data_7GUE
# 
_entry.id   7GUE 
# 
_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   7GUE         pdb_00007gue 10.2210/pdb7gue/pdb 
WWPDB D_1001406649 ?            ?                   
# 
_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                        7GUE 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              Rob.vanMontfort@icr.ac.uk 
_pdbx_contact_author.name_first         Rob 
_pdbx_contact_author.name_last          'van Montfort' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodrigues, M.J.'      1 0000-0003-1243-903X 
'Le Bihan, Y.V.'       2 0000-0002-6850-9706 
'van Montfort, R.L.M.' 3 0000-0002-5688-3450 
# 
_citation.id                        primary 
_citation.title                     
'Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.' 
_citation.journal_abbrev            J.Appl.Crystallogr. 
_citation.journal_volume            57 
_citation.page_first                1951 
_citation.page_last                 1965 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39628887 
_citation.pdbx_database_id_DOI      10.1107/S1600576724010549 
_citation.journal_id_ASTM           JACGAR 
_citation.country                   DK 
_citation.journal_id_ISSN           0021-8898 
_citation.journal_id_CSD            0228 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodrigues, M.J.'      1 0000-0003-1243-903X 
primary 'Cabry, M.'            2 0000-0002-9070-5498 
primary 'Collie, G.'           3 0000-0002-0406-922X 
primary 'Carter, M.'           4 ?                   
primary 'McAndrew, C.'         5 0000-0002-1366-088X 
primary 'Owen, R.L.'           6 0000-0002-2104-7057 
primary 'Bellenie, B.R.'       7 0000-0001-9987-3079 
primary 'Le Bihan, Y.V.'       8 0000-0002-6850-9706 
primary 'van Montfort, R.L.M.' 9 0000-0002-5688-3450 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'B-cell lymphoma 6 protein'                                   14536.915 1   ? ? ? ? 
2 polymer     syn 'WVIP tetrapeptide'                                           610.744   1   ? ? ? ? 
3 non-polymer syn '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' 260.679   1   ? ? ? ? 
4 non-polymer nat 'CHLORIDE ION'                                                35.453    1   ? ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                          78.133    1   ? ? ? ? 
6 water       nat water                                                         18.015    181 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'BCL-6,B-cell lymphoma 5 protein,BCL-5,Protein LAZ-3,Zinc finger and BTB domain-containing protein 27,Zinc finger protein 51' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
A ? 
2 'polypeptide(L)' no yes '(ACE)WVIPA' XWVIPA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' 7ZO 
4 'CHLORIDE ION'                                                CL  
5 'DIMETHYL SULFOXIDE'                                          DMS 
6 water                                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   ALA n 
1 5   ASP n 
1 6   SER n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  PHE n 
1 11  THR n 
1 12  ARG n 
1 13  HIS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  LEU n 
1 19  LEU n 
1 20  ASN n 
1 21  LEU n 
1 22  ASN n 
1 23  ARG n 
1 24  LEU n 
1 25  ARG n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  THR n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  ILE n 
1 36  VAL n 
1 37  VAL n 
1 38  SER n 
1 39  ARG n 
1 40  GLU n 
1 41  GLN n 
1 42  PHE n 
1 43  ARG n 
1 44  ALA n 
1 45  HIS n 
1 46  LYS n 
1 47  THR n 
1 48  VAL n 
1 49  LEU n 
1 50  MET n 
1 51  ALA n 
1 52  CYS n 
1 53  SER n 
1 54  GLY n 
1 55  LEU n 
1 56  PHE n 
1 57  TYR n 
1 58  SER n 
1 59  ILE n 
1 60  PHE n 
1 61  THR n 
1 62  ASP n 
1 63  GLN n 
1 64  LEU n 
1 65  LYS n 
1 66  CYS n 
1 67  ASN n 
1 68  LEU n 
1 69  SER n 
1 70  VAL n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ASP n 
1 75  PRO n 
1 76  GLU n 
1 77  ILE n 
1 78  ASN n 
1 79  PRO n 
1 80  GLU n 
1 81  GLY n 
1 82  PHE n 
1 83  CYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  ASP n 
1 88  PHE n 
1 89  MET n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ARG n 
1 94  LEU n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLU n 
1 99  GLY n 
1 100 ASN n 
1 101 ILE n 
1 102 MET n 
1 103 ALA n 
1 104 VAL n 
1 105 MET n 
1 106 ALA n 
1 107 THR n 
1 108 ALA n 
1 109 MET n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 MET n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 VAL n 
1 118 ASP n 
1 119 THR n 
1 120 CYS n 
1 121 ARG n 
1 122 LYS n 
1 123 PHE n 
1 124 ILE n 
1 125 LYS n 
1 126 ALA n 
1 127 SER n 
1 128 GLU n 
2 1   ACE n 
2 2   TRP n 
2 3   VAL n 
2 4   ILE n 
2 5   PRO n 
2 6   ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCL6, BCL5, LAZ3, ZBTB27, ZNF51' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21-AI 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET48b 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 6 'synthetic construct' ? 32630 ? 
3 2 sample ? ? 'synthetic construct' ? 32630 ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
7ZO non-polymer         . '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' ? 'C12 H9 Cl N4 O' 260.679 
ACE non-polymer         . 'ACETYL GROUP'                                                ? 'C2 H4 O'        44.053  
ALA 'L-peptide linking' y ALANINE                                                       ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                      ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                    ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                               ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'                                                ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                                                      ? 'C3 H7 N O2 S'   121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                          ? 'C2 H6 O S'      78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                     ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                               ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                       ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                     ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                         ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                    ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                       ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                        ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                    ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                 ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                       ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                        ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                     ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                    ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                      ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                        ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLY 3   4   ?   ?   ?   A . n 
A 1 4   ALA 4   5   ?   ?   ?   A . n 
A 1 5   ASP 5   6   6   ASP ASP A . n 
A 1 6   SER 6   7   7   SER SER A . n 
A 1 7   CYS 7   8   8   CYS CYS A . n 
A 1 8   ILE 8   9   9   ILE ILE A . n 
A 1 9   GLN 9   10  10  GLN GLN A . n 
A 1 10  PHE 10  11  11  PHE PHE A . n 
A 1 11  THR 11  12  12  THR THR A . n 
A 1 12  ARG 12  13  13  ARG ARG A . n 
A 1 13  HIS 13  14  14  HIS HIS A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ASP 16  17  17  ASP ASP A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  ASN 20  21  21  ASN ASN A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  ARG 23  24  24  ARG ARG A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  ARG 25  26  26  ARG ARG A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  THR 31  32  32  THR THR A . n 
A 1 32  ASP 32  33  33  ASP ASP A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  VAL 36  37  37  VAL VAL A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  SER 38  39  39  SER SER A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLN 41  42  42  GLN GLN A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  ALA 44  45  45  ALA ALA A . n 
A 1 45  HIS 45  46  46  HIS HIS A . n 
A 1 46  LYS 46  47  47  LYS LYS A . n 
A 1 47  THR 47  48  48  THR THR A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  MET 50  51  51  MET MET A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  CYS 52  53  53  CYS CYS A . n 
A 1 53  SER 53  54  54  SER SER A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  PHE 60  61  61  PHE PHE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  ASN 67  68  68  ASN ASN A . n 
A 1 68  LEU 68  69  69  LEU LEU A . n 
A 1 69  SER 69  70  70  SER SER A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ILE 71  72  72  ILE ILE A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  ASP 74  75  75  ASP ASP A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLU 76  77  77  GLU GLU A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  PRO 79  80  80  PRO PRO A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  CYS 83  84  84  CYS CYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  LEU 85  86  86  LEU LEU A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  PHE 88  89  89  PHE PHE A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  ASN 95  96  96  ASN ASN A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ARG 97  98  98  ARG ARG A . n 
A 1 98  GLU 98  99  99  GLU GLU A . n 
A 1 99  GLY 99  100 100 GLY GLY A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 MET 102 103 103 MET MET A . n 
A 1 103 ALA 103 104 104 ALA ALA A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 MET 105 106 106 MET MET A . n 
A 1 106 ALA 106 107 107 ALA ALA A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 MET 109 110 110 MET MET A . n 
A 1 110 TYR 110 111 111 TYR TYR A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLN 112 113 113 GLN GLN A . n 
A 1 113 MET 113 114 114 MET MET A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 HIS 115 116 116 HIS HIS A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 VAL 117 118 118 VAL VAL A . n 
A 1 118 ASP 118 119 119 ASP ASP A . n 
A 1 119 THR 119 120 120 THR THR A . n 
A 1 120 CYS 120 121 121 CYS CYS A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 PHE 123 124 124 PHE PHE A . n 
A 1 124 ILE 124 125 125 ILE ILE A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 SER 127 128 128 SER SER A . n 
A 1 128 GLU 128 129 129 GLU GLU A . n 
B 2 1   ACE 1   0   0   ACE ACE D . n 
B 2 2   TRP 2   1   1   TRP TRP D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ILE 4   3   3   ILE ILE D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   ALA 6   5   5   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 7ZO 1   201 1   7ZO 375 A . 
D 4 CL  1   202 1   CL  CL  A . 
E 5 DMS 1   101 1   DMS DMS D . 
F 6 HOH 1   301 42  HOH HOH A . 
F 6 HOH 2   302 15  HOH HOH A . 
F 6 HOH 3   303 81  HOH HOH A . 
F 6 HOH 4   304 166 HOH HOH A . 
F 6 HOH 5   305 88  HOH HOH A . 
F 6 HOH 6   306 159 HOH HOH A . 
F 6 HOH 7   307 84  HOH HOH A . 
F 6 HOH 8   308 149 HOH HOH A . 
F 6 HOH 9   309 92  HOH HOH A . 
F 6 HOH 10  310 23  HOH HOH A . 
F 6 HOH 11  311 32  HOH HOH A . 
F 6 HOH 12  312 187 HOH HOH A . 
F 6 HOH 13  313 189 HOH HOH A . 
F 6 HOH 14  314 87  HOH HOH A . 
F 6 HOH 15  315 85  HOH HOH A . 
F 6 HOH 16  316 130 HOH HOH A . 
F 6 HOH 17  317 230 HOH HOH A . 
F 6 HOH 18  318 114 HOH HOH A . 
F 6 HOH 19  319 83  HOH HOH A . 
F 6 HOH 20  320 14  HOH HOH A . 
F 6 HOH 21  321 113 HOH HOH A . 
F 6 HOH 22  322 5   HOH HOH A . 
F 6 HOH 23  323 143 HOH HOH A . 
F 6 HOH 24  324 196 HOH HOH A . 
F 6 HOH 25  325 103 HOH HOH A . 
F 6 HOH 26  326 135 HOH HOH A . 
F 6 HOH 27  327 24  HOH HOH A . 
F 6 HOH 28  328 97  HOH HOH A . 
F 6 HOH 29  329 100 HOH HOH A . 
F 6 HOH 30  330 134 HOH HOH A . 
F 6 HOH 31  331 13  HOH HOH A . 
F 6 HOH 32  332 109 HOH HOH A . 
F 6 HOH 33  333 44  HOH HOH A . 
F 6 HOH 34  334 33  HOH HOH A . 
F 6 HOH 35  335 3   HOH HOH A . 
F 6 HOH 36  336 112 HOH HOH A . 
F 6 HOH 37  337 165 HOH HOH A . 
F 6 HOH 38  338 50  HOH HOH A . 
F 6 HOH 39  339 94  HOH HOH A . 
F 6 HOH 40  340 63  HOH HOH A . 
F 6 HOH 41  341 90  HOH HOH A . 
F 6 HOH 42  342 141 HOH HOH A . 
F 6 HOH 43  343 213 HOH HOH A . 
F 6 HOH 44  344 11  HOH HOH A . 
F 6 HOH 45  345 246 HOH HOH A . 
F 6 HOH 46  346 184 HOH HOH A . 
F 6 HOH 47  347 110 HOH HOH A . 
F 6 HOH 48  348 86  HOH HOH A . 
F 6 HOH 49  349 115 HOH HOH A . 
F 6 HOH 50  350 18  HOH HOH A . 
F 6 HOH 51  351 180 HOH HOH A . 
F 6 HOH 52  352 136 HOH HOH A . 
F 6 HOH 53  353 51  HOH HOH A . 
F 6 HOH 54  354 192 HOH HOH A . 
F 6 HOH 55  355 121 HOH HOH A . 
F 6 HOH 56  356 101 HOH HOH A . 
F 6 HOH 57  357 119 HOH HOH A . 
F 6 HOH 58  358 102 HOH HOH A . 
F 6 HOH 59  359 117 HOH HOH A . 
F 6 HOH 60  360 116 HOH HOH A . 
F 6 HOH 61  361 35  HOH HOH A . 
F 6 HOH 62  362 74  HOH HOH A . 
F 6 HOH 63  363 95  HOH HOH A . 
F 6 HOH 64  364 231 HOH HOH A . 
F 6 HOH 65  365 89  HOH HOH A . 
F 6 HOH 66  366 6   HOH HOH A . 
F 6 HOH 67  367 105 HOH HOH A . 
F 6 HOH 68  368 147 HOH HOH A . 
F 6 HOH 69  369 20  HOH HOH A . 
F 6 HOH 70  370 62  HOH HOH A . 
F 6 HOH 71  371 151 HOH HOH A . 
F 6 HOH 72  372 150 HOH HOH A . 
F 6 HOH 73  373 49  HOH HOH A . 
F 6 HOH 74  374 25  HOH HOH A . 
F 6 HOH 75  375 26  HOH HOH A . 
F 6 HOH 76  376 66  HOH HOH A . 
F 6 HOH 77  377 164 HOH HOH A . 
F 6 HOH 78  378 29  HOH HOH A . 
F 6 HOH 79  379 123 HOH HOH A . 
F 6 HOH 80  380 178 HOH HOH A . 
F 6 HOH 81  381 22  HOH HOH A . 
F 6 HOH 82  382 107 HOH HOH A . 
F 6 HOH 83  383 244 HOH HOH A . 
F 6 HOH 84  384 238 HOH HOH A . 
F 6 HOH 85  385 60  HOH HOH A . 
F 6 HOH 86  386 168 HOH HOH A . 
F 6 HOH 87  387 57  HOH HOH A . 
F 6 HOH 88  388 39  HOH HOH A . 
F 6 HOH 89  389 28  HOH HOH A . 
F 6 HOH 90  390 82  HOH HOH A . 
F 6 HOH 91  391 10  HOH HOH A . 
F 6 HOH 92  392 99  HOH HOH A . 
F 6 HOH 93  393 203 HOH HOH A . 
F 6 HOH 94  394 40  HOH HOH A . 
F 6 HOH 95  395 104 HOH HOH A . 
F 6 HOH 96  396 21  HOH HOH A . 
F 6 HOH 97  397 193 HOH HOH A . 
F 6 HOH 98  398 239 HOH HOH A . 
F 6 HOH 99  399 93  HOH HOH A . 
F 6 HOH 100 400 171 HOH HOH A . 
F 6 HOH 101 401 242 HOH HOH A . 
F 6 HOH 102 402 56  HOH HOH A . 
F 6 HOH 103 403 36  HOH HOH A . 
F 6 HOH 104 404 53  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 45  HOH HOH A . 
F 6 HOH 108 408 30  HOH HOH A . 
F 6 HOH 109 409 37  HOH HOH A . 
F 6 HOH 110 410 52  HOH HOH A . 
F 6 HOH 111 411 38  HOH HOH A . 
F 6 HOH 112 412 17  HOH HOH A . 
F 6 HOH 113 413 167 HOH HOH A . 
F 6 HOH 114 414 176 HOH HOH A . 
F 6 HOH 115 415 54  HOH HOH A . 
F 6 HOH 116 416 79  HOH HOH A . 
F 6 HOH 117 417 209 HOH HOH A . 
F 6 HOH 118 418 55  HOH HOH A . 
F 6 HOH 119 419 96  HOH HOH A . 
F 6 HOH 120 420 69  HOH HOH A . 
F 6 HOH 121 421 237 HOH HOH A . 
F 6 HOH 122 422 186 HOH HOH A . 
F 6 HOH 123 423 241 HOH HOH A . 
F 6 HOH 124 424 200 HOH HOH A . 
F 6 HOH 125 425 148 HOH HOH A . 
F 6 HOH 126 426 31  HOH HOH A . 
F 6 HOH 127 427 146 HOH HOH A . 
F 6 HOH 128 428 145 HOH HOH A . 
F 6 HOH 129 429 43  HOH HOH A . 
F 6 HOH 130 430 98  HOH HOH A . 
F 6 HOH 131 431 185 HOH HOH A . 
F 6 HOH 132 432 153 HOH HOH A . 
F 6 HOH 133 433 191 HOH HOH A . 
F 6 HOH 134 434 106 HOH HOH A . 
F 6 HOH 135 435 139 HOH HOH A . 
F 6 HOH 136 436 76  HOH HOH A . 
F 6 HOH 137 437 188 HOH HOH A . 
F 6 HOH 138 438 158 HOH HOH A . 
F 6 HOH 139 439 232 HOH HOH A . 
F 6 HOH 140 440 80  HOH HOH A . 
F 6 HOH 141 441 204 HOH HOH A . 
F 6 HOH 142 442 137 HOH HOH A . 
F 6 HOH 143 443 111 HOH HOH A . 
F 6 HOH 144 444 108 HOH HOH A . 
F 6 HOH 145 445 70  HOH HOH A . 
F 6 HOH 146 446 140 HOH HOH A . 
F 6 HOH 147 447 169 HOH HOH A . 
F 6 HOH 148 448 247 HOH HOH A . 
F 6 HOH 149 449 221 HOH HOH A . 
F 6 HOH 150 450 206 HOH HOH A . 
F 6 HOH 151 451 228 HOH HOH A . 
F 6 HOH 152 452 161 HOH HOH A . 
F 6 HOH 153 453 215 HOH HOH A . 
F 6 HOH 154 454 243 HOH HOH A . 
F 6 HOH 155 455 212 HOH HOH A . 
F 6 HOH 156 456 131 HOH HOH A . 
F 6 HOH 157 457 142 HOH HOH A . 
F 6 HOH 158 458 183 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 65  HOH HOH A . 
F 6 HOH 162 462 170 HOH HOH A . 
F 6 HOH 163 463 175 HOH HOH A . 
F 6 HOH 164 464 245 HOH HOH A . 
F 6 HOH 165 465 179 HOH HOH A . 
F 6 HOH 166 466 152 HOH HOH A . 
F 6 HOH 167 467 181 HOH HOH A . 
F 6 HOH 168 468 195 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 172 472 144 HOH HOH A . 
F 6 HOH 173 473 225 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           7GUE 
_cell.length_a           67.550 
_cell.length_b           67.550 
_cell.length_c           166.080 
_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                         7GUE 
_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          7GUE 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.61 
_exptl_crystal.density_percent_sol   65.93 
_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                     7GUE 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.860 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   21696 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.129 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.400 
_reflns.B_iso_Wilson_estimate        26.260 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.137 
_reflns.pdbx_Rpim_I_all              0.045 
_reflns.pdbx_CC_half                 0.990 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     198174 
_reflns.pdbx_scaling_rejects         246 
_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  ? 11578 1245 ? 0.596 ? ? ? 9.300 ? 3.600  ? ? ? ? ? ? 100.000 0.631 0.205 0.934 ? 
1 2 9.000 33.860 ? 1654  240  ? 0.147 ? ? ? 6.900 ? 14.700 ? ? ? ? ? ? 98.800  0.158 0.056 0.989 ? 
# 
_refine.entry_id                                 7GUE 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8000 
_refine.ls_d_res_low                             33.8600 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    100.0000 
_refine.ls_number_reflns_obs                     21624 
_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                          0.1840 
_refine.ls_R_factor_R_work                       0.1830 
_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                 5.2100 
_refine.ls_number_reflns_R_free                  1126 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               31.1600 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.5495 
_refine.aniso_B[2][2]                            -0.5495 
_refine.aniso_B[3][3]                            1.0990 
_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               0.9550 
_refine.correlation_coeff_Fo_to_Fc_free          0.9470 
_refine.overall_SU_R_Cruickshank_DPI             0.0960 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0930 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1100 
_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                                116.380 
_refine.B_iso_min                                14.200 
_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                        7GUE 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.200 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.8000 
_refine_hist.d_res_low                        33.8600 
_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           25.89 
_refine_hist.pdbx_B_iso_mean_solvent          46.89 
_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      1651 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1236 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1693 0.910  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.420  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    16.170 ? ?      ?            
# 
_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               99.8200 
_refine_ls_shell.number_reflns_R_work             2687 
_refine_ls_shell.R_factor_all                     0.2613 
_refine_ls_shell.R_factor_R_work                  0.2615 
_refine_ls_shell.R_factor_R_free                  0.2579 
_refine_ls_shell.percent_reflns_R_free            4.6500 
_refine_ls_shell.number_reflns_R_free             131 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2818 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUE 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 3.02 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUE 
_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 7GUE       7GUE   ? 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 7GUE A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUE D 1 ? 6   ? 7GUE   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 7GUE GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUE PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUE 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)' 6380  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  13250 ? 
# 
_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 33.7750000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5000160256 0.0000000000 0.0000000000 -1.0000000000 27.6800000000 
# 
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                   7GUE 
_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 37.10 48.82   
2 1 SER A 39  ? B 61.60 -108.71 
3 1 SER A 93  ? ? 76.08 -0.64   
4 1 SER A 93  ? ? 76.08 -2.33   
5 1 GLN A 113 ? ? 62.85 63.32   
# 
_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   11.01 
# 
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 337 ? F HOH . 
2 1 A HOH 377 ? F HOH . 
3 1 A HOH 447 ? F HOH . 
4 1 A HOH 463 ? F HOH . 
5 1 A HOH 465 ? F HOH . 
6 1 A HOH 468 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.2805 -16.6200 24.3685 0.0039  -0.0525 -0.0760 -0.0388 0.0245  -0.0161 0.9648 1.8534  2.1354 
0.3969 -0.2906 1.1785 0.1349 -0.0894 -0.0455 -0.0538 0.0881 0.0678 0.2576  0.0141 -0.0537 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.0947 0.1179  -0.0575 -0.0466 -0.0196 -0.0797 1.0296 -0.1655 0.0000 
0.1539 -0.0952 0.5129 0.0169 0.0087  -0.0256 -0.0061 0.0307 0.0500 -0.0020 0.0213 0.0099  
# 
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                    7GUE 
_atom_sites.fract_transf_matrix[1][1]   0.014804 
_atom_sites.fract_transf_matrix[1][2]   0.008547 
_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]   0.017094 
_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]   0.006021 
_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   ? 17.534 -21.135 -4.885 1.00 61.49  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.385 -22.052 -5.646 1.00 60.52  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.886 -23.510 -5.538 1.00 60.40  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.810 -23.762 -4.984 1.00 61.03  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.856 -21.935 -5.172 1.00 61.36  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.888 -22.020 -6.289 1.00 75.16  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 20.941 -23.069 -6.977 1.00 75.96  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.653 -21.045 -6.465 1.00 81.93  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.663 -24.459 -6.088 1.00 51.78  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.378 -25.890 -6.055 1.00 49.23  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.378 -26.622 -5.106 1.00 45.24  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.690 -27.796 -5.316 1.00 45.17  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.435 -26.465 -7.466 1.00 54.89  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.709 -26.271 -8.060 1.00 66.53  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.854 -25.934 -4.052 1.00 35.33  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.801 -26.531 -3.098 1.00 31.66  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.173 -27.693 -2.303 1.00 32.59  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.958 -27.728 -2.111 1.00 32.58  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.327 -25.463 -2.136 1.00 32.01  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.443 -24.238 -2.885 1.00 36.69  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.007 -28.609 -1.810 1.00 24.72  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.631 -29.609 -0.807 1.00 22.17  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.243 -29.068 0.490  1.00 23.90  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.188 -28.278 0.431  1.00 22.82  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 21.013 -31.081 -1.123 1.00 25.46  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.538 -31.238 -1.410 1.00 25.81  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.148 -31.615 -2.281 1.00 26.86  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.070 -32.689 -1.554 1.00 27.84  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.757 -29.502 1.654  0.57 19.07  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.664 -29.432 1.638  0.43 18.92  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.287 -28.999 2.920  0.57 18.14  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.103 -28.959 2.947  0.43 17.69  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.622 -30.128 3.892  0.57 22.19  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.566 -30.111 3.828  0.43 20.51  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.818 -31.046 4.060  0.57 22.50  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.944 -31.173 3.837  0.43 20.32  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.267 -28.018 3.548  0.57 19.55  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.952 -28.175 3.632  0.43 18.91  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.717 -27.392 4.873  0.57 19.84  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.163 -27.885 5.141  0.43 26.25  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.589 -26.674 5.571  0.57 47.18  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.102 -26.429 5.536  0.43 35.58  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.604 -27.275 6.012  0.57 38.84  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.771 -25.536 4.739  0.43 23.71  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.713 -25.364 5.692  0.57 50.20  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.421 -26.160 6.799  0.43 24.07  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.792 -30.049 4.550  0.78 19.51  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.639 -29.883 4.590  0.22 17.11  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.168 -31.054 5.543  0.78 19.34  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.147 -30.853 5.546  0.22 16.87  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.688 -30.550 6.906  0.78 21.19  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.610 -30.412 6.890  0.22 20.40  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.247 -29.588 7.451  0.78 20.12  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 23.022 -29.362 7.401  0.22 19.21  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.689 -31.362 5.512  0.78 20.64  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.682 -30.910 5.491  0.22 18.08  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.066 -32.556 6.363  0.78 21.45  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.159 -31.834 4.397  0.22 20.13  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.675 -33.845 6.002  0.78 24.49  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 25.057 -31.468 3.058  0.22 23.75  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.829 -32.396 7.515  0.78 23.13  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.660 -33.092 4.700  0.22 23.36  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 25.010 -34.948 6.804  0.78 25.60  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.485 -32.328 2.047  0.22 25.14  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.156 -33.494 8.317  0.78 24.96  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.070 -33.959 3.684  0.22 26.84  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.752 -34.761 7.956  0.78 23.14  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 25.997 -33.563 2.369  0.22 24.90  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.603 -31.148 7.407  1.00 17.87  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.927 -30.766 8.665  1.00 18.04  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.882 -30.510 9.867  1.00 21.49  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.749 -29.482 10.550 1.00 20.70  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.859 -31.814 9.023  1.00 24.48  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.914 -31.905 7.938  1.00 24.84  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.109 -31.465 10.315 1.00 29.28  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.829 -31.433 10.097 0.50 18.85  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.822 -31.435 10.109 0.50 19.11  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.753 -31.365 11.242 0.50 18.65  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.743 -31.353 11.256 0.50 18.99  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 24.997 -30.483 11.038 0.50 20.43  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 24.983 -30.463 11.051 0.50 20.52  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.820 -30.395 11.956 0.50 19.24  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.791 -30.351 11.981 0.50 19.28  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.186 -32.790 11.659 0.50 22.14  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.181 -32.770 11.666 0.50 23.18  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.062 -33.687 12.206 0.50 30.42  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.200 -33.488 12.596 0.50 34.90  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.511 -33.218 13.544 0.50 40.14  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 22.910 -34.921 12.181 0.50 44.20  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.460 -33.394 14.645 0.50 47.36  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.120 -35.715 11.939 0.50 47.49  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.391 -32.749 15.806 0.50 54.53  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.322 -36.457 10.853 0.50 55.95  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.433 -31.856 16.023 0.50 36.41  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.444 -37.151 10.716 0.50 48.19  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.285 -32.984 16.755 0.50 42.93  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.398 -36.522 9.903  0.50 31.57  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.149 -29.847 9.859  1.00 16.76  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.360 -29.050 9.547  1.00 16.40  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.652 -27.943 10.558 1.00 18.90  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.791 -27.856 11.046 1.00 18.06  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.335 -28.480 8.118  1.00 16.39  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.606 -27.735 7.799  1.00 17.95  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.783 -28.408 7.581  1.00 18.59  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.834 -26.405 7.684  1.00 18.85  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.700 -27.483 7.339  1.00 18.02  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.173 -26.259 7.378  1.00 18.03  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.658 -27.076 10.835 1.00 16.43  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.870 -25.946 11.764 1.00 16.07  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.279 -26.435 13.159 1.00 18.27  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.189 -25.852 13.759 1.00 15.91  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.625 -25.059 11.829 1.00 17.30  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.622 -27.489 13.663 0.38 15.77  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.625 -27.497 13.661 0.33 16.19  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.620 -27.493 13.673 0.29 15.96  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.925 -28.064 14.973 0.38 15.73  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.919 -28.087 14.970 0.33 16.39  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.935 -28.053 14.991 0.29 16.05  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.338 -28.655 15.006 0.38 19.66  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.330 -28.670 15.011 0.33 20.16  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.331 -28.684 15.025 0.29 20.17  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.060 -28.438 15.983 0.38 17.14  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.043 -28.463 15.996 0.33 18.03  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.044 -28.509 16.015 0.29 18.35  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.883 -29.114 15.352 0.38 18.36  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.890 -29.160 15.319 0.33 19.92  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.859 -29.039 15.448 0.29 19.23  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.168 -29.661 16.628 0.38 19.44  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.586 -28.610 15.385 0.33 24.81  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.772 -30.175 14.604 0.29 23.33  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.738 -29.373 13.933 1.00 18.09  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.077 -29.986 13.825 1.00 18.56  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.137 -28.884 13.774 1.00 18.71  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.208 -29.044 14.361 1.00 18.40  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.174 -30.857 12.566 1.00 19.70  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.427 -32.182 12.643 1.00 26.74  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.880 -32.501 13.727 1.00 26.70  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.388 -32.893 11.626 1.00 27.22  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.844 -27.767 13.058 1.00 14.51  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.784 -26.632 13.021 1.00 14.20  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 30.974 -26.075 14.439 1.00 17.23  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.100 -25.868 14.876 1.00 16.40  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.308 -25.515 12.047 1.00 16.27  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.079 -24.205 12.277 1.00 16.35  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.406 -25.975 10.588 1.00 15.46  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.868 -25.856 15.159 1.00 15.25  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 29.971 -25.271 16.493 1.00 15.73  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.724 -26.207 17.445 1.00 18.57  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.564 -25.732 18.231 1.00 16.32  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.584 -24.921 17.044 1.00 16.47  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.601 -23.977 18.275 1.00 19.53  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.116 -22.578 17.905 1.00 19.52  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.204 -23.872 18.870 1.00 23.81  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.454 -27.522 17.341 1.00 17.30  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.128 -28.551 18.153 1.00 18.42  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.642 -28.481 17.908 1.00 19.14  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.433 -28.465 18.869 1.00 18.03  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.573 -29.945 17.800 1.00 20.51  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.161 -31.117 18.562 1.00 28.77  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.714 -31.079 20.028 1.00 31.10  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.709 -32.427 17.933 1.00 33.45  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.045 -28.374 16.630 1.00 16.18  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.465 -28.250 16.282 1.00 16.39  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.084 -26.937 16.777 1.00 18.22  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.238 -26.947 17.214 1.00 17.62  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.674 -28.465 14.794 1.00 17.41  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.623 -29.937 14.436 1.00 28.14  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.806 -30.808 15.293 1.00 22.93  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.349 -30.255 13.178 1.00 20.57  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.334 -25.816 16.704 1.00 16.13  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.806 -24.529 17.238 1.00 15.38  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.027 -24.677 18.741 1.00 17.55  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.022 -24.171 19.273 1.00 15.65  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.813 -23.374 16.940 1.00 14.72  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.739 -23.017 15.437 1.00 17.02  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.636 -21.973 15.177 1.00 16.80  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.112 -22.532 14.879 1.00 19.72  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.101 -25.376 19.438 1.00 15.28  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.288 -25.579 20.883 1.00 15.98  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.518 -26.477 21.183 1.00 20.18  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.227 -26.234 22.160 1.00 19.78  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.035 -26.138 21.523 1.00 18.39  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.062 -26.015 23.033 1.00 24.76  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.573 -25.037 23.594 1.00 21.54  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.512 -27.003 23.697 1.00 25.30  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.790 -27.495 20.326 1.00 17.64  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 36.986 -28.343 20.491 1.00 18.83  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.255 -27.496 20.326 1.00 22.52  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.209 -27.681 21.076 1.00 22.44  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 36.995 -29.484 19.466 1.00 18.15  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 36.016 -30.600 19.800 1.00 24.34  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.695 -31.443 18.576 1.00 28.25  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.854 -32.585 18.929 1.00 36.08  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.353 -33.455 18.060 1.00 53.18  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.561 -33.300 16.755 1.00 40.45  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.627 -34.480 18.484 1.00 41.81  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.254 -26.533 19.369 1.00 19.19  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.402 -25.642 19.206 1.00 18.29  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.557 -24.777 20.457 1.00 21.84  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.687 -24.620 20.951 1.00 22.32  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.239 -24.739 17.991 1.00 17.36  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.204 -25.439 16.611 1.00 20.46  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.053 -24.390 15.493 1.00 20.39  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.471 -26.300 16.382 1.00 22.31  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.427 -24.258 20.997 1.00 18.55  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.489 -23.459 22.237 1.00 19.05  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.119 -24.280 23.403 1.00 23.86  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.010 -23.758 24.114 1.00 23.20  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.087 -22.962 22.645 1.00 19.50  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.185 -22.048 23.879 1.00 24.33  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.874 -21.428 24.258 1.00 26.03  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.864 -22.419 24.621 1.00 23.93  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.245 -22.470 25.797 1.00 36.78  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.594 -21.640 26.778 1.00 31.29  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.298 -23.369 26.014 1.00 25.37  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.641 -25.523 23.597 0.40 22.15  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.644 -25.525 23.611 0.35 21.68  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.644 -25.529 23.604 0.25 21.30  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.109 -26.444 24.641 0.40 23.74  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.121 -26.406 24.689 0.35 23.02  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.102 -26.446 24.660 0.25 22.49  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.618 -26.624 24.576 0.40 28.14  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.617 -26.715 24.588 0.35 27.98  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.602 -26.734 24.579 0.25 27.69  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.292 -26.578 25.608 0.40 28.76  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.278 -26.865 25.617 0.35 28.72  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.250 -26.899 25.615 0.25 28.40  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.451 -27.811 24.478 0.40 28.06  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.302 -27.692 24.746 0.35 26.36  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.312 -27.752 24.613 0.25 25.54  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.082 -27.806 24.842 0.40 36.60  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.610 -28.586 23.688 0.35 31.78  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.767 -28.686 25.580 0.25 31.57  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.145 -26.803 23.353 1.00 24.17  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.568 -27.062 23.108 1.00 26.17  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.386 -25.779 22.919 1.00 28.31  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.598 -25.847 22.673 1.00 29.77  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.711 -28.020 21.929 1.00 28.46  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 41.954 -29.326 22.158 1.00 37.67  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 41.969 -30.197 20.933 1.00 44.32  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.306 -30.739 20.694 1.00 59.85  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.819 -30.934 19.488 1.00 75.69  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.040 -31.431 19.353 1.00 65.89  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.120 -30.630 18.408 1.00 61.68  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.727 -24.614 23.073 1.00 23.10  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.318 -23.276 22.935 1.00 23.30  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 43.941 -23.085 21.532 1.00 27.53  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.012 -22.487 21.380 1.00 27.96  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.350 -22.995 24.067 1.00 26.37  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.662 -21.531 24.239 1.00 32.66  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.747 -20.700 24.037 1.00 31.80  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.818 -21.210 24.577 1.00 36.29  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.273 -23.627 20.513 1.00 22.29  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.759 -23.541 19.137 1.00 21.74  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.160 -22.344 18.425 1.00 24.63  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 41.926 -22.216 18.330 1.00 21.62  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.527 -24.855 18.345 1.00 24.42  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.343 -26.037 18.950 1.00 26.08  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.863 -24.665 16.846 1.00 23.24  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.832 -27.415 18.441 1.00 27.47  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.042 -21.464 17.915 0.54 22.33  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.049 -21.466 17.916 0.46 23.15  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.696 -20.258 17.156 0.54 21.29  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.737 -20.246 17.167 0.46 22.67  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.816 -19.251 17.916 0.54 23.11  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.831 -19.251 17.914 0.46 23.96  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.208 -18.382 17.291 0.54 20.96  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.220 -18.388 17.281 0.46 22.04  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.081 -20.588 15.788 0.54 20.90  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.191 -20.547 15.774 0.46 22.75  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 44.000 -21.251 14.730 0.54 25.92  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.247 -20.447 14.676 0.46 28.82  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.519 -20.925 13.367 0.54 23.96  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.589 -21.814 14.110 0.46 29.67  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.446 -20.786 14.837 0.54 29.28  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.809 -19.493 13.594 0.46 30.06  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.820 -19.313 19.257 1.00 20.50  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.115 -18.317 20.090 1.00 20.47  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.928 -17.026 19.882 1.00 25.59  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.157 -17.083 19.715 1.00 26.05  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.080 -18.732 21.557 1.00 25.96  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.398 -19.125 21.927 1.00 27.49  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.093 -19.896 21.804 1.00 23.83  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.246 -15.896 19.752 1.00 21.95  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.899 -14.644 19.383 1.00 21.86  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.559 -13.483 20.283 1.00 23.98  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.874 -12.328 19.972 1.00 24.08  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.561 -14.324 17.919 1.00 22.32  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.072 -14.324 17.604 1.00 27.54  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.251 -14.343 18.560 1.00 23.25  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.727 -14.329 16.416 1.00 31.89  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.918 -13.779 21.408 1.00 19.62  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.586 -12.737 22.387 1.00 19.14  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.419 -13.337 23.769 1.00 22.84  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.042 -14.514 23.904 1.00 22.46  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.305 -11.919 21.955 1.00 21.92  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 39.002 -12.711 22.148 1.00 20.16  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.222 -10.560 22.676 1.00 21.79  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.693 -12.517 24.792 0.53 20.01  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.699 -12.531 24.799 0.47 20.26  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.461 -12.825 26.196 0.53 19.46  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.433 -12.894 26.179 0.47 19.88  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.390 -11.836 26.660 0.53 22.78  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.458 -11.860 26.764 0.47 23.23  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.519 -10.631 26.422 0.53 22.80  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.691 -10.653 26.662 0.47 23.48  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.746 -12.694 27.064 0.53 23.74  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.684 -13.189 27.057 0.47 24.43  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.469 -13.012 28.535 0.53 23.85  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.528 -11.946 27.314 0.47 25.17  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.864 -13.571 26.535 0.53 24.26  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.285 -13.859 28.369 0.47 24.50  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.338 -12.343 27.305 1.00 18.84  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.291 -11.522 27.909 1.00 18.81  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.583 -11.545 29.409 1.00 24.17  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.613 -12.625 30.019 1.00 22.81  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.852 -12.010 27.584 1.00 20.37  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.607 -12.163 26.048 1.00 19.42  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.809 -11.113 28.233 1.00 22.16  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 36.917 -10.901 25.162 1.00 20.16  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.813 -10.362 29.986 1.00 21.74  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.134 -10.220 31.410 1.00 22.46  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.875 -9.794  32.154 1.00 26.63  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.264 -8.770  31.817 1.00 24.98  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.326 -9.244  31.634 1.00 26.87  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.628 -9.049  33.124 1.00 27.59  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.578 -9.730  30.910 1.00 27.67  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.490 -10.582 33.176 1.00 23.53  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.290 -10.347 33.974 1.00 23.51  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.759 -10.385 35.415 1.00 28.28  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 37.006 -11.471 35.942 1.00 26.10  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.170 -11.374 33.660 1.00 26.77  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.843 -10.943 34.277 1.00 26.74  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 35.012 -11.581 32.146 1.00 25.50  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.648 -9.265  36.162 0.50 27.74  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.275 -9.191  35.796 0.50 25.01  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 37.012 -9.237  37.597 0.50 29.27  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.943 -8.824  37.029 0.50 25.47  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.264 -10.118 37.912 0.50 33.68  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.223 -9.653  37.195 0.50 28.60  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.217 -10.965 38.810 0.50 33.30  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.145 -9.439  36.409 0.50 27.76  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.821 -9.645  38.473 0.50 34.97  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 36.985 -8.865  38.212 0.50 29.52  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.822 -8.639  38.559 0.50 45.62  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.011 -7.850  38.023 0.50 35.58  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.350 -9.948  37.113 0.50 30.09  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.287 -10.621 38.133 0.50 25.75  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.627 -10.686 37.204 0.50 30.98  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.515 -11.410 38.260 0.50 26.24  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.488 -12.227 36.979 0.50 33.27  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.650 -12.431 37.086 0.50 30.57  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.215 -13.045 37.580 0.50 33.86  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.679 -12.447 36.392 0.50 30.48  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.392 -10.377 38.504 0.50 33.12  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.649 -12.045 39.669 0.50 27.00  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 41.937 -8.958  38.618 0.50 44.87  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 40.920 -10.999 40.762 0.50 33.41  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.045 -8.908  39.654 0.50 51.47  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.318 -11.599 42.104 0.50 34.45  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.394 -7.542  40.052 0.50 58.12  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.489 -10.579 43.140 0.50 35.22  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.814 -6.876  41.046 0.50 70.03  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.653 -10.030 43.486 0.50 50.04  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.822 -7.428  41.736 0.50 55.01  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.772 -10.379 42.865 0.50 37.51  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.207 -5.645  41.346 0.50 56.62  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.703 -9.122  44.449 0.50 41.49  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.549 -12.605 36.114 0.50 25.91  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.566 -13.164 36.793 0.50 24.63  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.339 -13.976 35.647 0.50 25.19  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.518 -14.230 35.785 0.50 23.27  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.483 -13.848 34.142 0.50 27.23  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.764 -13.780 34.338 0.50 25.31  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.914 -12.927 33.551 0.50 24.97  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.461 -12.651 33.961 0.50 21.99  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 37.966 -14.537 36.053 0.50 26.33  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.196 -15.016 35.878 0.50 24.15  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.852 -14.774 37.553 0.50 39.61  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.703 -15.200 37.309 0.50 39.18  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.821 -16.226 37.985 0.50 73.57  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.884 -16.556 37.964 0.50 76.21  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.790 -16.650 38.555 0.50 77.28  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.934 -17.203 37.743 0.50 77.35  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.827 -16.939 37.761 0.50 72.73  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 36.976 -16.959 38.726 0.50 78.54  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.293 -14.717 33.528 1.00 23.69  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.616 -14.575 32.116 1.00 23.16  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 39.994 -15.690 31.316 1.00 25.99  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.067 -16.848 31.727 1.00 25.91  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.145 -14.595 31.954 1.00 26.12  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.807 -13.348 32.537 1.00 40.23  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.266 -13.196 32.192 1.00 58.49  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.865 -13.996 31.461 1.00 51.76  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 44.869 -12.146 32.718 1.00 63.33  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.391 -15.346 30.167 1.00 20.05  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.761 -16.345 29.294 1.00 20.30  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.284 -16.184 27.888 1.00 24.57  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.107 -15.119 27.300 1.00 24.73  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.234 -16.155 29.294 1.00 21.54  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.616 -16.272 30.665 1.00 23.40  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.501 -15.155 31.496 1.00 25.61  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.131 -17.492 31.123 1.00 25.75  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 35.936 -15.266 32.769 1.00 27.70  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.561 -17.600 32.395 1.00 28.67  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.466 -16.487 33.209 1.00 26.92  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.886 -17.243 27.329 1.00 20.72  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.408 -17.195 25.957 1.00 19.45  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.282 -17.594 24.999 1.00 22.56  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.491 -18.496 25.301 1.00 21.33  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.635 -18.120 25.783 1.00 21.05  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.875 -17.688 26.625 1.00 29.47  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.211 -18.146 26.021 1.00 37.81  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.287 -17.801 24.593 1.00 47.59  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.793 -16.674 24.098 1.00 60.49  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.373 -15.791 24.897 1.00 51.81  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.765 -16.445 22.793 1.00 45.22  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.187 -16.926 23.849 1.00 19.25  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.104 -17.243 22.898 1.00 18.85  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.510 -16.840 21.492 1.00 20.17  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.618 -16.339 21.285 1.00 19.12  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.820 -16.501 23.297 1.00 19.97  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.607 -17.067 20.529 1.00 16.71  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.780 -16.649 19.141 1.00 15.90  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.869 -15.420 18.938 1.00 19.65  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.647 -15.488 19.197 1.00 18.44  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.351 -17.774 18.181 1.00 15.27  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.093 -19.061 18.403 1.00 18.28  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.562 -20.080 19.186 1.00 19.69  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.329 -19.432 17.981 1.00 19.05  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.483 -21.037 19.209 1.00 19.05  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.557 -20.702 18.479 1.00 18.90  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.463 -14.305 18.507 1.00 18.34  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.724 -13.064 18.230 1.00 17.35  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.497 -13.316 17.355 1.00 19.57  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.420 -12.820 17.687 1.00 17.91  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.623 -12.039 17.524 1.00 19.32  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.676 -11.457 18.457 1.00 18.05  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.586 -10.514 17.678 1.00 19.02  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.724 -10.085 18.558 1.00 23.90  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.665 -9.207  17.811 1.00 24.75  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.637 -14.134 16.277 1.00 16.81  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.496 -14.345 15.382 1.00 16.19  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.322 -15.021 16.058 1.00 17.01  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.185 -14.656 15.775 1.00 16.51  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.894 -15.056 14.104 1.00 22.06  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.518 -16.274 14.473 1.00 22.73  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.779 -14.180 13.218 1.00 24.77  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.584 -15.978 16.945 1.00 14.65  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.489 -16.676 17.646 1.00 14.81  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.818 -15.674 18.610 1.00 17.10  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.574 -15.636 18.716 1.00 15.49  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 32.995 -17.942 18.400 1.00 17.02  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.874 -18.558 19.257 1.00 16.93  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.524 -18.991 17.402 1.00 16.51  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.638 -14.897 19.349 1.00 14.68  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.068 -13.889 20.271 1.00 15.44  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.165 -12.895 19.500 1.00 17.83  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.052 -12.590 19.943 1.00 16.41  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.203 -13.099 20.969 1.00 15.63  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.168 -13.888 21.881 1.00 17.68  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.194 -12.917 22.511 1.00 17.97  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.402 -14.624 22.988 1.00 18.90  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.621 -12.428 18.331 1.00 15.25  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.845 -11.494 17.504 1.00 15.63  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.552 -12.139 17.023 1.00 18.80  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.507 -11.488 17.051 1.00 18.66  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.646 -11.018 16.286 1.00 17.09  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.880 -10.208 16.662 1.00 19.29  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.920 -10.116 15.205 1.00 22.78  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.186 -8.746  14.405 1.00 20.52  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.617 -13.419 16.629 1.00 16.61  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.463 -14.169 16.109 1.00 16.64  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.362 -14.348 17.182 1.00 18.74  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.192 -14.542 16.836 1.00 19.59  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.918 -15.547 15.592 1.00 16.89  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.747 -14.286 18.470 1.00 15.63  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.843 -14.518 19.600 1.00 15.88  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.393 -13.291 20.367 1.00 19.79  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.413 -13.392 21.121 1.00 19.39  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.501 -15.505 20.561 1.00 15.65  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.803 -17.133 19.843 1.00 18.79  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.151 -12.194 20.285 1.00 16.94  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.931 -11.050 21.164 1.00 15.86  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 26.966 -9.724  20.425 1.00 21.12  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.942 -9.441  19.720 1.00 18.74  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.021 -11.105 22.233 1.00 17.67  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.426 -9.854  22.769 1.00 20.85  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.928 -8.903  20.618 1.00 19.54  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.882 -7.570  20.019 1.00 20.30  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 27.009 -6.690  20.525 1.00 22.63  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.546 -5.867  19.770 1.00 22.45  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.415 -6.888  21.805 1.00 20.11  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.517 -6.108  22.374 1.00 19.91  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.841 -6.449  21.679 1.00 21.16  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.539 -5.526  21.239 1.00 20.74  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.640 -6.298  23.903 1.00 19.95  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.670 -5.378  24.588 1.00 24.32  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.192 -3.904  24.617 1.00 25.32  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 29.973 -5.861  25.991 1.00 23.32  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.166 -7.759  21.564 1.00 18.21  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.418 -8.164  20.902 1.00 17.69  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.409 -7.822  19.432 1.00 21.14  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.456 -7.458  18.894 1.00 19.47  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.762 -9.630  21.161 1.00 18.16  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.183 -9.859  22.598 1.00 18.50  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.248 -9.146  23.154 1.00 20.06  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.544 -10.817 23.384 1.00 19.20  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.627 -9.342  24.495 1.00 20.79  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 31.953 -11.049 24.709 1.00 21.50  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 32.983 -10.300 25.259 1.00 19.47  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.226 -7.897  18.788 1.00 18.76  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.110 -7.499  17.378 1.00 20.09  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.547 -6.025  17.218 1.00 24.64  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.364 -5.715  16.342 1.00 22.41  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.666 -7.714  16.897 1.00 22.02  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.440 -7.192  15.500 1.00 25.28  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 28.997 -7.831  14.396 1.00 26.80  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.676 -6.051  15.282 1.00 29.90  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.799 -7.342  13.103 1.00 29.01  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.478 -5.552  14.001 1.00 32.98  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.030 -6.207  12.917 1.00 39.92  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.798 -5.702  11.672 1.00 46.37  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.009 -5.133  18.071 0.52 22.27  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 30.008 -5.137  18.075 0.48 22.22  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.326 -3.705  18.079 0.52 23.14  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.324 -3.711  18.093 0.48 23.07  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.813 -3.460  18.395 0.52 27.45  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.819 -3.493  18.367 0.48 27.26  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.447 -2.654  17.719 0.52 28.66  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.460 -2.739  17.641 0.48 28.27  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.420 -2.972  19.065 0.52 25.61  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.477 -2.997  19.144 0.48 25.64  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.083 -2.949  18.592 0.52 27.24  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.780 -1.612  19.177 0.48 28.73  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.373 -4.181  19.389 1.00 23.30  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.786 -4.059  19.792 1.00 22.26  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.731 -4.438  18.668 1.00 24.28  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.627 -3.651  18.333 1.00 25.00  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.107 -4.893  21.094 1.00 23.80  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.419 -4.299  22.330 1.00 24.00  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.639 -5.012  21.338 1.00 22.52  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.402 -5.278  23.554 1.00 25.11  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.547 -5.629  18.085 1.00 19.49  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.519 -6.090  17.104 1.00 20.48  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.292 -5.547  15.687 1.00 24.45  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.142 -5.787  14.826 1.00 25.38  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.658 -7.626  17.146 1.00 20.59  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.083 -8.133  18.516 1.00 20.77  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.277 -7.705  19.099 1.00 23.59  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.275 -9.009  19.231 1.00 21.32  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.659 -8.158  20.372 1.00 24.19  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.669 -9.487  20.492 1.00 23.90  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.851 -9.053  21.058 1.00 22.06  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.224 -4.755  15.452 1.00 22.43  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.057 -4.061  14.158 1.00 22.92  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.615 -2.641  14.289 1.00 29.58  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.713 -1.907  13.298 1.00 29.18  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.628 -4.069  13.612 1.00 30.00  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.743 -3.573  14.608 1.00 25.94  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.185 -5.456  13.097 1.00 27.07  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.027 -2.263  15.509 1.00 26.13  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.636 -0.950  15.715 1.00 27.14  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.056 -1.005  15.155 1.00 33.03  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.813 -1.898  15.522 1.00 30.76  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.645 -0.572  17.199 1.00 27.52  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.378 0.729   17.409 1.00 38.00  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.756 1.788   17.229 1.00 42.17  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.601 0.684   17.671 1.00 37.74  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.428 -0.024  14.302 1.00 34.31  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.724 0.013   13.632 1.00 35.92  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 39.929 -0.037  14.577 1.00 40.62  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 40.978 -0.511  14.142 1.00 42.64  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.826 1.203   12.667 1.00 39.46  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 37.992 1.017   11.401 1.00 56.69  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.807 0.455   15.842 1.00 33.92  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 40.913 0.381   16.806 1.00 32.56  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.828 -0.864  17.662 1.00 35.28  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.847 -1.487  17.924 1.00 37.19  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 40.946 1.599   17.758 1.00 33.36  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.592 2.864   17.237 1.00 39.75  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.513 3.958   18.272 1.00 40.62  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.054 2.642   16.830 1.00 43.53  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.635 -1.182  18.180 1.00 28.46  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.470 -2.305  19.105 1.00 26.43  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.593 -3.666  18.433 1.00 31.36  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 39.969 -4.619  19.106 1.00 29.76  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.148 -2.216  19.891 1.00 27.35  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.035 -0.999  20.811 1.00 27.86  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.723 -1.081  21.593 1.00 25.63  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.404 0.229   22.294 1.00 29.92  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.877 1.252   21.360 1.00 29.95  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.317 -3.750  17.115 1.00 31.01  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.421 -5.004  16.347 1.00 30.82  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.813 -5.639  16.483 1.00 36.05  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 40.950 -6.853  16.317 1.00 36.34  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.058 -4.775  14.881 1.00 32.04  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.236 -3.736  13.970 1.00 37.91  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.837 -4.800  16.764 1.00 32.54  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.235 -5.204  16.876 1.00 33.51  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.720 -5.489  18.304 1.00 35.98  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.882 -5.857  18.499 1.00 35.67  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.134 -4.177  16.181 1.00 35.84  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 43.893 -4.133  14.681 1.00 47.67  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 43.850 -3.064  14.072 1.00 48.33  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.687 -5.290  14.051 1.00 38.85  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.837 -5.356  19.292 1.00 32.62  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.218 -5.625  20.674 1.00 31.71  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.198 -7.126  20.943 1.00 33.38  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.312 -7.812  20.427 1.00 30.56  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.239 -4.921  21.635 1.00 31.81  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.268 -3.385  21.613 1.00 36.56  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.176 -2.825  22.495 1.00 36.19  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.645 -2.831  22.052 1.00 37.85  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.162 -7.609  21.765 1.00 30.24  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.301 -9.012  22.169 0.42 29.22  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.238 -9.025  22.137 0.58 29.58  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.658 -9.231  23.542 1.00 29.87  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.493 -10.366 23.983 1.00 25.59  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.780 -9.391  22.235 0.42 33.40  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.679 -9.525  22.062 0.58 34.51  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.395 -9.299  20.962 0.42 38.39  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.500 -8.833  22.986 0.58 40.94  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.354 -8.127  24.252 1.00 26.14  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.756 -8.164  25.592 1.00 25.17  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.587 -7.183  25.631 1.00 26.73  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.737 -6.017  25.218 1.00 26.86  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.802 -7.831  26.709 1.00 30.29  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.163 -7.842  28.105 1.00 30.27  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 44.999 -8.783  26.663 1.00 31.04  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.437 -7.654  26.147 1.00 20.96  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.232 -6.845  26.361 1.00 20.14  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.841 -6.964  27.825 1.00 24.35  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.641 -8.078  28.318 1.00 24.22  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.059 -7.211  25.397 1.00 21.74  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.458 -7.064  23.894 1.00 22.50  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.778 -6.408  25.735 1.00 22.53  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.841 -5.617  23.399 1.00 26.94  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.713 -5.820  28.513 1.00 22.33  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.325 -5.799  29.915 1.00 23.11  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.850 -5.465  30.032 1.00 25.04  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.418 -4.389  29.595 1.00 22.76  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.153 -4.768  30.707 1.00 26.06  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.630 -4.983  30.629 1.00 43.61  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.147 -6.023  31.010 1.00 33.94  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.344 -3.992  30.152 1.00 40.24  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.080 -6.363  30.643 1.00 19.92  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.659 -6.113  30.833 1.00 19.62  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.418 -5.207  32.033 1.00 23.37  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.296 -5.043  32.893 1.00 24.15  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.842 -7.412  30.974 1.00 19.40  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.910 -8.430  29.799 1.00 22.31  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.787 -9.475  29.929 1.00 22.36  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.890 -7.731  28.414 1.00 23.33  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.223 -4.632  32.092 1.00 20.41  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.817 -3.726  33.181 1.00 21.92  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 32.995 -4.482  34.523 1.00 26.62  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.647 -5.668  34.598 1.00 25.45  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.348 -3.314  32.976 1.00 23.67  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.805 -2.293  33.961 1.00 31.01  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.689 -2.623  35.159 1.00 31.85  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.455 -1.184  33.525 1.00 32.26  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.591 -3.838  35.552 1.00 27.12  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.811 -4.550  36.835 1.00 27.66  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.569 -5.102  37.510 1.00 30.55  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.708 -5.922  38.409 1.00 31.88  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.514 -3.517  37.717 1.00 30.38  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.211 -2.181  37.085 1.00 35.70  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.087 -2.446  35.612 1.00 29.48  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.366 -4.674  37.098 1.00 27.35  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.130 -5.186  37.691 1.00 28.46  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.800 -6.589  37.150 1.00 28.12  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.946 -7.273  37.714 1.00 27.22  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.948 -4.223  37.451 1.00 31.11  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.899 -3.049  38.415 1.00 50.77  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.350 -3.400  39.783 1.00 81.73  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.121 -3.615  39.894 1.00 82.68  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.151 -3.474  40.743 1.00 81.45  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.480 -7.013  36.069 1.00 23.41  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.226 -8.323  35.467 1.00 22.62  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.816 -9.440  36.300 1.00 27.38  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 31.990 -9.404  36.667 1.00 26.33  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.667 -8.381  33.991 1.00 23.96  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.950 -7.279  33.155 1.00 24.82  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.449 -9.809  33.408 1.00 19.34  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.331 -7.308  33.174 1.00 30.83  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 29.982 -10.428 36.573 1.00 26.99  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.300 -11.604 37.355 1.00 27.87  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.023 -12.650 36.491 1.00 27.24  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.488 -13.053 35.457 1.00 25.38  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 28.997 -12.166 37.953 1.00 31.41  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.170 -13.474 38.683 1.00 43.96  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.830 -14.537 38.165 1.00 32.36  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.711 -13.425 39.894 1.00 38.53  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.221 -13.137 36.910 1.00 24.66  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.937 -14.145 36.100 1.00 24.07  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.158 -15.439 35.846 1.00 26.61  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.231 -15.972 34.732 1.00 25.52  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.205 -14.407 36.917 1.00 27.40  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.399 -13.147 37.713 1.00 32.32  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.014 -12.751 38.095 1.00 28.15  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.388 -15.927 36.841 1.00 24.33  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.621 -17.166 36.626 1.00 24.04  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.544 -16.960 35.555 1.00 25.85  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.435 -17.794 34.662 1.00 24.13  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.018 -17.710 37.929 1.00 26.47  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.371 -19.075 37.716 1.00 33.76  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.547 -19.641 38.859 1.00 57.98  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.636 -20.867 39.093 1.00 56.82  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 27.798 -18.874 39.507 1.00 53.09  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.822 -15.828 35.620 1.00 24.15  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.814 -15.467 34.622 1.00 23.56  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.431 -15.414 33.233 1.00 24.07  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.869 -15.950 32.261 1.00 21.46  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.629 -14.812 33.139 1.00 20.31  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.323 -14.749 31.849 1.00 18.67  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.691 -16.150 31.371 1.00 20.86  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.507 -16.454 30.202 1.00 19.88  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.590 -13.871 31.900 1.00 19.78  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.182 -13.753 30.509 1.00 19.75  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.617 -12.898 29.564 1.00 22.16  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.254 -14.547 30.123 1.00 20.17  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.112 -12.848 28.256 1.00 22.10  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.756 -14.490 28.819 1.00 21.95  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.172 -13.654 27.891 1.00 20.82  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.268 -16.967 32.254 1.00 20.25  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.684 -18.336 31.924 1.00 21.99  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.493 -19.151 31.354 1.00 23.34  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.629 -19.831 30.323 1.00 21.51  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.285 -19.010 33.155 1.00 25.56  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.923 -20.674 32.821 1.00 30.99  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.322 -19.060 32.026 1.00 20.95  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.097 -19.771 31.613 1.00 19.96  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.691 -19.321 30.204 1.00 20.99  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.322 -20.157 29.347 1.00 19.17  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.966 -19.543 32.665 1.00 23.03  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.252 -20.362 33.959 1.00 23.56  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.549 -19.848 32.086 1.00 22.54  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.479 -19.851 35.194 1.00 28.47  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.776 -18.020 29.962 1.00 18.27  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.417 -17.466 28.650 1.00 18.11  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.418 -17.824 27.582 1.00 20.31  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.009 -18.104 26.456 1.00 18.32  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.161 -15.974 28.717 1.00 19.30  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.868 -15.586 29.475 1.00 25.19  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.812 -14.114 29.686 1.00 26.23  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.613 -16.049 28.722 1.00 26.66  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.733 -17.837 27.926 1.00 17.99  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.759 -18.243 26.956 1.00 17.33  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.528 -19.708 26.553 1.00 20.12  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.616 -20.050 25.372 1.00 18.43  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.157 -18.047 27.556 1.00 17.30  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.329 -18.341 26.589 1.00 21.52  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.309 -17.404 25.361 1.00 20.74  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.687 -18.222 27.339 1.00 25.14  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.224 -20.571 27.535 1.00 18.49  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.912 -21.973 27.258 1.00 18.07  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.708 -22.084 26.332 1.00 20.61  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.750 -22.861 25.387 1.00 20.15  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.619 -22.698 28.570 1.00 20.59  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.866 -23.040 29.360 1.00 31.77  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.977 -22.966 28.783 1.00 31.32  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.734 -23.384 30.553 1.00 32.41  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.652 -21.299 26.589 1.00 18.73  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.451 -21.254 25.735 1.00 17.45  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.821 -20.857 24.296 1.00 18.80  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.341 -21.460 23.327 1.00 16.67  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.394 -20.297 26.336 1.00 17.92  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.284 -20.002 25.362 1.00 18.07  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.317 -20.962 25.079 1.00 20.47  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.293 -18.829 24.603 1.00 19.19  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.335 -20.726 24.122 1.00 20.13  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.308 -18.597 23.634 1.00 22.05  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.333 -19.544 23.406 1.00 20.84  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.643 -19.818 24.152 1.00 15.65  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.065 -19.378 22.805 1.00 14.46  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.619 -20.528 21.984 1.00 18.88  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.262 -20.679 20.820 1.00 18.27  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.159 -18.297 22.914 1.00 15.11  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.644 -16.999 23.498 1.00 16.77  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 29.999 -15.782 23.383 1.00 19.15  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.378 -14.564 24.600 1.00 19.16  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.476 -21.350 22.609 1.00 15.98  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.153 -22.448 21.927 1.00 15.31  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.402 -23.780 21.920 1.00 18.67  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.888 -24.725 21.293 1.00 18.40  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.539 -22.650 22.556 1.00 16.21  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.592 -21.678 22.062 1.00 16.73  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.765 -20.436 22.671 1.00 18.07  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.441 -22.017 21.008 1.00 17.73  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.752 -19.547 22.229 1.00 16.81  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.461 -21.162 20.594 1.00 17.97  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.595 -19.920 21.190 1.00 19.88  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.622 -19.108 20.784 1.00 18.41  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.243 -23.887 22.612 1.00 15.44  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.558 -25.193 22.672 1.00 16.53  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.051 -25.170 22.411 1.00 19.22  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.471 -26.258 22.250 1.00 18.76  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.743 -25.851 24.073 1.00 21.07  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.092 -25.043 25.060 1.00 21.76  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.208 -26.079 24.458 1.00 21.77  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.404 -23.983 22.500 1.00 16.01  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.926 -23.770 22.456 1.00 15.83  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.268 -24.172 23.800 1.00 19.53  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.055 -24.036 23.934 1.00 19.93  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.257 -24.577 21.331 1.00 18.27  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.893 -24.397 20.076 1.00 22.18  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.071 -24.649 24.776 0.60 17.73  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.050 -24.682 24.772 0.40 16.74  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.586 -25.123 26.076 0.60 18.58  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.493 -25.114 26.056 0.40 17.19  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.791 -24.056 27.137 0.60 21.78  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.776 -24.107 27.147 0.40 21.26  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.913 -23.560 27.315 0.60 20.35  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.922 -23.680 27.332 0.40 19.99  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.314 -26.417 26.490 0.60 22.05  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.949 -26.528 26.436 0.40 18.67  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.188 -27.563 25.472 0.60 28.53  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.312 -27.588 25.547 0.40 17.63  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.129 -28.721 25.788 0.60 31.58  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 24.063 -28.895 25.573 0.40 30.32  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.885 -29.271 27.125 0.60 36.21  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.467 -29.870 24.658 0.40 37.51  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 24.000 -30.224 27.395 0.60 48.63  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.347 -31.168 24.917 0.40 50.13  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.837 -30.651 28.638 0.60 36.59  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.799 -31.982 24.023 0.40 37.45  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.271 -30.759 26.422 0.60 37.32  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.774 -31.664 26.071 0.40 39.22  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.713 -23.723 27.859 1.00 18.99  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.754 -22.713 28.903 1.00 19.28  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.518 -23.347 30.263 1.00 24.33  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.447 -23.912 30.517 1.00 24.06  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.699 -21.635 28.582 1.00 19.52  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.708 -20.421 29.530 1.00 23.38  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 22.982 -19.586 29.322 1.00 22.27  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.467 -19.576 29.342 1.00 24.67  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.514 -23.240 31.157 1.00 23.79  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.402 -23.809 32.509 1.00 24.64  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.691 -22.801 33.423 1.00 28.98  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.330 -22.116 34.216 1.00 29.20  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.797 -24.197 33.060 1.00 28.27  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.756 -24.824 34.452 1.00 44.06  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.748 -25.384 34.882 1.00 37.52  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.845 -24.731 35.193 1.00 36.70  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.378 -22.685 33.265 1.00 25.68  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.562 -21.731 34.010 1.00 27.12  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.025 -22.374 35.270 1.00 32.01  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.376 -23.426 35.205 1.00 31.18  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.441 -21.237 33.086 1.00 28.08  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.723 -19.950 33.437 1.00 34.85  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.725 -18.754 33.563 1.00 34.93  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.661 -19.658 32.386 1.00 35.93  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.361 -21.777 36.436 1.00 29.38  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 19.982 -22.290 37.759 1.00 31.51  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.445 -21.173 38.641 1.00 33.17  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.773 -19.999 38.420 1.00 30.50  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.195 -22.955 38.448 1.00 33.17  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.826 -24.109 37.642 1.00 38.16  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.071 -24.696 38.298 1.00 54.06  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.813 -25.187 39.658 1.00 70.94  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.349 -26.400 39.955 1.00 90.94  ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.138 -26.744 41.219 1.00 79.38  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.089 -27.274 38.989 1.00 80.02  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.625 -21.518 39.661 1.00 30.74  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.096 -20.492 40.571 1.00 31.30  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.215 -19.592 41.131 1.00 36.05  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.034 -18.377 41.221 1.00 35.80  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.326 -21.154 41.739 1.00 34.77  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.613 -20.171 42.647 1.00 45.39  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.913 -20.810 43.830 1.00 76.90  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.517 -21.687 44.490 1.00 69.71  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.753 -20.426 44.101 1.00 80.80  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.345 -20.201 41.484 1.00 34.54  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.489 -19.512 42.076 1.00 34.92  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.312 -18.647 41.136 1.00 35.68  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.126 -17.841 41.597 1.00 35.26  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.106 -18.774 39.819 1.00 30.55  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.901 -17.976 38.880 1.00 28.04  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.078 -17.110 37.921 1.00 31.45  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.664 -16.301 37.190 1.00 28.93  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.876 -18.886 38.100 1.00 26.08  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.226 -19.827 37.098 1.00 33.30  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.193 -19.517 36.507 1.00 25.07  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.848 -20.975 36.836 1.00 28.20  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.740 -17.300 37.888 1.00 29.26  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.866 -16.644 36.902 1.00 28.74  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 19.991 -15.112 36.885 1.00 29.94  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 20.018 -14.528 35.793 1.00 27.82  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.389 -17.098 36.992 1.00 33.10  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.559 -16.514 35.809 1.00 33.71  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.763 -16.829 38.364 1.00 33.28  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.380 -17.346 35.375 1.00 35.20  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.082 -14.464 38.059 1.00 27.99  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.230 -13.010 38.084 1.00 28.41  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.542 -12.556 37.450 1.00 30.03  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.514 -11.631 36.643 1.00 27.95  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.063 -12.438 39.508 1.00 32.38  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.688 -12.694 40.117 1.00 38.74  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.262 -12.298 39.061 1.00 44.36  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.295 -10.488 39.129 1.00 42.16  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.684 -13.226 37.770 1.00 27.87  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 24.002 -12.874 37.195 1.00 27.07  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 24.014 -13.172 35.696 1.00 28.00  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.501 -12.356 34.905 1.00 25.64  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.114 -13.660 37.879 1.00 28.60  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.442 -14.320 35.304 1.00 23.75  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.370 -14.691 33.878 1.00 21.52  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.566 -13.659 33.074 1.00 24.20  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.057 -13.220 32.026 1.00 23.39  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.879 -16.146 33.656 1.00 24.67  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.617 -16.432 32.176 1.00 23.00  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.895 -17.141 34.206 1.00 24.63  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.362 -13.271 33.545 0.65 23.09  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.364 -13.271 33.549 0.35 23.26  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.545 -12.281 32.828 0.65 23.61  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.533 -12.284 32.850 0.35 23.99  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.255 -10.925 32.721 0.65 27.34  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.243 -10.933 32.728 0.35 27.76  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.246 -10.314 31.649 0.65 26.28  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.235 -10.342 31.646 0.35 26.88  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.173 -12.102 33.485 0.65 26.98  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.171 -12.110 33.531 0.35 27.71  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.258 -11.185 32.689 0.65 30.56  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.221 -11.259 32.720 0.35 31.89  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.572 -11.189 33.314 0.65 35.50  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.657 -11.007 33.563 0.35 37.74  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.749 -10.150 34.809 0.65 33.30  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.147 -9.498  32.802 0.35 35.37  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.857 -10.454 33.828 1.00 25.15  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.603 -9.171  33.846 1.00 24.83  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.758 -9.211  32.839 1.00 25.35  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.937 -8.256  32.062 1.00 23.52  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.127 -8.884  35.248 1.00 26.33  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.496 -10.341 32.796 1.00 21.63  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.603 -10.519 31.855 1.00 20.70  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.081 -10.561 30.405 1.00 24.12  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.674 -9.897  29.542 1.00 21.66  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.517 -11.711 32.234 1.00 25.93  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.807 -11.666 33.639 1.00 24.79  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.840 -11.719 31.433 1.00 24.55  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 23.971 -11.303 30.147 1.00 21.29  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.380 -11.392 28.804 1.00 19.98  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.860 -10.023 28.333 1.00 23.22  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.006 -9.694  27.156 1.00 21.93  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.284 -12.458 28.760 1.00 20.84  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.320 -9.189  29.256 1.00 21.02  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.872 -7.844  28.867 1.00 20.85  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.068 -6.983  28.428 1.00 23.65  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.021 -6.339  27.376 1.00 23.86  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.110 -7.188  30.028 1.00 24.10  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.737 -7.799  30.220 1.00 29.11  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 18.991 -7.220  31.752 1.00 36.28  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.644 -5.529  31.285 1.00 34.34  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.156 -7.038  29.198 1.00 22.01  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.400 -6.309  28.915 1.00 21.91  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.024 -6.794  27.587 1.00 23.63  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.424 -5.973  26.746 1.00 21.37  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.378 -6.533  30.074 1.00 22.60  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.796 -6.055  29.832 1.00 22.39  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.116 -4.700  29.883 1.00 25.23  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.833 -6.966  29.622 1.00 21.94  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.427 -4.260  29.687 1.00 21.72  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.150 -6.543  29.468 1.00 21.77  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.443 -5.188  29.522 1.00 21.82  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.743 -4.781  29.394 1.00 22.34  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.068 -8.122  27.385 1.00 20.02  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.655 -8.703  26.173 1.00 18.70  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.736 -8.585  24.962 1.00 22.07  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.177 -8.851  23.844 1.00 20.68  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.028 -10.176 26.403 1.00 17.14  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.143 -10.462 27.436 1.00 19.63  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.405 -11.982 27.517 1.00 19.02  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.467 -9.683  27.083 1.00 21.44  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.457 -8.230  25.189 1.00 20.51  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.446 -8.091  24.126 1.00 20.87  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.229 -9.447  23.449 1.00 22.74  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.535 -9.640  22.269 1.00 21.18  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.827 -6.990  23.114 1.00 21.86  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 24.011 -5.597  23.754 1.00 25.88  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.715 -4.659  22.805 1.00 34.74  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.570 -4.753  21.597 1.00 27.21  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.514 -3.747  23.329 1.00 30.64  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.737 -10.399 24.244 1.00 19.96  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.431 -11.774 23.807 1.00 19.08  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.924 -11.929 24.072 1.00 25.39  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.503 -12.413 25.126 1.00 23.95  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.285 -12.749 24.623 1.00 19.60  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.777 -12.630 24.290 1.00 20.70  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.789 -13.650 25.357 1.00 23.36  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.424 -15.326 24.621 1.00 20.62  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.117 -11.388 23.139 1.00 25.31  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.661 -11.248 23.279 1.00 27.55  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.908 -12.530 23.600 1.00 28.29  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.982 -12.480 24.407 1.00 28.61  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.045 -10.574 22.047 1.00 30.63  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.578 -9.167  21.824 1.00 43.99  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.269 -13.661 22.975 1.00 23.57  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.532 -14.897 23.262 1.00 25.28  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.746 -15.371 24.694 1.00 27.87  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.788 -15.814 25.334 1.00 28.81  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.837 -15.986 22.242 1.00 26.71  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.371 -15.646 20.862 1.00 31.56  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 16.031 -15.462 20.581 1.00 35.15  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 18.080 -15.523 19.717 1.00 32.85  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 15.971 -15.187 19.288 1.00 34.76  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.177 -15.226 18.726 1.00 33.75  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 18.984 -15.221 25.216 1.00 21.90  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.289 -15.567 26.607 1.00 21.60  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.502 -14.659 27.563 1.00 27.13  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.892 -15.149 28.527 1.00 25.69  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.802 -15.572 26.922 1.00 23.82  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.039 -15.825 28.417 1.00 23.79  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.523 -16.624 26.079 1.00 22.69  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.497 -13.335 27.285 1.00 23.87  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.753 -12.371 28.113 1.00 25.12  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.264 -12.782 28.178 1.00 30.88  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.699 -12.844 29.273 1.00 30.25  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.937 -10.898 27.643 1.00 27.97  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.098 -9.932  28.498 1.00 28.59  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.412 -10.490 27.673 1.00 27.01  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.632 -12.999 27.007 0.41 29.22  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.698 -13.188 27.026 0.59 28.15  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.210 -13.356 26.877 0.41 30.94  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.314 -13.655 26.901 0.59 29.31  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.784 -14.558 27.719 0.41 35.37  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 14.008 -14.872 27.790 0.59 31.70  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.710 -14.526 28.315 0.41 36.49  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.058 -14.801 28.567 0.59 31.38  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.835 -13.569 25.397 0.41 32.99  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 13.976 -13.946 25.427 0.59 31.30  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.665 -12.295 24.590 0.41 44.79  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.522 -14.296 25.176 0.59 43.76  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.180 -11.292 25.155 0.41 48.30  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.644 -13.486 25.544 0.59 45.91  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 13.998 -12.306 23.387 0.41 49.83  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.265 -15.369 24.596 0.59 48.49  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.626 -15.602 27.783 0.41 30.73  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.811 -15.966 27.714 0.59 26.82  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.347 -16.820 28.550 0.41 30.81  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.527 -17.146 28.555 0.59 27.11  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.540 -16.601 30.028 0.41 32.95  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.733 -16.864 30.060 0.59 30.89  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.700 -17.045 30.814 0.41 33.25  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 14.074 -17.503 30.883 0.59 30.62  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.151 -17.969 27.993 0.41 38.18  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.269 -18.410 28.091 0.59 26.98  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 14.729 -18.075 26.654 0.41 38.68  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.617 -19.535 28.691 0.59 28.53  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.878 -19.281 28.705 0.41 38.10  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.751 -18.414 28.466 0.59 20.37  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.640 -15.919 30.414 1.00 27.84  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.896 -15.560 31.823 1.00 28.12  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.676 -14.833 32.362 1.00 34.28  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.183 -15.185 33.443 1.00 33.75  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.140 -14.688 31.930 1.00 26.95  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.689 -15.595 31.754 1.00 29.17  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.148 -13.860 31.572 1.00 32.66  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.943 -13.099 31.936 1.00 34.84  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.754 -14.048 32.201 1.00 39.53  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.028 -13.874 33.189 1.00 39.56  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.567 -12.111 30.821 1.00 37.19  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.441 -10.876 30.765 1.00 52.43  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.631 -9.630  30.458 1.00 67.78  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 12.997 -9.045  29.166 1.00 75.98  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.933 -8.115  28.994 1.00 85.68  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.623 -7.657  30.032 1.00 66.83  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.191 -7.642  27.783 1.00 74.33  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.574 -15.048 31.323 1.00 37.28  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.491 -16.035 31.414 1.00 38.49  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.646 -16.945 32.628 1.00 41.69  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.661  -17.176 33.325 1.00 41.95  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.386 -16.868 30.119 1.00 39.96  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.874  -16.075 28.922 1.00 57.43  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.579  -16.975 27.724 1.00 68.40  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.640  -16.255 26.394 1.00 78.68  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.589  -15.211 26.244 1.00 87.62  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.874 -17.459 32.885 1.00 36.59  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.154 -18.326 34.038 1.00 36.94  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.961 -17.565 35.351 1.00 42.11  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.415 -18.130 36.307 1.00 41.93  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.558 -18.946 33.936 1.00 37.04  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.670 -20.239 33.146 1.00 38.10  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.090 -20.361 31.885 1.00 40.92  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.424 -21.305 33.628 1.00 39.99  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.208 -21.549 31.153 1.00 40.87  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.548 -22.489 32.889 1.00 41.56  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.938 -22.602 31.660 1.00 38.87  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.337 -16.265 35.378 1.00 37.48  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.126 -15.411 36.562 1.00 38.73  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.625 -15.180 36.809 1.00 45.40  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.170 -15.309 37.950 1.00 45.90  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.954 -14.093 36.483 1.00 40.48  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.447 -14.400 36.677 1.00 38.74  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.483 -13.042 37.528 1.00 43.20  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.378 -13.374 36.103 1.00 43.83  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.860  -14.880 35.734 1.00 44.06  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.410  -14.631 35.789 1.00 46.67  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.624  -15.854 36.304 1.00 51.90  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.638  -15.689 37.021 1.00 51.89  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.887  -14.188 34.412 1.00 50.07  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.540  -13.473 34.461 1.00 66.97  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.915  -13.361 33.079 1.00 79.06  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.495  -12.853 33.139 1.00 93.19  ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.835  -12.913 31.807 1.00 103.63 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.078  -17.071 35.958 1.00 48.01  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.447  -18.315 36.404 1.00 49.48  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.585  -18.537 37.924 1.00 54.81  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.715  -19.160 38.519 1.00 55.83  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.032  -19.497 35.641 1.00 48.55  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.671  -18.034 38.541 1.00 52.27  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 8.934  -18.183 39.980 1.00 54.70  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.261  -17.114 40.870 1.00 62.10  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.177  -17.317 42.087 1.00 64.37  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.436 -18.233 40.252 1.00 58.34  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 10.969 -19.522 39.993 1.00 69.19  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.769  -16.000 40.279 1.00 58.15  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.112  -14.926 41.036 1.00 76.30  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.655  -15.253 41.383 1.00 116.38 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.371  -16.314 41.933 1.00 83.59  ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.243  -13.562 40.325 1.00 76.74  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.258  -13.317 39.190 1.00 86.61  ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.476  -12.077 38.339 1.00 106.32 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.594  -11.511 38.362 1.00 96.31  ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.522  -11.682 37.630 1.00 100.71 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.246 -35.114 5.863  1.00 24.54  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.314 -33.964 6.327  1.00 25.25  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.439 -36.313 6.748  1.00 24.19  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.976 -35.367 4.587  0.78 23.23  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 21.003 -35.382 4.578  0.22 23.18  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.776 -34.312 3.604  0.78 22.40  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.746 -34.338 3.587  0.22 22.43  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.275 -34.164 3.302  0.78 26.55  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.246 -34.157 3.391  0.22 26.10  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.545 -35.165 3.253  0.78 26.10  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.493 -35.133 3.464  0.22 25.60  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.570 -34.646 2.327  0.78 21.36  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.446 -34.622 2.234  0.22 21.03  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.067 -34.618 2.521  0.78 21.78  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.796 -35.672 1.377  0.22 21.78  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.856 -35.627 2.995  0.78 24.49  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.120 -36.994 1.320  0.22 24.80  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.939 -33.503 2.286  0.78 21.31  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.742 -35.476 0.418  0.22 21.53  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.170 -35.205 3.071  0.78 23.63  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.302 -37.646 0.429  0.22 24.31  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.256 -33.927 2.586  0.78 24.77  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.459 -36.735 -0.154 0.22 25.46  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.736 -32.176 1.858  0.78 21.75  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 18.990 -34.361 0.006  0.22 22.47  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.367 -33.082 2.448  0.78 23.33  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.466 -36.910 -1.127 0.22 24.52  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.842 -31.350 1.701  0.78 22.45  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 18.004 -34.537 -0.952 0.22 24.08  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.136 -31.806 1.988  0.78 23.17  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.750 -35.799 -1.507 0.22 24.55  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.818 -32.917 3.117  1.00 22.30  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.405 -32.581 2.874  1.00 21.78  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.259 -31.537 1.769  1.00 23.25  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.223 -30.849 1.423  1.00 22.24  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.689 -32.065 4.178  1.00 24.57  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.678 -33.119 5.293  1.00 24.36  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.290 -30.735 4.677  1.00 24.13  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.019 -31.353 1.305  1.00 21.03  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.667 -30.261 0.407  1.00 21.21  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.286 -29.123 1.387  1.00 24.10  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.266 -29.257 2.083  1.00 22.99  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.461 -30.629 -0.500 1.00 22.68  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.734 -31.906 -1.378 1.00 21.76  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.023 -29.405 -1.353 1.00 23.55  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.063 -31.859 -2.292 1.00 24.72  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.085 -28.038 1.501  1.00 23.81  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.743 -26.972 2.464  1.00 24.40  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.481 -26.194 2.083  1.00 27.96  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.211 -25.982 0.899  1.00 27.90  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 16.990 -26.075 2.466  1.00 25.98  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.566 -26.257 1.068  1.00 29.50  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.315 -27.712 0.743  1.00 25.12  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.800 -25.646 3.093  1.00 25.42  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.278 -10.329 11.835 1.00 25.15  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.259 -9.396  12.203 1.00 26.97  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.959 -10.769 18.107 1.00 23.49  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.465 -9.470  18.155 1.00 24.15  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.511 -10.095 16.386 1.00 22.03  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.340 -10.251 14.019 1.00 21.84  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.935 -8.486  17.289 1.00 22.71  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.951 -8.812  16.396 1.00 21.96  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 24.977 -11.090 17.213 1.00 22.23  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.387 -10.644 13.180 1.00 22.00  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.244 -10.596 19.726 1.00 28.05  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.220 -11.587 19.126 1.00 26.07  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.216 -9.696  11.328 1.00 26.40  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.247 -9.632  13.520 1.00 25.53  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.459 -9.393  19.129 1.00 24.85  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.354 -10.552 15.350 1.00 20.40  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.402 -10.822 20.594 1.00 26.86  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.814 -11.407 13.772 0.99 21.28  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.325 -15.262 22.528 1.00 29.14  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.583 -35.357 -1.248 0.78 37.02  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.272 -35.128 -0.636 0.78 39.34  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.685 -34.463 -0.174 0.78 34.24  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 17.996 -36.995 -0.783 0.78 36.43  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 35.640 -25.705 25.532 1.00 35.54  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 38.358 -14.940 15.416 1.00 26.94  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 25.823 -3.425  26.368 1.00 29.64  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 22.728 -5.347  19.789 1.00 49.64  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 41.236 -21.695 25.243 1.00 36.88  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 44.444 -0.926  17.869 1.00 47.44  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 37.948 2.403   19.668 1.00 34.79  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 20.791 -5.870  25.981 1.00 36.56  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 44.967 -11.330 18.639 1.00 50.96  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 19.929 -9.502  36.977 1.00 34.54  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 37.573 -20.370 26.980 1.00 28.41  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 32.466 -24.677 32.147 1.00 54.51  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 33.331 -20.774 29.544 1.00 40.24  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 26.779 -31.953 16.116 1.00 39.44  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 31.765 -0.830  15.861 1.00 34.20  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 43.575 -6.675  31.973 1.00 40.65  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 27.220 -35.316 11.742 1.00 50.76  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 16.542 -27.461 -3.269 1.00 45.57  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 23.465 -5.728  32.871 1.00 33.65  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 41.294 -16.991 15.168 1.00 28.86  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 41.689 -12.803 14.411 1.00 58.24  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 22.944 -28.214 12.617 1.00 21.59  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 30.265 1.484   33.945 1.00 54.11  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 13.561 -14.431 21.766 1.00 60.44  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 22.551 -27.682 17.712 1.00 45.57  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 32.352 -9.009  39.614 1.00 46.96  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 27.284 -10.116 35.812 1.00 34.39  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 14.203 -16.841 23.395 1.00 37.52  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 15.437 -9.818  24.835 1.00 50.70  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 21.752 -29.561 -5.246 1.00 35.12  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 27.325 -28.152 18.613 1.00 26.49  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 20.468 -13.370 20.418 1.00 43.76  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 43.501 -10.721 35.343 1.00 55.80  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 17.972 -29.366 7.641  1.00 28.43  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 21.903 -24.958 18.300 1.00 20.48  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 12.612 -20.400 42.412 1.00 55.08  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 34.896 -18.853 13.840 0.50 20.45  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 28.274 -8.856  39.835 1.00 44.23  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 30.432 -0.513  36.874 1.00 42.32  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 29.903 -32.021 9.526  1.00 37.76  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 26.779 -16.491 38.634 1.00 40.81  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 29.545 -2.212  13.712 1.00 59.08  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 7.075  -17.018 32.440 1.00 48.78  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 26.133 -22.556 29.920 1.00 23.60  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 11.245 -14.987 40.458 1.00 79.48  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 26.408 -7.712  36.751 1.00 46.93  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 43.869 -4.349  25.706 1.00 39.40  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 24.870 -26.740 18.984 1.00 28.38  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 21.499 -29.972 14.190 1.00 70.45  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 36.827 -5.616  12.151 1.00 32.24  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 28.962 -31.150 7.207  1.00 25.45  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 25.663 -2.785  19.943 1.00 54.71  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 41.282 -6.967  35.856 1.00 40.66  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 47.140 -25.354 21.666 1.00 44.62  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 28.429 -24.224 34.290 1.00 49.50  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 10.825 -11.423 34.499 1.00 45.66  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 26.084 -19.199 41.682 1.00 62.79  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 20.820 -7.184  19.591 1.00 46.68  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 27.136 -2.451  16.015 1.00 58.32  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 44.386 -12.523 41.186 1.00 48.84  ? 360 HOH A O   1 
HETATM 1263 O  O   . HOH F 6 .   ? 28.180 -23.718 31.631 1.00 35.46  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 45.871 -14.234 21.486 1.00 50.48  ? 362 HOH A O   1 
HETATM 1265 O  O   . HOH F 6 .   ? 42.369 -10.336 15.351 1.00 38.88  ? 363 HOH A O   1 
HETATM 1266 O  O   A HOH F 6 .   ? 19.069 -23.029 4.290  0.60 32.87  ? 364 HOH A O   1 
HETATM 1267 O  O   . HOH F 6 .   ? 30.678 -28.814 22.590 1.00 34.31  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 29.344 -27.395 20.620 1.00 21.46  ? 366 HOH A O   1 
HETATM 1269 O  O   . HOH F 6 .   ? 4.306  -20.327 37.672 1.00 56.37  ? 367 HOH A O   1 
HETATM 1270 O  O   . HOH F 6 .   ? 46.309 -29.782 21.238 1.00 67.48  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 22.662 -34.027 8.843  1.00 29.86  ? 369 HOH A O   1 
HETATM 1272 O  O   . HOH F 6 .   ? 22.172 -33.973 26.085 1.00 66.60  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 21.392 -27.086 14.499 0.50 37.59  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 46.095 -15.737 27.617 1.00 55.38  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 26.032 -21.817 38.586 1.00 32.70  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 39.023 -18.986 33.238 1.00 44.61  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 24.022 -15.850 21.127 1.00 24.24  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 46.848 -21.857 17.917 1.00 40.06  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 27.615 -23.057 13.840 0.50 22.88  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 18.012 -34.559 8.334  1.00 29.76  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 23.133 -17.034 44.311 1.00 53.57  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 46.256 -18.986 19.664 1.00 42.41  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 34.143 -7.858  35.602 1.00 27.81  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 25.841 -4.525  17.859 1.00 44.28  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 17.466 -24.470 -2.316 1.00 56.63  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 42.113 -6.031  11.786 1.00 59.77  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 46.000 -8.919  43.909 1.00 42.85  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 18.039 -24.317 39.761 1.00 38.49  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 26.346 -7.948  9.064  1.00 40.67  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 45.211 -12.628 23.553 1.00 42.14  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 37.392 -6.468  34.251 1.00 35.50  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 37.847 -16.261 12.777 1.00 39.45  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 20.130 -15.741 40.768 1.00 30.90  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 33.041 -29.635 21.490 1.00 38.87  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 10.118 -11.658 39.802 1.00 55.61  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 31.824 -31.891 14.551 1.00 39.39  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 44.666 -8.717  17.944 1.00 52.18  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 40.370 -19.610 28.977 1.00 30.67  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 35.524 2.093   13.589 1.00 52.76  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 45.460 -10.595 30.293 1.00 52.10  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 22.439 -9.993  14.332 1.00 36.20  ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 25.962 -29.170 22.507 1.00 51.36  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 19.672 -27.424 10.050 1.00 54.57  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 20.996 -23.058 42.036 1.00 43.37  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 41.111 -17.085 35.185 1.00 38.31  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 44.575 -16.441 29.730 1.00 43.93  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 34.827 -33.386 21.832 1.00 48.77  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 22.895 -14.845 40.309 1.00 29.17  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 35.193 -29.753 23.511 1.00 43.68  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 23.571 -15.609 17.901 1.00 37.36  ? 408 HOH A O   1 
HETATM 1311 O  O   . HOH F 6 .   ? 32.119 -15.622 39.770 1.00 29.54  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 33.654 -33.054 12.229 1.00 36.39  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 27.113 -1.579  21.912 1.00 46.74  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 30.333 -10.498 40.513 1.00 37.13  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 37.110 -2.394  11.440 1.00 59.36  ? 413 HOH A O   1 
HETATM 1316 O  O   B HOH F 6 .   ? 37.150 -11.790 40.010 0.50 31.02  ? 414 HOH A O   1 
HETATM 1317 O  O   . HOH F 6 .   ? 33.576 -0.287  20.015 1.00 41.23  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 45.701 -17.047 17.047 1.00 57.33  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 29.616 -0.805  22.152 1.00 50.22  ? 417 HOH A O   1 
HETATM 1320 O  O   . HOH F 6 .   ? 27.260 -25.487 28.238 1.00 50.57  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 47.074 -20.237 21.892 1.00 58.14  ? 419 HOH A O   1 
HETATM 1322 O  O   . HOH F 6 .   ? 39.941 -5.598  33.839 1.00 39.17  ? 420 HOH A O   1 
HETATM 1323 O  O   . HOH F 6 .   ? 42.005 -8.056  13.603 1.00 53.81  ? 421 HOH A O   1 
HETATM 1324 O  O   . HOH F 6 .   ? 33.894 -17.652 39.307 1.00 53.97  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 28.981 -16.153 41.303 1.00 61.27  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 44.225 -25.950 26.639 1.00 54.35  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 28.448 -2.609  11.248 1.00 67.08  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 45.697 -5.506  23.609 1.00 41.60  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 23.452 -30.355 19.259 1.00 60.15  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 29.791 -22.602 36.617 1.00 67.48  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 25.573 -15.807 40.980 1.00 48.31  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 42.796 -18.274 30.710 1.00 42.43  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 32.464 -4.090  41.137 1.00 61.14  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 44.892 -8.173  15.269 1.00 66.84  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 47.848 -23.456 19.872 1.00 59.07  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 31.955 -26.285 27.021 1.00 41.40  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 32.050 0.199   13.369 1.00 51.37  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 20.105 -35.300 10.178 1.00 36.28  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 37.700 -27.023 28.506 1.00 56.06  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 27.255 -34.514 17.910 1.00 67.04  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 28.433 -29.191 26.799 1.00 74.87  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 35.221 -4.159  10.568 1.00 41.89  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 19.475 -31.782 13.987 1.00 60.30  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 36.926 -24.387 27.517 1.00 49.23  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 24.298 -21.505 40.970 1.00 49.55  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 30.888 -34.440 14.796 1.00 54.83  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 34.547 -18.789 36.026 1.00 58.11  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 22.958 -2.698  26.043 1.00 60.73  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 33.775 -10.911 41.520 0.50 52.75  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 12.003 -18.543 22.357 1.00 52.84  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 47.107 -12.983 28.413 1.00 55.79  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 46.600 -14.634 17.870 1.00 65.60  ? 450 HOH A O   1 
HETATM 1353 O  O   A HOH F 6 .   ? 12.055 -20.731 27.824 0.78 43.99  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 47.114 -11.934 25.366 1.00 60.49  ? 452 HOH A O   1 
HETATM 1355 O  O   . HOH F 6 .   ? 43.024 -3.047  33.646 1.00 61.46  ? 453 HOH A O   1 
HETATM 1356 O  O   . HOH F 6 .   ? 32.274 -1.061  22.271 1.00 50.05  ? 454 HOH A O   1 
HETATM 1357 O  O   . HOH F 6 .   ? 13.637 -16.167 39.865 1.00 75.59  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 32.727 -3.203  10.011 1.00 59.14  ? 456 HOH A O   1 
HETATM 1359 O  O   . HOH F 6 .   ? 17.078 -28.074 9.803  1.00 45.64  ? 457 HOH A O   1 
HETATM 1360 O  O   . HOH F 6 .   ? 19.247 -7.540  35.271 1.00 54.18  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 15.942 -15.543 41.162 1.00 56.19  ? 459 HOH A O   1 
HETATM 1362 O  O   . HOH F 6 .   ? 25.332 -5.713  35.233 1.00 51.42  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 31.960 -23.792 34.690 1.00 57.15  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 28.036 -29.770 24.170 1.00 58.63  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 33.775 -13.923 41.520 0.50 36.37  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 17.493 -8.109  24.851 1.00 54.01  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 44.284 -13.433 13.840 0.50 53.56  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 45.397 -12.776 16.266 1.00 57.66  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 32.650 -20.494 36.996 1.00 62.69  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 18.931 -28.070 13.840 0.50 61.52  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 23.189 -4.535  17.226 1.00 69.08  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 21.156 -5.682  34.690 1.00 49.73  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 34.929 -23.695 32.804 1.00 57.11  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 16.723 -6.699  34.625 1.00 71.15  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 16.779 -29.980 12.383 1.00 52.40  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.283 -24.263 0.012  1.00 45.15  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 15.020 -25.775 -1.761 1.00 36.26  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 20.997 -38.285 4.034  1.00 42.99  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 11.652 -23.590 3.103  1.00 45.87  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 17.716 -36.303 6.132  1.00 36.48  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 20.866 -39.478 -2.148 1.00 52.85  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 18.667 -40.677 0.663  1.00 69.93  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.624 -24.764 5.553  1.00 50.70  ? 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   ? 0.7667 0.9385 0.6310 0.0423  -0.1287 -0.0273 6   ASP A N   
2    C CA  . ASP A 5   ? 0.7629 0.9267 0.6099 0.0265  -0.1202 -0.0294 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7430 0.9370 0.6148 0.0139  -0.1164 -0.0452 6   ASP A C   
4    O O   . ASP A 5   ? 0.7322 0.9544 0.6324 0.0171  -0.1215 -0.0548 6   ASP A O   
5    C CB  . ASP A 5   ? 0.7868 0.9207 0.6239 0.0175  -0.1025 -0.0217 6   ASP A CB  
6    C CG  . ASP A 5   ? 0.9804 1.0920 0.7834 0.0087  -0.0974 -0.0171 6   ASP A CG  
7    O OD1 . ASP A 5   ? 0.9877 1.1103 0.7882 -0.0020 -0.0956 -0.0257 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.0841 1.1664 0.8626 0.0113  -0.0940 -0.0059 6   ASP A OD2 
9    N N   . SER A 6   ? 0.6399 0.8270 0.5003 -0.0008 -0.1069 -0.0489 7   SER A N   
10   C CA  . SER A 6   ? 0.5948 0.8027 0.4731 -0.0146 -0.1010 -0.0633 7   SER A CA  
11   C C   . SER A 6   ? 0.5452 0.7389 0.4350 -0.0260 -0.0821 -0.0642 7   SER A C   
12   O O   . SER A 6   ? 0.5428 0.7386 0.4348 -0.0388 -0.0738 -0.0728 7   SER A O   
13   C CB  . SER A 6   ? 0.6730 0.8838 0.5288 -0.0218 -0.1056 -0.0682 7   SER A CB  
14   O OG  . SER A 6   ? 0.8398 1.0212 0.6669 -0.0268 -0.0972 -0.0600 7   SER A OG  
15   N N   . CYS A 7   ? 0.4222 0.6012 0.3189 -0.0206 -0.0761 -0.0559 8   CYS A N   
16   C CA  . CYS A 7   ? 0.3771 0.5424 0.2836 -0.0290 -0.0608 -0.0561 8   CYS A CA  
17   C C   . CYS A 7   ? 0.3752 0.5568 0.3063 -0.0375 -0.0554 -0.0678 8   CYS A C   
18   O O   . CYS A 7   ? 0.3621 0.5667 0.3089 -0.0353 -0.0621 -0.0746 8   CYS A O   
19   C CB  . CYS A 7   ? 0.3865 0.5349 0.2947 -0.0210 -0.0575 -0.0454 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.4656 0.5857 0.3426 -0.0161 -0.0573 -0.0321 8   CYS A SG  
21   N N   . ILE A 8   ? 0.2789 0.4474 0.2130 -0.0470 -0.0430 -0.0703 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2390 0.4121 0.1915 -0.0550 -0.0354 -0.0784 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2646 0.4212 0.2225 -0.0504 -0.0296 -0.0700 9   ILE A C   
24   O O   . ILE A 8   ? 0.2596 0.4005 0.2069 -0.0445 -0.0290 -0.0606 9   ILE A O   
25   C CB  . ILE A 8   ? 0.2831 0.4509 0.2333 -0.0679 -0.0270 -0.0876 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.2999 0.4442 0.2366 -0.0686 -0.0200 -0.0826 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.2947 0.4833 0.2424 -0.0737 -0.0332 -0.0981 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3291 0.4636 0.2650 -0.0791 -0.0107 -0.0915 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.1977 0.3564 0.1703 -0.0542 -0.0244 -0.0739 10  GLN A N   
30   N N   B GLN A 9   ? 0.1951 0.3555 0.1683 -0.0537 -0.0252 -0.0740 10  GLN A N   
31   C CA  A GLN A 9   ? 0.1899 0.3332 0.1660 -0.0503 -0.0195 -0.0666 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.1827 0.3289 0.1605 -0.0501 -0.0202 -0.0672 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2449 0.3741 0.2240 -0.0593 -0.0096 -0.0703 10  GLN A C   
34   C C   B GLN A 9   ? 0.2232 0.3538 0.2024 -0.0593 -0.0101 -0.0706 10  GLN A C   
35   O O   A GLN A 9   ? 0.2441 0.3812 0.2296 -0.0684 -0.0063 -0.0796 10  GLN A O   
36   O O   B GLN A 9   ? 0.2175 0.3536 0.2009 -0.0690 -0.0063 -0.0800 10  GLN A O   
37   C CB  A GLN A 9   ? 0.1990 0.3566 0.1874 -0.0430 -0.0244 -0.0655 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.1880 0.3504 0.1801 -0.0446 -0.0242 -0.0683 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2067 0.3494 0.1979 -0.0393 -0.0195 -0.0585 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2831 0.4330 0.2811 -0.0441 -0.0174 -0.0643 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5429 0.7010 0.5488 -0.0344 -0.0219 -0.0610 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4008 0.5502 0.4009 -0.0322 -0.0218 -0.0565 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4279 0.6009 0.4468 -0.0412 -0.0189 -0.0708 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.2484 0.4065 0.2460 -0.0228 -0.0308 -0.0536 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.5830 0.7373 0.5871 -0.0231 -0.0265 -0.0531 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.2585 0.3951 0.2610 -0.0324 -0.0157 -0.0530 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2200 0.3277 0.1935 -0.0569 -0.0052 -0.0634 11  PHE A N   
48   N N   B PHE A 10  ? 0.1885 0.2986 0.1632 -0.0561 -0.0061 -0.0631 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2239 0.3140 0.1968 -0.0631 0.0023  -0.0654 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.1921 0.2836 0.1654 -0.0618 0.0015  -0.0645 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2462 0.3340 0.2249 -0.0619 0.0042  -0.0625 11  PHE A C   
52   C C   B PHE A 10  ? 0.2352 0.3250 0.2147 -0.0612 0.0036  -0.0622 11  PHE A C   
53   O O   A PHE A 10  ? 0.2352 0.3164 0.2130 -0.0545 0.0026  -0.0546 11  PHE A O   
54   O O   B PHE A 10  ? 0.2216 0.3072 0.2012 -0.0535 0.0016  -0.0546 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2498 0.3198 0.2146 -0.0604 0.0047  -0.0615 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2161 0.2890 0.1816 -0.0579 0.0031  -0.0593 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2680 0.3177 0.2294 -0.0653 0.0104  -0.0641 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2446 0.3157 0.2046 -0.0622 0.0048  -0.0652 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3088 0.3547 0.2672 -0.0742 0.0145  -0.0725 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.2875 0.3716 0.2433 -0.0617 0.0010  -0.0666 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.2959 0.3282 0.2548 -0.0609 0.0113  -0.0582 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.2920 0.3466 0.2492 -0.0668 0.0100  -0.0697 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3333 0.3550 0.2846 -0.0780 0.0196  -0.0741 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3076 0.3901 0.2576 -0.0667 0.0035  -0.0731 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3289 0.3389 0.2807 -0.0639 0.0150  -0.0596 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3380 0.3908 0.2910 -0.0707 0.0123  -0.0764 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3097 0.3128 0.2569 -0.0722 0.0192  -0.0671 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3096 0.3771 0.2595 -0.0711 0.0095  -0.0784 11  PHE A CZ  
69   N N   . THR A 11  ? 0.1999 0.2945 0.1844 -0.0703 0.0082  -0.0699 12  THR A N   
70   C CA  . THR A 11  ? 0.2000 0.2951 0.1903 -0.0719 0.0119  -0.0700 12  THR A CA  
71   C C   . THR A 11  ? 0.2548 0.3254 0.2364 -0.0684 0.0146  -0.0613 12  THR A C   
72   O O   . THR A 11  ? 0.2426 0.3158 0.2283 -0.0630 0.0136  -0.0571 12  THR A O   
73   C CB  . THR A 11  ? 0.2789 0.3786 0.2727 -0.0856 0.0192  -0.0810 12  THR A CB  
74   O OG1 . THR A 11  ? 0.2705 0.3981 0.2753 -0.0881 0.0153  -0.0902 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3375 0.4383 0.3367 -0.0894 0.0251  -0.0828 12  THR A CG2 
76   N N   A ARG A 12  ? 0.2331 0.2802 0.2029 -0.0708 0.0173  -0.0595 13  ARG A N   
77   N N   B ARG A 12  ? 0.2364 0.2835 0.2062 -0.0709 0.0173  -0.0596 13  ARG A N   
78   C CA  A ARG A 12  ? 0.2416 0.2652 0.2019 -0.0675 0.0183  -0.0525 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.2458 0.2695 0.2062 -0.0675 0.0184  -0.0525 13  ARG A CA  
80   C C   A ARG A 12  ? 0.2649 0.2860 0.2253 -0.0566 0.0128  -0.0451 13  ARG A C   
81   C C   B ARG A 12  ? 0.2659 0.2873 0.2265 -0.0566 0.0128  -0.0450 13  ARG A C   
82   O O   A ARG A 12  ? 0.2575 0.2620 0.2116 -0.0533 0.0123  -0.0403 13  ARG A O   
83   O O   B ARG A 12  ? 0.2577 0.2627 0.2121 -0.0533 0.0123  -0.0402 13  ARG A O   
84   C CB  A ARG A 12  ? 0.2990 0.2967 0.2457 -0.0735 0.0225  -0.0544 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.3121 0.3099 0.2588 -0.0734 0.0224  -0.0543 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.4078 0.3992 0.3489 -0.0868 0.0306  -0.0612 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.4666 0.4537 0.4057 -0.0853 0.0304  -0.0588 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.5338 0.5197 0.4714 -0.0905 0.0349  -0.0593 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.5910 0.5664 0.5221 -0.0954 0.0357  -0.0660 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.6410 0.5969 0.5614 -0.0869 0.0341  -0.0517 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.6439 0.5962 0.5642 -0.0900 0.0330  -0.0632 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.7359 0.6850 0.6510 -0.0866 0.0354  -0.0476 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.7500 0.7042 0.6718 -0.0914 0.0331  -0.0687 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.4952 0.4655 0.4226 -0.0891 0.0385  -0.0507 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.6614 0.5946 0.5751 -0.0853 0.0309  -0.0670 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.6040 0.5256 0.5016 -0.0831 0.0331  -0.0410 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.4301 0.4078 0.3618 -0.0986 0.0350  -0.0767 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.2113 0.2481 0.1775 -0.0519 0.0087  -0.0446 14  HIS A N   
99   C CA  . HIS A 13  ? 0.2081 0.2419 0.1732 -0.0441 0.0055  -0.0390 14  HIS A CA  
100  C C   . HIS A 13  ? 0.2410 0.2703 0.2067 -0.0392 0.0048  -0.0329 14  HIS A C   
101  O O   . HIS A 13  ? 0.2351 0.2530 0.1979 -0.0360 0.0041  -0.0300 14  HIS A O   
102  C CB  . HIS A 13  ? 0.2027 0.2510 0.1692 -0.0415 0.0024  -0.0392 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.2250 0.2684 0.1887 -0.0364 0.0016  -0.0348 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.2363 0.2714 0.1987 -0.0366 0.0034  -0.0373 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.2362 0.2815 0.1985 -0.0316 0.0001  -0.0294 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.2293 0.2642 0.1910 -0.0332 0.0035  -0.0342 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.2287 0.2679 0.1887 -0.0307 0.0019  -0.0290 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.2047 0.2442 0.1752 -0.0382 0.0046  -0.0319 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2016 0.2366 0.1724 -0.0339 0.0046  -0.0269 15  ALA A CA  
110  C C   . ALA A 14  ? 0.2371 0.2553 0.2017 -0.0368 0.0072  -0.0260 15  ALA A C   
111  O O   . ALA A 14  ? 0.2110 0.2206 0.1727 -0.0333 0.0061  -0.0221 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2101 0.2589 0.1884 -0.0317 0.0043  -0.0277 15  ALA A CB  
113  N N   A SER A 15  ? 0.2085 0.2210 0.1694 -0.0439 0.0107  -0.0300 16  SER A N   
114  N N   B SER A 15  ? 0.2139 0.2263 0.1748 -0.0439 0.0107  -0.0300 16  SER A N   
115  N N   C SER A 15  ? 0.2111 0.2235 0.1719 -0.0440 0.0108  -0.0300 16  SER A N   
116  C CA  A SER A 15  ? 0.2187 0.2108 0.1682 -0.0474 0.0130  -0.0287 16  SER A CA  
117  C CA  B SER A 15  ? 0.2272 0.2191 0.1765 -0.0475 0.0131  -0.0287 16  SER A CA  
118  C CA  C SER A 15  ? 0.2229 0.2147 0.1722 -0.0473 0.0130  -0.0286 16  SER A CA  
119  C C   A SER A 15  ? 0.2760 0.2525 0.2183 -0.0431 0.0088  -0.0262 16  SER A C   
120  C C   B SER A 15  ? 0.2825 0.2588 0.2245 -0.0432 0.0089  -0.0262 16  SER A C   
121  C C   C SER A 15  ? 0.2828 0.2589 0.2248 -0.0433 0.0089  -0.0262 16  SER A C   
122  O O   A SER A 15  ? 0.2507 0.2144 0.1860 -0.0403 0.0066  -0.0227 16  SER A O   
123  O O   B SER A 15  ? 0.2622 0.2256 0.1972 -0.0404 0.0067  -0.0227 16  SER A O   
124  O O   C SER A 15  ? 0.2666 0.2293 0.2012 -0.0406 0.0067  -0.0228 16  SER A O   
125  C CB  A SER A 15  ? 0.2557 0.2423 0.1996 -0.0576 0.0190  -0.0339 16  SER A CB  
126  C CB  B SER A 15  ? 0.2755 0.2621 0.2194 -0.0577 0.0190  -0.0341 16  SER A CB  
127  C CB  C SER A 15  ? 0.2668 0.2534 0.2107 -0.0576 0.0192  -0.0337 16  SER A CB  
128  O OG  A SER A 15  ? 0.2830 0.2452 0.2105 -0.0613 0.0213  -0.0317 16  SER A OG  
129  O OG  B SER A 15  ? 0.3281 0.3325 0.2820 -0.0616 0.0231  -0.0385 16  SER A OG  
130  O OG  C SER A 15  ? 0.3194 0.3049 0.2620 -0.0615 0.0199  -0.0380 16  SER A OG  
131  N N   . ASP A 16  ? 0.2545 0.2336 0.1993 -0.0422 0.0074  -0.0290 17  ASP A N   
132  C CA  . ASP A 16  ? 0.2653 0.2329 0.2071 -0.0370 0.0035  -0.0289 17  ASP A CA  
133  C C   . ASP A 16  ? 0.2622 0.2374 0.2111 -0.0301 -0.0001 -0.0262 17  ASP A C   
134  O O   . ASP A 16  ? 0.2622 0.2280 0.2090 -0.0252 -0.0041 -0.0256 17  ASP A O   
135  C CB  . ASP A 16  ? 0.2772 0.2491 0.2222 -0.0382 0.0043  -0.0340 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.3734 0.3328 0.3097 -0.0455 0.0081  -0.0379 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.3814 0.3260 0.3070 -0.0501 0.0105  -0.0364 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.3776 0.3407 0.3161 -0.0477 0.0095  -0.0430 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.2012 0.1927 0.1576 -0.0296 0.0011  -0.0251 18  VAL A N   
140  C CA  . VAL A 17  ? 0.1940 0.1905 0.1549 -0.0253 -0.0004 -0.0230 18  VAL A CA  
141  C C   . VAL A 17  ? 0.2366 0.2244 0.1936 -0.0242 -0.0016 -0.0199 18  VAL A C   
142  O O   . VAL A 17  ? 0.2267 0.2113 0.1849 -0.0209 -0.0046 -0.0202 18  VAL A O   
143  C CB  . VAL A 17  ? 0.2148 0.2243 0.1792 -0.0253 0.0014  -0.0213 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.2154 0.2249 0.1808 -0.0228 0.0018  -0.0185 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.2016 0.2187 0.1669 -0.0264 0.0020  -0.0245 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.2138 0.1990 0.1666 -0.0274 0.0008  -0.0181 19  LEU A N   
147  C CA  . LEU A 18  ? 0.2245 0.2013 0.1719 -0.0275 0.0006  -0.0156 19  LEU A CA  
148  C C   . LEU A 18  ? 0.2695 0.2294 0.2066 -0.0265 -0.0035 -0.0155 19  LEU A C   
149  O O   . LEU A 18  ? 0.2434 0.1987 0.1780 -0.0237 -0.0072 -0.0145 19  LEU A O   
150  C CB  . LEU A 18  ? 0.2339 0.2123 0.1796 -0.0318 0.0055  -0.0155 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.2761 0.2486 0.2174 -0.0322 0.0068  -0.0136 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.2709 0.2513 0.2195 -0.0278 0.0064  -0.0119 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.3302 0.3042 0.2704 -0.0374 0.0129  -0.0156 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.2591 0.2088 0.1893 -0.0286 -0.0036 -0.0170 20  LEU A N   
155  C CA  . LEU A 19  ? 0.2847 0.2135 0.2017 -0.0262 -0.0086 -0.0163 20  LEU A CA  
156  C C   . LEU A 19  ? 0.2896 0.2226 0.2148 -0.0175 -0.0159 -0.0181 20  LEU A C   
157  O O   . LEU A 19  ? 0.2809 0.2045 0.1997 -0.0129 -0.0224 -0.0170 20  LEU A O   
158  C CB  . LEU A 19  ? 0.3180 0.2345 0.2268 -0.0300 -0.0061 -0.0183 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.4376 0.3267 0.3288 -0.0269 -0.0113 -0.0170 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.4808 0.3497 0.3511 -0.0315 -0.0105 -0.0128 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5026 0.3804 0.3880 -0.0307 -0.0078 -0.0200 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.2420 0.1911 0.1818 -0.0155 -0.0148 -0.0217 21  ASN A N   
163  C CA  . ASN A 20  ? 0.2380 0.1955 0.1892 -0.0088 -0.0196 -0.0257 21  ASN A CA  
164  C C   . ASN A 20  ? 0.2560 0.2231 0.2131 -0.0081 -0.0208 -0.0254 21  ASN A C   
165  O O   . ASN A 20  ? 0.2462 0.2150 0.2082 -0.0026 -0.0271 -0.0288 21  ASN A O   
166  C CB  . ASN A 20  ? 0.2426 0.2135 0.2053 -0.0092 -0.0160 -0.0304 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.3836 0.3433 0.3422 -0.0075 -0.0171 -0.0334 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.3274 0.2683 0.2757 -0.0035 -0.0222 -0.0325 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.2831 0.2514 0.2469 -0.0106 -0.0123 -0.0370 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.2273 0.2008 0.1845 -0.0132 -0.0151 -0.0222 22  LEU A N   
171  C CA  . LEU A 21  ? 0.2150 0.1939 0.1752 -0.0138 -0.0148 -0.0219 22  LEU A CA  
172  C C   . LEU A 21  ? 0.2502 0.2166 0.1999 -0.0122 -0.0205 -0.0204 22  LEU A C   
173  O O   . LEU A 21  ? 0.2235 0.1939 0.1772 -0.0100 -0.0248 -0.0232 22  LEU A O   
174  C CB  . LEU A 21  ? 0.2054 0.1888 0.1651 -0.0182 -0.0078 -0.0183 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.2287 0.2229 0.1952 -0.0192 -0.0035 -0.0191 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.2263 0.2220 0.1902 -0.0209 0.0011  -0.0150 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.2572 0.2599 0.2323 -0.0190 -0.0028 -0.0238 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.2315 0.1823 0.1666 -0.0143 -0.0203 -0.0167 23  ASN A N   
179  C CA  . ASN A 22  ? 0.2509 0.1856 0.1705 -0.0136 -0.0257 -0.0148 23  ASN A CA  
180  C C   . ASN A 22  ? 0.3069 0.2350 0.2247 -0.0051 -0.0368 -0.0173 23  ASN A C   
181  O O   . ASN A 22  ? 0.3051 0.2291 0.2173 -0.0020 -0.0442 -0.0178 23  ASN A O   
182  C CB  . ASN A 22  ? 0.2931 0.2107 0.1951 -0.0196 -0.0212 -0.0110 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.3857 0.2865 0.2685 -0.0214 -0.0242 -0.0086 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.3423 0.2489 0.2273 -0.0209 -0.0263 -0.0094 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4070 0.2854 0.2688 -0.0247 -0.0239 -0.0059 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.2730 0.2009 0.1965 -0.0008 -0.0386 -0.0197 24  ARG A N   
187  C CA  . ARG A 23  ? 0.2889 0.2123 0.2143 0.0095  -0.0495 -0.0235 24  ARG A CA  
188  C C   . ARG A 23  ? 0.3212 0.2675 0.2669 0.0137  -0.0536 -0.0303 24  ARG A C   
189  O O   . ARG A 23  ? 0.3208 0.2657 0.2661 0.0213  -0.0646 -0.0333 24  ARG A O   
190  C CB  . ARG A 23  ? 0.2795 0.2003 0.2099 0.0128  -0.0485 -0.0262 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.3744 0.2680 0.2825 0.0097  -0.0466 -0.0212 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.4211 0.3164 0.3358 0.0084  -0.0412 -0.0244 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.5370 0.4043 0.4297 0.0047  -0.0390 -0.0209 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.7551 0.6179 0.6477 0.0012  -0.0334 -0.0234 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.5796 0.4647 0.4924 0.0013  -0.0297 -0.0290 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.6277 0.4625 0.4984 -0.0036 -0.0307 -0.0208 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.2668 0.2336 0.2287 0.0081  -0.0449 -0.0332 25  LEU A N   
198  C CA  . LEU A 24  ? 0.2425 0.2301 0.2222 0.0088  -0.0460 -0.0406 25  LEU A CA  
199  C C   . LEU A 24  ? 0.2908 0.2759 0.2630 0.0068  -0.0497 -0.0392 25  LEU A C   
200  O O   . LEU A 24  ? 0.2906 0.2857 0.2716 0.0115  -0.0578 -0.0459 25  LEU A O   
201  C CB  . LEU A 24  ? 0.2218 0.2246 0.2130 0.0013  -0.0345 -0.0423 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.2566 0.2650 0.2557 0.0017  -0.0299 -0.0453 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.2498 0.2701 0.2547 -0.0063 -0.0190 -0.0460 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.2720 0.2896 0.2859 0.0100  -0.0365 -0.0550 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.2583 0.2314 0.2153 0.0002  -0.0441 -0.0318 26  ARG A N   
206  C CA  . ARG A 25  ? 0.2693 0.2379 0.2167 -0.0025 -0.0466 -0.0308 26  ARG A CA  
207  C C   . ARG A 25  ? 0.3384 0.2948 0.2733 0.0051  -0.0606 -0.0312 26  ARG A C   
208  O O   . ARG A 25  ? 0.3263 0.2906 0.2645 0.0069  -0.0678 -0.0362 26  ARG A O   
209  C CB  . ARG A 25  ? 0.2840 0.2402 0.2167 -0.0100 -0.0379 -0.0238 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.3497 0.3018 0.2730 -0.0137 -0.0390 -0.0240 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.3777 0.3208 0.2904 -0.0209 -0.0293 -0.0194 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.3622 0.2883 0.2585 -0.0221 -0.0282 -0.0145 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.5372 0.4469 0.4134 -0.0267 -0.0270 -0.0119 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.4705 0.3784 0.3399 -0.0293 -0.0284 -0.0137 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.4026 0.2970 0.2643 -0.0299 -0.0236 -0.0085 26  ARG A NH2 
216  N N   A SER A 26  ? 0.3289 0.2649 0.2480 0.0092  -0.0645 -0.0263 27  SER A N   
217  N N   B SER A 26  ? 0.3230 0.2588 0.2419 0.0092  -0.0646 -0.0263 27  SER A N   
218  N N   C SER A 26  ? 0.3181 0.2540 0.2371 0.0092  -0.0646 -0.0263 27  SER A N   
219  C CA  A SER A 26  ? 0.3615 0.2784 0.2623 0.0174  -0.0783 -0.0247 27  SER A CA  
220  C CA  B SER A 26  ? 0.3523 0.2693 0.2529 0.0173  -0.0784 -0.0248 27  SER A CA  
221  C CA  C SER A 26  ? 0.3458 0.2624 0.2462 0.0173  -0.0783 -0.0247 27  SER A CA  
222  C C   A SER A 26  ? 0.4058 0.3391 0.3243 0.0286  -0.0912 -0.0335 27  SER A C   
223  C C   B SER A 26  ? 0.4046 0.3365 0.3222 0.0292  -0.0917 -0.0333 27  SER A C   
224  C C   C SER A 26  ? 0.4011 0.3327 0.3185 0.0292  -0.0917 -0.0332 27  SER A C   
225  O O   A SER A 26  ? 0.4175 0.3475 0.3278 0.0341  -0.1035 -0.0352 27  SER A O   
226  O O   B SER A 26  ? 0.4194 0.3449 0.3268 0.0360  -0.1051 -0.0344 27  SER A O   
227  O O   C SER A 26  ? 0.4159 0.3405 0.3226 0.0360  -0.1050 -0.0341 27  SER A O   
228  C CB  A SER A 26  ? 0.4297 0.3223 0.3140 0.0198  -0.0783 -0.0193 27  SER A CB  
229  C CB  B SER A 26  ? 0.4111 0.3003 0.2903 0.0181  -0.0779 -0.0181 27  SER A CB  
230  C CB  C SER A 26  ? 0.3997 0.2900 0.2808 0.0185  -0.0776 -0.0184 27  SER A CB  
231  O OG  A SER A 26  ? 0.5504 0.4255 0.4148 0.0093  -0.0682 -0.0124 27  SER A OG  
232  O OG  B SER A 26  ? 0.4740 0.3671 0.3662 0.0245  -0.0788 -0.0212 27  SER A OG  
233  O OG  C SER A 26  ? 0.4915 0.3576 0.3504 0.0272  -0.0912 -0.0158 27  SER A OG  
234  N N   . ARG A 27  ? 0.3408 0.2934 0.2842 0.0318  -0.0883 -0.0402 28  ARG A N   
235  C CA  . ARG A 27  ? 0.3520 0.3245 0.3177 0.0425  -0.0987 -0.0511 28  ARG A CA  
236  C C   . ARG A 27  ? 0.3611 0.3642 0.3502 0.0371  -0.0953 -0.0608 28  ARG A C   
237  O O   . ARG A 27  ? 0.3646 0.3900 0.3767 0.0439  -0.1021 -0.0725 28  ARG A O   
238  C CB  . ARG A 27  ? 0.3757 0.3511 0.3544 0.0480  -0.0963 -0.0547 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.5115 0.4542 0.4657 0.0527  -0.0994 -0.0461 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.5910 0.5359 0.5572 0.0559  -0.0946 -0.0498 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.7758 0.7351 0.7630 0.0699  -0.1054 -0.0610 28  ARG A NE  
242  C CZ  . ARG A 27  ? 0.9616 0.9409 0.9734 0.0713  -0.0998 -0.0705 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 0.8257 0.8195 0.8584 0.0847  -0.1097 -0.0823 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 0.7807 0.7664 0.7966 0.0597  -0.0844 -0.0692 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.2970 0.3006 0.2802 0.0247  -0.0845 -0.0568 29  ASP A N   
246  C CA  . ASP A 28  ? 0.2864 0.3126 0.2862 0.0165  -0.0784 -0.0646 29  ASP A CA  
247  C C   . ASP A 28  ? 0.3236 0.3729 0.3494 0.0140  -0.0698 -0.0736 29  ASP A C   
248  O O   . ASP A 28  ? 0.3144 0.3873 0.3605 0.0118  -0.0696 -0.0854 29  ASP A O   
249  C CB  . ASP A 28  ? 0.3210 0.3572 0.3238 0.0208  -0.0918 -0.0722 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.3928 0.4443 0.4038 0.0093  -0.0841 -0.0781 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.3881 0.4303 0.3898 -0.0012 -0.0706 -0.0715 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.4262 0.4991 0.4534 0.0109  -0.0915 -0.0902 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.2599 0.3025 0.2844 0.0134  -0.0622 -0.0689 30  ILE A N   
254  C CA  . ILE A 29  ? 0.2404 0.3010 0.2846 0.0103  -0.0532 -0.0766 30  ILE A CA  
255  C C   . ILE A 29  ? 0.2778 0.3391 0.3189 -0.0027 -0.0379 -0.0730 30  ILE A C   
256  O O   . ILE A 29  ? 0.2508 0.2954 0.2752 -0.0060 -0.0326 -0.0621 30  ILE A O   
257  C CB  . ILE A 29  ? 0.2762 0.3303 0.3213 0.0173  -0.0543 -0.0756 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.2957 0.3491 0.3461 0.0322  -0.0701 -0.0811 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.2503 0.3209 0.3116 0.0114  -0.0424 -0.0828 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.3216 0.3578 0.3642 0.0392  -0.0716 -0.0770 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.2371 0.3173 0.2939 -0.0099 -0.0308 -0.0829 31  LEU A N   
262  N N   B LEU A 30  ? 0.2474 0.3277 0.3044 -0.0099 -0.0308 -0.0830 31  LEU A N   
263  C CA  A LEU A 30  ? 0.2258 0.3047 0.2784 -0.0222 -0.0161 -0.0808 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.2429 0.3224 0.2960 -0.0223 -0.0162 -0.0812 31  LEU A CA  
265  C C   A LEU A 30  ? 0.2600 0.3229 0.2950 -0.0274 -0.0131 -0.0715 31  LEU A C   
266  C C   B LEU A 30  ? 0.2707 0.3338 0.3058 -0.0274 -0.0131 -0.0716 31  LEU A C   
267  O O   A LEU A 30  ? 0.2385 0.2932 0.2648 -0.0347 -0.0023 -0.0663 31  LEU A O   
268  O O   B LEU A 30  ? 0.2520 0.3069 0.2785 -0.0347 -0.0023 -0.0665 31  LEU A O   
269  C CB  A LEU A 30  ? 0.2239 0.2979 0.2724 -0.0243 -0.0075 -0.0764 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.2463 0.3219 0.2963 -0.0247 -0.0072 -0.0775 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.2758 0.3669 0.3421 -0.0235 -0.0048 -0.0876 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.3113 0.4055 0.3782 -0.0302 0.0008  -0.0899 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.2552 0.3415 0.3135 -0.0314 0.0077  -0.0844 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.3157 0.4178 0.3940 -0.0218 -0.0039 -0.0954 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.3036 0.4179 0.3911 -0.0274 -0.0034 -0.1033 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.3334 0.4199 0.3888 -0.0415 0.0152  -0.0858 31  LEU A CD2 
277  N N   . THR A 31  ? 0.2305 0.2887 0.2598 -0.0234 -0.0226 -0.0703 32  THR A N   
278  C CA  . THR A 31  ? 0.2396 0.2845 0.2538 -0.0288 -0.0193 -0.0640 32  THR A CA  
279  C C   . THR A 31  ? 0.2978 0.3536 0.3209 -0.0392 -0.0106 -0.0726 32  THR A C   
280  O O   . THR A 31  ? 0.2911 0.3668 0.3320 -0.0405 -0.0125 -0.0849 32  THR A O   
281  C CB  . THR A 31  ? 0.3145 0.3524 0.3193 -0.0234 -0.0313 -0.0625 32  THR A CB  
282  O OG1 . THR A 31  ? 0.3231 0.3786 0.3427 -0.0187 -0.0417 -0.0735 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.2981 0.3188 0.2883 -0.0161 -0.0368 -0.0528 32  THR A CG2 
284  N N   . ASP A 32  ? 0.2600 0.3026 0.2715 -0.0467 -0.0002 -0.0671 33  ASP A N   
285  C CA  . ASP A 32  ? 0.2562 0.3029 0.2716 -0.0581 0.0107  -0.0741 33  ASP A CA  
286  C C   . ASP A 32  ? 0.2910 0.3252 0.2950 -0.0640 0.0147  -0.0723 33  ASP A C   
287  O O   . ASP A 32  ? 0.2942 0.3245 0.2962 -0.0743 0.0257  -0.0761 33  ASP A O   
288  C CB  . ASP A 32  ? 0.2657 0.3055 0.2767 -0.0624 0.0224  -0.0701 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.3441 0.3641 0.3384 -0.0576 0.0240  -0.0562 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.2956 0.3061 0.2817 -0.0532 0.0193  -0.0501 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.4022 0.4175 0.3919 -0.0584 0.0299  -0.0522 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.2417 0.2676 0.2363 -0.0585 0.0068  -0.0671 34  VAL A N   
293  C CA  . VAL A 33  ? 0.2432 0.2575 0.2267 -0.0640 0.0104  -0.0665 34  VAL A CA  
294  C C   . VAL A 33  ? 0.2929 0.3056 0.2695 -0.0588 -0.0013 -0.0656 34  VAL A C   
295  O O   . VAL A 33  ? 0.2895 0.3007 0.2632 -0.0501 -0.0101 -0.0606 34  VAL A O   
296  C CB  . VAL A 33  ? 0.2903 0.2829 0.2596 -0.0652 0.0211  -0.0564 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.2741 0.2573 0.2348 -0.0563 0.0166  -0.0462 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.2956 0.2762 0.2562 -0.0730 0.0286  -0.0589 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.2594 0.2701 0.2308 -0.0649 -0.0009 -0.0707 35  VAL A N   
300  N N   B VAL A 34  ? 0.2625 0.2733 0.2339 -0.0649 -0.0011 -0.0708 35  VAL A N   
301  C CA  A VAL A 34  ? 0.2586 0.2633 0.2175 -0.0625 -0.0100 -0.0698 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.2640 0.2686 0.2228 -0.0619 -0.0104 -0.0694 35  VAL A CA  
303  C C   A VAL A 34  ? 0.3121 0.2973 0.2560 -0.0675 0.0004  -0.0647 35  VAL A C   
304  C C   B VAL A 34  ? 0.3177 0.3035 0.2613 -0.0676 -0.0006 -0.0653 35  VAL A C   
305  O O   A VAL A 34  ? 0.3133 0.2947 0.2584 -0.0755 0.0110  -0.0684 35  VAL A O   
306  O O   B VAL A 34  ? 0.3213 0.3047 0.2663 -0.0761 0.0092  -0.0701 35  VAL A O   
307  C CB  A VAL A 34  ? 0.3051 0.3262 0.2707 -0.0655 -0.0194 -0.0821 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.3139 0.3352 0.2790 -0.0614 -0.0235 -0.0801 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.3158 0.3273 0.2632 -0.0631 -0.0295 -0.0802 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.3177 0.3487 0.2900 -0.0729 -0.0176 -0.0918 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.2977 0.3414 0.2828 -0.0595 -0.0292 -0.0895 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.3249 0.3348 0.2711 -0.0562 -0.0350 -0.0757 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.2715 0.2432 0.2010 -0.0633 -0.0019 -0.0571 36  ILE A N   
314  C CA  . ILE A 35  ? 0.2810 0.2361 0.1975 -0.0672 0.0072  -0.0540 36  ILE A CA  
315  C C   . ILE A 35  ? 0.3544 0.3064 0.2576 -0.0707 0.0005  -0.0585 36  ILE A C   
316  O O   . ILE A 35  ? 0.3405 0.2915 0.2346 -0.0660 -0.0104 -0.0562 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3063 0.2506 0.2172 -0.0617 0.0112  -0.0446 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.2888 0.2376 0.2114 -0.0572 0.0150  -0.0401 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.3369 0.2671 0.2379 -0.0651 0.0210  -0.0439 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.2966 0.2438 0.2255 -0.0613 0.0248  -0.0422 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.3259 0.2745 0.2256 -0.0790 0.0069  -0.0650 37  VAL A N   
322  C CA  . VAL A 36  ? 0.3406 0.2865 0.2262 -0.0840 0.0012  -0.0706 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4054 0.3321 0.2743 -0.0869 0.0104  -0.0671 37  VAL A C   
324  O O   . VAL A 36  ? 0.3863 0.3046 0.2581 -0.0899 0.0236  -0.0672 37  VAL A O   
325  C CB  . VAL A 36  ? 0.3901 0.3472 0.2835 -0.0929 0.0018  -0.0828 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4055 0.3601 0.2828 -0.0985 -0.0045 -0.0892 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.3861 0.3660 0.2991 -0.0903 -0.0067 -0.0885 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.3749 0.2935 0.2254 -0.0859 0.0036  -0.0645 38  VAL A N   
329  C CA  . VAL A 37  ? 0.3859 0.2876 0.2197 -0.0897 0.0126  -0.0625 38  VAL A CA  
330  C C   . VAL A 37  ? 0.4553 0.3515 0.2676 -0.0959 0.0054  -0.0676 38  VAL A C   
331  O O   . VAL A 37  ? 0.4335 0.3267 0.2314 -0.0926 -0.0070 -0.0644 38  VAL A O   
332  C CB  . VAL A 37  ? 0.4307 0.3257 0.2606 -0.0840 0.0140  -0.0537 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.4383 0.3200 0.2577 -0.0886 0.0270  -0.0540 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.4044 0.3089 0.2555 -0.0766 0.0159  -0.0489 38  VAL A CG2 
335  N N   A SER A 38  ? 0.4533 0.3428 0.2581 -0.1048 0.0141  -0.0747 39  SER A N   
336  N N   B SER A 38  ? 0.4126 0.3110 0.2268 -0.1037 0.0103  -0.0766 39  SER A N   
337  C CA  A SER A 38  ? 0.4827 0.3656 0.2637 -0.1120 0.0080  -0.0803 39  SER A CA  
338  C CA  B SER A 38  ? 0.4240 0.3214 0.2224 -0.1116 0.0047  -0.0849 39  SER A CA  
339  C C   A SER A 38  ? 0.5365 0.4302 0.3129 -0.1078 -0.0127 -0.0814 39  SER A C   
340  C C   B SER A 38  ? 0.4584 0.3705 0.2576 -0.1071 -0.0152 -0.0872 39  SER A C   
341  O O   A SER A 38  ? 0.5435 0.4266 0.2952 -0.1068 -0.0228 -0.0783 39  SER A O   
342  O O   B SER A 38  ? 0.4343 0.3647 0.2557 -0.1055 -0.0183 -0.0919 39  SER A O   
343  C CB  A SER A 38  ? 0.5694 0.4331 0.3262 -0.1151 0.0142  -0.0765 39  SER A CB  
344  C CB  B SER A 38  ? 0.4906 0.3687 0.2622 -0.1171 0.0102  -0.0840 39  SER A CB  
345  O OG  A SER A 38  ? 0.7062 0.5616 0.4656 -0.1204 0.0323  -0.0798 39  SER A OG  
346  O OG  B SER A 38  ? 0.5684 0.4378 0.3458 -0.1208 0.0286  -0.0857 39  SER A OG  
347  N N   A ARG A 39  ? 0.4763 0.3905 0.2764 -0.1047 -0.0188 -0.0860 40  ARG A N   
348  N N   B ARG A 39  ? 0.4329 0.3369 0.2085 -0.1044 -0.0284 -0.0841 40  ARG A N   
349  C CA  A ARG A 39  ? 0.4807 0.4113 0.2852 -0.0989 -0.0384 -0.0897 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.4338 0.3518 0.2114 -0.0973 -0.0492 -0.0866 40  ARG A CA  
351  C C   A ARG A 39  ? 0.5133 0.4393 0.3114 -0.0867 -0.0509 -0.0797 40  ARG A C   
352  C C   B ARG A 39  ? 0.4797 0.4062 0.2756 -0.0851 -0.0550 -0.0796 40  ARG A C   
353  O O   A ARG A 39  ? 0.5239 0.4518 0.3107 -0.0806 -0.0691 -0.0804 40  ARG A O   
354  O O   B ARG A 39  ? 0.4631 0.4119 0.2831 -0.0809 -0.0619 -0.0855 40  ARG A O   
355  C CB  A ARG A 39  ? 0.5125 0.4456 0.3003 -0.1050 -0.0490 -0.0990 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.4598 0.3634 0.2026 -0.0975 -0.0633 -0.0857 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.6541 0.5977 0.4533 -0.1168 -0.0400 -0.1119 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.5460 0.4486 0.2750 -0.1095 -0.0611 -0.0961 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.7364 0.6924 0.5269 -0.1202 -0.0562 -0.1229 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.5743 0.4659 0.2688 -0.1091 -0.0787 -0.0966 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.8180 0.7788 0.6115 -0.1344 -0.0464 -0.1358 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.5896 0.4795 0.2693 -0.1219 -0.0752 -0.1069 40  ARG A NE  
363  C CZ  A ARG A 39  ? 0.9826 0.9256 0.7528 -0.1444 -0.0380 -0.1384 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.7674 0.6780 0.4557 -0.1250 -0.0859 -0.1195 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.8093 0.7292 0.5515 -0.1425 -0.0372 -0.1290 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.5914 0.5283 0.3056 -0.1159 -0.1006 -0.1242 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.8098 0.7573 0.5840 -0.1574 -0.0290 -0.1512 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.6659 0.5725 0.3382 -0.1378 -0.0814 -0.1290 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.4205 0.3392 0.2248 -0.0828 -0.0413 -0.0708 41  GLU A N   
370  N N   B GLU A 40  ? 0.4129 0.3232 0.1999 -0.0813 -0.0493 -0.0688 41  GLU A N   
371  C CA  A GLU A 40  ? 0.4136 0.3277 0.2157 -0.0725 -0.0494 -0.0619 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.3905 0.3043 0.1895 -0.0708 -0.0539 -0.0617 41  GLU A CA  
373  C C   A GLU A 40  ? 0.4239 0.3541 0.2566 -0.0685 -0.0433 -0.0617 41  GLU A C   
374  C C   B GLU A 40  ? 0.3991 0.3316 0.2310 -0.0689 -0.0461 -0.0638 41  GLU A C   
375  O O   A GLU A 40  ? 0.3915 0.3222 0.2351 -0.0734 -0.0282 -0.0620 41  GLU A O   
376  O O   B GLU A 40  ? 0.3527 0.2877 0.1951 -0.0758 -0.0321 -0.0669 41  GLU A O   
377  C CB  A GLU A 40  ? 0.4439 0.3338 0.2228 -0.0744 -0.0417 -0.0529 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.4154 0.3068 0.1956 -0.0702 -0.0473 -0.0513 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.6303 0.5009 0.3739 -0.0794 -0.0475 -0.0528 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.6254 0.4939 0.3694 -0.0765 -0.0485 -0.0496 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.0749 0.9273 0.7932 -0.0729 -0.0604 -0.0448 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.1099 0.9601 0.8256 -0.0706 -0.0636 -0.0432 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.1382 0.9674 0.8307 -0.0784 -0.0529 -0.0393 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.1192 0.9784 0.8413 -0.0602 -0.0808 -0.0437 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.0598 0.9202 0.7835 -0.0626 -0.0774 -0.0448 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.1576 0.9832 0.8434 -0.0766 -0.0580 -0.0382 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.3705 0.3134 0.2162 -0.0592 -0.0552 -0.0618 42  GLN A N   
388  C CA  . GLN A 41  ? 0.3488 0.3085 0.2226 -0.0566 -0.0499 -0.0634 42  GLN A CA  
389  C C   . GLN A 41  ? 0.3863 0.3397 0.2614 -0.0486 -0.0501 -0.0544 42  GLN A C   
390  O O   . GLN A 41  ? 0.3926 0.3373 0.2547 -0.0414 -0.0619 -0.0504 42  GLN A O   
391  C CB  . GLN A 41  ? 0.3718 0.3560 0.2647 -0.0536 -0.0615 -0.0742 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.5459 0.5403 0.4425 -0.0639 -0.0586 -0.0854 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.7592 0.7826 0.6806 -0.0635 -0.0664 -0.0987 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.6634 0.7014 0.6020 -0.0549 -0.0738 -0.1004 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.8162 0.8493 0.7409 -0.0738 -0.0638 -0.1098 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.3056 0.2617 0.1946 -0.0498 -0.0375 -0.0514 43  PHE A N   
397  C CA  . PHE A 42  ? 0.3091 0.2611 0.2009 -0.0434 -0.0367 -0.0439 43  PHE A CA  
398  C C   . PHE A 42  ? 0.3496 0.3186 0.2655 -0.0415 -0.0331 -0.0467 43  PHE A C   
399  O O   . PHE A 42  ? 0.3477 0.3200 0.2720 -0.0471 -0.0217 -0.0482 43  PHE A O   
400  C CB  . PHE A 42  ? 0.3334 0.2702 0.2147 -0.0471 -0.0245 -0.0369 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.3713 0.2904 0.2276 -0.0513 -0.0248 -0.0351 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.4028 0.3182 0.2519 -0.0590 -0.0187 -0.0394 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.4123 0.3161 0.2500 -0.0488 -0.0300 -0.0294 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.4432 0.3418 0.2674 -0.0641 -0.0180 -0.0384 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.4644 0.3494 0.2753 -0.0546 -0.0289 -0.0279 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.4449 0.3283 0.2495 -0.0622 -0.0229 -0.0326 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.2951 0.2721 0.2200 -0.0336 -0.0419 -0.0473 44  ARG A N   
408  C CA  . ARG A 43  ? 0.2663 0.2596 0.2130 -0.0325 -0.0378 -0.0509 44  ARG A CA  
409  C C   . ARG A 43  ? 0.3090 0.2939 0.2542 -0.0311 -0.0298 -0.0426 44  ARG A C   
410  O O   . ARG A 43  ? 0.3022 0.2738 0.2345 -0.0275 -0.0327 -0.0361 44  ARG A O   
411  C CB  . ARG A 43  ? 0.2771 0.2855 0.2371 -0.0244 -0.0507 -0.0578 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.3765 0.3998 0.3432 -0.0252 -0.0601 -0.0688 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.4656 0.5140 0.4573 -0.0194 -0.0677 -0.0800 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.5799 0.6391 0.5890 -0.0243 -0.0546 -0.0826 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.7349 0.8070 0.7566 -0.0349 -0.0437 -0.0905 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.6219 0.7017 0.6451 -0.0418 -0.0445 -0.0986 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.5367 0.6133 0.5681 -0.0394 -0.0317 -0.0911 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.2612 0.2527 0.2176 -0.0345 -0.0198 -0.0430 45  ALA A N   
419  C CA  . ALA A 44  ? 0.2586 0.2440 0.2135 -0.0329 -0.0134 -0.0358 45  ALA A CA  
420  C C   . ALA A 44  ? 0.2677 0.2632 0.2354 -0.0347 -0.0068 -0.0382 45  ALA A C   
421  O O   . ALA A 44  ? 0.2472 0.2540 0.2252 -0.0383 -0.0058 -0.0459 45  ALA A O   
422  C CB  . ALA A 44  ? 0.2811 0.2533 0.2245 -0.0362 -0.0054 -0.0302 45  ALA A CB  
423  N N   . HIS A 45  ? 0.2257 0.2172 0.1919 -0.0331 -0.0020 -0.0323 46  HIS A N   
424  C CA  . HIS A 45  ? 0.2117 0.2083 0.1842 -0.0353 0.0050  -0.0328 46  HIS A CA  
425  C C   . HIS A 45  ? 0.2659 0.2510 0.2297 -0.0382 0.0136  -0.0276 46  HIS A C   
426  O O   . HIS A 45  ? 0.2555 0.2327 0.2124 -0.0351 0.0139  -0.0217 46  HIS A O   
427  C CB  . HIS A 45  ? 0.2021 0.2014 0.1767 -0.0308 0.0031  -0.0300 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.2355 0.2419 0.2170 -0.0260 -0.0056 -0.0345 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.2587 0.2567 0.2326 -0.0213 -0.0126 -0.0310 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.2364 0.2562 0.2310 -0.0251 -0.0081 -0.0427 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.2462 0.2502 0.2272 -0.0163 -0.0202 -0.0362 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.2344 0.2535 0.2301 -0.0178 -0.0180 -0.0439 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.2498 0.2334 0.2137 -0.0441 0.0208  -0.0305 47  LYS A N   
434  C CA  . LYS A 46  ? 0.2455 0.2144 0.1993 -0.0458 0.0287  -0.0256 47  LYS A CA  
435  C C   . LYS A 46  ? 0.2770 0.2408 0.2259 -0.0396 0.0288  -0.0178 47  LYS A C   
436  O O   . LYS A 46  ? 0.2609 0.2156 0.2041 -0.0360 0.0300  -0.0133 47  LYS A O   
437  C CB  . LYS A 46  ? 0.2723 0.2375 0.2242 -0.0539 0.0373  -0.0295 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.2533 0.2228 0.2098 -0.0615 0.0389  -0.0384 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.2674 0.2334 0.2219 -0.0718 0.0493  -0.0436 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.3231 0.2990 0.2860 -0.0803 0.0503  -0.0550 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.3350 0.3087 0.2968 -0.0929 0.0622  -0.0622 47  LYS A NZ  
442  N N   . THR A 47  ? 0.2384 0.2098 0.1905 -0.0381 0.0270  -0.0173 48  THR A N   
443  C CA  . THR A 47  ? 0.2333 0.2016 0.1804 -0.0327 0.0263  -0.0109 48  THR A CA  
444  C C   . THR A 47  ? 0.2421 0.2128 0.1913 -0.0272 0.0214  -0.0083 48  THR A C   
445  O O   . THR A 47  ? 0.2384 0.2050 0.1841 -0.0227 0.0219  -0.0041 48  THR A O   
446  C CB  . THR A 47  ? 0.3048 0.2803 0.2533 -0.0335 0.0260  -0.0118 48  THR A CB  
447  O OG1 . THR A 47  ? 0.3056 0.2933 0.2648 -0.0333 0.0210  -0.0170 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.3433 0.3127 0.2851 -0.0402 0.0336  -0.0136 48  THR A CG2 
449  N N   . VAL A 48  ? 0.2087 0.1851 0.1628 -0.0276 0.0169  -0.0113 49  VAL A N   
450  C CA  . VAL A 48  ? 0.2110 0.1873 0.1644 -0.0248 0.0141  -0.0096 49  VAL A CA  
451  C C   . VAL A 48  ? 0.2440 0.2124 0.1934 -0.0251 0.0178  -0.0088 49  VAL A C   
452  O O   . VAL A 48  ? 0.2235 0.1918 0.1731 -0.0222 0.0191  -0.0073 49  VAL A O   
453  C CB  . VAL A 48  ? 0.2381 0.2164 0.1922 -0.0255 0.0084  -0.0123 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.2402 0.2139 0.1893 -0.0255 0.0079  -0.0109 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.2275 0.2131 0.1869 -0.0241 0.0053  -0.0139 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.2158 0.1790 0.1628 -0.0288 0.0197  -0.0114 50  LEU A N   
457  C CA  . LEU A 49  ? 0.2299 0.1844 0.1724 -0.0296 0.0242  -0.0117 50  LEU A CA  
458  C C   . LEU A 49  ? 0.2623 0.2110 0.2040 -0.0249 0.0287  -0.0083 50  LEU A C   
459  O O   . LEU A 49  ? 0.2449 0.1915 0.1872 -0.0215 0.0308  -0.0081 50  LEU A O   
460  C CB  . LEU A 49  ? 0.2348 0.1847 0.1745 -0.0353 0.0260  -0.0160 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.2588 0.2142 0.1987 -0.0385 0.0197  -0.0203 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.2635 0.2170 0.2022 -0.0446 0.0218  -0.0260 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.2779 0.2294 0.2109 -0.0379 0.0168  -0.0194 50  LEU A CD2 
464  N N   . MET A 50  ? 0.2314 0.1772 0.1709 -0.0243 0.0300  -0.0060 51  MET A N   
465  C CA  . MET A 50  ? 0.2409 0.1774 0.1755 -0.0184 0.0325  -0.0017 51  MET A CA  
466  C C   . MET A 50  ? 0.2762 0.2221 0.2162 -0.0109 0.0280  0.0005  51  MET A C   
467  O O   . MET A 50  ? 0.2753 0.2177 0.2161 -0.0040 0.0286  0.0016  51  MET A O   
468  C CB  . MET A 50  ? 0.2646 0.1935 0.1911 -0.0207 0.0348  0.0007  51  MET A CB  
469  C CG  . MET A 50  ? 0.2971 0.2170 0.2189 -0.0295 0.0410  -0.0030 51  MET A CG  
470  S SD  . MET A 50  ? 0.3449 0.2615 0.2591 -0.0354 0.0446  -0.0025 51  MET A SD  
471  C CE  . MET A 50  ? 0.3313 0.2217 0.2265 -0.0305 0.0490  0.0050  51  MET A CE  
472  N N   . ALA A 51  ? 0.2425 0.2010 0.1874 -0.0121 0.0237  -0.0001 52  ALA A N   
473  C CA  . ALA A 51  ? 0.2372 0.2070 0.1880 -0.0071 0.0197  0.0004  52  ALA A CA  
474  C C   . ALA A 51  ? 0.2597 0.2349 0.2175 -0.0060 0.0209  -0.0031 52  ALA A C   
475  O O   . ALA A 51  ? 0.2650 0.2498 0.2297 -0.0010 0.0191  -0.0042 52  ALA A O   
476  C CB  . ALA A 51  ? 0.2363 0.2158 0.1896 -0.0106 0.0161  -0.0007 52  ALA A CB  
477  N N   . CYS A 52  ? 0.2228 0.1926 0.1786 -0.0113 0.0242  -0.0058 53  CYS A N   
478  C CA  . CYS A 52  ? 0.2238 0.1966 0.1830 -0.0131 0.0272  -0.0099 53  CYS A CA  
479  C C   . CYS A 52  ? 0.2757 0.2411 0.2350 -0.0111 0.0326  -0.0121 53  CYS A C   
480  O O   . CYS A 52  ? 0.2674 0.2376 0.2316 -0.0117 0.0363  -0.0167 53  CYS A O   
481  C CB  . CYS A 52  ? 0.2239 0.1938 0.1770 -0.0209 0.0266  -0.0115 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.2613 0.2380 0.2148 -0.0227 0.0210  -0.0105 53  CYS A SG  
483  N N   . SER A 53  ? 0.2458 0.1989 0.1990 -0.0103 0.0344  -0.0100 54  SER A N   
484  C CA  . SER A 53  ? 0.2364 0.1790 0.1874 -0.0100 0.0404  -0.0128 54  SER A CA  
485  C C   . SER A 53  ? 0.3084 0.2382 0.2557 -0.0032 0.0420  -0.0097 54  SER A C   
486  O O   . SER A 53  ? 0.2836 0.2052 0.2231 -0.0053 0.0412  -0.0059 54  SER A O   
487  C CB  . SER A 53  ? 0.2643 0.2001 0.2070 -0.0196 0.0422  -0.0151 54  SER A CB  
488  O OG  . SER A 53  ? 0.3109 0.2333 0.2479 -0.0215 0.0476  -0.0170 54  SER A OG  
489  N N   . GLY A 54  ? 0.2880 0.2145 0.2399 0.0045  0.0448  -0.0118 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3057 0.2145 0.2511 0.0124  0.0462  -0.0085 55  GLY A CA  
491  C C   . GLY A 54  ? 0.3459 0.2353 0.2788 0.0044  0.0525  -0.0088 55  GLY A C   
492  O O   . GLY A 54  ? 0.3533 0.2250 0.2747 0.0057  0.0538  -0.0044 55  GLY A O   
493  N N   . LEU A 55  ? 0.3130 0.2049 0.2463 -0.0051 0.0566  -0.0144 56  LEU A N   
494  C CA  . LEU A 55  ? 0.3189 0.1958 0.2418 -0.0142 0.0622  -0.0166 56  LEU A CA  
495  C C   . LEU A 55  ? 0.3362 0.2139 0.2537 -0.0213 0.0595  -0.0138 56  LEU A C   
496  O O   . LEU A 55  ? 0.3395 0.2011 0.2475 -0.0244 0.0640  -0.0128 56  LEU A O   
497  C CB  . LEU A 55  ? 0.3182 0.1988 0.2411 -0.0226 0.0656  -0.0237 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.3815 0.2480 0.2946 -0.0320 0.0714  -0.0278 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.4028 0.2480 0.3111 -0.0274 0.0795  -0.0293 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.3675 0.2406 0.2780 -0.0412 0.0716  -0.0340 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.2912 0.1864 0.2143 -0.0240 0.0532  -0.0134 57  PHE A N   
502  C CA  . PHE A 56  ? 0.2838 0.1830 0.2051 -0.0300 0.0509  -0.0126 57  PHE A CA  
503  C C   . PHE A 56  ? 0.3317 0.2236 0.2480 -0.0257 0.0510  -0.0069 57  PHE A C   
504  O O   . PHE A 56  ? 0.3145 0.2003 0.2248 -0.0323 0.0542  -0.0074 57  PHE A O   
505  C CB  . PHE A 56  ? 0.2816 0.1987 0.2096 -0.0325 0.0439  -0.0139 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.2856 0.2050 0.2122 -0.0387 0.0432  -0.0193 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.3083 0.2229 0.2311 -0.0464 0.0459  -0.0244 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.2922 0.2180 0.2195 -0.0379 0.0397  -0.0199 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.3179 0.2346 0.2373 -0.0518 0.0439  -0.0296 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.3236 0.2484 0.2448 -0.0438 0.0382  -0.0241 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.3006 0.2213 0.2179 -0.0501 0.0395  -0.0288 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.3007 0.1933 0.2187 -0.0152 0.0479  -0.0023 58  TYR A N   
513  C CA  . TYR A 57  ? 0.3240 0.2064 0.2330 -0.0099 0.0468  0.0039  58  TYR A CA  
514  C C   . TYR A 57  ? 0.3957 0.2511 0.2893 -0.0120 0.0544  0.0054  58  TYR A C   
515  O O   . TYR A 57  ? 0.3752 0.2194 0.2567 -0.0175 0.0575  0.0078  58  TYR A O   
516  C CB  . TYR A 57  ? 0.3445 0.2333 0.2590 0.0030  0.0409  0.0070  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.3944 0.2699 0.2961 0.0103  0.0382  0.0140  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.4142 0.2939 0.3100 0.0068  0.0354  0.0171  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.4619 0.3186 0.3554 0.0211  0.0382  0.0173  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.4526 0.3175 0.3321 0.0127  0.0329  0.0239  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.5119 0.3523 0.3889 0.0286  0.0344  0.0247  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6011 0.4455 0.4700 0.0238  0.0318  0.0282  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.6957 0.5218 0.5445 0.0309  0.0279  0.0357  58  TYR A OH  
524  N N   A SER A 58  ? 0.3699 0.2135 0.2628 -0.0087 0.0585  0.0032  59  SER A N   
525  N N   B SER A 58  ? 0.3691 0.2129 0.2621 -0.0087 0.0584  0.0031  59  SER A N   
526  C CA  A SER A 58  ? 0.3957 0.2104 0.2732 -0.0105 0.0665  0.0038  59  SER A CA  
527  C CA  B SER A 58  ? 0.3947 0.2096 0.2724 -0.0106 0.0665  0.0037  59  SER A CA  
528  C C   A SER A 58  ? 0.4535 0.2640 0.3255 -0.0269 0.0738  -0.0013 59  SER A C   
529  C C   B SER A 58  ? 0.4509 0.2619 0.3230 -0.0269 0.0736  -0.0012 59  SER A C   
530  O O   A SER A 58  ? 0.4813 0.2703 0.3373 -0.0323 0.0802  0.0007  59  SER A O   
531  O O   B SER A 58  ? 0.4758 0.2662 0.3321 -0.0322 0.0796  0.0010  59  SER A O   
532  C CB  A SER A 58  ? 0.4283 0.2352 0.3098 -0.0037 0.0694  0.0004  59  SER A CB  
533  C CB  B SER A 58  ? 0.4282 0.2359 0.3101 -0.0046 0.0697  -0.0001 59  SER A CB  
534  O OG  A SER A 58  ? 0.4467 0.2552 0.3330 0.0124  0.0633  0.0040  59  SER A OG  
535  O OG  B SER A 58  ? 0.4828 0.2597 0.3489 -0.0064 0.0780  0.0000  59  SER A OG  
536  N N   . ILE A 59  ? 0.3900 0.2209 0.2744 -0.0349 0.0726  -0.0082 60  ILE A N   
537  C CA  . ILE A 59  ? 0.3761 0.2099 0.2599 -0.0496 0.0773  -0.0153 60  ILE A CA  
538  C C   . ILE A 59  ? 0.4008 0.2393 0.2823 -0.0558 0.0777  -0.0145 60  ILE A C   
539  O O   . ILE A 59  ? 0.4178 0.2426 0.2895 -0.0662 0.0863  -0.0175 60  ILE A O   
540  C CB  . ILE A 59  ? 0.3838 0.2398 0.2806 -0.0542 0.0726  -0.0223 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.3895 0.2375 0.2849 -0.0527 0.0757  -0.0256 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.3631 0.2295 0.2633 -0.0674 0.0739  -0.0305 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.3944 0.2616 0.2980 -0.0548 0.0696  -0.0302 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.3312 0.1883 0.2212 -0.0508 0.0698  -0.0115 61  PHE A N   
545  C CA  . PHE A 60  ? 0.3412 0.2059 0.2313 -0.0575 0.0707  -0.0128 61  PHE A CA  
546  C C   . PHE A 60  ? 0.4039 0.2485 0.2764 -0.0556 0.0746  -0.0054 61  PHE A C   
547  O O   . PHE A 60  ? 0.4157 0.2635 0.2852 -0.0633 0.0780  -0.0073 61  PHE A O   
548  C CB  . PHE A 60  ? 0.3280 0.2203 0.2342 -0.0549 0.0615  -0.0147 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.3210 0.2289 0.2394 -0.0578 0.0573  -0.0218 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.3544 0.2661 0.2759 -0.0685 0.0611  -0.0308 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.3225 0.2401 0.2474 -0.0505 0.0496  -0.0199 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.3547 0.2797 0.2848 -0.0702 0.0553  -0.0370 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.3499 0.2777 0.2807 -0.0532 0.0451  -0.0255 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.3247 0.2560 0.2575 -0.0622 0.0471  -0.0336 61  PHE A CZ  
555  N N   . THR A 61  ? 0.3900 0.2126 0.2495 -0.0458 0.0747  0.0021  62  THR A N   
556  C CA  . THR A 61  ? 0.4125 0.2092 0.2491 -0.0436 0.0780  0.0098  62  THR A CA  
557  C C   . THR A 61  ? 0.5136 0.2789 0.3314 -0.0525 0.0900  0.0085  62  THR A C   
558  O O   . THR A 61  ? 0.5261 0.2631 0.3194 -0.0543 0.0954  0.0142  62  THR A O   
559  C CB  . THR A 61  ? 0.5061 0.2962 0.3375 -0.0264 0.0693  0.0188  62  THR A CB  
560  O OG1 . THR A 61  ? 0.4536 0.2401 0.2919 -0.0175 0.0677  0.0181  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.4553 0.2729 0.3001 -0.0205 0.0592  0.0201  62  THR A CG2 
562  N N   . ASP A 62  ? 0.4658 0.2345 0.2927 -0.0594 0.0946  0.0005  63  ASP A N   
563  C CA  . ASP A 62  ? 0.4936 0.2337 0.3039 -0.0702 0.1071  -0.0027 63  ASP A CA  
564  C C   . ASP A 62  ? 0.5680 0.3120 0.3749 -0.0884 0.1160  -0.0094 63  ASP A C   
565  O O   . ASP A 62  ? 0.5217 0.2977 0.3494 -0.0950 0.1132  -0.0179 63  ASP A O   
566  C CB  . ASP A 62  ? 0.4931 0.2378 0.3146 -0.0729 0.1092  -0.0105 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.6406 0.3573 0.4457 -0.0865 0.1231  -0.0157 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.7117 0.3934 0.4972 -0.0806 0.1279  -0.0100 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.6311 0.3603 0.4424 -0.1031 0.1293  -0.0259 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.6045 0.3147 0.3845 -0.0967 0.1272  -0.0066 64  GLN A N   
571  C CA  . GLN A 63  ? 0.6265 0.3376 0.4006 -0.1155 0.1382  -0.0136 64  GLN A CA  
572  C C   . GLN A 63  ? 0.6712 0.4065 0.4659 -0.1318 0.1442  -0.0297 64  GLN A C   
573  O O   . GLN A 63  ? 0.6873 0.4420 0.4909 -0.1443 0.1487  -0.0383 64  GLN A O   
574  C CB  . GLN A 63  ? 0.6997 0.3635 0.4361 -0.1228 0.1509  -0.0075 64  GLN A CB  
575  C CG  . GLN A 63  ? 0.9313 0.5767 0.6459 -0.1099 0.1443  0.0067  64  GLN A CG  
576  N N   . LEU A 64  ? 0.5837 0.3189 0.3860 -0.1318 0.1442  -0.0347 65  LEU A N   
577  C CA  . LEU A 64  ? 0.5514 0.3120 0.3736 -0.1461 0.1475  -0.0504 65  LEU A CA  
578  C C   . LEU A 64  ? 0.5629 0.3638 0.4137 -0.1372 0.1325  -0.0540 65  LEU A C   
579  O O   . LEU A 64  ? 0.5705 0.4019 0.4408 -0.1454 0.1305  -0.0654 65  LEU A O   
580  C CB  . LEU A 64  ? 0.5721 0.3105 0.3850 -0.1535 0.1562  -0.0557 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.6729 0.3762 0.4612 -0.1710 0.1745  -0.0594 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.6933 0.3759 0.4742 -0.1765 0.1818  -0.0648 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.7102 0.4351 0.5085 -0.1917 0.1834  -0.0735 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.4761 0.2762 0.3291 -0.1207 0.1223  -0.0454 66  LYS A N   
585  C CA  . LYS A 65  ? 0.4324 0.2645 0.3074 -0.1131 0.1092  -0.0481 66  LYS A CA  
586  C C   . LYS A 65  ? 0.4820 0.3393 0.3701 -0.1072 0.1000  -0.0460 66  LYS A C   
587  O O   . LYS A 65  ? 0.4467 0.3313 0.3528 -0.1057 0.0909  -0.0517 66  LYS A O   
588  C CB  . LYS A 65  ? 0.4477 0.2710 0.3204 -0.0996 0.1035  -0.0413 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.4643 0.2667 0.3275 -0.1048 0.1117  -0.0456 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.4365 0.2358 0.3013 -0.0913 0.1060  -0.0407 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.5037 0.2764 0.3566 -0.0939 0.1154  -0.0436 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.5223 0.2596 0.3560 -0.0888 0.1229  -0.0358 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.4848 0.3311 0.3622 -0.1041 0.1021  -0.0383 67  CYS A N   
594  C CA  . CYS A 66  ? 0.4718 0.3395 0.3597 -0.0993 0.0949  -0.0367 67  CYS A CA  
595  C C   . CYS A 66  ? 0.5221 0.4184 0.4291 -0.1096 0.0949  -0.0499 67  CYS A C   
596  O O   . CYS A 66  ? 0.5130 0.4326 0.4350 -0.1040 0.0861  -0.0511 67  CYS A O   
597  C CB  . CYS A 66  ? 0.5002 0.3481 0.3691 -0.0977 0.0994  -0.0279 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.5873 0.4151 0.4382 -0.1172 0.1170  -0.0338 67  CYS A SG  
599  N N   . ASN A 67  ? 0.4782 0.3727 0.3853 -0.1247 0.1049  -0.0607 68  ASN A N   
600  C CA  . ASN A 67  ? 0.4744 0.3975 0.4015 -0.1357 0.1062  -0.0761 68  ASN A CA  
601  C C   . ASN A 67  ? 0.4918 0.4380 0.4374 -0.1355 0.0974  -0.0860 68  ASN A C   
602  O O   . ASN A 67  ? 0.4722 0.4456 0.4373 -0.1425 0.0959  -0.0999 68  ASN A O   
603  C CB  . ASN A 67  ? 0.5117 0.4218 0.4284 -0.1544 0.1236  -0.0841 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.6738 0.5652 0.5720 -0.1557 0.1312  -0.0761 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.7013 0.5606 0.5744 -0.1650 0.1445  -0.0726 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.5537 0.4616 0.4608 -0.1463 0.1229  -0.0724 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.4543 0.3909 0.3942 -0.1271 0.0910  -0.0795 69  LEU A N   
608  C CA  . LEU A 68  ? 0.4325 0.3874 0.3848 -0.1268 0.0819  -0.0876 69  LEU A CA  
609  C C   . LEU A 68  ? 0.4407 0.4197 0.4079 -0.1146 0.0661  -0.0865 69  LEU A C   
610  O O   . LEU A 68  ? 0.4083 0.3816 0.3712 -0.1038 0.0618  -0.0754 69  LEU A O   
611  C CB  . LEU A 68  ? 0.4457 0.3791 0.3837 -0.1233 0.0825  -0.0815 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.5201 0.4267 0.4423 -0.1347 0.0975  -0.0837 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.5263 0.4125 0.4362 -0.1285 0.0974  -0.0775 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.5290 0.4491 0.4600 -0.1519 0.1034  -0.1007 69  LEU A CD2 
615  N N   . SER A 69  ? 0.3871 0.3914 0.3705 -0.1163 0.0572  -0.0983 70  SER A N   
616  C CA  A SER A 69  ? 0.3633 0.3880 0.3591 -0.1046 0.0411  -0.0985 70  SER A CA  
617  C CA  B SER A 69  ? 0.3683 0.3920 0.3635 -0.1042 0.0412  -0.0977 70  SER A CA  
618  C C   . SER A 69  ? 0.3766 0.3949 0.3632 -0.0980 0.0311  -0.0940 70  SER A C   
619  O O   . SER A 69  ? 0.3191 0.3450 0.3081 -0.0875 0.0180  -0.0908 70  SER A O   
620  C CB  A SER A 69  ? 0.3982 0.4541 0.4169 -0.1090 0.0360  -0.1149 70  SER A CB  
621  C CB  B SER A 69  ? 0.4127 0.4676 0.4310 -0.1075 0.0360  -0.1132 70  SER A CB  
622  O OG  A SER A 69  ? 0.4557 0.5193 0.4835 -0.1160 0.0462  -0.1206 70  SER A OG  
623  O OG  B SER A 69  ? 0.4886 0.5544 0.5127 -0.1169 0.0356  -0.1261 70  SER A OG  
624  N N   . VAL A 70  ? 0.3385 0.3416 0.3131 -0.1051 0.0379  -0.0947 71  VAL A N   
625  C CA  . VAL A 70  ? 0.3325 0.3278 0.2960 -0.1016 0.0311  -0.0919 71  VAL A CA  
626  C C   . VAL A 70  ? 0.3672 0.3348 0.3138 -0.1031 0.0426  -0.0837 71  VAL A C   
627  O O   . VAL A 70  ? 0.3742 0.3295 0.3167 -0.1121 0.0554  -0.0865 71  VAL A O   
628  C CB  . VAL A 70  ? 0.3908 0.4010 0.3592 -0.1094 0.0256  -0.1057 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.3994 0.3989 0.3519 -0.1070 0.0194  -0.1028 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.3838 0.4240 0.3718 -0.1059 0.0127  -0.1154 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.3008 0.2580 0.2376 -0.0943 0.0384  -0.0745 72  ILE A N   
632  C CA  . ILE A 71  ? 0.3025 0.2367 0.2261 -0.0933 0.0474  -0.0682 72  ILE A CA  
633  C C   . ILE A 71  ? 0.3599 0.2911 0.2740 -0.0935 0.0428  -0.0699 72  ILE A C   
634  O O   . ILE A 71  ? 0.3565 0.2947 0.2689 -0.0875 0.0323  -0.0670 72  ILE A O   
635  C CB  . ILE A 71  ? 0.3263 0.2515 0.2483 -0.0833 0.0494  -0.0565 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.3340 0.2598 0.2612 -0.0839 0.0542  -0.0545 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.3466 0.2514 0.2581 -0.0803 0.0572  -0.0518 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.3980 0.3071 0.3183 -0.0932 0.0674  -0.0577 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.3416 0.2597 0.2471 -0.1008 0.0512  -0.0747 73  ASN A N   
640  C CA  . ASN A 72  ? 0.3570 0.2702 0.2509 -0.1028 0.0489  -0.0774 73  ASN A CA  
641  C C   . ASN A 72  ? 0.3901 0.2853 0.2760 -0.0976 0.0570  -0.0709 73  ASN A C   
642  O O   . ASN A 72  ? 0.3668 0.2467 0.2514 -0.0984 0.0683  -0.0704 73  ASN A O   
643  C CB  . ASN A 72  ? 0.3961 0.3081 0.2860 -0.1152 0.0531  -0.0892 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.6075 0.5409 0.5087 -0.1212 0.0456  -0.0987 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.4781 0.4285 0.3829 -0.1170 0.0315  -0.1000 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.5633 0.4959 0.4699 -0.1312 0.0551  -0.1063 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.3270 0.2229 0.2069 -0.0926 0.0517  -0.0667 74  LEU A N   
648  C CA  . LEU A 73  ? 0.3290 0.2123 0.2043 -0.0882 0.0597  -0.0629 74  LEU A CA  
649  C C   . LEU A 73  ? 0.3843 0.2557 0.2480 -0.0957 0.0673  -0.0702 74  LEU A C   
650  O O   . LEU A 73  ? 0.3959 0.2698 0.2520 -0.1042 0.0638  -0.0774 74  LEU A O   
651  C CB  . LEU A 73  ? 0.3253 0.2134 0.1985 -0.0820 0.0537  -0.0568 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.3549 0.2539 0.2388 -0.0744 0.0466  -0.0496 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.3564 0.2557 0.2375 -0.0695 0.0451  -0.0446 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.3646 0.2622 0.2596 -0.0703 0.0521  -0.0467 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.3510 0.2105 0.2140 -0.0920 0.0773  -0.0695 75  ASP A N   
656  C CA  . ASP A 74  ? 0.3777 0.2244 0.2307 -0.0982 0.0868  -0.0772 75  ASP A CA  
657  C C   . ASP A 74  ? 0.4410 0.2917 0.2789 -0.1054 0.0808  -0.0808 75  ASP A C   
658  O O   . ASP A 74  ? 0.4248 0.2822 0.2601 -0.1019 0.0739  -0.0756 75  ASP A O   
659  C CB  . ASP A 74  ? 0.4010 0.2389 0.2593 -0.0901 0.0966  -0.0757 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.5011 0.3250 0.3520 -0.0948 0.1085  -0.0845 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.5156 0.3401 0.3545 -0.1024 0.1091  -0.0897 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.5199 0.3303 0.3755 -0.0904 0.1173  -0.0861 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.4530 0.2984 0.2789 -0.1158 0.0829  -0.0897 76  PRO A N   
664  C CA  . PRO A 75  ? 0.4657 0.3125 0.2727 -0.1225 0.0757  -0.0927 76  PRO A CA  
665  C C   . PRO A 75  ? 0.5083 0.3482 0.3044 -0.1220 0.0808  -0.0911 76  PRO A C   
666  O O   . PRO A 75  ? 0.5317 0.3704 0.3091 -0.1266 0.0737  -0.0909 76  PRO A O   
667  C CB  . PRO A 75  ? 0.5054 0.3464 0.3024 -0.1340 0.0795  -0.1038 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.5726 0.4029 0.3809 -0.1334 0.0936  -0.1068 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.4861 0.3217 0.3123 -0.1226 0.0918  -0.0976 76  PRO A CD  
670  N N   . GLU A 76  ? 0.4658 0.3008 0.2724 -0.1166 0.0928  -0.0905 77  GLU A N   
671  C CA  . GLU A 76  ? 0.4833 0.3149 0.2830 -0.1172 0.0995  -0.0912 77  GLU A CA  
672  C C   . GLU A 76  ? 0.4752 0.3155 0.2778 -0.1114 0.0914  -0.0822 77  GLU A C   
673  O O   . GLU A 76  ? 0.4679 0.3056 0.2608 -0.1145 0.0954  -0.0826 77  GLU A O   
674  C CB  . GLU A 76  ? 0.5139 0.3406 0.3275 -0.1124 0.1147  -0.0959 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.7703 0.5841 0.5746 -0.1204 0.1261  -0.1070 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.1709 0.9794 0.9551 -0.1309 0.1323  -0.1138 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.1803 0.9907 0.9704 -0.1287 0.1417  -0.1164 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.1765 0.9795 0.9386 -0.1417 0.1278  -0.1171 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.4083 0.2581 0.2231 -0.1042 0.0811  -0.0750 78  ILE A N   
680  C CA  . ILE A 77  ? 0.3946 0.2519 0.2129 -0.0986 0.0736  -0.0670 78  ILE A CA  
681  C C   . ILE A 77  ? 0.4636 0.3171 0.2598 -0.1038 0.0628  -0.0648 78  ILE A C   
682  O O   . ILE A 77  ? 0.4528 0.3069 0.2408 -0.1064 0.0531  -0.0661 78  ILE A O   
683  C CB  . ILE A 77  ? 0.4014 0.2692 0.2398 -0.0892 0.0677  -0.0609 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.4068 0.2737 0.2626 -0.0828 0.0779  -0.0620 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.3397 0.2148 0.1804 -0.0842 0.0598  -0.0535 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.4800 0.3479 0.3433 -0.0786 0.0876  -0.0637 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.4632 0.3125 0.2497 -0.1050 0.0645  -0.0618 79  ASN A N   
688  C CA  . ASN A 78  ? 0.4862 0.3257 0.2469 -0.1094 0.0555  -0.0583 79  ASN A CA  
689  C C   . ASN A 78  ? 0.4739 0.3201 0.2410 -0.1010 0.0413  -0.0504 79  ASN A C   
690  O O   . ASN A 78  ? 0.4419 0.2962 0.2264 -0.0949 0.0433  -0.0464 79  ASN A O   
691  C CB  . ASN A 78  ? 0.5389 0.3685 0.2859 -0.1161 0.0667  -0.0595 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.7136 0.5272 0.4297 -0.1210 0.0589  -0.0545 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.5668 0.3794 0.2834 -0.1181 0.0564  -0.0488 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.6595 0.4584 0.3461 -0.1285 0.0546  -0.0566 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.4467 0.2902 0.2001 -0.1002 0.0263  -0.0488 80  PRO A N   
696  C CA  . PRO A 79  ? 0.4343 0.2847 0.1954 -0.0912 0.0128  -0.0426 80  PRO A CA  
697  C C   . PRO A 79  ? 0.4722 0.3137 0.2252 -0.0894 0.0132  -0.0359 80  PRO A C   
698  O O   . PRO A 79  ? 0.4493 0.3004 0.2200 -0.0818 0.0098  -0.0319 80  PRO A O   
699  C CB  . PRO A 79  ? 0.4835 0.3304 0.2273 -0.0910 -0.0030 -0.0440 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.5472 0.3943 0.2865 -0.0992 0.0027  -0.0523 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.5003 0.3366 0.2327 -0.1064 0.0201  -0.0536 80  PRO A CD  
702  N N   . GLU A 80  ? 0.4587 0.2812 0.1845 -0.0975 0.0187  -0.0354 81  GLU A N   
703  C CA  . GLU A 80  ? 0.4617 0.2737 0.1779 -0.0981 0.0209  -0.0300 81  GLU A CA  
704  C C   . GLU A 80  ? 0.4703 0.2975 0.2146 -0.0965 0.0333  -0.0313 81  GLU A C   
705  O O   . GLU A 80  ? 0.4437 0.2752 0.1978 -0.0912 0.0300  -0.0269 81  GLU A O   
706  C CB  . GLU A 80  ? 0.5138 0.2999 0.1920 -0.1095 0.0261  -0.0299 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.6154 0.3872 0.2803 -0.1114 0.0279  -0.0244 81  GLU A CG  
708  C CD  . GLU A 80  ? 0.9437 0.6883 0.5709 -0.1253 0.0377  -0.0249 81  GLU A CD  
709  O OE1 . GLU A 80  ? 0.9459 0.6671 0.5458 -0.1264 0.0318  -0.0184 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 0.8826 0.6278 0.5068 -0.1354 0.0522  -0.0321 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.4414 0.2771 0.1992 -0.0999 0.0463  -0.0377 82  GLY A N   
712  C CA  . GLY A 81  ? 0.4192 0.2710 0.2049 -0.0962 0.0563  -0.0399 82  GLY A CA  
713  C C   . GLY A 81  ? 0.4124 0.2797 0.2226 -0.0850 0.0479  -0.0357 82  GLY A C   
714  O O   . GLY A 81  ? 0.3714 0.2478 0.1961 -0.0808 0.0489  -0.0334 82  GLY A O   
715  N N   . PHE A 82  ? 0.3626 0.2330 0.1761 -0.0813 0.0397  -0.0354 83  PHE A N   
716  C CA  . PHE A 82  ? 0.3303 0.2143 0.1647 -0.0725 0.0328  -0.0323 83  PHE A CA  
717  C C   . PHE A 82  ? 0.3595 0.2428 0.1905 -0.0685 0.0230  -0.0267 83  PHE A C   
718  O O   . PHE A 82  ? 0.3381 0.2316 0.1857 -0.0629 0.0225  -0.0242 83  PHE A O   
719  C CB  . PHE A 82  ? 0.3417 0.2299 0.1801 -0.0717 0.0273  -0.0349 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.3298 0.2314 0.1893 -0.0645 0.0235  -0.0327 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.3530 0.2603 0.2288 -0.0613 0.0317  -0.0327 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.3324 0.2397 0.1940 -0.0606 0.0118  -0.0310 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.3440 0.2608 0.2348 -0.0559 0.0289  -0.0302 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.3448 0.2644 0.2249 -0.0554 0.0101  -0.0299 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.3249 0.2482 0.2178 -0.0538 0.0189  -0.0292 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.3637 0.2337 0.1722 -0.0707 0.0144  -0.0250 84  CYS A N   
727  C CA  . CYS A 83  ? 0.3895 0.2543 0.1916 -0.0659 0.0042  -0.0199 84  CYS A CA  
728  C C   . CYS A 83  ? 0.4066 0.2693 0.2110 -0.0675 0.0119  -0.0175 84  CYS A C   
729  O O   . CYS A 83  ? 0.3770 0.2467 0.1936 -0.0616 0.0079  -0.0148 84  CYS A O   
730  C CB  . CYS A 83  ? 0.4516 0.2966 0.2232 -0.0680 -0.0057 -0.0183 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.5274 0.3614 0.2886 -0.0597 -0.0200 -0.0121 84  CYS A SG  
732  N N   . ILE A 84  ? 0.3825 0.2372 0.1763 -0.0763 0.0237  -0.0200 85  ILE A N   
733  C CA  . ILE A 84  ? 0.3688 0.2238 0.1657 -0.0802 0.0328  -0.0203 85  ILE A CA  
734  C C   . ILE A 84  ? 0.3634 0.2418 0.1924 -0.0734 0.0356  -0.0215 85  ILE A C   
735  O O   . ILE A 84  ? 0.3362 0.2195 0.1729 -0.0715 0.0350  -0.0199 85  ILE A O   
736  C CB  . ILE A 84  ? 0.4155 0.2614 0.1982 -0.0920 0.0466  -0.0256 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.4452 0.2619 0.1883 -0.1002 0.0438  -0.0228 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.4004 0.2577 0.1982 -0.0961 0.0587  -0.0300 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.5168 0.3231 0.2419 -0.1127 0.0568  -0.0288 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.3195 0.2100 0.1647 -0.0698 0.0382  -0.0242 86  LEU A N   
741  C CA  . LEU A 85  ? 0.3025 0.2115 0.1739 -0.0626 0.0400  -0.0246 86  LEU A CA  
742  C C   . LEU A 85  ? 0.3255 0.2407 0.2055 -0.0553 0.0300  -0.0201 86  LEU A C   
743  O O   . LEU A 85  ? 0.2920 0.2180 0.1860 -0.0511 0.0300  -0.0190 86  LEU A O   
744  C CB  . LEU A 85  ? 0.3121 0.2269 0.1945 -0.0607 0.0463  -0.0284 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.3868 0.3015 0.2689 -0.0662 0.0584  -0.0350 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.3971 0.3129 0.2867 -0.0637 0.0637  -0.0389 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.3954 0.3240 0.2934 -0.0645 0.0633  -0.0376 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.3006 0.2103 0.1728 -0.0539 0.0213  -0.0186 87  LEU A N   
749  C CA  . LEU A 86  ? 0.2866 0.2037 0.1682 -0.0476 0.0125  -0.0163 87  LEU A CA  
750  C C   . LEU A 86  ? 0.3246 0.2379 0.2020 -0.0464 0.0089  -0.0135 87  LEU A C   
751  O O   . LEU A 86  ? 0.2955 0.2187 0.1860 -0.0419 0.0071  -0.0124 87  LEU A O   
752  C CB  . LEU A 86  ? 0.2891 0.2035 0.1646 -0.0467 0.0038  -0.0176 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.3344 0.2600 0.2232 -0.0406 -0.0043 -0.0178 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.3140 0.2526 0.2215 -0.0390 0.0016  -0.0186 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.3818 0.3076 0.2659 -0.0398 -0.0139 -0.0214 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.3165 0.2130 0.1730 -0.0513 0.0084  -0.0124 88  ASP A N   
757  C CA  . ASP A 87  ? 0.3167 0.2044 0.1652 -0.0517 0.0066  -0.0101 88  ASP A CA  
758  C C   . ASP A 87  ? 0.3400 0.2398 0.2032 -0.0537 0.0153  -0.0118 88  ASP A C   
759  O O   . ASP A 87  ? 0.3304 0.2345 0.2007 -0.0506 0.0126  -0.0108 88  ASP A O   
760  C CB  . ASP A 87  ? 0.3667 0.2299 0.1857 -0.0589 0.0074  -0.0087 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.5193 0.3677 0.3200 -0.0546 -0.0053 -0.0061 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.5055 0.3648 0.3197 -0.0458 -0.0151 -0.0062 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.5442 0.3705 0.3167 -0.0603 -0.0056 -0.0046 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.3121 0.2187 0.1810 -0.0582 0.0252  -0.0153 89  PHE A N   
765  C CA  . PHE A 88  ? 0.2848 0.2072 0.1709 -0.0587 0.0323  -0.0186 89  PHE A CA  
766  C C   . PHE A 88  ? 0.2898 0.2288 0.1959 -0.0498 0.0274  -0.0170 89  PHE A C   
767  O O   . PHE A 88  ? 0.2565 0.2049 0.1718 -0.0487 0.0273  -0.0176 89  PHE A O   
768  C CB  . PHE A 88  ? 0.2870 0.2154 0.1783 -0.0627 0.0425  -0.0241 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.2744 0.2238 0.1883 -0.0597 0.0469  -0.0283 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.3019 0.2572 0.2188 -0.0652 0.0515  -0.0323 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.2784 0.2410 0.2096 -0.0505 0.0452  -0.0281 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.2827 0.2604 0.2218 -0.0614 0.0534  -0.0371 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.3020 0.2833 0.2524 -0.0455 0.0465  -0.0314 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.2819 0.2726 0.2374 -0.0506 0.0500  -0.0363 89  PHE A CZ  
775  N N   . MET A 89  ? 0.2470 0.1892 0.1586 -0.0447 0.0242  -0.0156 90  MET A N   
776  C CA  . MET A 89  ? 0.2230 0.1773 0.1492 -0.0377 0.0207  -0.0139 90  MET A CA  
777  C C   . MET A 89  ? 0.2783 0.2339 0.2051 -0.0359 0.0149  -0.0122 90  MET A C   
778  O O   . MET A 89  ? 0.2637 0.2299 0.2006 -0.0331 0.0147  -0.0121 90  MET A O   
779  C CB  . MET A 89  ? 0.2314 0.1841 0.1584 -0.0352 0.0186  -0.0131 90  MET A CB  
780  C CG  . MET A 89  ? 0.2527 0.2038 0.1807 -0.0359 0.0250  -0.0151 90  MET A CG  
781  S SD  . MET A 89  ? 0.2833 0.2319 0.2124 -0.0346 0.0233  -0.0149 90  MET A SD  
782  C CE  . MET A 89  ? 0.2879 0.2282 0.2118 -0.0379 0.0313  -0.0184 90  MET A CE  
783  N N   . TYR A 90  ? 0.2494 0.1933 0.1645 -0.0369 0.0095  -0.0112 91  TYR A N   
784  C CA  . TYR A 90  ? 0.2410 0.1840 0.1566 -0.0339 0.0034  -0.0104 91  TYR A CA  
785  C C   . TYR A 90  ? 0.2891 0.2238 0.1965 -0.0377 0.0050  -0.0106 91  TYR A C   
786  O O   . TYR A 90  ? 0.2862 0.2190 0.1941 -0.0350 0.0007  -0.0105 91  TYR A O   
787  C CB  . TYR A 90  ? 0.2573 0.1924 0.1661 -0.0307 -0.0048 -0.0102 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.2557 0.2030 0.1771 -0.0272 -0.0071 -0.0120 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.2722 0.2207 0.1936 -0.0292 -0.0046 -0.0130 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.2614 0.2182 0.1941 -0.0230 -0.0106 -0.0139 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.2497 0.2077 0.1814 -0.0281 -0.0051 -0.0156 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.2573 0.2248 0.2006 -0.0219 -0.0111 -0.0170 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.2818 0.2494 0.2243 -0.0249 -0.0081 -0.0177 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.2568 0.2338 0.2088 -0.0257 -0.0073 -0.0218 91  TYR A OH  
795  N N   . THR A 91  ? 0.2525 0.1818 0.1522 -0.0447 0.0121  -0.0119 92  THR A N   
796  C CA  . THR A 91  ? 0.2732 0.1921 0.1627 -0.0508 0.0151  -0.0130 92  THR A CA  
797  C C   . THR A 91  ? 0.3006 0.2312 0.1984 -0.0576 0.0246  -0.0178 92  THR A C   
798  O O   . THR A 91  ? 0.2986 0.2235 0.1907 -0.0638 0.0281  -0.0201 92  THR A O   
799  C CB  . THR A 91  ? 0.3485 0.2406 0.2114 -0.0560 0.0147  -0.0110 92  THR A CB  
800  O OG1 . THR A 91  ? 0.3595 0.2505 0.2170 -0.0620 0.0217  -0.0127 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.3648 0.2444 0.2179 -0.0484 0.0032  -0.0072 92  THR A CG2 
802  N N   . SER A 92  ? 0.2510 0.1962 0.1610 -0.0569 0.0292  -0.0203 93  SER A N   
803  C CA  . SER A 92  ? 0.2402 0.1999 0.1612 -0.0622 0.0379  -0.0270 93  SER A CA  
804  C C   . SER A 92  ? 0.2975 0.2427 0.2020 -0.0738 0.0470  -0.0305 93  SER A C   
805  O O   . SER A 92  ? 0.2953 0.2529 0.2091 -0.0798 0.0558  -0.0380 93  SER A O   
806  C CB  . SER A 92  ? 0.2631 0.2361 0.1948 -0.0637 0.0383  -0.0307 93  SER A CB  
807  O OG  . SER A 92  ? 0.3060 0.2889 0.2479 -0.0547 0.0305  -0.0274 93  SER A OG  
808  N N   A ARG A 93  ? 0.2915 0.2109 0.1714 -0.0769 0.0446  -0.0259 94  ARG A N   
809  N N   B ARG A 93  ? 0.2790 0.1983 0.1587 -0.0771 0.0448  -0.0260 94  ARG A N   
810  C CA  A ARG A 93  ? 0.3167 0.2157 0.1734 -0.0889 0.0529  -0.0279 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.2984 0.1987 0.1561 -0.0893 0.0536  -0.0285 94  ARG A CA  
812  C C   A ARG A 93  ? 0.3610 0.2556 0.2111 -0.0890 0.0547  -0.0278 94  ARG A C   
813  C C   B ARG A 93  ? 0.3548 0.2487 0.2041 -0.0894 0.0548  -0.0278 94  ARG A C   
814  O O   A ARG A 93  ? 0.3461 0.2352 0.1919 -0.0815 0.0457  -0.0225 94  ARG A O   
815  O O   B ARG A 93  ? 0.3427 0.2301 0.1868 -0.0819 0.0456  -0.0223 94  ARG A O   
816  C CB  A ARG A 93  ? 0.3803 0.2489 0.2087 -0.0916 0.0479  -0.0223 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.3362 0.2070 0.1662 -0.0945 0.0511  -0.0242 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.4609 0.3298 0.2933 -0.0919 0.0465  -0.0227 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.3196 0.1947 0.1556 -0.0992 0.0547  -0.0277 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.5188 0.3562 0.3248 -0.0902 0.0390  -0.0164 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.4977 0.3441 0.3104 -0.0990 0.0488  -0.0222 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.5996 0.4048 0.3713 -0.1008 0.0444  -0.0149 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.5852 0.4358 0.4043 -0.1041 0.0529  -0.0265 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.7684 0.5565 0.5229 -0.1146 0.0552  -0.0182 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.7625 0.5849 0.5574 -0.1127 0.0566  -0.0261 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.6385 0.3941 0.3577 -0.1249 0.0605  -0.0162 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.5972 0.4256 0.4000 -0.1179 0.0609  -0.0312 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.6149 0.4174 0.3856 -0.1192 0.0611  -0.0240 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.6478 0.4339 0.4084 -0.1163 0.0559  -0.0206 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.3248 0.2225 0.1742 -0.0985 0.0669  -0.0349 95  LEU A N   
831  C CA  . LEU A 94  ? 0.3321 0.2255 0.1749 -0.1004 0.0709  -0.0366 95  LEU A CA  
832  C C   . LEU A 94  ? 0.4161 0.2824 0.2258 -0.1144 0.0787  -0.0376 95  LEU A C   
833  O O   . LEU A 94  ? 0.4144 0.2796 0.2201 -0.1266 0.0910  -0.0444 95  LEU A O   
834  C CB  . LEU A 94  ? 0.3165 0.2372 0.1878 -0.0983 0.0791  -0.0453 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.3668 0.2856 0.2359 -0.0986 0.0840  -0.0483 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.3533 0.2693 0.2235 -0.0875 0.0726  -0.0411 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.3662 0.3093 0.2618 -0.0976 0.0938  -0.0589 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.4250 0.2692 0.2097 -0.1134 0.0719  -0.0315 96  ASN A N   
839  C CA  . ASN A 95  ? 0.4587 0.2722 0.2052 -0.1263 0.0776  -0.0311 96  ASN A CA  
840  C C   . ASN A 95  ? 0.5117 0.3307 0.2586 -0.1345 0.0903  -0.0392 96  ASN A C   
841  O O   . ASN A 95  ? 0.5220 0.3319 0.2557 -0.1332 0.0865  -0.0374 96  ASN A O   
842  C CB  . ASN A 95  ? 0.5228 0.3103 0.2411 -0.1204 0.0624  -0.0213 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.7502 0.5010 0.4229 -0.1325 0.0660  -0.0192 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.6767 0.4151 0.3337 -0.1471 0.0801  -0.0235 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.6709 0.4034 0.3201 -0.1275 0.0534  -0.0131 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.4584 0.2946 0.2227 -0.1425 0.1051  -0.0494 97  LEU A N   
847  C CA  . LEU A 96  ? 0.4713 0.3171 0.2420 -0.1495 0.1188  -0.0597 97  LEU A CA  
848  C C   . LEU A 96  ? 0.5539 0.3735 0.2889 -0.1688 0.1323  -0.0637 97  LEU A C   
849  O O   . LEU A 96  ? 0.5494 0.3609 0.2745 -0.1800 0.1404  -0.0664 97  LEU A O   
850  C CB  . LEU A 96  ? 0.4573 0.3395 0.2701 -0.1456 0.1263  -0.0700 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.5296 0.4312 0.3636 -0.1445 0.1362  -0.0808 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.5308 0.4297 0.3664 -0.1324 0.1266  -0.0750 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.5175 0.4547 0.3928 -0.1379 0.1398  -0.0901 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.5339 0.3370 0.2456 -0.1737 0.1347  -0.0640 98  ARG A N   
855  C CA  . ARG A 97  ? 0.5845 0.3577 0.2549 -0.1927 0.1472  -0.0669 98  ARG A CA  
856  C C   . ARG A 97  ? 0.6019 0.3830 0.2755 -0.1997 0.1606  -0.0778 98  ARG A C   
857  O O   . ARG A 97  ? 0.5536 0.3536 0.2515 -0.1878 0.1554  -0.0793 98  ARG A O   
858  C CB  . ARG A 97  ? 0.6340 0.3680 0.2583 -0.1921 0.1330  -0.0535 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.7029 0.4254 0.3216 -0.1839 0.1190  -0.0428 98  ARG A CG  
860  C CD  . ARG A 97  ? 0.9303 0.6165 0.5071 -0.1796 0.1025  -0.0303 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.1743 0.8215 0.6996 -0.1965 0.1111  -0.0299 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.4494 1.0650 0.9409 -0.2094 0.1187  -0.0277 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.3323 0.9102 0.7736 -0.2255 0.1270  -0.0271 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.3053 0.9245 0.8105 -0.2074 0.1187  -0.0263 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.5853 0.3500 0.2328 -0.2199 0.1789  -0.0862 99  GLU A N   
866  C CA  . GLU A 98  ? 0.5899 0.3607 0.2386 -0.2280 0.1933  -0.0981 99  GLU A CA  
867  C C   . GLU A 98  ? 0.6582 0.4184 0.2932 -0.2192 0.1810  -0.0915 99  GLU A C   
868  O O   . GLU A 98  ? 0.6407 0.4202 0.2994 -0.2143 0.1856  -0.0996 99  GLU A O   
869  C CB  . GLU A 98  ? 0.6557 0.4005 0.2651 -0.2533 0.2135  -0.1057 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.7860 0.5397 0.3991 -0.2638 0.2320  -0.1210 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.2085 0.9343 0.7790 -0.2906 0.2531  -0.1289 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.1497 0.8326 0.6664 -0.2996 0.2479  -0.1173 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.2444 0.9908 0.8348 -0.3024 0.2751  -0.1472 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.6615 0.3914 0.2594 -0.2170 0.1652  -0.0778 100 GLY A N   
875  C CA  . GLY A 99  ? 0.6757 0.3945 0.2568 -0.2103 0.1519  -0.0720 100 GLY A CA  
876  C C   . GLY A 99  ? 0.6646 0.4086 0.2825 -0.1901 0.1365  -0.0681 100 GLY A C   
877  O O   . GLY A 99  ? 0.6622 0.4036 0.2739 -0.1858 0.1289  -0.0670 100 GLY A O   
878  N N   . ASN A 100 ? 0.5790 0.3473 0.2345 -0.1788 0.1327  -0.0668 101 ASN A N   
879  C CA  . ASN A 100 ? 0.5297 0.3191 0.2168 -0.1610 0.1192  -0.0628 101 ASN A CA  
880  C C   . ASN A 100 ? 0.5464 0.3686 0.2798 -0.1530 0.1269  -0.0707 101 ASN A C   
881  O O   . ASN A 100 ? 0.5018 0.3385 0.2587 -0.1396 0.1180  -0.0681 101 ASN A O   
882  C CB  . ASN A 100 ? 0.5076 0.2916 0.1919 -0.1506 0.1009  -0.0506 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.5907 0.3837 0.2907 -0.1494 0.1031  -0.0495 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.4692 0.2850 0.1985 -0.1497 0.1140  -0.0573 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.5373 0.3140 0.2201 -0.1467 0.0918  -0.0402 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.5106 0.3443 0.2567 -0.1609 0.1429  -0.0807 102 ILE A N   
887  C CA  . ILE A 101 ? 0.4784 0.3444 0.2690 -0.1517 0.1482  -0.0885 102 ILE A CA  
888  C C   . ILE A 101 ? 0.4828 0.3607 0.2941 -0.1419 0.1489  -0.0932 102 ILE A C   
889  O O   . ILE A 101 ? 0.4395 0.3362 0.2813 -0.1271 0.1423  -0.0916 102 ILE A O   
890  C CB  . ILE A 101 ? 0.5255 0.4047 0.3275 -0.1628 0.1657  -0.1013 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.5051 0.4204 0.3553 -0.1496 0.1665  -0.1085 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.5380 0.4061 0.3204 -0.1794 0.1837  -0.1127 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.5126 0.4459 0.3790 -0.1567 0.1758  -0.1176 102 ILE A CD1 
894  N N   . MET A 102 ? 0.4687 0.3333 0.2614 -0.1502 0.1568  -0.0987 103 MET A N   
895  C CA  . MET A 102 ? 0.4657 0.3379 0.2757 -0.1417 0.1583  -0.1035 103 MET A CA  
896  C C   . MET A 102 ? 0.4865 0.3557 0.2989 -0.1293 0.1413  -0.0925 103 MET A C   
897  O O   . MET A 102 ? 0.4467 0.3293 0.2861 -0.1167 0.1392  -0.0933 103 MET A O   
898  C CB  . MET A 102 ? 0.5282 0.3860 0.3160 -0.1547 0.1712  -0.1129 103 MET A CB  
899  C CG  . MET A 102 ? 0.6061 0.4701 0.3959 -0.1677 0.1912  -0.1270 103 MET A CG  
900  S SD  . MET A 102 ? 0.6471 0.5485 0.4901 -0.1565 0.1999  -0.1392 103 MET A SD  
901  C CE  . MET A 102 ? 0.6097 0.5174 0.4748 -0.1438 0.2029  -0.1468 103 MET A CE  
902  N N   . ALA A 103 ? 0.4744 0.3258 0.2588 -0.1326 0.1291  -0.0826 104 ALA A N   
903  C CA  . ALA A 103 ? 0.4633 0.3143 0.2510 -0.1224 0.1133  -0.0739 104 ALA A CA  
904  C C   . ALA A 103 ? 0.4606 0.3282 0.2750 -0.1097 0.1054  -0.0678 104 ALA A C   
905  O O   . ALA A 103 ? 0.4217 0.2977 0.2546 -0.0994 0.1000  -0.0656 104 ALA A O   
906  C CB  . ALA A 103 ? 0.5002 0.3318 0.2545 -0.1277 0.1015  -0.0665 104 ALA A CB  
907  N N   . VAL A 104 ? 0.4056 0.2765 0.2205 -0.1117 0.1057  -0.0657 105 VAL A N   
908  C CA  . VAL A 104 ? 0.3639 0.2509 0.2027 -0.1010 0.0986  -0.0608 105 VAL A CA  
909  C C   . VAL A 104 ? 0.3805 0.2874 0.2516 -0.0912 0.1041  -0.0664 105 VAL A C   
910  O O   . VAL A 104 ? 0.3625 0.2770 0.2491 -0.0798 0.0957  -0.0612 105 VAL A O   
911  C CB  . VAL A 104 ? 0.4068 0.2923 0.2385 -0.1064 0.0988  -0.0586 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.3702 0.2750 0.2286 -0.0961 0.0934  -0.0559 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.4244 0.2873 0.2242 -0.1112 0.0890  -0.0504 105 VAL A CG2 
914  N N   A MET A 105 ? 0.3607 0.2753 0.2413 -0.0953 0.1177  -0.0774 106 MET A N   
915  N N   B MET A 105 ? 0.3629 0.2775 0.2434 -0.0953 0.1177  -0.0774 106 MET A N   
916  C CA  A MET A 105 ? 0.3508 0.2839 0.2624 -0.0838 0.1217  -0.0836 106 MET A CA  
917  C CA  B MET A 105 ? 0.3556 0.2887 0.2671 -0.0840 0.1219  -0.0838 106 MET A CA  
918  C C   A MET A 105 ? 0.3993 0.3254 0.3142 -0.0751 0.1184  -0.0816 106 MET A C   
919  C C   B MET A 105 ? 0.4045 0.3308 0.3195 -0.0752 0.1185  -0.0817 106 MET A C   
920  O O   A MET A 105 ? 0.3768 0.3111 0.3105 -0.0619 0.1130  -0.0786 106 MET A O   
921  O O   B MET A 105 ? 0.3844 0.3189 0.3181 -0.0620 0.1130  -0.0786 106 MET A O   
922  C CB  A MET A 105 ? 0.3863 0.3301 0.3086 -0.0898 0.1374  -0.0979 106 MET A CB  
923  C CB  B MET A 105 ? 0.3960 0.3394 0.3175 -0.0903 0.1377  -0.0981 106 MET A CB  
924  C CG  A MET A 105 ? 0.4132 0.3782 0.3699 -0.0753 0.1393  -0.1051 106 MET A CG  
925  C CG  B MET A 105 ? 0.4300 0.3953 0.3863 -0.0761 0.1398  -0.1054 106 MET A CG  
926  S SD  A MET A 105 ? 0.4624 0.4477 0.4386 -0.0817 0.1572  -0.1245 106 MET A SD  
927  S SD  B MET A 105 ? 0.4934 0.4747 0.4659 -0.0830 0.1589  -0.1253 106 MET A SD  
928  C CE  A MET A 105 ? 0.4464 0.4131 0.4056 -0.0901 0.1702  -0.1327 106 MET A CE  
929  C CE  B MET A 105 ? 0.4477 0.4429 0.4534 -0.0612 0.1566  -0.1305 106 MET A CE  
930  N N   . ALA A 106 ? 0.3838 0.2934 0.2785 -0.0833 0.1221  -0.0835 107 ALA A N   
931  C CA  . ALA A 106 ? 0.3827 0.2831 0.2774 -0.0780 0.1205  -0.0827 107 ALA A CA  
932  C C   . ALA A 106 ? 0.3896 0.2884 0.2852 -0.0708 0.1068  -0.0717 107 ALA A C   
933  O O   . ALA A 106 ? 0.3623 0.2612 0.2704 -0.0609 0.1051  -0.0700 107 ALA A O   
934  C CB  . ALA A 106 ? 0.4156 0.2994 0.2853 -0.0904 0.1256  -0.0870 107 ALA A CB  
935  N N   . THR A 107 ? 0.3477 0.2443 0.2298 -0.0753 0.0976  -0.0646 108 THR A N   
936  C CA  . THR A 107 ? 0.3350 0.2325 0.2192 -0.0694 0.0854  -0.0557 108 THR A CA  
937  C C   . THR A 107 ? 0.3664 0.2774 0.2725 -0.0579 0.0824  -0.0521 108 THR A C   
938  O O   . THR A 107 ? 0.3332 0.2435 0.2462 -0.0508 0.0780  -0.0481 108 THR A O   
939  C CB  . THR A 107 ? 0.4095 0.3011 0.2747 -0.0755 0.0759  -0.0504 108 THR A CB  
940  O OG1 . THR A 107 ? 0.4071 0.2854 0.2495 -0.0857 0.0784  -0.0542 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.3902 0.2839 0.2587 -0.0704 0.0643  -0.0442 108 THR A CG2 
942  N N   . ALA A 108 ? 0.3236 0.2461 0.2391 -0.0571 0.0853  -0.0544 109 ALA A N   
943  C CA  . ALA A 108 ? 0.2954 0.2326 0.2311 -0.0464 0.0816  -0.0521 109 ALA A CA  
944  C C   . ALA A 108 ? 0.3307 0.2698 0.2818 -0.0355 0.0850  -0.0551 109 ALA A C   
945  O O   . ALA A 108 ? 0.3105 0.2524 0.2702 -0.0254 0.0787  -0.0497 109 ALA A O   
946  C CB  . ALA A 108 ? 0.2996 0.2501 0.2423 -0.0498 0.0849  -0.0562 109 ALA A CB  
947  N N   . MET A 109 ? 0.3040 0.2387 0.2559 -0.0373 0.0949  -0.0635 110 MET A N   
948  C CA  . MET A 109 ? 0.2985 0.2308 0.2631 -0.0256 0.0978  -0.0665 110 MET A CA  
949  C C   . MET A 109 ? 0.3430 0.2579 0.2976 -0.0227 0.0933  -0.0592 110 MET A C   
950  O O   . MET A 109 ? 0.3443 0.2564 0.3059 -0.0112 0.0892  -0.0549 110 MET A O   
951  C CB  . MET A 109 ? 0.3394 0.2697 0.3065 -0.0292 0.1104  -0.0783 110 MET A CB  
952  C CG  . MET A 109 ? 0.3907 0.3414 0.3740 -0.0298 0.1165  -0.0878 110 MET A CG  
953  S SD  . MET A 109 ? 0.4828 0.4308 0.4651 -0.0385 0.1335  -0.1032 110 MET A SD  
954  C CE  . MET A 109 ? 0.4543 0.3967 0.4536 -0.0203 0.1348  -0.1069 110 MET A CE  
955  N N   . TYR A 110 ? 0.3319 0.2353 0.2690 -0.0338 0.0935  -0.0581 111 TYR A N   
956  C CA  . TYR A 110 ? 0.3386 0.2277 0.2660 -0.0348 0.0904  -0.0535 111 TYR A CA  
957  C C   . TYR A 110 ? 0.3580 0.2517 0.2880 -0.0300 0.0807  -0.0443 111 TYR A C   
958  O O   . TYR A 110 ? 0.3326 0.2169 0.2626 -0.0244 0.0797  -0.0404 111 TYR A O   
959  C CB  . TYR A 110 ? 0.3554 0.2376 0.2656 -0.0483 0.0908  -0.0559 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.3584 0.2318 0.2604 -0.0520 0.0867  -0.0529 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.4002 0.2589 0.2995 -0.0522 0.0929  -0.0560 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.3522 0.2320 0.2494 -0.0563 0.0773  -0.0484 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.3604 0.2122 0.2527 -0.0581 0.0907  -0.0551 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.3530 0.2287 0.2455 -0.0609 0.0742  -0.0483 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.3589 0.2213 0.2490 -0.0629 0.0814  -0.0521 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.3676 0.2274 0.2538 -0.0696 0.0797  -0.0538 111 TYR A OH  
967  N N   . LEU A 111 ? 0.3078 0.2141 0.2387 -0.0325 0.0744  -0.0411 112 LEU A N   
968  C CA  . LEU A 111 ? 0.2885 0.2003 0.2218 -0.0289 0.0658  -0.0337 112 LEU A CA  
969  C C   . LEU A 111 ? 0.3245 0.2435 0.2705 -0.0171 0.0637  -0.0309 112 LEU A C   
970  O O   . LEU A 111 ? 0.3060 0.2272 0.2526 -0.0136 0.0575  -0.0249 112 LEU A O   
971  C CB  . LEU A 111 ? 0.2674 0.1876 0.1961 -0.0351 0.0599  -0.0319 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.3061 0.2195 0.2204 -0.0448 0.0577  -0.0333 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.2983 0.2172 0.2073 -0.0478 0.0505  -0.0305 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.3316 0.2393 0.2436 -0.0461 0.0554  -0.0322 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.2995 0.2238 0.2560 -0.0111 0.0683  -0.0362 113 GLN A N   
976  C CA  . GLN A 112 ? 0.2963 0.2302 0.2666 0.0018  0.0648  -0.0352 113 GLN A CA  
977  C C   . GLN A 112 ? 0.3122 0.2636 0.2881 0.0008  0.0582  -0.0327 113 GLN A C   
978  O O   . GLN A 112 ? 0.2921 0.2450 0.2675 0.0057  0.0511  -0.0263 113 GLN A O   
979  C CB  . GLN A 112 ? 0.3155 0.2340 0.2810 0.0113  0.0619  -0.0290 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.3755 0.2734 0.3343 0.0122  0.0694  -0.0320 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.4988 0.3756 0.4456 0.0169  0.0676  -0.0247 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.4034 0.2808 0.3498 0.0251  0.0608  -0.0183 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.4576 0.3142 0.3923 0.0104  0.0741  -0.0258 113 GLN A NE2 
984  N N   . MET A 113 ? 0.2726 0.2346 0.2511 -0.0072 0.0616  -0.0382 114 MET A N   
985  C CA  . MET A 113 ? 0.2552 0.2318 0.2378 -0.0105 0.0575  -0.0376 114 MET A CA  
986  C C   . MET A 113 ? 0.3237 0.3179 0.3230 -0.0088 0.0628  -0.0473 114 MET A C   
987  O O   . MET A 113 ? 0.3056 0.3018 0.3027 -0.0187 0.0705  -0.0540 114 MET A O   
988  C CB  . MET A 113 ? 0.2696 0.2386 0.2367 -0.0232 0.0579  -0.0360 114 MET A CB  
989  C CG  . MET A 113 ? 0.2913 0.2485 0.2469 -0.0240 0.0519  -0.0287 114 MET A CG  
990  S SD  . MET A 113 ? 0.3340 0.2819 0.2719 -0.0356 0.0501  -0.0278 114 MET A SD  
991  C CE  . MET A 113 ? 0.2948 0.2531 0.2356 -0.0366 0.0451  -0.0257 114 MET A CE  
992  N N   . GLU A 114 ? 0.3135 0.3193 0.3288 0.0043  0.0588  -0.0488 115 GLU A N   
993  C CA  . GLU A 114 ? 0.3281 0.3540 0.3645 0.0096  0.0627  -0.0599 115 GLU A CA  
994  C C   . GLU A 114 ? 0.3287 0.3734 0.3729 -0.0011 0.0670  -0.0678 115 GLU A C   
995  O O   . GLU A 114 ? 0.3254 0.3810 0.3807 -0.0051 0.0764  -0.0793 115 GLU A O   
996  C CB  . GLU A 114 ? 0.3592 0.3947 0.4098 0.0274  0.0537  -0.0588 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.5388 0.5520 0.5806 0.0381  0.0517  -0.0525 115 GLU A CG  
998  N N   . HIS A 115 ? 0.2698 0.3177 0.3082 -0.0064 0.0616  -0.0627 116 HIS A N   
999  C CA  . HIS A 115 ? 0.2847 0.3474 0.3284 -0.0179 0.0668  -0.0706 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.3278 0.3764 0.3550 -0.0337 0.0778  -0.0736 116 HIS A C   
1001 O O   . HIS A 115 ? 0.3336 0.3934 0.3678 -0.0428 0.0877  -0.0847 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.3022 0.3697 0.3428 -0.0196 0.0590  -0.0652 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.3528 0.4373 0.4092 -0.0057 0.0489  -0.0645 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.3813 0.4924 0.4621 0.0005  0.0490  -0.0758 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.3733 0.4519 0.4231 0.0022  0.0385  -0.0547 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.3718 0.4908 0.4583 0.0134  0.0371  -0.0714 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.3722 0.4711 0.4392 0.0140  0.0312  -0.0585 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.2676 0.2919 0.2725 -0.0373 0.0762  -0.0647 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.2761 0.2836 0.2609 -0.0510 0.0846  -0.0664 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.3427 0.3534 0.3346 -0.0525 0.0958  -0.0769 117 VAL A C   
1011 O O   . VAL A 116 ? 0.3265 0.3369 0.3126 -0.0652 0.1069  -0.0852 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.3198 0.3040 0.2813 -0.0529 0.0784  -0.0559 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.3329 0.2993 0.2717 -0.0659 0.0858  -0.0581 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.3083 0.2902 0.2637 -0.0525 0.0689  -0.0479 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.2971 0.3094 0.3007 -0.0399 0.0939  -0.0771 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.3088 0.3241 0.3216 -0.0390 0.1044  -0.0879 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.3656 0.4068 0.4007 -0.0417 0.1127  -0.1022 118 VAL A C   
1018 O O   . VAL A 117 ? 0.3582 0.3999 0.3911 -0.0529 0.1259  -0.1127 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.3434 0.3541 0.3654 -0.0231 0.1002  -0.0856 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.3463 0.3603 0.3797 -0.0212 0.1116  -0.0983 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.3466 0.3329 0.3468 -0.0239 0.0945  -0.0739 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.3300 0.3933 0.3869 -0.0315 0.1053  -0.1036 119 ASP A N   
1023 N N   B ASP A 118 ? 0.3176 0.3799 0.3720 -0.0336 0.1053  -0.1029 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.3328 0.4266 0.4163 -0.0323 0.1111  -0.1187 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.3142 0.4062 0.3934 -0.0358 0.1113  -0.1175 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.3912 0.4871 0.4656 -0.0536 0.1237  -0.1267 119 ASP A C   
1027 C C   B ASP A 118 ? 0.3493 0.4395 0.4157 -0.0576 0.1236  -0.1241 119 ASP A C   
1028 O O   A ASP A 118 ? 0.3943 0.5077 0.4846 -0.0599 0.1361  -0.1426 119 ASP A O   
1029 O O   B ASP A 118 ? 0.3374 0.4401 0.4147 -0.0656 0.1372  -0.1390 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.3453 0.4603 0.4480 -0.0192 0.0980  -0.1167 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.3264 0.4390 0.4238 -0.0238 0.0984  -0.1152 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.4878 0.6077 0.6063 0.0032  0.0880  -0.1147 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.4621 0.6104 0.5900 -0.0236 0.1025  -0.1319 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.5280 0.6495 0.6578 0.0100  0.0939  -0.1228 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.4768 0.6411 0.6266 -0.0167 0.1082  -0.1447 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.5517 0.6721 0.6697 0.0139  0.0746  -0.1053 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.5167 0.6779 0.6477 -0.0302 0.0999  -0.1332 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.3476 0.4243 0.3957 -0.0648 0.1210  -0.1163 120 THR A N   
1039 N N   B THR A 119 ? 0.3012 0.3743 0.3434 -0.0676 0.1198  -0.1137 120 THR A N   
1040 C CA  A THR A 119 ? 0.3561 0.4265 0.3879 -0.0854 0.1322  -0.1214 120 THR A CA  
1041 C CA  B THR A 119 ? 0.3133 0.3785 0.3382 -0.0884 0.1315  -0.1189 120 THR A CA  
1042 C C   A THR A 119 ? 0.3980 0.4470 0.4070 -0.0982 0.1445  -0.1242 120 THR A C   
1043 C C   B THR A 119 ? 0.3761 0.4195 0.3779 -0.1007 0.1437  -0.1216 120 THR A C   
1044 O O   A THR A 119 ? 0.4008 0.4543 0.4083 -0.1134 0.1596  -0.1366 120 THR A O   
1045 O O   B THR A 119 ? 0.3760 0.4180 0.3693 -0.1177 0.1579  -0.1314 120 THR A O   
1046 C CB  A THR A 119 ? 0.4606 0.5167 0.4733 -0.0896 0.1234  -0.1093 120 THR A CB  
1047 C CB  B THR A 119 ? 0.3235 0.3737 0.3279 -0.0946 0.1242  -0.1079 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.4507 0.5312 0.4878 -0.0787 0.1142  -0.1103 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.3473 0.3952 0.3413 -0.1137 0.1367  -0.1161 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.4704 0.5147 0.4626 -0.1104 0.1342  -0.1133 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.2606 0.2787 0.2344 -0.0940 0.1165  -0.0927 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.3473 0.3730 0.3375 -0.0933 0.1388  -0.1136 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.3656 0.3705 0.3326 -0.1043 0.1491  -0.1162 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.4299 0.4538 0.4189 -0.1059 0.1638  -0.1338 121 CYS A C   
1055 O O   . CYS A 120 ? 0.4297 0.4474 0.4051 -0.1229 0.1789  -0.1432 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.3616 0.3472 0.3151 -0.0955 0.1396  -0.1050 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.4084 0.3689 0.3310 -0.0976 0.1254  -0.0875 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.3904 0.4374 0.4131 -0.0881 0.1594  -0.1389 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.4013 0.4707 0.4516 -0.0854 0.1714  -0.1570 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.4496 0.5406 0.5117 -0.1005 0.1850  -0.1728 122 ARG A C   
1061 O O   . ARG A 121 ? 0.4474 0.5434 0.5122 -0.1120 0.2021  -0.1879 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.4130 0.5032 0.4968 -0.0612 0.1606  -0.1582 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.6155 0.6852 0.6913 -0.0477 0.1532  -0.1485 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.7942 0.8802 0.9007 -0.0291 0.1535  -0.1587 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.8958 0.9807 1.0105 -0.0083 0.1365  -0.1474 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.0320 1.0916 1.1320 0.0007  0.1301  -0.1361 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8083 0.8440 0.8869 -0.0089 0.1383  -0.1349 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.8872 0.9446 0.9923 0.0181  0.1159  -0.1263 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.4149 0.5182 0.4834 -0.1018 0.1783  -0.1700 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.4193 0.5438 0.4994 -0.1172 0.1905  -0.1848 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.4811 0.5788 0.5240 -0.1432 0.2058  -0.1857 123 LYS A C   
1072 O O   . LYS A 122 ? 0.4781 0.5882 0.5278 -0.1586 0.2241  -0.2033 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.4282 0.5691 0.5211 -0.1121 0.1783  -0.1804 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.6256 0.7987 0.7578 -0.0884 0.1653  -0.1841 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.7533 0.9466 0.8989 -0.0866 0.1556  -0.1836 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.8709 1.0802 1.0382 -0.0614 0.1363  -0.1774 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 0.9610 1.2019 1.1661 -0.0455 0.1361  -0.1927 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.4422 0.5030 0.4451 -0.1480 0.1983  -0.1676 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.4715 0.5000 0.4320 -0.1707 0.2098  -0.1655 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.5444 0.5626 0.4929 -0.1795 0.2245  -0.1744 124 PHE A C   
1081 O O   . PHE A 123 ? 0.5519 0.5601 0.4810 -0.2011 0.2423  -0.1841 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.4966 0.4902 0.4206 -0.1692 0.1950  -0.1443 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.5130 0.5036 0.4311 -0.1728 0.1886  -0.1378 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.5260 0.5490 0.4798 -0.1631 0.1827  -0.1424 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.5633 0.5171 0.4390 -0.1842 0.1868  -0.1266 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.5287 0.5481 0.4762 -0.1672 0.1774  -0.1373 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.5868 0.5355 0.4567 -0.1869 0.1812  -0.1210 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.5296 0.5114 0.4357 -0.1791 0.1773  -0.1268 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.4810 0.5018 0.4413 -0.1638 0.2184  -0.1725 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.5019 0.5152 0.4546 -0.1705 0.2324  -0.1825 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.5647 0.6104 0.5500 -0.1769 0.2513  -0.2067 125 ILE A C   
1092 O O   . ILE A 124 ? 0.5797 0.6164 0.5478 -0.1962 0.2704  -0.2183 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.5255 0.5311 0.4816 -0.1524 0.2213  -0.1745 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.5280 0.4991 0.4449 -0.1534 0.2077  -0.1546 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.5586 0.5647 0.5182 -0.1564 0.2369  -0.1891 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.5909 0.5587 0.5159 -0.1343 0.1925  -0.1441 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.5198 0.6033 0.5512 -0.1610 0.2459  -0.2150 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.5267 0.6487 0.5979 -0.1631 0.2609  -0.2397 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.5946 0.7212 0.6561 -0.1901 0.2795  -0.2526 126 LYS A C   
1100 O O   . LYS A 125 ? 0.5841 0.7278 0.6596 -0.2025 0.2999  -0.2740 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.5415 0.7010 0.6601 -0.1387 0.2463  -0.2430 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.7263 0.9267 0.8917 -0.1319 0.2572  -0.2683 126 LYS A CG  
1103 C CD  . LYS A 125 ? 0.8520 1.0909 1.0610 -0.1108 0.2420  -0.2726 126 LYS A CD  
1104 C CE  . LYS A 125 ? 0.9995 1.2838 1.2575 -0.1052 0.2526  -0.3004 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.1051 1.4287 1.4037 -0.0864 0.2369  -0.3056 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.5596 0.6689 0.5959 -0.2000 0.2736  -0.2401 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.5847 0.6905 0.6049 -0.2269 0.2910  -0.2499 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.6792 0.7494 0.6539 -0.2515 0.3102  -0.2523 127 ALA A C   
1109 O O   . ALA A 126 ? 0.6925 0.7669 0.6621 -0.2750 0.3318  -0.2686 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.5845 0.6746 0.5855 -0.2290 0.2783  -0.2339 127 ALA A CB  
1111 N N   . SER A 127 ? 0.6700 0.7052 0.6107 -0.2469 0.3026  -0.2368 128 SER A N   
1112 C CA  . SER A 127 ? 0.7294 0.7272 0.6217 -0.2684 0.3175  -0.2368 128 SER A CA  
1113 C C   . SER A 127 ? 0.8136 0.8252 0.7206 -0.2725 0.3355  -0.2561 128 SER A C   
1114 O O   . SER A 127 ? 0.8633 0.8494 0.7332 -0.2946 0.3530  -0.2616 128 SER A O   
1115 C CB  . SER A 127 ? 0.8048 0.7595 0.6523 -0.2625 0.2999  -0.2122 128 SER A CB  
1116 O OG  . SER A 127 ? 0.9615 0.8902 0.7772 -0.2700 0.2921  -0.1977 128 SER A OG  
1117 N N   . GLU A 128 ? 0.7337 0.7835 0.6924 -0.2514 0.3316  -0.2668 129 GLU A N   
1118 C CA  . GLU A 128 ? 0.9522 1.0170 0.9299 -0.2522 0.3480  -0.2863 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.4407 1.5371 1.4441 -0.2703 0.3735  -0.3146 129 GLU A C   
1120 O O   . GLU A 128 ? 1.0403 1.1216 1.0142 -0.2969 0.3889  -0.3186 129 GLU A O   
1121 C CB  . GLU A 128 ? 0.9370 1.0236 0.9552 -0.2213 0.3331  -0.2856 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.0256 1.1615 1.1036 -0.2033 0.3282  -0.2988 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.2593 1.4097 1.3707 -0.1710 0.3100  -0.2940 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.1504 1.2711 1.2380 -0.1609 0.2971  -0.2757 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.1582 1.3493 1.3190 -0.1557 0.3084  -0.3089 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.2136 0.4260 0.2430 -0.0450 -0.0201 -0.0797 1   TRP D N   
1130 N N   B TRP B 2   ? 0.2130 0.4254 0.2423 -0.0450 -0.0201 -0.0797 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.2025 0.4151 0.2336 -0.0454 -0.0198 -0.0807 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.2029 0.4154 0.2340 -0.0454 -0.0199 -0.0806 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.2544 0.4662 0.2882 -0.0464 -0.0197 -0.0796 1   TRP D C   
1134 C C   B TRP B 2   ? 0.2486 0.4605 0.2824 -0.0464 -0.0196 -0.0796 1   TRP D C   
1135 O O   A TRP B 2   ? 0.2492 0.4594 0.2833 -0.0466 -0.0202 -0.0787 1   TRP D O   
1136 O O   B TRP B 2   ? 0.2427 0.4532 0.2768 -0.0467 -0.0200 -0.0787 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.1900 0.4018 0.2200 -0.0451 -0.0215 -0.0817 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.1856 0.3974 0.2159 -0.0452 -0.0215 -0.0816 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.1960 0.4085 0.2231 -0.0443 -0.0217 -0.0840 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.1948 0.4059 0.2270 -0.0455 -0.0229 -0.0810 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.2312 0.4430 0.2564 -0.0435 -0.0228 -0.0847 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.2329 0.4435 0.2660 -0.0452 -0.0242 -0.0814 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.1901 0.4037 0.2160 -0.0443 -0.0206 -0.0862 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.1903 0.4025 0.2251 -0.0460 -0.0230 -0.0805 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.2209 0.4338 0.2433 -0.0428 -0.0226 -0.0878 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.2251 0.4367 0.2619 -0.0456 -0.0247 -0.0816 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.2348 0.4488 0.2576 -0.0434 -0.0211 -0.0890 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.2390 0.4521 0.2763 -0.0460 -0.0239 -0.0812 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.1946 0.4091 0.2226 -0.0448 -0.0191 -0.0862 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.2016 0.4145 0.2375 -0.0463 -0.0224 -0.0796 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.2168 0.4319 0.2376 -0.0431 -0.0199 -0.0924 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.2252 0.4408 0.2656 -0.0462 -0.0239 -0.0815 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.2037 0.4190 0.2304 -0.0447 -0.0178 -0.0888 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.2206 0.4353 0.2588 -0.0463 -0.0228 -0.0793 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.2139 0.4296 0.2368 -0.0439 -0.0180 -0.0923 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.2253 0.4419 0.2655 -0.0462 -0.0233 -0.0805 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.1993 0.4123 0.2358 -0.0468 -0.0189 -0.0800 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.1919 0.4044 0.2313 -0.0476 -0.0189 -0.0797 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.2096 0.4222 0.2515 -0.0474 -0.0193 -0.0791 2   VAL D C   
1160 O O   . VAL B 3   ? 0.1967 0.4099 0.2385 -0.0470 -0.0189 -0.0790 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2256 0.4403 0.2678 -0.0490 -0.0177 -0.0809 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2235 0.4389 0.2631 -0.0496 -0.0174 -0.0805 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2175 0.4357 0.2636 -0.0492 -0.0163 -0.0824 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.1808 0.3931 0.2250 -0.0476 -0.0198 -0.0788 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.1819 0.3946 0.2293 -0.0473 -0.0202 -0.0775 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.2165 0.4299 0.2693 -0.0482 -0.0192 -0.0788 3   ILE D C   
1167 O O   . ILE B 4   ? 0.2018 0.4154 0.2565 -0.0491 -0.0192 -0.0807 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.2003 0.4133 0.2481 -0.0468 -0.0213 -0.0771 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.1892 0.4038 0.2338 -0.0461 -0.0219 -0.0771 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.2098 0.4237 0.2613 -0.0463 -0.0220 -0.0750 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.2265 0.4435 0.2694 -0.0461 -0.0226 -0.0758 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.2113 0.4257 0.2676 -0.0482 -0.0182 -0.0787 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.2153 0.4322 0.2794 -0.0493 -0.0169 -0.0810 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.2585 0.4748 0.3289 -0.0496 -0.0181 -0.0807 4   PRO D C   
1175 O O   . PRO B 5   ? 0.2587 0.4729 0.3285 -0.0485 -0.0194 -0.0776 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.2341 0.4522 0.3010 -0.0489 -0.0151 -0.0811 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.2813 0.4966 0.3431 -0.0478 -0.0162 -0.0776 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.2286 0.4428 0.2830 -0.0475 -0.0178 -0.0771 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.2231 0.4422 0.3005 -0.0512 -0.0177 -0.0841 5   ALA D N   
# 
