data_7GUR
# 
_entry.id   7GUR 
# 
_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   7GUR         pdb_00007gur 10.2210/pdb7gur/pdb 
WWPDB D_1001406662 ?            ?                   
# 
_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                        7GUR 
_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   304 130 HOH HOH A . 
F 6 HOH 5   305 88  HOH HOH A . 
F 6 HOH 6   306 63  HOH HOH A . 
F 6 HOH 7   307 166 HOH HOH A . 
F 6 HOH 8   308 84  HOH HOH A . 
F 6 HOH 9   309 149 HOH HOH A . 
F 6 HOH 10  310 32  HOH HOH A . 
F 6 HOH 11  311 87  HOH HOH A . 
F 6 HOH 12  312 189 HOH HOH A . 
F 6 HOH 13  313 23  HOH HOH A . 
F 6 HOH 14  314 33  HOH HOH A . 
F 6 HOH 15  315 5   HOH HOH A . 
F 6 HOH 16  316 24  HOH HOH A . 
F 6 HOH 17  317 92  HOH HOH A . 
F 6 HOH 18  318 14  HOH HOH A . 
F 6 HOH 19  319 159 HOH HOH A . 
F 6 HOH 20  320 114 HOH HOH A . 
F 6 HOH 21  321 85  HOH HOH A . 
F 6 HOH 22  322 230 HOH HOH A . 
F 6 HOH 23  323 83  HOH HOH A . 
F 6 HOH 24  324 143 HOH HOH A . 
F 6 HOH 25  325 187 HOH HOH A . 
F 6 HOH 26  326 165 HOH HOH A . 
F 6 HOH 27  327 103 HOH HOH A . 
F 6 HOH 28  328 196 HOH HOH A . 
F 6 HOH 29  329 50  HOH HOH A . 
F 6 HOH 30  330 134 HOH HOH A . 
F 6 HOH 31  331 97  HOH HOH A . 
F 6 HOH 32  332 109 HOH HOH A . 
F 6 HOH 33  333 11  HOH HOH A . 
F 6 HOH 34  334 141 HOH HOH A . 
F 6 HOH 35  335 135 HOH HOH A . 
F 6 HOH 36  336 90  HOH HOH A . 
F 6 HOH 37  337 113 HOH HOH A . 
F 6 HOH 38  338 49  HOH HOH A . 
F 6 HOH 39  339 136 HOH HOH A . 
F 6 HOH 40  340 117 HOH HOH A . 
F 6 HOH 41  341 151 HOH HOH A . 
F 6 HOH 42  342 94  HOH HOH A . 
F 6 HOH 43  343 213 HOH HOH A . 
F 6 HOH 44  344 110 HOH HOH A . 
F 6 HOH 45  345 184 HOH HOH A . 
F 6 HOH 46  346 26  HOH HOH A . 
F 6 HOH 47  347 51  HOH HOH A . 
F 6 HOH 48  348 100 HOH HOH A . 
F 6 HOH 49  349 112 HOH HOH A . 
F 6 HOH 50  350 123 HOH HOH A . 
F 6 HOH 51  351 22  HOH HOH A . 
F 6 HOH 52  352 13  HOH HOH A . 
F 6 HOH 53  353 116 HOH HOH A . 
F 6 HOH 54  354 35  HOH HOH A . 
F 6 HOH 55  355 3   HOH HOH A . 
F 6 HOH 56  356 6   HOH HOH A . 
F 6 HOH 57  357 18  HOH HOH A . 
F 6 HOH 58  358 102 HOH HOH A . 
F 6 HOH 59  359 180 HOH HOH A . 
F 6 HOH 60  360 25  HOH HOH A . 
F 6 HOH 61  361 121 HOH HOH A . 
F 6 HOH 62  362 86  HOH HOH A . 
F 6 HOH 63  363 115 HOH HOH A . 
F 6 HOH 64  364 74  HOH HOH A . 
F 6 HOH 65  365 231 HOH HOH A . 
F 6 HOH 66  366 95  HOH HOH A . 
F 6 HOH 67  367 44  HOH HOH A . 
F 6 HOH 68  368 66  HOH HOH A . 
F 6 HOH 69  369 62  HOH HOH A . 
F 6 HOH 70  370 150 HOH HOH A . 
F 6 HOH 71  371 105 HOH HOH A . 
F 6 HOH 72  372 244 HOH HOH A . 
F 6 HOH 73  373 89  HOH HOH A . 
F 6 HOH 74  374 119 HOH HOH A . 
F 6 HOH 75  375 28  HOH HOH A . 
F 6 HOH 76  376 101 HOH HOH A . 
F 6 HOH 77  377 20  HOH HOH A . 
F 6 HOH 78  378 178 HOH HOH A . 
F 6 HOH 79  379 40  HOH HOH A . 
F 6 HOH 80  380 57  HOH HOH A . 
F 6 HOH 81  381 238 HOH HOH A . 
F 6 HOH 82  382 147 HOH HOH A . 
F 6 HOH 83  383 164 HOH HOH A . 
F 6 HOH 84  384 192 HOH HOH A . 
F 6 HOH 85  385 10  HOH HOH A . 
F 6 HOH 86  386 168 HOH HOH A . 
F 6 HOH 87  387 107 HOH HOH A . 
F 6 HOH 88  388 29  HOH HOH A . 
F 6 HOH 89  389 104 HOH HOH A . 
F 6 HOH 90  390 21  HOH HOH A . 
F 6 HOH 91  391 99  HOH HOH A . 
F 6 HOH 92  392 56  HOH HOH A . 
F 6 HOH 93  393 167 HOH HOH A . 
F 6 HOH 94  394 69  HOH HOH A . 
F 6 HOH 95  395 39  HOH HOH A . 
F 6 HOH 96  396 60  HOH HOH A . 
F 6 HOH 97  397 75  HOH HOH A . 
F 6 HOH 98  398 96  HOH HOH A . 
F 6 HOH 99  399 246 HOH HOH A . 
F 6 HOH 100 400 82  HOH HOH A . 
F 6 HOH 101 401 27  HOH HOH A . 
F 6 HOH 102 402 52  HOH HOH A . 
F 6 HOH 103 403 36  HOH HOH A . 
F 6 HOH 104 404 30  HOH HOH A . 
F 6 HOH 105 405 237 HOH HOH A . 
F 6 HOH 106 406 242 HOH HOH A . 
F 6 HOH 107 407 53  HOH HOH A . 
F 6 HOH 108 408 38  HOH HOH A . 
F 6 HOH 109 409 176 HOH HOH A . 
F 6 HOH 110 410 93  HOH HOH A . 
F 6 HOH 111 411 37  HOH HOH A . 
F 6 HOH 112 412 193 HOH HOH A . 
F 6 HOH 113 413 17  HOH HOH A . 
F 6 HOH 114 414 241 HOH HOH A . 
F 6 HOH 115 415 239 HOH HOH A . 
F 6 HOH 116 416 153 HOH HOH A . 
F 6 HOH 117 417 209 HOH HOH A . 
F 6 HOH 118 418 146 HOH HOH A . 
F 6 HOH 119 419 45  HOH HOH A . 
F 6 HOH 120 420 186 HOH HOH A . 
F 6 HOH 121 421 203 HOH HOH A . 
F 6 HOH 122 422 54  HOH HOH A . 
F 6 HOH 123 423 171 HOH HOH A . 
F 6 HOH 124 424 200 HOH HOH A . 
F 6 HOH 125 425 31  HOH HOH A . 
F 6 HOH 126 426 79  HOH HOH A . 
F 6 HOH 127 427 188 HOH HOH A . 
F 6 HOH 128 428 55  HOH HOH A . 
F 6 HOH 129 429 148 HOH HOH A . 
F 6 HOH 130 430 191 HOH HOH A . 
F 6 HOH 131 431 98  HOH HOH A . 
F 6 HOH 132 432 185 HOH HOH A . 
F 6 HOH 133 433 139 HOH HOH A . 
F 6 HOH 134 434 145 HOH HOH A . 
F 6 HOH 135 435 43  HOH HOH A . 
F 6 HOH 136 436 106 HOH HOH A . 
F 6 HOH 137 437 232 HOH HOH A . 
F 6 HOH 138 438 80  HOH HOH A . 
F 6 HOH 139 439 76  HOH HOH A . 
F 6 HOH 140 440 137 HOH HOH A . 
F 6 HOH 141 441 158 HOH HOH A . 
F 6 HOH 142 442 140 HOH HOH A . 
F 6 HOH 143 443 221 HOH HOH A . 
F 6 HOH 144 444 111 HOH HOH A . 
F 6 HOH 145 445 204 HOH HOH A . 
F 6 HOH 146 446 131 HOH HOH A . 
F 6 HOH 147 447 206 HOH HOH A . 
F 6 HOH 148 448 108 HOH HOH A . 
F 6 HOH 149 449 247 HOH HOH A . 
F 6 HOH 150 450 169 HOH HOH A . 
F 6 HOH 151 451 161 HOH HOH A . 
F 6 HOH 152 452 70  HOH HOH A . 
F 6 HOH 153 453 243 HOH HOH A . 
F 6 HOH 154 454 183 HOH HOH A . 
F 6 HOH 155 455 215 HOH HOH A . 
F 6 HOH 156 456 212 HOH HOH A . 
F 6 HOH 157 457 142 HOH HOH A . 
F 6 HOH 158 458 228 HOH HOH A . 
F 6 HOH 159 459 73  HOH HOH A . 
F 6 HOH 160 460 59  HOH HOH A . 
F 6 HOH 161 461 179 HOH HOH A . 
F 6 HOH 162 462 245 HOH HOH A . 
F 6 HOH 163 463 175 HOH HOH A . 
F 6 HOH 164 464 181 HOH HOH A . 
F 6 HOH 165 465 65  HOH HOH A . 
F 6 HOH 166 466 195 HOH HOH A . 
F 6 HOH 167 467 170 HOH HOH A . 
F 6 HOH 168 468 61  HOH HOH A . 
F 6 HOH 169 469 152 HOH HOH A . 
F 6 HOH 170 470 233 HOH HOH A . 
F 6 HOH 171 471 208 HOH HOH A . 
F 6 HOH 172 472 225 HOH HOH A . 
F 6 HOH 173 473 144 HOH HOH A . 
G 6 HOH 1   201 77  HOH HOH D . 
G 6 HOH 2   202 71  HOH HOH D . 
G 6 HOH 3   203 68  HOH HOH D . 
G 6 HOH 4   204 47  HOH HOH D . 
G 6 HOH 5   205 58  HOH HOH D . 
G 6 HOH 6   206 240 HOH HOH D . 
G 6 HOH 7   207 220 HOH HOH D . 
G 6 HOH 8   208 210 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
8  1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
9  1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
10 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com phasing           
http://www.globalphasing.com/buster/                ?   ? 
5 PDB_EXTRACT 3.24   'Sep. 1, 2017' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.entry_id           7GUR 
_cell.length_a           67.630 
_cell.length_b           67.630 
_cell.length_c           166.270 
_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                         7GUR 
_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          7GUR 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.62 
_exptl_crystal.density_percent_sol   66.05 
_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                     7GUR 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.900 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   21752 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.117 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        8.200 
_reflns.B_iso_Wilson_estimate        34.310 
_reflns.pdbx_redundancy              9.000 
_reflns.pdbx_Rrim_I_all              0.125 
_reflns.pdbx_Rpim_I_all              0.041 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     196160 
_reflns.pdbx_scaling_rejects         426 
_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  ? 11603 1251 ? 3.058 ? ? ? 9.300 ? 0.600  ? ? ? ? ? ? 100.000 3.236 1.046 0.458 ? 
1 2 9.000 33.900 ? 1542  226  ? 0.056 ? ? ? 6.800 ? 23.300 ? ? ? ? ? ? 98.700  0.060 0.022 0.997 ? 
# 
_refine.entry_id                                 7GUR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8000 
_refine.ls_d_res_low                             33.9000 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.8000 
_refine.ls_number_reflns_obs                     21655 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1820 
_refine.ls_R_factor_R_work                       0.1810 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2110 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1900 
_refine.ls_number_reflns_R_free                  1124 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               41.2600 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.3345 
_refine.aniso_B[2][2]                            -0.3345 
_refine.aniso_B[3][3]                            0.6690 
_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               0.9640 
_refine.correlation_coeff_Fo_to_Fc_free          0.9520 
_refine.overall_SU_R_Cruickshank_DPI             0.0950 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0960 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1090 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1050 
_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                                141.550 
_refine.B_iso_min                                21.950 
_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                        7GUR 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.210 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.8000 
_refine_hist.d_res_low                        33.9000 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.number_atoms_solvent             181 
_refine_hist.number_atoms_total               1230 
_refine_hist.pdbx_number_residues_total       130 
_refine_hist.pdbx_B_iso_mean_ligand           36.16 
_refine_hist.pdbx_B_iso_mean_solvent          59.90 
_refine_hist.pdbx_number_atoms_protein        1026 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' t_dihedral_angle_d        451  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              233  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1236 ?      ? 20.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 162  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        7    ?      ? 1.000  HARMONIC     
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1615 ?      ? 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           ?    3.360  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    16.280 ? ?      ?            
# 
_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               99.2200 
_refine_ls_shell.number_reflns_R_work             2668 
_refine_ls_shell.R_factor_all                     0.2759 
_refine_ls_shell.R_factor_R_work                  0.2766 
_refine_ls_shell.R_factor_R_free                  0.2610 
_refine_ls_shell.percent_reflns_R_free            4.5800 
_refine_ls_shell.number_reflns_R_free             128 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2796 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUR 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 22.65 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUR 
_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 7GUR       7GUR   ? 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 7GUR A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUR D 1 ? 6   ? 7GUR   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 7GUR GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUR PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUR 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)'  13300 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_545 x,x-y-1,-z+1/6 0.5000000000 0.8660254038 0.0000000000 33.8150000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5692980579 0.0000000000 0.0000000000 -1.0000000000 27.7116666667 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ARG A 12  ? ARG A 27  ? ARG A 13  ARG A 28  1 ? 16 
HELX_P HELX_P2 AA2 HIS A 45  ? SER A 53  ? HIS A 46  SER A 54  1 ? 9  
HELX_P HELX_P3 AA3 SER A 53  ? THR A 61  ? SER A 54  THR A 62  1 ? 9  
HELX_P HELX_P4 AA4 LEU A 64  ? LEU A 68  ? LEU A 65  LEU A 69  5 ? 5  
HELX_P HELX_P5 AA5 ASN A 78  ? SER A 92  ? ASN A 79  SER A 93  1 ? 15 
HELX_P HELX_P6 AA6 ASN A 100 ? GLN A 112 ? ASN A 101 GLN A 113 1 ? 13 
HELX_P HELX_P7 AA7 MET A 113 ? GLU A 128 ? MET A 114 GLU A 129 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N A ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ACE B 1 ? TRP B 2 A ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
2 ACE B 1 ? TRP B 2 B ACE D 0 ? 1_555 TRP D 1 ? 1_555 . . TRP 16 ACE None 'Terminal acetylation' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40 ? ALA A 44 ? GLU A 41 ALA A 45 
AA1 2 VAL A 33 ? VAL A 37 ? VAL A 34 VAL A 38 
AA1 3 VAL A 70 ? ASN A 72 ? VAL A 71 ASN A 73 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O 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                   7GUR 
_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 39.00   48.66   
2 1 SER A 39  ? B 61.10   -109.77 
3 1 SER A 93  ? ? 78.24   -0.26   
4 1 SER A 93  ? ? 78.24   -2.55   
5 1 GLN A 113 ? ? 62.80   63.15   
6 1 MET A 114 ? ? -119.46 79.89   
# 
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 326 ? F HOH . 
2 1 A HOH 383 ? F HOH . 
3 1 A HOH 450 ? F HOH . 
4 1 A HOH 461 ? F HOH . 
5 1 A HOH 463 ? F HOH . 
6 1 A HOH 466 ? 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  -0.0595 -0.0605 -0.0414 0.0287  -0.0164 1.1047 1.8993 2.2850 
0.4900 -0.2415 1.2615 0.1348 -0.0957 -0.0391 -0.0655 0.1018 0.0898 0.2663  0.0115 -0.0501 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.1185 0.1233  -0.0392 -0.0655 -0.0080 -0.0832 0.5677 0.0870 0.0000 
0.2392 0.0468  0.2375 0.0057 0.0159  -0.0216 0.0085  0.0179 0.0352 -0.0148 0.0165 0.0017  
# 
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                    7GUR 
_atom_sites.fract_transf_matrix[1][1]   0.014786 
_atom_sites.fract_transf_matrix[1][2]   0.008537 
_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]   0.017074 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006014 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP A 1 5   ? 17.575 -21.166 -4.927 1.00 74.30  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.441 -22.085 -5.671 1.00 73.21  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.940 -23.550 -5.583 1.00 72.99  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.861 -23.805 -5.035 1.00 73.70  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.899 -21.963 -5.162 1.00 73.82  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.952 -22.036 -6.260 1.00 87.04  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 21.018 -23.078 -6.957 1.00 87.78  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.717 -21.057 -6.413 1.00 93.58  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.721 -24.499 -6.137 1.00 64.36  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.429 -25.932 -6.115 1.00 61.76  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.416 -26.697 -5.170 1.00 57.70  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.719 -27.871 -5.398 1.00 57.20  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.467 -26.493 -7.532 1.00 67.60  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.736 -26.294 -8.137 1.00 80.29  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.894 -26.025 -4.105 1.00 47.73  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.824 -26.601 -3.127 1.00 44.12  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.205 -27.765 -2.327 1.00 42.63  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.984 -27.846 -2.177 1.00 43.26  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.321 -25.512 -2.175 1.00 44.87  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.439 -24.287 -2.924 1.00 49.84  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.052 -28.650 -1.798 1.00 32.96  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.675 -29.655 -0.801 1.00 30.22  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.276 -29.117 0.491  1.00 31.97  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.223 -28.324 0.438  1.00 30.56  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 21.043 -31.129 -1.117 1.00 33.24  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.570 -31.303 -1.388 1.00 33.25  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.180 -31.656 -2.281 1.00 34.59  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.073 -32.761 -1.562 1.00 35.40  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.786 -29.547 1.648  0.57 27.54  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.682 -29.470 1.629  0.43 27.52  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.317 -29.020 2.905  0.57 26.19  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.116 -28.993 2.938  0.43 26.11  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.661 -30.144 3.885  0.57 29.77  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.575 -30.155 3.807  0.43 28.84  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.864 -31.071 4.039  0.57 29.36  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.942 -31.209 3.805  0.43 28.42  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.282 -28.046 3.513  0.57 27.58  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.959 -28.228 3.628  0.43 27.46  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.708 -27.357 4.813  0.57 26.60  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.181 -27.944 5.134  0.43 36.34  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.524 -26.713 5.494  0.57 55.26  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.078 -26.493 5.530  0.43 45.05  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.579 -27.378 5.936  0.57 47.19  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.777 -25.604 4.717  0.43 34.59  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.545 -25.396 5.590  0.57 59.02  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.324 -26.226 6.811  0.43 34.39  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.828 -30.061 4.550  0.78 27.60  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.646 -29.941 4.574  0.22 25.37  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.221 -31.055 5.557  0.78 27.00  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.165 -30.912 5.528  0.22 24.95  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.723 -30.562 6.916  0.78 28.77  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.653 -30.454 6.882  0.22 28.63  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.277 -29.612 7.471  0.78 27.20  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 23.097 -29.418 7.389  0.22 27.61  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.751 -31.338 5.550  0.78 28.33  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.700 -30.960 5.460  0.22 26.08  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.124 -32.566 6.360  0.78 29.67  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.209 -31.851 4.352  0.22 28.07  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.712 -33.837 5.964  0.78 33.74  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 25.020 -31.509 3.016  0.22 31.65  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.867 -32.449 7.531  0.78 31.66  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.866 -33.038 4.642  0.22 30.81  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 25.040 -34.969 6.728  0.78 34.74  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.489 -32.334 1.993  0.22 32.89  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.178 -33.575 8.300  0.78 33.79  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.330 -33.863 3.615  0.22 34.15  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.769 -34.826 7.894  0.78 32.46  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 26.145 -33.501 2.302  0.22 32.33  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.641 -31.166 7.416  1.00 26.21  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.971 -30.779 8.677  1.00 26.79  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.919 -30.537 9.882  1.00 29.95  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.779 -29.519 10.573 1.00 28.24  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.893 -31.816 9.025  1.00 35.06  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.969 -31.892 7.926  1.00 34.53  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.126 -31.469 10.311 1.00 39.14  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.866 -31.460 10.111 0.50 27.33  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.860 -31.466 10.116 0.50 27.54  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.775 -31.394 11.262 0.50 27.33  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.788 -31.417 11.255 0.50 27.64  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 25.035 -30.536 11.059 0.50 28.52  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 25.028 -30.529 11.063 0.50 28.69  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.856 -30.462 11.976 0.50 26.86  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.840 -30.440 11.988 0.50 27.06  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.169 -32.820 11.705 0.50 30.13  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.229 -32.847 11.611 0.50 30.87  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.010 -33.681 12.242 0.50 37.90  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.311 -33.550 12.612 0.50 41.17  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.475 -33.200 13.585 0.50 49.88  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 23.039 -35.007 12.279 0.50 47.49  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.424 -33.406 14.682 0.50 56.15  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.249 -35.780 11.981 0.50 49.64  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.400 -32.740 15.833 0.50 63.40  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.436 -36.475 10.862 0.50 60.59  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.490 -31.796 16.043 0.50 42.01  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.559 -37.156 10.676 0.50 52.25  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.292 -33.003 16.775 0.50 52.52  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.494 -36.507 9.926  0.50 36.67  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.196 -29.898 9.884  1.00 24.62  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.401 -29.103 9.580  1.00 24.38  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.692 -27.988 10.587 1.00 26.94  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.825 -27.928 11.094 1.00 26.05  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.389 -28.548 8.144  1.00 24.30  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.651 -27.797 7.819  1.00 26.01  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.845 -28.455 7.643  1.00 26.36  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.857 -26.466 7.680  1.00 26.41  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.744 -27.519 7.384  1.00 25.94  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.195 -26.303 7.399  1.00 25.89  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.706 -27.102 10.860 1.00 23.86  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.914 -25.978 11.790 1.00 23.28  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.324 -26.456 13.194 1.00 25.89  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.238 -25.885 13.779 1.00 25.02  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.663 -25.089 11.845 1.00 24.52  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.660 -27.502 13.709 0.38 24.03  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.664 -27.508 13.709 0.33 23.98  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.660 -27.507 13.716 0.29 23.74  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.950 -28.085 15.016 0.38 24.28  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.953 -28.095 15.018 0.33 24.24  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.959 -28.080 15.031 0.29 23.91  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.363 -28.686 15.041 0.38 28.66  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.361 -28.694 15.045 0.33 28.76  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.361 -28.703 15.054 0.29 28.70  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.094 -28.473 16.012 0.38 26.81  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.083 -28.499 16.025 0.33 27.18  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.078 -28.532 16.042 0.29 27.36  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.899 -29.134 15.377 0.38 28.46  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.912 -29.156 15.372 0.33 28.36  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.895 -29.099 15.435 0.29 27.61  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.107 -29.636 16.686 0.38 34.97  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.605 -28.608 15.353 0.33 34.76  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.906 -30.231 14.581 0.29 32.72  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.757 -29.390 13.958 1.00 26.54  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.098 -30.009 13.822 1.00 27.91  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.176 -28.919 13.797 1.00 27.78  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.219 -29.079 14.430 1.00 27.23  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.185 -30.860 12.543 1.00 30.12  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.430 -32.190 12.619 1.00 41.65  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.883 -32.509 13.706 1.00 41.86  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.374 -32.902 11.592 1.00 42.10  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.918 -27.805 13.072 1.00 23.33  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.861 -26.671 13.024 1.00 23.14  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 31.058 -26.118 14.457 1.00 24.74  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.189 -25.920 14.903 1.00 23.47  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.373 -25.557 12.055 1.00 24.93  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.117 -24.241 12.281 1.00 24.55  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.479 -26.003 10.596 1.00 24.69  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.954 -25.860 15.164 1.00 23.38  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 30.030 -25.284 16.509 1.00 24.30  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.774 -26.199 17.486 1.00 27.25  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.609 -25.711 18.272 1.00 24.83  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.645 -24.898 17.040 1.00 25.16  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.645 -23.944 18.274 1.00 28.00  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.198 -22.558 17.922 1.00 27.25  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.226 -23.807 18.837 1.00 32.14  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.491 -27.512 17.413 1.00 25.71  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.168 -28.540 18.213 1.00 26.80  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.688 -28.492 17.951 1.00 26.89  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.471 -28.484 18.906 1.00 25.31  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.597 -29.928 17.879 1.00 28.95  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.198 -31.104 18.643 1.00 37.26  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.699 -31.120 20.107 1.00 39.32  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.811 -32.412 17.985 1.00 41.20  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.102 -28.388 16.670 1.00 23.71  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.521 -28.275 16.335 1.00 23.70  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.145 -26.967 16.812 1.00 25.70  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.302 -26.966 17.225 1.00 25.59  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.760 -28.509 14.852 1.00 23.76  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.667 -29.974 14.510 1.00 36.67  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.818 -30.841 15.375 1.00 31.62  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.396 -30.283 13.248 1.00 27.55  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.393 -25.854 16.749 1.00 23.65  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.886 -24.564 17.262 1.00 23.24  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.099 -24.696 18.770 1.00 25.48  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.094 -24.186 19.297 1.00 23.96  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.908 -23.404 16.938 1.00 22.81  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.804 -23.043 15.431 1.00 26.12  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.716 -21.984 15.203 1.00 25.97  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.139 -22.572 14.868 1.00 28.59  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.174 -25.388 19.471 1.00 22.97  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.351 -25.604 20.920 1.00 23.97  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.579 -26.496 21.235 1.00 28.19  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.276 -26.246 22.221 1.00 29.39  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.091 -26.162 21.566 1.00 24.45  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.118 -26.010 23.066 1.00 31.52  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.629 -25.032 23.608 1.00 28.98  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.565 -26.965 23.753 1.00 31.67  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.866 -27.505 20.388 1.00 25.23  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 37.068 -28.352 20.555 1.00 26.18  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.341 -27.516 20.371 1.00 30.27  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.300 -27.709 21.097 1.00 30.76  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 37.065 -29.502 19.544 1.00 26.40  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 36.056 -30.591 19.883 1.00 32.54  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.806 -31.473 18.671 1.00 37.73  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.956 -32.609 19.010 1.00 43.06  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.489 -33.490 18.132 1.00 63.68  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.737 -33.343 16.834 1.00 48.59  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.762 -34.521 18.543 1.00 52.18  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.340 -26.568 19.413 1.00 27.08  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.487 -25.681 19.233 1.00 25.77  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.644 -24.803 20.481 1.00 30.07  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.766 -24.657 20.980 1.00 29.83  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.308 -24.807 18.011 1.00 24.96  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.277 -25.505 16.637 1.00 29.18  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.097 -24.442 15.531 1.00 28.60  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.559 -26.339 16.402 1.00 31.66  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.525 -24.263 21.017 1.00 26.56  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.602 -23.472 22.254 1.00 27.75  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.202 -24.289 23.432 1.00 33.09  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.068 -23.769 24.148 1.00 33.18  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.220 -22.911 22.653 1.00 27.50  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.317 -22.033 23.913 1.00 31.98  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.994 -21.425 24.295 1.00 32.66  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.983 -22.422 24.656 1.00 32.39  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.367 -22.472 25.831 1.00 45.99  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.725 -21.651 26.814 1.00 41.44  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.413 -23.365 26.046 1.00 34.62  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.726 -25.530 23.634 0.40 31.37  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.731 -25.538 23.632 0.35 31.44  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.732 -25.541 23.627 0.25 30.93  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.200 -26.419 24.699 0.40 32.90  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.186 -26.427 24.710 0.35 33.02  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.174 -26.450 24.696 0.25 32.33  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.714 -26.594 24.626 0.40 38.15  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.685 -26.742 24.630 0.35 38.55  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.672 -26.775 24.624 0.25 38.06  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.397 -26.485 25.648 0.40 39.05  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.327 -26.914 25.667 0.35 39.95  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.296 -27.001 25.661 0.25 39.26  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.546 -27.793 24.576 0.40 36.82  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.368 -27.715 24.739 0.35 36.91  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.355 -27.738 24.679 0.25 35.73  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.212 -27.805 25.049 0.40 44.38  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.657 -28.571 23.645 0.35 45.34  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.738 -28.624 25.719 0.25 43.83  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.233 -26.810 23.404 1.00 34.22  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.657 -27.084 23.153 1.00 35.85  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.481 -25.807 22.956 1.00 38.65  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.688 -25.880 22.717 1.00 39.18  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.789 -28.047 21.974 1.00 37.83  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 42.028 -29.352 22.205 1.00 47.28  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 42.021 -30.230 20.978 1.00 55.41  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.356 -30.772 20.719 1.00 75.49  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.878 -30.912 19.508 1.00 93.42  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.100 -31.405 19.359 1.00 84.05  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.186 -30.558 18.437 1.00 80.54  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.827 -24.638 23.097 1.00 32.94  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.415 -23.299 22.962 1.00 34.08  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 44.013 -23.081 21.550 1.00 38.37  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.076 -22.474 21.398 1.00 39.09  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.457 -23.027 24.083 1.00 37.26  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.771 -21.558 24.267 1.00 46.95  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.851 -20.721 24.075 1.00 46.55  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.936 -21.238 24.587 1.00 52.06  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.341 -23.604 20.526 1.00 32.33  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.843 -23.496 19.152 1.00 30.88  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.240 -22.300 18.447 1.00 33.85  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 42.001 -22.168 18.372 1.00 30.49  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.641 -24.810 18.350 1.00 33.63  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.438 -25.982 18.973 1.00 35.66  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.976 -24.626 16.843 1.00 33.12  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.917 -27.390 18.470 1.00 37.44  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.118 -21.424 17.922 0.54 31.70  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.123 -21.426 17.924 0.46 32.25  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.769 -20.222 17.160 0.54 31.07  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.801 -20.215 17.169 0.46 31.92  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.880 -19.226 17.924 0.54 33.07  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.890 -19.227 17.922 0.46 33.48  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.242 -18.378 17.297 0.54 31.78  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.252 -18.385 17.289 0.46 32.21  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.158 -20.568 15.784 0.54 31.04  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.244 -20.545 15.777 0.46 32.18  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 44.086 -21.219 14.730 0.54 36.55  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.289 -20.458 14.667 0.46 38.45  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.545 -20.992 13.360 0.54 34.90  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.497 -21.800 14.005 0.46 38.86  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.502 -20.649 14.768 0.54 40.09  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.904 -19.419 13.649 0.46 40.45  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.889 -19.283 19.272 1.00 29.36  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.164 -18.304 20.109 1.00 29.33  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.973 -17.001 19.917 1.00 35.56  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.202 -17.051 19.798 1.00 35.58  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.097 -18.726 21.577 1.00 34.07  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.409 -19.087 21.983 1.00 36.58  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.115 -19.884 21.807 1.00 32.19  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.291 -15.882 19.736 1.00 31.57  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.960 -14.633 19.384 1.00 31.79  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.628 -13.489 20.309 1.00 34.05  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.982 -12.341 20.024 1.00 34.39  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.644 -14.283 17.915 1.00 32.96  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.159 -14.299 17.561 1.00 42.75  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.320 -14.361 18.491 1.00 38.33  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.839 -14.262 16.359 1.00 51.91  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.976 -13.792 21.437 1.00 29.00  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.653 -12.753 22.415 1.00 28.14  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.471 -13.337 23.795 1.00 31.48  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.065 -14.500 23.942 1.00 31.08  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.400 -11.903 21.967 1.00 31.09  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 39.082 -12.676 22.124 1.00 29.55  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.339 -10.535 22.685 1.00 31.29  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.765 -12.519 24.811 0.53 28.12  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.781 -12.536 24.816 0.47 28.33  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.545 -12.827 26.218 0.53 27.64  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.512 -12.885 26.200 0.47 27.95  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.494 -11.828 26.714 0.53 31.43  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.527 -11.850 26.765 0.47 31.72  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.658 -10.617 26.528 0.53 32.23  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.740 -10.640 26.624 0.47 32.55  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.861 -12.735 27.045 0.53 32.22  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.768 -13.154 27.081 0.47 32.76  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.609 -12.948 28.540 0.53 32.42  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.619 -11.906 27.283 0.47 33.43  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.893 -13.726 26.534 0.53 32.59  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.383 -13.773 28.420 0.47 32.88  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.420 -12.334 27.332 1.00 27.28  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.375 -11.501 27.930 1.00 26.45  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.661 -11.538 29.428 1.00 31.59  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.701 -12.623 30.023 1.00 30.54  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.936 -11.983 27.600 1.00 27.92  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.692 -12.138 26.066 1.00 27.76  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.894 -11.094 28.251 1.00 29.90  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 36.999 -10.885 25.162 1.00 29.19  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.887 -10.356 30.021 1.00 29.20  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.209 -10.229 31.446 1.00 29.80  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.948 -9.787  32.178 1.00 34.15  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.360 -8.746  31.842 1.00 32.10  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.403 -9.255  31.692 1.00 34.40  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.740 -9.149  33.181 1.00 35.25  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.636 -9.694  30.913 1.00 34.80  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.548 -10.572 33.199 1.00 31.66  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.351 -10.339 34.007 1.00 31.67  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.811 -10.406 35.451 1.00 37.92  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 37.050 -11.497 35.972 1.00 35.68  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.220 -11.351 33.666 1.00 35.22  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.902 -10.927 34.303 1.00 35.29  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 35.057 -11.514 32.148 1.00 33.69  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.726 -9.284  36.200 0.50 37.51  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.281 -9.209  35.882 0.50 35.41  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 37.081 -9.252  37.634 0.50 39.54  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.943 -8.868  37.128 0.50 36.40  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.339 -10.122 37.953 0.50 43.86  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.249 -9.660  37.254 0.50 38.69  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.295 -10.968 38.852 0.50 43.99  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.153 -9.399  36.465 0.50 36.92  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.886 -9.682  38.493 0.50 45.14  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 36.997 -8.982  38.318 0.50 41.17  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.763 -8.824  38.351 0.50 56.88  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.049 -7.929  38.234 0.50 50.74  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.425 -9.944  37.156 0.50 39.83  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.350 -10.646 38.168 0.50 36.06  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.709 -10.669 37.246 0.50 40.42  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.589 -11.420 38.282 0.50 36.71  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.587 -12.206 36.988 0.50 43.13  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.719 -12.450 37.118 0.50 41.32  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.365 -13.014 37.529 0.50 43.94  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.756 -12.499 36.438 0.50 41.80  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.460 -10.376 38.560 0.50 42.41  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.745 -12.047 39.695 0.50 36.40  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 41.994 -8.953  38.682 0.50 53.48  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 41.022 -11.000 40.794 0.50 44.85  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.075 -8.879  39.742 0.50 60.22  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.387 -11.608 42.145 0.50 42.82  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.437 -7.501  40.079 0.50 67.85  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.555 -10.593 43.190 0.50 44.25  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.878 -6.795  41.058 0.50 81.44  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.718 -10.047 43.541 0.50 58.88  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.907 -7.320  41.796 0.50 66.57  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.839 -10.396 42.923 0.50 48.17  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.278 -5.554  41.300 0.50 69.07  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.766 -9.139  44.505 0.50 48.40  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.613 -12.591 36.160 0.50 36.17  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.625 -13.173 36.826 0.50 35.42  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.412 -13.963 35.685 0.50 35.36  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.564 -14.238 35.818 0.50 34.15  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.550 -13.843 34.179 0.50 35.98  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.807 -13.784 34.368 0.50 35.04  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.960 -12.935 33.585 0.50 32.92  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.472 -12.667 33.987 0.50 31.80  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 38.048 -14.540 36.101 0.50 36.68  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.237 -15.020 35.917 0.50 35.18  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.944 -14.780 37.601 0.50 51.02  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.753 -15.221 37.351 0.50 51.00  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.874 -16.229 38.042 0.50 87.36  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.933 -16.583 37.997 0.50 89.29  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.845 -16.611 38.646 0.50 90.35  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.978 -17.234 37.763 0.50 92.71  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.845 -16.981 37.794 0.50 89.57  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 37.031 -16.987 38.767 0.50 90.71  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.382 -14.698 33.568 1.00 32.59  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.701 -14.570 32.153 1.00 31.82  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 40.071 -15.687 31.352 1.00 35.43  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.146 -16.845 31.757 1.00 36.54  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.226 -14.578 31.975 1.00 34.52  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.897 -13.345 32.560 1.00 49.76  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.375 -13.235 32.273 1.00 72.88  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.956 -13.962 31.452 1.00 65.96  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 45.017 -12.298 32.952 1.00 76.29  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.473 -15.351 30.203 1.00 28.95  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.829 -16.344 29.334 1.00 28.30  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.337 -16.183 27.918 1.00 32.39  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.161 -15.116 27.334 1.00 32.16  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.298 -16.162 29.350 1.00 29.81  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.677 -16.256 30.719 1.00 31.99  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.562 -15.128 31.529 1.00 33.87  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.194 -17.470 31.198 1.00 33.86  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 36.006 -15.218 32.807 1.00 35.90  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.633 -17.558 32.477 1.00 37.17  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.532 -16.429 33.268 1.00 35.20  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.946 -17.240 27.350 1.00 29.48  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.455 -17.197 25.979 1.00 28.42  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.335 -17.589 25.029 1.00 31.87  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.530 -18.469 25.342 1.00 31.07  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.689 -18.112 25.792 1.00 28.99  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.922 -17.684 26.637 1.00 39.13  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.249 -18.084 25.989 1.00 51.18  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.266 -17.708 24.567 1.00 63.22  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.885 -16.647 24.057 1.00 76.19  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.630 -15.870 24.830 1.00 68.09  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.802 -16.383 22.761 1.00 59.15  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.243 -16.912 23.878 1.00 27.71  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.173 -17.223 22.917 1.00 27.10  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.572 -16.816 21.507 1.00 28.58  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.669 -16.282 21.285 1.00 27.54  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.878 -16.497 23.315 1.00 28.03  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.674 -17.081 20.556 1.00 25.10  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.826 -16.662 19.172 1.00 24.69  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.939 -15.416 18.986 1.00 28.42  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.724 -15.455 19.251 1.00 27.26  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.387 -17.775 18.202 1.00 24.41  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.136 -19.065 18.401 1.00 28.34  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.621 -20.090 19.181 1.00 29.93  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.364 -19.431 17.956 1.00 29.18  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.542 -21.049 19.177 1.00 29.21  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.604 -20.701 18.446 1.00 29.24  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.542 -14.327 18.532 1.00 26.27  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.815 -13.080 18.248 1.00 26.32  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.585 -13.316 17.374 1.00 28.53  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.530 -12.791 17.699 1.00 26.61  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.726 -12.081 17.527 1.00 29.40  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.732 -11.442 18.466 1.00 29.25  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.662 -10.521 17.687 1.00 30.64  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.816 -10.107 18.559 1.00 34.13  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.742 -9.190  17.841 1.00 36.57  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.699 -14.144 16.306 1.00 24.83  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.558 -14.351 15.402 1.00 24.25  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.383 -15.016 16.065 1.00 26.26  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.255 -14.626 15.780 1.00 25.19  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.950 -15.058 14.116 1.00 31.87  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.545 -16.294 14.467 1.00 32.41  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.872 -14.190 13.244 1.00 33.35  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.624 -15.971 16.962 1.00 23.34  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.535 -16.651 17.679 1.00 23.77  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.858 -15.656 18.635 1.00 26.62  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.618 -15.604 18.726 1.00 24.42  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 33.038 -17.926 18.412 1.00 26.08  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.925 -18.529 19.285 1.00 26.03  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.518 -18.963 17.392 1.00 25.84  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.678 -14.870 19.365 1.00 23.54  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.133 -13.850 20.283 1.00 24.19  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.240 -12.856 19.522 1.00 26.29  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.138 -12.551 19.974 1.00 25.42  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.279 -13.080 20.968 1.00 24.31  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.205 -13.865 21.906 1.00 27.42  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.266 -12.923 22.497 1.00 28.00  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.424 -14.541 23.021 1.00 28.69  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.682 -12.416 18.346 1.00 23.64  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.910 -11.480 17.506 1.00 24.33  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.628 -12.125 17.003 1.00 28.71  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.584 -11.478 17.020 1.00 28.71  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.720 -11.010 16.299 1.00 26.20  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.933 -10.191 16.673 1.00 29.45  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.940 -10.069 15.199 1.00 33.48  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.161 -8.707  14.431 1.00 29.87  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.688 -13.412 16.608 1.00 25.91  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.523 -14.138 16.091 1.00 25.91  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.405 -14.316 17.154 1.00 28.21  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.239 -14.491 16.802 1.00 28.92  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.959 -15.497 15.540 1.00 26.27  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.774 -14.259 18.447 1.00 24.76  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.874 -14.494 19.570 1.00 24.97  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.423 -13.267 20.344 1.00 28.06  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.456 -13.373 21.110 1.00 27.97  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.538 -15.480 20.527 1.00 25.74  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.837 -17.114 19.817 1.00 29.31  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.182 -12.166 20.270 1.00 24.64  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.968 -11.029 21.153 1.00 23.59  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 27.015 -9.703  20.420 1.00 29.09  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.983 -9.436  19.703 1.00 27.21  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.047 -11.100 22.238 1.00 25.51  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.467 -9.857  22.780 1.00 30.38  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.983 -8.876  20.619 1.00 27.32  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.930 -7.541  20.033 1.00 27.39  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 27.047 -6.657  20.548 1.00 30.38  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.570 -5.822  19.806 1.00 30.07  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.450 -6.855  21.830 1.00 28.06  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.552 -6.081  22.404 1.00 27.69  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.877 -6.438  21.718 1.00 29.44  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.562 -5.520  21.257 1.00 29.21  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.665 -6.269  23.929 1.00 27.20  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.713 -5.359  24.605 1.00 31.91  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.266 -3.875  24.622 1.00 33.37  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 30.042 -5.847  25.998 1.00 32.39  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.212 -7.750  21.598 1.00 24.64  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.473 -8.131  20.925 1.00 24.53  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.455 -7.792  19.447 1.00 29.22  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.490 -7.423  18.900 1.00 28.23  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.869 -9.579  21.180 1.00 24.83  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.270 -9.813  22.622 1.00 26.05  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.361 -9.141  23.179 1.00 29.44  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.604 -10.759 23.401 1.00 27.81  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.728 -9.350  24.522 1.00 29.99  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 32.002 -11.004 24.727 1.00 30.52  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 33.048 -10.277 25.284 1.00 28.61  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.274 -7.860  18.810 1.00 27.23  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.160 -7.447  17.410 1.00 28.22  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.598 -5.968  17.242 1.00 32.37  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.386 -5.657  16.344 1.00 30.64  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.723 -7.665  16.925 1.00 30.63  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.501 -7.166  15.521 1.00 33.94  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 29.051 -7.830  14.429 1.00 35.43  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.746 -6.023  15.282 1.00 38.19  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.854 -7.364  13.128 1.00 38.44  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.545 -5.549  13.992 1.00 41.22  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.090 -6.230  12.920 1.00 47.51  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.862 -5.746  11.669 1.00 53.67  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.095 -5.071  18.106 0.52 29.41  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 30.086 -5.081  18.113 0.48 30.25  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.428 -3.643  18.077 0.52 30.63  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.400 -3.653  18.119 0.48 31.82  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.908 -3.414  18.389 0.52 35.86  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.895 -3.437  18.381 0.48 36.22  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.557 -2.645  17.687 0.52 37.55  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.536 -2.703  17.635 0.48 37.57  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.540 -2.876  19.053 0.52 32.91  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.567 -2.941  19.184 0.48 35.39  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.190 -2.961  18.630 0.52 35.16  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.807 -1.544  19.159 0.48 45.17  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.451 -4.127  19.401 1.00 31.87  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.864 -4.024  19.802 1.00 31.35  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.809 -4.421  18.670 1.00 34.58  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.726 -3.660  18.344 1.00 36.31  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.172 -4.861  21.099 1.00 32.42  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.461 -4.284  22.338 1.00 32.72  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.700 -4.974  21.351 1.00 30.50  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.409 -5.287  23.566 1.00 34.94  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.600 -5.602  18.076 1.00 29.09  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.559 -6.072  17.086 1.00 29.41  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.314 -5.538  15.668 1.00 34.49  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.159 -5.773  14.809 1.00 35.69  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.701 -7.605  17.135 1.00 29.63  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.127 -8.102  18.504 1.00 30.32  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.313 -7.659  19.090 1.00 33.95  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.321 -8.971  19.224 1.00 31.35  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.696 -8.107  20.361 1.00 34.47  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.716 -9.443  20.483 1.00 34.39  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.890 -8.998  21.050 1.00 32.76  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.260 -4.730  15.440 1.00 31.74  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.101 -4.045  14.142 1.00 32.85  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.659 -2.612  14.268 1.00 39.80  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.729 -1.867  13.285 1.00 39.42  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.674 -4.085  13.584 1.00 39.62  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.775 -3.573  14.555 1.00 37.44  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.250 -5.489  13.112 1.00 35.39  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.097 -2.240  15.481 1.00 36.60  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.702 -0.933  15.698 1.00 38.07  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.141 -1.015  15.184 1.00 44.14  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.881 -1.898  15.612 1.00 42.12  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.678 -0.556  17.188 1.00 39.35  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.433 0.731   17.426 1.00 54.56  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.820 1.803   17.294 1.00 59.39  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.661 0.664   17.677 1.00 56.96  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.541 -0.067  14.307 1.00 45.66  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.862 -0.018  13.669 1.00 47.05  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 40.044 -0.079  14.642 1.00 51.28  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 41.070 -0.635  14.267 1.00 53.40  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.993 1.190   12.729 1.00 50.59  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 38.148 1.081   11.464 1.00 70.55  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.922 0.479   15.872 1.00 44.60  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 41.014 0.404   16.851 1.00 43.61  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.937 -0.842  17.713 1.00 45.98  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.972 -1.413  18.043 1.00 47.35  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 41.018 1.613   17.801 1.00 44.68  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.703 2.885   17.338 1.00 52.07  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.511 3.970   18.361 1.00 52.88  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.198 2.673   17.086 1.00 57.06  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.734 -1.198  18.183 1.00 39.23  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.583 -2.320  19.111 1.00 37.33  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.714 -3.685  18.456 1.00 41.50  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 40.077 -4.634  19.146 1.00 39.12  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.265 -2.233  19.900 1.00 38.32  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.162 -1.031  20.822 1.00 38.54  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.863 -1.112  21.593 1.00 34.23  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.550 0.177   22.316 1.00 41.64  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.967 1.197   21.416 1.00 39.38  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.434 -3.785  17.132 1.00 41.46  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.524 -5.046  16.374 1.00 41.99  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.909 -5.693  16.516 1.00 47.21  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 41.031 -6.913  16.372 1.00 46.98  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.159 -4.833  14.904 1.00 43.68  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.350 -3.820  13.970 1.00 50.12  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.937 -4.858  16.802 1.00 43.89  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.345 -5.232  16.931 1.00 44.92  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.824 -5.507  18.359 1.00 47.30  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.993 -5.853  18.557 1.00 47.33  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.235 -4.174  16.261 1.00 47.15  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 44.022 -4.104  14.762 1.00 62.25  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 43.938 -3.025  14.176 1.00 61.47  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.891 -5.254  14.109 1.00 50.49  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.943 -5.368  19.346 1.00 42.59  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.323 -5.625  20.730 1.00 41.84  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.313 -7.136  21.000 1.00 42.96  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.445 -7.842  20.468 1.00 40.77  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.344 -4.911  21.692 1.00 41.94  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.339 -3.375  21.650 1.00 47.49  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.269 -2.820  22.562 1.00 47.72  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.721 -2.786  22.022 1.00 48.86  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.276 -7.612  21.821 1.00 38.92  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.403 -9.022  22.207 0.42 38.05  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.367 -9.030  22.190 0.58 38.35  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.764 -9.238  23.582 1.00 39.13  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.549 -10.372 24.003 1.00 35.52  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.874 -9.435  22.242 0.42 42.56  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.816 -9.512  22.145 0.58 43.38  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.468 -9.360  20.956 0.42 48.92  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.627 -8.791  23.056 0.58 51.65  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.489 -8.135  24.296 1.00 35.22  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.883 -8.159  25.630 1.00 34.48  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.696 -7.191  25.678 1.00 36.19  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.831 -6.026  25.279 1.00 35.74  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.928 -7.820  26.741 1.00 40.45  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.306 -7.882  28.133 1.00 40.64  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 45.159 -8.726  26.663 1.00 41.22  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.538 -7.673  26.181 1.00 30.65  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.337 -6.862  26.385 1.00 29.78  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.946 -6.953  27.854 1.00 32.70  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.738 -8.053  28.361 1.00 32.58  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.164 -7.242  25.428 1.00 31.15  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.556 -7.112  23.926 1.00 32.10  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.873 -6.454  25.756 1.00 32.44  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.914 -5.668  23.399 1.00 36.72  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.819 -5.809  28.532 1.00 29.94  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.417 -5.801  29.932 1.00 30.16  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.931 -5.484  30.050 1.00 32.87  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.490 -4.411  29.615 1.00 32.28  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.233 -4.775  30.731 1.00 33.96  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.714 -5.009  30.687 1.00 52.98  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.223 -6.000  31.195 1.00 43.18  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.445 -4.091  30.101 1.00 49.22  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.171 -6.372  30.681 1.00 27.58  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.745 -6.121  30.859 1.00 27.61  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.503 -5.219  32.071 1.00 32.38  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.378 -5.081  32.939 1.00 33.61  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.949 -7.432  31.001 1.00 27.72  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.985 -8.422  29.810 1.00 30.98  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.833 -9.458  29.948 1.00 31.51  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.926 -7.699  28.443 1.00 31.21  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.310 -4.622  32.133 1.00 29.31  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.885 -3.740  33.229 1.00 30.80  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 33.048 -4.490  34.575 1.00 36.50  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.686 -5.668  34.653 1.00 34.83  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.417 -3.321  33.009 1.00 32.67  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.875 -2.299  33.995 1.00 43.94  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.672 -2.659  35.173 1.00 45.02  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.615 -1.155  33.578 1.00 48.76  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.618 -3.840  35.618 1.00 37.68  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.820 -4.538  36.910 1.00 38.35  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.579 -5.107  37.573 1.00 41.69  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.717 -5.981  38.424 1.00 43.15  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.479 -3.477  37.804 1.00 41.32  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.187 -2.162  37.143 1.00 46.03  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.141 -2.457  35.671 1.00 40.11  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.378 -4.663  37.181 1.00 37.46  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.141 -5.201  37.760 1.00 38.51  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.830 -6.605  37.207 1.00 38.95  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.980 -7.301  37.760 1.00 38.43  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.957 -4.250  37.509 1.00 41.21  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.935 -3.035  38.426 1.00 61.98  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.403 -3.301  39.821 1.00 96.56  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.167 -3.430  39.972 1.00 98.97  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.224 -3.385  40.764 1.00 95.78  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.497 -7.004  36.103 1.00 33.42  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.264 -8.314  35.494 1.00 32.58  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.868 -9.422  36.342 1.00 36.55  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 32.044 -9.381  36.690 1.00 35.30  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.704 -8.370  34.007 1.00 33.92  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.970 -7.282  33.168 1.00 34.84  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.503 -9.788  33.415 1.00 29.64  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.348 -7.332  33.218 1.00 39.67  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 30.047 -10.410 36.634 1.00 36.22  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.373 -11.586 37.420 1.00 36.48  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.095 -12.630 36.545 1.00 36.80  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.557 -13.021 35.509 1.00 34.41  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 29.064 -12.153 38.004 1.00 39.20  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.232 -13.456 38.735 1.00 56.74  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.899 -14.520 38.215 1.00 47.53  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.755 -13.398 39.955 1.00 50.05  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.295 -13.121 36.948 1.00 34.72  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.997 -14.126 36.119 1.00 34.12  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.201 -15.413 35.868 1.00 37.35  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.269 -15.940 34.762 1.00 36.12  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.268 -14.421 36.917 1.00 36.90  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.460 -13.219 37.793 1.00 41.91  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.080 -12.777 38.154 1.00 37.43  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.445 -15.907 36.867 1.00 34.63  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.664 -17.136 36.662 1.00 34.36  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.575 -16.923 35.603 1.00 35.56  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.434 -17.761 34.718 1.00 33.56  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.076 -17.675 37.977 1.00 36.88  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.432 -19.046 37.789 1.00 49.68  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.608 -19.592 38.943 1.00 78.51  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.532 -20.836 39.069 1.00 78.65  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 28.027 -18.790 39.711 1.00 73.61  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.859 -15.791 35.678 1.00 32.80  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.852 -15.438 34.682 1.00 31.79  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.471 -15.389 33.295 1.00 33.18  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.898 -15.918 32.332 1.00 30.83  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.685 -14.807 33.186 1.00 28.74  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.362 -14.751 31.889 1.00 27.30  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.726 -16.155 31.400 1.00 29.48  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.545 -16.450 30.229 1.00 27.80  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.637 -13.886 31.930 1.00 28.55  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.236 -13.750 30.546 1.00 28.90  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.668 -12.894 29.605 1.00 31.20  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.310 -14.542 30.152 1.00 29.53  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.182 -12.814 28.306 1.00 31.54  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.816 -14.468 28.853 1.00 30.96  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.241 -13.613 27.935 1.00 29.51  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.306 -16.978 32.275 1.00 30.20  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.718 -18.353 31.949 1.00 31.90  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.526 -19.176 31.383 1.00 32.56  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.672 -19.857 30.358 1.00 30.89  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.328 -19.021 33.181 1.00 35.77  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.992 -20.682 32.868 1.00 41.85  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.347 -19.083 32.042 1.00 28.74  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.110 -19.788 31.627 1.00 27.39  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.699 -19.319 30.225 1.00 28.44  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.307 -20.137 29.378 1.00 26.26  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.986 -19.559 32.685 1.00 30.38  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.254 -20.395 33.979 1.00 30.95  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.558 -19.805 32.115 1.00 30.18  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.588 -19.820 35.199 1.00 37.49  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.791 -18.020 29.975 1.00 25.97  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.441 -17.467 28.657 1.00 25.77  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.445 -17.814 27.588 1.00 28.85  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.048 -18.063 26.450 1.00 26.98  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.192 -15.959 28.738 1.00 27.00  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.880 -15.606 29.481 1.00 33.46  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.783 -14.157 29.713 1.00 35.10  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.645 -16.066 28.695 1.00 35.47  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.750 -17.816 27.933 1.00 26.12  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.796 -18.226 26.986 1.00 24.82  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.558 -19.696 26.588 1.00 28.34  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.636 -20.027 25.407 1.00 27.44  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.194 -18.036 27.604 1.00 24.47  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.360 -18.330 26.649 1.00 29.16  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.327 -17.393 25.422 1.00 27.85  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.719 -18.252 27.396 1.00 33.34  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.257 -20.572 27.567 1.00 26.99  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.918 -21.972 27.293 1.00 26.60  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.703 -22.060 26.374 1.00 28.56  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.726 -22.837 25.428 1.00 27.76  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.633 -22.723 28.596 1.00 29.56  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.877 -23.070 29.399 1.00 44.12  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.999 -23.011 28.824 1.00 43.93  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.732 -23.408 30.604 1.00 46.92  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.656 -21.251 26.628 1.00 26.06  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.469 -21.205 25.760 1.00 24.68  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.838 -20.836 24.310 1.00 25.64  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.344 -21.434 23.343 1.00 23.88  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.403 -20.245 26.334 1.00 25.82  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.293 -19.971 25.349 1.00 26.55  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.309 -20.927 25.102 1.00 28.52  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.283 -18.794 24.593 1.00 28.01  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.326 -20.706 24.140 1.00 28.67  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.287 -18.568 23.635 1.00 30.73  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.304 -19.517 23.429 1.00 29.51  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.672 -19.816 24.155 1.00 22.99  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.088 -19.370 22.811 1.00 21.95  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.655 -20.513 21.999 1.00 26.21  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.329 -20.637 20.824 1.00 25.92  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.174 -18.286 22.932 1.00 23.40  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.661 -16.983 23.501 1.00 25.66  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 30.020 -15.771 23.392 1.00 29.72  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.402 -14.512 24.530 1.00 29.46  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.508 -21.345 22.629 1.00 23.05  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.189 -22.438 21.939 1.00 23.20  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.430 -23.771 21.922 1.00 27.41  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.923 -24.717 21.294 1.00 26.73  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.560 -22.654 22.593 1.00 24.04  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.635 -21.699 22.107 1.00 25.06  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.798 -20.446 22.691 1.00 26.09  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.460 -22.036 21.033 1.00 25.91  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.799 -19.572 22.259 1.00 26.00  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.488 -21.192 20.619 1.00 26.49  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.641 -19.952 21.222 1.00 28.32  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.669 -19.139 20.821 1.00 27.20  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.284 -23.887 22.639 1.00 23.72  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.596 -25.192 22.700 1.00 24.88  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.077 -25.143 22.434 1.00 28.00  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.487 -26.209 22.251 1.00 28.12  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.795 -25.872 24.098 1.00 31.26  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.119 -25.090 25.084 1.00 29.95  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.275 -26.054 24.502 1.00 30.77  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.431 -23.958 22.561 1.00 23.58  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.953 -23.768 22.502 1.00 23.21  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.291 -24.180 23.834 1.00 27.02  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.076 -24.057 23.962 1.00 27.85  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.301 -24.575 21.365 1.00 24.21  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.963 -24.408 20.122 1.00 32.21  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.094 -24.637 24.817 0.60 25.35  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.074 -24.684 24.813 0.40 24.61  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.600 -25.097 26.115 0.60 26.75  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.521 -25.116 26.100 0.40 25.62  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.815 -24.041 27.182 0.60 30.38  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.805 -24.114 27.201 0.40 30.00  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.939 -23.547 27.364 0.60 28.23  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.956 -23.701 27.400 0.40 28.38  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.293 -26.407 26.533 0.60 30.25  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.970 -26.539 26.480 0.40 27.21  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.078 -27.574 25.562 0.60 37.53  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.335 -27.600 25.592 0.40 29.20  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.051 -28.711 25.841 0.60 44.03  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 24.023 -28.943 25.688 0.40 40.90  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.843 -29.288 27.173 0.60 47.80  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.440 -29.904 24.750 0.40 45.15  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 23.986 -30.270 27.437 0.60 59.85  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.356 -31.213 24.967 0.40 58.75  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.851 -30.723 28.675 0.60 44.94  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.816 -32.009 24.054 0.40 48.82  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.260 -30.807 26.464 0.60 49.76  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.807 -31.736 26.100 0.40 45.66  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.735 -23.699 27.891 1.00 27.75  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.776 -22.703 28.939 1.00 27.47  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.527 -23.338 30.304 1.00 33.69  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.441 -23.862 30.561 1.00 32.73  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.743 -21.606 28.626 1.00 27.66  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.770 -20.386 29.560 1.00 31.76  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 23.015 -19.519 29.285 1.00 30.59  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.495 -19.569 29.429 1.00 33.30  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.535 -23.269 31.187 1.00 32.60  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.445 -23.813 32.548 1.00 33.87  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.732 -22.799 33.465 1.00 38.78  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.367 -22.106 34.259 1.00 38.79  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.848 -24.199 33.076 1.00 36.88  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.837 -24.822 34.467 1.00 56.54  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.844 -25.386 34.921 1.00 46.39  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.940 -24.722 35.185 1.00 48.83  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.414 -22.686 33.309 1.00 35.67  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.603 -21.729 34.055 1.00 36.60  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.072 -22.363 35.323 1.00 40.97  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.431 -23.420 35.261 1.00 40.30  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.465 -21.252 33.141 1.00 37.48  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.786 -19.930 33.460 1.00 44.12  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.804 -18.756 33.480 1.00 44.01  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.679 -19.664 32.446 1.00 45.32  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.395 -21.760 36.485 1.00 37.95  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 19.987 -22.282 37.802 1.00 39.90  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.468 -21.160 38.687 1.00 43.14  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.809 -19.994 38.465 1.00 42.04  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.169 -22.984 38.502 1.00 41.19  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.794 -24.145 37.706 1.00 51.27  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.067 -24.699 38.342 1.00 68.08  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.849 -25.190 39.709 1.00 88.03  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.404 -26.406 40.021 1.00 107.05 ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.228 -26.749 41.291 1.00 94.86  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.127 -27.286 39.065 1.00 95.03  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.646 -21.494 39.702 1.00 40.81  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.128 -20.479 40.634 1.00 41.51  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.253 -19.583 41.203 1.00 46.35  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.075 -18.366 41.304 1.00 46.04  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.353 -21.156 41.784 1.00 45.07  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.641 -20.178 42.706 1.00 57.99  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.928 -20.797 43.893 1.00 93.46  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.507 -21.693 44.551 1.00 94.74  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.786 -20.369 44.174 1.00 97.07  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.390 -20.194 41.542 1.00 44.14  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.541 -19.500 42.118 1.00 44.16  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.365 -18.640 41.174 1.00 45.53  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.211 -17.869 41.625 1.00 44.71  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.143 -18.752 39.859 1.00 40.40  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.938 -17.959 38.921 1.00 37.94  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.106 -17.094 37.968 1.00 40.82  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.685 -16.288 37.235 1.00 38.69  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.904 -18.882 38.136 1.00 36.30  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.247 -19.819 37.132 1.00 42.60  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.200 -19.515 36.557 1.00 34.82  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.873 -20.964 36.849 1.00 34.42  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.766 -17.289 37.936 1.00 38.26  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.884 -16.633 36.959 1.00 37.49  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 20.021 -15.099 36.935 1.00 39.78  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 20.040 -14.521 35.840 1.00 37.39  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.401 -17.080 37.058 1.00 41.51  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.563 -16.472 35.899 1.00 42.43  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.776 -16.832 38.446 1.00 39.94  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.410 -17.320 35.421 1.00 44.16  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.133 -14.447 38.100 1.00 38.33  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.277 -12.990 38.131 1.00 38.93  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.584 -12.520 37.501 1.00 40.03  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.549 -11.596 36.691 1.00 38.01  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.082 -12.422 39.551 1.00 43.43  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.695 -12.714 40.145 1.00 50.40  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.273 -12.263 39.096 1.00 56.63  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.321 -10.443 39.236 1.00 54.14  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.723 -13.194 37.813 1.00 37.28  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 24.048 -12.872 37.246 1.00 36.29  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 24.054 -13.165 35.736 1.00 37.68  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.556 -12.355 34.959 1.00 35.74  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.131 -13.699 37.930 1.00 37.37  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.465 -14.308 35.329 1.00 32.24  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.381 -14.695 33.906 1.00 29.96  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.581 -13.656 33.109 1.00 32.91  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.070 -13.214 32.063 1.00 31.04  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.887 -16.155 33.690 1.00 33.49  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.628 -16.456 32.214 1.00 32.00  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.882 -17.155 34.266 1.00 33.38  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.386 -13.252 33.594 0.65 31.33  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.385 -13.252 33.593 0.35 31.66  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.569 -12.254 32.892 0.65 32.72  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.564 -12.254 32.895 0.35 32.79  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.277 -10.902 32.771 0.65 35.70  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.275 -10.904 32.772 0.35 36.00  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.237 -10.286 31.699 0.65 34.06  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.248 -10.303 31.694 0.35 34.75  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.198 -12.069 33.552 0.65 36.90  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.187 -12.076 33.550 0.35 37.00  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.276 -11.166 32.742 0.65 41.46  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.262 -11.194 32.729 0.35 41.65  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.582 -11.180 33.344 0.65 48.13  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.624 -11.024 33.446 0.35 48.43  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.727 -10.094 34.821 0.65 46.00  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.192 -9.411  32.841 0.35 46.06  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.907 -10.435 33.864 1.00 33.14  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.648 -9.151  33.875 1.00 32.80  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.811 -9.191  32.878 1.00 33.32  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.977 -8.246  32.100 1.00 32.18  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.142 -8.831  35.281 1.00 34.18  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.544 -10.324 32.820 1.00 29.35  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.641 -10.506 31.872 1.00 27.97  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.118 -10.555 30.419 1.00 31.82  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.706 -9.905  29.553 1.00 30.13  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.542 -11.704 32.242 1.00 32.82  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.829 -11.687 33.645 1.00 33.30  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.852 -11.713 31.453 1.00 30.97  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 24.003 -11.282 30.166 1.00 28.52  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.412 -11.378 28.823 1.00 27.72  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.907 -10.011 28.354 1.00 29.84  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.062 -9.686  27.185 1.00 28.24  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.295 -12.427 28.795 1.00 28.90  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.374 -9.174  29.270 1.00 28.75  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.921 -7.820  28.899 1.00 30.32  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.108 -6.945  28.457 1.00 32.86  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.044 -6.269  27.429 1.00 33.37  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.164 -7.171  30.061 1.00 34.18  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.754 -7.709  30.210 1.00 40.12  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 18.992 -7.150  31.750 1.00 48.32  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.765 -5.399  31.379 1.00 46.34  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.197 -7.004  29.217 1.00 29.48  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.441 -6.281  28.942 1.00 29.09  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.073 -6.782  27.619 1.00 30.96  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.491 -5.971  26.789 1.00 30.05  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.396 -6.508  30.112 1.00 30.06  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.812 -6.030  29.883 1.00 31.02  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.134 -4.677  29.955 1.00 33.40  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.848 -6.939  29.678 1.00 30.42  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.440 -4.234  29.747 1.00 30.82  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.165 -6.513  29.525 1.00 29.93  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.455 -5.158  29.563 1.00 31.61  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.753 -4.744  29.451 1.00 31.95  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.103 -8.108  27.410 1.00 27.84  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.689 -8.697  26.199 1.00 26.15  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.777 -8.567  24.982 1.00 29.72  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.219 -8.838  23.867 1.00 28.88  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.070 -10.173 26.435 1.00 24.89  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.200 -10.447 27.463 1.00 28.50  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.476 -11.980 27.558 1.00 27.99  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.525 -9.669  27.090 1.00 29.02  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.493 -8.210  25.202 1.00 28.30  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.474 -8.061  24.152 1.00 28.82  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.247 -9.414  23.466 1.00 31.01  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.551 -9.599  22.289 1.00 29.77  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.851 -6.955  23.146 1.00 30.25  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 23.991 -5.563  23.777 1.00 35.08  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.739 -4.624  22.857 1.00 44.56  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.655 -4.719  21.634 1.00 36.93  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.503 -3.710  23.421 1.00 41.21  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.764 -10.376 24.255 1.00 27.64  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.461 -11.750 23.803 1.00 27.38  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.967 -11.906 24.068 1.00 33.92  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.554 -12.384 25.130 1.00 32.59  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.310 -12.735 24.614 1.00 28.26  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.803 -12.600 24.317 1.00 30.16  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.821 -13.631 25.380 1.00 33.10  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.486 -15.301 24.632 1.00 29.79  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.159 -11.354 23.150 1.00 34.32  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.703 -11.210 23.283 1.00 36.74  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.926 -12.495 23.580 1.00 38.13  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.991 -12.439 24.372 1.00 37.77  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.100 -10.508 22.055 1.00 40.02  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.674 -9.116  21.826 1.00 54.10  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.302 -13.638 22.987 1.00 33.44  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.579 -14.883 23.257 1.00 34.90  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.787 -15.359 24.696 1.00 36.74  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.821 -15.796 25.329 1.00 37.24  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.913 -15.963 22.229 1.00 36.11  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.437 -15.639 20.848 1.00 40.72  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 16.096 -15.448 20.576 1.00 44.54  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 18.134 -15.544 19.693 1.00 42.22  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 16.023 -15.197 19.278 1.00 44.24  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.222 -15.253 18.705 1.00 43.37  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 19.016 -15.190 25.237 1.00 30.73  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.325 -15.534 26.633 1.00 30.11  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.536 -14.620 27.584 1.00 36.03  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.926 -15.107 28.548 1.00 34.49  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.842 -15.538 26.945 1.00 32.24  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.090 -15.788 28.434 1.00 31.91  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.573 -16.577 26.093 1.00 31.00  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.521 -13.299 27.300 1.00 32.65  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.766 -12.334 28.112 1.00 33.14  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.279 -12.746 28.180 1.00 39.21  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.718 -12.794 29.278 1.00 38.68  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.939 -10.865 27.627 1.00 35.89  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.105 -9.895  28.476 1.00 36.57  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.411 -10.449 27.644 1.00 34.61  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.634 -12.953 27.012 0.41 37.64  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.704 -13.147 27.029 0.59 36.51  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.209 -13.298 26.892 0.41 39.64  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.318 -13.607 26.895 0.59 38.05  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.784 -14.503 27.736 0.41 44.30  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 14.002 -14.811 27.793 0.59 40.71  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.712 -14.478 28.334 0.41 46.00  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.041 -14.741 28.559 0.59 41.34  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.821 -13.513 25.415 0.41 41.85  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 13.996 -13.929 25.421 0.59 40.11  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.641 -12.238 24.609 0.41 54.80  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.537 -14.255 25.154 0.59 55.31  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.074 -11.265 25.151 0.41 58.37  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.669 -13.412 25.478 0.59 59.23  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 14.059 -12.217 23.431 0.41 59.65  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.263 -15.344 24.606 0.59 59.85  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.633 -15.538 27.797 0.41 39.64  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.804 -15.902 27.726 0.59 35.78  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.381 -16.772 28.548 0.41 39.82  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.521 -17.077 28.567 0.59 36.06  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.552 -16.562 30.025 0.41 42.76  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.718 -16.791 30.062 0.59 40.68  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.716 -17.037 30.796 0.41 43.29  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 14.033 -17.413 30.873 0.59 40.90  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.264 -17.868 28.008 0.41 48.18  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.272 -18.344 28.114 0.59 35.57  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 15.054 -17.841 26.616 0.41 48.48  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.640 -19.460 28.742 0.59 37.09  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.908 -19.237 28.556 0.41 48.06  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.749 -18.337 28.491 0.59 26.75  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.634 -15.857 30.425 1.00 38.02  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.891 -15.501 31.833 1.00 38.27  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.687 -14.777 32.374 1.00 44.96  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.208 -15.124 33.461 1.00 45.12  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.147 -14.650 31.956 1.00 37.29  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.679 -15.584 31.761 1.00 39.51  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.149 -13.822 31.573 1.00 42.81  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.947 -13.056 31.903 1.00 44.90  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.751 -13.993 32.154 1.00 50.00  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.027 -13.818 33.140 1.00 50.18  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.611 -12.074 30.776 1.00 46.86  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.417 -10.796 30.829 1.00 61.78  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.584 -9.593  30.424 1.00 76.65  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 12.998 -9.052  29.127 1.00 85.02  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.921 -8.106  28.962 1.00 93.16  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.548 -7.588  30.013 1.00 72.35  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.226 -7.674  27.746 1.00 80.11  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.568 -14.994 31.272 1.00 46.66  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.475 -15.968 31.374 1.00 48.05  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.628 -16.870 32.595 1.00 51.57  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.641  -17.113 33.279 1.00 51.61  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.356 -16.805 30.088 1.00 50.05  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.848  -16.009 28.889 1.00 67.69  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.526  -16.913 27.700 1.00 79.02  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.563  -16.194 26.367 1.00 88.46  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.499  -15.160 26.234 1.00 97.25  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.860 -17.365 32.868 1.00 47.38  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.133 -18.228 34.024 1.00 48.27  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.938 -17.469 35.343 1.00 53.49  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.406 -18.043 36.300 1.00 53.73  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.531 -18.850 33.926 1.00 48.69  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.647 -20.154 33.154 1.00 50.67  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.121 -20.276 31.869 1.00 54.13  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.356 -21.230 33.678 1.00 53.65  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.246 -21.472 31.150 1.00 54.50  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.492 -22.424 32.952 1.00 55.62  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.936 -22.536 31.696 1.00 53.05  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.306 -16.168 35.375 1.00 49.57  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.105 -15.316 36.561 1.00 50.84  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.606 -15.066 36.803 1.00 57.76  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.142 -15.175 37.948 1.00 58.77  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.956 -14.016 36.488 1.00 52.71  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.448 -14.354 36.669 1.00 50.97  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.507 -12.958 37.535 1.00 55.27  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.411 -13.317 36.112 1.00 56.48  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.850  -14.774 35.720 1.00 55.86  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.401  -14.520 35.774 1.00 58.59  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.619  -15.746 36.300 1.00 64.29  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.646  -15.574 37.031 1.00 65.68  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.877  -14.079 34.398 1.00 61.60  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.509  -13.403 34.442 1.00 79.72  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.887  -13.327 33.055 1.00 93.37  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.451  -12.863 33.094 1.00 108.15 ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.811  -12.950 31.755 1.00 118.05 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.069  -16.968 35.960 1.00 59.93  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.449  -18.216 36.416 1.00 61.23  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.623  -18.437 37.931 1.00 67.35  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.771  -19.070 38.545 1.00 68.16  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.030  -19.396 35.645 1.00 60.12  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.724  -17.928 38.522 1.00 65.40  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 9.027  -18.075 39.952 1.00 68.09  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.348  -17.032 40.865 1.00 76.19  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.284  -17.252 42.078 1.00 78.58  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.537 -18.087 40.186 1.00 71.29  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 11.071 -19.389 40.005 1.00 81.97  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.830  -15.917 40.296 1.00 72.82  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.160  -14.868 41.075 1.00 99.04  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.713  -15.237 41.432 1.00 141.55 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.466  -16.259 42.071 1.00 108.94 ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.250  -13.495 40.375 1.00 99.60  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.257  -13.274 39.240 1.00 110.03 ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.441  -12.035 38.380 1.00 130.85 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.541  -11.435 38.403 1.00 124.46 ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.479  -11.674 37.664 1.00 124.75 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.264 -35.145 5.857  1.00 32.52  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.315 -33.995 6.319  1.00 33.36  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.475 -36.352 6.748  1.00 32.35  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.997 -35.401 4.582  0.78 31.28  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 21.038 -35.414 4.571  0.22 31.06  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.777 -34.347 3.604  0.78 30.95  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.775 -34.371 3.581  0.22 30.47  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.286 -34.195 3.319  0.78 34.80  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.272 -34.192 3.394  0.22 34.06  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.554 -35.191 3.290  0.78 34.85  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.523 -35.171 3.470  0.22 33.64  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.554 -34.650 2.311  0.78 29.47  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.475 -34.656 2.229  0.22 28.97  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.049 -34.633 2.503  0.78 29.89  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.814 -35.695 1.368  0.22 29.75  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.830 -35.652 2.969  0.78 32.69  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.113 -37.024 1.314  0.22 32.76  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.929 -33.525 2.275  0.78 29.15  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.756 -35.483 0.421  0.22 29.54  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.141 -35.235 3.067  0.78 31.55  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.281 -37.662 0.425  0.22 32.21  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.242 -33.963 2.569  0.78 32.48  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.445 -36.739 -0.147 0.22 33.58  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.740 -32.204 1.837  0.78 29.62  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 19.018 -34.356 0.016  0.22 30.54  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.357 -33.125 2.441  0.78 31.37  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.437 -36.898 -1.107 0.22 32.81  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.851 -31.397 1.655  0.78 30.22  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 18.012 -34.518 -0.925 0.22 32.16  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.136 -31.851 1.974  0.78 31.09  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.737 -35.774 -1.483 0.22 32.76  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.835 -32.950 3.133  1.00 30.22  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.421 -32.618 2.894  1.00 29.69  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.294 -31.567 1.788  1.00 32.04  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.271 -30.887 1.445  1.00 29.78  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.703 -32.096 4.189  1.00 32.17  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.672 -33.149 5.299  1.00 32.13  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.322 -30.780 4.696  1.00 31.41  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.060 -31.376 1.311  1.00 29.49  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.694 -30.289 0.413  1.00 30.22  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.308 -29.154 1.395  1.00 33.88  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.312 -29.298 2.110  1.00 32.84  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.491 -30.663 -0.493 1.00 32.99  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.764 -31.940 -1.354 1.00 32.69  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.059 -29.447 -1.352 1.00 34.67  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.030 -31.872 -2.357 1.00 33.58  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.095 -28.062 1.480  1.00 33.03  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.768 -26.987 2.438  1.00 33.82  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.507 -26.213 2.052  1.00 38.32  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.240 -26.043 0.859  1.00 36.50  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 17.019 -26.095 2.411  1.00 35.55  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.586 -26.291 1.032  1.00 38.99  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.297 -27.733 0.678  1.00 34.50  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.858 -25.583 3.045  1.00 36.45  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.336 -10.299 11.824 1.00 32.51  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.327 -9.344  12.183 1.00 34.64  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.986 -10.722 18.072 1.00 32.59  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.491 -9.424  18.131 1.00 34.61  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.545 -10.033 16.369 1.00 30.03  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.400 -10.193 14.010 1.00 31.01  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.967 -8.428  17.280 1.00 32.20  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.988 -8.749  16.391 1.00 30.51  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 25.010 -11.033 17.185 1.00 30.34  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.443 -10.602 13.171 1.00 30.86  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.269 -10.563 19.688 1.00 38.37  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.232 -11.554 19.068 1.00 35.41  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.281 -9.663  11.310 1.00 34.57  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.317 -9.564  13.503 1.00 33.88  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.487 -9.355  19.103 1.00 35.70  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.392 -10.498 15.339 1.00 28.86  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.419 -10.799 20.545 1.00 38.79  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.862 -11.388 13.760 0.99 30.77  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.341 -15.199 22.576 1.00 39.77  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.599 -35.420 -1.242 0.78 54.27  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.326 -35.195 -0.590 0.78 55.68  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.730 -34.508 -0.226 0.78 53.76  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 18.029 -37.056 -0.755 0.78 53.83  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 35.768 -25.691 25.605 1.00 44.80  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 38.431 -14.867 15.432 1.00 39.49  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 25.919 -3.415  26.366 1.00 38.77  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 43.719 -6.564  31.969 1.00 53.92  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 41.349 -21.649 25.157 1.00 52.04  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 29.961 -32.132 9.581  1.00 51.11  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 22.744 -5.335  19.861 1.00 63.78  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 37.972 2.460   19.641 1.00 48.05  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 20.823 -5.815  25.995 1.00 48.97  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 37.684 -20.415 26.985 1.00 40.65  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 26.791 -32.019 16.112 1.00 53.44  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 33.322 -20.810 29.620 1.00 57.09  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 19.874 -9.509  36.972 1.00 45.93  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 18.005 -29.392 7.670  1.00 41.63  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 22.963 -28.273 12.645 1.00 30.73  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 27.281 -10.186 35.837 1.00 45.05  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 45.061 -11.224 18.721 1.00 65.73  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 41.382 -16.930 15.188 1.00 41.64  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 44.622 -0.915  17.905 1.00 62.94  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 16.558 -27.525 -3.323 1.00 66.29  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 31.816 -0.827  15.824 1.00 47.09  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 27.344 -35.392 11.839 1.00 64.52  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 23.565 -5.708  32.949 1.00 43.29  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 30.299 1.514   33.932 1.00 67.18  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 32.463 -24.730 32.222 1.00 70.11  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 34.946 -18.870 13.856 0.50 35.70  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 22.644 -27.651 17.705 1.00 57.63  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 13.415 -14.285 21.792 1.00 73.98  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 28.146 -8.699  39.937 1.00 54.82  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 19.024 -24.882 33.003 1.00 44.14  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 14.254 -16.758 23.404 1.00 47.81  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 20.513 -13.363 20.422 1.00 57.11  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 26.095 -22.519 29.899 1.00 31.49  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 29.627 -2.104  13.749 1.00 70.86  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 32.402 -8.921  39.715 1.00 65.67  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 26.914 -16.543 38.628 1.00 55.85  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 41.670 -12.865 14.163 1.00 99.57  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 26.034 -21.885 38.704 1.00 43.01  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 25.800 -2.779  19.946 1.00 66.55  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 27.247 -2.442  16.115 1.00 69.17  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 21.504 -27.059 14.519 0.50 45.39  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 30.327 -0.460  36.782 1.00 63.34  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 7.094  -16.820 32.289 1.00 64.52  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 43.967 -4.367  25.774 1.00 56.11  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 26.444 -7.763  36.802 1.00 63.15  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 24.108 -15.770 21.150 1.00 36.08  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 41.325 -6.974  35.893 1.00 49.65  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 15.394 -9.817  24.813 1.00 57.43  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 12.621 -20.519 42.465 1.00 69.23  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 23.407 -17.171 44.293 1.00 71.00  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 34.160 -7.828  35.560 1.00 41.50  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 27.310 -28.123 18.673 1.00 36.68  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 44.497 -12.423 41.147 1.00 59.31  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 28.194 -23.745 31.673 1.00 48.45  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 21.929 -24.950 18.311 1.00 29.10  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 29.384 -27.358 20.624 1.00 32.63  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 36.832 -5.544  12.123 1.00 45.73  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 20.852 -7.185  19.701 1.00 63.07  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 29.121 -31.202 7.292  1.00 37.06  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 39.156 -18.901 33.356 1.00 54.83  ? 360 HOH A O   1 
HETATM 1263 O  O   . HOH F 6 .   ? 28.565 -24.285 34.354 1.00 59.48  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 24.865 -26.805 19.013 1.00 42.10  ? 362 HOH A O   1 
HETATM 1265 O  O   . HOH F 6 .   ? 21.463 -29.976 14.187 1.00 82.75  ? 363 HOH A O   1 
HETATM 1266 O  O   . HOH F 6 .   ? 46.091 -14.237 21.515 1.00 67.37  ? 364 HOH A O   1 
HETATM 1267 O  O   A HOH F 6 .   ? 19.055 -22.948 4.321  0.60 43.18  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 42.481 -10.355 15.401 1.00 55.73  ? 366 HOH A O   1 
HETATM 1269 O  O   . HOH F 6 .   ? 43.534 -10.628 35.335 1.00 66.36  ? 367 HOH A O   1 
HETATM 1270 O  O   . HOH F 6 .   ? 46.903 -21.812 17.841 1.00 48.25  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 22.340 -34.138 26.191 1.00 79.95  ? 369 HOH A O   1 
HETATM 1272 O  O   . HOH F 6 .   ? 46.268 -15.915 27.574 1.00 69.73  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 4.255  -20.165 37.892 1.00 74.57  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 21.409 -31.268 29.982 1.00 72.42  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 30.726 -28.824 22.686 1.00 45.91  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 26.081 -19.166 41.723 1.00 75.03  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 37.456 -6.446  34.296 1.00 45.23  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 10.878 -11.300 34.433 1.00 58.36  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 22.724 -34.009 8.818  1.00 39.96  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 46.321 -18.959 19.688 1.00 60.52  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 31.894 -31.846 14.649 1.00 49.40  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 26.281 -7.905  9.052  1.00 53.98  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 42.219 -6.036  11.921 1.00 68.46  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 46.417 -29.748 21.306 1.00 78.57  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 27.712 -23.047 13.856 0.50 32.14  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 47.279 -25.266 21.616 1.00 64.73  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 20.113 -15.717 40.841 1.00 39.44  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 17.971 -24.306 39.760 1.00 45.96  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 25.850 -4.513  17.882 1.00 56.49  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 18.055 -34.613 8.348  1.00 36.80  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 44.848 -8.669  17.808 1.00 69.51  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 40.341 -19.652 28.984 1.00 42.48  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 33.053 -29.665 21.566 1.00 50.74  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 21.087 -23.006 42.070 1.00 57.09  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 37.080 -2.422  11.595 1.00 64.56  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 40.002 -5.571  33.852 1.00 49.54  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 45.335 -12.695 23.605 1.00 51.87  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 46.098 -8.839  44.082 1.00 60.82  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 34.861 -33.243 21.923 1.00 69.41  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 46.991 -20.145 22.014 1.00 67.42  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 11.308 -14.809 40.688 1.00 100.03 ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 37.994 -16.317 12.719 1.00 62.79  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 22.872 -14.776 40.372 1.00 41.05  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 33.841 -33.093 12.309 1.00 49.12  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 41.231 -17.103 35.197 1.00 48.88  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 23.678 -15.742 17.831 1.00 46.71  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 41.925 -8.168  13.746 1.00 73.77  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 19.674 -27.365 10.096 1.00 64.84  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 44.583 -16.408 29.663 1.00 54.21  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 27.150 -1.577  21.983 1.00 58.38  ? 408 HOH A O   1 
HETATM 1311 O  O   B HOH F 6 .   ? 37.333 -11.933 40.078 0.50 42.28  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 22.449 -10.166 14.396 1.00 47.17  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 32.077 -15.583 39.857 1.00 43.03  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 35.478 2.103   13.601 1.00 64.82  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 30.312 -10.391 40.558 1.00 50.87  ? 413 HOH A O   1 
HETATM 1316 O  O   . HOH F 6 .   ? 28.776 -16.018 41.349 1.00 74.05  ? 414 HOH A O   1 
HETATM 1317 O  O   . HOH F 6 .   ? 45.536 -10.461 30.475 1.00 61.21  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 44.775 -8.081  15.143 1.00 80.43  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 29.676 -0.762  22.203 1.00 66.06  ? 417 HOH A O   1 
HETATM 1320 O  O   . HOH F 6 .   ? 23.442 -30.520 19.229 1.00 71.64  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 35.275 -29.840 23.589 1.00 56.79  ? 419 HOH A O   1 
HETATM 1322 O  O   . HOH F 6 .   ? 33.952 -17.564 39.545 1.00 74.99  ? 420 HOH A O   1 
HETATM 1323 O  O   . HOH F 6 .   ? 10.269 -11.758 40.000 1.00 66.40  ? 421 HOH A O   1 
HETATM 1324 O  O   . HOH F 6 .   ? 33.539 -0.253  19.927 1.00 53.24  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 26.047 -29.345 22.587 1.00 66.02  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 44.379 -25.882 26.654 1.00 66.00  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 45.825 -5.550  23.738 1.00 54.29  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 46.057 -17.185 17.173 1.00 69.89  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 37.621 -27.225 28.406 1.00 71.85  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 27.446 -25.630 28.267 1.00 63.25  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 28.316 -2.551  11.297 1.00 72.99  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 47.900 -23.223 19.939 1.00 70.38  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 42.888 -18.321 30.728 1.00 54.05  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 32.422 -3.949  41.224 1.00 64.26  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 32.075 0.207   13.310 1.00 67.24  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 30.019 -22.695 36.683 1.00 80.07  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 25.915 -15.899 41.081 1.00 59.48  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 31.810 -26.241 27.024 1.00 55.53  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 28.266 -29.238 26.828 1.00 89.66  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 35.164 -4.066  10.598 1.00 51.34  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 20.032 -35.333 10.211 1.00 46.35  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 37.113 -24.356 27.573 1.00 61.51  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 27.348 -34.628 18.062 1.00 77.51  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 23.067 -2.767  26.203 1.00 69.60  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 47.171 -13.022 28.606 1.00 70.84  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 24.369 -21.557 41.071 1.00 64.10  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 19.381 -31.678 13.864 1.00 75.99  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 47.396 -28.671 17.854 1.00 76.17  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 46.646 -14.632 17.971 1.00 72.26  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 31.073 -34.424 14.856 1.00 69.75  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 12.061 -18.649 22.510 1.00 63.66  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 33.815 -10.895 41.568 0.50 59.72  ? 450 HOH A O   1 
HETATM 1353 O  O   . HOH F 6 .   ? 47.135 -11.861 25.478 1.00 75.51  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 34.516 -18.952 36.193 1.00 68.47  ? 452 HOH A O   1 
HETATM 1355 O  O   . HOH F 6 .   ? 32.348 -1.036  22.236 1.00 64.43  ? 453 HOH A O   1 
HETATM 1356 O  O   . HOH F 6 .   ? 19.276 -7.547  35.199 1.00 63.23  ? 454 HOH A O   1 
HETATM 1357 O  O   . HOH F 6 .   ? 43.166 -3.099  33.744 1.00 64.57  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 13.739 -16.144 39.966 1.00 83.80  ? 456 HOH A O   1 
HETATM 1359 O  O   . HOH F 6 .   ? 17.092 -28.052 9.821  1.00 64.47  ? 457 HOH A O   1 
HETATM 1360 O  O   A HOH F 6 .   ? 12.050 -20.690 27.780 0.78 54.34  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 25.405 -5.730  35.294 1.00 58.69  ? 459 HOH A O   1 
HETATM 1362 O  O   . HOH F 6 .   ? 15.950 -15.367 41.358 1.00 77.24  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 44.319 -13.458 13.856 0.50 96.80  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 17.461 -8.091  24.831 1.00 73.62  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 33.815 -13.857 41.567 0.50 46.72  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 32.449 -20.576 37.000 1.00 78.95  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 32.083 -23.827 34.887 1.00 76.11  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 19.039 -28.054 13.856 0.50 75.28  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 28.181 -29.875 24.182 1.00 75.38  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 21.168 -5.595  34.685 1.00 65.29  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 45.574 -12.784 16.191 1.00 80.87  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 34.949 -23.667 32.632 1.00 65.75  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 23.210 -4.575  17.053 1.00 82.71  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 32.952 -0.672  42.885 1.00 60.76  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 16.747 -6.618  34.676 1.00 89.63  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.331 -24.312 0.006  1.00 56.05  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 14.986 -25.876 -1.834 1.00 51.07  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 11.774 -23.566 2.919  1.00 59.77  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 21.092 -38.362 4.019  1.00 53.14  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 17.756 -36.435 6.116  1.00 46.13  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 21.041 -39.622 -2.045 1.00 71.17  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 18.686 -40.718 0.721  1.00 72.98  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.742 -24.794 5.548  1.00 63.73  ? 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   ? 0.9161 1.1027 0.8044 0.0271  -0.1332 -0.0209 6   ASP A N   
2    C CA  . ASP A 5   ? 0.9100 1.0906 0.7809 0.0097  -0.1235 -0.0236 6   ASP A CA  
3    C C   . ASP A 5   ? 0.8883 1.1003 0.7846 -0.0025 -0.1184 -0.0407 6   ASP A C   
4    O O   . ASP A 5   ? 0.8783 1.1180 0.8039 0.0019  -0.1232 -0.0505 6   ASP A O   
5    C CB  . ASP A 5   ? 0.9312 1.0815 0.7921 0.0007  -0.1055 -0.0163 6   ASP A CB  
6    C CG  . ASP A 5   ? 1.1173 1.2468 0.9432 -0.0101 -0.1004 -0.0117 6   ASP A CG  
7    O OD1 . ASP A 5   ? 1.1230 1.2656 0.9465 -0.0217 -0.0976 -0.0211 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.2184 1.3183 1.0191 -0.0083 -0.0978 0.0002  6   ASP A OD2 
9    N N   . SER A 6   ? 0.7845 0.9916 0.6694 -0.0183 -0.1079 -0.0454 7   SER A N   
10   C CA  . SER A 6   ? 0.7380 0.9672 0.6416 -0.0318 -0.1007 -0.0611 7   SER A CA  
11   C C   . SER A 6   ? 0.6875 0.9020 0.6029 -0.0426 -0.0809 -0.0635 7   SER A C   
12   O O   . SER A 6   ? 0.6791 0.8972 0.5971 -0.0557 -0.0718 -0.0734 7   SER A O   
13   C CB  . SER A 6   ? 0.8173 1.0527 0.6985 -0.0406 -0.1055 -0.0664 7   SER A CB  
14   O OG  . SER A 6   ? 0.9972 1.2046 0.8487 -0.0468 -0.0976 -0.0584 7   SER A OG  
15   N N   . CYS A 7   ? 0.5646 0.7621 0.4866 -0.0364 -0.0751 -0.0549 8   CYS A N   
16   C CA  . CYS A 7   ? 0.5206 0.7033 0.4526 -0.0436 -0.0592 -0.0558 8   CYS A CA  
17   C C   . CYS A 7   ? 0.4882 0.6861 0.4454 -0.0511 -0.0526 -0.0682 8   CYS A C   
18   O O   . CYS A 7   ? 0.4832 0.7042 0.4563 -0.0489 -0.0592 -0.0752 8   CYS A O   
19   C CB  . CYS A 7   ? 0.5359 0.7000 0.4689 -0.0346 -0.0569 -0.0444 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.6188 0.7554 0.5194 -0.0310 -0.0579 -0.0303 8   CYS A SG  
21   N N   . ILE A 8   ? 0.3693 0.5533 0.3297 -0.0598 -0.0395 -0.0714 9   ILE A N   
22   C CA  . ILE A 8   ? 0.3276 0.5144 0.3064 -0.0667 -0.0311 -0.0800 9   ILE A CA  
23   C C   . ILE A 8   ? 0.3543 0.5226 0.3380 -0.0611 -0.0256 -0.0714 9   ILE A C   
24   O O   . ILE A 8   ? 0.3452 0.4980 0.3179 -0.0555 -0.0256 -0.0617 9   ILE A O   
25   C CB  . ILE A 8   ? 0.3677 0.5501 0.3449 -0.0798 -0.0219 -0.0906 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.3799 0.5397 0.3438 -0.0809 -0.0149 -0.0864 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.3779 0.5832 0.3532 -0.0866 -0.0277 -0.1013 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.4102 0.5611 0.3739 -0.0914 -0.0051 -0.0969 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.2932 0.4618 0.2914 -0.0639 -0.0200 -0.0755 10  GLN A N   
30   N N   B GLN A 9   ? 0.2921 0.4627 0.2910 -0.0633 -0.0209 -0.0755 10  GLN A N   
31   C CA  A GLN A 9   ? 0.2809 0.4323 0.2819 -0.0589 -0.0155 -0.0677 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.2782 0.4327 0.2812 -0.0587 -0.0161 -0.0684 10  GLN A CA  
33   C C   A GLN A 9   ? 0.3306 0.4662 0.3343 -0.0671 -0.0049 -0.0719 10  GLN A C   
34   C C   B GLN A 9   ? 0.3181 0.4557 0.3222 -0.0673 -0.0054 -0.0725 10  GLN A C   
35   O O   A GLN A 9   ? 0.3208 0.4638 0.3309 -0.0761 -0.0010 -0.0816 10  GLN A O   
36   O O   B GLN A 9   ? 0.3093 0.4526 0.3178 -0.0770 -0.0011 -0.0824 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2899 0.4548 0.3031 -0.0511 -0.0208 -0.0660 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2853 0.4551 0.3027 -0.0529 -0.0202 -0.0690 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2822 0.4310 0.2977 -0.0460 -0.0165 -0.0585 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.4010 0.5560 0.4236 -0.0514 -0.0133 -0.0648 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.6346 0.7993 0.6658 -0.0412 -0.0190 -0.0614 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.5106 0.6652 0.5356 -0.0393 -0.0186 -0.0567 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.5234 0.7021 0.5676 -0.0484 -0.0149 -0.0717 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.3759 0.5398 0.3984 -0.0303 -0.0282 -0.0531 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.6833 0.8456 0.7136 -0.0294 -0.0248 -0.0535 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.3792 0.5205 0.4069 -0.0387 -0.0124 -0.0535 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.3126 0.4258 0.3103 -0.0641 -0.0008 -0.0651 11  PHE A N   
48   N N   B PHE A 10  ? 0.2829 0.3989 0.2819 -0.0636 -0.0016 -0.0651 11  PHE A N   
49   C CA  A PHE A 10  ? 0.3120 0.4056 0.3085 -0.0694 0.0071  -0.0674 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2851 0.3807 0.2822 -0.0687 0.0063  -0.0669 11  PHE A CA  
51   C C   A PHE A 10  ? 0.3339 0.4235 0.3356 -0.0677 0.0090  -0.0640 11  PHE A C   
52   C C   B PHE A 10  ? 0.3312 0.4228 0.3337 -0.0672 0.0084  -0.0638 11  PHE A C   
53   O O   A PHE A 10  ? 0.3168 0.3993 0.3173 -0.0600 0.0071  -0.0558 11  PHE A O   
54   O O   B PHE A 10  ? 0.3201 0.4067 0.3221 -0.0593 0.0061  -0.0557 11  PHE A O   
55   C CB  A PHE A 10  ? 0.3380 0.4117 0.3266 -0.0663 0.0091  -0.0639 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.3080 0.3856 0.2972 -0.0645 0.0076  -0.0622 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.3635 0.4155 0.3483 -0.0706 0.0151  -0.0672 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.3350 0.4123 0.3194 -0.0691 0.0093  -0.0688 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.4169 0.4657 0.3994 -0.0796 0.0195  -0.0764 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.3761 0.4694 0.3570 -0.0700 0.0054  -0.0707 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.3962 0.4289 0.3778 -0.0656 0.0158  -0.0613 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.3765 0.4359 0.3581 -0.0722 0.0146  -0.0736 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.4406 0.4636 0.4158 -0.0830 0.0247  -0.0787 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3935 0.4869 0.3692 -0.0753 0.0080  -0.0780 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.4336 0.4423 0.4078 -0.0682 0.0196  -0.0633 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.4200 0.4792 0.3984 -0.0762 0.0170  -0.0812 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.4204 0.4226 0.3905 -0.0766 0.0242  -0.0715 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3918 0.4688 0.3677 -0.0784 0.0144  -0.0838 11  PHE A CZ  
69   N N   . THR A 11  ? 0.2978 0.3931 0.3051 -0.0761 0.0136  -0.0715 12  THR A N   
70   C CA  . THR A 11  ? 0.3036 0.3979 0.3162 -0.0772 0.0174  -0.0710 12  THR A CA  
71   C C   . THR A 11  ? 0.3556 0.4237 0.3585 -0.0733 0.0200  -0.0623 12  THR A C   
72   O O   . THR A 11  ? 0.3318 0.4024 0.3387 -0.0678 0.0189  -0.0577 12  THR A O   
73   C CB  . THR A 11  ? 0.4059 0.5045 0.4218 -0.0911 0.0254  -0.0824 12  THR A CB  
74   O OG1 . THR A 11  ? 0.3854 0.5134 0.4130 -0.0940 0.0216  -0.0916 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.4557 0.5547 0.4767 -0.0948 0.0315  -0.0842 12  THR A CG2 
76   N N   A ARG A 12  ? 0.3345 0.3785 0.3252 -0.0753 0.0225  -0.0608 13  ARG A N   
77   N N   B ARG A 12  ? 0.3373 0.3813 0.3280 -0.0753 0.0226  -0.0608 13  ARG A N   
78   C CA  A ARG A 12  ? 0.3463 0.3655 0.3267 -0.0714 0.0233  -0.0537 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.3504 0.3693 0.3307 -0.0715 0.0233  -0.0537 13  ARG A CA  
80   C C   A ARG A 12  ? 0.3619 0.3792 0.3426 -0.0603 0.0172  -0.0462 13  ARG A C   
81   C C   B ARG A 12  ? 0.3640 0.3813 0.3446 -0.0603 0.0172  -0.0462 13  ARG A C   
82   O O   A ARG A 12  ? 0.3491 0.3487 0.3226 -0.0565 0.0165  -0.0413 13  ARG A O   
83   O O   B ARG A 12  ? 0.3516 0.3515 0.3252 -0.0565 0.0165  -0.0412 13  ARG A O   
84   C CB  A ARG A 12  ? 0.3956 0.3873 0.3618 -0.0774 0.0277  -0.0559 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.4048 0.3968 0.3712 -0.0771 0.0274  -0.0560 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.4980 0.4832 0.4586 -0.0912 0.0364  -0.0628 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.5431 0.5209 0.5001 -0.0887 0.0356  -0.0597 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.6535 0.6320 0.6095 -0.0947 0.0409  -0.0603 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.6310 0.5944 0.5789 -0.0991 0.0414  -0.0670 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.7498 0.6963 0.6873 -0.0909 0.0397  -0.0524 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.6689 0.6101 0.6072 -0.0928 0.0379  -0.0648 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.8461 0.7851 0.7776 -0.0900 0.0407  -0.0477 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.8051 0.7504 0.7466 -0.0942 0.0379  -0.0711 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.5635 0.5248 0.5079 -0.0921 0.0438  -0.0503 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.7086 0.6337 0.6431 -0.0873 0.0351  -0.0702 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.7244 0.6341 0.6372 -0.0863 0.0380  -0.0409 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.4902 0.4606 0.4423 -0.1021 0.0404  -0.0792 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.3046 0.3392 0.2916 -0.0560 0.0129  -0.0458 14  HIS A N   
99   C CA  . HIS A 13  ? 0.3024 0.3353 0.2886 -0.0482 0.0092  -0.0403 14  HIS A CA  
100  C C   . HIS A 13  ? 0.3366 0.3643 0.3227 -0.0430 0.0082  -0.0336 14  HIS A C   
101  O O   . HIS A 13  ? 0.3305 0.3462 0.3131 -0.0395 0.0073  -0.0310 14  HIS A O   
102  C CB  . HIS A 13  ? 0.2953 0.3446 0.2834 -0.0466 0.0059  -0.0406 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.3191 0.3649 0.3043 -0.0417 0.0046  -0.0364 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.3264 0.3645 0.3106 -0.0416 0.0062  -0.0396 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.3239 0.3723 0.3074 -0.0374 0.0026  -0.0304 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.3210 0.3603 0.3043 -0.0387 0.0058  -0.0365 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.3197 0.3631 0.3008 -0.0367 0.0040  -0.0304 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.2927 0.3303 0.2836 -0.0421 0.0080  -0.0320 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2872 0.3195 0.2779 -0.0376 0.0078  -0.0266 15  ALA A CA  
110  C C   . ALA A 14  ? 0.3286 0.3427 0.3123 -0.0399 0.0106  -0.0258 15  ALA A C   
111  O O   . ALA A 14  ? 0.3217 0.3271 0.3020 -0.0361 0.0092  -0.0218 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2956 0.3417 0.2943 -0.0355 0.0075  -0.0271 15  ALA A CB  
113  N N   A SER A 15  ? 0.3087 0.3161 0.2884 -0.0468 0.0146  -0.0298 16  SER A N   
114  N N   B SER A 15  ? 0.3081 0.3154 0.2877 -0.0468 0.0146  -0.0298 16  SER A N   
115  N N   C SER A 15  ? 0.3050 0.3123 0.2847 -0.0468 0.0146  -0.0298 16  SER A N   
116  C CA  A SER A 15  ? 0.3232 0.3088 0.2905 -0.0500 0.0170  -0.0285 16  SER A CA  
117  C CA  B SER A 15  ? 0.3229 0.3083 0.2900 -0.0500 0.0170  -0.0285 16  SER A CA  
118  C CA  C SER A 15  ? 0.3187 0.3040 0.2858 -0.0500 0.0170  -0.0284 16  SER A CA  
119  C C   A SER A 15  ? 0.3865 0.3563 0.3461 -0.0453 0.0124  -0.0262 16  SER A C   
120  C C   B SER A 15  ? 0.3878 0.3575 0.3473 -0.0453 0.0124  -0.0263 16  SER A C   
121  C C   C SER A 15  ? 0.3871 0.3567 0.3466 -0.0454 0.0124  -0.0263 16  SER A C   
122  O O   A SER A 15  ? 0.3701 0.3264 0.3220 -0.0421 0.0099  -0.0226 16  SER A O   
123  O O   B SER A 15  ? 0.3750 0.3310 0.3267 -0.0422 0.0100  -0.0226 16  SER A O   
124  O O   C SER A 15  ? 0.3775 0.3330 0.3288 -0.0423 0.0100  -0.0227 16  SER A O   
125  C CB  A SER A 15  ? 0.3801 0.3596 0.3417 -0.0604 0.0235  -0.0338 16  SER A CB  
126  C CB  B SER A 15  ? 0.3789 0.3582 0.3404 -0.0604 0.0235  -0.0339 16  SER A CB  
127  C CB  C SER A 15  ? 0.3695 0.3487 0.3309 -0.0604 0.0236  -0.0337 16  SER A CB  
128  O OG  A SER A 15  ? 0.4767 0.4308 0.4210 -0.0643 0.0262  -0.0315 16  SER A OG  
129  O OG  B SER A 15  ? 0.4499 0.4483 0.4225 -0.0645 0.0277  -0.0384 16  SER A OG  
130  O OG  C SER A 15  ? 0.4353 0.4126 0.3954 -0.0639 0.0240  -0.0379 16  SER A OG  
131  N N   . ASP A 16  ? 0.3573 0.3309 0.3204 -0.0444 0.0108  -0.0295 17  ASP A N   
132  C CA  . ASP A 16  ? 0.3791 0.3418 0.3394 -0.0386 0.0064  -0.0300 17  ASP A CA  
133  C C   . ASP A 16  ? 0.3725 0.3435 0.3395 -0.0316 0.0024  -0.0273 17  ASP A C   
134  O O   . ASP A 16  ? 0.3698 0.3307 0.3340 -0.0263 -0.0020 -0.0268 17  ASP A O   
135  C CB  . ASP A 16  ? 0.4038 0.3723 0.3685 -0.0400 0.0073  -0.0358 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.5574 0.5119 0.5133 -0.0473 0.0114  -0.0399 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.5695 0.5073 0.5139 -0.0518 0.0140  -0.0378 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.5605 0.5197 0.5195 -0.0499 0.0129  -0.0457 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.3077 0.2962 0.2827 -0.0317 0.0035  -0.0261 18  VAL A N   
140  C CA  . VAL A 17  ? 0.3017 0.2964 0.2811 -0.0276 0.0017  -0.0240 18  VAL A CA  
141  C C   . VAL A 17  ? 0.3270 0.3116 0.3015 -0.0261 0.0004  -0.0204 18  VAL A C   
142  O O   . VAL A 17  ? 0.3116 0.2934 0.2870 -0.0224 -0.0029 -0.0211 18  VAL A O   
143  C CB  . VAL A 17  ? 0.3185 0.3271 0.3015 -0.0285 0.0035  -0.0220 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.3134 0.3226 0.2970 -0.0264 0.0035  -0.0189 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.3118 0.3298 0.2967 -0.0303 0.0040  -0.0257 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.3123 0.2934 0.2826 -0.0292 0.0032  -0.0181 19  LEU A N   
147  C CA  . LEU A 18  ? 0.3293 0.3009 0.2932 -0.0292 0.0032  -0.0153 19  LEU A CA  
148  C C   . LEU A 18  ? 0.3763 0.3301 0.3291 -0.0277 -0.0011 -0.0153 19  LEU A C   
149  O O   . LEU A 18  ? 0.3480 0.2974 0.2978 -0.0247 -0.0049 -0.0142 19  LEU A O   
150  C CB  . LEU A 18  ? 0.3402 0.3129 0.3028 -0.0336 0.0084  -0.0148 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.3800 0.3464 0.3376 -0.0340 0.0100  -0.0128 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.3654 0.3399 0.3302 -0.0298 0.0091  -0.0111 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.4321 0.3999 0.3894 -0.0393 0.0166  -0.0148 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.3628 0.3054 0.3086 -0.0296 -0.0011 -0.0167 20  LEU A N   
155  C CA  . LEU A 19  ? 0.3885 0.3093 0.3204 -0.0266 -0.0064 -0.0161 20  LEU A CA  
156  C C   . LEU A 19  ? 0.3850 0.3113 0.3255 -0.0173 -0.0144 -0.0184 20  LEU A C   
157  O O   . LEU A 19  ? 0.3707 0.2869 0.3039 -0.0124 -0.0212 -0.0173 20  LEU A O   
158  C CB  . LEU A 19  ? 0.4230 0.3304 0.3467 -0.0304 -0.0039 -0.0181 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.5440 0.4223 0.4493 -0.0265 -0.0097 -0.0167 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.5854 0.4410 0.4676 -0.0319 -0.0083 -0.0118 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5994 0.4659 0.4999 -0.0295 -0.0067 -0.0200 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.3336 0.2775 0.2897 -0.0155 -0.0134 -0.0227 21  ASN A N   
163  C CA  . ASN A 20  ? 0.3264 0.2802 0.2940 -0.0084 -0.0188 -0.0275 21  ASN A CA  
164  C C   . ASN A 20  ? 0.3463 0.3107 0.3194 -0.0079 -0.0200 -0.0270 21  ASN A C   
165  O O   . ASN A 20  ? 0.3423 0.3094 0.3204 -0.0020 -0.0266 -0.0309 21  ASN A O   
166  C CB  . ASN A 20  ? 0.3178 0.2866 0.2982 -0.0090 -0.0154 -0.0331 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.4866 0.4435 0.4632 -0.0069 -0.0165 -0.0364 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.4331 0.3694 0.3988 -0.0024 -0.0218 -0.0351 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.3656 0.3326 0.3487 -0.0104 -0.0115 -0.0405 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.3184 0.2889 0.2913 -0.0137 -0.0139 -0.0233 22  LEU A N   
171  C CA  . LEU A 21  ? 0.3103 0.2870 0.2859 -0.0146 -0.0136 -0.0229 22  LEU A CA  
172  C C   . LEU A 21  ? 0.3470 0.3100 0.3112 -0.0126 -0.0193 -0.0211 22  LEU A C   
173  O O   . LEU A 21  ? 0.3249 0.2928 0.2926 -0.0103 -0.0238 -0.0241 22  LEU A O   
174  C CB  . LEU A 21  ? 0.3034 0.2845 0.2787 -0.0198 -0.0064 -0.0189 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.3388 0.3320 0.3216 -0.0216 -0.0020 -0.0198 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.3377 0.3314 0.3177 -0.0239 0.0027  -0.0150 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.3641 0.3674 0.3549 -0.0219 -0.0017 -0.0249 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.3260 0.2717 0.2752 -0.0145 -0.0189 -0.0169 23  ASN A N   
179  C CA  . ASN A 22  ? 0.3499 0.2783 0.2825 -0.0134 -0.0244 -0.0145 23  ASN A CA  
180  C C   . ASN A 22  ? 0.4063 0.3282 0.3368 -0.0042 -0.0362 -0.0173 23  ASN A C   
181  O O   . ASN A 22  ? 0.4250 0.3428 0.3489 -0.0009 -0.0437 -0.0177 23  ASN A O   
182  C CB  . ASN A 22  ? 0.3683 0.2780 0.2829 -0.0196 -0.0195 -0.0102 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.4701 0.3626 0.3647 -0.0216 -0.0224 -0.0074 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.4351 0.3343 0.3319 -0.0212 -0.0243 -0.0084 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4874 0.3560 0.3601 -0.0250 -0.0220 -0.0043 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.3666 0.2886 0.3035 0.0007  -0.0384 -0.0202 24  ARG A N   
187  C CA  . ARG A 23  ? 0.3793 0.2972 0.3183 0.0119  -0.0502 -0.0245 24  ARG A CA  
188  C C   . ARG A 23  ? 0.4158 0.3590 0.3755 0.0161  -0.0545 -0.0322 24  ARG A C   
189  O O   . ARG A 23  ? 0.4223 0.3646 0.3818 0.0245  -0.0659 -0.0355 24  ARG A O   
190  C CB  . ARG A 23  ? 0.3812 0.2960 0.3258 0.0156  -0.0495 -0.0278 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.4764 0.3617 0.3982 0.0124  -0.0474 -0.0220 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.5390 0.4258 0.4687 0.0120  -0.0426 -0.0261 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.6240 0.4806 0.5314 0.0083  -0.0404 -0.0221 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.8863 0.7382 0.7948 0.0052  -0.0349 -0.0251 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.6798 0.5562 0.6101 0.0054  -0.0312 -0.0318 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.7585 0.5799 0.6443 0.0004  -0.0322 -0.0220 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.3625 0.3276 0.3389 0.0098  -0.0454 -0.0354 25  LEU A N   
198  C CA  . LEU A 24  ? 0.3323 0.3204 0.3266 0.0103  -0.0465 -0.0435 25  LEU A CA  
199  C C   . LEU A 24  ? 0.3904 0.3759 0.3764 0.0081  -0.0500 -0.0416 25  LEU A C   
200  O O   . LEU A 24  ? 0.3810 0.3773 0.3752 0.0131  -0.0586 -0.0487 25  LEU A O   
201  C CB  . LEU A 24  ? 0.3125 0.3171 0.3187 0.0019  -0.0347 -0.0455 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.3607 0.3721 0.3759 0.0022  -0.0303 -0.0492 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.3472 0.3715 0.3680 -0.0073 -0.0191 -0.0497 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.3830 0.4057 0.4141 0.0111  -0.0374 -0.0604 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.3556 0.3278 0.3259 0.0010  -0.0439 -0.0335 26  ARG A N   
206  C CA  . ARG A 25  ? 0.3756 0.3430 0.3356 -0.0018 -0.0463 -0.0321 26  ARG A CA  
207  C C   . ARG A 25  ? 0.4521 0.4064 0.3986 0.0064  -0.0607 -0.0322 26  ARG A C   
208  O O   . ARG A 25  ? 0.4498 0.4125 0.3985 0.0081  -0.0678 -0.0371 26  ARG A O   
209  C CB  . ARG A 25  ? 0.3817 0.3359 0.3272 -0.0101 -0.0368 -0.0245 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.4437 0.3931 0.3785 -0.0140 -0.0379 -0.0244 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.4593 0.3983 0.3832 -0.0217 -0.0276 -0.0193 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.4676 0.3881 0.3751 -0.0227 -0.0264 -0.0139 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.6525 0.5558 0.5392 -0.0275 -0.0249 -0.0110 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.5978 0.4998 0.4771 -0.0303 -0.0263 -0.0128 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.5189 0.4057 0.3908 -0.0307 -0.0214 -0.0072 26  ARG A NH2 
216  N N   A SER A 26  ? 0.4430 0.3754 0.3735 0.0110  -0.0649 -0.0269 27  SER A N   
217  N N   B SER A 26  ? 0.4439 0.3762 0.3744 0.0111  -0.0650 -0.0269 27  SER A N   
218  N N   C SER A 26  ? 0.4375 0.3699 0.3680 0.0111  -0.0650 -0.0269 27  SER A N   
219  C CA  A SER A 26  ? 0.4753 0.3880 0.3869 0.0198  -0.0793 -0.0251 27  SER A CA  
220  C CA  B SER A 26  ? 0.4771 0.3893 0.3882 0.0198  -0.0793 -0.0249 27  SER A CA  
221  C CA  C SER A 26  ? 0.4685 0.3805 0.3796 0.0199  -0.0793 -0.0249 27  SER A CA  
222  C C   A SER A 26  ? 0.5295 0.4606 0.4594 0.0318  -0.0929 -0.0347 27  SER A C   
223  C C   B SER A 26  ? 0.5361 0.4645 0.4643 0.0327  -0.0936 -0.0342 27  SER A C   
224  C C   C SER A 26  ? 0.5302 0.4580 0.4581 0.0328  -0.0937 -0.0340 27  SER A C   
225  O O   A SER A 26  ? 0.5441 0.4735 0.4660 0.0370  -0.1051 -0.0365 27  SER A O   
226  O O   B SER A 26  ? 0.5599 0.4814 0.4767 0.0398  -0.1074 -0.0349 27  SER A O   
227  O O   C SER A 26  ? 0.5521 0.4717 0.4678 0.0403  -0.1077 -0.0345 27  SER A O   
228  C CB  A SER A 26  ? 0.5395 0.4254 0.4340 0.0228  -0.0800 -0.0192 27  SER A CB  
229  C CB  B SER A 26  ? 0.5432 0.4259 0.4333 0.0210  -0.0789 -0.0178 27  SER A CB  
230  C CB  C SER A 26  ? 0.5278 0.4109 0.4187 0.0210  -0.0786 -0.0179 27  SER A CB  
231  O OG  A SER A 26  ? 0.6497 0.5147 0.5216 0.0120  -0.0703 -0.0113 27  SER A OG  
232  O OG  B SER A 26  ? 0.6433 0.5310 0.5482 0.0276  -0.0797 -0.0216 27  SER A OG  
233  O OG  C SER A 26  ? 0.6475 0.5042 0.5136 0.0294  -0.0925 -0.0144 27  SER A OG  
234  N N   . ARG A 27  ? 0.4646 0.4157 0.4200 0.0355  -0.0904 -0.0422 28  ARG A N   
235  C CA  . ARG A 27  ? 0.4703 0.4432 0.4488 0.0471  -0.1016 -0.0542 28  ARG A CA  
236  C C   . ARG A 27  ? 0.4868 0.4930 0.4888 0.0410  -0.0978 -0.0646 28  ARG A C   
237  O O   . ARG A 27  ? 0.4776 0.5081 0.5031 0.0482  -0.1051 -0.0773 28  ARG A O   
238  C CB  . ARG A 27  ? 0.4894 0.4657 0.4822 0.0531  -0.0995 -0.0585 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.6292 0.5698 0.5973 0.0584  -0.1030 -0.0493 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.7270 0.6700 0.7083 0.0619  -0.0983 -0.0538 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.9685 0.9279 0.9720 0.0768  -0.1098 -0.0663 28  ARG A NE  
242  C CZ  . ARG A 27  ? 1.1788 1.1616 1.2091 0.0779  -0.1039 -0.0775 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 1.0472 1.0466 1.0998 0.0921  -0.1144 -0.0906 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 1.0115 1.0020 1.0465 0.0649  -0.0876 -0.0763 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.4165 0.4230 0.4122 0.0274  -0.0862 -0.0601 29  ASP A N   
246  C CA  . ASP A 28  ? 0.4174 0.4484 0.4293 0.0184  -0.0796 -0.0683 29  ASP A CA  
247  C C   . ASP A 28  ? 0.4544 0.5105 0.4930 0.0151  -0.0706 -0.0782 29  ASP A C   
248  O O   . ASP A 28  ? 0.4483 0.5301 0.5069 0.0123  -0.0704 -0.0908 29  ASP A O   
249  C CB  . ASP A 28  ? 0.4531 0.4952 0.4675 0.0231  -0.0933 -0.0762 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.5678 0.6263 0.5896 0.0104  -0.0851 -0.0822 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.5698 0.6175 0.5815 -0.0010 -0.0711 -0.0749 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.6193 0.7015 0.6575 0.0120  -0.0926 -0.0951 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.3805 0.4295 0.4185 0.0142  -0.0628 -0.0736 30  ILE A N   
254  C CA  . ILE A 29  ? 0.3484 0.4179 0.4071 0.0103  -0.0538 -0.0824 30  ILE A CA  
255  C C   . ILE A 29  ? 0.3871 0.4569 0.4419 -0.0040 -0.0380 -0.0783 30  ILE A C   
256  O O   . ILE A 29  ? 0.3565 0.4076 0.3945 -0.0075 -0.0325 -0.0664 30  ILE A O   
257  C CB  . ILE A 29  ? 0.3842 0.4479 0.4457 0.0182  -0.0553 -0.0822 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.4085 0.4711 0.4753 0.0345  -0.0719 -0.0881 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.3657 0.4484 0.4443 0.0114  -0.0433 -0.0906 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.4396 0.4836 0.4994 0.0425  -0.0739 -0.0840 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.3478 0.4386 0.4180 -0.0123 -0.0307 -0.0888 31  LEU A N   
262  N N   B LEU A 30  ? 0.3547 0.4456 0.4249 -0.0122 -0.0308 -0.0889 31  LEU A N   
263  C CA  A LEU A 30  ? 0.3420 0.4315 0.4072 -0.0261 -0.0157 -0.0863 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.3524 0.4423 0.4180 -0.0261 -0.0158 -0.0866 31  LEU A CA  
265  C C   A LEU A 30  ? 0.3796 0.4506 0.4262 -0.0314 -0.0125 -0.0757 31  LEU A C   
266  C C   B LEU A 30  ? 0.3848 0.4559 0.4315 -0.0314 -0.0125 -0.0758 31  LEU A C   
267  O O   A LEU A 30  ? 0.3695 0.4311 0.4068 -0.0396 -0.0017 -0.0698 31  LEU A O   
268  O O   B LEU A 30  ? 0.3749 0.4366 0.4123 -0.0396 -0.0017 -0.0698 31  LEU A O   
269  C CB  A LEU A 30  ? 0.3442 0.4291 0.4062 -0.0286 -0.0072 -0.0821 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.3578 0.4440 0.4208 -0.0289 -0.0071 -0.0830 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.4012 0.5060 0.4817 -0.0282 -0.0047 -0.0948 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.4244 0.5321 0.5043 -0.0353 0.0008  -0.0964 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.3846 0.4846 0.4569 -0.0366 0.0073  -0.0909 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.4236 0.5387 0.5143 -0.0268 -0.0032 -0.1017 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.4309 0.5612 0.5313 -0.0339 -0.0021 -0.1113 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.4560 0.5566 0.5241 -0.0488 0.0154  -0.0923 31  LEU A CD2 
277  N N   . THR A 31  ? 0.3365 0.4019 0.3772 -0.0268 -0.0219 -0.0743 32  THR A N   
278  C CA  . THR A 31  ? 0.3466 0.3966 0.3714 -0.0323 -0.0183 -0.0670 32  THR A CA  
279  C C   . THR A 31  ? 0.4190 0.4807 0.4514 -0.0439 -0.0096 -0.0759 32  THR A C   
280  O O   . THR A 31  ? 0.4060 0.4898 0.4559 -0.0453 -0.0119 -0.0890 32  THR A O   
281  C CB  . THR A 31  ? 0.4128 0.4544 0.4274 -0.0260 -0.0301 -0.0648 32  THR A CB  
282  O OG1 . THR A 31  ? 0.4335 0.4941 0.4622 -0.0211 -0.0408 -0.0765 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.3997 0.4228 0.4005 -0.0180 -0.0355 -0.0548 32  THR A CG2 
284  N N   . ASP A 32  ? 0.3770 0.4246 0.3978 -0.0523 0.0012  -0.0698 33  ASP A N   
285  C CA  . ASP A 32  ? 0.3773 0.4296 0.4010 -0.0649 0.0120  -0.0771 33  ASP A CA  
286  C C   . ASP A 32  ? 0.4145 0.4531 0.4263 -0.0710 0.0159  -0.0750 33  ASP A C   
287  O O   . ASP A 32  ? 0.4206 0.4559 0.4300 -0.0825 0.0266  -0.0792 33  ASP A O   
288  C CB  . ASP A 32  ? 0.3958 0.4413 0.4151 -0.0707 0.0236  -0.0731 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.5325 0.5562 0.5358 -0.0656 0.0253  -0.0582 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.4828 0.4954 0.4784 -0.0600 0.0205  -0.0515 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.6515 0.6705 0.6502 -0.0676 0.0312  -0.0543 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.3568 0.3857 0.3595 -0.0645 0.0083  -0.0692 34  VAL A N   
293  C CA  . VAL A 33  ? 0.3539 0.3701 0.3452 -0.0703 0.0122  -0.0686 34  VAL A CA  
294  C C   . VAL A 33  ? 0.3992 0.4133 0.3835 -0.0642 0.0010  -0.0676 34  VAL A C   
295  O O   . VAL A 33  ? 0.3958 0.4078 0.3774 -0.0547 -0.0077 -0.0621 34  VAL A O   
296  C CB  . VAL A 33  ? 0.4036 0.3962 0.3813 -0.0722 0.0231  -0.0581 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.3904 0.3720 0.3605 -0.0624 0.0190  -0.0473 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.4135 0.3932 0.3821 -0.0808 0.0310  -0.0607 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.3592 0.3715 0.3379 -0.0708 0.0018  -0.0730 35  VAL A N   
300  N N   B VAL A 34  ? 0.3616 0.3742 0.3405 -0.0707 0.0016  -0.0731 35  VAL A N   
301  C CA  A VAL A 34  ? 0.3592 0.3655 0.3255 -0.0678 -0.0070 -0.0721 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.3633 0.3693 0.3295 -0.0672 -0.0073 -0.0716 35  VAL A CA  
303  C C   A VAL A 34  ? 0.4191 0.4044 0.3707 -0.0733 0.0036  -0.0671 35  VAL A C   
304  C C   B VAL A 34  ? 0.4227 0.4084 0.3741 -0.0733 0.0031  -0.0673 35  VAL A C   
305  O O   A VAL A 34  ? 0.4303 0.4117 0.3827 -0.0823 0.0141  -0.0712 35  VAL A O   
306  O O   B VAL A 34  ? 0.4339 0.4165 0.3863 -0.0824 0.0132  -0.0721 35  VAL A O   
307  C CB  A VAL A 34  ? 0.4087 0.4338 0.3816 -0.0706 -0.0166 -0.0850 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.4162 0.4407 0.3880 -0.0669 -0.0201 -0.0829 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.4206 0.4360 0.3751 -0.0687 -0.0256 -0.0835 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.4187 0.4540 0.3974 -0.0794 -0.0135 -0.0951 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.3998 0.4478 0.3908 -0.0630 -0.0276 -0.0916 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.4278 0.4408 0.3806 -0.0615 -0.0312 -0.0785 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.3760 0.3467 0.3139 -0.0685 0.0018  -0.0590 36  ILE A N   
314  C CA  . ILE A 35  ? 0.3756 0.3284 0.3010 -0.0726 0.0113  -0.0561 36  ILE A CA  
315  C C   . ILE A 35  ? 0.4460 0.3967 0.3577 -0.0761 0.0050  -0.0608 36  ILE A C   
316  O O   . ILE A 35  ? 0.4359 0.3861 0.3385 -0.0709 -0.0059 -0.0582 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3997 0.3406 0.3207 -0.0666 0.0154  -0.0463 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.3922 0.3370 0.3254 -0.0621 0.0186  -0.0414 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.4327 0.3586 0.3447 -0.0703 0.0255  -0.0460 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.4090 0.3518 0.3484 -0.0669 0.0280  -0.0435 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.4182 0.3653 0.3260 -0.0851 0.0118  -0.0678 37  VAL A N   
322  C CA  . VAL A 36  ? 0.4312 0.3766 0.3244 -0.0902 0.0065  -0.0737 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4981 0.4236 0.3758 -0.0933 0.0164  -0.0706 37  VAL A C   
324  O O   . VAL A 36  ? 0.4740 0.3902 0.3554 -0.0967 0.0296  -0.0712 37  VAL A O   
325  C CB  . VAL A 36  ? 0.4832 0.4408 0.3831 -0.0999 0.0072  -0.0864 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4997 0.4566 0.3830 -0.1053 0.0004  -0.0931 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.4740 0.4552 0.3930 -0.0974 -0.0011 -0.0919 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.4754 0.3931 0.3343 -0.0923 0.0101  -0.0678 38  VAL A N   
329  C CA  . VAL A 37  ? 0.4866 0.3872 0.3296 -0.0963 0.0196  -0.0664 38  VAL A CA  
330  C C   . VAL A 37  ? 0.5747 0.4710 0.3951 -0.1030 0.0128  -0.0717 38  VAL A C   
331  O O   . VAL A 37  ? 0.5522 0.4461 0.3573 -0.0996 0.0003  -0.0679 38  VAL A O   
332  C CB  . VAL A 37  ? 0.5349 0.4282 0.3750 -0.0901 0.0210  -0.0572 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.5435 0.4233 0.3739 -0.0950 0.0343  -0.0583 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.5055 0.4071 0.3675 -0.0823 0.0227  -0.0520 38  VAL A CG2 
335  N N   A SER A 38  ? 0.5737 0.4642 0.3872 -0.1125 0.0218  -0.0798 39  SER A N   
336  N N   B SER A 38  ? 0.5420 0.4403 0.3633 -0.1116 0.0183  -0.0814 39  SER A N   
337  C CA  A SER A 38  ? 0.6094 0.4947 0.3983 -0.1205 0.0164  -0.0858 39  SER A CA  
338  C CA  B SER A 38  ? 0.5602 0.4587 0.3643 -0.1201 0.0129  -0.0899 39  SER A CA  
339  C C   A SER A 38  ? 0.6622 0.5595 0.4449 -0.1163 -0.0047 -0.0862 39  SER A C   
340  C C   B SER A 38  ? 0.5837 0.4984 0.3879 -0.1154 -0.0071 -0.0917 39  SER A C   
341  O O   A SER A 38  ? 0.6756 0.5631 0.4329 -0.1155 -0.0148 -0.0827 39  SER A O   
342  O O   B SER A 38  ? 0.5480 0.4808 0.3742 -0.1139 -0.0102 -0.0964 39  SER A O   
343  C CB  A SER A 38  ? 0.6945 0.5610 0.4597 -0.1238 0.0228  -0.0821 39  SER A CB  
344  C CB  B SER A 38  ? 0.6357 0.5156 0.4129 -0.1258 0.0184  -0.0893 39  SER A CB  
345  O OG  A SER A 38  ? 0.8432 0.7018 0.6161 -0.1270 0.0414  -0.0844 39  SER A OG  
346  O OG  B SER A 38  ? 0.7580 0.6285 0.5413 -0.1307 0.0371  -0.0929 39  SER A OG  
347  N N   A ARG A 39  ? 0.5965 0.5142 0.4024 -0.1130 -0.0110 -0.0907 40  ARG A N   
348  N N   B ARG A 39  ? 0.5606 0.4687 0.3409 -0.1127 -0.0208 -0.0882 40  ARG A N   
349  C CA  A ARG A 39  ? 0.5969 0.5325 0.4064 -0.1069 -0.0310 -0.0939 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.5633 0.4867 0.3447 -0.1053 -0.0421 -0.0902 40  ARG A CA  
351  C C   A ARG A 39  ? 0.6346 0.5658 0.4383 -0.0939 -0.0442 -0.0830 40  ARG A C   
352  C C   B ARG A 39  ? 0.6133 0.5440 0.4126 -0.0921 -0.0489 -0.0824 40  ARG A C   
353  O O   A ARG A 39  ? 0.6464 0.5826 0.4405 -0.0873 -0.0630 -0.0838 40  ARG A O   
354  O O   B ARG A 39  ? 0.6042 0.5576 0.4266 -0.0870 -0.0572 -0.0880 40  ARG A O   
355  C CB  A ARG A 39  ? 0.6268 0.5662 0.4181 -0.1137 -0.0412 -0.1034 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.5756 0.4861 0.3213 -0.1060 -0.0563 -0.0892 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.7598 0.7102 0.5621 -0.1264 -0.0317 -0.1172 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.6871 0.5982 0.4187 -0.1191 -0.0533 -0.1005 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.8443 0.8083 0.6357 -0.1306 -0.0473 -0.1283 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.6769 0.5778 0.3721 -0.1194 -0.0706 -0.1004 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.9373 0.9074 0.7332 -0.1456 -0.0365 -0.1423 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.7002 0.6008 0.3802 -0.1334 -0.0663 -0.1116 40  ARG A NE  
363  C CZ  A ARG A 39  ? 1.1224 1.0756 0.8962 -0.1567 -0.0270 -0.1460 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.8755 0.7982 0.5633 -0.1367 -0.0770 -0.1245 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.9511 0.8813 0.6968 -0.1553 -0.0260 -0.1371 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.7227 0.6719 0.4358 -0.1269 -0.0925 -0.1287 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.9622 0.9207 0.7414 -0.1704 -0.0170 -0.1597 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.7490 0.6691 0.4208 -0.1507 -0.0715 -0.1349 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.5480 0.4692 0.3571 -0.0897 -0.0348 -0.0736 41  GLU A N   
370  N N   B GLU A 40  ? 0.5471 0.4603 0.3383 -0.0881 -0.0429 -0.0712 41  GLU A N   
371  C CA  A GLU A 40  ? 0.5402 0.4563 0.3471 -0.0786 -0.0437 -0.0640 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.5261 0.4418 0.3295 -0.0767 -0.0483 -0.0634 41  GLU A CA  
373  C C   A GLU A 40  ? 0.5325 0.4640 0.3706 -0.0738 -0.0380 -0.0636 41  GLU A C   
374  C C   B GLU A 40  ? 0.5201 0.4540 0.3572 -0.0744 -0.0406 -0.0656 41  GLU A C   
375  O O   A GLU A 40  ? 0.4900 0.4209 0.3397 -0.0790 -0.0226 -0.0640 41  GLU A O   
376  O O   B GLU A 40  ? 0.4749 0.4105 0.3229 -0.0816 -0.0260 -0.0689 41  GLU A O   
377  C CB  A GLU A 40  ? 0.5730 0.4639 0.3567 -0.0805 -0.0361 -0.0547 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.5533 0.4453 0.3381 -0.0760 -0.0417 -0.0525 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.7729 0.6453 0.5202 -0.0862 -0.0418 -0.0545 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.7735 0.6430 0.5213 -0.0832 -0.0424 -0.0509 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.2486 1.1017 0.9690 -0.0798 -0.0546 -0.0455 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.2746 1.1253 0.9925 -0.0773 -0.0579 -0.0435 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.3030 1.1326 0.9972 -0.0863 -0.0466 -0.0402 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.3132 1.1727 1.0366 -0.0662 -0.0759 -0.0434 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.2725 1.1330 0.9976 -0.0686 -0.0722 -0.0444 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.3110 1.1369 0.9986 -0.0841 -0.0519 -0.0385 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.4808 0.4256 0.3319 -0.0640 -0.0507 -0.0636 42  GLN A N   
388  C CA  . GLN A 41  ? 0.4560 0.4173 0.3356 -0.0609 -0.0457 -0.0651 42  GLN A CA  
389  C C   . GLN A 41  ? 0.5037 0.4575 0.3850 -0.0523 -0.0464 -0.0556 42  GLN A C   
390  O O   . GLN A 41  ? 0.5250 0.4701 0.3931 -0.0446 -0.0585 -0.0511 42  GLN A O   
391  C CB  . GLN A 41  ? 0.4752 0.4628 0.3737 -0.0580 -0.0574 -0.0763 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.6634 0.6623 0.5650 -0.0690 -0.0543 -0.0881 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.9382 0.9678 0.8632 -0.0683 -0.0632 -0.1018 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.8391 0.8842 0.7827 -0.0596 -0.0698 -0.1036 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.9774 1.0179 0.9033 -0.0782 -0.0628 -0.1135 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.4160 0.3717 0.3121 -0.0535 -0.0339 -0.0526 43  PHE A N   
397  C CA  . PHE A 42  ? 0.4084 0.3590 0.3077 -0.0466 -0.0333 -0.0447 43  PHE A CA  
398  C C   . PHE A 42  ? 0.4463 0.4143 0.3702 -0.0446 -0.0299 -0.0476 43  PHE A C   
399  O O   . PHE A 42  ? 0.4394 0.4106 0.3720 -0.0507 -0.0185 -0.0493 43  PHE A O   
400  C CB  . PHE A 42  ? 0.4364 0.3705 0.3258 -0.0505 -0.0207 -0.0376 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.4784 0.3946 0.3425 -0.0552 -0.0204 -0.0358 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.5055 0.4186 0.3628 -0.0634 -0.0136 -0.0406 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.5138 0.4140 0.3585 -0.0525 -0.0257 -0.0297 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.5452 0.4417 0.3773 -0.0690 -0.0124 -0.0399 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.5710 0.4526 0.3886 -0.0589 -0.0242 -0.0283 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.5483 0.4292 0.3600 -0.0672 -0.0173 -0.0336 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.4034 0.3802 0.3365 -0.0362 -0.0393 -0.0483 44  ARG A N   
408  C CA  . ARG A 43  ? 0.3770 0.3706 0.3322 -0.0351 -0.0355 -0.0521 44  ARG A CA  
409  C C   . ARG A 43  ? 0.4240 0.4083 0.3786 -0.0336 -0.0276 -0.0435 44  ARG A C   
410  O O   . ARG A 43  ? 0.4230 0.3929 0.3648 -0.0297 -0.0303 -0.0366 44  ARG A O   
411  C CB  . ARG A 43  ? 0.3741 0.3846 0.3427 -0.0264 -0.0488 -0.0594 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.4952 0.5219 0.4696 -0.0273 -0.0582 -0.0708 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.6302 0.6843 0.6301 -0.0218 -0.0655 -0.0829 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.7737 0.8380 0.7904 -0.0275 -0.0520 -0.0853 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.9281 1.0083 0.9586 -0.0385 -0.0418 -0.0946 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.8204 0.9123 0.8543 -0.0450 -0.0438 -0.1044 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.7081 0.7920 0.7475 -0.0440 -0.0296 -0.0949 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.3653 0.3562 0.3314 -0.0376 -0.0175 -0.0441 45  ALA A N   
419  C CA  . ALA A 44  ? 0.3600 0.3441 0.3256 -0.0359 -0.0112 -0.0366 45  ALA A CA  
420  C C   . ALA A 44  ? 0.3708 0.3658 0.3493 -0.0384 -0.0048 -0.0391 45  ALA A C   
421  O O   . ALA A 44  ? 0.3503 0.3578 0.3384 -0.0427 -0.0037 -0.0472 45  ALA A O   
422  C CB  . ALA A 44  ? 0.3804 0.3498 0.3348 -0.0394 -0.0030 -0.0306 45  ALA A CB  
423  N N   . HIS A 45  ? 0.3285 0.3190 0.3062 -0.0367 -0.0004 -0.0329 46  HIS A N   
424  C CA  . HIS A 45  ? 0.3193 0.3154 0.3032 -0.0396 0.0062  -0.0334 46  HIS A CA  
425  C C   . HIS A 45  ? 0.3738 0.3570 0.3491 -0.0432 0.0148  -0.0278 46  HIS A C   
426  O O   . HIS A 45  ? 0.3642 0.3381 0.3334 -0.0398 0.0154  -0.0217 46  HIS A O   
427  C CB  . HIS A 45  ? 0.3139 0.3128 0.3006 -0.0348 0.0043  -0.0305 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.3585 0.3657 0.3525 -0.0293 -0.0044 -0.0356 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.3841 0.3821 0.3709 -0.0237 -0.0113 -0.0321 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.3597 0.3822 0.3668 -0.0286 -0.0070 -0.0445 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.3701 0.3753 0.3644 -0.0181 -0.0191 -0.0378 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.3601 0.3822 0.3688 -0.0202 -0.0170 -0.0461 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.3470 0.3293 0.3220 -0.0500 0.0216  -0.0308 47  LYS A N   
434  C CA  . LYS A 46  ? 0.3563 0.3224 0.3213 -0.0524 0.0294  -0.0255 47  LYS A CA  
435  C C   . LYS A 46  ? 0.3877 0.3477 0.3485 -0.0461 0.0293  -0.0171 47  LYS A C   
436  O O   . LYS A 46  ? 0.3688 0.3180 0.3244 -0.0424 0.0307  -0.0124 47  LYS A O   
437  C CB  . LYS A 46  ? 0.3972 0.3604 0.3594 -0.0618 0.0375  -0.0295 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.3931 0.3600 0.3582 -0.0697 0.0397  -0.0384 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.4124 0.3770 0.3747 -0.0815 0.0496  -0.0440 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.4504 0.4261 0.4203 -0.0904 0.0509  -0.0561 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.4830 0.4566 0.4500 -0.1047 0.0626  -0.0633 47  LYS A NZ  
442  N N   . THR A 47  ? 0.3368 0.3055 0.3010 -0.0447 0.0272  -0.0166 48  THR A N   
443  C CA  . THR A 47  ? 0.3321 0.2971 0.2921 -0.0393 0.0263  -0.0097 48  THR A CA  
444  C C   . THR A 47  ? 0.3561 0.3224 0.3191 -0.0327 0.0219  -0.0070 48  THR A C   
445  O O   . THR A 47  ? 0.3453 0.3064 0.3054 -0.0282 0.0222  -0.0023 48  THR A O   
446  C CB  . THR A 47  ? 0.4253 0.3989 0.3866 -0.0406 0.0258  -0.0107 48  THR A CB  
447  O OG1 . THR A 47  ? 0.4240 0.4111 0.3962 -0.0396 0.0212  -0.0164 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.4482 0.4169 0.4021 -0.0490 0.0330  -0.0126 48  THR A CG2 
449  N N   . VAL A 48  ? 0.3155 0.2878 0.2834 -0.0323 0.0179  -0.0103 49  VAL A N   
450  C CA  . VAL A 48  ? 0.3213 0.2926 0.2892 -0.0288 0.0156  -0.0086 49  VAL A CA  
451  C C   . VAL A 48  ? 0.3616 0.3240 0.3258 -0.0289 0.0194  -0.0078 49  VAL A C   
452  O O   . VAL A 48  ? 0.3336 0.2952 0.2990 -0.0257 0.0208  -0.0062 49  VAL A O   
453  C CB  . VAL A 48  ? 0.3494 0.3235 0.3180 -0.0288 0.0103  -0.0116 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.3523 0.3208 0.3161 -0.0283 0.0102  -0.0101 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.3419 0.3242 0.3156 -0.0274 0.0071  -0.0132 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.3254 0.2825 0.2864 -0.0328 0.0214  -0.0106 50  LEU A N   
457  C CA  . LEU A 49  ? 0.3384 0.2857 0.2952 -0.0336 0.0261  -0.0111 50  LEU A CA  
458  C C   . LEU A 49  ? 0.3673 0.3077 0.3240 -0.0291 0.0301  -0.0074 50  LEU A C   
459  O O   . LEU A 49  ? 0.3567 0.2943 0.3151 -0.0254 0.0322  -0.0075 50  LEU A O   
460  C CB  . LEU A 49  ? 0.3424 0.2857 0.2957 -0.0397 0.0279  -0.0156 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.3799 0.3295 0.3324 -0.0426 0.0220  -0.0201 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.3882 0.3366 0.3389 -0.0491 0.0241  -0.0261 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.3997 0.3449 0.3456 -0.0415 0.0200  -0.0194 50  LEU A CD2 
464  N N   . MET A 50  ? 0.3355 0.2732 0.2897 -0.0291 0.0306  -0.0047 51  MET A N   
465  C CA  . MET A 50  ? 0.3491 0.2763 0.2989 -0.0235 0.0323  0.0001  51  MET A CA  
466  C C   . MET A 50  ? 0.3993 0.3358 0.3556 -0.0154 0.0278  0.0025  51  MET A C   
467  O O   . MET A 50  ? 0.4002 0.3322 0.3583 -0.0082 0.0280  0.0037  51  MET A O   
468  C CB  . MET A 50  ? 0.3783 0.2982 0.3190 -0.0270 0.0339  0.0030  51  MET A CB  
469  C CG  . MET A 50  ? 0.4246 0.3352 0.3592 -0.0364 0.0401  -0.0008 51  MET A CG  
470  S SD  . MET A 50  ? 0.4797 0.3875 0.4050 -0.0436 0.0432  0.0003  51  MET A SD  
471  C CE  . MET A 50  ? 0.4497 0.3292 0.3562 -0.0389 0.0461  0.0087  51  MET A CE  
472  N N   . ALA A 51  ? 0.3576 0.3080 0.3188 -0.0165 0.0237  0.0019  52  ALA A N   
473  C CA  . ALA A 51  ? 0.3516 0.3133 0.3197 -0.0110 0.0198  0.0025  52  ALA A CA  
474  C C   . ALA A 51  ? 0.3762 0.3431 0.3525 -0.0090 0.0215  -0.0015 52  ALA A C   
475  O O   . ALA A 51  ? 0.3795 0.3559 0.3636 -0.0037 0.0195  -0.0026 52  ALA A O   
476  C CB  . ALA A 51  ? 0.3517 0.3244 0.3219 -0.0145 0.0166  0.0014  52  ALA A CB  
477  N N   . CYS A 52  ? 0.3350 0.2966 0.3091 -0.0141 0.0253  -0.0046 53  CYS A N   
478  C CA  . CYS A 52  ? 0.3353 0.2998 0.3136 -0.0154 0.0289  -0.0094 53  CYS A CA  
479  C C   . CYS A 52  ? 0.3768 0.3333 0.3559 -0.0131 0.0343  -0.0121 53  CYS A C   
480  O O   . CYS A 52  ? 0.3722 0.3337 0.3570 -0.0136 0.0384  -0.0174 53  CYS A O   
481  C CB  . CYS A 52  ? 0.3481 0.3105 0.3194 -0.0232 0.0290  -0.0111 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.3909 0.3607 0.3620 -0.0250 0.0236  -0.0098 53  CYS A SG  
483  N N   . SER A 53  ? 0.3401 0.2834 0.3125 -0.0128 0.0357  -0.0098 54  SER A N   
484  C CA  . SER A 53  ? 0.3310 0.2633 0.3019 -0.0124 0.0417  -0.0133 54  SER A CA  
485  C C   . SER A 53  ? 0.4066 0.3246 0.3739 -0.0059 0.0423  -0.0098 54  SER A C   
486  O O   . SER A 53  ? 0.3886 0.2983 0.3470 -0.0086 0.0409  -0.0054 54  SER A O   
487  C CB  . SER A 53  ? 0.3605 0.2866 0.3220 -0.0223 0.0442  -0.0159 54  SER A CB  
488  O OG  . SER A 53  ? 0.4289 0.3408 0.3845 -0.0245 0.0494  -0.0181 54  SER A OG  
489  N N   . GLY A 54  ? 0.3836 0.2974 0.3569 0.0024  0.0447  -0.0125 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3929 0.2874 0.3602 0.0102  0.0451  -0.0091 55  GLY A CA  
491  C C   . GLY A 54  ? 0.4421 0.3164 0.3958 0.0017  0.0514  -0.0094 55  GLY A C   
492  O O   . GLY A 54  ? 0.4486 0.3037 0.3901 0.0025  0.0518  -0.0043 55  GLY A O   
493  N N   . LEU A 55  ? 0.4115 0.2892 0.3654 -0.0079 0.0566  -0.0158 56  LEU A N   
494  C CA  . LEU A 55  ? 0.4158 0.2781 0.3582 -0.0175 0.0623  -0.0181 56  LEU A CA  
495  C C   . LEU A 55  ? 0.4400 0.3036 0.3749 -0.0256 0.0595  -0.0145 56  LEU A C   
496  O O   . LEU A 55  ? 0.4462 0.2927 0.3708 -0.0293 0.0632  -0.0130 56  LEU A O   
497  C CB  . LEU A 55  ? 0.4079 0.2751 0.3505 -0.0258 0.0669  -0.0262 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.4760 0.3287 0.4078 -0.0359 0.0728  -0.0306 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.5036 0.3330 0.4315 -0.0313 0.0802  -0.0325 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.4803 0.3411 0.4091 -0.0452 0.0740  -0.0374 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.3712 0.2539 0.3112 -0.0284 0.0537  -0.0137 57  PHE A N   
502  C CA  . PHE A 56  ? 0.3696 0.2567 0.3059 -0.0352 0.0513  -0.0123 57  PHE A CA  
503  C C   . PHE A 56  ? 0.4333 0.3124 0.3643 -0.0313 0.0505  -0.0058 57  PHE A C   
504  O O   . PHE A 56  ? 0.4254 0.2983 0.3490 -0.0388 0.0533  -0.0059 57  PHE A O   
505  C CB  . PHE A 56  ? 0.3648 0.2713 0.3073 -0.0376 0.0451  -0.0138 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.3796 0.2894 0.3206 -0.0435 0.0452  -0.0198 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.4256 0.3312 0.3618 -0.0519 0.0479  -0.0252 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.3992 0.3159 0.3416 -0.0420 0.0423  -0.0206 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.4327 0.3415 0.3654 -0.0571 0.0464  -0.0308 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.4357 0.3523 0.3716 -0.0478 0.0415  -0.0252 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.4143 0.3272 0.3453 -0.0546 0.0428  -0.0302 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.4072 0.2862 0.3411 -0.0204 0.0469  -0.0010 58  TYR A N   
513  C CA  . TYR A 57  ? 0.4267 0.2945 0.3512 -0.0157 0.0448  0.0060  58  TYR A CA  
514  C C   . TYR A 57  ? 0.4943 0.3331 0.4024 -0.0185 0.0516  0.0078  58  TYR A C   
515  O O   . TYR A 57  ? 0.4807 0.3081 0.3753 -0.0248 0.0540  0.0111  58  TYR A O   
516  C CB  . TYR A 57  ? 0.4528 0.3266 0.3843 -0.0020 0.0384  0.0094  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.5038 0.3636 0.4223 0.0046  0.0344  0.0172  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.5228 0.3886 0.4349 0.0003  0.0314  0.0209  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.5671 0.4060 0.4781 0.0156  0.0333  0.0209  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.5715 0.4221 0.4670 0.0053  0.0276  0.0285  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.6166 0.4387 0.5109 0.0225  0.0281  0.0293  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6973 0.5252 0.5827 0.0167  0.0253  0.0333  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.7883 0.5975 0.6534 0.0228  0.0200  0.0419  58  TYR A OH  
524  N N   A SER A 58  ? 0.4611 0.2867 0.3695 -0.0149 0.0557  0.0050  59  SER A N   
525  N N   B SER A 58  ? 0.4717 0.2975 0.3802 -0.0149 0.0557  0.0050  59  SER A N   
526  C CA  A SER A 58  ? 0.4925 0.2868 0.3845 -0.0175 0.0630  0.0059  59  SER A CA  
527  C CA  B SER A 58  ? 0.5072 0.3020 0.3998 -0.0173 0.0629  0.0057  59  SER A CA  
528  C C   A SER A 58  ? 0.5622 0.3533 0.4471 -0.0349 0.0706  0.0008  59  SER A C   
529  C C   B SER A 58  ? 0.5666 0.3580 0.4516 -0.0348 0.0705  0.0008  59  SER A C   
530  O O   A SER A 58  ? 0.5967 0.3658 0.4643 -0.0416 0.0761  0.0034  59  SER A O   
531  O O   B SER A 58  ? 0.5965 0.3666 0.4643 -0.0413 0.0756  0.0037  59  SER A O   
532  C CB  A SER A 58  ? 0.5229 0.3074 0.4202 -0.0097 0.0660  0.0016  59  SER A CB  
533  C CB  B SER A 58  ? 0.5532 0.3398 0.4518 -0.0106 0.0663  0.0008  59  SER A CB  
534  O OG  A SER A 58  ? 0.5476 0.3354 0.4528 0.0071  0.0589  0.0051  59  SER A OG  
535  O OG  B SER A 58  ? 0.6936 0.4467 0.5758 -0.0120 0.0735  0.0014  59  SER A OG  
536  N N   . ILE A 59  ? 0.5001 0.3135 0.3973 -0.0425 0.0706  -0.0069 60  ILE A N   
537  C CA  . ILE A 59  ? 0.4928 0.3105 0.3880 -0.0581 0.0758  -0.0142 60  ILE A CA  
538  C C   . ILE A 59  ? 0.5329 0.3566 0.4243 -0.0654 0.0758  -0.0127 60  ILE A C   
539  O O   . ILE A 59  ? 0.5630 0.3733 0.4434 -0.0772 0.0839  -0.0157 60  ILE A O   
540  C CB  . ILE A 59  ? 0.4939 0.3356 0.4024 -0.0618 0.0723  -0.0220 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.5004 0.3338 0.4090 -0.0595 0.0757  -0.0261 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.4650 0.3187 0.3753 -0.0759 0.0740  -0.0303 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.5185 0.3730 0.4359 -0.0607 0.0706  -0.0313 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.4539 0.2973 0.3541 -0.0598 0.0680  -0.0094 61  PHE A N   
545  C CA  . PHE A 60  ? 0.4554 0.3078 0.3541 -0.0675 0.0687  -0.0103 61  PHE A CA  
546  C C   . PHE A 60  ? 0.5329 0.3641 0.4133 -0.0664 0.0714  -0.0019 61  PHE A C   
547  O O   . PHE A 60  ? 0.5482 0.3837 0.4242 -0.0752 0.0746  -0.0036 61  PHE A O   
548  C CB  . PHE A 60  ? 0.4427 0.3250 0.3581 -0.0643 0.0602  -0.0126 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.4419 0.3406 0.3696 -0.0664 0.0570  -0.0204 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.4857 0.3887 0.4153 -0.0778 0.0613  -0.0298 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.4490 0.3576 0.3845 -0.0579 0.0499  -0.0188 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.4848 0.4021 0.4230 -0.0788 0.0564  -0.0367 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.4819 0.4015 0.4233 -0.0601 0.0463  -0.0250 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.4596 0.3833 0.4019 -0.0697 0.0486  -0.0334 61  PHE A CZ  
555  N N   . THR A 61  ? 0.5104 0.3171 0.3785 -0.0564 0.0707  0.0060  62  THR A N   
556  C CA  . THR A 61  ? 0.5413 0.3209 0.3858 -0.0555 0.0727  0.0147  62  THR A CA  
557  C C   . THR A 61  ? 0.6474 0.3933 0.4715 -0.0656 0.0841  0.0137  62  THR A C   
558  O O   . THR A 61  ? 0.6613 0.3771 0.4595 -0.0684 0.0883  0.0204  62  THR A O   
559  C CB  . THR A 61  ? 0.6305 0.4031 0.4717 -0.0374 0.0629  0.0243  62  THR A CB  
560  O OG1 . THR A 61  ? 0.6020 0.3690 0.4514 -0.0269 0.0614  0.0232  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.5619 0.3647 0.4180 -0.0313 0.0535  0.0252  62  THR A CG2 
562  N N   . ASP A 62  ? 0.6027 0.3519 0.4359 -0.0723 0.0895  0.0049  63  ASP A N   
563  C CA  . ASP A 62  ? 0.6374 0.3564 0.4528 -0.0842 0.1016  0.0016  63  ASP A CA  
564  C C   . ASP A 62  ? 0.7135 0.4395 0.5243 -0.1044 0.1106  -0.0055 63  ASP A C   
565  O O   . ASP A 62  ? 0.6691 0.4301 0.5011 -0.1106 0.1086  -0.0148 63  ASP A O   
566  C CB  . ASP A 62  ? 0.6481 0.3713 0.4757 -0.0855 0.1043  -0.0070 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.8562 0.5505 0.6664 -0.1006 0.1178  -0.0125 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.9362 0.5927 0.7275 -0.0951 0.1217  -0.0068 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.8800 0.5889 0.6952 -0.1182 0.1245  -0.0231 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.7536 0.4452 0.5361 -0.1147 0.1207  -0.0020 64  GLN A N   
571  C CA  . GLN A 63  ? 0.7729 0.4673 0.5475 -0.1360 0.1320  -0.0094 64  GLN A CA  
572  C C   . GLN A 63  ? 0.8108 0.5318 0.6057 -0.1521 0.1387  -0.0265 64  GLN A C   
573  O O   . GLN A 63  ? 0.8260 0.5718 0.6310 -0.1648 0.1427  -0.0358 64  GLN A O   
574  C CB  . GLN A 63  ? 0.8474 0.4921 0.5826 -0.1458 0.1436  -0.0026 64  GLN A CB  
575  C CG  . GLN A 63  ? 1.1151 0.7381 0.8272 -0.1334 0.1364  0.0131  64  GLN A CG  
576  N N   . LEU A 64  ? 0.7251 0.4427 0.5268 -0.1516 0.1399  -0.0319 65  LEU A N   
577  C CA  . LEU A 64  ? 0.6970 0.4419 0.5180 -0.1659 0.1441  -0.0487 65  LEU A CA  
578  C C   . LEU A 64  ? 0.7025 0.4904 0.5539 -0.1552 0.1302  -0.0531 65  LEU A C   
579  O O   . LEU A 64  ? 0.7026 0.5234 0.5729 -0.1642 0.1292  -0.0658 65  LEU A O   
580  C CB  . LEU A 64  ? 0.7220 0.4422 0.5334 -0.1729 0.1526  -0.0539 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.8363 0.5206 0.6216 -0.1930 0.1703  -0.0579 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.8572 0.5172 0.6347 -0.1966 0.1770  -0.0625 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.8873 0.5981 0.6825 -0.2158 0.1794  -0.0737 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.6162 0.4027 0.4718 -0.1367 0.1198  -0.0441 66  LYS A N   
585  C CA  . LYS A 65  ? 0.5731 0.3934 0.4520 -0.1276 0.1077  -0.0476 66  LYS A CA  
586  C C   . LYS A 65  ? 0.6120 0.4600 0.5046 -0.1214 0.0986  -0.0456 66  LYS A C   
587  O O   . LYS A 65  ? 0.5660 0.4432 0.4770 -0.1188 0.0902  -0.0517 66  LYS A O   
588  C CB  . LYS A 65  ? 0.5892 0.3991 0.4678 -0.1126 0.1021  -0.0409 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.6024 0.3902 0.4720 -0.1179 0.1102  -0.0457 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.5480 0.3316 0.4211 -0.1030 0.1048  -0.0411 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.6547 0.4105 0.5168 -0.1058 0.1138  -0.0447 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.6451 0.3627 0.4884 -0.1005 0.1198  -0.0361 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.6188 0.4558 0.5005 -0.1189 0.1000  -0.0371 67  CYS A N   
594  C CA  . CYS A 66  ? 0.6141 0.4746 0.5067 -0.1138 0.0927  -0.0354 67  CYS A CA  
595  C C   . CYS A 66  ? 0.6635 0.5559 0.5746 -0.1244 0.0932  -0.0495 67  CYS A C   
596  O O   . CYS A 66  ? 0.6469 0.5645 0.5737 -0.1178 0.0846  -0.0511 67  CYS A O   
597  C CB  . CYS A 66  ? 0.6485 0.4890 0.5220 -0.1131 0.0961  -0.0257 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.7435 0.5645 0.5965 -0.1352 0.1130  -0.0314 67  CYS A SG  
599  N N   . ASN A 67  ? 0.6222 0.5133 0.5320 -0.1406 0.1032  -0.0608 68  ASN A N   
600  C CA  . ASN A 67  ? 0.6186 0.5410 0.5473 -0.1524 0.1052  -0.0772 68  ASN A CA  
601  C C   . ASN A 67  ? 0.6346 0.5808 0.5820 -0.1511 0.0972  -0.0878 68  ASN A C   
602  O O   . ASN A 67  ? 0.6188 0.5945 0.5848 -0.1587 0.0962  -0.1028 68  ASN A O   
603  C CB  . ASN A 67  ? 0.6555 0.5645 0.5715 -0.1734 0.1222  -0.0853 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.8594 0.7495 0.7563 -0.1766 0.1295  -0.0769 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.8700 0.7254 0.7401 -0.1871 0.1418  -0.0724 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.7007 0.6099 0.6079 -0.1676 0.1219  -0.0742 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.5802 0.5150 0.5229 -0.1416 0.0911  -0.0811 69  LEU A N   
608  C CA  . LEU A 68  ? 0.5603 0.5141 0.5155 -0.1404 0.0828  -0.0899 69  LEU A CA  
609  C C   . LEU A 68  ? 0.5605 0.5402 0.5317 -0.1268 0.0673  -0.0891 69  LEU A C   
610  O O   . LEU A 68  ? 0.5356 0.5095 0.5039 -0.1152 0.0626  -0.0776 69  LEU A O   
611  C CB  . LEU A 68  ? 0.5741 0.5039 0.5156 -0.1364 0.0837  -0.0836 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.6599 0.5601 0.5843 -0.1487 0.0984  -0.0852 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.6736 0.5522 0.5874 -0.1417 0.0983  -0.0794 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.6703 0.5846 0.6014 -0.1674 0.1054  -0.1028 69  LEU A CD2 
615  N N   . SER A 69  ? 0.4949 0.5020 0.4821 -0.1282 0.0588  -0.1016 70  SER A N   
616  C CA  A SER A 69  ? 0.4722 0.5009 0.4724 -0.1149 0.0429  -0.1019 70  SER A CA  
617  C CA  B SER A 69  ? 0.4764 0.5046 0.4763 -0.1147 0.0429  -0.1015 70  SER A CA  
618  C C   . SER A 69  ? 0.4912 0.5127 0.4829 -0.1073 0.0333  -0.0973 70  SER A C   
619  O O   . SER A 69  ? 0.4423 0.4709 0.4365 -0.0954 0.0206  -0.0935 70  SER A O   
620  C CB  A SER A 69  ? 0.5106 0.5736 0.5331 -0.1192 0.0377  -0.1190 70  SER A CB  
621  C CB  B SER A 69  ? 0.5211 0.5836 0.5436 -0.1184 0.0377  -0.1181 70  SER A CB  
622  O OG  A SER A 69  ? 0.5853 0.6572 0.6164 -0.1271 0.0475  -0.1247 70  SER A OG  
623  O OG  B SER A 69  ? 0.6206 0.6942 0.6475 -0.1285 0.0381  -0.1313 70  SER A OG  
624  N N   . VAL A 70  ? 0.4510 0.4564 0.4307 -0.1150 0.0404  -0.0983 71  VAL A N   
625  C CA  . VAL A 70  ? 0.4481 0.4448 0.4171 -0.1108 0.0343  -0.0954 71  VAL A CA  
626  C C   . VAL A 70  ? 0.4853 0.4517 0.4379 -0.1123 0.0456  -0.0868 71  VAL A C   
627  O O   . VAL A 70  ? 0.4858 0.4387 0.4335 -0.1222 0.0581  -0.0895 71  VAL A O   
628  C CB  . VAL A 70  ? 0.5170 0.5300 0.4900 -0.1190 0.0293  -0.1099 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.5279 0.5304 0.4860 -0.1156 0.0230  -0.1070 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.5093 0.5552 0.5019 -0.1159 0.0168  -0.1205 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.4219 0.3769 0.3658 -0.1025 0.0415  -0.0772 72  ILE A N   
632  C CA  . ILE A 71  ? 0.4232 0.3533 0.3549 -0.1014 0.0506  -0.0708 72  ILE A CA  
633  C C   . ILE A 71  ? 0.4643 0.3913 0.3868 -0.1013 0.0468  -0.0731 72  ILE A C   
634  O O   . ILE A 71  ? 0.4608 0.3955 0.3817 -0.0948 0.0367  -0.0701 72  ILE A O   
635  C CB  . ILE A 71  ? 0.4442 0.3641 0.3754 -0.0909 0.0520  -0.0586 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.4544 0.3748 0.3903 -0.0921 0.0561  -0.0560 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.4709 0.3688 0.3930 -0.0875 0.0597  -0.0539 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.5217 0.4238 0.4498 -0.1023 0.0689  -0.0588 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.4367 0.3500 0.3509 -0.1092 0.0556  -0.0785 73  ASN A N   
640  C CA  . ASN A 72  ? 0.4446 0.3535 0.3477 -0.1108 0.0539  -0.0816 73  ASN A CA  
641  C C   . ASN A 72  ? 0.4875 0.3770 0.3842 -0.1050 0.0620  -0.0752 73  ASN A C   
642  O O   . ASN A 72  ? 0.4859 0.3586 0.3820 -0.1059 0.0730  -0.0749 73  ASN A O   
643  C CB  . ASN A 72  ? 0.4947 0.4028 0.3929 -0.1239 0.0586  -0.0940 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.7246 0.6561 0.6324 -0.1303 0.0508  -0.1034 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.5939 0.5433 0.5036 -0.1264 0.0368  -0.1052 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.6751 0.6063 0.5887 -0.1405 0.0598  -0.1106 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.4220 0.3128 0.3132 -0.0996 0.0571  -0.0712 74  LEU A N   
648  C CA  . LEU A 73  ? 0.4279 0.3051 0.3162 -0.0948 0.0652  -0.0678 74  LEU A CA  
649  C C   . LEU A 73  ? 0.4959 0.3615 0.3731 -0.1026 0.0734  -0.0763 74  LEU A C   
650  O O   . LEU A 73  ? 0.5129 0.3826 0.3816 -0.1116 0.0701  -0.0837 74  LEU A O   
651  C CB  . LEU A 73  ? 0.4280 0.3108 0.3145 -0.0881 0.0591  -0.0615 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.4623 0.3554 0.3594 -0.0799 0.0518  -0.0533 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.4696 0.3630 0.3646 -0.0745 0.0507  -0.0482 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.4626 0.3525 0.3709 -0.0758 0.0568  -0.0500 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.4609 0.3136 0.3391 -0.0988 0.0835  -0.0764 75  ASP A N   
656  C CA  . ASP A 74  ? 0.4869 0.3273 0.3562 -0.1052 0.0935  -0.0853 75  ASP A CA  
657  C C   . ASP A 74  ? 0.5623 0.4088 0.4158 -0.1128 0.0886  -0.0894 75  ASP A C   
658  O O   . ASP A 74  ? 0.5397 0.3934 0.3902 -0.1091 0.0819  -0.0837 75  ASP A O   
659  C CB  . ASP A 74  ? 0.5112 0.3420 0.3882 -0.0963 0.1031  -0.0846 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.6605 0.4775 0.5316 -0.1012 0.1154  -0.0950 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.6770 0.4967 0.5368 -0.1086 0.1171  -0.1008 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.7249 0.5264 0.6012 -0.0974 0.1235  -0.0974 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.5829 0.4247 0.4239 -0.1239 0.0915  -0.0991 76  PRO A N   
664  C CA  . PRO A 75  ? 0.5969 0.4421 0.4181 -0.1313 0.0854  -0.1024 76  PRO A CA  
665  C C   . PRO A 75  ? 0.6445 0.4838 0.4558 -0.1307 0.0908  -0.1013 76  PRO A C   
666  O O   . PRO A 75  ? 0.6691 0.5092 0.4613 -0.1353 0.0837  -0.1004 76  PRO A O   
667  C CB  . PRO A 75  ? 0.6399 0.4794 0.4507 -0.1435 0.0904  -0.1145 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.6992 0.5265 0.5231 -0.1424 0.1037  -0.1180 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.6169 0.4485 0.4584 -0.1311 0.1001  -0.1076 76  PRO A CD  
670  N N   . GLU A 76  ? 0.5887 0.4222 0.4123 -0.1250 0.1028  -0.1018 77  GLU A N   
671  C CA  . GLU A 76  ? 0.6046 0.4360 0.4226 -0.1255 0.1099  -0.1031 77  GLU A CA  
672  C C   . GLU A 76  ? 0.6065 0.4466 0.4267 -0.1193 0.1012  -0.0928 77  GLU A C   
673  O O   . GLU A 76  ? 0.6036 0.4422 0.4145 -0.1227 0.1056  -0.0935 77  GLU A O   
674  C CB  . GLU A 76  ? 0.6350 0.4611 0.4697 -0.1201 0.1248  -0.1093 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.9045 0.7185 0.7318 -0.1283 0.1366  -0.1219 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.3502 1.1609 1.1579 -0.1399 0.1446  -0.1307 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.3775 1.1902 1.1928 -0.1377 0.1549  -0.1351 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.3494 1.1562 1.1337 -0.1517 0.1405  -0.1339 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.5299 0.3782 0.3618 -0.1115 0.0904  -0.0843 78  ILE A N   
680  C CA  . ILE A 77  ? 0.5159 0.3715 0.3506 -0.1055 0.0824  -0.0751 78  ILE A CA  
681  C C   . ILE A 77  ? 0.5752 0.4280 0.3857 -0.1114 0.0719  -0.0723 78  ILE A C   
682  O O   . ILE A 77  ? 0.5620 0.4160 0.3634 -0.1141 0.0622  -0.0731 78  ILE A O   
683  C CB  . ILE A 77  ? 0.5232 0.3878 0.3779 -0.0953 0.0757  -0.0679 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.5291 0.3916 0.4031 -0.0882 0.0853  -0.0694 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.4659 0.3377 0.3224 -0.0899 0.0674  -0.0594 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.5869 0.4504 0.4699 -0.0839 0.0952  -0.0722 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.5756 0.4245 0.3759 -0.1129 0.0737  -0.0693 79  ASN A N   
688  C CA  . ASN A 78  ? 0.5913 0.4311 0.3638 -0.1179 0.0648  -0.0651 79  ASN A CA  
689  C C   . ASN A 78  ? 0.5915 0.4371 0.3696 -0.1088 0.0498  -0.0556 79  ASN A C   
690  O O   . ASN A 78  ? 0.5528 0.4056 0.3491 -0.1020 0.0516  -0.0514 79  ASN A O   
691  C CB  . ASN A 78  ? 0.6331 0.4638 0.3926 -0.1251 0.0764  -0.0668 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.8714 0.6865 0.5980 -0.1308 0.0689  -0.0610 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.7554 0.5687 0.4819 -0.1276 0.0659  -0.0543 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.8014 0.6030 0.4972 -0.1395 0.0654  -0.0633 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.5708 0.4144 0.3339 -0.1079 0.0345  -0.0532 80  PRO A N   
696  C CA  . PRO A 79  ? 0.5588 0.4085 0.3291 -0.0981 0.0205  -0.0458 80  PRO A CA  
697  C C   . PRO A 79  ? 0.6058 0.4458 0.3677 -0.0963 0.0209  -0.0385 80  PRO A C   
698  O O   . PRO A 79  ? 0.5813 0.4299 0.3610 -0.0881 0.0170  -0.0340 80  PRO A O   
699  C CB  . PRO A 79  ? 0.6011 0.4482 0.3526 -0.0980 0.0042  -0.0465 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.6667 0.5139 0.4117 -0.1071 0.0100  -0.0555 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.6150 0.4521 0.3553 -0.1150 0.0285  -0.0581 80  PRO A CD  
702  N N   . GLU A 80  ? 0.5867 0.4082 0.3207 -0.1052 0.0266  -0.0381 81  GLU A N   
703  C CA  . GLU A 80  ? 0.5906 0.4006 0.3144 -0.1061 0.0289  -0.0323 81  GLU A CA  
704  C C   . GLU A 80  ? 0.5911 0.4156 0.3444 -0.1041 0.0415  -0.0341 81  GLU A C   
705  O O   . GLU A 80  ? 0.5616 0.3892 0.3244 -0.0984 0.0380  -0.0291 81  GLU A O   
706  C CB  . GLU A 80  ? 0.6440 0.4288 0.3284 -0.1188 0.0344  -0.0323 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.8164 0.5853 0.4858 -0.1209 0.0358  -0.0260 81  GLU A CG  
708  C CD  . GLU A 80  ? 1.2033 0.9458 0.8341 -0.1364 0.0461  -0.0267 81  GLU A CD  
709  O OE1 . GLU A 80  ? 1.2212 0.9409 0.8263 -0.1384 0.0419  -0.0196 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 1.1431 0.8858 0.7679 -0.1472 0.0594  -0.0348 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.5481 0.3817 0.3163 -0.1076 0.0549  -0.0417 82  GLY A N   
712  C CA  . GLY A 81  ? 0.5203 0.3695 0.3182 -0.1034 0.0649  -0.0444 82  GLY A CA  
713  C C   . GLY A 81  ? 0.5249 0.3884 0.3474 -0.0912 0.0557  -0.0394 82  GLY A C   
714  O O   . GLY A 81  ? 0.4873 0.3591 0.3248 -0.0865 0.0566  -0.0369 82  GLY A O   
715  N N   . PHE A 82  ? 0.4666 0.3333 0.2921 -0.0871 0.0469  -0.0387 83  PHE A N   
716  C CA  . PHE A 82  ? 0.4371 0.3165 0.2837 -0.0776 0.0395  -0.0349 83  PHE A CA  
717  C C   . PHE A 82  ? 0.4665 0.3448 0.3088 -0.0732 0.0293  -0.0284 83  PHE A C   
718  O O   . PHE A 82  ? 0.4362 0.3242 0.2958 -0.0671 0.0284  -0.0256 83  PHE A O   
719  C CB  . PHE A 82  ? 0.4502 0.3341 0.3003 -0.0766 0.0336  -0.0375 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.4433 0.3401 0.3147 -0.0690 0.0292  -0.0350 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.4650 0.3667 0.3539 -0.0657 0.0372  -0.0351 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.4488 0.3516 0.3215 -0.0648 0.0171  -0.0325 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.4613 0.3720 0.3652 -0.0600 0.0339  -0.0323 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.4567 0.3715 0.3481 -0.0593 0.0149  -0.0312 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.4327 0.3505 0.3379 -0.0579 0.0237  -0.0307 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.4878 0.3532 0.3064 -0.0756 0.0206  -0.0262 84  CYS A N   
727  C CA  . CYS A 83  ? 0.5139 0.3732 0.3248 -0.0705 0.0099  -0.0203 84  CYS A CA  
728  C C   . CYS A 83  ? 0.5223 0.3787 0.3359 -0.0721 0.0177  -0.0177 84  CYS A C   
729  O O   . CYS A 83  ? 0.4950 0.3576 0.3208 -0.0656 0.0131  -0.0146 84  CYS A O   
730  C CB  . CYS A 83  ? 0.5801 0.4200 0.3590 -0.0730 0.0000  -0.0182 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.6651 0.4928 0.4322 -0.0640 -0.0156 -0.0110 84  CYS A SG  
732  N N   . ILE A 84  ? 0.4799 0.3287 0.2835 -0.0815 0.0302  -0.0207 85  ILE A N   
733  C CA  . ILE A 84  ? 0.4615 0.3103 0.2687 -0.0856 0.0395  -0.0212 85  ILE A CA  
734  C C   . ILE A 84  ? 0.4558 0.3280 0.2969 -0.0781 0.0422  -0.0226 85  ILE A C   
735  O O   . ILE A 84  ? 0.4241 0.3007 0.2731 -0.0761 0.0417  -0.0208 85  ILE A O   
736  C CB  . ILE A 84  ? 0.5069 0.3474 0.2999 -0.0985 0.0541  -0.0272 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.5378 0.3490 0.2891 -0.1077 0.0516  -0.0240 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.4948 0.3472 0.3046 -0.1026 0.0667  -0.0324 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.6292 0.4319 0.3633 -0.1205 0.0642  -0.0308 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.4146 0.2993 0.2730 -0.0742 0.0447  -0.0258 86  LEU A N   
741  C CA  . LEU A 85  ? 0.3967 0.2997 0.2828 -0.0663 0.0460  -0.0262 86  LEU A CA  
742  C C   . LEU A 85  ? 0.4310 0.3398 0.3253 -0.0585 0.0354  -0.0210 86  LEU A C   
743  O O   . LEU A 85  ? 0.3988 0.3183 0.3080 -0.0539 0.0351  -0.0197 86  LEU A O   
744  C CB  . LEU A 85  ? 0.4062 0.3152 0.3044 -0.0644 0.0524  -0.0309 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.4876 0.3973 0.3867 -0.0703 0.0651  -0.0385 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.5050 0.4160 0.4127 -0.0678 0.0706  -0.0434 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.5025 0.4263 0.4187 -0.0682 0.0697  -0.0412 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.4012 0.3046 0.2866 -0.0572 0.0267  -0.0192 87  LEU A N   
749  C CA  . LEU A 86  ? 0.3794 0.2900 0.2736 -0.0505 0.0172  -0.0164 87  LEU A CA  
750  C C   . LEU A 86  ? 0.4270 0.3332 0.3165 -0.0492 0.0134  -0.0132 87  LEU A C   
751  O O   . LEU A 86  ? 0.4077 0.3238 0.3109 -0.0444 0.0114  -0.0120 87  LEU A O   
752  C CB  . LEU A 86  ? 0.3783 0.2864 0.2649 -0.0498 0.0083  -0.0176 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.4297 0.3491 0.3291 -0.0433 -0.0004 -0.0176 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.4022 0.3347 0.3211 -0.0418 0.0053  -0.0185 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.4842 0.4046 0.3779 -0.0424 -0.0103 -0.0211 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.4229 0.3119 0.2906 -0.0542 0.0131  -0.0120 88  ASP A N   
757  C CA  . ASP A 87  ? 0.4240 0.3034 0.2832 -0.0547 0.0114  -0.0092 88  ASP A CA  
758  C C   . ASP A 87  ? 0.4395 0.3310 0.3146 -0.0568 0.0204  -0.0112 88  ASP A C   
759  O O   . ASP A 87  ? 0.4255 0.3211 0.3080 -0.0535 0.0176  -0.0100 88  ASP A O   
760  C CB  . ASP A 87  ? 0.4802 0.3344 0.3084 -0.0624 0.0123  -0.0076 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.6764 0.5153 0.4847 -0.0581 -0.0008 -0.0045 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.6658 0.5157 0.4876 -0.0485 -0.0113 -0.0045 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.7291 0.5456 0.5080 -0.0645 -0.0008 -0.0028 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.4031 0.3020 0.2851 -0.0615 0.0307  -0.0153 89  PHE A N   
765  C CA  . PHE A 88  ? 0.3741 0.2890 0.2746 -0.0619 0.0378  -0.0188 89  PHE A CA  
766  C C   . PHE A 88  ? 0.3737 0.3053 0.2950 -0.0525 0.0323  -0.0170 89  PHE A C   
767  O O   . PHE A 88  ? 0.3452 0.2860 0.2760 -0.0513 0.0322  -0.0175 89  PHE A O   
768  C CB  . PHE A 88  ? 0.3839 0.3059 0.2911 -0.0660 0.0485  -0.0251 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.3781 0.3213 0.3093 -0.0627 0.0528  -0.0296 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.4002 0.3491 0.3342 -0.0687 0.0578  -0.0339 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.3860 0.3425 0.3357 -0.0532 0.0507  -0.0296 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.3866 0.3584 0.3442 -0.0647 0.0596  -0.0389 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.4073 0.3828 0.3775 -0.0480 0.0519  -0.0333 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.3869 0.3720 0.3623 -0.0534 0.0558  -0.0384 89  PHE A CZ  
775  N N   . MET A 89  ? 0.3373 0.2722 0.2640 -0.0472 0.0287  -0.0155 90  MET A N   
776  C CA  . MET A 89  ? 0.3150 0.2622 0.2569 -0.0400 0.0248  -0.0136 90  MET A CA  
777  C C   . MET A 89  ? 0.3684 0.3168 0.3105 -0.0380 0.0186  -0.0116 90  MET A C   
778  O O   . MET A 89  ? 0.3575 0.3168 0.3104 -0.0351 0.0182  -0.0114 90  MET A O   
779  C CB  . MET A 89  ? 0.3337 0.2793 0.2760 -0.0376 0.0224  -0.0128 90  MET A CB  
780  C CG  . MET A 89  ? 0.3623 0.3062 0.3064 -0.0384 0.0289  -0.0152 90  MET A CG  
781  S SD  . MET A 89  ? 0.4144 0.3559 0.3589 -0.0374 0.0269  -0.0150 90  MET A SD  
782  C CE  . MET A 89  ? 0.4151 0.3485 0.3558 -0.0403 0.0352  -0.0191 90  MET A CE  
783  N N   . TYR A 90  ? 0.3367 0.2732 0.2659 -0.0389 0.0132  -0.0104 91  TYR A N   
784  C CA  . TYR A 90  ? 0.3387 0.2745 0.2683 -0.0356 0.0068  -0.0095 91  TYR A CA  
785  C C   . TYR A 90  ? 0.3977 0.3247 0.3192 -0.0393 0.0086  -0.0096 91  TYR A C   
786  O O   . TYR A 90  ? 0.3896 0.3146 0.3116 -0.0363 0.0040  -0.0095 91  TYR A O   
787  C CB  . TYR A 90  ? 0.3547 0.2825 0.2762 -0.0323 -0.0017 -0.0093 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.3590 0.2999 0.2932 -0.0287 -0.0044 -0.0113 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.3716 0.3141 0.3058 -0.0311 -0.0017 -0.0124 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.3623 0.3138 0.3082 -0.0244 -0.0082 -0.0134 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.3636 0.3164 0.3079 -0.0301 -0.0026 -0.0152 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.3624 0.3256 0.3188 -0.0235 -0.0090 -0.0167 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.3858 0.3492 0.3410 -0.0269 -0.0060 -0.0175 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.3651 0.3389 0.3294 -0.0281 -0.0055 -0.0218 91  TYR A OH  
795  N N   . THR A 91  ? 0.3558 0.2764 0.2691 -0.0467 0.0161  -0.0109 92  THR A N   
796  C CA  . THR A 91  ? 0.3778 0.2871 0.2805 -0.0529 0.0193  -0.0118 92  THR A CA  
797  C C   . THR A 91  ? 0.4101 0.3317 0.3221 -0.0601 0.0293  -0.0169 92  THR A C   
798  O O   . THR A 91  ? 0.4153 0.3312 0.3219 -0.0664 0.0330  -0.0192 92  THR A O   
799  C CB  . THR A 91  ? 0.4773 0.3586 0.3517 -0.0583 0.0188  -0.0094 92  THR A CB  
800  O OG1 . THR A 91  ? 0.4630 0.3433 0.3318 -0.0650 0.0264  -0.0114 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.4787 0.3476 0.3427 -0.0501 0.0066  -0.0054 92  THR A CG2 
802  N N   . SER A 92  ? 0.3451 0.2814 0.2696 -0.0598 0.0342  -0.0198 93  SER A N   
803  C CA  . SER A 92  ? 0.3314 0.2827 0.2677 -0.0654 0.0434  -0.0269 93  SER A CA  
804  C C   . SER A 92  ? 0.3903 0.3269 0.3094 -0.0777 0.0530  -0.0307 93  SER A C   
805  O O   . SER A 92  ? 0.3933 0.3428 0.3222 -0.0841 0.0623  -0.0388 93  SER A O   
806  C CB  . SER A 92  ? 0.3359 0.3005 0.2836 -0.0667 0.0437  -0.0305 93  SER A CB  
807  O OG  . SER A 92  ? 0.4305 0.4048 0.3886 -0.0574 0.0353  -0.0268 93  SER A OG  
808  N N   A ARG A 93  ? 0.3866 0.2968 0.2797 -0.0808 0.0506  -0.0257 94  ARG A N   
809  N N   B ARG A 93  ? 0.3774 0.2873 0.2702 -0.0811 0.0508  -0.0257 94  ARG A N   
810  C CA  A ARG A 93  ? 0.4192 0.3089 0.2881 -0.0936 0.0593  -0.0278 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.4044 0.2949 0.2740 -0.0942 0.0600  -0.0283 94  ARG A CA  
812  C C   A ARG A 93  ? 0.4689 0.3546 0.3308 -0.0940 0.0613  -0.0280 94  ARG A C   
813  C C   B ARG A 93  ? 0.4649 0.3495 0.3257 -0.0945 0.0615  -0.0280 94  ARG A C   
814  O O   A ARG A 93  ? 0.4451 0.3250 0.3024 -0.0861 0.0520  -0.0225 94  ARG A O   
815  O O   B ARG A 93  ? 0.4486 0.3262 0.3035 -0.0867 0.0518  -0.0221 94  ARG A O   
816  C CB  A ARG A 93  ? 0.4842 0.3421 0.3230 -0.0968 0.0543  -0.0216 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.4448 0.3043 0.2847 -0.0997 0.0574  -0.0234 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.5755 0.4326 0.4178 -0.0980 0.0537  -0.0222 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.4670 0.3299 0.3128 -0.1045 0.0609  -0.0268 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.6778 0.5022 0.4927 -0.0958 0.0453  -0.0149 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.6344 0.4657 0.4542 -0.1051 0.0551  -0.0207 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.7489 0.5397 0.5274 -0.1072 0.0506  -0.0129 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.6843 0.5198 0.5114 -0.1099 0.0591  -0.0250 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.9141 0.6860 0.6738 -0.1217 0.0613  -0.0159 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.8748 0.6806 0.6767 -0.1187 0.0625  -0.0241 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.7491 0.4870 0.4713 -0.1328 0.0664  -0.0134 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.7440 0.5562 0.5549 -0.1237 0.0667  -0.0293 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.7761 0.5620 0.5525 -0.1262 0.0673  -0.0219 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.7339 0.5016 0.4993 -0.1228 0.0615  -0.0180 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.4342 0.3241 0.2961 -0.1042 0.0742  -0.0359 95  LEU A N   
831  C CA  . LEU A 94  ? 0.4341 0.3204 0.2893 -0.1065 0.0786  -0.0382 95  LEU A CA  
832  C C   . LEU A 94  ? 0.5334 0.3928 0.3540 -0.1219 0.0870  -0.0394 95  LEU A C   
833  O O   . LEU A 94  ? 0.5225 0.3818 0.3394 -0.1349 0.0999  -0.0468 95  LEU A O   
834  C CB  . LEU A 94  ? 0.4168 0.3315 0.3026 -0.1041 0.0869  -0.0479 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.4694 0.3834 0.3539 -0.1044 0.0918  -0.0517 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.4542 0.3663 0.3416 -0.0920 0.0800  -0.0443 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.4715 0.4103 0.3834 -0.1040 0.1026  -0.0639 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.5360 0.3725 0.3299 -0.1211 0.0797  -0.0327 96  ASN A N   
839  C CA  . ASN A 95  ? 0.5757 0.3815 0.3297 -0.1350 0.0856  -0.0320 96  ASN A CA  
840  C C   . ASN A 95  ? 0.6352 0.4483 0.3902 -0.1440 0.0990  -0.0414 96  ASN A C   
841  O O   . ASN A 95  ? 0.6423 0.4472 0.3842 -0.1428 0.0954  -0.0398 96  ASN A O   
842  C CB  . ASN A 95  ? 0.6325 0.4117 0.3571 -0.1287 0.0696  -0.0212 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.9097 0.6519 0.5865 -0.1419 0.0729  -0.0185 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.7913 0.5204 0.4508 -0.1577 0.0873  -0.0228 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.8259 0.5503 0.4790 -0.1365 0.0597  -0.0118 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.5835 0.4148 0.3569 -0.1525 0.1145  -0.0526 97  LEU A N   
847  C CA  . LEU A 96  ? 0.5889 0.4318 0.3700 -0.1601 0.1289  -0.0644 97  LEU A CA  
848  C C   . LEU A 96  ? 0.6653 0.4827 0.4087 -0.1813 0.1429  -0.0687 97  LEU A C   
849  O O   . LEU A 96  ? 0.6635 0.4720 0.3956 -0.1933 0.1510  -0.0710 97  LEU A O   
850  C CB  . LEU A 96  ? 0.5730 0.4531 0.3982 -0.1560 0.1368  -0.0759 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.6417 0.5435 0.4910 -0.1540 0.1465  -0.0882 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.6396 0.5396 0.4930 -0.1401 0.1357  -0.0819 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.6305 0.5685 0.5228 -0.1474 0.1508  -0.0988 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.6398 0.4422 0.3599 -0.1870 0.1458  -0.0696 98  ARG A N   
855  C CA  . ARG A 97  ? 0.6884 0.4621 0.3656 -0.2082 0.1592  -0.0731 98  ARG A CA  
856  C C   . ARG A 97  ? 0.7245 0.5085 0.4062 -0.2158 0.1731  -0.0857 98  ARG A C   
857  O O   . ARG A 97  ? 0.6955 0.4988 0.4032 -0.2026 0.1677  -0.0876 98  ARG A O   
858  C CB  . ARG A 97  ? 0.7348 0.4673 0.3627 -0.2086 0.1449  -0.0581 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.8698 0.5878 0.4904 -0.1999 0.1301  -0.0457 98  ARG A CG  
860  C CD  . ARG A 97  ? 1.1096 0.7904 0.6868 -0.1951 0.1124  -0.0316 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.3933 1.0353 0.9163 -0.2138 0.1207  -0.0307 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.6575 1.2660 1.1439 -0.2280 0.1280  -0.0276 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.5333 1.1042 0.9668 -0.2457 0.1360  -0.0265 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.5002 1.1104 1.0000 -0.2257 0.1279  -0.0257 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.7086 0.4782 0.3636 -0.2378 0.1921  -0.0950 99  GLU A N   
866  C CA  . GLU A 98  ? 0.7143 0.4921 0.3709 -0.2470 0.2075  -0.1088 99  GLU A CA  
867  C C   . GLU A 98  ? 0.7838 0.5509 0.4265 -0.2380 0.1950  -0.1021 99  GLU A C   
868  O O   . GLU A 98  ? 0.7644 0.5523 0.4328 -0.2326 0.2001  -0.1118 99  GLU A O   
869  C CB  . GLU A 98  ? 0.7810 0.5347 0.3968 -0.2748 0.2283  -0.1170 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.9390 0.7046 0.5596 -0.2865 0.2478  -0.1347 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.4115 1.1517 0.9881 -0.3161 0.2699  -0.1436 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.4613 1.1573 0.9809 -0.3269 0.2648  -0.1305 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.4419 1.2059 1.0405 -0.3284 0.2925  -0.1642 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.7793 0.5148 0.3829 -0.2357 0.1784  -0.0865 100 GLY A N   
875  C CA  . GLY A 99  ? 0.7887 0.5135 0.3757 -0.2285 0.1648  -0.0803 100 GLY A CA  
876  C C   . GLY A 99  ? 0.7851 0.5342 0.4108 -0.2063 0.1489  -0.0762 100 GLY A C   
877  O O   . GLY A 99  ? 0.7778 0.5241 0.3968 -0.2016 0.1406  -0.0748 100 GLY A O   
878  N N   . ASN A 100 ? 0.6994 0.4717 0.3640 -0.1935 0.1449  -0.0746 101 ASN A N   
879  C CA  . ASN A 100 ? 0.6506 0.4427 0.3481 -0.1740 0.1308  -0.0703 101 ASN A CA  
880  C C   . ASN A 100 ? 0.6598 0.4850 0.4063 -0.1650 0.1387  -0.0795 101 ASN A C   
881  O O   . ASN A 100 ? 0.6199 0.4589 0.3911 -0.1503 0.1294  -0.0768 101 ASN A O   
882  C CB  . ASN A 100 ? 0.6339 0.4183 0.3269 -0.1628 0.1116  -0.0561 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.7057 0.4982 0.4148 -0.1611 0.1137  -0.0546 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.5891 0.4049 0.3290 -0.1614 0.1251  -0.0635 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.6140 0.3889 0.3048 -0.1581 0.1016  -0.0438 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.6186 0.4563 0.3787 -0.1735 0.1552  -0.0906 102 ILE A N   
887  C CA  . ILE A 101 ? 0.5823 0.4527 0.3895 -0.1632 0.1605  -0.0996 102 ILE A CA  
888  C C   . ILE A 101 ? 0.5995 0.4823 0.4296 -0.1524 0.1609  -0.1053 102 ILE A C   
889  O O   . ILE A 101 ? 0.5527 0.4532 0.4147 -0.1362 0.1537  -0.1035 102 ILE A O   
890  C CB  . ILE A 101 ? 0.6243 0.5094 0.4435 -0.1752 0.1787  -0.1137 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.6069 0.5281 0.4770 -0.1607 0.1795  -0.1221 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.6142 0.4902 0.4131 -0.1938 0.1978  -0.1268 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.6171 0.5570 0.5038 -0.1677 0.1883  -0.1309 102 ILE A CD1 
894  N N   . MET A 102 ? 0.5912 0.4623 0.4030 -0.1614 0.1691  -0.1118 103 MET A N   
895  C CA  . MET A 102 ? 0.5898 0.4687 0.4207 -0.1522 0.1707  -0.1179 103 MET A CA  
896  C C   . MET A 102 ? 0.6046 0.4786 0.4378 -0.1388 0.1531  -0.1057 103 MET A C   
897  O O   . MET A 102 ? 0.5652 0.4518 0.4272 -0.1250 0.1505  -0.1068 103 MET A O   
898  C CB  . MET A 102 ? 0.6578 0.5250 0.4674 -0.1666 0.1847  -0.1292 103 MET A CB  
899  C CG  . MET A 102 ? 0.7421 0.6182 0.5548 -0.1807 0.2055  -0.1451 103 MET A CG  
900  S SD  . MET A 102 ? 0.7894 0.7035 0.6590 -0.1679 0.2140  -0.1590 103 MET A SD  
901  C CE  . MET A 102 ? 0.7481 0.6677 0.6411 -0.1549 0.2173  -0.1686 103 MET A CE  
902  N N   . ALA A 103 ? 0.5859 0.4416 0.3888 -0.1424 0.1407  -0.0942 104 ALA A N   
903  C CA  . ALA A 103 ? 0.5735 0.4268 0.3784 -0.1315 0.1242  -0.0841 104 ALA A CA  
904  C C   . ALA A 103 ? 0.5770 0.4454 0.4093 -0.1176 0.1155  -0.0770 104 ALA A C   
905  O O   . ALA A 103 ? 0.5437 0.4193 0.3949 -0.1065 0.1095  -0.0746 104 ALA A O   
906  C CB  . ALA A 103 ? 0.6059 0.4396 0.3745 -0.1378 0.1125  -0.0754 104 ALA A CB  
907  N N   . VAL A 104 ? 0.5069 0.3786 0.3395 -0.1196 0.1158  -0.0743 105 VAL A N   
908  C CA  . VAL A 104 ? 0.4651 0.3515 0.3219 -0.1079 0.1081  -0.0685 105 VAL A CA  
909  C C   . VAL A 104 ? 0.4843 0.3905 0.3758 -0.0973 0.1133  -0.0752 105 VAL A C   
910  O O   . VAL A 104 ? 0.4531 0.3656 0.3605 -0.0850 0.1042  -0.0693 105 VAL A O   
911  C CB  . VAL A 104 ? 0.5132 0.3977 0.3615 -0.1139 0.1084  -0.0656 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.4793 0.3818 0.3547 -0.1027 0.1023  -0.0622 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.5313 0.3922 0.3448 -0.1195 0.0989  -0.0563 105 VAL A CG2 
914  N N   A MET A 105 ? 0.4576 0.3727 0.3600 -0.1017 0.1275  -0.0878 106 MET A N   
915  N N   B MET A 105 ? 0.4617 0.3769 0.3642 -0.1016 0.1274  -0.0878 106 MET A N   
916  C CA  A MET A 105 ? 0.4580 0.3915 0.3939 -0.0893 0.1311  -0.0951 106 MET A CA  
917  C CA  B MET A 105 ? 0.4588 0.3924 0.3948 -0.0893 0.1311  -0.0952 106 MET A CA  
918  C C   A MET A 105 ? 0.4968 0.4226 0.4370 -0.0799 0.1273  -0.0932 106 MET A C   
919  C C   B MET A 105 ? 0.5005 0.4264 0.4408 -0.0799 0.1273  -0.0932 106 MET A C   
920  O O   A MET A 105 ? 0.4669 0.3999 0.4274 -0.0656 0.1212  -0.0901 106 MET A O   
921  O O   B MET A 105 ? 0.4757 0.4087 0.4360 -0.0656 0.1210  -0.0899 106 MET A O   
922  C CB  A MET A 105 ? 0.5026 0.4488 0.4508 -0.0957 0.1475  -0.1115 106 MET A CB  
923  C CB  B MET A 105 ? 0.5037 0.4500 0.4520 -0.0957 0.1475  -0.1115 106 MET A CB  
924  C CG  A MET A 105 ? 0.5406 0.5084 0.5264 -0.0800 0.1487  -0.1196 106 MET A CG  
925  C CG  B MET A 105 ? 0.5429 0.5109 0.5288 -0.0801 0.1487  -0.1196 106 MET A CG  
926  S SD  A MET A 105 ? 0.6099 0.6011 0.6178 -0.0866 0.1671  -0.1415 106 MET A SD  
927  S SD  B MET A 105 ? 0.6146 0.6039 0.6215 -0.0865 0.1679  -0.1420 106 MET A SD  
928  C CE  A MET A 105 ? 0.5932 0.5679 0.5865 -0.0949 0.1809  -0.1519 106 MET A CE  
929  C CE  B MET A 105 ? 0.5700 0.5694 0.6104 -0.0639 0.1655  -0.1486 106 MET A CE  
930  N N   . ALA A 106 ? 0.4768 0.3865 0.3960 -0.0886 0.1311  -0.0953 107 ALA A N   
931  C CA  . ALA A 106 ? 0.4754 0.3752 0.3954 -0.0829 0.1292  -0.0949 107 ALA A CA  
932  C C   . ALA A 106 ? 0.4835 0.3797 0.4028 -0.0753 0.1147  -0.0821 107 ALA A C   
933  O O   . ALA A 106 ? 0.4649 0.3599 0.3977 -0.0648 0.1123  -0.0804 107 ALA A O   
934  C CB  . ALA A 106 ? 0.5063 0.3910 0.4013 -0.0962 0.1355  -0.1003 107 ALA A CB  
935  N N   . THR A 107 ? 0.4391 0.3331 0.3431 -0.0801 0.1056  -0.0736 108 THR A N   
936  C CA  . THR A 107 ? 0.4214 0.3150 0.3264 -0.0737 0.0927  -0.0633 108 THR A CA  
937  C C   . THR A 107 ? 0.4585 0.3645 0.3862 -0.0616 0.0889  -0.0591 108 THR A C   
938  O O   . THR A 107 ? 0.4352 0.3395 0.3699 -0.0541 0.0838  -0.0544 108 THR A O   
939  C CB  . THR A 107 ? 0.4916 0.3798 0.3756 -0.0803 0.0835  -0.0568 108 THR A CB  
940  O OG1 . THR A 107 ? 0.5096 0.3857 0.3699 -0.0914 0.0867  -0.0612 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.4673 0.3565 0.3532 -0.0750 0.0714  -0.0495 108 THR A CG2 
942  N N   . ALA A 108 ? 0.4092 0.3272 0.3471 -0.0606 0.0921  -0.0616 109 ALA A N   
943  C CA  . ALA A 108 ? 0.3874 0.3193 0.3464 -0.0492 0.0877  -0.0588 109 ALA A CA  
944  C C   . ALA A 108 ? 0.4082 0.3412 0.3843 -0.0377 0.0902  -0.0625 109 ALA A C   
945  O O   . ALA A 108 ? 0.3846 0.3192 0.3693 -0.0272 0.0831  -0.0563 109 ALA A O   
946  C CB  . ALA A 108 ? 0.3951 0.3413 0.3616 -0.0528 0.0915  -0.0634 109 ALA A CB  
947  N N   . MET A 109 ? 0.3950 0.3242 0.3733 -0.0395 0.1004  -0.0723 110 MET A N   
948  C CA  . MET A 109 ? 0.4111 0.3370 0.4041 -0.0271 0.1028  -0.0762 110 MET A CA  
949  C C   . MET A 109 ? 0.4532 0.3599 0.4354 -0.0242 0.0976  -0.0681 110 MET A C   
950  O O   . MET A 109 ? 0.4587 0.3608 0.4485 -0.0120 0.0927  -0.0635 110 MET A O   
951  C CB  . MET A 109 ? 0.4588 0.3840 0.4558 -0.0309 0.1159  -0.0900 110 MET A CB  
952  C CG  . MET A 109 ? 0.5203 0.4678 0.5364 -0.0302 0.1223  -0.1008 110 MET A CG  
953  S SD  . MET A 109 ? 0.6238 0.5712 0.6407 -0.0396 0.1404  -0.1189 110 MET A SD  
954  C CE  . MET A 109 ? 0.5964 0.5341 0.6302 -0.0213 0.1410  -0.1235 110 MET A CE  
955  N N   . TYR A 110 ? 0.4204 0.3160 0.3835 -0.0359 0.0983  -0.0667 111 TYR A N   
956  C CA  . TYR A 110 ? 0.4243 0.3043 0.3765 -0.0373 0.0949  -0.0614 111 TYR A CA  
957  C C   . TYR A 110 ? 0.4464 0.3301 0.3998 -0.0325 0.0843  -0.0505 111 TYR A C   
958  O O   . TYR A 110 ? 0.4386 0.3114 0.3916 -0.0271 0.0824  -0.0461 111 TYR A O   
959  C CB  . TYR A 110 ? 0.4448 0.3191 0.3784 -0.0515 0.0963  -0.0641 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.4634 0.3280 0.3871 -0.0557 0.0920  -0.0603 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.4997 0.3484 0.4210 -0.0561 0.0979  -0.0640 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.4560 0.3273 0.3727 -0.0604 0.0827  -0.0547 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.4724 0.3136 0.3852 -0.0624 0.0954  -0.0624 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.4533 0.3200 0.3639 -0.0654 0.0794  -0.0541 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.4800 0.3324 0.3887 -0.0675 0.0864  -0.0582 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.4870 0.3366 0.3902 -0.0749 0.0846  -0.0595 111 TYR A OH  
967  N N   . LEU A 111 ? 0.4024 0.2996 0.3558 -0.0350 0.0784  -0.0467 112 LEU A N   
968  C CA  . LEU A 111 ? 0.3790 0.2811 0.3337 -0.0315 0.0693  -0.0379 112 LEU A CA  
969  C C   . LEU A 111 ? 0.4174 0.3259 0.3859 -0.0191 0.0663  -0.0348 112 LEU A C   
970  O O   . LEU A 111 ? 0.4063 0.3166 0.3746 -0.0158 0.0596  -0.0277 112 LEU A O   
971  C CB  . LEU A 111 ? 0.3618 0.2734 0.3105 -0.0380 0.0640  -0.0356 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.4148 0.3203 0.3476 -0.0482 0.0623  -0.0369 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.4087 0.3202 0.3347 -0.0513 0.0553  -0.0335 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.4247 0.3239 0.3542 -0.0496 0.0595  -0.0353 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.3935 0.3075 0.3745 -0.0125 0.0708  -0.0410 113 GLN A N   
976  C CA  . GLN A 112 ? 0.3919 0.3150 0.3882 0.0010  0.0666  -0.0400 113 GLN A CA  
977  C C   . GLN A 112 ? 0.4119 0.3532 0.4132 0.0000  0.0602  -0.0368 113 GLN A C   
978  O O   . GLN A 112 ? 0.3962 0.3383 0.3965 0.0050  0.0525  -0.0294 113 GLN A O   
979  C CB  . GLN A 112 ? 0.4173 0.3231 0.4088 0.0106  0.0624  -0.0331 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.4875 0.3719 0.4735 0.0119  0.0696  -0.0370 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.6199 0.4808 0.5925 0.0159  0.0668  -0.0287 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.5239 0.3840 0.4951 0.0236  0.0591  -0.0210 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.5884 0.4285 0.5488 0.0091  0.0735  -0.0304 113 GLN A NE2 
984  N N   . MET A 113 ? 0.3642 0.3176 0.3682 -0.0081 0.0644  -0.0427 114 MET A N   
985  C CA  . MET A 113 ? 0.3547 0.3234 0.3622 -0.0115 0.0606  -0.0416 114 MET A CA  
986  C C   . MET A 113 ? 0.4253 0.4124 0.4509 -0.0094 0.0661  -0.0523 114 MET A C   
987  O O   . MET A 113 ? 0.4083 0.3984 0.4316 -0.0197 0.0747  -0.0598 114 MET A O   
988  C CB  . MET A 113 ? 0.3739 0.3357 0.3642 -0.0247 0.0618  -0.0397 114 MET A CB  
989  C CG  . MET A 113 ? 0.4066 0.3556 0.3836 -0.0259 0.0557  -0.0316 114 MET A CG  
990  S SD  . MET A 113 ? 0.4532 0.3937 0.4106 -0.0381 0.0546  -0.0304 114 MET A SD  
991  C CE  . MET A 113 ? 0.4072 0.3580 0.3668 -0.0390 0.0496  -0.0276 114 MET A CE  
992  N N   . GLU A 114 ? 0.4209 0.4191 0.4640 0.0042  0.0614  -0.0539 115 GLU A N   
993  C CA  . GLU A 114 ? 0.4368 0.4561 0.5031 0.0101  0.0652  -0.0662 115 GLU A CA  
994  C C   . GLU A 114 ? 0.4447 0.4849 0.5191 -0.0007 0.0704  -0.0746 115 GLU A C   
995  O O   . GLU A 114 ? 0.4319 0.4845 0.5189 -0.0045 0.0801  -0.0876 115 GLU A O   
996  C CB  . GLU A 114 ? 0.4705 0.4980 0.5521 0.0287  0.0550  -0.0646 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.6601 0.6630 0.7324 0.0395  0.0518  -0.0578 115 GLU A CG  
998  N N   . HIS A 115 ? 0.3869 0.4299 0.4536 -0.0068 0.0653  -0.0685 116 HIS A N   
999  C CA  . HIS A 115 ? 0.3985 0.4574 0.4700 -0.0187 0.0712  -0.0765 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.4322 0.4777 0.4862 -0.0353 0.0832  -0.0801 116 HIS A C   
1001 O O   . HIS A 115 ? 0.4316 0.4899 0.4933 -0.0447 0.0937  -0.0923 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.4141 0.4770 0.4810 -0.0205 0.0630  -0.0696 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.4612 0.5411 0.5450 -0.0062 0.0521  -0.0686 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.4918 0.5991 0.6016 0.0004  0.0521  -0.0807 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.4846 0.5582 0.5614 0.0016  0.0410  -0.0577 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.4832 0.5984 0.5994 0.0134  0.0394  -0.0757 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.4861 0.5803 0.5814 0.0137  0.0331  -0.0616 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.3722 0.3927 0.4027 -0.0391 0.0819  -0.0709 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.3769 0.3811 0.3861 -0.0536 0.0911  -0.0730 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.4474 0.4560 0.4654 -0.0551 0.1027  -0.0851 117 VAL A C   
1011 O O   . VAL A 116 ? 0.4296 0.4392 0.4415 -0.0685 0.1145  -0.0942 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.4203 0.4002 0.4046 -0.0557 0.0848  -0.0615 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.4297 0.3925 0.3901 -0.0695 0.0929  -0.0641 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.4080 0.3849 0.3848 -0.0551 0.0749  -0.0519 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.3997 0.4097 0.4311 -0.0417 0.1001  -0.0859 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.4006 0.4150 0.4436 -0.0405 0.1108  -0.0985 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.4604 0.5024 0.5271 -0.0432 0.1194  -0.1141 118 VAL A C   
1018 O O   . VAL A 117 ? 0.4535 0.4977 0.5183 -0.0549 0.1335  -0.1260 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.4336 0.4426 0.4876 -0.0234 0.1054  -0.0964 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.4362 0.4495 0.5038 -0.0212 0.1169  -0.1110 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.4338 0.4168 0.4645 -0.0242 0.0994  -0.0835 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.4255 0.4897 0.5150 -0.0324 0.1114  -0.1153 119 ASP A N   
1023 N N   B ASP A 118 ? 0.4125 0.4757 0.4991 -0.0346 0.1115  -0.1144 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.4307 0.5271 0.5483 -0.0330 0.1176  -0.1317 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.4128 0.5074 0.5257 -0.0366 0.1177  -0.1301 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.4919 0.5921 0.5993 -0.0556 0.1314  -0.1402 119 ASP A C   
1027 C C   B ASP A 118 ? 0.4511 0.5457 0.5501 -0.0597 0.1313  -0.1372 119 ASP A C   
1028 O O   A ASP A 118 ? 0.5012 0.6209 0.6256 -0.0623 0.1444  -0.1578 119 ASP A O   
1029 O O   B ASP A 118 ? 0.4500 0.5594 0.5614 -0.0680 0.1455  -0.1539 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.4451 0.5622 0.5827 -0.0192 0.1037  -0.1289 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.4263 0.5406 0.5571 -0.0242 0.1040  -0.1266 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.6018 0.7230 0.7573 0.0045  0.0925  -0.1271 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.5953 0.7474 0.7586 -0.0236 0.1080  -0.1445 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.6406 0.7661 0.8111 0.0120  0.0982  -0.1377 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.6311 0.8004 0.8190 -0.0152 0.1129  -0.1586 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.6652 0.7833 0.8181 0.0155  0.0781  -0.1154 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.6478 0.8132 0.8132 -0.0312 0.1063  -0.1456 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.4493 0.5292 0.5278 -0.0675 0.1290  -0.1282 120 THR A N   
1039 N N   B THR A 119 ? 0.4037 0.4800 0.4759 -0.0705 0.1279  -0.1253 120 THR A N   
1040 C CA  A THR A 119 ? 0.4596 0.5336 0.5196 -0.0894 0.1408  -0.1330 120 THR A CA  
1041 C CA  B THR A 119 ? 0.4157 0.4852 0.4691 -0.0926 0.1406  -0.1307 120 THR A CA  
1042 C C   A THR A 119 ? 0.5112 0.5653 0.5481 -0.1033 0.1541  -0.1369 120 THR A C   
1043 C C   B THR A 119 ? 0.4889 0.5379 0.5190 -0.1057 0.1535  -0.1344 120 THR A C   
1044 O O   A THR A 119 ? 0.5164 0.5768 0.5516 -0.1197 0.1698  -0.1503 120 THR A O   
1045 O O   B THR A 119 ? 0.4939 0.5441 0.5161 -0.1237 0.1686  -0.1455 120 THR A O   
1046 C CB  A THR A 119 ? 0.5787 0.6356 0.6164 -0.0934 0.1314  -0.1182 120 THR A CB  
1047 C CB  B THR A 119 ? 0.4229 0.4755 0.4529 -0.0994 0.1333  -0.1178 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.5678 0.6453 0.6289 -0.0794 0.1196  -0.1162 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.4468 0.4976 0.4648 -0.1199 0.1467  -0.1263 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.5863 0.6351 0.6048 -0.1146 0.1423  -0.1225 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.3333 0.3522 0.3310 -0.0990 0.1255  -0.1014 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.4655 0.4956 0.4836 -0.0981 0.1484  -0.1262 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.4831 0.4934 0.4776 -0.1101 0.1594  -0.1297 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.5529 0.5842 0.5713 -0.1118 0.1743  -0.1494 121 CYS A C   
1055 O O   . CYS A 120 ? 0.5612 0.5879 0.5654 -0.1300 0.1903  -0.1598 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.4826 0.4718 0.4625 -0.1011 0.1496  -0.1177 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.5308 0.4932 0.4772 -0.1036 0.1350  -0.0978 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.5058 0.5603 0.5606 -0.0926 0.1691  -0.1552 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.5136 0.5930 0.5993 -0.0891 0.1810  -0.1756 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.5659 0.6697 0.6641 -0.1049 0.1951  -0.1924 122 ARG A C   
1061 O O   . ARG A 121 ? 0.5646 0.6758 0.6663 -0.1172 0.2130  -0.2095 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.5204 0.6188 0.6412 -0.0631 0.1685  -0.1763 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.7189 0.7956 0.8329 -0.0496 0.1621  -0.1680 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.8894 0.9841 1.0388 -0.0288 0.1605  -0.1796 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.9946 1.0848 1.1510 -0.0073 0.1419  -0.1660 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.1116 1.1745 1.2534 0.0023  0.1349  -0.1542 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8624 0.9024 0.9841 -0.0071 0.1441  -0.1546 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.9468 1.0045 1.0925 0.0199  0.1192  -0.1424 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.5179 0.6335 0.6215 -0.1062 0.1882  -0.1884 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.5239 0.6627 0.6391 -0.1225 0.2012  -0.2043 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.5901 0.7033 0.6659 -0.1506 0.2178  -0.2054 123 LYS A C   
1072 O O   . LYS A 122 ? 0.5831 0.7115 0.6664 -0.1672 0.2367  -0.2246 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.5400 0.6942 0.6674 -0.1172 0.1888  -0.1987 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.7388 0.9251 0.9081 -0.0917 0.1747  -0.2027 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.8712 1.0776 1.0536 -0.0900 0.1650  -0.2015 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.9777 1.1995 1.1840 -0.0631 0.1445  -0.1949 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 1.0643 1.3191 1.3115 -0.0462 0.1439  -0.2121 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.5644 0.6384 0.5975 -0.1560 0.2105  -0.1854 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.6011 0.6434 0.5894 -0.1807 0.2229  -0.1832 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.6737 0.7080 0.6508 -0.1905 0.2384  -0.1940 124 PHE A C   
1081 O O   . PHE A 123 ? 0.6865 0.7124 0.6428 -0.2140 0.2570  -0.2045 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.6319 0.6368 0.5813 -0.1793 0.2078  -0.1596 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.6616 0.6613 0.6025 -0.1834 0.2013  -0.1514 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.6829 0.7137 0.6600 -0.1721 0.1941  -0.1551 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.7272 0.6888 0.6225 -0.1969 0.2006  -0.1394 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.6922 0.7175 0.6609 -0.1766 0.1887  -0.1484 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.7574 0.7114 0.6445 -0.1998 0.1947  -0.1322 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.7017 0.6881 0.6260 -0.1904 0.1896  -0.1372 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.6186 0.6554 0.6095 -0.1737 0.2321  -0.1930 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.6388 0.6701 0.6229 -0.1811 0.2466  -0.2048 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.7027 0.7697 0.7222 -0.1875 0.2660  -0.2318 125 ILE A C   
1092 O O   . ILE A 124 ? 0.7232 0.7842 0.7258 -0.2083 0.2861  -0.2451 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.6642 0.6860 0.6524 -0.1619 0.2348  -0.1965 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.6686 0.6534 0.6147 -0.1633 0.2210  -0.1742 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.6941 0.7184 0.6874 -0.1661 0.2507  -0.2133 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.7377 0.7164 0.6918 -0.1427 0.2048  -0.1627 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.6501 0.7547 0.7178 -0.1700 0.2597  -0.2404 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.6565 0.8028 0.7667 -0.1719 0.2749  -0.2677 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.7305 0.8833 0.8290 -0.2012 0.2946  -0.2811 126 LYS A C   
1100 O O   . LYS A 125 ? 0.7365 0.9093 0.8498 -0.2146 0.3158  -0.3049 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.6660 0.8488 0.8257 -0.1455 0.2592  -0.2710 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.8636 1.0911 1.0741 -0.1384 0.2702  -0.2995 126 LYS A CG  
1103 C CD  . LYS A 125 ? 1.0091 1.2743 1.2643 -0.1160 0.2540  -0.3033 126 LYS A CD  
1104 C CE  . LYS A 125 ? 1.1623 1.4769 1.4700 -0.1103 0.2646  -0.3341 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.2610 1.6141 1.6101 -0.0903 0.2477  -0.3385 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.6911 0.8247 0.7613 -0.2120 0.2889  -0.2664 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.7146 0.8458 0.7662 -0.2412 0.3070  -0.2761 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.8198 0.9161 0.8232 -0.2677 0.3266  -0.2785 127 ALA A C   
1109 O O   . ALA A 126 ? 0.8305 0.9325 0.8268 -0.2935 0.3491  -0.2957 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.7138 0.8267 0.7439 -0.2432 0.2939  -0.2575 127 ALA A CB  
1111 N N   . SER A 127 ? 0.8186 0.8788 0.7876 -0.2626 0.3184  -0.2619 128 SER A N   
1112 C CA  . SER A 127 ? 0.8816 0.9053 0.8000 -0.2858 0.3334  -0.2617 128 SER A CA  
1113 C C   . SER A 127 ? 0.9733 1.0138 0.9078 -0.2911 0.3526  -0.2841 128 SER A C   
1114 O O   . SER A 127 ? 1.0247 1.0410 0.9199 -0.3155 0.3706  -0.2899 128 SER A O   
1115 C CB  . SER A 127 ? 0.9522 0.9311 0.8254 -0.2788 0.3149  -0.2348 128 SER A CB  
1116 O OG  . SER A 127 ? 1.1100 1.0589 0.9456 -0.2884 0.3078  -0.2182 128 SER A OG  
1117 N N   . GLU A 128 ? 0.8990 0.9788 0.8890 -0.2686 0.3490  -0.2971 129 GLU A N   
1118 C CA  . GLU A 128 ? 1.2180 1.3160 1.2292 -0.2703 0.3664  -0.3201 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.7363 1.8690 1.7729 -0.2905 0.3928  -0.3505 129 GLU A C   
1120 O O   . GLU A 128 ? 1.3403 1.4567 1.3422 -0.3201 0.4095  -0.3540 129 GLU A O   
1121 C CB  . GLU A 128 ? 1.2027 1.3225 1.2590 -0.2370 0.3513  -0.3210 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.2975 1.4671 1.4162 -0.2176 0.3459  -0.3353 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.5439 1.7274 1.7002 -0.1824 0.3266  -0.3311 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.4813 1.6333 1.6144 -0.1712 0.3134  -0.3120 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.4353 1.6609 1.6438 -0.1662 0.3244  -0.3474 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.2907 0.5313 0.3664 -0.0646 -0.0085 -0.0844 1   TRP D N   
1130 N N   B TRP B 2   ? 0.2880 0.5285 0.3637 -0.0646 -0.0085 -0.0844 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.2863 0.5274 0.3625 -0.0646 -0.0080 -0.0847 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.2802 0.5212 0.3565 -0.0646 -0.0080 -0.0847 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.3345 0.5756 0.4122 -0.0652 -0.0081 -0.0837 1   TRP D C   
1134 C C   B TRP B 2   ? 0.3251 0.5662 0.4028 -0.0653 -0.0081 -0.0836 1   TRP D C   
1135 O O   A TRP B 2   ? 0.3353 0.5756 0.4131 -0.0655 -0.0088 -0.0831 1   TRP D O   
1136 O O   B TRP B 2   ? 0.3200 0.5604 0.3978 -0.0656 -0.0087 -0.0831 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.2678 0.5085 0.3432 -0.0645 -0.0087 -0.0857 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.2616 0.5022 0.3370 -0.0646 -0.0087 -0.0856 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.2736 0.5143 0.3479 -0.0640 -0.0085 -0.0873 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.2714 0.5116 0.3473 -0.0650 -0.0098 -0.0854 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.3092 0.5493 0.3834 -0.0635 -0.0093 -0.0881 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.3096 0.5492 0.3860 -0.0649 -0.0108 -0.0861 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.2642 0.5057 0.3378 -0.0638 -0.0075 -0.0884 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.2684 0.5092 0.3449 -0.0656 -0.0101 -0.0846 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.2950 0.5353 0.3683 -0.0630 -0.0088 -0.0899 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.3022 0.5422 0.3797 -0.0654 -0.0113 -0.0860 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.3067 0.5480 0.3795 -0.0632 -0.0076 -0.0902 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.3193 0.5601 0.3965 -0.0658 -0.0109 -0.0851 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.2697 0.5120 0.3438 -0.0641 -0.0066 -0.0879 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.2806 0.5220 0.3577 -0.0659 -0.0098 -0.0836 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.2928 0.5346 0.3647 -0.0629 -0.0066 -0.0919 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.3090 0.5507 0.3869 -0.0664 -0.0113 -0.0848 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.2774 0.5201 0.3507 -0.0639 -0.0057 -0.0893 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.3008 0.5427 0.3784 -0.0665 -0.0105 -0.0829 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.2889 0.5315 0.3609 -0.0633 -0.0055 -0.0915 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.3083 0.5505 0.3860 -0.0667 -0.0111 -0.0836 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.2756 0.5176 0.3550 -0.0654 -0.0075 -0.0835 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.2682 0.5103 0.3496 -0.0659 -0.0078 -0.0828 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.2975 0.5397 0.3801 -0.0660 -0.0082 -0.0822 2   VAL D C   
1160 O O   . VAL B 3   ? 0.2689 0.5114 0.3511 -0.0658 -0.0078 -0.0823 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2983 0.5418 0.3821 -0.0665 -0.0068 -0.0833 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2983 0.5420 0.3805 -0.0670 -0.0067 -0.0834 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2873 0.5326 0.3733 -0.0664 -0.0056 -0.0842 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.2646 0.5067 0.3491 -0.0664 -0.0089 -0.0814 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.2731 0.5154 0.3598 -0.0666 -0.0096 -0.0803 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.3177 0.5609 0.4088 -0.0666 -0.0088 -0.0810 3   ILE D C   
1167 O O   . ILE B 4   ? 0.3036 0.5472 0.3969 -0.0670 -0.0086 -0.0818 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.3081 0.5501 0.3953 -0.0669 -0.0109 -0.0794 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.3054 0.5475 0.3891 -0.0671 -0.0114 -0.0795 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.3285 0.5707 0.4183 -0.0673 -0.0121 -0.0777 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.3173 0.5602 0.3983 -0.0675 -0.0117 -0.0793 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.3060 0.5499 0.3989 -0.0665 -0.0082 -0.0810 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.3137 0.5592 0.4120 -0.0666 -0.0072 -0.0822 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.3689 0.6144 0.4726 -0.0670 -0.0085 -0.0816 4   PRO D C   
1175 O O   . PRO B 5   ? 0.3465 0.5907 0.4497 -0.0670 -0.0101 -0.0795 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.3353 0.5814 0.4341 -0.0662 -0.0063 -0.0824 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.3807 0.6252 0.4756 -0.0662 -0.0074 -0.0805 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.3256 0.5692 0.4161 -0.0663 -0.0082 -0.0803 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.3428 0.5902 0.4521 -0.0674 -0.0077 -0.0835 5   ALA D N   
# 
