALA A N   
473  C CA  . ALA A 51  ? 0.2854 0.2512 0.2443 -0.0083 0.0190  0.0008  52  ALA A CA  
474  C C   . ALA A 51  ? 0.3103 0.2816 0.2770 -0.0069 0.0205  -0.0029 52  ALA A C   
475  O O   . ALA A 51  ? 0.3238 0.3050 0.2980 -0.0016 0.0185  -0.0041 52  ALA A O   
476  C CB  . ALA A 51  ? 0.2872 0.2635 0.2485 -0.0118 0.0154  -0.0002 52  ALA A CB  
477  N N   . CYS A 52  ? 0.2706 0.2366 0.2353 -0.0122 0.0241  -0.0059 53  CYS A N   
478  C CA  . CYS A 52  ? 0.2703 0.2393 0.2388 -0.0140 0.0274  -0.0103 53  CYS A CA  
479  C C   . CYS A 52  ? 0.3214 0.2828 0.2903 -0.0118 0.0329  -0.0127 53  CYS A C   
480  O O   . CYS A 52  ? 0.3153 0.2816 0.2895 -0.0125 0.0368  -0.0177 53  CYS A O   
481  C CB  . CYS A 52  ? 0.2758 0.2422 0.2377 -0.0219 0.0270  -0.0120 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.3156 0.2892 0.2776 -0.0238 0.0213  -0.0108 53  CYS A SG  
483  N N   . SER A 53  ? 0.2910 0.2395 0.2534 -0.0112 0.0346  -0.0105 54  SER A N   
484  C CA  . SER A 53  ? 0.2725 0.2105 0.2332 -0.0108 0.0407  -0.0136 54  SER A CA  
485  C C   . SER A 53  ? 0.3477 0.2721 0.3048 -0.0040 0.0419  -0.0103 54  SER A C   
486  O O   . SER A 53  ? 0.3247 0.2406 0.2734 -0.0063 0.0410  -0.0062 54  SER A O   
487  C CB  . SER A 53  ? 0.2987 0.2301 0.2507 -0.0206 0.0429  -0.0160 54  SER A CB  
488  O OG  . SER A 53  ? 0.3485 0.2661 0.2950 -0.0225 0.0484  -0.0182 54  SER A OG  
489  N N   . GLY A 54  ? 0.3308 0.2518 0.2933 0.0040  0.0446  -0.0127 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3429 0.2453 0.2990 0.0121  0.0456  -0.0093 55  GLY A CA  
491  C C   . GLY A 54  ? 0.3904 0.2730 0.3337 0.0039  0.0521  -0.0095 55  GLY A C   
492  O O   . GLY A 54  ? 0.3994 0.2634 0.3307 0.0052  0.0531  -0.0048 55  GLY A O   
493  N N   . LEU A 55  ? 0.3593 0.2449 0.3031 -0.0057 0.0567  -0.0156 56  LEU A N   
494  C CA  . LEU A 55  ? 0.3665 0.2370 0.2996 -0.0151 0.0626  -0.0179 56  LEU A CA  
495  C C   . LEU A 55  ? 0.3878 0.2588 0.3144 -0.0225 0.0600  -0.0148 56  LEU A C   
496  O O   . LEU A 55  ? 0.3853 0.2396 0.3021 -0.0256 0.0643  -0.0135 56  LEU A O   
497  C CB  . LEU A 55  ? 0.3650 0.2402 0.2986 -0.0235 0.0664  -0.0254 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.4300 0.2909 0.3537 -0.0331 0.0725  -0.0298 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.4563 0.2954 0.3760 -0.0283 0.0804  -0.0314 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.4190 0.2875 0.3402 -0.0424 0.0732  -0.0364 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.3278 0.2169 0.2595 -0.0254 0.0538  -0.0143 57  PHE A N   
502  C CA  . PHE A 56  ? 0.3204 0.2135 0.2493 -0.0317 0.0514  -0.0133 57  PHE A CA  
503  C C   . PHE A 56  ? 0.3802 0.2655 0.3039 -0.0275 0.0511  -0.0071 57  PHE A C   
504  O O   . PHE A 56  ? 0.3646 0.2432 0.2813 -0.0344 0.0544  -0.0074 57  PHE A O   
505  C CB  . PHE A 56  ? 0.3192 0.2309 0.2545 -0.0343 0.0446  -0.0147 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.3278 0.2424 0.2618 -0.0405 0.0444  -0.0206 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.3542 0.2643 0.2841 -0.0485 0.0472  -0.0259 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.3457 0.2668 0.2806 -0.0395 0.0412  -0.0212 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.3688 0.2818 0.2955 -0.0538 0.0454  -0.0315 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.3805 0.3013 0.3093 -0.0454 0.0399  -0.0258 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.3567 0.2738 0.2814 -0.0518 0.0414  -0.0308 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.3514 0.2373 0.2773 -0.0168 0.0476  -0.0023 58  TYR A N   
513  C CA  . TYR A 57  ? 0.3701 0.2452 0.2866 -0.0117 0.0462  0.0043  58  TYR A CA  
514  C C   . TYR A 57  ? 0.4394 0.2863 0.3400 -0.0139 0.0537  0.0059  58  TYR A C   
515  O O   . TYR A 57  ? 0.4242 0.2596 0.3120 -0.0197 0.0566  0.0087  58  TYR A O   
516  C CB  . TYR A 57  ? 0.3889 0.2703 0.3113 0.0016  0.0399  0.0077  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.4400 0.3076 0.3493 0.0088  0.0367  0.0151  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.4619 0.3342 0.3648 0.0050  0.0338  0.0184  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.5050 0.3528 0.4063 0.0198  0.0364  0.0186  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.4978 0.3551 0.3842 0.0108  0.0307  0.0257  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.5554 0.3866 0.4399 0.0274  0.0320  0.0264  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6394 0.4752 0.5153 0.0223  0.0292  0.0302  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.7335 0.5505 0.5890 0.0293  0.0248  0.0382  58  TYR A OH  
524  N N   A SER A 58  ? 0.4089 0.2437 0.3095 -0.0105 0.0579  0.0034  59  SER A N   
525  N N   B SER A 58  ? 0.4132 0.2480 0.3138 -0.0105 0.0579  0.0034  59  SER A N   
526  C CA  A SER A 58  ? 0.4388 0.2434 0.3236 -0.0126 0.0659  0.0041  59  SER A CA  
527  C CA  B SER A 58  ? 0.4449 0.2497 0.3300 -0.0125 0.0658  0.0040  59  SER A CA  
528  C C   A SER A 58  ? 0.5002 0.3007 0.3788 -0.0294 0.0735  -0.0010 59  SER A C   
529  C C   B SER A 58  ? 0.5013 0.3022 0.3800 -0.0293 0.0734  -0.0009 59  SER A C   
530  O O   A SER A 58  ? 0.5313 0.3098 0.3932 -0.0353 0.0797  0.0013  59  SER A O   
531  O O   B SER A 58  ? 0.5292 0.3085 0.3913 -0.0350 0.0793  0.0015  59  SER A O   
532  C CB  A SER A 58  ? 0.4730 0.2692 0.3625 -0.0055 0.0689  0.0003  59  SER A CB  
533  C CB  B SER A 58  ? 0.4872 0.2847 0.3776 -0.0063 0.0691  -0.0003 59  SER A CB  
534  O OG  A SER A 58  ? 0.4898 0.2876 0.3849 0.0111  0.0623  0.0041  59  SER A OG  
535  O OG  B SER A 58  ? 0.5838 0.3492 0.4581 -0.0076 0.0771  0.0002  59  SER A OG  
536  N N   . ILE A 59  ? 0.4415 0.2632 0.3325 -0.0374 0.0728  -0.0084 60  ILE A N   
537  C CA  . ILE A 59  ? 0.4281 0.2533 0.3181 -0.0526 0.0779  -0.0158 60  ILE A CA  
538  C C   . ILE A 59  ? 0.4605 0.2907 0.3473 -0.0592 0.0781  -0.0148 60  ILE A C   
539  O O   . ILE A 59  ? 0.4837 0.2999 0.3600 -0.0702 0.0868  -0.0179 60  ILE A O   
540  C CB  . ILE A 59  ? 0.4308 0.2793 0.3341 -0.0567 0.0736  -0.0233 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.4370 0.2780 0.3402 -0.0547 0.0768  -0.0269 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.4073 0.2667 0.3133 -0.0704 0.0753  -0.0319 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.4489 0.3101 0.3605 -0.0567 0.0711  -0.0319 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.3931 0.2425 0.2883 -0.0540 0.0700  -0.0116 61  PHE A N   
545  C CA  . PHE A 60  ? 0.3976 0.2547 0.2918 -0.0613 0.0709  -0.0128 61  PHE A CA  
546  C C   . PHE A 60  ? 0.4636 0.2999 0.3397 -0.0594 0.0742  -0.0048 61  PHE A C   
547  O O   . PHE A 60  ? 0.4779 0.3175 0.3501 -0.0676 0.0775  -0.0066 61  PHE A O   
548  C CB  . PHE A 60  ? 0.3841 0.2699 0.2944 -0.0588 0.0618  -0.0150 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.3788 0.2807 0.3015 -0.0614 0.0580  -0.0226 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.4155 0.3214 0.3409 -0.0724 0.0622  -0.0321 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.3824 0.2943 0.3122 -0.0536 0.0504  -0.0207 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.4132 0.3332 0.3473 -0.0738 0.0568  -0.0388 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.4129 0.3356 0.3488 -0.0561 0.0463  -0.0267 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.3905 0.3171 0.3280 -0.0653 0.0485  -0.0353 61  PHE A CZ  
555  N N   . THR A 61  ? 0.4414 0.2551 0.3052 -0.0493 0.0739  0.0031  62  THR A N   
556  C CA  . THR A 61  ? 0.4722 0.2591 0.3125 -0.0476 0.0768  0.0113  62  THR A CA  
557  C C   . THR A 61  ? 0.5815 0.3358 0.4024 -0.0569 0.0889  0.0100  62  THR A C   
558  O O   . THR A 61  ? 0.5954 0.3201 0.3910 -0.0589 0.0940  0.0163  62  THR A O   
559  C CB  . THR A 61  ? 0.5585 0.3389 0.3943 -0.0299 0.0675  0.0207  62  THR A CB  
560  O OG1 . THR A 61  ? 0.5199 0.2958 0.3632 -0.0203 0.0660  0.0199  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.4915 0.3009 0.3414 -0.0241 0.0574  0.0219  62  THR A CG2 
562  N N   . ASP A 62  ? 0.5335 0.2913 0.3639 -0.0638 0.0941  0.0015  63  ASP A N   
563  C CA  . ASP A 62  ? 0.5617 0.2901 0.3752 -0.0751 0.1068  -0.0019 63  ASP A CA  
564  C C   . ASP A 62  ? 0.6381 0.3712 0.4475 -0.0942 0.1159  -0.0089 63  ASP A C   
565  O O   . ASP A 62  ? 0.5933 0.3599 0.4236 -0.1007 0.1132  -0.0178 63  ASP A O   
566  C CB  . ASP A 62  ? 0.5664 0.2993 0.3917 -0.0772 0.1093  -0.0101 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.7433 0.4475 0.5519 -0.0914 0.1234  -0.0155 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.8296 0.4976 0.6191 -0.0855 0.1280  -0.0097 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.7421 0.4594 0.5563 -0.1086 0.1301  -0.0261 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.6722 0.3708 0.4540 -0.1032 0.1270  -0.0058 64  GLN A N   
571  C CA  . GLN A 63  ? 0.6956 0.3957 0.4706 -0.1232 0.1382  -0.0133 64  GLN A CA  
572  C C   . GLN A 63  ? 0.7360 0.4617 0.5318 -0.1395 0.1446  -0.0302 64  GLN A C   
573  O O   . GLN A 63  ? 0.7516 0.4997 0.5572 -0.1518 0.1484  -0.0392 64  GLN A O   
574  C CB  . GLN A 63  ? 0.7704 0.4218 0.5069 -0.1314 0.1509  -0.0068 64  GLN A CB  
575  C CG  . GLN A 63  ? 1.0285 0.6604 0.7425 -0.1191 0.1441  0.0081  64  GLN A CG  
576  N N   . LEU A 64  ? 0.6483 0.3719 0.4512 -0.1397 0.1457  -0.0356 65  LEU A N   
577  C CA  . LEU A 64  ? 0.6203 0.3705 0.4431 -0.1541 0.1494  -0.0522 65  LEU A CA  
578  C C   . LEU A 64  ? 0.6334 0.4254 0.4856 -0.1445 0.1345  -0.0562 65  LEU A C   
579  O O   . LEU A 64  ? 0.6413 0.4650 0.5127 -0.1532 0.1329  -0.0686 65  LEU A O   
580  C CB  . LEU A 64  ? 0.6432 0.3706 0.4573 -0.1612 0.1584  -0.0576 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.7569 0.4479 0.5456 -0.1795 0.1769  -0.0614 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.7764 0.4452 0.5580 -0.1836 0.1840  -0.0663 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.8094 0.5231 0.6075 -0.2016 0.1864  -0.0768 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.5429 0.3343 0.3982 -0.1270 0.1240  -0.0470 66  LYS A N   
585  C CA  . LYS A 65  ? 0.4982 0.3226 0.3760 -0.1187 0.1110  -0.0501 66  LYS A CA  
586  C C   . LYS A 65  ? 0.5421 0.3927 0.4329 -0.1129 0.1015  -0.0479 66  LYS A C   
587  O O   . LYS A 65  ? 0.4950 0.3740 0.4039 -0.1110 0.0926  -0.0540 66  LYS A O   
588  C CB  . LYS A 65  ? 0.5149 0.3302 0.3916 -0.1045 0.1052  -0.0430 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.5209 0.3154 0.3891 -0.1096 0.1134  -0.0476 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.4788 0.2705 0.3498 -0.0957 0.1076  -0.0428 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.5881 0.3529 0.4480 -0.0985 0.1172  -0.0461 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.5961 0.3242 0.4371 -0.0929 0.1240  -0.0376 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.5483 0.3876 0.4280 -0.1099 0.1031  -0.0396 67  CYS A N   
594  C CA  . CYS A 66  ? 0.5413 0.4030 0.4314 -0.1049 0.0954  -0.0378 67  CYS A CA  
595  C C   . CYS A 66  ? 0.5898 0.4814 0.4986 -0.1155 0.0956  -0.0518 67  CYS A C   
596  O O   . CYS A 66  ? 0.5788 0.4946 0.5025 -0.1096 0.0867  -0.0532 67  CYS A O   
597  C CB  . CYS A 66  ? 0.5737 0.4154 0.4447 -0.1035 0.0993  -0.0283 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.6656 0.4868 0.5172 -0.1240 0.1169  -0.0342 67  CYS A SG  
599  N N   . ASN A 67  ? 0.5446 0.4343 0.4528 -0.1310 0.1060  -0.0631 68  ASN A N   
600  C CA  . ASN A 67  ? 0.5391 0.4582 0.4665 -0.1426 0.1077  -0.0794 68  ASN A CA  
601  C C   . ASN A 67  ? 0.5545 0.4974 0.5007 -0.1418 0.0992  -0.0898 68  ASN A C   
602  O O   . ASN A 67  ? 0.5401 0.5109 0.5050 -0.1494 0.0982  -0.1047 68  ASN A O   
603  C CB  . ASN A 67  ? 0.5877 0.4931 0.5036 -0.1623 0.1253  -0.0876 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.7883 0.6753 0.6857 -0.1646 0.1328  -0.0795 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.7935 0.6474 0.6654 -0.1747 0.1461  -0.0758 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.6516 0.5565 0.5584 -0.1553 0.1242  -0.0760 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.5102 0.4434 0.4516 -0.1326 0.0927  -0.0830 69  LEU A N   
608  C CA  . LEU A 68  ? 0.4899 0.4421 0.4440 -0.1320 0.0841  -0.0919 69  LEU A CA  
609  C C   . LEU A 68  ? 0.4945 0.4715 0.4635 -0.1192 0.0681  -0.0908 69  LEU A C   
610  O O   . LEU A 68  ? 0.4724 0.4434 0.4374 -0.1081 0.0633  -0.0791 69  LEU A O   
611  C CB  . LEU A 68  ? 0.5030 0.4332 0.4437 -0.1284 0.0850  -0.0858 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.5818 0.4840 0.5066 -0.1401 0.1003  -0.0878 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.5919 0.4740 0.5058 -0.1336 0.1002  -0.0817 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.5874 0.5034 0.5203 -0.1579 0.1071  -0.1055 69  LEU A CD2 
615  N N   . SER A 69  ? 0.4339 0.4372 0.4189 -0.1207 0.0594  -0.1033 70  SER A N   
616  C CA  A SER A 69  ? 0.4106 0.4349 0.4078 -0.1084 0.0430  -0.1037 70  SER A CA  
617  C CA  B SER A 69  ? 0.4137 0.4371 0.4104 -0.1080 0.0431  -0.1029 70  SER A CA  
618  C C   . SER A 69  ? 0.4264 0.4444 0.4150 -0.1013 0.0333  -0.0992 70  SER A C   
619  O O   . SER A 69  ? 0.3699 0.3953 0.3606 -0.0902 0.0201  -0.0957 70  SER A O   
620  C CB  A SER A 69  ? 0.4529 0.5096 0.4723 -0.1126 0.0379  -0.1208 70  SER A CB  
621  C CB  B SER A 69  ? 0.4609 0.5166 0.4800 -0.1113 0.0378  -0.1192 70  SER A CB  
622  O OG  A SER A 69  ? 0.5213 0.5858 0.5493 -0.1201 0.0478  -0.1265 70  SER A OG  
623  O OG  B SER A 69  ? 0.5399 0.6073 0.5649 -0.1211 0.0384  -0.1330 70  SER A OG  
624  N N   . VAL A 70  ? 0.3868 0.3897 0.3642 -0.1087 0.0406  -0.1003 71  VAL A N   
625  C CA  . VAL A 70  ? 0.3826 0.3779 0.3494 -0.1047 0.0340  -0.0975 71  VAL A CA  
626  C C   . VAL A 70  ? 0.4177 0.3843 0.3684 -0.1062 0.0456  -0.0887 71  VAL A C   
627  O O   . VAL A 70  ? 0.4197 0.3735 0.3662 -0.1157 0.0584  -0.0916 71  VAL A O   
628  C CB  . VAL A 70  ? 0.4419 0.4530 0.4135 -0.1126 0.0291  -0.1122 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.4515 0.4523 0.4080 -0.1098 0.0232  -0.1094 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.4353 0.4774 0.4258 -0.1090 0.0162  -0.1226 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.3513 0.3072 0.2928 -0.0970 0.0413  -0.0789 72  ILE A N   
632  C CA  . ILE A 71  ? 0.3570 0.2892 0.2861 -0.0960 0.0504  -0.0723 72  ILE A CA  
633  C C   . ILE A 71  ? 0.4030 0.3326 0.3232 -0.0958 0.0461  -0.0742 72  ILE A C   
634  O O   . ILE A 71  ? 0.4008 0.3376 0.3190 -0.0896 0.0357  -0.0711 72  ILE A O   
635  C CB  . ILE A 71  ? 0.3805 0.3029 0.3082 -0.0859 0.0519  -0.0599 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.3912 0.3137 0.3236 -0.0870 0.0565  -0.0576 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.4013 0.3030 0.3196 -0.0826 0.0595  -0.0549 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.4476 0.3530 0.3731 -0.0967 0.0697  -0.0609 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.3870 0.3037 0.2993 -0.1032 0.0550  -0.0793 73  ASN A N   
640  C CA  . ASN A 72  ? 0.3951 0.3074 0.2964 -0.1049 0.0530  -0.0823 73  ASN A CA  
641  C C   . ASN A 72  ? 0.4340 0.3279 0.3284 -0.0996 0.0610  -0.0754 73  ASN A C   
642  O O   . ASN A 72  ? 0.4122 0.2902 0.3059 -0.1004 0.0722  -0.0748 73  ASN A O   
643  C CB  . ASN A 72  ? 0.4386 0.3501 0.3362 -0.1174 0.0579  -0.0947 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.6593 0.5929 0.5669 -0.1235 0.0504  -0.1046 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.5273 0.4782 0.4375 -0.1191 0.0362  -0.1061 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.6129 0.5461 0.5263 -0.1337 0.0598  -0.1126 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.3718 0.2668 0.2602 -0.0944 0.0556  -0.0712 74  LEU A N   
648  C CA  . LEU A 73  ? 0.3738 0.2559 0.2585 -0.0900 0.0635  -0.0672 74  LEU A CA  
649  C C   . LEU A 73  ? 0.4279 0.2990 0.3020 -0.0974 0.0713  -0.0751 74  LEU A C   
650  O O   . LEU A 73  ? 0.4515 0.3261 0.3179 -0.1059 0.0681  -0.0827 74  LEU A O   
651  C CB  . LEU A 73  ? 0.3726 0.2597 0.2552 -0.0836 0.0573  -0.0608 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.4011 0.2985 0.2936 -0.0759 0.0498  -0.0531 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.4059 0.3037 0.2957 -0.0710 0.0481  -0.0478 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.4082 0.3032 0.3118 -0.0719 0.0550  -0.0498 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.3889 0.2479 0.2633 -0.0937 0.0812  -0.0744 75  ASP A N   
656  C CA  . ASP A 74  ? 0.4243 0.2714 0.2900 -0.0998 0.0909  -0.0826 75  ASP A CA  
657  C C   . ASP A 74  ? 0.4952 0.3476 0.3458 -0.1069 0.0854  -0.0865 75  ASP A C   
658  O O   . ASP A 74  ? 0.4754 0.3343 0.3227 -0.1034 0.0786  -0.0810 75  ASP A O   
659  C CB  . ASP A 74  ? 0.4507 0.2888 0.3228 -0.0915 0.1003  -0.0811 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.5713 0.3961 0.4372 -0.0963 0.1123  -0.0906 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.5892 0.4161 0.4437 -0.1038 0.1132  -0.0962 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.6197 0.4302 0.4908 -0.0923 0.1209  -0.0925 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.5169 0.3647 0.3557 -0.1173 0.0880  -0.0960 76  PRO A N   
664  C CA  . PRO A 75  ? 0.5241 0.3746 0.3439 -0.1241 0.0813  -0.0992 76  PRO A CA  
665  C C   . PRO A 75  ? 0.5677 0.4119 0.3770 -0.1236 0.0863  -0.0976 76  PRO A C   
666  O O   . PRO A 75  ? 0.5884 0.4324 0.3788 -0.1280 0.0792  -0.0971 76  PRO A O   
667  C CB  . PRO A 75  ? 0.5663 0.4118 0.3768 -0.1355 0.0859  -0.1110 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.6333 0.4676 0.4562 -0.1349 0.0996  -0.1142 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.5510 0.3895 0.3909 -0.1243 0.0968  -0.1043 76  PRO A CD  
670  N N   . GLU A 76  ? 0.5186 0.3575 0.3392 -0.1184 0.0981  -0.0973 77  GLU A N   
671  C CA  . GLU A 76  ? 0.5356 0.3718 0.3499 -0.1191 0.1048  -0.0980 77  GLU A CA  
672  C C   . GLU A 76  ? 0.5241 0.3685 0.3403 -0.1132 0.0962  -0.0882 77  GLU A C   
673  O O   . GLU A 76  ? 0.5224 0.3647 0.3288 -0.1165 0.1001  -0.0886 77  GLU A O   
674  C CB  . GLU A 76  ? 0.5669 0.3984 0.3967 -0.1141 0.1195  -0.1030 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.8342 0.6540 0.6571 -0.1217 0.1311  -0.1148 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.2599 1.0755 1.0631 -0.1327 0.1381  -0.1226 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.2657 1.0834 1.0750 -0.1309 0.1475  -0.1257 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.2686 1.0797 1.0500 -0.1436 0.1341  -0.1263 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.4555 0.3083 0.2833 -0.1058 0.0859  -0.0806 78  ILE A N   
680  C CA  . ILE A 77  ? 0.4438 0.3034 0.2739 -0.1003 0.0781  -0.0720 78  ILE A CA  
681  C C   . ILE A 77  ? 0.5091 0.3653 0.3161 -0.1055 0.0675  -0.0696 78  ILE A C   
682  O O   . ILE A 77  ? 0.4927 0.3499 0.2912 -0.1079 0.0579  -0.0709 78  ILE A O   
683  C CB  . ILE A 77  ? 0.4574 0.3264 0.3072 -0.0907 0.0719  -0.0654 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.4645 0.3322 0.3327 -0.0841 0.0817  -0.0665 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.4039 0.2795 0.2549 -0.0857 0.0636  -0.0574 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.5149 0.3839 0.3913 -0.0800 0.0911  -0.0684 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.5062 0.3581 0.3029 -0.1070 0.0690  -0.0665 79  ASN A N   
688  C CA  . ASN A 78  ? 0.5257 0.3679 0.2955 -0.1115 0.0601  -0.0627 79  ASN A CA  
689  C C   . ASN A 78  ? 0.5203 0.3683 0.2955 -0.1028 0.0456  -0.0542 79  ASN A C   
690  O O   . ASN A 78  ? 0.4897 0.3451 0.2824 -0.0967 0.0475  -0.0500 79  ASN A O   
691  C CB  . ASN A 78  ? 0.5805 0.4132 0.3369 -0.1185 0.0714  -0.0640 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.7843 0.6009 0.5084 -0.1237 0.0639  -0.0587 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.6516 0.4663 0.3753 -0.1209 0.0611  -0.0525 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.7285 0.5312 0.4228 -0.1315 0.0605  -0.0612 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.4924 0.3380 0.2533 -0.1017 0.0306  -0.0525 80  PRO A N   
696  C CA  . PRO A 79  ? 0.4822 0.3337 0.2497 -0.0925 0.0169  -0.0459 80  PRO A CA  
697  C C   . PRO A 79  ? 0.5274 0.3692 0.2860 -0.0909 0.0173  -0.0388 80  PRO A C   
698  O O   . PRO A 79  ? 0.5107 0.3612 0.2863 -0.0834 0.0135  -0.0345 80  PRO A O   
699  C CB  . PRO A 79  ? 0.5255 0.3741 0.2749 -0.0920 0.0012  -0.0474 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.5883 0.4375 0.3330 -0.1003 0.0071  -0.0562 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.5406 0.3798 0.2801 -0.1079 0.0248  -0.0577 80  PRO A CD  
702  N N   . GLU A 80  ? 0.5072 0.3303 0.2383 -0.0994 0.0230  -0.0383 81  GLU A N   
703  C CA  . GLU A 80  ? 0.5189 0.3307 0.2398 -0.1003 0.0252  -0.0325 81  GLU A CA  
704  C C   . GLU A 80  ? 0.5212 0.3479 0.2712 -0.0988 0.0376  -0.0338 81  GLU A C   
705  O O   . GLU A 80  ? 0.4890 0.3190 0.2480 -0.0937 0.0341  -0.0291 81  GLU A O   
706  C CB  . GLU A 80  ? 0.5749 0.3613 0.2574 -0.1121 0.0308  -0.0325 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.7077 0.4783 0.3754 -0.1139 0.0316  -0.0262 81  GLU A CG  
708  C CD  . GLU A 80  ? 1.0732 0.8173 0.7037 -0.1284 0.0422  -0.0267 81  GLU A CD  
709  O OE1 . GLU A 80  ? 1.0873 0.8082 0.6911 -0.1298 0.0372  -0.0199 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 0.9964 0.7415 0.6235 -0.1389 0.0563  -0.0343 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.4916 0.3277 0.2566 -0.1022 0.0505  -0.0407 82  GLY A N   
712  C CA  . GLY A 81  ? 0.4678 0.3197 0.2615 -0.0986 0.0603  -0.0429 82  GLY A CA  
713  C C   . GLY A 81  ? 0.4634 0.3299 0.2810 -0.0871 0.0515  -0.0383 82  GLY A C   
714  O O   . GLY A 81  ? 0.4252 0.3001 0.2572 -0.0829 0.0522  -0.0358 82  GLY A O   
715  N N   . PHE A 82  ? 0.4077 0.2774 0.2286 -0.0831 0.0432  -0.0380 83  PHE A N   
716  C CA  . PHE A 82  ? 0.3816 0.2642 0.2230 -0.0741 0.0360  -0.0346 83  PHE A CA  
717  C C   . PHE A 82  ? 0.4056 0.2868 0.2425 -0.0701 0.0260  -0.0287 83  PHE A C   
718  O O   . PHE A 82  ? 0.3851 0.2762 0.2388 -0.0644 0.0252  -0.0260 83  PHE A O   
719  C CB  . PHE A 82  ? 0.3923 0.2792 0.2374 -0.0730 0.0303  -0.0374 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.3788 0.2787 0.2449 -0.0658 0.0262  -0.0352 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.4107 0.3161 0.2939 -0.0627 0.0342  -0.0351 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.3811 0.2866 0.2486 -0.0617 0.0144  -0.0332 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.4066 0.3210 0.3045 -0.0573 0.0312  -0.0324 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.3966 0.3140 0.2825 -0.0565 0.0123  -0.0321 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.3797 0.3005 0.2789 -0.0552 0.0211  -0.0313 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.4159 0.2838 0.2295 -0.0722 0.0175  -0.0269 84  CYS A N   
727  C CA  . CYS A 83  ? 0.4451 0.3071 0.2513 -0.0673 0.0071  -0.0215 84  CYS A CA  
728  C C   . CYS A 83  ? 0.4558 0.3152 0.2644 -0.0692 0.0147  -0.0188 84  CYS A C   
729  O O   . CYS A 83  ? 0.4197 0.2854 0.2401 -0.0633 0.0104  -0.0159 84  CYS A O   
730  C CB  . CYS A 83  ? 0.5132 0.3558 0.2882 -0.0692 -0.0027 -0.0198 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.5972 0.4278 0.3606 -0.0607 -0.0176 -0.0133 84  CYS A SG  
732  N N   . ILE A 84  ? 0.4212 0.2729 0.2197 -0.0783 0.0269  -0.0214 85  ILE A N   
733  C CA  . ILE A 84  ? 0.4062 0.2580 0.2080 -0.0825 0.0360  -0.0217 85  ILE A CA  
734  C C   . ILE A 84  ? 0.4032 0.2784 0.2380 -0.0755 0.0385  -0.0229 85  ILE A C   
735  O O   . ILE A 84  ? 0.3705 0.2503 0.2130 -0.0738 0.0379  -0.0211 85  ILE A O   
736  C CB  . ILE A 84  ? 0.4528 0.2960 0.2407 -0.0947 0.0501  -0.0272 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.4778 0.2914 0.2248 -0.1032 0.0475  -0.0242 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.4447 0.2994 0.2485 -0.0990 0.0623  -0.0317 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.5598 0.3646 0.2902 -0.1156 0.0605  -0.0305 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.3643 0.2522 0.2163 -0.0718 0.0410  -0.0258 86  LEU A N   
741  C CA  . LEU A 85  ? 0.3458 0.2521 0.2246 -0.0643 0.0425  -0.0261 86  LEU A CA  
742  C C   . LEU A 85  ? 0.3679 0.2801 0.2550 -0.0568 0.0322  -0.0214 86  LEU A C   
743  O O   . LEU A 85  ? 0.3379 0.2611 0.2396 -0.0524 0.0320  -0.0202 86  LEU A O   
744  C CB  . LEU A 85  ? 0.3546 0.2671 0.2452 -0.0624 0.0488  -0.0303 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.4269 0.3397 0.3179 -0.0682 0.0612  -0.0373 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.4426 0.3570 0.3420 -0.0655 0.0665  -0.0416 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.4390 0.3658 0.3464 -0.0665 0.0658  -0.0399 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.3423 0.2490 0.2210 -0.0554 0.0237  -0.0199 87  LEU A N   
749  C CA  . LEU A 86  ? 0.3292 0.2430 0.2167 -0.0488 0.0144  -0.0174 87  LEU A CA  
750  C C   . LEU A 86  ? 0.3665 0.2759 0.2491 -0.0478 0.0106  -0.0144 87  LEU A C   
751  O O   . LEU A 86  ? 0.3430 0.2622 0.2388 -0.0433 0.0086  -0.0132 87  LEU A O   
752  C CB  . LEU A 86  ? 0.3310 0.2422 0.2116 -0.0480 0.0058  -0.0189 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.3830 0.3052 0.2763 -0.0417 -0.0026 -0.0191 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.3602 0.2955 0.2727 -0.0402 0.0031  -0.0199 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.4348 0.3574 0.3226 -0.0407 -0.0123 -0.0229 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.3621 0.2544 0.2232 -0.0528 0.0104  -0.0133 88  ASP A N   
757  C CA  . ASP A 87  ? 0.3602 0.2432 0.2129 -0.0534 0.0086  -0.0107 88  ASP A CA  
758  C C   . ASP A 87  ? 0.3784 0.2737 0.2467 -0.0555 0.0173  -0.0124 88  ASP A C   
759  O O   . ASP A 87  ? 0.3738 0.2735 0.2494 -0.0523 0.0143  -0.0113 88  ASP A O   
760  C CB  . ASP A 87  ? 0.4143 0.2723 0.2366 -0.0608 0.0098  -0.0093 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.5957 0.4385 0.3986 -0.0564 -0.0031 -0.0066 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.5865 0.4403 0.4028 -0.0472 -0.0132 -0.0068 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.6246 0.4448 0.3984 -0.0622 -0.0032 -0.0050 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.3497 0.2523 0.2247 -0.0601 0.0274  -0.0162 89  PHE A N   
765  C CA  . PHE A 88  ? 0.3218 0.2405 0.2149 -0.0606 0.0344  -0.0195 89  PHE A CA  
766  C C   . PHE A 88  ? 0.3284 0.2639 0.2418 -0.0515 0.0291  -0.0178 89  PHE A C   
767  O O   . PHE A 88  ? 0.2896 0.2345 0.2125 -0.0503 0.0289  -0.0184 89  PHE A O   
768  C CB  . PHE A 88  ? 0.3254 0.2509 0.2247 -0.0646 0.0448  -0.0254 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.3136 0.2604 0.2363 -0.0615 0.0492  -0.0297 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.3375 0.2900 0.2631 -0.0673 0.0538  -0.0338 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.3276 0.2877 0.2682 -0.0522 0.0474  -0.0297 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.3263 0.3016 0.2749 -0.0635 0.0557  -0.0388 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.3507 0.3299 0.3113 -0.0471 0.0486  -0.0333 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.3320 0.3208 0.2978 -0.0524 0.0521  -0.0383 89  PHE A CZ  
775  N N   . MET A 89  ? 0.2747 0.2132 0.1933 -0.0462 0.0257  -0.0163 90  MET A N   
776  C CA  . MET A 89  ? 0.2585 0.2093 0.1920 -0.0391 0.0219  -0.0145 90  MET A CA  
777  C C   . MET A 89  ? 0.3083 0.2604 0.2422 -0.0372 0.0158  -0.0127 90  MET A C   
778  O O   . MET A 89  ? 0.2959 0.2589 0.2403 -0.0344 0.0154  -0.0125 90  MET A O   
779  C CB  . MET A 89  ? 0.2727 0.2219 0.2069 -0.0366 0.0198  -0.0138 90  MET A CB  
780  C CG  . MET A 89  ? 0.2960 0.2437 0.2319 -0.0372 0.0264  -0.0159 90  MET A CG  
781  S SD  . MET A 89  ? 0.3403 0.2853 0.2767 -0.0359 0.0245  -0.0158 90  MET A SD  
782  C CE  . MET A 89  ? 0.3443 0.2816 0.2773 -0.0386 0.0331  -0.0195 90  MET A CE  
783  N N   . TYR A 90  ? 0.2806 0.2207 0.2020 -0.0382 0.0104  -0.0117 91  TYR A N   
784  C CA  . TYR A 90  ? 0.2839 0.2231 0.2055 -0.0351 0.0040  -0.0109 91  TYR A CA  
785  C C   . TYR A 90  ? 0.3412 0.2720 0.2548 -0.0390 0.0057  -0.0110 91  TYR A C   
786  O O   . TYR A 90  ? 0.3296 0.2582 0.2433 -0.0362 0.0011  -0.0109 91  TYR A O   
787  C CB  . TYR A 90  ? 0.3037 0.2346 0.2173 -0.0319 -0.0043 -0.0108 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.3085 0.2519 0.2347 -0.0283 -0.0068 -0.0127 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.3230 0.2678 0.2494 -0.0304 -0.0040 -0.0138 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.3117 0.2651 0.2492 -0.0241 -0.0106 -0.0147 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.3005 0.2550 0.2368 -0.0292 -0.0048 -0.0166 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.3114 0.2758 0.2594 -0.0231 -0.0113 -0.0180 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.3324 0.2970 0.2795 -0.0261 -0.0081 -0.0188 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.3045 0.2787 0.2607 -0.0271 -0.0074 -0.0231 91  TYR A OH  
795  N N   . THR A 91  ? 0.3049 0.2301 0.2109 -0.0462 0.0131  -0.0123 92  THR A N   
796  C CA  . THR A 91  ? 0.3287 0.2432 0.2245 -0.0524 0.0163  -0.0134 92  THR A CA  
797  C C   . THR A 91  ? 0.3490 0.2756 0.2539 -0.0594 0.0261  -0.0183 92  THR A C   
798  O O   . THR A 91  ? 0.3477 0.2683 0.2468 -0.0658 0.0298  -0.0207 92  THR A O   
799  C CB  . THR A 91  ? 0.4068 0.2935 0.2748 -0.0578 0.0161  -0.0112 92  THR A CB  
800  O OG1 . THR A 91  ? 0.4031 0.2885 0.2654 -0.0643 0.0237  -0.0131 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.4162 0.2901 0.2734 -0.0499 0.0043  -0.0073 92  THR A CG2 
802  N N   . SER A 92  ? 0.2932 0.2346 0.2106 -0.0588 0.0308  -0.0210 93  SER A N   
803  C CA  . SER A 92  ? 0.2830 0.2391 0.2119 -0.0643 0.0399  -0.0279 93  SER A CA  
804  C C   . SER A 92  ? 0.3351 0.2764 0.2471 -0.0764 0.0494  -0.0316 93  SER A C   
805  O O   . SER A 92  ? 0.3381 0.2922 0.2599 -0.0826 0.0584  -0.0394 93  SER A O   
806  C CB  . SER A 92  ? 0.2923 0.2618 0.2323 -0.0659 0.0402  -0.0317 93  SER A CB  
807  O OG  . SER A 92  ? 0.3499 0.3297 0.3005 -0.0567 0.0320  -0.0283 93  SER A OG  
808  N N   A ARG A 93  ? 0.3327 0.2477 0.2192 -0.0794 0.0471  -0.0267 94  ARG A N   
809  N N   B ARG A 93  ? 0.3173 0.2320 0.2035 -0.0797 0.0472  -0.0268 94  ARG A N   
810  C CA  A ARG A 93  ? 0.3585 0.2527 0.2211 -0.0919 0.0557  -0.0288 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.3363 0.2316 0.1999 -0.0923 0.0564  -0.0293 94  ARG A CA  
812  C C   A ARG A 93  ? 0.4031 0.2930 0.2588 -0.0921 0.0576  -0.0288 94  ARG A C   
813  C C   B ARG A 93  ? 0.3953 0.2845 0.2503 -0.0925 0.0578  -0.0288 94  ARG A C   
814  O O   A ARG A 93  ? 0.3882 0.2725 0.2394 -0.0843 0.0485  -0.0233 94  ARG A O   
815  O O   B ARG A 93  ? 0.3841 0.2668 0.2337 -0.0847 0.0484  -0.0231 94  ARG A O   
816  C CB  A ARG A 93  ? 0.4282 0.2912 0.2615 -0.0948 0.0507  -0.0228 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.3715 0.2363 0.2061 -0.0977 0.0539  -0.0248 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.5199 0.3831 0.3575 -0.0952 0.0494  -0.0234 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.3363 0.2049 0.1768 -0.1028 0.0577  -0.0284 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.5944 0.4251 0.4045 -0.0936 0.0418  -0.0167 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.5220 0.3611 0.3385 -0.1026 0.0517  -0.0225 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.6566 0.4545 0.4316 -0.1047 0.0476  -0.0151 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.6188 0.4620 0.4420 -0.1079 0.0559  -0.0270 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.8311 0.6114 0.5886 -0.1189 0.0587  -0.0184 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.8102 0.6244 0.6087 -0.1168 0.0597  -0.0264 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.6838 0.4309 0.4051 -0.1297 0.0644  -0.0163 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.6422 0.4627 0.4493 -0.1222 0.0641  -0.0317 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.6788 0.4739 0.4534 -0.1236 0.0646  -0.0244 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.7058 0.4825 0.4686 -0.1205 0.0590  -0.0206 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.3653 0.2592 0.2212 -0.1019 0.0703  -0.0363 95  LEU A N   
831  C CA  . LEU A 94  ? 0.3684 0.2585 0.2178 -0.1038 0.0745  -0.0383 95  LEU A CA  
832  C C   . LEU A 94  ? 0.4650 0.3279 0.2806 -0.1185 0.0828  -0.0394 95  LEU A C   
833  O O   . LEU A 94  ? 0.4687 0.3308 0.2805 -0.1312 0.0954  -0.0465 95  LEU A O   
834  C CB  . LEU A 94  ? 0.3505 0.2687 0.2298 -0.1014 0.0824  -0.0474 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.4072 0.3239 0.2844 -0.1019 0.0874  -0.0507 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.3922 0.3063 0.2710 -0.0902 0.0758  -0.0433 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.4040 0.3454 0.3084 -0.1011 0.0975  -0.0620 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.4696 0.3099 0.2593 -0.1174 0.0757  -0.0329 96  ASN A N   
839  C CA  . ASN A 95  ? 0.5075 0.3167 0.2579 -0.1306 0.0816  -0.0322 96  ASN A CA  
840  C C   . ASN A 95  ? 0.5644 0.3802 0.3158 -0.1391 0.0947  -0.0410 96  ASN A C   
841  O O   . ASN A 95  ? 0.5714 0.3788 0.3100 -0.1376 0.0911  -0.0393 96  ASN A O   
842  C CB  . ASN A 95  ? 0.5604 0.3434 0.2820 -0.1240 0.0660  -0.0221 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.8259 0.5719 0.5007 -0.1364 0.0696  -0.0196 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.7300 0.4626 0.3880 -0.1515 0.0836  -0.0237 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.7674 0.4961 0.4190 -0.1311 0.0571  -0.0136 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.5135 0.3469 0.2829 -0.1475 0.1097  -0.0516 97  LEU A N   
847  C CA  . LEU A 96  ? 0.5238 0.3681 0.3007 -0.1547 0.1236  -0.0625 97  LEU A CA  
848  C C   . LEU A 96  ? 0.6031 0.4215 0.3435 -0.1748 0.1375  -0.0667 97  LEU A C   
849  O O   . LEU A 96  ? 0.6010 0.4105 0.3305 -0.1865 0.1457  -0.0692 97  LEU A O   
850  C CB  . LEU A 96  ? 0.5069 0.3882 0.3270 -0.1507 0.1309  -0.0734 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.5740 0.4761 0.4167 -0.1498 0.1410  -0.0850 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.5751 0.4755 0.4209 -0.1369 0.1311  -0.0793 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.5552 0.4932 0.4398 -0.1436 0.1450  -0.0952 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.5829 0.3858 0.3003 -0.1798 0.1402  -0.0672 98  ARG A N   
855  C CA  . ARG A 97  ? 0.6298 0.4031 0.3051 -0.1997 0.1532  -0.0703 98  ARG A CA  
856  C C   . ARG A 97  ? 0.6509 0.4336 0.3303 -0.2068 0.1666  -0.0820 98  ARG A C   
857  O O   . ARG A 97  ? 0.6048 0.4069 0.3096 -0.1943 0.1611  -0.0836 98  ARG A O   
858  C CB  . ARG A 97  ? 0.6771 0.4101 0.3047 -0.1992 0.1391  -0.0562 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.7795 0.4994 0.4004 -0.1908 0.1249  -0.0448 98  ARG A CG  
860  C CD  . ARG A 97  ? 1.0233 0.7062 0.6013 -0.1860 0.1081  -0.0316 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.2807 0.9245 0.8059 -0.2034 0.1167  -0.0308 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.5515 1.1625 1.0416 -0.2169 0.1245  -0.0283 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.4241 0.9973 0.8627 -0.2334 0.1328  -0.0274 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.4040 1.0180 0.9080 -0.2151 0.1247  -0.0269 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.6409 0.4079 0.2939 -0.2279 0.1853  -0.0907 99  GLU A N   
866  C CA  . GLU A 98  ? 0.6469 0.4212 0.3014 -0.2364 0.2000  -0.1034 99  GLU A CA  
867  C C   . GLU A 98  ? 0.7184 0.4823 0.3592 -0.2272 0.1874  -0.0965 99  GLU A C   
868  O O   . GLU A 98  ? 0.6956 0.4796 0.3610 -0.2222 0.1919  -0.1053 99  GLU A O   
869  C CB  . GLU A 98  ? 0.7124 0.4611 0.3268 -0.2628 0.2206  -0.1111 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.8604 0.6204 0.4801 -0.2740 0.2396  -0.1277 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.3098 1.0423 0.8855 -0.3019 0.2610  -0.1357 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.3043 0.9930 0.8248 -0.3112 0.2559  -0.1233 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.3406 1.0947 0.9365 -0.3143 0.2832  -0.1551 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.7153 0.4483 0.3182 -0.2245 0.1713  -0.0819 100 GLY A N   
875  C CA  . GLY A 99  ? 0.7260 0.4481 0.3121 -0.2172 0.1578  -0.0759 100 GLY A CA  
876  C C   . GLY A 99  ? 0.7149 0.4623 0.3390 -0.1963 0.1423  -0.0721 100 GLY A C   
877  O O   . GLY A 99  ? 0.7087 0.4538 0.3267 -0.1915 0.1343  -0.0709 100 GLY A O   
878  N N   . ASN A 100 ? 0.6235 0.3946 0.2856 -0.1847 0.1385  -0.0708 101 ASN A N   
879  C CA  . ASN A 100 ? 0.5764 0.3682 0.2708 -0.1662 0.1247  -0.0668 101 ASN A CA  
880  C C   . ASN A 100 ? 0.5884 0.4133 0.3305 -0.1580 0.1322  -0.0752 101 ASN A C   
881  O O   . ASN A 100 ? 0.5464 0.3856 0.3126 -0.1440 0.1230  -0.0725 101 ASN A O   
882  C CB  . ASN A 100 ? 0.5608 0.3457 0.2510 -0.1555 0.1061  -0.0538 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.6426 0.4358 0.3485 -0.1542 0.1081  -0.0523 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.5231 0.3392 0.2588 -0.1547 0.1191  -0.0606 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.5717 0.3475 0.2593 -0.1513 0.0965  -0.0424 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.5546 0.3916 0.3100 -0.1664 0.1484  -0.0857 102 ILE A N   
887  C CA  . ILE A 101 ? 0.5222 0.3918 0.3233 -0.1568 0.1534  -0.0940 102 ILE A CA  
888  C C   . ILE A 101 ? 0.5290 0.4109 0.3519 -0.1465 0.1536  -0.0989 102 ILE A C   
889  O O   . ILE A 101 ? 0.4815 0.3818 0.3354 -0.1312 0.1466  -0.0972 102 ILE A O   
890  C CB  . ILE A 101 ? 0.5689 0.4525 0.3820 -0.1685 0.1711  -0.1075 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.5440 0.4637 0.4064 -0.1548 0.1715  -0.1152 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.5747 0.4488 0.3688 -0.1857 0.1895  -0.1197 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.5468 0.4848 0.4256 -0.1622 0.1809  -0.1244 102 ILE A CD1 
894  N N   . MET A 102 ? 0.5183 0.3882 0.3232 -0.1550 0.1617  -0.1049 103 MET A N   
895  C CA  . MET A 102 ? 0.5187 0.3965 0.3416 -0.1463 0.1630  -0.1102 103 MET A CA  
896  C C   . MET A 102 ? 0.5349 0.4088 0.3602 -0.1333 0.1458  -0.0987 103 MET A C   
897  O O   . MET A 102 ? 0.4984 0.3855 0.3516 -0.1202 0.1435  -0.0998 103 MET A O   
898  C CB  . MET A 102 ? 0.5859 0.4507 0.3872 -0.1598 0.1762  -0.1203 103 MET A CB  
899  C CG  . MET A 102 ? 0.6714 0.5437 0.4754 -0.1734 0.1965  -0.1352 103 MET A CG  
900  S SD  . MET A 102 ? 0.7230 0.6330 0.5817 -0.1618 0.2048  -0.1482 103 MET A SD  
901  C CE  . MET A 102 ? 0.6794 0.5959 0.5612 -0.1487 0.2073  -0.1562 103 MET A CE  
902  N N   . ALA A 103 ? 0.5130 0.3688 0.3095 -0.1364 0.1338  -0.0882 104 ALA A N   
903  C CA  . ALA A 103 ? 0.5041 0.3587 0.3035 -0.1257 0.1179  -0.0790 104 ALA A CA  
904  C C   . ALA A 103 ? 0.5061 0.3764 0.3322 -0.1127 0.1097  -0.0726 104 ALA A C   
905  O O   . ALA A 103 ? 0.4653 0.3434 0.3101 -0.1020 0.1041  -0.0703 104 ALA A O   
906  C CB  . ALA A 103 ? 0.5395 0.3747 0.3044 -0.1310 0.1061  -0.0710 104 ALA A CB  
907  N N   . VAL A 104 ? 0.4436 0.3167 0.2695 -0.1150 0.1100  -0.0701 105 VAL A N   
908  C CA  . VAL A 104 ? 0.4062 0.2943 0.2556 -0.1040 0.1026  -0.0649 105 VAL A CA  
909  C C   . VAL A 104 ? 0.4244 0.3326 0.3073 -0.0940 0.1078  -0.0710 105 VAL A C   
910  O O   . VAL A 104 ? 0.3965 0.3116 0.2950 -0.0823 0.0992  -0.0656 105 VAL A O   
911  C CB  . VAL A 104 ? 0.4547 0.3409 0.2963 -0.1097 0.1028  -0.0623 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.4216 0.3263 0.2898 -0.0992 0.0970  -0.0593 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.4713 0.3343 0.2796 -0.1146 0.0932  -0.0536 105 VAL A CG2 
914  N N   A MET A 105 ? 0.4072 0.3239 0.3003 -0.0984 0.1216  -0.0827 106 MET A N   
915  N N   B MET A 105 ? 0.4072 0.3240 0.3005 -0.0983 0.1216  -0.0827 106 MET A N   
916  C CA  A MET A 105 ? 0.4040 0.3393 0.3294 -0.0866 0.1253  -0.0894 106 MET A CA  
917  C CA  B MET A 105 ? 0.4028 0.3381 0.3281 -0.0866 0.1253  -0.0894 106 MET A CA  
918  C C   A MET A 105 ? 0.4450 0.3733 0.3743 -0.0774 0.1217  -0.0873 106 MET A C   
919  C C   B MET A 105 ? 0.4480 0.3763 0.3774 -0.0774 0.1217  -0.0873 106 MET A C   
920  O O   A MET A 105 ? 0.4168 0.3527 0.3654 -0.0637 0.1159  -0.0843 106 MET A O   
921  O O   B MET A 105 ? 0.4243 0.3603 0.3729 -0.0638 0.1158  -0.0842 106 MET A O   
922  C CB  A MET A 105 ? 0.4451 0.3921 0.3818 -0.0930 0.1411  -0.1047 106 MET A CB  
923  C CB  B MET A 105 ? 0.4453 0.3925 0.3822 -0.0929 0.1411  -0.1047 106 MET A CB  
924  C CG  A MET A 105 ? 0.4784 0.4470 0.4509 -0.0781 0.1427  -0.1124 106 MET A CG  
925  C CG  B MET A 105 ? 0.4815 0.4508 0.4544 -0.0781 0.1424  -0.1122 106 MET A CG  
926  S SD  A MET A 105 ? 0.5400 0.5299 0.5323 -0.0853 0.1609  -0.1331 106 MET A SD  
927  S SD  B MET A 105 ? 0.5491 0.5376 0.5411 -0.0847 0.1611  -0.1333 106 MET A SD  
928  C CE  A MET A 105 ? 0.5215 0.4943 0.4993 -0.0925 0.1735  -0.1418 106 MET A CE  
929  C CE  B MET A 105 ? 0.5039 0.5032 0.5276 -0.0630 0.1589  -0.1390 106 MET A CE  
930  N N   . ALA A 106 ? 0.4257 0.3378 0.3346 -0.0857 0.1254  -0.0892 107 ALA A N   
931  C CA  . ALA A 106 ? 0.4267 0.3296 0.3363 -0.0801 0.1237  -0.0886 107 ALA A CA  
932  C C   . ALA A 106 ? 0.4315 0.3316 0.3412 -0.0726 0.1099  -0.0769 107 ALA A C   
933  O O   . ALA A 106 ? 0.4057 0.3055 0.3286 -0.0624 0.1079  -0.0752 107 ALA A O   
934  C CB  . ALA A 106 ? 0.4572 0.3447 0.3425 -0.0926 0.1294  -0.0935 107 ALA A CB  
935  N N   . THR A 107 ? 0.3893 0.2869 0.2845 -0.0771 0.1008  -0.0692 108 THR A N   
936  C CA  . THR A 107 ? 0.3775 0.2752 0.2741 -0.0710 0.0884  -0.0598 108 THR A CA  
937  C C   . THR A 107 ? 0.4086 0.3190 0.3271 -0.0594 0.0851  -0.0559 108 THR A C   
938  O O   . THR A 107 ? 0.3819 0.2911 0.3075 -0.0520 0.0804  -0.0516 108 THR A O   
939  C CB  . THR A 107 ? 0.4522 0.3439 0.3287 -0.0773 0.0793  -0.0541 108 THR A CB  
940  O OG1 . THR A 107 ? 0.4626 0.3419 0.3162 -0.0878 0.0823  -0.0583 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.4424 0.3354 0.3212 -0.0720 0.0676  -0.0475 108 THR A CG2 
942  N N   . ALA A 108 ? 0.3599 0.2820 0.2880 -0.0587 0.0880  -0.0583 109 ALA A N   
943  C CA  . ALA A 108 ? 0.3302 0.2664 0.2786 -0.0478 0.0839  -0.0557 109 ALA A CA  
944  C C   . ALA A 108 ? 0.3594 0.2973 0.3239 -0.0366 0.0868  -0.0590 109 ALA A C   
945  O O   . ALA A 108 ? 0.3384 0.2784 0.3114 -0.0263 0.0801  -0.0533 109 ALA A O   
946  C CB  . ALA A 108 ? 0.3353 0.2852 0.2907 -0.0514 0.0873  -0.0601 109 ALA A CB  
947  N N   . MET A 109 ? 0.3414 0.2753 0.3074 -0.0384 0.0967  -0.0679 110 MET A N   
948  C CA  . MET A 109 ? 0.3441 0.2754 0.3238 -0.0265 0.0994  -0.0714 110 MET A CA  
949  C C   . MET A 109 ? 0.3907 0.3038 0.3601 -0.0234 0.0946  -0.0637 110 MET A C   
950  O O   . MET A 109 ? 0.3887 0.2982 0.3652 -0.0115 0.0901  -0.0591 110 MET A O   
951  C CB  . MET A 109 ? 0.3893 0.3194 0.3721 -0.0304 0.1121  -0.0840 110 MET A CB  
952  C CG  . MET A 109 ? 0.4463 0.3978 0.4469 -0.0302 0.1181  -0.0942 110 MET A CG  
953  S SD  . MET A 109 ? 0.5455 0.4960 0.5462 -0.0394 0.1353  -0.1106 110 MET A SD  
954  C CE  . MET A 109 ? 0.5175 0.4612 0.5355 -0.0212 0.1364  -0.1149 110 MET A CE  
955  N N   . TYR A 110 ? 0.3671 0.2688 0.3185 -0.0346 0.0953  -0.0625 111 TYR A N   
956  C CA  . TYR A 110 ? 0.3723 0.2592 0.3138 -0.0356 0.0922  -0.0576 111 TYR A CA  
957  C C   . TYR A 110 ? 0.3945 0.2851 0.3376 -0.0307 0.0822  -0.0477 111 TYR A C   
958  O O   . TYR A 110 ? 0.3748 0.2551 0.3178 -0.0250 0.0810  -0.0436 111 TYR A O   
959  C CB  . TYR A 110 ? 0.3903 0.2711 0.3143 -0.0493 0.0932  -0.0602 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.4047 0.2762 0.3198 -0.0532 0.0892  -0.0570 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.4446 0.3010 0.3574 -0.0535 0.0954  -0.0604 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.3960 0.2737 0.3051 -0.0575 0.0799  -0.0521 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.4167 0.2660 0.3220 -0.0595 0.0933  -0.0594 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.3958 0.2691 0.2997 -0.0621 0.0769  -0.0519 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.4089 0.2687 0.3108 -0.0642 0.0842  -0.0560 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.4108 0.2676 0.3082 -0.0711 0.0828  -0.0577 111 TYR A OH  
967  N N   . LEU A 111 ? 0.3507 0.2541 0.2941 -0.0333 0.0760  -0.0442 112 LEU A N   
968  C CA  . LEU A 111 ? 0.3290 0.2375 0.2740 -0.0298 0.0672  -0.0362 112 LEU A CA  
969  C C   . LEU A 111 ? 0.3645 0.2796 0.3224 -0.0177 0.0646  -0.0332 112 LEU A C   
970  O O   . LEU A 111 ? 0.3474 0.2643 0.3053 -0.0142 0.0583  -0.0267 112 LEU A O   
971  C CB  . LEU A 111 ? 0.3143 0.2315 0.2539 -0.0362 0.0616  -0.0343 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.3567 0.2674 0.2813 -0.0460 0.0597  -0.0357 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.3447 0.2609 0.2631 -0.0492 0.0526  -0.0326 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.3714 0.2760 0.2933 -0.0472 0.0574  -0.0345 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.3383 0.2589 0.3076 -0.0114 0.0691  -0.0389 113 GLN A N   
976  C CA  . GLN A 112 ? 0.3360 0.2660 0.3195 0.0017  0.0651  -0.0378 113 GLN A CA  
977  C C   . GLN A 112 ? 0.3534 0.3011 0.3422 0.0008  0.0586  -0.0351 113 GLN A C   
978  O O   . GLN A 112 ? 0.3356 0.2847 0.3239 0.0062  0.0512  -0.0284 113 GLN A O   
979  C CB  . GLN A 112 ? 0.3609 0.2744 0.3393 0.0114  0.0618  -0.0313 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.4160 0.3085 0.3883 0.0124  0.0693  -0.0346 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.5729 0.4431 0.5327 0.0171  0.0671  -0.0268 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.4577 0.3280 0.4166 0.0254  0.0600  -0.0200 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.5176 0.3672 0.4653 0.0105  0.0739  -0.0281 113 GLN A NE2 
984  N N   . MET A 113 ? 0.3128 0.2718 0.3041 -0.0076 0.0623  -0.0408 114 MET A N   
985  C CA  . MET A 113 ? 0.2928 0.2668 0.2881 -0.0109 0.0583  -0.0402 114 MET A CA  
986  C C   . MET A 113 ? 0.3633 0.3555 0.3760 -0.0091 0.0636  -0.0504 114 MET A C   
987  O O   . MET A 113 ? 0.3442 0.3390 0.3549 -0.0192 0.0718  -0.0576 114 MET A O   
988  C CB  . MET A 113 ? 0.3081 0.2746 0.2871 -0.0239 0.0591  -0.0384 114 MET A CB  
989  C CG  . MET A 113 ? 0.3361 0.2901 0.3027 -0.0248 0.0532  -0.0307 114 MET A CG  
990  S SD  . MET A 113 ? 0.3874 0.3325 0.3354 -0.0367 0.0517  -0.0296 114 MET A SD  
991  C CE  . MET A 113 ? 0.3453 0.3007 0.2959 -0.0378 0.0468  -0.0273 114 MET A CE  
992  N N   . GLU A 114 ? 0.3540 0.3577 0.3832 0.0044  0.0591  -0.0520 115 GLU A N   
993  C CA  . GLU A 114 ? 0.3730 0.3975 0.4243 0.0099  0.0629  -0.0638 115 GLU A CA  
994  C C   . GLU A 114 ? 0.3726 0.4169 0.4318 -0.0010 0.0676  -0.0720 115 GLU A C   
995  O O   . GLU A 114 ? 0.3694 0.4252 0.4402 -0.0053 0.0772  -0.0843 115 GLU A O   
996  C CB  . GLU A 114 ? 0.4083 0.4418 0.4741 0.0283  0.0534  -0.0627 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.5870 0.5969 0.6433 0.0391  0.0508  -0.0559 115 GLU A CG  
998  N N   . HIS A 115 ? 0.3188 0.3661 0.3715 -0.0066 0.0623  -0.0665 116 HIS A N   
999  C CA  . HIS A 115 ? 0.3330 0.3957 0.3909 -0.0184 0.0680  -0.0747 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.3703 0.4189 0.4113 -0.0348 0.0795  -0.0779 116 HIS A C   
1001 O O   . HIS A 115 ? 0.3715 0.4320 0.4199 -0.0441 0.0896  -0.0895 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.3530 0.4204 0.4074 -0.0203 0.0602  -0.0690 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.4033 0.4877 0.4738 -0.0060 0.0496  -0.0682 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.4342 0.5457 0.5298 0.0007  0.0495  -0.0800 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.4258 0.5038 0.4892 0.0021  0.0389  -0.0577 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.4238 0.5429 0.5251 0.0139  0.0372  -0.0753 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.4263 0.5248 0.5074 0.0143  0.0313  -0.0617 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.3094 0.3333 0.3276 -0.0384 0.0781  -0.0686 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.3198 0.3269 0.3173 -0.0526 0.0869  -0.0704 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.3895 0.4007 0.3951 -0.0542 0.0982  -0.0816 117 VAL A C   
1011 O O   . VAL A 116 ? 0.3720 0.3835 0.3717 -0.0673 0.1096  -0.0903 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.3618 0.3451 0.3352 -0.0546 0.0807  -0.0593 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.3747 0.3405 0.3251 -0.0681 0.0885  -0.0617 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.3515 0.3318 0.3180 -0.0541 0.0711  -0.0506 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.3467 0.3593 0.3645 -0.0412 0.0959  -0.0820 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.3558 0.3724 0.3840 -0.0403 0.1064  -0.0936 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.4137 0.4570 0.4648 -0.0430 0.1147  -0.1087 118 VAL A C   
1018 O O   . VAL A 117 ? 0.4045 0.4492 0.4537 -0.0546 0.1282  -0.1199 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.3881 0.3996 0.4261 -0.0238 0.1016  -0.0913 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.3893 0.4054 0.4404 -0.0215 0.1128  -0.1049 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.3902 0.3764 0.4057 -0.0246 0.0961  -0.0791 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.3767 0.4422 0.4501 -0.0324 0.1070  -0.1102 119 ASP A N   
1023 N N   B ASP A 118 ? 0.3682 0.4326 0.4387 -0.0346 0.1070  -0.1093 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.3800 0.4768 0.4805 -0.0331 0.1128  -0.1261 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.3670 0.4619 0.4628 -0.0368 0.1130  -0.1246 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.4370 0.5368 0.5282 -0.0551 0.1260  -0.1344 119 ASP A C   
1027 C C   B ASP A 118 ? 0.4005 0.4945 0.4834 -0.0594 0.1261  -0.1316 119 ASP A C   
1028 O O   A ASP A 118 ? 0.4439 0.5623 0.5517 -0.0616 0.1385  -0.1513 119 ASP A O   
1029 O O   B ASP A 118 ? 0.3962 0.5036 0.4905 -0.0676 0.1398  -0.1474 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.3936 0.5114 0.5137 -0.0194 0.0994  -0.1240 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.3807 0.4956 0.4943 -0.0246 0.0997  -0.1219 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.5502 0.6731 0.6873 0.0037  0.0890  -0.1226 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.5348 0.6865 0.6795 -0.0244 0.1037  -0.1394 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.5940 0.7198 0.7438 0.0105  0.0950  -0.1319 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.5592 0.7279 0.7270 -0.0170 0.1090  -0.1530 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.6180 0.7404 0.7542 0.0150  0.0752  -0.1124 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.5930 0.7574 0.7402 -0.0314 0.1015  -0.1406 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.3933 0.4732 0.4571 -0.0667 0.1237  -0.1233 120 THR A N   
1039 N N   B THR A 119 ? 0.3514 0.4275 0.4089 -0.0698 0.1226  -0.1205 120 THR A N   
1040 C CA  A THR A 119 ? 0.4039 0.4775 0.4505 -0.0881 0.1353  -0.1282 120 THR A CA  
1041 C CA  B THR A 119 ? 0.3641 0.4324 0.4035 -0.0914 0.1349  -0.1257 120 THR A CA  
1042 C C   A THR A 119 ? 0.4503 0.5033 0.4743 -0.1013 0.1480  -0.1314 120 THR A C   
1043 C C   B THR A 119 ? 0.4289 0.4760 0.4452 -0.1040 0.1473  -0.1286 120 THR A C   
1044 O O   A THR A 119 ? 0.4569 0.5156 0.4798 -0.1170 0.1634  -0.1445 120 THR A O   
1045 O O   B THR A 119 ? 0.4296 0.4757 0.4369 -0.1218 0.1618  -0.1386 120 THR A O   
1046 C CB  A THR A 119 ? 0.5221 0.5797 0.5479 -0.0922 0.1264  -0.1149 120 THR A CB  
1047 C CB  B THR A 119 ? 0.3792 0.4311 0.3966 -0.0977 0.1275  -0.1136 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.5171 0.5977 0.5668 -0.0801 0.1161  -0.1148 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.3980 0.4473 0.4039 -0.1176 0.1405  -0.1218 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.5332 0.5800 0.5386 -0.1135 0.1375  -0.1189 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.3207 0.3397 0.3068 -0.0969 0.1199  -0.0976 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.3970 0.4262 0.4018 -0.0964 0.1423  -0.1204 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.4180 0.4269 0.3996 -0.1077 0.1528  -0.1233 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.4858 0.5148 0.4903 -0.1095 0.1675  -0.1419 121 CYS A C   
1055 O O   . CYS A 120 ? 0.4957 0.5193 0.4865 -0.1271 0.1830  -0.1517 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.4155 0.4044 0.3832 -0.0988 0.1432  -0.1115 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.4648 0.4276 0.4004 -0.1009 0.1290  -0.0929 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.4386 0.4908 0.4779 -0.0911 0.1625  -0.1474 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.4463 0.5224 0.5148 -0.0880 0.1742  -0.1666 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.4960 0.5948 0.5765 -0.1036 0.1881  -0.1831 122 ARG A C   
1061 O O   . ARG A 121 ? 0.4883 0.5932 0.5717 -0.1156 0.2054  -0.1991 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.4616 0.5579 0.5641 -0.0630 0.1624  -0.1677 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.6557 0.7309 0.7506 -0.0493 0.1554  -0.1582 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.8338 0.9263 0.9613 -0.0299 0.1547  -0.1692 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.9490 1.0386 1.0838 -0.0085 0.1371  -0.1570 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.0903 1.1539 1.2108 0.0008  0.1305  -0.1453 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8621 0.9025 0.9621 -0.0087 0.1392  -0.1447 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.9405 1.0003 1.0652 0.0185  0.1158  -0.1347 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.4572 0.5682 0.5439 -0.1049 0.1815  -0.1801 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.4620 0.5951 0.5604 -0.1209 0.1942  -0.1958 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.5260 0.6327 0.5863 -0.1479 0.2103  -0.1967 123 LYS A C   
1072 O O   . LYS A 122 ? 0.5195 0.6398 0.5869 -0.1641 0.2289  -0.2151 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.4741 0.6230 0.5848 -0.1158 0.1822  -0.1912 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.6719 0.8525 0.8222 -0.0910 0.1682  -0.1946 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.7986 0.9994 0.9622 -0.0893 0.1588  -0.1942 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.9139 1.1306 1.1000 -0.0632 0.1389  -0.1879 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 1.0071 1.2552 1.2315 -0.0465 0.1382  -0.2039 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.4943 0.5629 0.5135 -0.1529 0.2030  -0.1774 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.5272 0.5634 0.5029 -0.1764 0.2150  -0.1751 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.5979 0.6250 0.5621 -0.1857 0.2300  -0.1847 124 PHE A C   
1081 O O   . PHE A 123 ? 0.6073 0.6252 0.5517 -0.2082 0.2483  -0.1949 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.5554 0.5556 0.4939 -0.1745 0.2002  -0.1525 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.5800 0.5755 0.5107 -0.1788 0.1942  -0.1455 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.5963 0.6232 0.5624 -0.1683 0.1874  -0.1495 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.6416 0.5993 0.5280 -0.1916 0.1936  -0.1341 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.6065 0.6283 0.5648 -0.1729 0.1824  -0.1438 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.6658 0.6165 0.5446 -0.1947 0.1883  -0.1279 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.6107 0.5939 0.5259 -0.1861 0.1834  -0.1332 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.5372 0.5669 0.5139 -0.1695 0.2236  -0.1829 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.5593 0.5826 0.5288 -0.1764 0.2375  -0.1935 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.6237 0.6809 0.6269 -0.1830 0.2564  -0.2192 125 ILE A C   
1092 O O   . ILE A 124 ? 0.6442 0.6937 0.6304 -0.2031 0.2759  -0.2314 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.5825 0.5975 0.5557 -0.1578 0.2259  -0.1852 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.5854 0.5650 0.5187 -0.1584 0.2121  -0.1639 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.6118 0.6276 0.5880 -0.1625 0.2416  -0.2005 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.6604 0.6355 0.6018 -0.1386 0.1966  -0.1530 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.5733 0.6683 0.6234 -0.1666 0.2506  -0.2279 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.5806 0.7156 0.6715 -0.1689 0.2655  -0.2541 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.6558 0.7956 0.7356 -0.1972 0.2849  -0.2672 126 LYS A C   
1100 O O   . LYS A 125 ? 0.6541 0.8115 0.7473 -0.2105 0.3055  -0.2896 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.5944 0.7667 0.7334 -0.1438 0.2505  -0.2578 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.8123 1.0277 0.9998 -0.1372 0.2612  -0.2849 126 LYS A CG  
1103 C CD  . LYS A 125 ? 0.9464 1.1997 1.1776 -0.1153 0.2453  -0.2891 126 LYS A CD  
1104 C CE  . LYS A 125 ? 1.1021 1.4028 1.3837 -0.1096 0.2555  -0.3185 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.2061 1.5454 1.5282 -0.0898 0.2390  -0.3235 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.6143 0.7362 0.6683 -0.2071 0.2792  -0.2539 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.6421 0.7602 0.6784 -0.2352 0.2970  -0.2635 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.7470 0.8299 0.7369 -0.2606 0.3165  -0.2658 127 ALA A C   
1109 O O   . ALA A 126 ? 0.7575 0.8457 0.7423 -0.2850 0.3387  -0.2831 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.6425 0.7430 0.6581 -0.2370 0.2843  -0.2461 127 ALA A CB  
1111 N N   . SER A 127 ? 0.7458 0.7931 0.7013 -0.2557 0.3084  -0.2493 128 SER A N   
1112 C CA  . SER A 127 ? 0.8081 0.8186 0.7147 -0.2777 0.3234  -0.2491 128 SER A CA  
1113 C C   . SER A 127 ? 0.9008 0.9274 0.8234 -0.2827 0.3419  -0.2701 128 SER A C   
1114 O O   . SER A 127 ? 0.9512 0.9537 0.8365 -0.3061 0.3601  -0.2761 128 SER A O   
1115 C CB  . SER A 127 ? 0.8821 0.8491 0.7443 -0.2708 0.3055  -0.2233 128 SER A CB  
1116 O OG  . SER A 127 ? 1.0445 0.9829 0.8719 -0.2788 0.2980  -0.2075 128 SER A OG  
1117 N N   . GLU A 128 ? 0.8259 0.8912 0.8016 -0.2609 0.3376  -0.2817 129 GLU A N   
1118 C CA  . GLU A 128 ? 1.0990 1.1820 1.0957 -0.2622 0.3542  -0.3030 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.6108 1.7272 1.6334 -0.2813 0.3798  -0.3325 129 GLU A C   
1120 O O   . GLU A 128 ? 1.2081 1.3083 1.1987 -0.3095 0.3963  -0.3366 129 GLU A O   
1121 C CB  . GLU A 128 ? 1.0839 1.1890 1.1229 -0.2302 0.3389  -0.3030 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.1758 1.3308 1.2758 -0.2120 0.3342  -0.3177 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.4217 1.5912 1.5569 -0.1783 0.3150  -0.3129 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.3507 1.4899 1.4627 -0.1675 0.3020  -0.2939 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.3164 1.5273 1.5018 -0.1627 0.3127  -0.3285 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.2473 0.4756 0.3045 -0.0554 -0.0175 -0.0834 1   TRP D N   
1130 N N   B TRP B 2   ? 0.2491 0.4774 0.3063 -0.0554 -0.0176 -0.0834 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.2354 0.4641 0.2937 -0.0555 -0.0170 -0.0838 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.2410 0.4696 0.2993 -0.0555 -0.0170 -0.0837 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.2823 0.5104 0.3425 -0.0561 -0.0169 -0.0828 1   TRP D C   
1134 C C   B TRP B 2   ? 0.2796 0.5077 0.3399 -0.0561 -0.0168 -0.0828 1   TRP D C   
1135 O O   A TRP B 2   ? 0.2791 0.5061 0.3395 -0.0561 -0.0175 -0.0821 1   TRP D O   
1136 O O   B TRP B 2   ? 0.2735 0.5005 0.3338 -0.0562 -0.0174 -0.0821 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.2218 0.4505 0.2794 -0.0553 -0.0180 -0.0846 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.2263 0.4549 0.2840 -0.0553 -0.0181 -0.0845 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.2266 0.4559 0.2826 -0.0548 -0.0181 -0.0864 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.2378 0.4660 0.2965 -0.0554 -0.0193 -0.0841 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.2613 0.4904 0.3168 -0.0543 -0.0191 -0.0873 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.2762 0.5042 0.3355 -0.0550 -0.0205 -0.0846 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.2202 0.4505 0.2755 -0.0550 -0.0170 -0.0878 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.2356 0.4640 0.2956 -0.0557 -0.0194 -0.0833 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.2484 0.4783 0.3026 -0.0539 -0.0188 -0.0894 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.2686 0.4970 0.3298 -0.0552 -0.0210 -0.0845 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.2625 0.4932 0.3163 -0.0544 -0.0174 -0.0899 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.2857 0.5144 0.3469 -0.0556 -0.0204 -0.0837 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.2261 0.4569 0.2821 -0.0555 -0.0158 -0.0875 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.2486 0.4770 0.3094 -0.0562 -0.0189 -0.0824 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.2478 0.4795 0.3006 -0.0543 -0.0163 -0.0921 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.2746 0.5042 0.3373 -0.0558 -0.0206 -0.0833 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.2385 0.4701 0.2935 -0.0556 -0.0149 -0.0892 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.2689 0.4976 0.3310 -0.0563 -0.0195 -0.0818 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.2503 0.4824 0.3035 -0.0550 -0.0149 -0.0916 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.2752 0.5047 0.3380 -0.0561 -0.0202 -0.0823 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.2267 0.4554 0.2888 -0.0565 -0.0161 -0.0828 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.2214 0.4495 0.2860 -0.0569 -0.0162 -0.0824 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.2494 0.4773 0.3156 -0.0570 -0.0166 -0.0818 2   VAL D C   
1160 O O   . VAL B 3   ? 0.2258 0.4543 0.2914 -0.0569 -0.0164 -0.0819 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2572 0.4865 0.3242 -0.0579 -0.0150 -0.0832 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2580 0.4876 0.3229 -0.0584 -0.0147 -0.0832 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2533 0.4847 0.3225 -0.0581 -0.0138 -0.0842 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.2158 0.4430 0.2842 -0.0572 -0.0173 -0.0813 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.2194 0.4464 0.2902 -0.0573 -0.0180 -0.0804 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.2616 0.4892 0.3368 -0.0578 -0.0171 -0.0814 3   ILE D C   
1167 O O   . ILE B 4   ? 0.2484 0.4762 0.3259 -0.0582 -0.0168 -0.0826 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.2413 0.4675 0.3130 -0.0572 -0.0193 -0.0796 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.2326 0.4594 0.3011 -0.0569 -0.0199 -0.0793 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.2504 0.4762 0.3249 -0.0575 -0.0206 -0.0782 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.2759 0.5040 0.3417 -0.0573 -0.0204 -0.0788 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.2524 0.4808 0.3292 -0.0580 -0.0165 -0.0814 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.2592 0.4893 0.3417 -0.0585 -0.0155 -0.0830 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.3082 0.5375 0.3964 -0.0589 -0.0168 -0.0829 4   PRO D C   
1175 O O   . PRO B 5   ? 0.3013 0.5287 0.3892 -0.0586 -0.0185 -0.0807 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.2772 0.5084 0.3601 -0.0584 -0.0144 -0.0830 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.3278 0.5569 0.4065 -0.0582 -0.0158 -0.0808 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.2740 0.5024 0.3483 -0.0579 -0.0166 -0.0805 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.2758 0.5071 0.3699 -0.0597 -0.0159 -0.0853 5   ALA D N   
# 
