data_7GUG
# 
_entry.id   7GUG 
# 
_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   7GUG         pdb_00007gug 10.2210/pdb7gug/pdb 
WWPDB D_1001406651 ?            ?                   
# 
_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                        7GUG 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              Rob.vanMontfort@icr.ac.uk 
_pdbx_contact_author.name_first         Rob 
_pdbx_contact_author.name_last          'van Montfort' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodrigues, M.J.'      1 0000-0003-1243-903X 
'Le Bihan, Y.V.'       2 0000-0002-6850-9706 
'van Montfort, R.L.M.' 3 0000-0002-5688-3450 
# 
_citation.id                        primary 
_citation.title                     
'Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.' 
_citation.journal_abbrev            J.Appl.Crystallogr. 
_citation.journal_volume            57 
_citation.page_first                1951 
_citation.page_last                 1965 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39628887 
_citation.pdbx_database_id_DOI      10.1107/S1600576724010549 
_citation.journal_id_ASTM           JACGAR 
_citation.country                   DK 
_citation.journal_id_ISSN           0021-8898 
_citation.journal_id_CSD            0228 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodrigues, M.J.'      1 0000-0003-1243-903X 
primary 'Cabry, M.'            2 0000-0002-9070-5498 
primary 'Collie, G.'           3 0000-0002-0406-922X 
primary 'Carter, M.'           4 ?                   
primary 'McAndrew, C.'         5 0000-0002-1366-088X 
primary 'Owen, R.L.'           6 0000-0002-2104-7057 
primary 'Bellenie, B.R.'       7 0000-0001-9987-3079 
primary 'Le Bihan, Y.V.'       8 0000-0002-6850-9706 
primary 'van Montfort, R.L.M.' 9 0000-0002-5688-3450 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'B-cell lymphoma 6 protein'                                   14536.915 1   ? ? ? ? 
2 polymer     syn 'WVIP tetrapeptide'                                           610.744   1   ? ? ? ? 
3 non-polymer syn '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' 260.679   1   ? ? ? ? 
4 non-polymer nat 'CHLORIDE ION'                                                35.453    1   ? ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                          78.133    1   ? ? ? ? 
6 water       nat water                                                         18.015    181 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'BCL-6,B-cell lymphoma 5 protein,BCL-5,Protein LAZ-3,Zinc finger and BTB domain-containing protein 27,Zinc finger protein 51' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
;GPGADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPE
GFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASE
;
A ? 
2 'polypeptide(L)' no yes '(ACE)WVIPA' XWVIPA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' 7ZO 
4 'CHLORIDE ION'                                                CL  
5 'DIMETHYL SULFOXIDE'                                          DMS 
6 water                                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   ALA n 
1 5   ASP n 
1 6   SER n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  PHE n 
1 11  THR n 
1 12  ARG n 
1 13  HIS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  VAL n 
1 18  LEU n 
1 19  LEU n 
1 20  ASN n 
1 21  LEU n 
1 22  ASN n 
1 23  ARG n 
1 24  LEU n 
1 25  ARG n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  THR n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  ILE n 
1 36  VAL n 
1 37  VAL n 
1 38  SER n 
1 39  ARG n 
1 40  GLU n 
1 41  GLN n 
1 42  PHE n 
1 43  ARG n 
1 44  ALA n 
1 45  HIS n 
1 46  LYS n 
1 47  THR n 
1 48  VAL n 
1 49  LEU n 
1 50  MET n 
1 51  ALA n 
1 52  CYS n 
1 53  SER n 
1 54  GLY n 
1 55  LEU n 
1 56  PHE n 
1 57  TYR n 
1 58  SER n 
1 59  ILE n 
1 60  PHE n 
1 61  THR n 
1 62  ASP n 
1 63  GLN n 
1 64  LEU n 
1 65  LYS n 
1 66  CYS n 
1 67  ASN n 
1 68  LEU n 
1 69  SER n 
1 70  VAL n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ASP n 
1 75  PRO n 
1 76  GLU n 
1 77  ILE n 
1 78  ASN n 
1 79  PRO n 
1 80  GLU n 
1 81  GLY n 
1 82  PHE n 
1 83  CYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  ASP n 
1 88  PHE n 
1 89  MET n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ARG n 
1 94  LEU n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLU n 
1 99  GLY n 
1 100 ASN n 
1 101 ILE n 
1 102 MET n 
1 103 ALA n 
1 104 VAL n 
1 105 MET n 
1 106 ALA n 
1 107 THR n 
1 108 ALA n 
1 109 MET n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 MET n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 VAL n 
1 118 ASP n 
1 119 THR n 
1 120 CYS n 
1 121 ARG n 
1 122 LYS n 
1 123 PHE n 
1 124 ILE n 
1 125 LYS n 
1 126 ALA n 
1 127 SER n 
1 128 GLU n 
2 1   ACE n 
2 2   TRP n 
2 3   VAL n 
2 4   ILE n 
2 5   PRO n 
2 6   ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCL6, BCL5, LAZ3, ZBTB27, ZNF51' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21-AI 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET48b 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 6 'synthetic construct' ? 32630 ? 
3 2 sample ? ? 'synthetic construct' ? 32630 ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
7ZO non-polymer         . '5-[(5-chloranylpyrimidin-4-yl)amino]-1,3-dihydroindol-2-one' ? 'C12 H9 Cl N4 O' 260.679 
ACE non-polymer         . 'ACETYL GROUP'                                                ? 'C2 H4 O'        44.053  
ALA 'L-peptide linking' y ALANINE                                                       ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                      ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                    ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                               ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'                                                ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                                                      ? 'C3 H7 N O2 S'   121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                          ? 'C2 H6 O S'      78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                     ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                               ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                       ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                     ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                         ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                    ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                       ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                        ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                    ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                 ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                       ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                        ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                     ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                    ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                      ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                        ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLY 3   4   ?   ?   ?   A . n 
A 1 4   ALA 4   5   ?   ?   ?   A . n 
A 1 5   ASP 5   6   6   ASP ASP A . n 
A 1 6   SER 6   7   7   SER SER A . n 
A 1 7   CYS 7   8   8   CYS CYS A . n 
A 1 8   ILE 8   9   9   ILE ILE A . n 
A 1 9   GLN 9   10  10  GLN GLN A . n 
A 1 10  PHE 10  11  11  PHE PHE A . n 
A 1 11  THR 11  12  12  THR THR A . n 
A 1 12  ARG 12  13  13  ARG ARG A . n 
A 1 13  HIS 13  14  14  HIS HIS A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ASP 16  17  17  ASP ASP A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  ASN 20  21  21  ASN ASN A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  ARG 23  24  24  ARG ARG A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  ARG 25  26  26  ARG ARG A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  THR 31  32  32  THR THR A . n 
A 1 32  ASP 32  33  33  ASP ASP A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  VAL 36  37  37  VAL VAL A . n 
A 1 37  VAL 37  38  38  VAL VAL A . n 
A 1 38  SER 38  39  39  SER SER A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLN 41  42  42  GLN GLN A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  ALA 44  45  45  ALA ALA A . n 
A 1 45  HIS 45  46  46  HIS HIS A . n 
A 1 46  LYS 46  47  47  LYS LYS A . n 
A 1 47  THR 47  48  48  THR THR A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  MET 50  51  51  MET MET A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  CYS 52  53  53  CYS CYS A . n 
A 1 53  SER 53  54  54  SER SER A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  ILE 59  60  60  ILE ILE A . n 
A 1 60  PHE 60  61  61  PHE PHE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ASP 62  63  63  ASP ASP A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  ASN 67  68  68  ASN ASN A . n 
A 1 68  LEU 68  69  69  LEU LEU A . n 
A 1 69  SER 69  70  70  SER SER A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ILE 71  72  72  ILE ILE A . n 
A 1 72  ASN 72  73  73  ASN ASN A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  ASP 74  75  75  ASP ASP A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLU 76  77  77  GLU GLU A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  PRO 79  80  80  PRO PRO A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  CYS 83  84  84  CYS CYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  LEU 85  86  86  LEU LEU A . n 
A 1 86  LEU 86  87  87  LEU LEU A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  PHE 88  89  89  PHE PHE A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  TYR 90  91  91  TYR TYR A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  ASN 95  96  96  ASN ASN A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ARG 97  98  98  ARG ARG A . n 
A 1 98  GLU 98  99  99  GLU GLU A . n 
A 1 99  GLY 99  100 100 GLY GLY A . n 
A 1 100 ASN 100 101 101 ASN ASN A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 MET 102 103 103 MET MET A . n 
A 1 103 ALA 103 104 104 ALA ALA A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 MET 105 106 106 MET MET A . n 
A 1 106 ALA 106 107 107 ALA ALA A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 MET 109 110 110 MET MET A . n 
A 1 110 TYR 110 111 111 TYR TYR A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLN 112 113 113 GLN GLN A . n 
A 1 113 MET 113 114 114 MET MET A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 HIS 115 116 116 HIS HIS A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 VAL 117 118 118 VAL VAL A . n 
A 1 118 ASP 118 119 119 ASP ASP A . n 
A 1 119 THR 119 120 120 THR THR A . n 
A 1 120 CYS 120 121 121 CYS CYS A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 PHE 123 124 124 PHE PHE A . n 
A 1 124 ILE 124 125 125 ILE ILE A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 SER 127 128 128 SER SER A . n 
A 1 128 GLU 128 129 129 GLU GLU A . n 
B 2 1   ACE 1   0   0   ACE ACE D . n 
B 2 2   TRP 2   1   1   TRP TRP D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ILE 4   3   3   ILE ILE D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   ALA 6   5   5   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 7ZO 1   201 1   7ZO 375 A . 
D 4 CL  1   202 1   CL  CL  A . 
E 5 DMS 1   101 1   DMS DMS D . 
F 6 HOH 1   301 81  HOH HOH A . 
F 6 HOH 2   302 42  HOH HOH A . 
F 6 HOH 3   303 84  HOH HOH A . 
F 6 HOH 4   304 166 HOH HOH A . 
F 6 HOH 5   305 88  HOH HOH A . 
F 6 HOH 6   306 32  HOH HOH A . 
F 6 HOH 7   307 159 HOH HOH A . 
F 6 HOH 8   308 92  HOH HOH A . 
F 6 HOH 9   309 15  HOH HOH A . 
F 6 HOH 10  310 114 HOH HOH A . 
F 6 HOH 11  311 230 HOH HOH A . 
F 6 HOH 12  312 85  HOH HOH A . 
F 6 HOH 13  313 5   HOH HOH A . 
F 6 HOH 14  314 130 HOH HOH A . 
F 6 HOH 15  315 87  HOH HOH A . 
F 6 HOH 16  316 149 HOH HOH A . 
F 6 HOH 17  317 187 HOH HOH A . 
F 6 HOH 18  318 189 HOH HOH A . 
F 6 HOH 19  319 14  HOH HOH A . 
F 6 HOH 20  320 113 HOH HOH A . 
F 6 HOH 21  321 23  HOH HOH A . 
F 6 HOH 22  322 196 HOH HOH A . 
F 6 HOH 23  323 63  HOH HOH A . 
F 6 HOH 24  324 33  HOH HOH A . 
F 6 HOH 25  325 103 HOH HOH A . 
F 6 HOH 26  326 24  HOH HOH A . 
F 6 HOH 27  327 35  HOH HOH A . 
F 6 HOH 28  328 135 HOH HOH A . 
F 6 HOH 29  329 143 HOH HOH A . 
F 6 HOH 30  330 83  HOH HOH A . 
F 6 HOH 31  331 13  HOH HOH A . 
F 6 HOH 32  332 97  HOH HOH A . 
F 6 HOH 33  333 90  HOH HOH A . 
F 6 HOH 34  334 112 HOH HOH A . 
F 6 HOH 35  335 134 HOH HOH A . 
F 6 HOH 36  336 44  HOH HOH A . 
F 6 HOH 37  337 105 HOH HOH A . 
F 6 HOH 38  338 100 HOH HOH A . 
F 6 HOH 39  339 109 HOH HOH A . 
F 6 HOH 40  340 50  HOH HOH A . 
F 6 HOH 41  341 51  HOH HOH A . 
F 6 HOH 42  342 3   HOH HOH A . 
F 6 HOH 43  343 141 HOH HOH A . 
F 6 HOH 44  344 49  HOH HOH A . 
F 6 HOH 45  345 94  HOH HOH A . 
F 6 HOH 46  346 213 HOH HOH A . 
F 6 HOH 47  347 136 HOH HOH A . 
F 6 HOH 48  348 18  HOH HOH A . 
F 6 HOH 49  349 165 HOH HOH A . 
F 6 HOH 50  350 184 HOH HOH A . 
F 6 HOH 51  351 117 HOH HOH A . 
F 6 HOH 52  352 115 HOH HOH A . 
F 6 HOH 53  353 180 HOH HOH A . 
F 6 HOH 54  354 11  HOH HOH A . 
F 6 HOH 55  355 123 HOH HOH A . 
F 6 HOH 56  356 116 HOH HOH A . 
F 6 HOH 57  357 86  HOH HOH A . 
F 6 HOH 58  358 74  HOH HOH A . 
F 6 HOH 59  359 102 HOH HOH A . 
F 6 HOH 60  360 95  HOH HOH A . 
F 6 HOH 61  361 110 HOH HOH A . 
F 6 HOH 62  362 101 HOH HOH A . 
F 6 HOH 63  363 246 HOH HOH A . 
F 6 HOH 64  364 107 HOH HOH A . 
F 6 HOH 65  365 6   HOH HOH A . 
F 6 HOH 66  366 62  HOH HOH A . 
F 6 HOH 67  367 121 HOH HOH A . 
F 6 HOH 68  368 231 HOH HOH A . 
F 6 HOH 69  369 147 HOH HOH A . 
F 6 HOH 70  370 26  HOH HOH A . 
F 6 HOH 71  371 151 HOH HOH A . 
F 6 HOH 72  372 22  HOH HOH A . 
F 6 HOH 73  373 150 HOH HOH A . 
F 6 HOH 74  374 28  HOH HOH A . 
F 6 HOH 75  375 66  HOH HOH A . 
F 6 HOH 76  376 89  HOH HOH A . 
F 6 HOH 77  377 60  HOH HOH A . 
F 6 HOH 78  378 168 HOH HOH A . 
F 6 HOH 79  379 25  HOH HOH A . 
F 6 HOH 80  380 244 HOH HOH A . 
F 6 HOH 81  381 119 HOH HOH A . 
F 6 HOH 82  382 20  HOH HOH A . 
F 6 HOH 83  383 10  HOH HOH A . 
F 6 HOH 84  384 40  HOH HOH A . 
F 6 HOH 85  385 178 HOH HOH A . 
F 6 HOH 86  386 192 HOH HOH A . 
F 6 HOH 87  387 29  HOH HOH A . 
F 6 HOH 88  388 104 HOH HOH A . 
F 6 HOH 89  389 164 HOH HOH A . 
F 6 HOH 90  390 57  HOH HOH A . 
F 6 HOH 91  391 39  HOH HOH A . 
F 6 HOH 92  392 21  HOH HOH A . 
F 6 HOH 93  393 82  HOH HOH A . 
F 6 HOH 94  394 99  HOH HOH A . 
F 6 HOH 95  395 242 HOH HOH A . 
F 6 HOH 96  396 238 HOH HOH A . 
F 6 HOH 97  397 30  HOH HOH A . 
F 6 HOH 98  398 93  HOH HOH A . 
F 6 HOH 99  399 38  HOH HOH A . 
F 6 HOH 100 400 36  HOH HOH A . 
F 6 HOH 101 401 56  HOH HOH A . 
F 6 HOH 102 402 53  HOH HOH A . 
F 6 HOH 103 403 193 HOH HOH A . 
F 6 HOH 104 404 27  HOH HOH A . 
F 6 HOH 105 405 45  HOH HOH A . 
F 6 HOH 106 406 239 HOH HOH A . 
F 6 HOH 107 407 37  HOH HOH A . 
F 6 HOH 108 408 52  HOH HOH A . 
F 6 HOH 109 409 203 HOH HOH A . 
F 6 HOH 110 410 17  HOH HOH A . 
F 6 HOH 111 411 167 HOH HOH A . 
F 6 HOH 112 412 96  HOH HOH A . 
F 6 HOH 113 413 75  HOH HOH A . 
F 6 HOH 114 414 237 HOH HOH A . 
F 6 HOH 115 415 171 HOH HOH A . 
F 6 HOH 116 416 209 HOH HOH A . 
F 6 HOH 117 417 55  HOH HOH A . 
F 6 HOH 118 418 200 HOH HOH A . 
F 6 HOH 119 419 145 HOH HOH A . 
F 6 HOH 120 420 79  HOH HOH A . 
F 6 HOH 121 421 146 HOH HOH A . 
F 6 HOH 122 422 176 HOH HOH A . 
F 6 HOH 123 423 69  HOH HOH A . 
F 6 HOH 124 424 186 HOH HOH A . 
F 6 HOH 125 425 54  HOH HOH A . 
F 6 HOH 126 426 153 HOH HOH A . 
F 6 HOH 127 427 241 HOH HOH A . 
F 6 HOH 128 428 98  HOH HOH A . 
F 6 HOH 129 429 148 HOH HOH A . 
F 6 HOH 130 430 31  HOH HOH A . 
F 6 HOH 131 431 43  HOH HOH A . 
F 6 HOH 132 432 106 HOH HOH A . 
F 6 HOH 133 433 185 HOH HOH A . 
F 6 HOH 134 434 191 HOH HOH A . 
F 6 HOH 135 435 139 HOH HOH A . 
F 6 HOH 136 436 188 HOH HOH A . 
F 6 HOH 137 437 80  HOH HOH A . 
F 6 HOH 138 438 158 HOH HOH A . 
F 6 HOH 139 439 232 HOH HOH A . 
F 6 HOH 140 440 76  HOH HOH A . 
F 6 HOH 141 441 204 HOH HOH A . 
F 6 HOH 142 442 137 HOH HOH A . 
F 6 HOH 143 443 111 HOH HOH A . 
F 6 HOH 144 444 108 HOH HOH A . 
F 6 HOH 145 445 140 HOH HOH A . 
F 6 HOH 146 446 169 HOH HOH A . 
F 6 HOH 147 447 206 HOH HOH A . 
F 6 HOH 148 448 70  HOH HOH A . 
F 6 HOH 149 449 221 HOH HOH A . 
F 6 HOH 150 450 247 HOH HOH A . 
F 6 HOH 151 451 243 HOH HOH A . 
F 6 HOH 152 452 161 HOH HOH A . 
F 6 HOH 153 453 212 HOH HOH A . 
F 6 HOH 154 454 228 HOH HOH A . 
F 6 HOH 155 455 131 HOH HOH A . 
F 6 HOH 156 456 183 HOH HOH A . 
F 6 HOH 157 457 215 HOH HOH A . 
F 6 HOH 158 458 142 HOH HOH A . 
F 6 HOH 159 459 59  HOH HOH A . 
F 6 HOH 160 460 73  HOH HOH A . 
F 6 HOH 161 461 179 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 65  HOH HOH A . 
F 6 HOH 165 465 170 HOH HOH A . 
F 6 HOH 166 466 195 HOH HOH A . 
F 6 HOH 167 467 152 HOH HOH A . 
F 6 HOH 168 468 208 HOH HOH A . 
F 6 HOH 169 469 181 HOH HOH A . 
F 6 HOH 170 470 61  HOH HOH A . 
F 6 HOH 171 471 233 HOH HOH A . 
F 6 HOH 172 472 144 HOH HOH A . 
F 6 HOH 173 473 225 HOH HOH A . 
G 6 HOH 1   201 77  HOH HOH D . 
G 6 HOH 2   202 71  HOH HOH D . 
G 6 HOH 3   203 47  HOH HOH D . 
G 6 HOH 4   204 68  HOH HOH D . 
G 6 HOH 5   205 58  HOH HOH D . 
G 6 HOH 6   206 240 HOH HOH D . 
G 6 HOH 7   207 220 HOH HOH D . 
G 6 HOH 8   208 210 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 64  ? CD  ? A GLN 63  CD  
2  1 Y 1 A GLN 64  ? OE1 ? A GLN 63  OE1 
3  1 Y 1 A GLN 64  ? NE2 ? A GLN 63  NE2 
4  1 Y 1 A GLU 115 ? CD  ? A GLU 114 CD  
5  1 Y 1 A GLU 115 ? OE1 ? A GLU 114 OE1 
6  1 Y 1 A GLU 115 ? OE2 ? A GLU 114 OE2 
7  1 Y 1 D ALA 5   ? CA  ? B ALA 6   CA  
8  1 Y 1 D ALA 5   ? C   ? B ALA 6   C   
9  1 Y 1 D ALA 5   ? O   ? B ALA 6   O   
10 1 Y 1 D ALA 5   ? CB  ? B ALA 6   CB  
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 Aimless     0.5.32 29/03/17       program 'Phil Evans'      ?                                'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
4 BUSTER      2.10.3 ?              program 'Gerard Bricogne' buster-develop@GlobalPhasing.com phasing           
http://www.globalphasing.com/buster/                ?   ? 
5 PDB_EXTRACT 3.24   'Sep. 1, 2017' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.entry_id           7GUG 
_cell.length_a           67.550 
_cell.length_b           67.550 
_cell.length_c           166.150 
_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                         7GUG 
_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          7GUG 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.61 
_exptl_crystal.density_percent_sol   65.95 
_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                     7GUG 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.870 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   21698 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.089 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.900 
_reflns.B_iso_Wilson_estimate        28.330 
_reflns.pdbx_redundancy              9.100 
_reflns.pdbx_Rrim_I_all              0.095 
_reflns.pdbx_Rpim_I_all              0.031 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     196945 
_reflns.pdbx_scaling_rejects         588 
_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  ? 11604 1246 ? 0.808 ? ? ? 9.300 ? 2.800  ? ? ? ? ? ? 100.000 0.855 0.278 0.881 ? 
1 2 9.000 33.870 ? 1590  238  ? 0.074 ? ? ? 6.700 ? 20.500 ? ? ? ? ? ? 98.800  0.080 0.029 0.995 ? 
# 
_refine.entry_id                                 7GUG 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8000 
_refine.ls_d_res_low                             33.8700 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    100.0000 
_refine.ls_number_reflns_obs                     21630 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1810 
_refine.ls_R_factor_R_work                       0.1790 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2030 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.2100 
_refine.ls_number_reflns_R_free                  1126 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               33.4800 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -1.6170 
_refine.aniso_B[2][2]                            -1.6170 
_refine.aniso_B[3][3]                            3.2340 
_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               0.9560 
_refine.correlation_coeff_Fo_to_Fc_free          0.9460 
_refine.overall_SU_R_Cruickshank_DPI             0.0940 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0920 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1080 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1010 
_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                                123.960 
_refine.B_iso_min                                15.620 
_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                        7GUG 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.190 
_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                        33.8700 
_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           28.46 
_refine_hist.pdbx_B_iso_mean_solvent          50.29 
_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      1657 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1236 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               1693 0.920  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.390  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    16.080 ? ?      ?            
# 
_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               99.8900 
_refine_ls_shell.number_reflns_R_work             2682 
_refine_ls_shell.R_factor_all                     0.2479 
_refine_ls_shell.R_factor_R_work                  0.2484 
_refine_ls_shell.R_factor_R_free                  0.2387 
_refine_ls_shell.percent_reflns_R_free            4.6600 
_refine_ls_shell.number_reflns_R_free             131 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                2813 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7GUG 
_struct.title                     
'Crystal Structure of B-cell lymphoma 6 protein BTB domain in complex with ligand 1 at 6.04 MGy X-ray dose.' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7GUG 
_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 7GUG       7GUG   ? 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 7GUG A 4 ? 128 ? P41182 5 ? 129 ? 5 129 
2 2 7GUG D 1 ? 6   ? 7GUG   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 7GUG GLY A 1 ? UNP P41182 ? ? 'expression tag' 2 1 
1 7GUG PRO A 2 ? UNP P41182 ? ? 'expression tag' 3 2 
1 7GUG GLY A 3 ? UNP P41182 ? ? 'expression tag' 4 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6370  ? 
1 MORE         -68   ? 
1 'SSA (A^2)'  13260 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_545 x,x-y-1,-z+1/6 0.5000000000 0.8660254038 0.0000000000 33.7750000000 0.8660254038 
-0.5000000000 0.0000000000 -58.5000160256 0.0000000000 0.0000000000 -1.0000000000 27.6916666667 
# 
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 ? ? ? ? ? ? ? 1.326 ? ? 
covale2 covale both ? B ACE 1 C ? ? ? 1_555 B TRP 2 N B ? D ACE 0 D TRP 1 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
# 
_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                   7GUG 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 39  ? A 37.02 48.61   
2 1 SER A 39  ? B 62.36 -107.95 
3 1 SER A 93  ? ? 77.05 -0.09   
4 1 SER A 93  ? ? 77.05 -3.18   
5 1 GLN A 113 ? ? 63.10 63.96   
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             VAL 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              38 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   11.35 
# 
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 349 ? F HOH . 
2 1 A HOH 389 ? F HOH . 
3 1 A HOH 446 ? 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 -0.0041 -0.0657 -0.0418 -0.0403 0.0235  -0.0163 1.0216 1.7666  2.0978 
0.4430 -0.3087 1.1700 0.1459 -0.0968 -0.0491 -0.0522 0.0961 0.0711 0.2539  0.0072 -0.0458 
'X-RAY DIFFRACTION' 2 ? refined 18.9623 -32.3913 1.8231  -0.1205 0.1121  -0.0231 -0.0652 -0.0136 -0.0787 0.5101 -0.0247 0.0000 
0.1259 0.1270  0.4915 0.0141 -0.0004 -0.0137 -0.0066 0.0111 0.0233 -0.0124 0.0046 0.0069  
# 
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                    7GUG 
_atom_sites.fract_transf_matrix[1][1]   0.014804 
_atom_sites.fract_transf_matrix[1][2]   0.008547 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017094 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006019 
_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   ? 17.549 -21.126 -4.897 1.00 64.42  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 5   ? 18.392 -22.053 -5.655 1.00 63.42  ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 5   ? 17.873 -23.507 -5.555 1.00 63.43  ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 5   ? 16.777 -23.744 -5.034 1.00 64.21  ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 5   ? 19.860 -21.954 -5.170 1.00 64.22  ? 6   ASP A CB  1 
ATOM   6    C  CG  . ASP A 1 5   ? 20.897 -22.046 -6.281 1.00 78.22  ? 6   ASP A CG  1 
ATOM   7    O  OD1 . ASP A 1 5   ? 20.944 -23.094 -6.971 1.00 78.95  ? 6   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A 1 5   ? 21.673 -21.078 -6.450 1.00 84.96  ? 6   ASP A OD2 1 
ATOM   9    N  N   . SER A 1 6   ? 18.656 -24.468 -6.079 1.00 54.81  ? 7   SER A N   1 
ATOM   10   C  CA  . SER A 1 6   ? 18.360 -25.898 -6.051 1.00 52.15  ? 7   SER A CA  1 
ATOM   11   C  C   . SER A 1 6   ? 19.368 -26.642 -5.118 1.00 47.67  ? 7   SER A C   1 
ATOM   12   O  O   . SER A 1 6   ? 19.683 -27.813 -5.342 1.00 47.60  ? 7   SER A O   1 
ATOM   13   C  CB  . SER A 1 6   ? 18.391 -26.464 -7.465 1.00 57.81  ? 7   SER A CB  1 
ATOM   14   O  OG  . SER A 1 6   ? 19.657 -26.272 -8.078 1.00 70.27  ? 7   SER A OG  1 
ATOM   15   N  N   . CYS A 1 7   ? 19.847 -25.959 -4.065 1.00 37.42  ? 8   CYS A N   1 
ATOM   16   C  CA  . CYS A 1 7   ? 20.805 -26.535 -3.112 1.00 33.98  ? 8   CYS A CA  1 
ATOM   17   C  C   . CYS A 1 7   ? 20.183 -27.697 -2.307 1.00 34.32  ? 8   CYS A C   1 
ATOM   18   O  O   . CYS A 1 7   ? 18.964 -27.755 -2.133 1.00 34.42  ? 8   CYS A O   1 
ATOM   19   C  CB  . CYS A 1 7   ? 21.313 -25.447 -2.163 1.00 34.66  ? 8   CYS A CB  1 
ATOM   20   S  SG  . CYS A 1 7   ? 22.449 -24.242 -2.914 1.00 39.63  ? 8   CYS A SG  1 
ATOM   21   N  N   . ILE A 1 8   ? 21.021 -28.606 -1.810 1.00 26.12  ? 9   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 8   ? 20.643 -29.605 -0.810 1.00 23.51  ? 9   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 8   ? 21.249 -29.062 0.492  1.00 25.49  ? 9   ILE A C   1 
ATOM   24   O  O   . ILE A 1 8   ? 22.186 -28.258 0.441  1.00 24.35  ? 9   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 8   ? 21.019 -31.079 -1.129 1.00 26.68  ? 9   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 8   ? 22.544 -31.250 -1.395 1.00 27.33  ? 9   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 8   ? 20.149 -31.615 -2.287 1.00 28.37  ? 9   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 8   ? 23.047 -32.706 -1.561 1.00 31.20  ? 9   ILE A CD1 1 
ATOM   29   N  N   A GLN A 1 9   ? 20.775 -29.513 1.651  0.57 20.86  ? 10  GLN A N   1 
ATOM   30   N  N   B GLN A 1 9   ? 20.667 -29.436 1.632  0.43 21.46  ? 10  GLN A N   1 
ATOM   31   C  CA  A GLN A 1 9   ? 21.292 -28.986 2.916  0.57 20.09  ? 10  GLN A CA  1 
ATOM   32   C  CA  B GLN A 1 9   ? 21.092 -28.956 2.942  0.43 20.51  ? 10  GLN A CA  1 
ATOM   33   C  C   A GLN A 1 9   ? 21.619 -30.107 3.896  0.57 23.30  ? 10  GLN A C   1 
ATOM   34   C  C   B GLN A 1 9   ? 21.536 -30.106 3.825  0.43 23.13  ? 10  GLN A C   1 
ATOM   35   O  O   A GLN A 1 9   ? 20.804 -31.009 4.078  0.57 23.39  ? 10  GLN A O   1 
ATOM   36   O  O   B GLN A 1 9   ? 20.894 -31.154 3.847  0.43 23.34  ? 10  GLN A O   1 
ATOM   37   C  CB  A GLN A 1 9   ? 20.257 -28.002 3.521  0.57 21.42  ? 10  GLN A CB  1 
ATOM   38   C  CB  B GLN A 1 9   ? 19.942 -28.167 3.617  0.43 21.77  ? 10  GLN A CB  1 
ATOM   39   C  CG  A GLN A 1 9   ? 20.642 -27.402 4.877  0.57 22.31  ? 10  GLN A CG  1 
ATOM   40   C  CG  B GLN A 1 9   ? 20.142 -27.896 5.128  0.43 26.37  ? 10  GLN A CG  1 
ATOM   41   C  CD  A GLN A 1 9   ? 19.480 -26.702 5.541  0.57 48.63  ? 10  GLN A CD  1 
ATOM   42   C  CD  B GLN A 1 9   ? 20.077 -26.445 5.530  0.43 37.68  ? 10  GLN A CD  1 
ATOM   43   O  OE1 A GLN A 1 9   ? 18.478 -27.314 5.931  0.57 39.29  ? 10  GLN A OE1 1 
ATOM   44   O  OE1 B GLN A 1 9   ? 19.732 -25.551 4.742  0.43 26.55  ? 10  GLN A OE1 1 
ATOM   45   N  NE2 A GLN A 1 9   ? 19.589 -25.396 5.690  0.57 51.79  ? 10  GLN A NE2 1 
ATOM   46   N  NE2 B GLN A 1 9   ? 20.406 -26.185 6.789  0.43 27.82  ? 10  GLN A NE2 1 
ATOM   47   N  N   A PHE A 1 10  ? 22.793 -30.036 4.552  0.78 20.90  ? 11  PHE A N   1 
ATOM   48   N  N   B PHE A 1 10  ? 22.612 -29.886 4.579  0.22 19.61  ? 11  PHE A N   1 
ATOM   49   C  CA  A PHE A 1 10  ? 23.155 -31.051 5.542  0.78 20.58  ? 11  PHE A CA  1 
ATOM   50   C  CA  B PHE A 1 10  ? 23.116 -30.854 5.538  0.22 19.19  ? 11  PHE A CA  1 
ATOM   51   C  C   A PHE A 1 10  ? 22.683 -30.553 6.909  0.78 22.51  ? 11  PHE A C   1 
ATOM   52   C  C   B PHE A 1 10  ? 22.579 -30.401 6.878  0.22 22.13  ? 11  PHE A C   1 
ATOM   53   O  O   A PHE A 1 10  ? 23.257 -29.605 7.464  0.78 21.32  ? 11  PHE A O   1 
ATOM   54   O  O   B PHE A 1 10  ? 22.972 -29.334 7.369  0.22 20.99  ? 11  PHE A O   1 
ATOM   55   C  CB  A PHE A 1 10  ? 24.672 -31.384 5.496  0.78 21.86  ? 11  PHE A CB  1 
ATOM   56   C  CB  B PHE A 1 10  ? 24.650 -30.909 5.485  0.22 20.48  ? 11  PHE A CB  1 
ATOM   57   C  CG  A PHE A 1 10  ? 25.047 -32.578 6.348  0.78 22.75  ? 11  PHE A CG  1 
ATOM   58   C  CG  B PHE A 1 10  ? 25.137 -31.808 4.374  0.22 22.51  ? 11  PHE A CG  1 
ATOM   59   C  CD1 A PHE A 1 10  ? 24.628 -33.862 6.004  0.78 25.83  ? 11  PHE A CD1 1 
ATOM   60   C  CD1 B PHE A 1 10  ? 24.901 -31.489 3.040  0.22 26.11  ? 11  PHE A CD1 1 
ATOM   61   C  CD2 A PHE A 1 10  ? 25.833 -32.421 7.487  0.78 23.90  ? 11  PHE A CD2 1 
ATOM   62   C  CD2 B PHE A 1 10  ? 25.805 -32.991 4.659  0.22 25.53  ? 11  PHE A CD2 1 
ATOM   63   C  CE1 A PHE A 1 10  ? 24.962 -34.966 6.808  0.78 26.96  ? 11  PHE A CE1 1 
ATOM   64   C  CE1 B PHE A 1 10  ? 25.339 -32.327 2.016  0.22 27.48  ? 11  PHE A CE1 1 
ATOM   65   C  CE2 A PHE A 1 10  ? 26.153 -33.518 8.293  0.78 25.65  ? 11  PHE A CE2 1 
ATOM   66   C  CE2 B PHE A 1 10  ? 26.230 -33.834 3.632  0.22 28.91  ? 11  PHE A CE2 1 
ATOM   67   C  CZ  A PHE A 1 10  ? 25.727 -34.783 7.946  0.78 24.14  ? 11  PHE A CZ  1 
ATOM   68   C  CZ  B PHE A 1 10  ? 26.005 -33.490 2.320  0.22 27.12  ? 11  PHE A CZ  1 
ATOM   69   N  N   . THR A 1 11  ? 21.596 -31.149 7.414  1.00 19.11  ? 12  THR A N   1 
ATOM   70   C  CA  . THR A 1 11  ? 20.925 -30.758 8.672  1.00 19.88  ? 12  THR A CA  1 
ATOM   71   C  C   . THR A 1 11  ? 21.872 -30.510 9.874  1.00 23.28  ? 12  THR A C   1 
ATOM   72   O  O   . THR A 1 11  ? 21.743 -29.481 10.561 1.00 22.24  ? 12  THR A O   1 
ATOM   73   C  CB  . THR A 1 11  ? 19.864 -31.808 9.021  1.00 26.93  ? 12  THR A CB  1 
ATOM   74   O  OG1 . THR A 1 11  ? 18.938 -31.887 7.925  1.00 28.15  ? 12  THR A OG1 1 
ATOM   75   C  CG2 . THR A 1 11  ? 19.098 -31.465 10.317 1.00 30.70  ? 12  THR A CG2 1 
ATOM   76   N  N   A ARG A 1 12  ? 22.810 -31.439 10.104 0.50 20.09  ? 13  ARG A N   1 
ATOM   77   N  N   B ARG A 1 12  ? 22.804 -31.440 10.118 0.50 20.38  ? 13  ARG A N   1 
ATOM   78   C  CA  A ARG A 1 12  ? 23.732 -31.378 11.248 0.50 20.20  ? 13  ARG A CA  1 
ATOM   79   C  CA  B ARG A 1 12  ? 23.726 -31.361 11.263 0.50 20.56  ? 13  ARG A CA  1 
ATOM   80   C  C   A ARG A 1 12  ? 24.984 -30.502 11.044 0.50 22.45  ? 13  ARG A C   1 
ATOM   81   C  C   B ARG A 1 12  ? 24.961 -30.462 11.063 0.50 22.46  ? 13  ARG A C   1 
ATOM   82   O  O   A ARG A 1 12  ? 25.806 -30.411 11.963 0.50 21.20  ? 13  ARG A O   1 
ATOM   83   O  O   B ARG A 1 12  ? 25.757 -30.325 12.001 0.50 21.08  ? 13  ARG A O   1 
ATOM   84   C  CB  A ARG A 1 12  ? 24.147 -32.805 11.667 0.50 23.26  ? 13  ARG A CB  1 
ATOM   85   C  CB  B ARG A 1 12  ? 24.173 -32.776 11.661 0.50 24.46  ? 13  ARG A CB  1 
ATOM   86   C  CG  A ARG A 1 12  ? 23.007 -33.687 12.207 0.50 30.98  ? 13  ARG A CG  1 
ATOM   87   C  CG  B ARG A 1 12  ? 23.214 -33.489 12.612 0.50 36.39  ? 13  ARG A CG  1 
ATOM   88   C  CD  A ARG A 1 12  ? 22.470 -33.211 13.549 0.50 42.21  ? 13  ARG A CD  1 
ATOM   89   C  CD  B ARG A 1 12  ? 22.958 -34.940 12.243 0.50 43.35  ? 13  ARG A CD  1 
ATOM   90   N  NE  A ARG A 1 12  ? 23.440 -33.364 14.636 0.50 48.31  ? 13  ARG A NE  1 
ATOM   91   N  NE  B ARG A 1 12  ? 24.180 -35.707 11.980 0.50 46.29  ? 13  ARG A NE  1 
ATOM   92   C  CZ  A ARG A 1 12  ? 23.372 -32.725 15.800 0.50 55.56  ? 13  ARG A CZ  1 
ATOM   93   C  CZ  B ARG A 1 12  ? 24.377 -36.447 10.892 0.50 56.72  ? 13  ARG A CZ  1 
ATOM   94   N  NH1 A ARG A 1 12  ? 22.392 -31.860 16.034 0.50 38.13  ? 13  ARG A NH1 1 
ATOM   95   N  NH1 B ARG A 1 12  ? 25.511 -37.117 10.734 0.50 49.21  ? 13  ARG A NH1 1 
ATOM   96   N  NH2 A ARG A 1 12  ? 24.286 -32.939 16.734 0.50 44.50  ? 13  ARG A NH2 1 
ATOM   97   N  NH2 B ARG A 1 12  ? 23.437 -36.533 9.959  0.50 33.00  ? 13  ARG A NH2 1 
ATOM   98   N  N   . HIS A 1 13  ? 25.141 -29.872 9.863  1.00 18.57  ? 14  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 26.353 -29.071 9.552  1.00 17.76  ? 14  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 26.649 -27.960 10.563 1.00 20.49  ? 14  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 27.780 -27.873 11.053 1.00 19.30  ? 14  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 26.317 -28.495 8.123  1.00 17.70  ? 14  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 27.587 -27.744 7.807  1.00 19.17  ? 14  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 28.763 -28.413 7.609  1.00 19.80  ? 14  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 27.810 -26.413 7.694  1.00 20.19  ? 14  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 29.683 -27.488 7.357  1.00 19.06  ? 14  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 29.157 -26.261 7.403  1.00 19.00  ? 14  HIS A NE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 25.662 -27.087 10.833 1.00 17.25  ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.869 -25.960 11.769 1.00 17.78  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 26.267 -26.442 13.174 1.00 20.29  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 27.169 -25.861 13.771 1.00 18.54  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 24.627 -25.073 11.826 1.00 18.71  ? 15  ALA A CB  1 
ATOM   113  N  N   A SER A 1 15  ? 25.601 -27.489 13.684 0.38 17.79  ? 16  SER A N   1 
ATOM   114  N  N   B SER A 1 15  ? 25.605 -27.500 13.684 0.33 18.11  ? 16  SER A N   1 
ATOM   115  N  N   C SER A 1 15  ? 25.600 -27.495 13.694 0.29 17.76  ? 16  SER A N   1 
ATOM   116  C  CA  A SER A 1 15  ? 25.908 -28.046 15.000 0.38 17.74  ? 16  SER A CA  1 
ATOM   117  C  CA  B SER A 1 15  ? 25.899 -28.079 14.998 0.33 18.26  ? 16  SER A CA  1 
ATOM   118  C  CA  C SER A 1 15  ? 25.913 -28.044 15.018 0.29 17.74  ? 16  SER A CA  1 
ATOM   119  C  C   A SER A 1 15  ? 27.322 -28.641 15.024 0.38 22.02  ? 16  SER A C   1 
ATOM   120  C  C   B SER A 1 15  ? 27.312 -28.661 15.030 0.33 22.40  ? 16  SER A C   1 
ATOM   121  C  C   C SER A 1 15  ? 27.314 -28.671 15.043 0.29 22.28  ? 16  SER A C   1 
ATOM   122  O  O   A SER A 1 15  ? 28.044 -28.440 16.004 0.38 19.74  ? 16  SER A O   1 
ATOM   123  O  O   B SER A 1 15  ? 28.025 -28.468 16.018 0.33 20.47  ? 16  SER A O   1 
ATOM   124  O  O   C SER A 1 15  ? 28.028 -28.507 16.034 0.29 20.58  ? 16  SER A O   1 
ATOM   125  C  CB  A SER A 1 15  ? 24.876 -29.100 15.392 0.38 20.80  ? 16  SER A CB  1 
ATOM   126  C  CB  B SER A 1 15  ? 24.883 -29.166 15.347 0.33 21.91  ? 16  SER A CB  1 
ATOM   127  C  CB  C SER A 1 15  ? 24.849 -29.046 15.468 0.29 20.82  ? 16  SER A CB  1 
ATOM   128  O  OG  A SER A 1 15  ? 25.217 -29.660 16.647 0.38 21.86  ? 16  SER A OG  1 
ATOM   129  O  OG  B SER A 1 15  ? 23.573 -28.632 15.408 0.33 26.11  ? 16  SER A OG  1 
ATOM   130  O  OG  C SER A 1 15  ? 24.836 -30.211 14.661 0.29 23.21  ? 16  SER A OG  1 
ATOM   131  N  N   . ASP A 1 16  ? 27.717 -29.351 13.943 1.00 20.21  ? 17  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 16  ? 29.052 -29.974 13.816 1.00 20.69  ? 17  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 16  ? 30.119 -28.886 13.774 1.00 20.65  ? 17  ASP A C   1 
ATOM   134  O  O   . ASP A 1 16  ? 31.171 -29.053 14.385 1.00 20.33  ? 17  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 16  ? 29.144 -30.853 12.551 1.00 22.37  ? 17  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 16  ? 28.393 -32.179 12.626 1.00 30.41  ? 17  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 16  ? 27.877 -32.517 13.719 1.00 29.90  ? 17  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 16  ? 28.309 -32.869 11.589 1.00 31.04  ? 17  ASP A OD2 1 
ATOM   139  N  N   . VAL A 1 17  ? 29.845 -27.772 13.056 1.00 15.81  ? 18  VAL A N   1 
ATOM   140  C  CA  . VAL A 1 17  ? 30.794 -26.634 13.019 1.00 15.74  ? 18  VAL A CA  1 
ATOM   141  C  C   . VAL A 1 17  ? 30.996 -26.080 14.450 1.00 18.92  ? 18  VAL A C   1 
ATOM   142  O  O   . VAL A 1 17  ? 32.123 -25.870 14.891 1.00 17.31  ? 18  VAL A O   1 
ATOM   143  C  CB  . VAL A 1 17  ? 30.317 -25.517 12.051 1.00 18.19  ? 18  VAL A CB  1 
ATOM   144  C  CG1 . VAL A 1 17  ? 31.104 -24.210 12.274 1.00 17.82  ? 18  VAL A CG1 1 
ATOM   145  C  CG2 . VAL A 1 17  ? 30.424 -25.974 10.591 1.00 17.85  ? 18  VAL A CG2 1 
ATOM   146  N  N   . LEU A 1 18  ? 29.899 -25.840 15.167 1.00 17.02  ? 19  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 18  ? 29.993 -25.260 16.505 1.00 17.55  ? 19  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 18  ? 30.726 -26.200 17.468 1.00 20.39  ? 19  LEU A C   1 
ATOM   149  O  O   . LEU A 1 18  ? 31.564 -25.736 18.254 1.00 18.39  ? 19  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 18  ? 28.599 -24.886 17.037 1.00 18.37  ? 19  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 18  ? 28.614 -23.987 18.288 1.00 21.85  ? 19  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 18  ? 29.143 -22.596 17.960 1.00 21.41  ? 19  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 18  ? 27.208 -23.877 18.878 1.00 26.01  ? 19  LEU A CD2 1 
ATOM   154  N  N   . LEU A 1 19  ? 30.457 -27.514 17.356 1.00 18.74  ? 20  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 19  ? 31.128 -28.546 18.160 1.00 19.99  ? 20  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 19  ? 32.642 -28.470 17.913 1.00 20.99  ? 20  LEU A C   1 
ATOM   157  O  O   . LEU A 1 19  ? 33.432 -28.446 18.876 1.00 19.54  ? 20  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 19  ? 30.580 -29.929 17.783 1.00 22.13  ? 20  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 19  ? 31.176 -31.113 18.533 1.00 31.27  ? 20  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 19  ? 30.737 -31.091 20.001 1.00 34.07  ? 20  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 19  ? 30.722 -32.418 17.898 1.00 36.45  ? 20  LEU A CD2 1 
ATOM   162  N  N   . ASN A 1 20  ? 33.045 -28.363 16.634 1.00 17.32  ? 21  ASN A N   1 
ATOM   163  C  CA  . ASN A 1 20  ? 34.469 -28.249 16.301 1.00 16.75  ? 21  ASN A CA  1 
ATOM   164  C  C   . ASN A 1 20  ? 35.087 -26.940 16.787 1.00 19.10  ? 21  ASN A C   1 
ATOM   165  O  O   . ASN A 1 20  ? 36.235 -26.946 17.221 1.00 18.96  ? 21  ASN A O   1 
ATOM   166  C  CB  . ASN A 1 20  ? 34.703 -28.478 14.814 1.00 18.03  ? 21  ASN A CB  1 
ATOM   167  C  CG  . ASN A 1 20  ? 34.623 -29.947 14.463 1.00 28.94  ? 21  ASN A CG  1 
ATOM   168  O  OD1 . ASN A 1 20  ? 34.781 -30.814 15.323 1.00 24.89  ? 21  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A 1 20  ? 34.357 -30.259 13.207 1.00 21.56  ? 21  ASN A ND2 1 
ATOM   170  N  N   . LEU A 1 21  ? 34.345 -25.822 16.713 1.00 17.43  ? 22  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 21  ? 34.844 -24.545 17.236 1.00 17.31  ? 22  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 21  ? 35.062 -24.685 18.747 1.00 19.02  ? 22  LEU A C   1 
ATOM   173  O  O   . LEU A 1 21  ? 36.042 -24.157 19.283 1.00 17.15  ? 22  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 21  ? 33.847 -23.404 16.930 1.00 16.87  ? 22  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 21  ? 33.752 -23.053 15.424 1.00 18.69  ? 22  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 21  ? 32.662 -22.004 15.186 1.00 19.05  ? 22  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 21  ? 35.131 -22.611 14.835 1.00 22.25  ? 22  LEU A CD2 1 
ATOM   178  N  N   . ASN A 1 22  ? 34.136 -25.379 19.443 1.00 16.90  ? 23  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 22  ? 34.313 -25.570 20.898 1.00 18.04  ? 23  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 22  ? 35.543 -26.463 21.201 1.00 22.70  ? 23  ASN A C   1 
ATOM   181  O  O   . ASN A 1 22  ? 36.265 -26.211 22.170 1.00 22.46  ? 23  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 22  ? 33.048 -26.129 21.534 1.00 20.29  ? 23  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 22  ? 33.069 -26.003 23.045 1.00 26.55  ? 23  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 22  ? 33.566 -25.026 23.604 1.00 24.24  ? 23  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 22  ? 32.541 -26.995 23.709 1.00 27.75  ? 23  ASN A ND2 1 
ATOM   186  N  N   . ARG A 1 23  ? 35.803 -27.482 20.353 1.00 19.81  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 23  ? 36.999 -28.339 20.502 1.00 20.04  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 23  ? 38.271 -27.495 20.338 1.00 23.61  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 23  ? 39.221 -27.683 21.088 1.00 23.72  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 23  ? 37.004 -29.476 19.471 1.00 20.31  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 23  ? 36.015 -30.587 19.805 1.00 26.16  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 23  ? 35.739 -31.458 18.587 1.00 29.43  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 23  ? 34.880 -32.591 18.917 1.00 36.97  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 23  ? 34.397 -33.456 18.030 1.00 56.41  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 23  ? 34.631 -33.289 16.731 1.00 41.90  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 23  ? 33.662 -34.483 18.433 1.00 44.75  ? 24  ARG A NH2 1 
ATOM   197  N  N   . LEU A 1 24  ? 38.282 -26.548 19.369 1.00 20.27  ? 25  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 24  ? 39.427 -25.647 19.205 1.00 19.64  ? 25  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 24  ? 39.579 -24.784 20.458 1.00 24.14  ? 25  LEU A C   1 
ATOM   200  O  O   . LEU A 1 24  ? 40.705 -24.610 20.953 1.00 24.69  ? 25  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 24  ? 39.256 -24.745 17.987 1.00 19.29  ? 25  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 24  ? 39.221 -25.452 16.608 1.00 23.63  ? 25  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 24  ? 39.070 -24.414 15.485 1.00 23.27  ? 25  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 24  ? 40.474 -26.295 16.380 1.00 25.79  ? 25  LEU A CD2 1 
ATOM   205  N  N   . ARG A 1 25  ? 38.447 -24.255 20.988 1.00 20.11  ? 26  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 25  ? 38.516 -23.458 22.222 1.00 21.00  ? 26  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 25  ? 39.137 -24.273 23.396 1.00 25.78  ? 26  ARG A C   1 
ATOM   208  O  O   . ARG A 1 25  ? 40.029 -23.751 24.095 1.00 25.43  ? 26  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 25  ? 37.124 -22.923 22.620 1.00 21.63  ? 26  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 25  ? 37.220 -22.071 23.896 1.00 26.87  ? 26  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 25  ? 35.912 -21.422 24.245 1.00 27.40  ? 26  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 25  ? 34.890 -22.396 24.614 1.00 26.11  ? 26  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 25  ? 34.282 -22.451 25.796 1.00 38.87  ? 26  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 25  ? 34.653 -21.640 26.782 1.00 32.58  ? 26  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 25  ? 33.324 -23.338 26.013 1.00 29.03  ? 26  ARG A NH2 1 
ATOM   216  N  N   A SER A 1 26  ? 38.658 -25.510 23.609 0.40 23.77  ? 27  SER A N   1 
ATOM   217  N  N   B SER A 1 26  ? 38.660 -25.515 23.613 0.35 23.63  ? 27  SER A N   1 
ATOM   218  N  N   C SER A 1 26  ? 38.661 -25.520 23.601 0.25 23.32  ? 27  SER A N   1 
ATOM   219  C  CA  A SER A 1 26  ? 39.137 -26.400 24.675 0.40 25.42  ? 27  SER A CA  1 
ATOM   220  C  CA  B SER A 1 26  ? 39.128 -26.396 24.693 0.35 25.19  ? 27  SER A CA  1 
ATOM   221  C  CA  C SER A 1 26  ? 39.102 -26.444 24.658 0.25 24.71  ? 27  SER A CA  1 
ATOM   222  C  C   A SER A 1 26  ? 40.646 -26.583 24.600 0.40 30.08  ? 27  SER A C   1 
ATOM   223  C  C   B SER A 1 26  ? 40.624 -26.706 24.604 0.35 30.32  ? 27  SER A C   1 
ATOM   224  C  C   C SER A 1 26  ? 40.601 -26.749 24.592 0.25 30.03  ? 27  SER A C   1 
ATOM   225  O  O   A SER A 1 26  ? 41.333 -26.504 25.623 0.40 30.73  ? 27  SER A O   1 
ATOM   226  O  O   B SER A 1 26  ? 41.278 -26.861 25.637 0.35 31.40  ? 27  SER A O   1 
ATOM   227  O  O   C SER A 1 26  ? 41.229 -26.963 25.631 0.25 30.98  ? 27  SER A O   1 
ATOM   228  C  CB  A SER A 1 26  ? 38.474 -27.769 24.563 0.40 29.64  ? 27  SER A CB  1 
ATOM   229  C  CB  B SER A 1 26  ? 38.312 -27.685 24.738 0.35 28.92  ? 27  SER A CB  1 
ATOM   230  C  CB  C SER A 1 26  ? 38.302 -27.742 24.596 0.25 28.14  ? 27  SER A CB  1 
ATOM   231  O  OG  A SER A 1 26  ? 37.089 -27.721 24.851 0.40 37.76  ? 27  SER A OG  1 
ATOM   232  O  OG  B SER A 1 26  ? 38.578 -28.534 23.634 0.35 35.65  ? 27  SER A OG  1 
ATOM   233  O  OG  C SER A 1 26  ? 38.697 -28.662 25.601 0.25 35.73  ? 27  SER A OG  1 
ATOM   234  N  N   . ARG A 1 27  ? 41.161 -26.781 23.374 1.00 26.34  ? 28  ARG A N   1 
ATOM   235  C  CA  . ARG A 1 27  ? 42.584 -27.046 23.129 1.00 28.38  ? 28  ARG A CA  1 
ATOM   236  C  C   . ARG A 1 27  ? 43.390 -25.766 22.924 1.00 30.75  ? 28  ARG A C   1 
ATOM   237  O  O   . ARG A 1 27  ? 44.600 -25.829 22.685 1.00 32.10  ? 28  ARG A O   1 
ATOM   238  C  CB  . ARG A 1 27  ? 42.718 -28.021 21.961 1.00 30.94  ? 28  ARG A CB  1 
ATOM   239  C  CG  . ARG A 1 27  ? 41.956 -29.324 22.209 1.00 41.43  ? 28  ARG A CG  1 
ATOM   240  C  CD  . ARG A 1 27  ? 41.945 -30.206 20.992 1.00 49.29  ? 28  ARG A CD  1 
ATOM   241  N  NE  . ARG A 1 27  ? 43.275 -30.759 20.737 1.00 66.40  ? 28  ARG A NE  1 
ATOM   242  C  CZ  . ARG A 1 27  ? 43.784 -30.927 19.525 1.00 82.08  ? 28  ARG A CZ  1 
ATOM   243  N  NH1 . ARG A 1 27  ? 45.000 -31.433 19.375 1.00 72.01  ? 28  ARG A NH1 1 
ATOM   244  N  NH2 . ARG A 1 27  ? 43.085 -30.588 18.455 1.00 68.18  ? 28  ARG A NH2 1 
ATOM   245  N  N   . ASP A 1 28  ? 42.727 -24.602 23.074 1.00 25.13  ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 28  ? 43.314 -23.263 22.930 1.00 25.93  ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 28  ? 43.949 -23.066 21.529 1.00 30.61  ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 28  ? 45.022 -22.469 21.388 1.00 31.40  ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 28  ? 44.322 -22.968 24.076 1.00 28.80  ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 28  ? 44.655 -21.505 24.238 1.00 36.70  ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 28  ? 43.749 -20.661 24.035 1.00 35.64  ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 28  ? 45.821 -21.198 24.558 1.00 41.33  ? 29  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 29  ? 43.294 -23.611 20.508 1.00 24.72  ? 30  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 29  ? 43.778 -23.523 19.130 1.00 23.66  ? 30  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 29  ? 43.179 -22.323 18.424 1.00 26.10  ? 30  ILE A C   1 
ATOM   256  O  O   . ILE A 1 29  ? 41.946 -22.199 18.336 1.00 22.77  ? 30  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 29  ? 43.537 -24.834 18.339 1.00 26.46  ? 30  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 29  ? 44.334 -26.022 18.958 1.00 28.23  ? 30  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 29  ? 43.877 -24.654 16.833 1.00 25.05  ? 30  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 29  ? 43.801 -27.400 18.477 1.00 28.87  ? 30  ILE A CD1 1 
ATOM   261  N  N   A LEU A 1 30  ? 44.054 -21.432 17.920 0.54 24.23  ? 31  LEU A N   1 
ATOM   262  N  N   B LEU A 1 30  ? 44.062 -21.436 17.924 0.46 24.83  ? 31  LEU A N   1 
ATOM   263  C  CA  A LEU A 1 30  ? 43.693 -20.230 17.157 0.54 23.98  ? 31  LEU A CA  1 
ATOM   264  C  CA  B LEU A 1 30  ? 43.736 -20.222 17.170 0.46 24.93  ? 31  LEU A CA  1 
ATOM   265  C  C   A LEU A 1 30  ? 42.814 -19.227 17.917 0.54 25.65  ? 31  LEU A C   1 
ATOM   266  C  C   B LEU A 1 30  ? 42.828 -19.230 17.914 0.46 26.30  ? 31  LEU A C   1 
ATOM   267  O  O   A LEU A 1 30  ? 42.201 -18.356 17.294 0.54 23.36  ? 31  LEU A O   1 
ATOM   268  O  O   B LEU A 1 30  ? 42.210 -18.369 17.281 0.46 24.29  ? 31  LEU A O   1 
ATOM   269  C  CB  A LEU A 1 30  ? 43.066 -20.578 15.795 0.54 23.90  ? 31  LEU A CB  1 
ATOM   270  C  CB  B LEU A 1 30  ? 43.180 -20.545 15.782 0.46 25.19  ? 31  LEU A CB  1 
ATOM   271  C  CG  A LEU A 1 30  ? 43.993 -21.216 14.727 0.54 29.23  ? 31  LEU A CG  1 
ATOM   272  C  CG  B LEU A 1 30  ? 44.223 -20.413 14.676 0.46 31.10  ? 31  LEU A CG  1 
ATOM   273  C  CD1 A LEU A 1 30  ? 43.482 -20.915 13.368 0.54 27.53  ? 31  LEU A CD1 1 
ATOM   274  C  CD1 B LEU A 1 30  ? 44.618 -21.770 14.117 0.46 31.74  ? 31  LEU A CD1 1 
ATOM   275  C  CD2 A LEU A 1 30  ? 45.427 -20.704 14.806 0.54 32.25  ? 31  LEU A CD2 1 
ATOM   276  C  CD2 B LEU A 1 30  ? 43.739 -19.485 13.593 0.46 32.82  ? 31  LEU A CD2 1 
ATOM   277  N  N   . THR A 1 31  ? 42.817 -19.291 19.257 1.00 22.99  ? 32  THR A N   1 
ATOM   278  C  CA  . THR A 1 31  ? 42.101 -18.302 20.086 1.00 22.33  ? 32  THR A CA  1 
ATOM   279  C  C   . THR A 1 31  ? 42.921 -17.014 19.888 1.00 27.46  ? 32  THR A C   1 
ATOM   280  O  O   . THR A 1 31  ? 44.155 -17.072 19.738 1.00 27.78  ? 32  THR A O   1 
ATOM   281  C  CB  . THR A 1 31  ? 42.063 -18.721 21.556 1.00 27.97  ? 32  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 31  ? 43.383 -19.097 21.914 1.00 29.32  ? 32  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 31  ? 41.099 -19.903 21.799 1.00 25.83  ? 32  THR A CG2 1 
ATOM   284  N  N   . ASP A 1 32  ? 42.241 -15.886 19.744 1.00 23.90  ? 33  ASP A N   1 
ATOM   285  C  CA  . ASP A 1 32  ? 42.914 -14.638 19.395 1.00 23.89  ? 33  ASP A CA  1 
ATOM   286  C  C   . ASP A 1 32  ? 42.574 -13.479 20.297 1.00 25.96  ? 33  ASP A C   1 
ATOM   287  O  O   . ASP A 1 32  ? 42.903 -12.332 19.983 1.00 25.49  ? 33  ASP A O   1 
ATOM   288  C  CB  . ASP A 1 32  ? 42.600 -14.291 17.936 1.00 24.80  ? 33  ASP A CB  1 
ATOM   289  C  CG  . ASP A 1 32  ? 41.113 -14.303 17.592 1.00 31.87  ? 33  ASP A CG  1 
ATOM   290  O  OD1 . ASP A 1 32  ? 40.276 -14.340 18.532 1.00 27.95  ? 33  ASP A OD1 1 
ATOM   291  O  OD2 . ASP A 1 32  ? 40.789 -14.302 16.396 1.00 39.48  ? 33  ASP A OD2 1 
ATOM   292  N  N   . VAL A 1 33  ? 41.926 -13.767 21.424 1.00 21.92  ? 34  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 33  ? 41.596 -12.720 22.398 1.00 21.40  ? 34  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 33  ? 41.424 -13.320 23.776 1.00 25.03  ? 34  VAL A C   1 
ATOM   295  O  O   . VAL A 1 33  ? 41.033 -14.494 23.910 1.00 25.06  ? 34  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 33  ? 40.313 -11.908 21.967 1.00 23.82  ? 34  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 33  ? 39.011 -12.713 22.136 1.00 22.17  ? 34  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 33  ? 40.217 -10.549 22.694 1.00 24.15  ? 34  VAL A CG2 1 
ATOM   299  N  N   A VAL A 1 34  ? 41.700 -12.499 24.801 0.53 22.72  ? 35  VAL A N   1 
ATOM   300  N  N   B VAL A 1 34  ? 41.709 -12.517 24.804 0.47 22.61  ? 35  VAL A N   1 
ATOM   301  C  CA  A VAL A 1 34  ? 41.478 -12.813 26.204 0.53 22.35  ? 35  VAL A CA  1 
ATOM   302  C  CA  B VAL A 1 34  ? 41.439 -12.883 26.180 0.47 22.21  ? 35  VAL A CA  1 
ATOM   303  C  C   A VAL A 1 34  ? 40.411 -11.827 26.683 0.53 25.03  ? 35  VAL A C   1 
ATOM   304  C  C   B VAL A 1 34  ? 40.457 -11.853 26.753 0.47 25.24  ? 35  VAL A C   1 
ATOM   305  O  O   A VAL A 1 34  ? 40.549 -10.613 26.479 0.53 25.40  ? 35  VAL A O   1 
ATOM   306  O  O   B VAL A 1 34  ? 40.668 -10.642 26.624 0.47 25.81  ? 35  VAL A O   1 
ATOM   307  C  CB  A VAL A 1 34  ? 42.774 -12.690 27.060 0.53 27.22  ? 35  VAL A CB  1 
ATOM   308  C  CB  B VAL A 1 34  ? 42.688 -13.169 27.064 0.47 27.00  ? 35  VAL A CB  1 
ATOM   309  C  CG1 A VAL A 1 34  ? 42.503 -12.956 28.542 0.53 27.29  ? 35  VAL A CG1 1 
ATOM   310  C  CG1 B VAL A 1 34  ? 43.557 -11.934 27.265 0.47 27.69  ? 35  VAL A CG1 1 
ATOM   311  C  CG2 A VAL A 1 34  ? 43.861 -13.616 26.548 0.53 27.82  ? 35  VAL A CG2 1 
ATOM   312  C  CG2 B VAL A 1 34  ? 42.290 -13.775 28.406 0.47 27.17  ? 35  VAL A CG2 1 
ATOM   313  N  N   . ILE A 1 35  ? 39.355 -12.342 27.308 1.00 20.98  ? 36  ILE A N   1 
ATOM   314  C  CA  . ILE A 1 35  ? 38.316 -11.515 27.911 1.00 20.28  ? 36  ILE A CA  1 
ATOM   315  C  C   . ILE A 1 35  ? 38.603 -11.537 29.413 1.00 25.52  ? 36  ILE A C   1 
ATOM   316  O  O   . ILE A 1 35  ? 38.637 -12.617 30.028 1.00 24.84  ? 36  ILE A O   1 
ATOM   317  C  CB  . ILE A 1 35  ? 36.872 -11.990 27.593 1.00 21.53  ? 36  ILE A CB  1 
ATOM   318  C  CG1 . ILE A 1 35  ? 36.637 -12.164 26.058 1.00 21.05  ? 36  ILE A CG1 1 
ATOM   319  C  CG2 . ILE A 1 35  ? 35.845 -11.049 28.224 1.00 23.24  ? 36  ILE A CG2 1 
ATOM   320  C  CD1 . ILE A 1 35  ? 36.943 -10.902 25.163 1.00 21.94  ? 36  ILE A CD1 1 
ATOM   321  N  N   . VAL A 1 36  ? 38.819 -10.350 29.989 1.00 22.66  ? 37  VAL A N   1 
ATOM   322  C  CA  . VAL A 1 36  ? 39.129 -10.207 31.418 1.00 23.34  ? 37  VAL A CA  1 
ATOM   323  C  C   . VAL A 1 36  ? 37.866 -9.771  32.159 1.00 27.81  ? 37  VAL A C   1 
ATOM   324  O  O   . VAL A 1 36  ? 37.271 -8.730  31.835 1.00 26.92  ? 37  VAL A O   1 
ATOM   325  C  CB  . VAL A 1 36  ? 40.326 -9.234  31.653 1.00 27.85  ? 37  VAL A CB  1 
ATOM   326  C  CG1 . VAL A 1 36  ? 40.637 -9.074  33.143 1.00 28.55  ? 37  VAL A CG1 1 
ATOM   327  C  CG2 . VAL A 1 36  ? 41.574 -9.707  30.913 1.00 28.59  ? 37  VAL A CG2 1 
ATOM   328  N  N   . VAL A 1 37  ? 37.484 -10.550 33.188 1.00 24.74  ? 38  VAL A N   1 
ATOM   329  C  CA  . VAL A 1 37  ? 36.285 -10.315 33.992 1.00 24.72  ? 38  VAL A CA  1 
ATOM   330  C  C   . VAL A 1 37  ? 36.754 -10.381 35.439 1.00 29.94  ? 38  VAL A C   1 
ATOM   331  O  O   . VAL A 1 37  ? 36.998 -11.476 35.950 1.00 28.13  ? 38  VAL A O   1 
ATOM   332  C  CB  . VAL A 1 37  ? 35.181 -11.351 33.662 1.00 27.94  ? 38  VAL A CB  1 
ATOM   333  C  CG1 . VAL A 1 37  ? 33.847 -10.951 34.288 1.00 28.06  ? 38  VAL A CG1 1 
ATOM   334  C  CG2 . VAL A 1 37  ? 35.028 -11.535 32.146 1.00 26.62  ? 38  VAL A CG2 1 
ATOM   335  N  N   A SER A 1 38  ? 36.636 -9.282  36.208 0.50 29.83  ? 39  SER A N   1 
ATOM   336  N  N   B SER A 1 38  ? 37.288 -9.193  35.827 0.50 26.77  ? 39  SER A N   1 
ATOM   337  C  CA  A SER A 1 38  ? 37.005 -9.280  37.641 0.50 31.44  ? 39  SER A CA  1 
ATOM   338  C  CA  B SER A 1 38  ? 37.963 -8.825  37.060 0.50 27.09  ? 39  SER A CA  1 
ATOM   339  C  C   A SER A 1 38  ? 38.267 -10.158 37.934 0.50 36.25  ? 39  SER A C   1 
ATOM   340  C  C   B SER A 1 38  ? 39.239 -9.649  37.218 0.50 30.06  ? 39  SER A C   1 
ATOM   341  O  O   A SER A 1 38  ? 38.232 -11.024 38.813 0.50 36.08  ? 39  SER A O   1 
ATOM   342  O  O   B SER A 1 38  ? 40.164 -9.431  36.435 0.50 28.12  ? 39  SER A O   1 
ATOM   343  C  CB  A SER A 1 38  ? 35.819 -9.718  38.508 0.50 36.49  ? 39  SER A CB  1 
ATOM   344  C  CB  B SER A 1 38  ? 37.014 -8.870  38.251 0.50 31.50  ? 39  SER A CB  1 
ATOM   345  O  OG  A SER A 1 38  ? 34.766 -8.765  38.537 0.50 47.68  ? 39  SER A OG  1 
ATOM   346  O  OG  B SER A 1 38  ? 36.026 -7.866  38.081 0.50 37.10  ? 39  SER A OG  1 
ATOM   347  N  N   A ARG A 1 39  ? 39.346 -9.965  37.131 0.50 33.01  ? 40  ARG A N   1 
ATOM   348  N  N   B ARG A 1 39  ? 39.295 -10.624 38.145 0.50 27.68  ? 40  ARG A N   1 
ATOM   349  C  CA  A ARG A 1 39  ? 40.629 -10.694 37.194 0.50 33.67  ? 40  ARG A CA  1 
ATOM   350  C  CA  B ARG A 1 39  ? 40.520 -11.415 38.273 0.50 28.68  ? 40  ARG A CA  1 
ATOM   351  C  C   A ARG A 1 39  ? 40.503 -12.235 36.951 0.50 35.90  ? 40  ARG A C   1 
ATOM   352  C  C   B ARG A 1 39  ? 40.654 -12.434 37.101 0.50 33.18  ? 40  ARG A C   1 
ATOM   353  O  O   A ARG A 1 39  ? 41.277 -13.044 37.499 0.50 36.87  ? 40  ARG A O   1 
ATOM   354  O  O   B ARG A 1 39  ? 41.680 -12.440 36.401 0.50 33.60  ? 40  ARG A O   1 
ATOM   355  C  CB  A ARG A 1 39  ? 41.411 -10.398 38.488 0.50 35.11  ? 40  ARG A CB  1 
ATOM   356  C  CB  B ARG A 1 39  ? 40.652 -12.048 39.682 0.50 29.96  ? 40  ARG A CB  1 
ATOM   357  C  CG  A ARG A 1 39  ? 41.938 -8.974  38.616 0.50 46.59  ? 40  ARG A CG  1 
ATOM   358  C  CG  B ARG A 1 39  ? 40.945 -11.001 40.774 0.50 36.70  ? 40  ARG A CG  1 
ATOM   359  C  CD  A ARG A 1 39  ? 43.046 -8.922  39.652 0.50 53.57  ? 40  ARG A CD  1 
ATOM   360  C  CD  B ARG A 1 39  ? 41.337 -11.590 42.123 0.50 36.66  ? 40  ARG A CD  1 
ATOM   361  N  NE  A ARG A 1 39  ? 43.403 -7.557  40.043 0.50 60.14  ? 40  ARG A NE  1 
ATOM   362  N  NE  B ARG A 1 39  ? 41.504 -10.564 43.157 0.50 38.10  ? 40  ARG A NE  1 
ATOM   363  C  CZ  A ARG A 1 39  ? 42.824 -6.880  41.032 0.50 72.01  ? 40  ARG A CZ  1 
ATOM   364  C  CZ  B ARG A 1 39  ? 42.666 -10.022 43.519 0.50 51.77  ? 40  ARG A CZ  1 
ATOM   365  N  NH1 A ARG A 1 39  ? 41.828 -7.422  41.724 0.50 56.43  ? 40  ARG A NH1 1 
ATOM   366  N  NH1 B ARG A 1 39  ? 43.793 -10.386 42.921 0.50 38.36  ? 40  ARG A NH1 1 
ATOM   367  N  NH2 A ARG A 1 39  ? 43.225 -5.649  41.325 0.50 58.85  ? 40  ARG A NH2 1 
ATOM   368  N  NH2 B ARG A 1 39  ? 42.708 -9.107  44.476 0.50 44.46  ? 40  ARG A NH2 1 
ATOM   369  N  N   A GLU A 1 40  ? 39.526 -12.624 36.130 0.50 28.57  ? 41  GLU A N   1 
ATOM   370  N  N   B GLU A 1 40  ? 39.573 -13.178 36.811 0.50 27.07  ? 41  GLU A N   1 
ATOM   371  C  CA  A GLU A 1 40  ? 39.329 -13.996 35.661 0.50 27.86  ? 41  GLU A CA  1 
ATOM   372  C  CA  B GLU A 1 40  ? 39.532 -14.242 35.802 0.50 25.61  ? 41  GLU A CA  1 
ATOM   373  C  C   A GLU A 1 40  ? 39.468 -13.865 34.154 0.50 29.24  ? 41  GLU A C   1 
ATOM   374  C  C   B GLU A 1 40  ? 39.769 -13.788 34.353 0.50 27.34  ? 41  GLU A C   1 
ATOM   375  O  O   A GLU A 1 40  ? 38.890 -12.947 33.563 0.50 26.68  ? 41  GLU A O   1 
ATOM   376  O  O   B GLU A 1 40  ? 39.470 -12.657 33.976 0.50 23.91  ? 41  GLU A O   1 
ATOM   377  C  CB  A GLU A 1 40  ? 37.964 -14.574 36.075 0.50 29.15  ? 41  GLU A CB  1 
ATOM   378  C  CB  B GLU A 1 40  ? 38.220 -15.047 35.898 0.50 26.50  ? 41  GLU A CB  1 
ATOM   379  C  CG  A GLU A 1 40  ? 37.855 -14.797 37.579 0.50 42.96  ? 41  GLU A CG  1 
ATOM   380  C  CG  B GLU A 1 40  ? 37.715 -15.209 37.328 0.50 41.65  ? 41  GLU A CG  1 
ATOM   381  C  CD  A GLU A 1 40  ? 37.829 -16.243 38.032 0.50 76.74  ? 41  GLU A CD  1 
ATOM   382  C  CD  B GLU A 1 40  ? 37.883 -16.555 38.005 0.50 77.83  ? 41  GLU A CD  1 
ATOM   383  O  OE1 A GLU A 1 40  ? 36.798 -16.662 38.608 0.50 79.06  ? 41  GLU A OE1 1 
ATOM   384  O  OE1 B GLU A 1 40  ? 38.940 -17.203 37.819 0.50 78.58  ? 41  GLU A OE1 1 
ATOM   385  O  OE2 A GLU A 1 40  ? 38.836 -16.957 37.820 0.50 76.00  ? 41  GLU A OE2 1 
ATOM   386  O  OE2 B GLU A 1 40  ? 36.959 -16.950 38.752 0.50 79.14  ? 41  GLU A OE2 1 
ATOM   387  N  N   . GLN A 1 41  ? 40.293 -14.724 33.541 1.00 25.43  ? 42  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 41  ? 40.617 -14.582 32.129 1.00 25.06  ? 42  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 41  ? 40.007 -15.695 31.324 1.00 27.75  ? 42  GLN A C   1 
ATOM   390  O  O   . GLN A 1 41  ? 40.078 -16.854 31.735 1.00 28.06  ? 42  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 41  ? 42.147 -14.582 31.975 1.00 27.92  ? 42  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 41  ? 42.795 -13.321 32.533 1.00 43.37  ? 42  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 41  ? 44.272 -13.207 32.248 1.00 62.54  ? 42  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 41  ? 44.871 -13.989 31.495 1.00 55.34  ? 42  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 41  ? 44.890 -12.209 32.850 1.00 66.38  ? 42  GLN A NE2 1 
ATOM   396  N  N   . PHE A 1 42  ? 39.411 -15.351 30.169 1.00 21.81  ? 43  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 42  ? 38.769 -16.342 29.297 1.00 22.18  ? 43  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 42  ? 39.291 -16.184 27.887 1.00 26.41  ? 43  PHE A C   1 
ATOM   399  O  O   . PHE A 1 42  ? 39.135 -15.115 27.303 1.00 26.48  ? 43  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 42  ? 37.241 -16.140 29.302 1.00 23.33  ? 43  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 42  ? 36.628 -16.256 30.674 1.00 25.27  ? 43  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 42  ? 36.498 -15.136 31.495 1.00 26.57  ? 43  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 42  ? 36.145 -17.477 31.135 1.00 27.27  ? 43  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 42  ? 35.940 -15.247 32.771 1.00 28.87  ? 43  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 42  ? 35.586 -17.587 32.411 1.00 30.51  ? 43  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 42  ? 35.472 -16.468 33.216 1.00 28.41  ? 43  PHE A CZ  1 
ATOM   407  N  N   . ARG A 1 43  ? 39.904 -17.238 27.333 1.00 22.83  ? 44  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 43  ? 40.416 -17.185 25.958 1.00 21.47  ? 44  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 43  ? 39.273 -17.579 25.001 1.00 25.35  ? 44  ARG A C   1 
ATOM   410  O  O   . ARG A 1 43  ? 38.466 -18.470 25.312 1.00 23.93  ? 44  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 43  ? 41.649 -18.104 25.784 1.00 23.77  ? 44  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 43  ? 42.875 -17.687 26.645 1.00 32.08  ? 44  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 43  ? 44.208 -18.111 26.018 1.00 42.42  ? 44  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 43  ? 44.250 -17.730 24.600 1.00 53.86  ? 44  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 43  ? 44.782 -16.610 24.119 1.00 64.77  ? 44  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 43  ? 45.432 -15.779 24.920 1.00 58.26  ? 44  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 43  ? 44.717 -16.343 22.823 1.00 46.42  ? 44  ARG A NH2 1 
ATOM   418  N  N   . ALA A 1 44  ? 39.177 -16.912 23.847 1.00 21.23  ? 45  ALA A N   1 
ATOM   419  C  CA  . ALA A 1 44  ? 38.098 -17.214 22.895 1.00 21.07  ? 45  ALA A CA  1 
ATOM   420  C  C   . ALA A 1 44  ? 38.506 -16.808 21.493 1.00 22.04  ? 45  ALA A C   1 
ATOM   421  O  O   . ALA A 1 44  ? 39.608 -16.260 21.292 1.00 21.33  ? 45  ALA A O   1 
ATOM   422  C  CB  . ALA A 1 44  ? 36.815 -16.472 23.302 1.00 21.48  ? 45  ALA A CB  1 
ATOM   423  N  N   . HIS A 1 45  ? 37.609 -17.059 20.534 1.00 18.52  ? 46  HIS A N   1 
ATOM   424  C  CA  . HIS A 1 45  ? 37.775 -16.662 19.143 1.00 17.69  ? 46  HIS A CA  1 
ATOM   425  C  C   . HIS A 1 45  ? 36.885 -15.428 18.944 1.00 21.12  ? 46  HIS A C   1 
ATOM   426  O  O   . HIS A 1 45  ? 35.672 -15.476 19.218 1.00 20.55  ? 46  HIS A O   1 
ATOM   427  C  CB  . HIS A 1 45  ? 37.323 -17.781 18.197 1.00 17.13  ? 46  HIS A CB  1 
ATOM   428  C  CG  . HIS A 1 45  ? 38.071 -19.062 18.404 1.00 20.56  ? 46  HIS A CG  1 
ATOM   429  N  ND1 . HIS A 1 45  ? 37.541 -20.094 19.160 1.00 22.09  ? 46  HIS A ND1 1 
ATOM   430  C  CD2 . HIS A 1 45  ? 39.315 -19.416 17.989 1.00 21.44  ? 46  HIS A CD2 1 
ATOM   431  C  CE1 . HIS A 1 45  ? 38.471 -21.042 19.185 1.00 21.52  ? 46  HIS A CE1 1 
ATOM   432  N  NE2 . HIS A 1 45  ? 39.555 -20.684 18.487 1.00 21.20  ? 46  HIS A NE2 1 
ATOM   433  N  N   . LYS A 1 46  ? 37.492 -14.321 18.518 1.00 19.19  ? 47  LYS A N   1 
ATOM   434  C  CA  . LYS A 1 46  ? 36.746 -13.080 18.244 1.00 19.36  ? 47  LYS A CA  1 
ATOM   435  C  C   . LYS A 1 46  ? 35.507 -13.336 17.374 1.00 21.60  ? 47  LYS A C   1 
ATOM   436  O  O   . LYS A 1 46  ? 34.431 -12.830 17.690 1.00 19.66  ? 47  LYS A O   1 
ATOM   437  C  CB  . LYS A 1 46  ? 37.640 -12.057 17.526 1.00 21.32  ? 47  LYS A CB  1 
ATOM   438  C  CG  . LYS A 1 46  ? 38.690 -11.451 18.452 1.00 22.32  ? 47  LYS A CG  1 
ATOM   439  C  CD  . LYS A 1 46  ? 39.594 -10.526 17.668 1.00 22.48  ? 47  LYS A CD  1 
ATOM   440  C  CE  . LYS A 1 46  ? 40.746 -10.068 18.530 1.00 26.64  ? 47  LYS A CE  1 
ATOM   441  N  NZ  . LYS A 1 46  ? 41.654 -9.167  17.767 1.00 28.14  ? 47  LYS A NZ  1 
ATOM   442  N  N   . THR A 1 47  ? 35.651 -14.112 16.283 1.00 19.50  ? 48  THR A N   1 
ATOM   443  C  CA  . THR A 1 47  ? 34.498 -14.324 15.395 1.00 19.27  ? 48  THR A CA  1 
ATOM   444  C  C   . THR A 1 47  ? 33.325 -15.004 16.075 1.00 19.42  ? 48  THR A C   1 
ATOM   445  O  O   . THR A 1 47  ? 32.189 -14.628 15.798 1.00 18.14  ? 48  THR A O   1 
ATOM   446  C  CB  . THR A 1 47  ? 34.890 -15.035 14.108 1.00 24.61  ? 48  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 47  ? 35.497 -16.263 14.462 1.00 24.63  ? 48  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 47  ? 35.800 -14.159 13.225 1.00 27.35  ? 48  THR A CG2 1 
ATOM   449  N  N   . VAL A 1 48  ? 33.583 -15.977 16.954 1.00 17.10  ? 49  VAL A N   1 
ATOM   450  C  CA  . VAL A 1 48  ? 32.496 -16.671 17.667 1.00 16.82  ? 49  VAL A CA  1 
ATOM   451  C  C   . VAL A 1 48  ? 31.818 -15.664 18.630 1.00 19.08  ? 49  VAL A C   1 
ATOM   452  O  O   . VAL A 1 48  ? 30.576 -15.610 18.717 1.00 18.10  ? 49  VAL A O   1 
ATOM   453  C  CB  . VAL A 1 48  ? 32.999 -17.931 18.425 1.00 19.17  ? 49  VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 48  ? 31.854 -18.541 19.266 1.00 19.29  ? 49  VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 48  ? 33.546 -18.969 17.430 1.00 18.96  ? 49  VAL A CG2 1 
ATOM   456  N  N   . LEU A 1 49  ? 32.640 -14.871 19.361 1.00 16.97  ? 50  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 49  ? 32.076 -13.860 20.280 1.00 17.32  ? 50  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 49  ? 31.181 -12.867 19.511 1.00 19.90  ? 50  LEU A C   1 
ATOM   459  O  O   . LEU A 1 49  ? 30.067 -12.574 19.949 1.00 18.63  ? 50  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 49  ? 33.214 -13.080 20.981 1.00 17.29  ? 50  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 49  ? 34.167 -13.878 21.900 1.00 19.88  ? 50  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 49  ? 35.226 -12.916 22.512 1.00 20.48  ? 50  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 49  ? 33.382 -14.603 23.003 1.00 21.73  ? 50  LEU A CD2 1 
ATOM   464  N  N   . MET A 1 50  ? 31.626 -12.417 18.328 1.00 17.08  ? 51  MET A N   1 
ATOM   465  C  CA  . MET A 1 50  ? 30.845 -11.493 17.484 1.00 17.57  ? 51  MET A CA  1 
ATOM   466  C  C   . MET A 1 50  ? 29.551 -12.132 17.010 1.00 20.09  ? 51  MET A C   1 
ATOM   467  O  O   . MET A 1 50  ? 28.505 -11.483 17.043 1.00 19.79  ? 51  MET A O   1 
ATOM   468  C  CB  . MET A 1 50  ? 31.658 -11.034 16.268 1.00 19.52  ? 51  MET A CB  1 
ATOM   469  C  CG  . MET A 1 50  ? 32.867 -10.214 16.661 1.00 22.33  ? 51  MET A CG  1 
ATOM   470  S  SD  . MET A 1 50  ? 33.925 -10.108 15.214 1.00 25.73  ? 51  MET A SD  1 
ATOM   471  C  CE  . MET A 1 50  ? 33.180 -8.757  14.437 1.00 22.84  ? 51  MET A CE  1 
ATOM   472  N  N   . ALA A 1 51  ? 29.606 -13.414 16.618 1.00 17.89  ? 52  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 51  ? 28.443 -14.141 16.100 1.00 18.30  ? 52  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 51  ? 27.353 -14.325 17.178 1.00 21.00  ? 52  ALA A C   1 
ATOM   475  O  O   . ALA A 1 51  ? 26.187 -14.516 16.837 1.00 21.49  ? 52  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 51  ? 28.885 -15.518 15.569 1.00 18.39  ? 52  ALA A CB  1 
ATOM   477  N  N   . CYS A 1 52  ? 27.745 -14.274 18.465 1.00 17.66  ? 53  CYS A N   1 
ATOM   478  C  CA  . CYS A 1 52  ? 26.841 -14.497 19.596 1.00 18.30  ? 53  CYS A CA  1 
ATOM   479  C  C   . CYS A 1 52  ? 26.394 -13.272 20.363 1.00 21.22  ? 53  CYS A C   1 
ATOM   480  O  O   . CYS A 1 52  ? 25.438 -13.391 21.141 1.00 20.50  ? 53  CYS A O   1 
ATOM   481  C  CB  . CYS A 1 52  ? 27.500 -15.475 20.557 1.00 18.76  ? 53  CYS A CB  1 
ATOM   482  S  SG  . CYS A 1 52  ? 27.806 -17.098 19.839 1.00 21.33  ? 53  CYS A SG  1 
ATOM   483  N  N   . SER A 1 53  ? 27.152 -12.171 20.287 1.00 18.89  ? 54  SER A N   1 
ATOM   484  C  CA  . SER A 1 53  ? 26.936 -11.035 21.180 1.00 18.25  ? 54  SER A CA  1 
ATOM   485  C  C   . SER A 1 53  ? 26.966 -9.715  20.435 1.00 22.65  ? 54  SER A C   1 
ATOM   486  O  O   . SER A 1 53  ? 27.949 -9.431  19.739 1.00 20.75  ? 54  SER A O   1 
ATOM   487  C  CB  . SER A 1 53  ? 28.060 -11.077 22.220 1.00 19.62  ? 54  SER A CB  1 
ATOM   488  O  OG  . SER A 1 53  ? 28.400 -9.829  22.801 1.00 22.51  ? 54  SER A OG  1 
ATOM   489  N  N   . GLY A 1 54  ? 25.924 -8.897  20.626 1.00 21.97  ? 55  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 54  ? 25.869 -7.560  20.038 1.00 22.63  ? 55  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 54  ? 26.996 -6.679  20.542 1.00 25.01  ? 55  GLY A C   1 
ATOM   492  O  O   . GLY A 1 54  ? 27.527 -5.847  19.787 1.00 24.43  ? 55  GLY A O   1 
ATOM   493  N  N   . LEU A 1 55  ? 27.407 -6.879  21.824 1.00 22.02  ? 56  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 55  ? 28.517 -6.094  22.386 1.00 21.33  ? 56  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 55  ? 29.840 -6.437  21.683 1.00 22.88  ? 56  LEU A C   1 
ATOM   496  O  O   . LEU A 1 55  ? 30.539 -5.522  21.231 1.00 21.96  ? 56  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 55  ? 28.648 -6.296  23.916 1.00 21.07  ? 56  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 55  ? 29.688 -5.372  24.597 1.00 26.17  ? 56  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 55  ? 29.239 -3.886  24.578 1.00 27.13  ? 56  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 55  ? 29.987 -5.832  26.009 1.00 26.20  ? 56  LEU A CD2 1 
ATOM   501  N  N   . PHE A 1 56  ? 30.168 -7.737  21.574 1.00 20.43  ? 57  PHE A N   1 
ATOM   502  C  CA  . PHE A 1 56  ? 31.418 -8.137  20.913 1.00 19.25  ? 57  PHE A CA  1 
ATOM   503  C  C   . PHE A 1 56  ? 31.395 -7.800  19.445 1.00 22.74  ? 57  PHE A C   1 
ATOM   504  O  O   . PHE A 1 56  ? 32.426 -7.411  18.908 1.00 20.99  ? 57  PHE A O   1 
ATOM   505  C  CB  . PHE A 1 56  ? 31.766 -9.603  21.172 1.00 19.83  ? 57  PHE A CB  1 
ATOM   506  C  CG  . PHE A 1 56  ? 32.196 -9.842  22.605 1.00 20.00  ? 57  PHE A CG  1 
ATOM   507  C  CD1 . PHE A 1 56  ? 33.276 -9.141  23.155 1.00 21.70  ? 57  PHE A CD1 1 
ATOM   508  C  CD2 . PHE A 1 56  ? 31.553 -10.795 23.392 1.00 20.62  ? 57  PHE A CD2 1 
ATOM   509  C  CE1 . PHE A 1 56  ? 33.658 -9.340  24.492 1.00 22.59  ? 57  PHE A CE1 1 
ATOM   510  C  CE2 . PHE A 1 56  ? 31.972 -11.034 24.715 1.00 22.95  ? 57  PHE A CE2 1 
ATOM   511  C  CZ  . PHE A 1 56  ? 33.009 -10.289 25.259 1.00 20.88  ? 57  PHE A CZ  1 
ATOM   512  N  N   . TYR A 1 57  ? 30.210 -7.878  18.808 1.00 20.49  ? 58  TYR A N   1 
ATOM   513  C  CA  . TYR A 1 57  ? 30.094 -7.478  17.401 1.00 21.43  ? 58  TYR A CA  1 
ATOM   514  C  C   . TYR A 1 57  ? 30.530 -6.000  17.243 1.00 25.37  ? 58  TYR A C   1 
ATOM   515  O  O   . TYR A 1 57  ? 31.329 -5.679  16.356 1.00 24.13  ? 58  TYR A O   1 
ATOM   516  C  CB  . TYR A 1 57  ? 28.659 -7.691  16.913 1.00 23.34  ? 58  TYR A CB  1 
ATOM   517  C  CG  . TYR A 1 57  ? 28.455 -7.189  15.507 1.00 26.74  ? 58  TYR A CG  1 
ATOM   518  C  CD1 . TYR A 1 57  ? 29.046 -7.832  14.423 1.00 27.95  ? 58  TYR A CD1 1 
ATOM   519  C  CD2 . TYR A 1 57  ? 27.678 -6.065  15.258 1.00 31.80  ? 58  TYR A CD2 1 
ATOM   520  C  CE1 . TYR A 1 57  ? 28.866 -7.363  13.120 1.00 30.32  ? 58  TYR A CE1 1 
ATOM   521  C  CE2 . TYR A 1 57  ? 27.495 -5.587  13.968 1.00 35.03  ? 58  TYR A CE2 1 
ATOM   522  C  CZ  . TYR A 1 57  ? 28.081 -6.245  12.904 1.00 42.28  ? 58  TYR A CZ  1 
ATOM   523  O  OH  . TYR A 1 57  ? 27.871 -5.753  11.652 1.00 49.18  ? 58  TYR A OH  1 
ATOM   524  N  N   A SER A 1 58  ? 30.007 -5.114  18.107 0.52 23.72  ? 59  SER A N   1 
ATOM   525  N  N   B SER A 1 58  ? 29.999 -5.120  18.106 0.48 23.73  ? 59  SER A N   1 
ATOM   526  C  CA  A SER A 1 58  ? 30.330 -3.689  18.113 0.52 24.69  ? 59  SER A CA  1 
ATOM   527  C  CA  B SER A 1 58  ? 30.327 -3.702  18.118 0.48 24.73  ? 59  SER A CA  1 
ATOM   528  C  C   A SER A 1 58  ? 31.814 -3.444  18.431 0.52 29.22  ? 59  SER A C   1 
ATOM   529  C  C   B SER A 1 58  ? 31.825 -3.498  18.382 0.48 28.87  ? 59  SER A C   1 
ATOM   530  O  O   A SER A 1 58  ? 32.442 -2.621  17.773 0.52 30.01  ? 59  SER A O   1 
ATOM   531  O  O   B SER A 1 58  ? 32.471 -2.770  17.633 0.48 29.24  ? 59  SER A O   1 
ATOM   532  C  CB  A SER A 1 58  ? 29.425 -2.947  19.091 0.52 27.52  ? 59  SER A CB  1 
ATOM   533  C  CB  B SER A 1 58  ? 29.493 -2.978  19.173 0.48 28.00  ? 59  SER A CB  1 
ATOM   534  O  OG  A SER A 1 58  ? 28.089 -2.954  18.616 0.52 27.69  ? 59  SER A OG  1 
ATOM   535  O  OG  B SER A 1 58  ? 29.830 -1.601  19.207 0.48 31.52  ? 59  SER A OG  1 
ATOM   536  N  N   . ILE A 1 59  ? 32.376 -4.180  19.411 1.00 25.32  ? 60  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 33.791 -4.062  19.807 1.00 24.81  ? 60  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 34.734 -4.446  18.667 1.00 26.66  ? 60  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 35.633 -3.661  18.336 1.00 27.61  ? 60  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 34.118 -4.897  21.107 1.00 26.39  ? 60  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 33.396 -4.333  22.352 1.00 26.50  ? 60  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 35.650 -5.009  21.352 1.00 25.40  ? 60  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 33.414 -5.308  23.573 1.00 27.93  ? 60  ILE A CD1 1 
ATOM   544  N  N   . PHE A 1 60  ? 34.551 -5.641  18.081 1.00 22.25  ? 61  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 60  ? 35.522 -6.094  17.096 1.00 22.12  ? 61  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 60  ? 35.287 -5.546  15.688 1.00 26.21  ? 61  PHE A C   1 
ATOM   547  O  O   . PHE A 1 60  ? 36.120 -5.792  14.822 1.00 27.56  ? 61  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 60  ? 35.659 -7.633  17.130 1.00 22.50  ? 61  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 60  ? 36.082 -8.125  18.502 1.00 22.86  ? 61  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 60  ? 37.284 -7.703  19.074 1.00 25.83  ? 61  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 60  ? 35.291 -9.019  19.210 1.00 23.78  ? 61  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 60  ? 37.663 -8.145  20.353 1.00 26.92  ? 61  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 60  ? 35.672 -9.465  20.486 1.00 26.38  ? 61  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 60  ? 36.851 -9.027  21.048 1.00 24.79  ? 61  PHE A CZ  1 
ATOM   555  N  N   . THR A 1 61  ? 34.238 -4.732  15.470 1.00 24.52  ? 62  THR A N   1 
ATOM   556  C  CA  . THR A 1 61  ? 34.076 -4.035  14.180 1.00 24.81  ? 62  THR A CA  1 
ATOM   557  C  C   . THR A 1 61  ? 34.629 -2.616  14.306 1.00 31.85  ? 62  THR A C   1 
ATOM   558  O  O   . THR A 1 61  ? 34.728 -1.892  13.309 1.00 31.51  ? 62  THR A O   1 
ATOM   559  C  CB  . THR A 1 61  ? 32.653 -4.069  13.619 1.00 31.91  ? 62  THR A CB  1 
ATOM   560  O  OG1 . THR A 1 61  ? 31.750 -3.565  14.595 1.00 28.78  ? 62  THR A OG1 1 
ATOM   561  C  CG2 . THR A 1 61  ? 32.231 -5.470  13.137 1.00 27.51  ? 62  THR A CG2 1 
ATOM   562  N  N   . ASP A 1 62  ? 35.043 -2.232  15.524 1.00 27.61  ? 63  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 62  ? 35.648 -0.917  15.722 1.00 28.67  ? 63  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 62  ? 37.069 -1.001  15.185 1.00 35.72  ? 63  ASP A C   1 
ATOM   565  O  O   . ASP A 1 62  ? 37.797 -1.916  15.556 1.00 34.11  ? 63  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 62  ? 35.649 -0.529  17.206 1.00 29.03  ? 63  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 62  ? 36.395 0.766   17.414 1.00 41.61  ? 63  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 62  ? 35.784 1.830   17.221 1.00 45.48  ? 63  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 62  ? 37.617 0.709   17.685 1.00 41.80  ? 63  ASP A OD2 1 
ATOM   570  N  N   . GLN A 1 63  ? 37.468 -0.025  14.339 1.00 36.78  ? 64  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 63  ? 38.766 0.020   13.669 1.00 38.48  ? 64  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 63  ? 39.971 -0.033  14.611 1.00 43.29  ? 64  GLN A C   1 
ATOM   573  O  O   . GLN A 1 63  ? 41.022 -0.506  14.177 1.00 45.42  ? 64  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 63  ? 38.863 1.229   12.722 1.00 42.14  ? 64  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 63  ? 37.974 1.100   11.486 1.00 61.99  ? 64  GLN A CG  1 
ATOM   576  N  N   . LEU A 1 64  ? 39.847 0.461   15.873 1.00 35.90  ? 65  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 64  ? 40.946 0.379   16.842 1.00 35.01  ? 65  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 64  ? 40.851 -0.866  17.702 1.00 37.96  ? 65  LEU A C   1 
ATOM   579  O  O   . LEU A 1 64  ? 41.869 -1.487  17.987 1.00 40.52  ? 65  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 64  ? 40.977 1.603   17.789 1.00 35.99  ? 65  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 64  ? 41.596 2.881   17.270 1.00 43.22  ? 65  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 64  ? 41.469 3.969   18.300 1.00 43.58  ? 65  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 64  ? 43.073 2.704   16.901 1.00 47.48  ? 65  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 65  ? 39.646 -1.192  18.193 1.00 29.65  ? 66  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 65  ? 39.478 -2.306  19.122 1.00 28.42  ? 66  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 65  ? 39.599 -3.671  18.453 1.00 33.45  ? 66  LYS A C   1 
ATOM   587  O  O   . LYS A 1 65  ? 39.953 -4.629  19.136 1.00 32.74  ? 66  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 65  ? 38.157 -2.203  19.903 1.00 29.22  ? 66  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 65  ? 38.074 -0.984  20.830 1.00 29.46  ? 66  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 65  ? 36.771 -1.067  21.617 1.00 27.74  ? 66  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 65  ? 36.455 0.244   22.313 1.00 32.36  ? 66  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 65  ? 35.905 1.263   21.393 1.00 33.75  ? 66  LYS A NZ  1 
ATOM   593  N  N   . CYS A 1 66  ? 39.329 -3.758  17.126 1.00 33.84  ? 67  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 66  ? 39.428 -5.022  16.364 1.00 33.68  ? 67  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 66  ? 40.823 -5.647  16.504 1.00 38.36  ? 67  CYS A C   1 
ATOM   596  O  O   . CYS A 1 66  ? 40.967 -6.860  16.336 1.00 38.74  ? 67  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 66  ? 39.065 -4.809  14.894 1.00 35.20  ? 67  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 66  ? 40.222 -3.744  13.980 1.00 41.24  ? 67  CYS A SG  1 
ATOM   599  N  N   . ASN A 1 67  ? 41.842 -4.801  16.779 1.00 35.01  ? 68  ASN A N   1 
ATOM   600  C  CA  . ASN A 1 67  ? 43.243 -5.193  16.904 1.00 36.11  ? 68  ASN A CA  1 
ATOM   601  C  C   . ASN A 1 67  ? 43.713 -5.495  18.331 1.00 38.87  ? 68  ASN A C   1 
ATOM   602  O  O   . ASN A 1 67  ? 44.871 -5.879  18.526 1.00 38.06  ? 68  ASN A O   1 
ATOM   603  C  CB  . ASN A 1 67  ? 44.142 -4.145  16.241 1.00 38.14  ? 68  ASN A CB  1 
ATOM   604  C  CG  . ASN A 1 67  ? 43.957 -4.118  14.735 1.00 52.27  ? 68  ASN A CG  1 
ATOM   605  O  OD1 . ASN A 1 67  ? 43.966 -3.060  14.112 1.00 52.79  ? 68  ASN A OD1 1 
ATOM   606  N  ND2 . ASN A 1 67  ? 43.743 -5.280  14.117 1.00 42.65  ? 68  ASN A ND2 1 
ATOM   607  N  N   . LEU A 1 68  ? 42.824 -5.363  19.318 1.00 35.10  ? 69  LEU A N   1 
ATOM   608  C  CA  . LEU A 1 68  ? 43.207 -5.635  20.696 1.00 34.03  ? 69  LEU A CA  1 
ATOM   609  C  C   . LEU A 1 68  ? 43.187 -7.137  20.966 1.00 35.29  ? 69  LEU A C   1 
ATOM   610  O  O   . LEU A 1 68  ? 42.285 -7.825  20.473 1.00 33.70  ? 69  LEU A O   1 
ATOM   611  C  CB  . LEU A 1 68  ? 42.246 -4.923  21.668 1.00 33.85  ? 69  LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 68  ? 42.279 -3.386  21.654 1.00 38.61  ? 69  LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 68  ? 41.209 -2.828  22.561 1.00 38.44  ? 69  LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 68  ? 43.662 -2.844  22.059 1.00 39.47  ? 69  LEU A CD2 1 
ATOM   615  N  N   . SER A 1 69  ? 44.169 -7.619  21.765 1.00 31.42  ? 70  SER A N   1 
ATOM   616  C  CA  A SER A 1 69  ? 44.298 -9.025  22.164 0.42 30.73  ? 70  SER A CA  1 
ATOM   617  C  CA  B SER A 1 69  ? 44.242 -9.036  22.136 0.58 31.13  ? 70  SER A CA  1 
ATOM   618  C  C   . SER A 1 69  ? 43.663 -9.238  23.545 1.00 31.64  ? 70  SER A C   1 
ATOM   619  O  O   . SER A 1 69  ? 43.505 -10.368 23.990 1.00 27.59  ? 70  SER A O   1 
ATOM   620  C  CB  A SER A 1 69  ? 45.772 -9.422  22.212 0.42 35.07  ? 70  SER A CB  1 
ATOM   621  C  CB  B SER A 1 69  ? 45.681 -9.541  22.061 0.58 36.20  ? 70  SER A CB  1 
ATOM   622  O  OG  A SER A 1 69  ? 46.371 -9.326  20.931 0.42 40.25  ? 70  SER A OG  1 
ATOM   623  O  OG  B SER A 1 69  ? 46.513 -8.829  22.959 0.58 43.36  ? 70  SER A OG  1 
ATOM   624  N  N   . VAL A 1 70  ? 43.367 -8.130  24.257 1.00 28.56  ? 71  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 70  ? 42.774 -8.173  25.601 1.00 27.75  ? 71  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 70  ? 41.596 -7.205  25.647 1.00 29.04  ? 71  VAL A C   1 
ATOM   627  O  O   . VAL A 1 70  ? 41.743 -6.040  25.250 1.00 28.95  ? 71  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 70  ? 43.819 -7.830  26.714 1.00 33.09  ? 71  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 70  ? 43.187 -7.845  28.111 1.00 33.25  ? 71  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 70  ? 45.036 -8.760  26.660 1.00 33.79  ? 71  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 71  ? 40.446 -7.678  26.164 1.00 22.71  ? 72  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 71  ? 39.246 -6.860  26.365 1.00 22.41  ? 72  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 71  ? 38.849 -6.967  27.831 1.00 26.92  ? 72  ILE A C   1 
ATOM   634  O  O   . ILE A 1 71  ? 38.635 -8.076  28.327 1.00 26.38  ? 72  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 71  ? 38.070 -7.221  25.396 1.00 23.65  ? 72  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 71  ? 38.477 -7.067  23.885 1.00 24.53  ? 72  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 71  ? 36.781 -6.432  25.735 1.00 25.41  ? 72  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 71  ? 38.872 -5.619  23.395 1.00 28.34  ? 72  ILE A CD1 1 
ATOM   639  N  N   . ASN A 1 72  ? 38.723 -5.823  28.511 1.00 23.86  ? 73  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 72  ? 38.333 -5.790  29.913 1.00 24.12  ? 73  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 72  ? 36.857 -5.469  30.035 1.00 27.22  ? 73  ASN A C   1 
ATOM   642  O  O   . ASN A 1 72  ? 36.414 -4.398  29.596 1.00 26.01  ? 73  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 72  ? 39.159 -4.742  30.702 1.00 28.11  ? 73  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 72  ? 40.637 -4.960  30.632 1.00 46.66  ? 73  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 72  ? 41.147 -6.003  31.016 1.00 36.91  ? 73  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 72  ? 41.362 -3.976  30.147 1.00 42.75  ? 73  ASN A ND2 1 
ATOM   647  N  N   . LEU A 1 73  ? 36.094 -6.374  30.644 1.00 22.61  ? 74  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 73  ? 34.673 -6.123  30.855 1.00 21.70  ? 74  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 73  ? 34.437 -5.211  32.063 1.00 25.25  ? 74  LEU A C   1 
ATOM   650  O  O   . LEU A 1 73  ? 35.320 -5.043  32.918 1.00 26.11  ? 74  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 73  ? 33.854 -7.422  30.984 1.00 21.43  ? 74  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 73  ? 33.927 -8.422  29.806 1.00 23.97  ? 74  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 73  ? 32.802 -9.477  29.932 1.00 23.62  ? 74  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 73  ? 33.889 -7.722  28.426 1.00 24.27  ? 74  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 74  ? 33.247 -4.623  32.120 1.00 22.27  ? 75  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 74  ? 32.828 -3.722  33.201 1.00 23.49  ? 75  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 74  ? 33.011 -4.467  34.537 1.00 28.58  ? 75  ASP A C   1 
ATOM   658  O  O   . ASP A 1 74  ? 32.656 -5.646  34.611 1.00 26.28  ? 75  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 74  ? 31.354 -3.328  32.992 1.00 25.30  ? 75  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 74  ? 30.805 -2.315  33.986 1.00 35.79  ? 75  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 74  ? 30.659 -2.666  35.180 1.00 36.52  ? 75  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 74  ? 30.472 -1.199  33.565 1.00 36.98  ? 75  ASP A OD2 1 
ATOM   663  N  N   . PRO A 1 75  ? 33.599 -3.826  35.569 1.00 29.40  ? 76  PRO A N   1 
ATOM   664  C  CA  . PRO A 1 75  ? 33.810 -4.536  36.854 1.00 30.22  ? 76  PRO A CA  1 
ATOM   665  C  C   . PRO A 1 75  ? 32.565 -5.107  37.519 1.00 33.55  ? 76  PRO A C   1 
ATOM   666  O  O   . PRO A 1 75  ? 32.702 -5.965  38.386 1.00 34.54  ? 76  PRO A O   1 
ATOM   667  C  CB  . PRO A 1 75  ? 34.492 -3.496  37.746 1.00 32.98  ? 76  PRO A CB  1 
ATOM   668  C  CG  . PRO A 1 75  ? 34.205 -2.167  37.101 1.00 37.60  ? 76  PRO A CG  1 
ATOM   669  C  CD  . PRO A 1 75  ? 34.109 -2.437  35.630 1.00 31.23  ? 76  PRO A CD  1 
ATOM   670  N  N   . GLU A 1 76  ? 31.360 -4.662  37.128 1.00 30.06  ? 77  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 76  ? 30.125 -5.192  37.705 1.00 31.33  ? 77  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 76  ? 29.812 -6.592  37.160 1.00 31.17  ? 77  GLU A C   1 
ATOM   673  O  O   . GLU A 1 76  ? 28.965 -7.285  37.721 1.00 30.46  ? 77  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 76  ? 28.937 -4.242  37.454 1.00 34.11  ? 77  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 76  ? 28.901 -3.036  38.379 1.00 54.45  ? 77  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 76  ? 28.358 -3.337  39.762 1.00 86.01  ? 77  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 76  ? 27.128 -3.541  39.887 1.00 85.94  ? 77  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 76  ? 29.163 -3.382  40.721 1.00 85.70  ? 77  GLU A OE2 1 
ATOM   679  N  N   . ILE A 1 77  ? 30.487 -7.002  36.071 1.00 25.67  ? 78  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 77  ? 30.225 -8.320  35.480 1.00 24.37  ? 78  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 77  ? 30.824 -9.426  36.321 1.00 28.85  ? 78  ILE A C   1 
ATOM   682  O  O   . ILE A 1 77  ? 32.002 -9.399  36.659 1.00 27.63  ? 78  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 77  ? 30.648 -8.389  33.995 1.00 26.28  ? 78  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 77  ? 29.928 -7.279  33.165 1.00 27.23  ? 78  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 77  ? 30.426 -9.807  33.407 1.00 22.77  ? 78  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 77  ? 28.306 -7.276  33.224 1.00 34.88  ? 78  ILE A CD1 1 
ATOM   687  N  N   . ASN A 1 78  ? 29.999 -10.423 36.587 1.00 28.72  ? 79  ASN A N   1 
ATOM   688  C  CA  . ASN A 1 78  ? 30.317 -11.597 37.376 1.00 29.84  ? 79  ASN A CA  1 
ATOM   689  C  C   . ASN A 1 78  ? 31.032 -12.647 36.511 1.00 29.06  ? 79  ASN A C   1 
ATOM   690  O  O   . ASN A 1 78  ? 30.499 -13.027 35.469 1.00 26.13  ? 79  ASN A O   1 
ATOM   691  C  CB  . ASN A 1 78  ? 29.011 -12.147 37.968 1.00 33.33  ? 79  ASN A CB  1 
ATOM   692  C  CG  . ASN A 1 78  ? 29.178 -13.451 38.698 1.00 46.73  ? 79  ASN A CG  1 
ATOM   693  O  OD1 . ASN A 1 78  ? 28.831 -14.511 38.181 1.00 35.71  ? 79  ASN A OD1 1 
ATOM   694  N  ND2 . ASN A 1 78  ? 29.720 -13.398 39.908 1.00 40.70  ? 79  ASN A ND2 1 
ATOM   695  N  N   . PRO A 1 79  ? 32.237 -13.133 36.921 1.00 27.07  ? 80  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 79  ? 32.953 -14.136 36.100 1.00 26.26  ? 80  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 79  ? 32.164 -15.423 35.851 1.00 28.69  ? 80  PRO A C   1 
ATOM   698  O  O   . PRO A 1 79  ? 32.249 -15.974 34.752 1.00 27.39  ? 80  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 79  ? 34.214 -14.422 36.919 1.00 29.44  ? 80  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 79  ? 34.408 -13.183 37.750 1.00 34.56  ? 80  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 79  ? 33.026 -12.758 38.114 1.00 30.32  ? 80  PRO A CD  1 
ATOM   702  N  N   . GLU A 1 80  ? 31.395 -15.896 36.849 1.00 26.10  ? 81  GLU A N   1 
ATOM   703  C  CA  . GLU A 1 80  ? 30.613 -17.126 36.642 1.00 25.80  ? 81  GLU A CA  1 
ATOM   704  C  C   . GLU A 1 80  ? 29.530 -16.931 35.562 1.00 27.11  ? 81  GLU A C   1 
ATOM   705  O  O   . GLU A 1 80  ? 29.397 -17.784 34.689 1.00 25.84  ? 81  GLU A O   1 
ATOM   706  C  CB  . GLU A 1 80  ? 30.009 -17.643 37.951 1.00 28.62  ? 81  GLU A CB  1 
ATOM   707  C  CG  . GLU A 1 80  ? 29.414 -19.033 37.753 1.00 36.65  ? 81  GLU A CG  1 
ATOM   708  C  CD  . GLU A 1 80  ? 28.545 -19.606 38.860 1.00 62.29  ? 81  GLU A CD  1 
ATOM   709  O  OE1 . GLU A 1 80  ? 28.554 -20.847 39.022 1.00 57.82  ? 81  GLU A OE1 1 
ATOM   710  O  OE2 . GLU A 1 80  ? 27.840 -18.831 39.545 1.00 57.15  ? 81  GLU A OE2 1 
ATOM   711  N  N   . GLY A 1 81  ? 28.795 -15.810 35.626 1.00 25.01  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 81  ? 27.793 -15.465 34.621 1.00 24.18  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 81  ? 28.432 -15.405 33.243 1.00 25.41  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 81  ? 27.881 -15.944 32.270 1.00 23.48  ? 82  GLY A O   1 
ATOM   715  N  N   . PHE A 1 82  ? 29.632 -14.794 33.153 1.00 21.60  ? 83  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 82  ? 30.334 -14.742 31.861 1.00 19.90  ? 83  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 82  ? 30.689 -16.148 31.382 1.00 22.95  ? 83  PHE A C   1 
ATOM   718  O  O   . PHE A 1 82  ? 30.488 -16.453 30.216 1.00 21.44  ? 83  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 82  ? 31.613 -13.873 31.909 1.00 21.24  ? 83  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 82  ? 32.203 -13.746 30.518 1.00 21.07  ? 83  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 82  ? 31.622 -12.902 29.572 1.00 23.54  ? 83  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 82  ? 33.277 -14.538 30.126 1.00 21.31  ? 83  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 82  ? 32.121 -12.841 28.264 1.00 23.86  ? 83  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 82  ? 33.780 -14.469 28.825 1.00 22.53  ? 83  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 82  ? 33.193 -13.630 27.901 1.00 21.86  ? 83  PHE A CZ  1 
ATOM   726  N  N   . CYS A 1 83  ? 31.272 -16.966 32.258 1.00 23.31  ? 84  CYS A N   1 
ATOM   727  C  CA  . CYS A 1 83  ? 31.687 -18.339 31.934 1.00 24.74  ? 84  CYS A CA  1 
ATOM   728  C  C   . CYS A 1 83  ? 30.497 -19.158 31.367 1.00 25.94  ? 84  CYS A C   1 
ATOM   729  O  O   . CYS A 1 83  ? 30.638 -19.851 30.344 1.00 24.14  ? 84  CYS A O   1 
ATOM   730  C  CB  . CYS A 1 83  ? 32.294 -19.006 33.165 1.00 28.22  ? 84  CYS A CB  1 
ATOM   731  S  SG  . CYS A 1 83  ? 32.954 -20.665 32.841 1.00 33.80  ? 84  CYS A SG  1 
ATOM   732  N  N   . ILE A 1 84  ? 29.322 -19.041 32.025 1.00 22.45  ? 85  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 84  ? 28.091 -19.743 31.612 1.00 20.75  ? 85  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 84  ? 27.694 -19.287 30.204 1.00 21.41  ? 85  ILE A C   1 
ATOM   735  O  O   . ILE A 1 84  ? 27.311 -20.113 29.354 1.00 20.95  ? 85  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 84  ? 26.967 -19.503 32.657 1.00 24.04  ? 85  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 84  ? 27.275 -20.307 33.959 1.00 25.65  ? 85  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 84  ? 25.554 -19.868 32.086 1.00 23.88  ? 85  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 84  ? 26.504 -19.777 35.177 1.00 32.20  ? 85  ILE A CD1 1 
ATOM   740  N  N   . LEU A 1 85  ? 27.761 -17.979 29.970 1.00 19.47  ? 86  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 85  ? 27.416 -17.434 28.653 1.00 19.17  ? 86  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 85  ? 28.420 -17.800 27.584 1.00 22.48  ? 86  LEU A C   1 
ATOM   743  O  O   . LEU A 1 85  ? 28.014 -18.074 26.455 1.00 20.13  ? 86  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 85  ? 27.168 -15.935 28.727 1.00 20.50  ? 86  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 85  ? 25.871 -15.588 29.502 1.00 26.28  ? 86  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 85  ? 25.787 -14.125 29.726 1.00 27.42  ? 86  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 85  ? 24.619 -16.070 28.746 1.00 27.47  ? 86  LEU A CD2 1 
ATOM   748  N  N   . LEU A 1 86  ? 29.726 -17.835 27.930 1.00 19.69  ? 87  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 86  ? 30.757 -18.247 26.965 1.00 19.28  ? 87  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 86  ? 30.522 -19.714 26.570 1.00 22.23  ? 87  LEU A C   1 
ATOM   751  O  O   . LEU A 1 86  ? 30.574 -20.059 25.388 1.00 20.06  ? 87  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 86  ? 32.160 -18.035 27.568 1.00 19.03  ? 87  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 86  ? 33.333 -18.343 26.613 1.00 23.59  ? 87  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 86  ? 33.303 -17.426 25.376 1.00 22.52  ? 87  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 86  ? 34.698 -18.232 27.371 1.00 26.35  ? 87  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 87  ? 30.217 -20.568 27.554 1.00 20.34  ? 88  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 87  ? 29.892 -21.962 27.281 1.00 19.54  ? 88  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 87  ? 28.689 -22.061 26.347 1.00 21.69  ? 88  ASP A C   1 
ATOM   759  O  O   . ASP A 1 87  ? 28.727 -22.842 25.402 1.00 21.81  ? 88  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 87  ? 29.596 -22.681 28.598 1.00 22.33  ? 88  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 87  ? 30.849 -23.037 29.379 1.00 35.45  ? 88  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 87  ? 31.962 -22.948 28.797 1.00 34.69  ? 88  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 87  ? 30.720 -23.412 30.568 1.00 37.27  ? 88  ASP A OD2 1 
ATOM   764  N  N   . PHE A 1 88  ? 27.632 -21.270 26.604 1.00 19.12  ? 89  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 88  ? 26.441 -21.225 25.738 1.00 18.13  ? 89  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 88  ? 26.820 -20.836 24.300 1.00 19.71  ? 89  PHE A C   1 
ATOM   767  O  O   . PHE A 1 88  ? 26.337 -21.436 23.335 1.00 18.18  ? 89  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 88  ? 25.379 -20.260 26.319 1.00 19.10  ? 89  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 88  ? 24.269 -19.978 25.338 1.00 19.21  ? 89  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 88  ? 23.291 -20.936 25.078 1.00 21.09  ? 89  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 88  ? 24.260 -18.799 24.588 1.00 21.38  ? 89  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 88  ? 22.299 -20.701 24.130 1.00 20.98  ? 89  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 88  ? 23.266 -18.567 23.627 1.00 23.92  ? 89  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 88  ? 22.291 -19.516 23.408 1.00 22.25  ? 89  PHE A CZ  1 
ATOM   775  N  N   . MET A 1 89  ? 27.642 -19.797 24.149 1.00 16.69  ? 90  MET A N   1 
ATOM   776  C  CA  . MET A 1 89  ? 28.068 -19.371 22.798 1.00 15.62  ? 90  MET A CA  1 
ATOM   777  C  C   . MET A 1 89  ? 28.624 -20.523 21.984 1.00 19.89  ? 90  MET A C   1 
ATOM   778  O  O   . MET A 1 89  ? 28.285 -20.663 20.812 1.00 19.27  ? 90  MET A O   1 
ATOM   779  C  CB  . MET A 1 89  ? 29.159 -18.285 22.919 1.00 16.34  ? 90  MET A CB  1 
ATOM   780  C  CG  . MET A 1 89  ? 28.635 -16.978 23.490 1.00 18.48  ? 90  MET A CG  1 
ATOM   781  S  SD  . MET A 1 89  ? 30.008 -15.770 23.381 1.00 21.43  ? 90  MET A SD  1 
ATOM   782  C  CE  . MET A 1 89  ? 29.371 -14.492 24.537 1.00 21.35  ? 90  MET A CE  1 
ATOM   783  N  N   . TYR A 1 90  ? 29.473 -21.347 22.612 1.00 17.20  ? 91  TYR A N   1 
ATOM   784  C  CA  . TYR A 1 90  ? 30.150 -22.449 21.936 1.00 17.09  ? 91  TYR A CA  1 
ATOM   785  C  C   . TYR A 1 90  ? 29.397 -23.763 21.923 1.00 20.98  ? 91  TYR A C   1 
ATOM   786  O  O   . TYR A 1 90  ? 29.881 -24.721 21.306 1.00 19.68  ? 91  TYR A O   1 
ATOM   787  C  CB  . TYR A 1 90  ? 31.517 -22.663 22.585 1.00 18.44  ? 91  TYR A CB  1 
ATOM   788  C  CG  . TYR A 1 90  ? 32.578 -21.701 22.096 1.00 19.10  ? 91  TYR A CG  1 
ATOM   789  C  CD1 . TYR A 1 90  ? 32.736 -20.444 22.684 1.00 20.60  ? 91  TYR A CD1 1 
ATOM   790  C  CD2 . TYR A 1 90  ? 33.404 -22.032 21.022 1.00 19.94  ? 91  TYR A CD2 1 
ATOM   791  C  CE1 . TYR A 1 90  ? 33.727 -19.562 22.246 1.00 20.24  ? 91  TYR A CE1 1 
ATOM   792  C  CE2 . TYR A 1 90  ? 34.439 -21.188 20.621 1.00 20.27  ? 91  TYR A CE2 1 
ATOM   793  C  CZ  . TYR A 1 90  ? 34.568 -19.937 21.205 1.00 23.57  ? 91  TYR A CZ  1 
ATOM   794  O  OH  . TYR A 1 90  ? 35.597 -19.126 20.802 1.00 20.97  ? 91  TYR A OH  1 
ATOM   795  N  N   . THR A 1 91  ? 28.242 -23.847 22.614 1.00 17.76  ? 92  THR A N   1 
ATOM   796  C  CA  . THR A 1 91  ? 27.557 -25.146 22.686 1.00 18.16  ? 92  THR A CA  1 
ATOM   797  C  C   . THR A 1 91  ? 26.047 -25.126 22.426 1.00 20.74  ? 92  THR A C   1 
ATOM   798  O  O   . THR A 1 91  ? 25.481 -26.210 22.267 1.00 20.65  ? 92  THR A O   1 
ATOM   799  C  CB  . THR A 1 91  ? 27.756 -25.819 24.079 1.00 22.92  ? 92  THR A CB  1 
ATOM   800  O  OG1 . THR A 1 91  ? 27.099 -25.040 25.081 1.00 22.85  ? 92  THR A OG1 1 
ATOM   801  C  CG2 . THR A 1 91  ? 29.221 -26.042 24.465 1.00 21.45  ? 92  THR A CG2 1 
ATOM   802  N  N   . SER A 1 92  ? 25.394 -23.951 22.527 1.00 17.56  ? 93  SER A N   1 
ATOM   803  C  CA  . SER A 1 92  ? 23.916 -23.767 22.471 1.00 17.66  ? 93  SER A CA  1 
ATOM   804  C  C   . SER A 1 92  ? 23.260 -24.181 23.814 1.00 21.29  ? 93  SER A C   1 
ATOM   805  O  O   . SER A 1 92  ? 22.047 -24.048 23.950 1.00 21.11  ? 93  SER A O   1 
ATOM   806  C  CB  . SER A 1 92  ? 23.275 -24.597 21.345 1.00 19.69  ? 93  SER A CB  1 
ATOM   807  O  OG  . SER A 1 92  ? 23.909 -24.385 20.094 1.00 24.03  ? 93  SER A OG  1 
ATOM   808  N  N   A ARG A 1 93  ? 24.071 -24.628 24.794 0.60 19.39  ? 94  ARG A N   1 
ATOM   809  N  N   B ARG A 1 93  ? 24.043 -24.691 24.788 0.40 18.72  ? 94  ARG A N   1 
ATOM   810  C  CA  A ARG A 1 93  ? 23.603 -25.109 26.099 0.60 20.18  ? 94  ARG A CA  1 
ATOM   811  C  CA  B ARG A 1 93  ? 23.484 -25.121 26.075 0.40 19.20  ? 94  ARG A CA  1 
ATOM   812  C  C   A ARG A 1 93  ? 23.793 -24.043 27.160 0.60 24.01  ? 94  ARG A C   1 
ATOM   813  C  C   B ARG A 1 93  ? 23.772 -24.116 27.163 0.40 23.59  ? 94  ARG A C   1 
ATOM   814  O  O   A ARG A 1 93  ? 24.907 -23.535 27.343 0.60 22.12  ? 94  ARG A O   1 
ATOM   815  O  O   B ARG A 1 93  ? 24.920 -23.694 27.344 0.40 21.98  ? 94  ARG A O   1 
ATOM   816  C  CB  A ARG A 1 93  ? 24.352 -26.388 26.513 0.60 22.98  ? 94  ARG A CB  1 
ATOM   817  C  CB  B ARG A 1 93  ? 23.927 -26.537 26.466 0.40 20.48  ? 94  ARG A CB  1 
ATOM   818  C  CG  A ARG A 1 93  ? 24.220 -27.544 25.506 0.60 29.37  ? 94  ARG A CG  1 
ATOM   819  C  CG  B ARG A 1 93  ? 23.284 -27.607 25.592 0.40 21.21  ? 94  ARG A CG  1 
ATOM   820  C  CD  A ARG A 1 93  ? 25.143 -28.705 25.849 0.60 36.48  ? 94  ARG A CD  1 
ATOM   821  C  CD  B ARG A 1 93  ? 24.033 -28.917 25.631 0.40 32.33  ? 94  ARG A CD  1 
ATOM   822  N  NE  A ARG A 1 93  ? 24.877 -29.233 27.191 0.60 40.63  ? 94  ARG A NE  1 
ATOM   823  N  NE  B ARG A 1 93  ? 23.448 -29.891 24.707 0.40 39.33  ? 94  ARG A NE  1 
ATOM   824  C  CZ  A ARG A 1 93  ? 23.984 -30.180 27.462 0.60 52.53  ? 94  ARG A CZ  1 
ATOM   825  C  CZ  B ARG A 1 93  ? 23.339 -31.192 24.956 0.40 50.69  ? 94  ARG A CZ  1 
ATOM   826  N  NH1 A ARG A 1 93  ? 23.804 -30.590 28.708 0.60 39.70  ? 94  ARG A NH1 1 
ATOM   827  N  NH1 B ARG A 1 93  ? 22.801 -32.003 24.055 0.40 39.40  ? 94  ARG A NH1 1 
ATOM   828  N  NH2 A ARG A 1 93  ? 23.261 -30.719 26.488 0.60 38.38  ? 94  ARG A NH2 1 
ATOM   829  N  NH2 B ARG A 1 93  ? 23.766 -31.693 26.108 0.40 38.64  ? 94  ARG A NH2 1 
ATOM   830  N  N   . LEU A 1 94  ? 22.713 -23.726 27.875 1.00 21.31  ? 95  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 94  ? 22.762 -22.715 28.919 1.00 21.23  ? 95  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 94  ? 22.508 -23.343 30.282 1.00 25.99  ? 95  LEU A C   1 
ATOM   833  O  O   . LEU A 1 94  ? 21.431 -23.903 30.528 1.00 25.41  ? 95  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 94  ? 21.734 -21.621 28.588 1.00 21.62  ? 95  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 94  ? 21.728 -20.414 29.538 1.00 25.58  ? 95  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 94  ? 22.979 -19.557 29.328 1.00 24.30  ? 95  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 94  ? 20.447 -19.615 29.389 1.00 27.41  ? 95  LEU A CD2 1 
ATOM   838  N  N   . ASN A 1 95  ? 23.506 -23.251 31.173 1.00 25.23  ? 96  ASN A N   1 
ATOM   839  C  CA  . ASN A 1 95  ? 23.402 -23.797 32.534 1.00 26.28  ? 96  ASN A CA  1 
ATOM   840  C  C   . ASN A 1 95  ? 22.703 -22.781 33.453 1.00 30.64  ? 96  ASN A C   1 
ATOM   841  O  O   . ASN A 1 95  ? 23.352 -22.083 34.233 1.00 31.02  ? 96  ASN A O   1 
ATOM   842  C  CB  . ASN A 1 95  ? 24.791 -24.204 33.075 1.00 29.80  ? 96  ASN A CB  1 
ATOM   843  C  CG  . ASN A 1 95  ? 24.738 -24.839 34.462 1.00 46.80  ? 96  ASN A CG  1 
ATOM   844  O  OD1 . ASN A 1 95  ? 23.730 -25.406 34.881 1.00 41.28  ? 96  ASN A OD1 1 
ATOM   845  N  ND2 . ASN A 1 95  ? 25.823 -24.755 35.205 1.00 39.57  ? 96  ASN A ND2 1 
ATOM   846  N  N   . LEU A 1 96  ? 21.396 -22.645 33.278 1.00 27.66  ? 97  LEU A N   1 
ATOM   847  C  CA  . LEU A 1 96  ? 20.573 -21.693 34.027 1.00 29.06  ? 97  LEU A CA  1 
ATOM   848  C  C   . LEU A 1 96  ? 20.043 -22.349 35.288 1.00 33.75  ? 97  LEU A C   1 
ATOM   849  O  O   . LEU A 1 96  ? 19.388 -23.402 35.222 1.00 32.50  ? 97  LEU A O   1 
ATOM   850  C  CB  . LEU A 1 96  ? 19.441 -21.214 33.111 1.00 29.90  ? 97  LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 96  ? 18.713 -19.934 33.453 1.00 36.26  ? 97  LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 96  ? 19.709 -18.737 33.576 1.00 35.86  ? 97  LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 96  ? 17.655 -19.651 32.394 1.00 37.13  ? 97  LEU A CD2 1 
ATOM   854  N  N   . ARG A 1 97  ? 20.381 -21.753 36.454 1.00 30.85  ? 98  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 97  ? 19.999 -22.271 37.777 1.00 33.47  ? 98  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 97  ? 19.462 -21.154 38.658 1.00 34.85  ? 98  ARG A C   1 
ATOM   857  O  O   . ARG A 1 97  ? 19.815 -19.985 38.454 1.00 32.31  ? 98  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 97  ? 21.209 -22.936 38.466 1.00 36.03  ? 98  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 97  ? 21.803 -24.123 37.690 1.00 43.54  ? 98  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 97  ? 23.054 -24.706 38.334 1.00 58.61  ? 98  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 97  ? 22.807 -25.218 39.688 1.00 76.72  ? 98  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 97  ? 22.342 -26.434 39.968 1.00 95.97  ? 98  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 97  ? 22.142 -26.800 41.227 1.00 84.16  ? 98  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 97  ? 22.070 -27.291 38.990 1.00 84.74  ? 98  ARG A NH2 1 
ATOM   865  N  N   . GLU A 1 98  ? 18.629 -21.494 39.667 1.00 33.02  ? 99  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 98  ? 18.103 -20.474 40.587 1.00 33.38  ? 99  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 98  ? 19.224 -19.578 41.153 1.00 37.45  ? 99  GLU A C   1 
ATOM   868  O  O   . GLU A 1 98  ? 19.052 -18.361 41.242 1.00 37.70  ? 99  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 98  ? 17.332 -21.141 41.752 1.00 36.80  ? 99  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 98  ? 16.631 -20.155 42.668 1.00 47.05  ? 99  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 98  ? 15.909 -20.781 43.845 1.00 80.14  ? 99  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 98  ? 16.488 -21.673 44.509 1.00 75.95  ? 99  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 98  ? 14.758 -20.367 44.112 1.00 83.58  ? 99  GLU A OE2 1 
ATOM   874  N  N   . GLY A 1 99  ? 20.351 -20.192 41.505 1.00 35.42  ? 100 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 99  ? 21.499 -19.502 42.090 1.00 36.11  ? 100 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 99  ? 22.319 -18.642 41.144 1.00 37.58  ? 100 GLY A C   1 
ATOM   877  O  O   . GLY A 1 99  ? 23.139 -17.840 41.598 1.00 36.98  ? 100 GLY A O   1 
ATOM   878  N  N   . ASN A 1 100 ? 22.107 -18.767 39.824 1.00 32.64  ? 101 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 100 ? 22.908 -17.962 38.895 1.00 30.65  ? 101 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 100 ? 22.090 -17.096 37.935 1.00 33.31  ? 101 ASN A C   1 
ATOM   881  O  O   . ASN A 1 100 ? 22.673 -16.302 37.194 1.00 31.31  ? 101 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 100 ? 23.886 -18.871 38.118 1.00 30.28  ? 101 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 100 ? 23.230 -19.812 37.118 1.00 37.28  ? 101 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 100 ? 22.192 -19.502 36.533 1.00 27.67  ? 101 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 100 ? 23.840 -20.966 36.865 1.00 30.99  ? 101 ASN A ND2 1 
ATOM   886  N  N   . ILE A 1 101 ? 20.755 -17.275 37.907 1.00 31.13  ? 102 ILE A N   1 
ATOM   887  C  CA  . ILE A 1 101 ? 19.887 -16.621 36.915 1.00 30.39  ? 102 ILE A CA  1 
ATOM   888  C  C   . ILE A 1 101 ? 20.009 -15.096 36.900 1.00 32.39  ? 102 ILE A C   1 
ATOM   889  O  O   . ILE A 1 101 ? 20.041 -14.511 35.809 1.00 29.52  ? 102 ILE A O   1 
ATOM   890  C  CB  . ILE A 1 101 ? 18.412 -17.077 37.004 1.00 34.32  ? 102 ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 101 ? 17.575 -16.493 35.826 1.00 34.95  ? 102 ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 101 ? 17.784 -16.814 38.376 1.00 33.95  ? 102 ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 101 ? 16.366 -17.323 35.417 1.00 37.03  ? 102 ILE A CD1 1 
ATOM   894  N  N   . MET A 1 102 ? 20.091 -14.448 38.076 1.00 30.55  ? 103 MET A N   1 
ATOM   895  C  CA  . MET A 1 102 ? 20.235 -12.996 38.096 1.00 31.18  ? 103 MET A CA  1 
ATOM   896  C  C   . MET A 1 102 ? 21.540 -12.535 37.452 1.00 32.46  ? 103 MET A C   1 
ATOM   897  O  O   . MET A 1 102 ? 21.501 -11.610 36.644 1.00 30.36  ? 103 MET A O   1 
ATOM   898  C  CB  . MET A 1 102 ? 20.065 -12.417 39.520 1.00 35.45  ? 103 MET A CB  1 
ATOM   899  C  CG  . MET A 1 102 ? 18.703 -12.717 40.140 1.00 41.93  ? 103 MET A CG  1 
ATOM   900  S  SD  . MET A 1 102 ? 17.264 -12.361 39.088 1.00 48.01  ? 103 MET A SD  1 
ATOM   901  C  CE  . MET A 1 102 ? 17.291 -10.544 39.101 1.00 45.24  ? 103 MET A CE  1 
ATOM   902  N  N   . ALA A 1 103 ? 22.684 -13.204 37.768 1.00 29.19  ? 104 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 103 ? 24.003 -12.859 37.197 1.00 28.42  ? 104 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 103 ? 24.000 -13.156 35.705 1.00 29.67  ? 104 ALA A C   1 
ATOM   905  O  O   . ALA A 1 103 ? 24.478 -12.342 34.909 1.00 27.47  ? 104 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 103 ? 25.106 -13.668 37.868 1.00 29.80  ? 104 ALA A CB  1 
ATOM   907  N  N   . VAL A 1 104 ? 23.428 -14.309 35.322 1.00 24.20  ? 105 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 104 ? 23.361 -14.684 33.897 1.00 22.93  ? 105 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 104 ? 22.555 -13.652 33.098 1.00 25.93  ? 105 VAL A C   1 
ATOM   910  O  O   . VAL A 1 104 ? 23.041 -13.217 32.048 1.00 24.81  ? 105 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 104 ? 22.877 -16.142 33.675 1.00 26.03  ? 105 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 104 ? 22.624 -16.433 32.193 1.00 24.31  ? 105 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 104 ? 23.894 -17.133 34.232 1.00 26.10  ? 105 VAL A CG2 1 
ATOM   914  N  N   A MET A 1 105 ? 21.354 -13.256 33.581 0.65 24.51  ? 106 MET A N   1 
ATOM   915  N  N   B MET A 1 105 ? 21.353 -13.263 33.579 0.35 24.63  ? 106 MET A N   1 
ATOM   916  C  CA  A MET A 1 105 ? 20.534 -12.273 32.858 0.65 25.56  ? 106 MET A CA  1 
ATOM   917  C  CA  B MET A 1 105 ? 20.524 -12.280 32.872 0.35 25.53  ? 106 MET A CA  1 
ATOM   918  C  C   A MET A 1 105 ? 21.248 -10.928 32.741 0.65 29.26  ? 106 MET A C   1 
ATOM   919  C  C   B MET A 1 105 ? 21.239 -10.935 32.745 0.35 29.53  ? 106 MET A C   1 
ATOM   920  O  O   A MET A 1 105 ? 21.246 -10.326 31.661 0.65 27.44  ? 106 MET A O   1 
ATOM   921  O  O   B MET A 1 105 ? 21.239 -10.349 31.659 0.35 28.24  ? 106 MET A O   1 
ATOM   922  C  CB  A MET A 1 105 ? 19.169 -12.080 33.520 0.65 29.32  ? 106 MET A CB  1 
ATOM   923  C  CB  B MET A 1 105 ? 19.162 -12.094 33.546 0.35 29.34  ? 106 MET A CB  1 
ATOM   924  C  CG  A MET A 1 105 ? 18.232 -11.215 32.688 0.65 33.45  ? 106 MET A CG  1 
ATOM   925  C  CG  B MET A 1 105 ? 18.219 -11.248 32.719 0.35 33.60  ? 106 MET A CG  1 
ATOM   926  S  SD  A MET A 1 105 ? 16.556 -11.234 33.340 0.65 39.12  ? 106 MET A SD  1 
ATOM   927  S  SD  B MET A 1 105 ? 16.642 -10.992 33.533 0.35 39.57  ? 106 MET A SD  1 
ATOM   928  C  CE  A MET A 1 105 ? 16.730 -10.096 34.767 0.65 37.05  ? 106 MET A CE  1 
ATOM   929  C  CE  B MET A 1 105 ? 16.170 -9.467  32.790 0.35 37.00  ? 106 MET A CE  1 
ATOM   930  N  N   . ALA A 1 106 ? 21.848 -10.457 33.846 1.00 27.19  ? 107 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 106 ? 22.598 -9.174  33.859 1.00 27.28  ? 107 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 106 ? 23.756 -9.213  32.853 1.00 27.41  ? 107 ALA A C   1 
ATOM   933  O  O   . ALA A 1 106 ? 23.946 -8.245  32.094 1.00 25.79  ? 107 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 106 ? 23.114 -8.877  35.258 1.00 29.14  ? 107 ALA A CB  1 
ATOM   935  N  N   . THR A 1 107 ? 24.495 -10.345 32.806 1.00 23.23  ? 108 THR A N   1 
ATOM   936  C  CA  . THR A 1 107 ? 25.607 -10.510 31.862 1.00 22.47  ? 108 THR A CA  1 
ATOM   937  C  C   . THR A 1 107 ? 25.084 -10.552 30.414 1.00 25.63  ? 108 THR A C   1 
ATOM   938  O  O   . THR A 1 107 ? 25.668 -9.901  29.551 1.00 23.14  ? 108 THR A O   1 
ATOM   939  C  CB  . THR A 1 107 ? 26.515 -11.704 32.235 1.00 28.30  ? 108 THR A CB  1 
ATOM   940  O  OG1 . THR A 1 107 ? 26.788 -11.683 33.641 1.00 27.05  ? 108 THR A OG1 1 
ATOM   941  C  CG2 . THR A 1 107 ? 27.840 -11.711 31.447 1.00 26.52  ? 108 THR A CG2 1 
ATOM   942  N  N   . ALA A 1 108 ? 23.977 -11.293 30.158 1.00 22.05  ? 109 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 108 ? 23.396 -11.389 28.811 1.00 20.86  ? 109 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 108 ? 22.882 -10.018 28.346 1.00 24.12  ? 109 ALA A C   1 
ATOM   945  O  O   . ALA A 1 108 ? 23.033 -9.679  27.170 1.00 22.58  ? 109 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 108 ? 22.283 -12.443 28.784 1.00 21.44  ? 109 ALA A CB  1 
ATOM   947  N  N   . MET A 1 109 ? 22.329 -9.198  29.268 1.00 22.22  ? 110 MET A N   1 
ATOM   948  C  CA  . MET A 1 109 ? 21.881 -7.856  28.878 1.00 22.53  ? 110 MET A CA  1 
ATOM   949  C  C   . MET A 1 109 ? 23.078 -6.988  28.441 1.00 25.34  ? 110 MET A C   1 
ATOM   950  O  O   . MET A 1 109 ? 23.030 -6.332  27.396 1.00 26.00  ? 110 MET A O   1 
ATOM   951  C  CB  . MET A 1 109 ? 21.115 -7.195  30.039 1.00 26.21  ? 110 MET A CB  1 
ATOM   952  C  CG  . MET A 1 109 ? 19.733 -7.786  30.222 1.00 31.47  ? 110 MET A CG  1 
ATOM   953  S  SD  . MET A 1 109 ? 18.986 -7.192  31.753 1.00 38.63  ? 110 MET A SD  1 
ATOM   954  C  CE  . MET A 1 109 ? 18.684 -5.478  31.308 1.00 36.71  ? 110 MET A CE  1 
ATOM   955  N  N   . TYR A 1 110 ? 24.158 -7.040  29.212 1.00 24.04  ? 111 TYR A N   1 
ATOM   956  C  CA  . TYR A 1 110 ? 25.395 -6.295  28.936 1.00 24.06  ? 111 TYR A CA  1 
ATOM   957  C  C   . TYR A 1 110 ? 26.021 -6.780  27.600 1.00 25.53  ? 111 TYR A C   1 
ATOM   958  O  O   . TYR A 1 110 ? 26.401 -5.959  26.758 1.00 23.85  ? 111 TYR A O   1 
ATOM   959  C  CB  . TYR A 1 110 ? 26.371 -6.517  30.093 1.00 24.68  ? 111 TYR A CB  1 
ATOM   960  C  CG  . TYR A 1 110 ? 27.791 -6.048  29.849 1.00 24.64  ? 111 TYR A CG  1 
ATOM   961  C  CD1 . TYR A 1 110 ? 28.120 -4.694  29.910 1.00 27.06  ? 111 TYR A CD1 1 
ATOM   962  C  CD2 . TYR A 1 110 ? 28.823 -6.964  29.649 1.00 23.78  ? 111 TYR A CD2 1 
ATOM   963  C  CE1 . TYR A 1 110 ? 29.435 -4.260  29.717 1.00 24.34  ? 111 TYR A CE1 1 
ATOM   964  C  CE2 . TYR A 1 110 ? 30.145 -6.545  29.498 1.00 23.20  ? 111 TYR A CE2 1 
ATOM   965  C  CZ  . TYR A 1 110 ? 30.444 -5.191  29.549 1.00 25.81  ? 111 TYR A CZ  1 
ATOM   966  O  OH  . TYR A 1 110 ? 31.737 -4.783  29.422 1.00 24.32  ? 111 TYR A OH  1 
ATOM   967  N  N   . LEU A 1 111 ? 26.085 -8.105  27.396 1.00 21.24  ? 112 LEU A N   1 
ATOM   968  C  CA  . LEU A 1 111 ? 26.669 -8.685  26.179 1.00 19.66  ? 112 LEU A CA  1 
ATOM   969  C  C   . LEU A 1 111 ? 25.749 -8.548  24.964 1.00 23.62  ? 112 LEU A C   1 
ATOM   970  O  O   . LEU A 1 111 ? 26.181 -8.828  23.846 1.00 22.51  ? 112 LEU A O   1 
ATOM   971  C  CB  . LEU A 1 111 ? 27.026 -10.171 26.411 1.00 18.03  ? 112 LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 111 ? 28.156 -10.449 27.441 1.00 20.93  ? 112 LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 111 ? 28.429 -11.976 27.541 1.00 21.22  ? 112 LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 111 ? 29.472 -9.663  27.070 1.00 22.67  ? 112 LEU A CD2 1 
ATOM   975  N  N   . GLN A 1 112 ? 24.461 -8.203  25.192 1.00 21.86  ? 113 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 112 ? 23.452 -8.074  24.128 1.00 23.12  ? 113 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 112 ? 23.236 -9.434  23.446 1.00 25.10  ? 113 GLN A C   1 
ATOM   978  O  O   . GLN A 1 112 ? 23.547 -9.629  22.264 1.00 22.85  ? 113 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 112 ? 23.814 -6.964  23.119 1.00 24.73  ? 113 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 112 ? 23.971 -5.568  23.751 1.00 26.50  ? 113 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 112 ? 24.708 -4.635  22.813 1.00 35.68  ? 113 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 112 ? 24.586 -4.725  21.601 1.00 29.50  ? 113 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 112 ? 25.512 -3.737  23.348 1.00 32.63  ? 113 GLN A NE2 1 
ATOM   984  N  N   . MET A 1 113 ? 22.733 -10.383 24.236 1.00 21.86  ? 114 MET A N   1 
ATOM   985  C  CA  . MET A 1 113 ? 22.432 -11.762 23.810 1.00 21.55  ? 114 MET A CA  1 
ATOM   986  C  C   . MET A 1 113 ? 20.930 -11.922 24.067 1.00 27.18  ? 114 MET A C   1 
ATOM   987  O  O   . MET A 1 113 ? 20.499 -12.397 25.127 1.00 25.55  ? 114 MET A O   1 
ATOM   988  C  CB  . MET A 1 113 ? 23.287 -12.733 24.628 1.00 22.45  ? 114 MET A CB  1 
ATOM   989  C  CG  . MET A 1 113 ? 24.780 -12.616 24.299 1.00 23.15  ? 114 MET A CG  1 
ATOM   990  S  SD  . MET A 1 113 ? 25.788 -13.649 25.367 1.00 25.01  ? 114 MET A SD  1 
ATOM   991  C  CE  . MET A 1 113 ? 25.406 -15.332 24.642 1.00 22.30  ? 114 MET A CE  1 
ATOM   992  N  N   . GLU A 1 114 ? 20.138 -11.378 23.132 1.00 27.44  ? 115 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 114 ? 18.681 -11.232 23.269 1.00 29.61  ? 115 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 114 ? 17.914 -12.511 23.582 1.00 30.87  ? 115 GLU A C   1 
ATOM   995  O  O   . GLU A 1 114 ? 16.986 -12.441 24.381 1.00 30.61  ? 115 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 114 ? 18.065 -10.550 22.040 1.00 32.91  ? 115 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 114 ? 18.621 -9.155  21.796 1.00 46.20  ? 115 GLU A CG  1 
ATOM   998  N  N   . HIS A 1 115 ? 18.272 -13.659 22.977 1.00 26.41  ? 116 HIS A N   1 
ATOM   999  C  CA  . HIS A 1 115 ? 17.529 -14.894 23.263 1.00 28.19  ? 116 HIS A CA  1 
ATOM   1000 C  C   . HIS A 1 115 ? 17.747 -15.374 24.702 1.00 29.64  ? 116 HIS A C   1 
ATOM   1001 O  O   . HIS A 1 115 ? 16.794 -15.826 25.343 1.00 30.62  ? 116 HIS A O   1 
ATOM   1002 C  CB  . HIS A 1 115 ? 17.818 -15.989 22.236 1.00 29.75  ? 116 HIS A CB  1 
ATOM   1003 C  CG  . HIS A 1 115 ? 17.353 -15.641 20.859 1.00 34.58  ? 116 HIS A CG  1 
ATOM   1004 N  ND1 . HIS A 1 115 ? 16.013 -15.430 20.585 1.00 38.23  ? 116 HIS A ND1 1 
ATOM   1005 C  CD2 . HIS A 1 115 ? 18.060 -15.511 19.713 1.00 35.99  ? 116 HIS A CD2 1 
ATOM   1006 C  CE1 . HIS A 1 115 ? 15.951 -15.143 19.294 1.00 37.94  ? 116 HIS A CE1 1 
ATOM   1007 N  NE2 . HIS A 1 115 ? 17.153 -15.198 18.726 1.00 36.96  ? 116 HIS A NE2 1 
ATOM   1008 N  N   . VAL A 1 116 ? 18.985 -15.218 25.224 1.00 24.09  ? 117 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 116 ? 19.287 -15.554 26.620 1.00 24.12  ? 117 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 116 ? 18.502 -14.639 27.574 1.00 29.73  ? 117 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 116 ? 17.873 -15.128 28.529 1.00 27.78  ? 117 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 116 ? 20.804 -15.574 26.934 1.00 25.84  ? 117 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 116 ? 21.043 -15.811 28.430 1.00 25.50  ? 117 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 116 ? 21.513 -16.644 26.100 1.00 25.01  ? 117 VAL A CG2 1 
ATOM   1015 N  N   . VAL A 1 117 ? 18.507 -13.315 27.302 1.00 26.17  ? 118 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 117 ? 17.754 -12.347 28.118 1.00 27.09  ? 118 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 117 ? 16.267 -12.767 28.184 1.00 32.96  ? 118 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 117 ? 15.709 -12.841 29.282 1.00 32.30  ? 118 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 117 ? 17.938 -10.882 27.632 1.00 29.87  ? 118 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 117 ? 17.113 -9.903  28.482 1.00 30.74  ? 118 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 117 ? 19.413 -10.480 27.659 1.00 28.33  ? 118 VAL A CG2 1 
ATOM   1022 N  N   A ASP A 1 118 ? 15.627 -12.970 27.014 0.41 31.35  ? 119 ASP A N   1 
ATOM   1023 N  N   B ASP A 1 118 ? 15.699 -13.165 27.029 0.59 30.32  ? 119 ASP A N   1 
ATOM   1024 C  CA  A ASP A 1 118 ? 14.207 -13.334 26.892 0.41 32.91  ? 119 ASP A CA  1 
ATOM   1025 C  CA  B ASP A 1 118 ? 14.320 -13.648 26.893 0.59 31.09  ? 119 ASP A CA  1 
ATOM   1026 C  C   A ASP A 1 118 ? 13.791 -14.538 27.737 0.41 37.16  ? 119 ASP A C   1 
ATOM   1027 C  C   B ASP A 1 118 ? 14.013 -14.863 27.781 0.59 33.50  ? 119 ASP A C   1 
ATOM   1028 O  O   A ASP A 1 118 ? 12.731 -14.501 28.354 0.41 38.45  ? 119 ASP A O   1 
ATOM   1029 O  O   B ASP A 1 118 ? 13.050 -14.802 28.544 0.59 33.46  ? 119 ASP A O   1 
ATOM   1030 C  CB  A ASP A 1 118 ? 13.817 -13.546 25.418 0.41 35.00  ? 119 ASP A CB  1 
ATOM   1031 C  CB  B ASP A 1 118 ? 13.989 -13.942 25.417 0.59 33.10  ? 119 ASP A CB  1 
ATOM   1032 C  CG  A ASP A 1 118 ? 13.624 -12.268 24.622 0.41 47.73  ? 119 ASP A CG  1 
ATOM   1033 C  CG  B ASP A 1 118 ? 12.535 -14.295 25.160 0.59 47.42  ? 119 ASP A CG  1 
ATOM   1034 O  OD1 A ASP A 1 118 ? 13.097 -11.287 25.188 0.41 51.38  ? 119 ASP A OD1 1 
ATOM   1035 O  OD1 B ASP A 1 118 ? 11.656 -13.468 25.486 0.59 50.28  ? 119 ASP A OD1 1 
ATOM   1036 O  OD2 A ASP A 1 118 ? 13.991 -12.251 23.430 0.41 53.34  ? 119 ASP A OD2 1 
ATOM   1037 O  OD2 B ASP A 1 118 ? 12.278 -15.391 24.620 0.59 52.85  ? 119 ASP A OD2 1 
ATOM   1038 N  N   A THR A 1 119 ? 14.629 -15.586 27.783 0.41 32.14  ? 120 THR A N   1 
ATOM   1039 N  N   B THR A 1 119 ? 14.822 -15.947 27.714 0.59 28.36  ? 120 THR A N   1 
ATOM   1040 C  CA  A THR A 1 119 ? 14.354 -16.803 28.555 0.41 32.28  ? 120 THR A CA  1 
ATOM   1041 C  CA  B THR A 1 119 ? 14.541 -17.127 28.554 0.59 28.80  ? 120 THR A CA  1 
ATOM   1042 C  C   A THR A 1 119 ? 14.538 -16.578 30.031 0.41 34.49  ? 120 THR A C   1 
ATOM   1043 C  C   B THR A 1 119 ? 14.738 -16.847 30.059 0.59 32.59  ? 120 THR A C   1 
ATOM   1044 O  O   A THR A 1 119 ? 13.694 -17.017 30.813 0.41 34.95  ? 120 THR A O   1 
ATOM   1045 O  O   B THR A 1 119 ? 14.087 -17.499 30.877 0.59 32.36  ? 120 THR A O   1 
ATOM   1046 C  CB  A THR A 1 119 ? 15.170 -17.952 28.016 0.41 38.71  ? 120 THR A CB  1 
ATOM   1047 C  CB  B THR A 1 119 ? 15.291 -18.383 28.095 0.59 30.14  ? 120 THR A CB  1 
ATOM   1048 O  OG1 A THR A 1 119 ? 14.811 -18.042 26.657 0.41 37.66  ? 120 THR A OG1 1 
ATOM   1049 O  OG1 B THR A 1 119 ? 14.636 -19.509 28.686 0.59 29.97  ? 120 THR A OG1 1 
ATOM   1050 C  CG2 A THR A 1 119 ? 14.853 -19.271 28.700 0.41 38.60  ? 120 THR A CG2 1 
ATOM   1051 C  CG2 B THR A 1 119 ? 16.766 -18.380 28.489 0.59 22.35  ? 120 THR A CG2 1 
ATOM   1052 N  N   . CYS A 1 120 ? 15.639 -15.902 30.421 1.00 29.38  ? 121 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 120 ? 15.890 -15.553 31.831 1.00 30.19  ? 121 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 120 ? 14.673 -14.830 32.377 1.00 36.79  ? 121 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 120 ? 14.184 -15.179 33.462 1.00 35.93  ? 121 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 120 ? 17.136 -14.686 31.946 1.00 29.20  ? 121 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 120 ? 18.677 -15.603 31.772 1.00 31.70  ? 121 CYS A SG  1 
ATOM   1058 N  N   . ARG A 1 121 ? 14.153 -13.850 31.593 1.00 35.43  ? 122 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 121 ? 12.947 -13.086 31.934 1.00 37.30  ? 122 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 121 ? 11.751 -14.031 32.193 1.00 41.68  ? 122 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 121 ? 11.029 -13.861 33.183 1.00 41.47  ? 122 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 121 ? 12.601 -12.101 30.806 1.00 39.01  ? 122 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 121 ? 13.456 -10.851 30.795 1.00 55.17  ? 122 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 121 ? 12.638 -9.614  30.478 1.00 70.26  ? 122 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 121 ? 13.009 -9.030  29.187 1.00 78.86  ? 122 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 121 ? 13.938 -8.092  29.020 1.00 87.90  ? 122 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 121 ? 14.614 -7.623  30.063 1.00 69.05  ? 122 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 121 ? 14.201 -7.621  27.809 1.00 75.10  ? 122 ARG A NH2 1 
ATOM   1069 N  N   . LYS A 1 122 ? 11.571 -15.036 31.314 1.00 39.33  ? 123 LYS A N   1 
ATOM   1070 C  CA  . LYS A 1 122 ? 10.488 -16.024 31.403 1.00 40.79  ? 123 LYS A CA  1 
ATOM   1071 C  C   . LYS A 1 122 ? 10.642 -16.931 32.622 1.00 44.23  ? 123 LYS A C   1 
ATOM   1072 O  O   . LYS A 1 122 ? 9.655  -17.171 33.311 1.00 44.73  ? 123 LYS A O   1 
ATOM   1073 C  CB  . LYS A 1 122 ? 10.390 -16.859 30.109 1.00 42.23  ? 123 LYS A CB  1 
ATOM   1074 C  CG  . LYS A 1 122 ? 9.880  -16.067 28.911 1.00 59.70  ? 123 LYS A CG  1 
ATOM   1075 C  CD  . LYS A 1 122 ? 9.531  -16.973 27.731 1.00 71.00  ? 123 LYS A CD  1 
ATOM   1076 C  CE  . LYS A 1 122 ? 9.574  -16.263 26.393 1.00 80.95  ? 123 LYS A CE  1 
ATOM   1077 N  NZ  . LYS A 1 122 ? 8.557  -15.183 26.274 1.00 89.22  ? 123 LYS A NZ  1 
ATOM   1078 N  N   . PHE A 1 123 ? 11.875 -17.430 32.893 1.00 39.26  ? 124 PHE A N   1 
ATOM   1079 C  CA  . PHE A 1 123 ? 12.151 -18.289 34.052 1.00 39.49  ? 124 PHE A CA  1 
ATOM   1080 C  C   . PHE A 1 123 ? 11.951 -17.520 35.366 1.00 43.96  ? 124 PHE A C   1 
ATOM   1081 O  O   . PHE A 1 123 ? 11.408 -18.082 36.324 1.00 43.84  ? 124 PHE A O   1 
ATOM   1082 C  CB  . PHE A 1 123 ? 13.552 -18.908 33.957 1.00 39.64  ? 124 PHE A CB  1 
ATOM   1083 C  CG  . PHE A 1 123 ? 13.673 -20.202 33.169 1.00 41.01  ? 124 PHE A CG  1 
ATOM   1084 C  CD1 . PHE A 1 123 ? 13.092 -20.331 31.908 1.00 43.97  ? 124 PHE A CD1 1 
ATOM   1085 C  CD2 . PHE A 1 123 ? 14.419 -21.269 33.661 1.00 43.24  ? 124 PHE A CD2 1 
ATOM   1086 C  CE1 . PHE A 1 123 ? 13.213 -21.521 31.180 1.00 44.08  ? 124 PHE A CE1 1 
ATOM   1087 C  CE2 . PHE A 1 123 ? 14.546 -22.456 32.926 1.00 44.91  ? 124 PHE A CE2 1 
ATOM   1088 C  CZ  . PHE A 1 123 ? 13.941 -22.573 31.693 1.00 42.38  ? 124 PHE A CZ  1 
ATOM   1089 N  N   . ILE A 1 124 ? 12.330 -16.222 35.395 1.00 39.23  ? 125 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 124 ? 12.114 -15.375 36.582 1.00 40.65  ? 125 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 124 ? 10.612 -15.149 36.837 1.00 47.81  ? 125 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 124 ? 10.167 -15.268 37.985 1.00 48.69  ? 125 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 124 ? 12.937 -14.059 36.507 1.00 42.62  ? 125 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 124 ? 14.430 -14.372 36.652 1.00 40.93  ? 125 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 124 ? 12.492 -13.024 37.579 1.00 45.74  ? 125 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 124 ? 15.349 -13.293 36.128 1.00 45.05  ? 125 ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 125 ? 9.838  -14.860 35.765 1.00 46.19  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 125 ? 8.388  -14.608 35.829 1.00 48.71  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 125 ? 7.612  -15.832 36.349 1.00 53.73  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 125 ? 6.635  -15.669 37.082 1.00 54.08  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 125 ? 7.860  -14.165 34.455 1.00 52.14  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 125 ? 6.508  -13.461 34.504 1.00 70.23  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 125 ? 5.889  -13.350 33.118 1.00 82.80  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 125 ? 4.468  -12.843 33.165 1.00 97.47  ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 125 ? 3.821  -12.904 31.827 1.00 108.18 ? 126 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 126 ? 8.067  -17.047 35.994 1.00 49.13  ? 127 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 126 ? 7.448  -18.300 36.439 1.00 50.52  ? 127 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 126 ? 7.595  -18.519 37.958 1.00 56.73  ? 127 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 126 ? 6.729  -19.141 38.560 1.00 57.68  ? 127 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 126 ? 8.050  -19.473 35.676 1.00 49.53  ? 127 ALA A CB  1 
ATOM   1111 N  N   . SER A 1 127 ? 8.685  -18.015 38.565 1.00 54.99  ? 128 SER A N   1 
ATOM   1112 C  CA  . SER A 1 127 ? 8.962  -18.162 39.999 1.00 57.45  ? 128 SER A CA  1 
ATOM   1113 C  C   . SER A 1 127 ? 8.286  -17.098 40.895 1.00 65.00  ? 128 SER A C   1 
ATOM   1114 O  O   . SER A 1 127 ? 8.198  -17.310 42.108 1.00 67.28  ? 128 SER A O   1 
ATOM   1115 C  CB  . SER A 1 127 ? 10.468 -18.197 40.254 1.00 61.23  ? 128 SER A CB  1 
ATOM   1116 O  OG  . SER A 1 127 ? 10.996 -19.493 40.022 1.00 73.07  ? 128 SER A OG  1 
ATOM   1117 N  N   . GLU A 1 128 ? 7.792  -15.981 40.307 1.00 61.04  ? 129 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 128 ? 7.131  -14.909 41.062 1.00 81.36  ? 129 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 128 ? 5.675  -15.241 41.412 1.00 123.96 ? 129 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 128 ? 5.394  -16.297 41.975 1.00 91.73  ? 129 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 128 ? 7.254  -13.548 40.343 1.00 81.87  ? 129 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 128 ? 6.237  -13.295 39.237 1.00 91.69  ? 129 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 128 ? 6.442  -12.063 38.374 1.00 111.46 ? 129 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 128 ? 7.545  -11.469 38.411 1.00 100.95 ? 129 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 128 ? 5.492  -11.698 37.644 1.00 106.04 ? 129 GLU A OE2 1 
HETATM 1126 C  C   . ACE B 2 1   ? 21.227 -35.099 5.870  1.00 26.48  ? 0   ACE D C   1 
HETATM 1127 O  O   . ACE B 2 1   ? 21.293 -33.944 6.317  1.00 27.79  ? 0   ACE D O   1 
HETATM 1128 C  CH3 . ACE B 2 1   ? 21.411 -36.289 6.771  1.00 26.19  ? 0   ACE D CH3 1 
ATOM   1129 N  N   A TRP B 2 2   ? 20.962 -35.366 4.598  0.78 24.61  ? 1   TRP D N   1 
ATOM   1130 N  N   B TRP B 2 2   ? 20.988 -35.384 4.589  0.22 24.88  ? 1   TRP D N   1 
ATOM   1131 C  CA  A TRP B 2 2   ? 20.774 -34.315 3.607  0.78 23.79  ? 1   TRP D CA  1 
ATOM   1132 C  CA  B TRP B 2 2   ? 20.740 -34.352 3.580  0.22 24.08  ? 1   TRP D CA  1 
ATOM   1133 C  C   A TRP B 2 2   ? 19.275 -34.170 3.302  0.78 27.69  ? 1   TRP D C   1 
ATOM   1134 C  C   B TRP B 2 2   ? 19.241 -34.167 3.386  0.22 27.27  ? 1   TRP D C   1 
ATOM   1135 O  O   A TRP B 2 2   ? 18.547 -35.170 3.270  0.78 28.58  ? 1   TRP D O   1 
ATOM   1136 O  O   B TRP B 2 2   ? 18.485 -35.140 3.468  0.22 27.04  ? 1   TRP D O   1 
ATOM   1137 C  CB  A TRP B 2 2   ? 21.566 -34.660 2.330  0.78 22.36  ? 1   TRP D CB  1 
ATOM   1138 C  CB  B TRP B 2 2   ? 21.436 -34.666 2.231  0.22 22.64  ? 1   TRP D CB  1 
ATOM   1139 C  CG  A TRP B 2 2   ? 23.065 -34.613 2.519  0.78 22.67  ? 1   TRP D CG  1 
ATOM   1140 C  CG  B TRP B 2 2   ? 20.754 -35.693 1.370  0.22 23.42  ? 1   TRP D CG  1 
ATOM   1141 C  CD1 A TRP B 2 2   ? 23.869 -35.616 2.981  0.78 25.28  ? 1   TRP D CD1 1 
ATOM   1142 C  CD1 B TRP B 2 2   ? 21.030 -37.026 1.316  0.22 26.48  ? 1   TRP D CD1 1 
ATOM   1143 C  CD2 A TRP B 2 2   ? 23.924 -33.493 2.271  0.78 22.46  ? 1   TRP D CD2 1 
ATOM   1144 C  CD2 B TRP B 2 2   ? 19.709 -35.461 0.411  0.22 23.13  ? 1   TRP D CD2 1 
ATOM   1145 N  NE1 A TRP B 2 2   ? 25.176 -35.172 3.071  0.78 24.58  ? 1   TRP D NE1 1 
ATOM   1146 N  NE1 B TRP B 2 2   ? 20.186 -37.651 0.429  0.22 25.99  ? 1   TRP D NE1 1 
ATOM   1147 C  CE2 A TRP B 2 2   ? 25.247 -33.899 2.573  0.78 25.69  ? 1   TRP D CE2 1 
ATOM   1148 C  CE2 B TRP B 2 2   ? 19.377 -36.712 -0.156 0.22 27.10  ? 1   TRP D CE2 1 
ATOM   1149 C  CE3 A TRP B 2 2   ? 23.705 -32.170 1.846  0.78 23.18  ? 1   TRP D CE3 1 
ATOM   1150 C  CE3 B TRP B 2 2   ? 18.995 -34.322 0.000  0.22 24.10  ? 1   TRP D CE3 1 
ATOM   1151 C  CZ2 A TRP B 2 2   ? 26.346 -33.041 2.432  0.78 24.84  ? 1   TRP D CZ2 1 
ATOM   1152 C  CZ2 B TRP B 2 2   ? 18.378 -36.853 -1.127 0.22 26.19  ? 1   TRP D CZ2 1 
ATOM   1153 C  CZ3 A TRP B 2 2   ? 24.801 -31.340 1.665  0.78 23.77  ? 1   TRP D CZ3 1 
ATOM   1154 C  CZ3 B TRP B 2 2   ? 17.995 -34.466 -0.949 0.22 25.73  ? 1   TRP D CZ3 1 
ATOM   1155 C  CH2 A TRP B 2 2   ? 26.098 -31.771 1.972  0.78 24.68  ? 1   TRP D CH2 1 
ATOM   1156 C  CH2 B TRP B 2 2   ? 17.703 -35.717 -1.511 0.22 26.20  ? 1   TRP D CH2 1 
ATOM   1157 N  N   . VAL B 2 3   ? 18.813 -32.927 3.113  1.00 23.17  ? 2   VAL D N   1 
ATOM   1158 C  CA  . VAL B 2 3   ? 17.397 -32.598 2.873  1.00 22.93  ? 2   VAL D CA  1 
ATOM   1159 C  C   . VAL B 2 3   ? 17.252 -31.541 1.772  1.00 24.58  ? 2   VAL D C   1 
ATOM   1160 O  O   . VAL B 2 3   ? 18.219 -30.852 1.423  1.00 24.51  ? 2   VAL D O   1 
ATOM   1161 C  CB  . VAL B 2 3   ? 16.675 -32.101 4.182  1.00 25.98  ? 2   VAL D CB  1 
ATOM   1162 C  CG1 . VAL B 2 3   ? 16.725 -33.139 5.314  1.00 25.42  ? 2   VAL D CG1 1 
ATOM   1163 C  CG2 . VAL B 2 3   ? 17.213 -30.740 4.660  1.00 25.73  ? 2   VAL D CG2 1 
ATOM   1164 N  N   . ILE B 2 4   ? 16.015 -31.365 1.299  1.00 22.49  ? 3   ILE D N   1 
ATOM   1165 C  CA  . ILE B 2 4   ? 15.663 -30.271 0.408  1.00 23.74  ? 3   ILE D CA  1 
ATOM   1166 C  C   . ILE B 2 4   ? 15.293 -29.122 1.392  1.00 27.05  ? 3   ILE D C   1 
ATOM   1167 O  O   . ILE B 2 4   ? 14.277 -29.243 2.090  1.00 27.08  ? 3   ILE D O   1 
ATOM   1168 C  CB  . ILE B 2 4   ? 14.460 -30.630 -0.508 1.00 25.71  ? 3   ILE D CB  1 
ATOM   1169 C  CG1 . ILE B 2 4   ? 14.752 -31.896 -1.408 1.00 24.37  ? 3   ILE D CG1 1 
ATOM   1170 C  CG2 . ILE B 2 4   ? 14.046 -29.390 -1.350 1.00 27.46  ? 3   ILE D CG2 1 
ATOM   1171 C  CD1 . ILE B 2 4   ? 16.074 -31.792 -2.349 1.00 27.00  ? 3   ILE D CD1 1 
ATOM   1172 N  N   . PRO B 2 5   ? 16.092 -28.035 1.499  1.00 26.03  ? 4   PRO D N   1 
ATOM   1173 C  CA  . PRO B 2 5   ? 15.748 -26.968 2.460  1.00 26.54  ? 4   PRO D CA  1 
ATOM   1174 C  C   . PRO B 2 5   ? 14.479 -26.195 2.086  1.00 30.75  ? 4   PRO D C   1 
ATOM   1175 O  O   . PRO B 2 5   ? 14.204 -25.997 0.903  1.00 30.27  ? 4   PRO D O   1 
ATOM   1176 C  CB  . PRO B 2 5   ? 16.991 -26.065 2.455  1.00 28.02  ? 4   PRO D CB  1 
ATOM   1177 C  CG  . PRO B 2 5   ? 17.572 -26.254 1.061  1.00 31.71  ? 4   PRO D CG  1 
ATOM   1178 C  CD  . PRO B 2 5   ? 17.327 -27.710 0.742  1.00 27.38  ? 4   PRO D CD  1 
ATOM   1179 N  N   . ALA B 2 6   ? 13.823 -25.600 3.091  1.00 28.33  ? 5   ALA D N   1 
HETATM 1180 C  C4  . 7ZO C 3 .   ? 27.273 -10.323 11.841 1.00 25.94  ? 201 7ZO A C4  1 
HETATM 1181 C  C5  . 7ZO C 3 .   ? 25.253 -9.395  12.213 1.00 28.03  ? 201 7ZO A C5  1 
HETATM 1182 C  C6  . 7ZO C 3 .   ? 23.946 -10.749 18.098 1.00 26.43  ? 201 7ZO A C6  1 
HETATM 1183 C  C7  . 7ZO C 3 .   ? 23.462 -9.447  18.151 1.00 26.93  ? 201 7ZO A C7  1 
HETATM 1184 C  C8  . 7ZO C 3 .   ? 25.513 -10.077 16.392 1.00 24.54  ? 201 7ZO A C8  1 
HETATM 1185 C  C10 . 7ZO C 3 .   ? 26.340 -10.246 14.028 1.00 22.88  ? 201 7ZO A C10 1 
HETATM 1186 C  C1  . 7ZO C 3 .   ? 23.944 -8.461  17.296 1.00 26.13  ? 201 7ZO A C1  1 
HETATM 1187 C  C2  . 7ZO C 3 .   ? 24.960 -8.790  16.406 1.00 24.45  ? 201 7ZO A C2  1 
HETATM 1188 C  C3  . 7ZO C 3 .   ? 24.968 -11.073 17.209 1.00 24.17  ? 201 7ZO A C3  1 
HETATM 1189 C  C9  . 7ZO C 3 .   ? 27.384 -10.636 13.185 1.00 23.17  ? 201 7ZO A C9  1 
HETATM 1190 C  C11 . 7ZO C 3 .   ? 22.228 -10.570 19.714 1.00 31.22  ? 201 7ZO A C11 1 
HETATM 1191 C  C12 . 7ZO C 3 .   ? 23.194 -11.567 19.109 1.00 28.73  ? 201 7ZO A C12 1 
HETATM 1192 N  N13 . 7ZO C 3 .   ? 26.207 -9.697  11.336 1.00 29.18  ? 201 7ZO A N13 1 
HETATM 1193 N  N14 . 7ZO C 3 .   ? 25.244 -9.631  13.530 1.00 26.66  ? 201 7ZO A N14 1 
HETATM 1194 N  N15 . 7ZO C 3 .   ? 22.453 -9.367  19.123 1.00 26.76  ? 201 7ZO A N15 1 
HETATM 1195 N  N16 . 7ZO C 3 .   ? 26.360 -10.530 15.357 1.00 21.57  ? 201 7ZO A N16 1 
HETATM 1196 O  O17 . 7ZO C 3 .   ? 21.380 -10.794 20.576 1.00 29.97  ? 201 7ZO A O17 1 
HETATM 1197 CL CL1 . 7ZO C 3 .   ? 28.810 -11.403 13.773 0.99 23.19  ? 201 7ZO A CL1 1 
HETATM 1198 CL CL  . CL  D 4 .   ? 21.311 -15.222 22.551 1.00 31.93  ? 202 CL  A CL  1 
HETATM 1199 S  S   A DMS E 5 .   ? 17.570 -35.356 -1.242 0.78 42.26  ? 101 DMS D S   1 
HETATM 1200 O  O   A DMS E 5 .   ? 16.283 -35.121 -0.601 0.78 43.85  ? 101 DMS D O   1 
HETATM 1201 C  C1  A DMS E 5 .   ? 18.708 -34.475 -0.199 0.78 40.64  ? 101 DMS D C1  1 
HETATM 1202 C  C2  A DMS E 5 .   ? 17.983 -36.998 -0.783 0.78 41.75  ? 101 DMS D C2  1 
HETATM 1203 O  O   . HOH F 6 .   ? 25.825 -3.416  26.373 1.00 32.86  ? 301 HOH A O   1 
HETATM 1204 O  O   . HOH F 6 .   ? 35.582 -25.677 25.568 1.00 35.86  ? 302 HOH A O   1 
HETATM 1205 O  O   . HOH F 6 .   ? 37.936 2.454   19.639 1.00 37.14  ? 303 HOH A O   1 
HETATM 1206 O  O   . HOH F 6 .   ? 22.767 -5.355  19.774 1.00 55.99  ? 304 HOH A O   1 
HETATM 1207 O  O   . HOH F 6 .   ? 41.276 -21.688 25.208 1.00 40.87  ? 305 HOH A O   1 
HETATM 1208 O  O   . HOH F 6 .   ? 37.604 -20.373 26.964 1.00 30.78  ? 306 HOH A O   1 
HETATM 1209 O  O   . HOH F 6 .   ? 44.469 -0.891  17.879 1.00 50.11  ? 307 HOH A O   1 
HETATM 1210 O  O   . HOH F 6 .   ? 44.959 -11.286 18.639 1.00 53.85  ? 308 HOH A O   1 
HETATM 1211 O  O   . HOH F 6 .   ? 38.376 -14.937 15.446 1.00 31.14  ? 309 HOH A O   1 
HETATM 1212 O  O   . HOH F 6 .   ? 16.534 -27.546 -3.249 1.00 46.99  ? 310 HOH A O   1 
HETATM 1213 O  O   . HOH F 6 .   ? 27.315 -35.350 11.827 1.00 54.47  ? 311 HOH A O   1 
HETATM 1214 O  O   . HOH F 6 .   ? 31.831 -0.828  15.869 1.00 36.49  ? 312 HOH A O   1 
HETATM 1215 O  O   . HOH F 6 .   ? 22.941 -28.212 12.607 1.00 23.86  ? 313 HOH A O   1 
HETATM 1216 O  O   . HOH F 6 .   ? 43.597 -6.612  31.948 1.00 45.99  ? 314 HOH A O   1 
HETATM 1217 O  O   . HOH F 6 .   ? 26.790 -31.935 16.116 1.00 41.72  ? 315 HOH A O   1 
HETATM 1218 O  O   . HOH F 6 .   ? 20.794 -5.856  25.964 1.00 38.15  ? 316 HOH A O   1 
HETATM 1219 O  O   . HOH F 6 .   ? 32.428 -24.716 32.201 1.00 58.65  ? 317 HOH A O   1 
HETATM 1220 O  O   . HOH F 6 .   ? 33.307 -20.726 29.531 1.00 46.96  ? 318 HOH A O   1 
HETATM 1221 O  O   . HOH F 6 .   ? 41.280 -16.943 15.182 1.00 33.53  ? 319 HOH A O   1 
HETATM 1222 O  O   . HOH F 6 .   ? 41.611 -12.794 14.306 1.00 72.95  ? 320 HOH A O   1 
HETATM 1223 O  O   . HOH F 6 .   ? 19.795 -9.528  36.941 1.00 39.44  ? 321 HOH A O   1 
HETATM 1224 O  O   . HOH F 6 .   ? 13.501 -14.331 21.766 1.00 65.70  ? 322 HOH A O   1 
HETATM 1225 O  O   . HOH F 6 .   ? 29.872 -32.058 9.531  1.00 41.47  ? 323 HOH A O   1 
HETATM 1226 O  O   . HOH F 6 .   ? 17.992 -29.360 7.640  1.00 30.44  ? 324 HOH A O   1 
HETATM 1227 O  O   . HOH F 6 .   ? 22.542 -27.583 17.684 1.00 50.54  ? 325 HOH A O   1 
HETATM 1228 O  O   . HOH F 6 .   ? 27.247 -10.116 35.804 1.00 35.68  ? 326 HOH A O   1 
HETATM 1229 O  O   . HOH F 6 .   ? 28.248 -23.680 31.649 1.00 37.82  ? 327 HOH A O   1 
HETATM 1230 O  O   . HOH F 6 .   ? 32.287 -8.938  39.624 1.00 51.35  ? 328 HOH A O   1 
HETATM 1231 O  O   . HOH F 6 .   ? 30.277 1.482   33.942 1.00 57.33  ? 329 HOH A O   1 
HETATM 1232 O  O   . HOH F 6 .   ? 23.465 -5.694  32.891 1.00 35.99  ? 330 HOH A O   1 
HETATM 1233 O  O   . HOH F 6 .   ? 27.321 -28.144 18.634 1.00 27.92  ? 331 HOH A O   1 
HETATM 1234 O  O   . HOH F 6 .   ? 14.236 -16.831 23.401 1.00 40.92  ? 332 HOH A O   1 
HETATM 1235 O  O   . HOH F 6 .   ? 26.778 -16.496 38.623 1.00 47.33  ? 333 HOH A O   1 
HETATM 1236 O  O   . HOH F 6 .   ? 12.617 -20.426 42.423 1.00 57.68  ? 334 HOH A O   1 
HETATM 1237 O  O   . HOH F 6 .   ? 21.740 -29.603 -5.255 1.00 36.37  ? 335 HOH A O   1 
HETATM 1238 O  O   . HOH F 6 .   ? 43.537 -10.721 35.379 1.00 59.16  ? 336 HOH A O   1 
HETATM 1239 O  O   . HOH F 6 .   ? 4.337  -20.226 37.815 1.00 57.45  ? 337 HOH A O   1 
HETATM 1240 O  O   . HOH F 6 .   ? 15.404 -9.877  24.809 1.00 49.26  ? 338 HOH A O   1 
HETATM 1241 O  O   . HOH F 6 .   ? 20.524 -13.379 20.374 1.00 47.79  ? 339 HOH A O   1 
HETATM 1242 O  O   . HOH F 6 .   ? 28.216 -8.807  39.861 1.00 43.58  ? 340 HOH A O   1 
HETATM 1243 O  O   . HOH F 6 .   ? 41.294 -7.009  35.867 1.00 42.42  ? 341 HOH A O   1 
HETATM 1244 O  O   . HOH F 6 .   ? 21.916 -24.941 18.309 1.00 21.17  ? 342 HOH A O   1 
HETATM 1245 O  O   . HOH F 6 .   ? 29.579 -2.151  13.726 1.00 58.77  ? 343 HOH A O   1 
HETATM 1246 O  O   . HOH F 6 .   ? 26.026 -21.788 38.584 1.00 36.27  ? 344 HOH A O   1 
HETATM 1247 O  O   . HOH F 6 .   ? 30.456 -0.501  36.841 1.00 48.49  ? 345 HOH A O   1 
HETATM 1248 O  O   . HOH F 6 .   ? 7.069  -16.984 32.433 1.00 52.32  ? 346 HOH A O   1 
HETATM 1249 O  O   . HOH F 6 .   ? 25.696 -2.828  19.966 1.00 58.04  ? 347 HOH A O   1 
HETATM 1250 O  O   . HOH F 6 .   ? 36.821 -5.636  12.175 1.00 34.25  ? 348 HOH A O   1 
HETATM 1251 O  O   . HOH F 6 .   ? 34.874 -18.866 13.846 0.50 24.99  ? 349 HOH A O   1 
HETATM 1252 O  O   . HOH F 6 .   ? 26.419 -7.710  36.774 1.00 52.05  ? 350 HOH A O   1 
HETATM 1253 O  O   . HOH F 6 .   ? 27.212 -2.472  16.053 1.00 61.04  ? 351 HOH A O   1 
HETATM 1254 O  O   . HOH F 6 .   ? 21.494 -29.965 14.195 1.00 68.73  ? 352 HOH A O   1 
HETATM 1255 O  O   . HOH F 6 .   ? 29.011 -31.143 7.224  1.00 28.36  ? 353 HOH A O   1 
HETATM 1256 O  O   . HOH F 6 .   ? 26.107 -22.549 29.887 1.00 25.88  ? 354 HOH A O   1 
HETATM 1257 O  O   . HOH F 6 .   ? 23.254 -17.114 44.268 1.00 59.81  ? 355 HOH A O   1 
HETATM 1258 O  O   . HOH F 6 .   ? 44.388 -12.495 41.206 1.00 49.97  ? 356 HOH A O   1 
HETATM 1259 O  O   . HOH F 6 .   ? 24.845 -26.765 18.991 1.00 32.54  ? 357 HOH A O   1 
HETATM 1260 O  O   . HOH F 6 .   ? 45.899 -14.213 21.472 1.00 56.18  ? 358 HOH A O   1 
HETATM 1261 O  O   . HOH F 6 .   ? 20.825 -7.178  19.693 1.00 51.49  ? 359 HOH A O   1 
HETATM 1262 O  O   . HOH F 6 .   ? 42.388 -10.400 15.376 1.00 42.43  ? 360 HOH A O   1 
HETATM 1263 O  O   . HOH F 6 .   ? 43.911 -4.341  25.694 1.00 44.68  ? 361 HOH A O   1 
HETATM 1264 O  O   . HOH F 6 .   ? 10.814 -11.382 34.454 1.00 48.19  ? 362 HOH A O   1 
HETATM 1265 O  O   . HOH F 6 .   ? 11.266 -14.923 40.533 1.00 85.39  ? 363 HOH A O   1 
HETATM 1266 O  O   . HOH F 6 .   ? 25.904 -4.536  17.877 1.00 45.82  ? 364 HOH A O   1 
HETATM 1267 O  O   . HOH F 6 .   ? 29.359 -27.386 20.628 1.00 25.10  ? 365 HOH A O   1 
HETATM 1268 O  O   . HOH F 6 .   ? 22.184 -34.003 26.127 1.00 69.44  ? 366 HOH A O   1 
HETATM 1269 O  O   . HOH F 6 .   ? 28.433 -24.288 34.301 1.00 53.06  ? 367 HOH A O   1 
HETATM 1270 O  O   A HOH F 6 .   ? 19.090 -23.047 4.245  0.60 35.50  ? 368 HOH A O   1 
HETATM 1271 O  O   . HOH F 6 .   ? 46.253 -29.822 21.299 1.00 68.74  ? 369 HOH A O   1 
HETATM 1272 O  O   . HOH F 6 .   ? 24.040 -15.824 21.156 1.00 27.46  ? 370 HOH A O   1 
HETATM 1273 O  O   . HOH F 6 .   ? 21.421 -27.076 14.502 0.50 37.08  ? 371 HOH A O   1 
HETATM 1274 O  O   . HOH F 6 .   ? 34.100 -7.848  35.620 1.00 31.87  ? 372 HOH A O   1 
HETATM 1275 O  O   . HOH F 6 .   ? 46.170 -15.816 27.632 1.00 62.20  ? 373 HOH A O   1 
HETATM 1276 O  O   . HOH F 6 .   ? 37.379 -6.435  34.232 1.00 37.14  ? 374 HOH A O   1 
HETATM 1277 O  O   . HOH F 6 .   ? 46.848 -21.825 17.870 1.00 42.00  ? 375 HOH A O   1 
HETATM 1278 O  O   . HOH F 6 .   ? 30.685 -28.818 22.628 1.00 36.82  ? 376 HOH A O   1 
HETATM 1279 O  O   . HOH F 6 .   ? 45.952 -8.898  43.960 1.00 47.33  ? 377 HOH A O   1 
HETATM 1280 O  O   . HOH F 6 .   ? 37.503 3.419   15.646 1.00 41.71  ? 378 HOH A O   1 
HETATM 1281 O  O   . HOH F 6 .   ? 38.986 -18.838 33.420 1.00 47.40  ? 379 HOH A O   1 
HETATM 1282 O  O   . HOH F 6 .   ? 21.338 -31.196 29.969 1.00 62.31  ? 380 HOH A O   1 
HETATM 1283 O  O   . HOH F 6 .   ? 26.024 -19.150 41.701 1.00 68.44  ? 381 HOH A O   1 
HETATM 1284 O  O   . HOH F 6 .   ? 22.646 -34.038 8.855  1.00 31.37  ? 382 HOH A O   1 
HETATM 1285 O  O   . HOH F 6 .   ? 20.106 -15.756 40.793 1.00 33.62  ? 383 HOH A O   1 
HETATM 1286 O  O   . HOH F 6 .   ? 31.831 -31.829 14.595 1.00 41.08  ? 384 HOH A O   1 
HETATM 1287 O  O   . HOH F 6 .   ? 46.241 -19.030 19.667 1.00 47.28  ? 385 HOH A O   1 
HETATM 1288 O  O   . HOH F 6 .   ? 47.211 -25.263 21.656 1.00 51.01  ? 386 HOH A O   1 
HETATM 1289 O  O   . HOH F 6 .   ? 18.039 -34.577 8.322  1.00 32.45  ? 387 HOH A O   1 
HETATM 1290 O  O   . HOH F 6 .   ? 44.658 -8.678  17.928 1.00 57.20  ? 388 HOH A O   1 
HETATM 1291 O  O   . HOH F 6 .   ? 27.667 -23.026 13.846 0.50 24.48  ? 389 HOH A O   1 
HETATM 1292 O  O   . HOH F 6 .   ? 26.333 -7.910  9.081  1.00 44.50  ? 390 HOH A O   1 
HETATM 1293 O  O   . HOH F 6 .   ? 45.255 -12.653 23.589 1.00 44.87  ? 391 HOH A O   1 
HETATM 1294 O  O   . HOH F 6 .   ? 40.384 -19.600 28.977 1.00 33.32  ? 392 HOH A O   1 
HETATM 1295 O  O   . HOH F 6 .   ? 37.875 -16.257 12.769 1.00 46.28  ? 393 HOH A O   1 
HETATM 1296 O  O   . HOH F 6 .   ? 33.022 -29.656 21.502 1.00 40.88  ? 394 HOH A O   1 
HETATM 1297 O  O   . HOH F 6 .   ? 19.686 -27.445 10.066 1.00 54.02  ? 395 HOH A O   1 
HETATM 1298 O  O   . HOH F 6 .   ? 42.071 -6.127  11.855 1.00 64.11  ? 396 HOH A O   1 
HETATM 1299 O  O   . HOH F 6 .   ? 23.603 -15.559 17.861 1.00 42.20  ? 397 HOH A O   1 
HETATM 1300 O  O   . HOH F 6 .   ? 22.436 -10.052 14.399 1.00 38.17  ? 398 HOH A O   1 
HETATM 1301 O  O   . HOH F 6 .   ? 27.072 -1.616  21.969 1.00 51.26  ? 399 HOH A O   1 
HETATM 1302 O  O   . HOH F 6 .   ? 41.165 -17.059 35.181 1.00 41.36  ? 400 HOH A O   1 
HETATM 1303 O  O   . HOH F 6 .   ? 20.995 -23.065 42.032 1.00 47.63  ? 401 HOH A O   1 
HETATM 1304 O  O   . HOH F 6 .   ? 44.548 -16.397 29.713 1.00 47.24  ? 402 HOH A O   1 
HETATM 1305 O  O   . HOH F 6 .   ? 35.447 2.087   13.608 1.00 55.99  ? 403 HOH A O   1 
HETATM 1306 O  O   . HOH F 6 .   ? 22.873 -14.809 40.325 1.00 32.19  ? 404 HOH A O   1 
HETATM 1307 O  O   . HOH F 6 .   ? 35.209 -29.691 23.525 1.00 46.56  ? 405 HOH A O   1 
HETATM 1308 O  O   . HOH F 6 .   ? 45.509 -10.679 30.304 1.00 57.40  ? 406 HOH A O   1 
HETATM 1309 O  O   . HOH F 6 .   ? 32.093 -15.604 39.788 1.00 32.86  ? 407 HOH A O   1 
HETATM 1310 O  O   . HOH F 6 .   ? 33.775 -33.093 12.279 1.00 40.23  ? 408 HOH A O   1 
HETATM 1311 O  O   . HOH F 6 .   ? 10.217 -11.598 39.863 1.00 59.81  ? 409 HOH A O   1 
HETATM 1312 O  O   . HOH F 6 .   ? 30.274 -10.460 40.544 1.00 42.73  ? 410 HOH A O   1 
HETATM 1313 O  O   . HOH F 6 .   ? 37.203 -2.525  11.625 1.00 55.00  ? 411 HOH A O   1 
HETATM 1314 O  O   . HOH F 6 .   ? 47.058 -20.245 21.923 1.00 62.97  ? 412 HOH A O   1 
HETATM 1315 O  O   . HOH F 6 .   ? 34.874 -33.406 21.884 1.00 55.51  ? 413 HOH A O   1 
HETATM 1316 O  O   . HOH F 6 .   ? 41.958 -8.120  13.709 1.00 57.96  ? 414 HOH A O   1 
HETATM 1317 O  O   . HOH F 6 .   ? 26.036 -29.223 22.570 1.00 55.45  ? 415 HOH A O   1 
HETATM 1318 O  O   . HOH F 6 .   ? 29.572 -0.803  22.176 1.00 54.37  ? 416 HOH A O   1 
HETATM 1319 O  O   . HOH F 6 .   ? 27.302 -25.461 28.265 1.00 54.39  ? 417 HOH A O   1 
HETATM 1320 O  O   . HOH F 6 .   ? 44.217 -25.931 26.628 1.00 57.87  ? 418 HOH A O   1 
HETATM 1321 O  O   . HOH F 6 .   ? 29.768 -22.572 36.730 1.00 71.97  ? 419 HOH A O   1 
HETATM 1322 O  O   . HOH F 6 .   ? 45.839 -17.080 17.116 1.00 65.84  ? 420 HOH A O   1 
HETATM 1323 O  O   . HOH F 6 .   ? 23.487 -30.268 19.169 1.00 64.63  ? 421 HOH A O   1 
HETATM 1324 O  O   B HOH F 6 .   ? 37.187 -11.940 40.029 0.50 33.15  ? 422 HOH A O   1 
HETATM 1325 O  O   . HOH F 6 .   ? 39.914 -5.559  33.846 1.00 39.97  ? 423 HOH A O   1 
HETATM 1326 O  O   . HOH F 6 .   ? 33.900 -17.606 39.332 1.00 57.18  ? 424 HOH A O   1 
HETATM 1327 O  O   . HOH F 6 .   ? 33.559 -0.279  19.993 1.00 45.71  ? 425 HOH A O   1 
HETATM 1328 O  O   . HOH F 6 .   ? 44.753 -8.099  15.155 1.00 68.85  ? 426 HOH A O   1 
HETATM 1329 O  O   . HOH F 6 .   ? 28.836 -16.133 41.328 1.00 65.34  ? 427 HOH A O   1 
HETATM 1330 O  O   . HOH F 6 .   ? 42.802 -18.236 30.717 1.00 46.05  ? 428 HOH A O   1 
HETATM 1331 O  O   . HOH F 6 .   ? 28.448 -2.590  11.274 1.00 73.16  ? 429 HOH A O   1 
HETATM 1332 O  O   . HOH F 6 .   ? 45.772 -5.514  23.668 1.00 46.56  ? 430 HOH A O   1 
HETATM 1333 O  O   . HOH F 6 .   ? 25.663 -15.818 41.010 1.00 49.63  ? 431 HOH A O   1 
HETATM 1334 O  O   . HOH F 6 .   ? 31.863 -26.166 27.030 1.00 44.57  ? 432 HOH A O   1 
HETATM 1335 O  O   . HOH F 6 .   ? 32.454 -4.068  41.185 1.00 63.82  ? 433 HOH A O   1 
HETATM 1336 O  O   . HOH F 6 .   ? 47.891 -23.397 19.820 1.00 62.99  ? 434 HOH A O   1 
HETATM 1337 O  O   . HOH F 6 .   ? 31.911 0.103   13.316 1.00 54.36  ? 435 HOH A O   1 
HETATM 1338 O  O   . HOH F 6 .   ? 37.668 -26.984 28.470 1.00 62.16  ? 436 HOH A O   1 
HETATM 1339 O  O   . HOH F 6 .   ? 35.249 -4.127  10.609 1.00 45.06  ? 437 HOH A O   1 
HETATM 1340 O  O   . HOH F 6 .   ? 27.234 -34.530 17.927 1.00 72.81  ? 438 HOH A O   1 
HETATM 1341 O  O   . HOH F 6 .   ? 28.419 -29.221 26.789 1.00 74.40  ? 439 HOH A O   1 
HETATM 1342 O  O   . HOH F 6 .   ? 20.098 -35.273 10.183 1.00 37.11  ? 440 HOH A O   1 
HETATM 1343 O  O   . HOH F 6 .   ? 19.438 -31.737 14.016 1.00 63.14  ? 441 HOH A O   1 
HETATM 1344 O  O   . HOH F 6 .   ? 36.982 -24.354 27.487 1.00 54.86  ? 442 HOH A O   1 
HETATM 1345 O  O   . HOH F 6 .   ? 24.290 -21.468 40.970 1.00 53.72  ? 443 HOH A O   1 
HETATM 1346 O  O   . HOH F 6 .   ? 30.919 -34.390 14.852 1.00 59.48  ? 444 HOH A O   1 
HETATM 1347 O  O   . HOH F 6 .   ? 23.007 -2.759  26.225 1.00 61.21  ? 445 HOH A O   1 
HETATM 1348 O  O   . HOH F 6 .   ? 33.775 -10.956 41.538 0.50 55.03  ? 446 HOH A O   1 
HETATM 1349 O  O   . HOH F 6 .   ? 46.605 -14.632 18.024 1.00 65.94  ? 447 HOH A O   1 
HETATM 1350 O  O   . HOH F 6 .   ? 34.582 -18.759 36.059 1.00 61.71  ? 448 HOH A O   1 
HETATM 1351 O  O   . HOH F 6 .   ? 47.073 -12.964 28.448 1.00 60.77  ? 449 HOH A O   1 
HETATM 1352 O  O   . HOH F 6 .   ? 12.017 -18.562 22.367 1.00 57.88  ? 450 HOH A O   1 
HETATM 1353 O  O   . HOH F 6 .   ? 32.231 -1.025  22.239 1.00 60.05  ? 451 HOH A O   1 
HETATM 1354 O  O   . HOH F 6 .   ? 47.103 -11.859 25.418 1.00 67.63  ? 452 HOH A O   1 
HETATM 1355 O  O   . HOH F 6 .   ? 13.617 -16.079 39.745 1.00 74.96  ? 453 HOH A O   1 
HETATM 1356 O  O   A HOH F 6 .   ? 12.046 -20.748 27.814 0.78 46.65  ? 454 HOH A O   1 
HETATM 1357 O  O   . HOH F 6 .   ? 32.762 -3.219  9.976  1.00 59.55  ? 455 HOH A O   1 
HETATM 1358 O  O   . HOH F 6 .   ? 19.242 -7.548  35.197 1.00 58.79  ? 456 HOH A O   1 
HETATM 1359 O  O   . HOH F 6 .   ? 43.092 -3.092  33.799 1.00 57.68  ? 457 HOH A O   1 
HETATM 1360 O  O   . HOH F 6 .   ? 17.108 -28.094 9.843  1.00 49.21  ? 458 HOH A O   1 
HETATM 1361 O  O   . HOH F 6 .   ? 15.867 -15.589 41.178 1.00 58.04  ? 459 HOH A O   1 
HETATM 1362 O  O   . HOH F 6 .   ? 25.338 -5.711  35.229 1.00 53.71  ? 460 HOH A O   1 
HETATM 1363 O  O   . HOH F 6 .   ? 44.222 -13.469 13.846 0.50 61.28  ? 461 HOH A O   1 
HETATM 1364 O  O   . HOH F 6 .   ? 17.404 -8.100  24.785 1.00 58.77  ? 462 HOH A O   1 
HETATM 1365 O  O   . HOH F 6 .   ? 33.775 -13.991 41.537 0.50 38.23  ? 463 HOH A O   1 
HETATM 1366 O  O   . HOH F 6 .   ? 32.079 -23.830 34.768 1.00 63.33  ? 464 HOH A O   1 
HETATM 1367 O  O   . HOH F 6 .   ? 28.184 -29.784 24.142 1.00 64.23  ? 465 HOH A O   1 
HETATM 1368 O  O   . HOH F 6 .   ? 18.961 -28.054 13.846 0.50 65.70  ? 466 HOH A O   1 
HETATM 1369 O  O   . HOH F 6 .   ? 45.414 -12.918 16.249 1.00 61.65  ? 467 HOH A O   1 
HETATM 1370 O  O   . HOH F 6 .   ? 23.256 -4.531  17.219 1.00 70.44  ? 468 HOH A O   1 
HETATM 1371 O  O   . HOH F 6 .   ? 32.674 -20.444 37.029 1.00 67.38  ? 469 HOH A O   1 
HETATM 1372 O  O   . HOH F 6 .   ? 21.143 -5.640  34.737 1.00 56.14  ? 470 HOH A O   1 
HETATM 1373 O  O   . HOH F 6 .   ? 34.910 -23.682 32.713 1.00 63.14  ? 471 HOH A O   1 
HETATM 1374 O  O   . HOH F 6 .   ? 16.673 -6.647  34.595 1.00 74.52  ? 472 HOH A O   1 
HETATM 1375 O  O   . HOH F 6 .   ? 32.989 -0.701  42.889 1.00 55.09  ? 473 HOH A O   1 
HETATM 1376 O  O   . HOH G 6 .   ? 12.330 -24.281 -0.064 1.00 47.50  ? 201 HOH D O   1 
HETATM 1377 O  O   . HOH G 6 .   ? 15.020 -25.794 -1.805 1.00 40.21  ? 202 HOH D O   1 
HETATM 1378 O  O   . HOH G 6 .   ? 21.037 -38.262 4.032  1.00 43.51  ? 203 HOH D O   1 
HETATM 1379 O  O   . HOH G 6 .   ? 11.617 -23.567 3.170  1.00 50.53  ? 204 HOH D O   1 
HETATM 1380 O  O   . HOH G 6 .   ? 17.693 -36.343 6.149  1.00 39.95  ? 205 HOH D O   1 
HETATM 1381 O  O   . HOH G 6 .   ? 20.867 -39.501 -2.197 1.00 55.38  ? 206 HOH D O   1 
HETATM 1382 O  O   . HOH G 6 .   ? 18.682 -40.700 0.658  1.00 66.21  ? 207 HOH D O   1 
HETATM 1383 O  O   . HOH G 6 .   ? 10.697 -24.738 5.529  1.00 56.32  ? 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   ? 0.7753 0.9764 0.6960 0.0392  -0.1223 -0.0216 6   ASP A N   
2    C CA  . ASP A 5   ? 0.7695 0.9653 0.6747 0.0229  -0.1140 -0.0245 6   ASP A CA  
3    C C   . ASP A 5   ? 0.7515 0.9777 0.6808 0.0108  -0.1099 -0.0412 6   ASP A C   
4    O O   . ASP A 5   ? 0.7435 0.9968 0.6993 0.0148  -0.1149 -0.0506 6   ASP A O   
5    C CB  . ASP A 5   ? 0.7930 0.9582 0.6889 0.0139  -0.0974 -0.0176 6   ASP A CB  
6    C CG  . ASP A 5   ? 0.9873 1.1332 0.8514 0.0043  -0.0927 -0.0134 6   ASP A CG  
7    O OD1 . ASP A 5   ? 0.9926 1.1518 0.8552 -0.0068 -0.0905 -0.0225 6   ASP A OD1 
8    O OD2 . ASP A 5   ? 1.0902 1.2073 0.9307 0.0065  -0.0898 -0.0018 6   ASP A OD2 
9    N N   . SER A 6   ? 0.6472 0.8684 0.5669 -0.0045 -0.1002 -0.0457 7   SER A N   
10   C CA  . SER A 6   ? 0.6006 0.8431 0.5380 -0.0180 -0.0939 -0.0610 7   SER A CA  
11   C C   . SER A 6   ? 0.5457 0.7719 0.4937 -0.0291 -0.0758 -0.0629 7   SER A C   
12   O O   . SER A 6   ? 0.5430 0.7721 0.4936 -0.0420 -0.0674 -0.0722 7   SER A O   
13   C CB  . SER A 6   ? 0.6766 0.9264 0.5937 -0.0258 -0.0982 -0.0661 7   SER A CB  
14   O OG  . SER A 6   ? 0.8525 1.0749 0.7424 -0.0313 -0.0908 -0.0582 7   SER A OG  
15   N N   . CYS A 7   ? 0.4198 0.6284 0.3736 -0.0233 -0.0706 -0.0544 8   CYS A N   
16   C CA  . CYS A 7   ? 0.3786 0.5712 0.3413 -0.0311 -0.0561 -0.0551 8   CYS A CA  
17   C C   . CYS A 7   ? 0.3702 0.5774 0.3564 -0.0390 -0.0502 -0.0672 8   CYS A C   
18   O O   . CYS A 7   ? 0.3591 0.5889 0.3598 -0.0367 -0.0562 -0.0740 8   CYS A O   
19   C CB  . CYS A 7   ? 0.3935 0.5668 0.3566 -0.0226 -0.0539 -0.0440 8   CYS A CB  
20   S SG  . CYS A 7   ? 0.4753 0.6218 0.4086 -0.0185 -0.0542 -0.0304 8   CYS A SG  
21   N N   . ILE A 8   ? 0.2699 0.4634 0.2593 -0.0482 -0.0384 -0.0705 9   ILE A N   
22   C CA  . ILE A 8   ? 0.2301 0.4263 0.2367 -0.0556 -0.0307 -0.0790 9   ILE A CA  
23   C C   . ILE A 8   ? 0.2602 0.4371 0.2712 -0.0505 -0.0258 -0.0706 9   ILE A C   
24   O O   . ILE A 8   ? 0.2543 0.4156 0.2551 -0.0448 -0.0259 -0.0610 9   ILE A O   
25   C CB  . ILE A 8   ? 0.2719 0.4642 0.2775 -0.0685 -0.0221 -0.0891 9   ILE A CB  
26   C CG1 . ILE A 8   ? 0.2916 0.4613 0.2854 -0.0698 -0.0157 -0.0847 9   ILE A CG1 
27   C CG2 . ILE A 8   ? 0.2860 0.5019 0.2899 -0.0747 -0.0272 -0.0997 9   ILE A CG2 
28   C CD1 . ILE A 8   ? 0.3433 0.5048 0.3375 -0.0805 -0.0064 -0.0946 9   ILE A CD1 
29   N N   A GLN A 9   ? 0.1972 0.3738 0.2214 -0.0538 -0.0206 -0.0747 10  GLN A N   
30   N N   B GLN A 9   ? 0.2039 0.3826 0.2288 -0.0532 -0.0214 -0.0748 10  GLN A N   
31   C CA  A GLN A 9   ? 0.1926 0.3516 0.2193 -0.0494 -0.0166 -0.0672 10  GLN A CA  
32   C CA  B GLN A 9   ? 0.1963 0.3584 0.2247 -0.0492 -0.0172 -0.0679 10  GLN A CA  
33   C C   A GLN A 9   ? 0.2374 0.3812 0.2669 -0.0580 -0.0070 -0.0715 10  GLN A C   
34   C C   B GLN A 9   ? 0.2344 0.3801 0.2642 -0.0581 -0.0075 -0.0720 10  GLN A C   
35   O O   A GLN A 9   ? 0.2337 0.3855 0.2694 -0.0666 -0.0033 -0.0810 10  GLN A O   
36   O O   B GLN A 9   ? 0.2335 0.3854 0.2678 -0.0675 -0.0033 -0.0818 10  GLN A O   
37   C CB  A GLN A 9   ? 0.2016 0.3734 0.2389 -0.0418 -0.0215 -0.0656 10  GLN A CB  
38   C CB  B GLN A 9   ? 0.2033 0.3798 0.2442 -0.0433 -0.0211 -0.0684 10  GLN A CB  
39   C CG  A GLN A 9   ? 0.2175 0.3728 0.2574 -0.0380 -0.0172 -0.0590 10  GLN A CG  
40   C CG  B GLN A 9   ? 0.2649 0.4263 0.3106 -0.0425 -0.0149 -0.0646 10  GLN A CG  
41   C CD  A GLN A 9   ? 0.5415 0.7115 0.5949 -0.0329 -0.0196 -0.0614 10  GLN A CD  
42   C CD  B GLN A 9   ? 0.4082 0.5679 0.4554 -0.0308 -0.0195 -0.0563 10  GLN A CD  
43   O OE1 A GLN A 9   ? 0.4139 0.5990 0.4797 -0.0394 -0.0165 -0.0716 10  GLN A OE1 
44   O OE1 B GLN A 9   ? 0.2646 0.4342 0.3099 -0.0217 -0.0282 -0.0530 10  GLN A OE1 
45   N NE2 A GLN A 9   ? 0.5835 0.7492 0.6352 -0.0217 -0.0243 -0.0531 10  GLN A NE2 
46   N NE2 B GLN A 9   ? 0.2879 0.4327 0.3366 -0.0307 -0.0139 -0.0528 10  GLN A NE2 
47   N N   A PHE A 10  ? 0.2163 0.3376 0.2403 -0.0557 -0.0033 -0.0648 11  PHE A N   
48   N N   B PHE A 10  ? 0.1986 0.3227 0.2238 -0.0549 -0.0041 -0.0646 11  PHE A N   
49   C CA  A PHE A 10  ? 0.2185 0.3214 0.2419 -0.0616 0.0039  -0.0674 11  PHE A CA  
50   C CA  B PHE A 10  ? 0.2003 0.3047 0.2241 -0.0604 0.0031  -0.0664 11  PHE A CA  
51   C C   A PHE A 10  ? 0.2433 0.3413 0.2708 -0.0600 0.0055  -0.0642 11  PHE A C   
52   C C   B PHE A 10  ? 0.2372 0.3378 0.2657 -0.0593 0.0048  -0.0639 11  PHE A C   
53   O O   A PHE A 10  ? 0.2313 0.3212 0.2574 -0.0527 0.0036  -0.0560 11  PHE A O   
54   O O   B PHE A 10  ? 0.2245 0.3202 0.2527 -0.0516 0.0024  -0.0560 11  PHE A O   
55   C CB  A PHE A 10  ? 0.2437 0.3270 0.2600 -0.0595 0.0058  -0.0640 11  PHE A CB  
56   C CB  B PHE A 10  ? 0.2250 0.3112 0.2419 -0.0569 0.0041  -0.0615 11  PHE A CB  
57   C CG  A PHE A 10  ? 0.2629 0.3253 0.2761 -0.0641 0.0114  -0.0670 11  PHE A CG  
58   C CG  B PHE A 10  ? 0.2518 0.3386 0.2648 -0.0615 0.0059  -0.0678 11  PHE A CG  
59   C CD1 A PHE A 10  ? 0.3035 0.3634 0.3147 -0.0730 0.0160  -0.0759 11  PHE A CD1 
60   C CD1 B PHE A 10  ? 0.2929 0.3961 0.3031 -0.0619 0.0024  -0.0697 11  PHE A CD1 
61   C CD2 A PHE A 10  ? 0.2848 0.3281 0.2950 -0.0595 0.0116  -0.0610 11  PHE A CD2 
62   C CD2 B PHE A 10  ? 0.2965 0.3662 0.3073 -0.0651 0.0109  -0.0721 11  PHE A CD2 
63   C CE1 A PHE A 10  ? 0.3283 0.3634 0.3329 -0.0766 0.0210  -0.0779 11  PHE A CE1 
64   C CE1 B PHE A 10  ? 0.3116 0.4154 0.3173 -0.0673 0.0050  -0.0765 11  PHE A CE1 
65   C CE2 A PHE A 10  ? 0.3169 0.3374 0.3205 -0.0624 0.0152  -0.0628 11  PHE A CE2 
66   C CE2 B PHE A 10  ? 0.3399 0.4102 0.3483 -0.0692 0.0134  -0.0792 11  PHE A CE2 
67   C CZ  A PHE A 10  ? 0.3009 0.3156 0.3008 -0.0706 0.0199  -0.0707 11  PHE A CZ  
68   C CZ  B PHE A 10  ? 0.3122 0.4001 0.3183 -0.0710 0.0111  -0.0817 11  PHE A CZ  
69   N N   . THR A 11  ? 0.1965 0.3005 0.2291 -0.0679 0.0099  -0.0717 12  THR A N   
70   C CA  . THR A 11  ? 0.2053 0.3078 0.2423 -0.0690 0.0132  -0.0714 12  THR A CA  
71   C C   . THR A 11  ? 0.2599 0.3365 0.2880 -0.0657 0.0153  -0.0629 12  THR A C   
72   O O   . THR A 11  ? 0.2453 0.3231 0.2765 -0.0603 0.0141  -0.0583 12  THR A O   
73   C CB  . THR A 11  ? 0.2922 0.3990 0.3320 -0.0822 0.0209  -0.0827 12  THR A CB  
74   O OG1 . THR A 11  ? 0.2944 0.4302 0.3451 -0.0845 0.0175  -0.0916 12  THR A OG1 
75   C CG2 . THR A 11  ? 0.3389 0.4449 0.3827 -0.0858 0.0264  -0.0845 12  THR A CG2 
76   N N   A ARG A 12  ? 0.2309 0.2845 0.2481 -0.0683 0.0177  -0.0615 13  ARG A N   
77   N N   B ARG A 12  ? 0.2345 0.2881 0.2517 -0.0683 0.0178  -0.0616 13  ARG A N   
78   C CA  A ARG A 12  ? 0.2436 0.2727 0.2513 -0.0650 0.0182  -0.0546 13  ARG A CA  
79   C CA  B ARG A 12  ? 0.2482 0.2773 0.2559 -0.0650 0.0182  -0.0545 13  ARG A CA  
80   C C   A ARG A 12  ? 0.2728 0.2993 0.2808 -0.0546 0.0123  -0.0469 13  ARG A C   
81   C C   B ARG A 12  ? 0.2728 0.2997 0.2810 -0.0545 0.0123  -0.0468 13  ARG A C   
82   O O   A ARG A 12  ? 0.2650 0.2741 0.2665 -0.0513 0.0114  -0.0421 13  ARG A O   
83   O O   B ARG A 12  ? 0.2631 0.2730 0.2650 -0.0512 0.0114  -0.0419 13  ARG A O   
84   C CB  A ARG A 12  ? 0.2952 0.2987 0.2901 -0.0710 0.0223  -0.0569 13  ARG A CB  
85   C CB  B ARG A 12  ? 0.3102 0.3139 0.3052 -0.0707 0.0221  -0.0567 13  ARG A CB  
86   C CG  A ARG A 12  ? 0.3967 0.3942 0.3860 -0.0839 0.0306  -0.0640 13  ARG A CG  
87   C CG  B ARG A 12  ? 0.4682 0.4598 0.4548 -0.0820 0.0300  -0.0611 13  ARG A CG  
88   C CD  A ARG A 12  ? 0.5430 0.5333 0.5275 -0.0872 0.0345  -0.0618 13  ARG A CD  
89   C CD  B ARG A 12  ? 0.5629 0.5426 0.5418 -0.0918 0.0357  -0.0685 13  ARG A CD  
90   N NE  A ARG A 12  ? 0.6359 0.5959 0.6038 -0.0835 0.0330  -0.0540 13  ARG A NE  
91   N NE  B ARG A 12  ? 0.6100 0.5684 0.5803 -0.0864 0.0326  -0.0659 13  ARG A NE  
92   C CZ  A ARG A 12  ? 0.7324 0.6843 0.6942 -0.0833 0.0339  -0.0497 13  ARG A CZ  
93   C CZ  B ARG A 12  ? 0.7401 0.7020 0.7131 -0.0879 0.0332  -0.0717 13  ARG A CZ  
94   N NH1 A ARG A 12  ? 0.5014 0.4732 0.4740 -0.0860 0.0373  -0.0528 13  ARG A NH1 
95   N NH1 B ARG A 12  ? 0.6534 0.5959 0.6203 -0.0818 0.0306  -0.0703 13  ARG A NH1 
96   N NH2 A ARG A 12  ? 0.6071 0.5316 0.5522 -0.0797 0.0310  -0.0430 13  ARG A NH2 
97   N NH2 B ARG A 12  ? 0.4285 0.4143 0.4110 -0.0953 0.0359  -0.0799 13  ARG A NH2 
98   N N   . HIS A 13  ? 0.2162 0.2592 0.2302 -0.0501 0.0085  -0.0463 14  HIS A N   
99   C CA  . HIS A 13  ? 0.2070 0.2475 0.2203 -0.0427 0.0049  -0.0406 14  HIS A CA  
100  C C   . HIS A 13  ? 0.2437 0.2781 0.2566 -0.0378 0.0038  -0.0341 14  HIS A C   
101  O O   . HIS A 13  ? 0.2336 0.2561 0.2436 -0.0348 0.0027  -0.0313 14  HIS A O   
102  C CB  . HIS A 13  ? 0.2002 0.2569 0.2155 -0.0404 0.0020  -0.0407 14  HIS A CB  
103  C CG  . HIS A 13  ? 0.2212 0.2732 0.2341 -0.0356 0.0007  -0.0362 14  HIS A CG  
104  N ND1 . HIS A 13  ? 0.2319 0.2762 0.2442 -0.0361 0.0021  -0.0389 14  HIS A ND1 
105  C CD2 . HIS A 13  ? 0.2342 0.2878 0.2452 -0.0310 -0.0010 -0.0303 14  HIS A CD2 
106  C CE1 . HIS A 13  ? 0.2228 0.2670 0.2343 -0.0330 0.0018  -0.0357 14  HIS A CE1 
107  N NE2 . HIS A 13  ? 0.2216 0.2695 0.2308 -0.0304 0.0003  -0.0299 14  HIS A NE2 
108  N N   . ALA A 14  ? 0.1983 0.2421 0.2152 -0.0366 0.0037  -0.0328 15  ALA A N   
109  C CA  . ALA A 14  ? 0.2072 0.2450 0.2235 -0.0324 0.0035  -0.0275 15  ALA A CA  
110  C C   . ALA A 14  ? 0.2470 0.2670 0.2568 -0.0353 0.0059  -0.0268 15  ALA A C   
111  O O   . ALA A 14  ? 0.2290 0.2398 0.2357 -0.0319 0.0044  -0.0228 15  ALA A O   
112  C CB  . ALA A 14  ? 0.2123 0.2633 0.2354 -0.0300 0.0035  -0.0280 15  ALA A CB  
113  N N   A SER A 15  ? 0.2185 0.2327 0.2246 -0.0421 0.0095  -0.0310 16  SER A N   
114  N N   B SER A 15  ? 0.2226 0.2367 0.2286 -0.0421 0.0095  -0.0310 16  SER A N   
115  N N   C SER A 15  ? 0.2183 0.2323 0.2243 -0.0421 0.0095  -0.0310 16  SER A N   
116  C CA  A SER A 15  ? 0.2288 0.2219 0.2234 -0.0454 0.0114  -0.0297 16  SER A CA  
117  C CA  B SER A 15  ? 0.2355 0.2284 0.2300 -0.0456 0.0115  -0.0298 16  SER A CA  
118  C CA  C SER A 15  ? 0.2289 0.2217 0.2233 -0.0455 0.0114  -0.0297 16  SER A CA  
119  C C   A SER A 15  ? 0.2901 0.2682 0.2782 -0.0414 0.0070  -0.0274 16  SER A C   
120  C C   B SER A 15  ? 0.2951 0.2730 0.2831 -0.0416 0.0070  -0.0274 16  SER A C   
121  C C   C SER A 15  ? 0.2937 0.2714 0.2815 -0.0416 0.0071  -0.0274 16  SER A C   
122  O O   A SER A 15  ? 0.2682 0.2327 0.2490 -0.0389 0.0045  -0.0238 16  SER A O   
123  O O   B SER A 15  ? 0.2777 0.2418 0.2582 -0.0390 0.0046  -0.0239 16  SER A O   
124  O O   C SER A 15  ? 0.2793 0.2429 0.2595 -0.0391 0.0046  -0.0239 16  SER A O   
125  C CB  A SER A 15  ? 0.2714 0.2588 0.2603 -0.0553 0.0175  -0.0352 16  SER A CB  
126  C CB  B SER A 15  ? 0.2855 0.2727 0.2743 -0.0554 0.0175  -0.0354 16  SER A CB  
127  C CB  C SER A 15  ? 0.2718 0.2590 0.2605 -0.0553 0.0177  -0.0350 16  SER A CB  
128  O OG  A SER A 15  ? 0.2988 0.2608 0.2711 -0.0587 0.0191  -0.0328 16  SER A OG  
129  O OG  B SER A 15  ? 0.3299 0.3343 0.3278 -0.0592 0.0218  -0.0398 16  SER A OG  
130  O OG  C SER A 15  ? 0.3029 0.2886 0.2904 -0.0590 0.0184  -0.0393 16  SER A OG  
131  N N   . ASP A 16  ? 0.2647 0.2468 0.2563 -0.0406 0.0057  -0.0304 17  ASP A N   
132  C CA  . ASP A 16  ? 0.2751 0.2465 0.2646 -0.0357 0.0016  -0.0305 17  ASP A CA  
133  C C   . ASP A 16  ? 0.2700 0.2484 0.2660 -0.0291 -0.0023 -0.0276 17  ASP A C   
134  O O   . ASP A 16  ? 0.2701 0.2385 0.2639 -0.0246 -0.0065 -0.0269 17  ASP A O   
135  C CB  . ASP A 16  ? 0.2930 0.2702 0.2869 -0.0370 0.0026  -0.0360 17  ASP A CB  
136  C CG  . ASP A 16  ? 0.4015 0.3667 0.3873 -0.0440 0.0067  -0.0402 17  ASP A CG  
137  O OD1 . ASP A 16  ? 0.4040 0.3531 0.3787 -0.0482 0.0089  -0.0386 17  ASP A OD1 
138  O OD2 . ASP A 16  ? 0.4064 0.3773 0.3956 -0.0465 0.0085  -0.0457 17  ASP A OD2 
139  N N   . VAL A 17  ? 0.2010 0.1957 0.2042 -0.0286 -0.0010 -0.0264 18  VAL A N   
140  C CA  . VAL A 17  ? 0.1972 0.1965 0.2044 -0.0246 -0.0027 -0.0240 18  VAL A CA  
141  C C   . VAL A 17  ? 0.2425 0.2316 0.2449 -0.0234 -0.0041 -0.0207 18  VAL A C   
142  O O   . VAL A 17  ? 0.2228 0.2086 0.2263 -0.0204 -0.0073 -0.0210 18  VAL A O   
143  C CB  . VAL A 17  ? 0.2227 0.2353 0.2331 -0.0246 -0.0008 -0.0220 18  VAL A CB  
144  C CG1 . VAL A 17  ? 0.2181 0.2301 0.2290 -0.0223 -0.0006 -0.0190 18  VAL A CG1 
145  C CG2 . VAL A 17  ? 0.2146 0.2365 0.2271 -0.0258 -0.0002 -0.0254 18  VAL A CG2 
146  N N   . LEU A 18  ? 0.2210 0.2069 0.2189 -0.0264 -0.0015 -0.0188 19  LEU A N   
147  C CA  . LEU A 18  ? 0.2329 0.2093 0.2246 -0.0266 -0.0018 -0.0162 19  LEU A CA  
148  C C   . LEU A 18  ? 0.2780 0.2373 0.2596 -0.0259 -0.0061 -0.0162 19  LEU A C   
149  O O   . LEU A 18  ? 0.2552 0.2095 0.2340 -0.0234 -0.0098 -0.0150 19  LEU A O   
150  C CB  . LEU A 18  ? 0.2436 0.2212 0.2334 -0.0307 0.0032  -0.0159 19  LEU A CB  
151  C CG  . LEU A 18  ? 0.2918 0.2621 0.2763 -0.0314 0.0046  -0.0140 19  LEU A CG  
152  C CD1 . LEU A 18  ? 0.2816 0.2591 0.2728 -0.0273 0.0042  -0.0121 19  LEU A CD1 
153  C CD2 . LEU A 18  ? 0.3446 0.3159 0.3277 -0.0365 0.0108  -0.0160 19  LEU A CD2 
154  N N   . LEU A 19  ? 0.2621 0.2120 0.2377 -0.0277 -0.0061 -0.0178 20  LEU A N   
155  C CA  . LEU A 19  ? 0.2890 0.2183 0.2520 -0.0255 -0.0113 -0.0172 20  LEU A CA  
156  C C   . LEU A 19  ? 0.2974 0.2313 0.2688 -0.0171 -0.0187 -0.0189 20  LEU A C   
157  O O   . LEU A 19  ? 0.2845 0.2087 0.2493 -0.0129 -0.0252 -0.0177 20  LEU A O   
158  C CB  . LEU A 19  ? 0.3221 0.2404 0.2783 -0.0290 -0.0088 -0.0195 20  LEU A CB  
159  C CG  . LEU A 19  ? 0.4524 0.3437 0.3920 -0.0259 -0.0141 -0.0183 20  LEU A CG  
160  C CD1 . LEU A 19  ? 0.5020 0.3722 0.4202 -0.0305 -0.0135 -0.0139 20  LEU A CD1 
161  C CD2 . LEU A 19  ? 0.5229 0.4040 0.4579 -0.0294 -0.0105 -0.0215 20  LEU A CD2 
162  N N   . ASN A 20  ? 0.2405 0.1910 0.2266 -0.0152 -0.0176 -0.0226 21  ASN A N   
163  C CA  . ASN A 20  ? 0.2268 0.1857 0.2241 -0.0088 -0.0226 -0.0266 21  ASN A CA  
164  C C   . ASN A 20  ? 0.2519 0.2197 0.2541 -0.0082 -0.0238 -0.0260 21  ASN A C   
165  O O   . ASN A 20  ? 0.2481 0.2175 0.2549 -0.0031 -0.0302 -0.0293 21  ASN A O   
166  C CB  . ASN A 20  ? 0.2342 0.2074 0.2437 -0.0090 -0.0192 -0.0317 21  ASN A CB  
167  C CG  . ASN A 20  ? 0.3768 0.3396 0.3832 -0.0074 -0.0202 -0.0348 21  ASN A CG  
168  O OD1 . ASN A 20  ? 0.3351 0.2790 0.3315 -0.0036 -0.0252 -0.0337 21  ASN A OD1 
169  N ND2 . ASN A 20  ? 0.2780 0.2506 0.2905 -0.0104 -0.0154 -0.0386 21  ASN A ND2 
170  N N   . LEU A 21  ? 0.2288 0.2026 0.2306 -0.0132 -0.0180 -0.0228 22  LEU A N   
171  C CA  . LEU A 21  ? 0.2250 0.2037 0.2291 -0.0139 -0.0178 -0.0223 22  LEU A CA  
172  C C   . LEU A 21  ? 0.2547 0.2202 0.2480 -0.0125 -0.0234 -0.0208 22  LEU A C   
173  O O   . LEU A 21  ? 0.2285 0.1979 0.2251 -0.0107 -0.0275 -0.0234 22  LEU A O   
174  C CB  . LEU A 21  ? 0.2184 0.2011 0.2216 -0.0182 -0.0106 -0.0187 22  LEU A CB  
175  C CG  . LEU A 21  ? 0.2352 0.2294 0.2454 -0.0191 -0.0063 -0.0195 22  LEU A CG  
176  C CD1 . LEU A 21  ? 0.2404 0.2357 0.2477 -0.0208 -0.0015 -0.0151 22  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.2746 0.2778 0.2932 -0.0191 -0.0060 -0.0242 22  LEU A CD2 
178  N N   . ASN A 22  ? 0.2377 0.1876 0.2167 -0.0145 -0.0232 -0.0171 23  ASN A N   
179  C CA  . ASN A 22  ? 0.2628 0.1964 0.2263 -0.0141 -0.0285 -0.0150 23  ASN A CA  
180  C C   . ASN A 22  ? 0.3242 0.2518 0.2864 -0.0059 -0.0396 -0.0174 23  ASN A C   
181  O O   . ASN A 22  ? 0.3244 0.2481 0.2809 -0.0031 -0.0469 -0.0178 23  ASN A O   
182  C CB  . ASN A 22  ? 0.3026 0.2192 0.2490 -0.0200 -0.0239 -0.0113 23  ASN A CB  
183  C CG  . ASN A 22  ? 0.3939 0.2936 0.3211 -0.0222 -0.0268 -0.0087 23  ASN A CG  
184  O OD1 . ASN A 22  ? 0.3623 0.2675 0.2912 -0.0221 -0.0286 -0.0094 23  ASN A OD1 
185  N ND2 . ASN A 22  ? 0.4233 0.3009 0.3302 -0.0253 -0.0269 -0.0061 23  ASN A ND2 
186  N N   . ARG A 23  ? 0.2855 0.2133 0.2538 -0.0015 -0.0415 -0.0199 24  ARG A N   
187  C CA  . ARG A 23  ? 0.2889 0.2129 0.2598 0.0085  -0.0525 -0.0236 24  ARG A CA  
188  C C   . ARG A 23  ? 0.3202 0.2667 0.3103 0.0124  -0.0566 -0.0303 24  ARG A C   
189  O O   . ARG A 23  ? 0.3222 0.2672 0.3119 0.0197  -0.0675 -0.0330 24  ARG A O   
190  C CB  . ARG A 23  ? 0.2909 0.2130 0.2678 0.0119  -0.0515 -0.0266 24  ARG A CB  
191  C CG  . ARG A 23  ? 0.3809 0.2764 0.3367 0.0091  -0.0496 -0.0216 24  ARG A CG  
192  C CD  . ARG A 23  ? 0.4191 0.3167 0.3825 0.0085  -0.0446 -0.0253 24  ARG A CD  
193  N NE  . ARG A 23  ? 0.5305 0.4009 0.4731 0.0048  -0.0421 -0.0219 24  ARG A NE  
194  C CZ  . ARG A 23  ? 0.7774 0.6445 0.7214 0.0018  -0.0365 -0.0249 24  ARG A CZ  
195  N NH1 . ARG A 23  ? 0.5793 0.4692 0.5437 0.0020  -0.0329 -0.0308 24  ARG A NH1 
196  N NH2 . ARG A 23  ? 0.6459 0.4856 0.5690 -0.0029 -0.0336 -0.0224 24  ARG A NH2 
197  N N   . LEU A 24  ? 0.2659 0.2326 0.2717 0.0071  -0.0480 -0.0334 25  LEU A N   
198  C CA  . LEU A 24  ? 0.2455 0.2328 0.2681 0.0075  -0.0490 -0.0406 25  LEU A CA  
199  C C   . LEU A 24  ? 0.3062 0.2905 0.3206 0.0053  -0.0525 -0.0390 25  LEU A C   
200  O O   . LEU A 24  ? 0.3071 0.3013 0.3297 0.0095  -0.0604 -0.0455 25  LEU A O   
201  C CB  . LEU A 24  ? 0.2323 0.2348 0.2660 0.0002  -0.0377 -0.0425 25  LEU A CB  
202  C CG  . LEU A 24  ? 0.2822 0.2911 0.3245 0.0008  -0.0334 -0.0457 25  LEU A CG  
203  C CD1 . LEU A 24  ? 0.2718 0.2927 0.3197 -0.0071 -0.0227 -0.0464 25  LEU A CD1 
204  C CD2 . LEU A 24  ? 0.3014 0.3198 0.3586 0.0087  -0.0402 -0.0554 25  LEU A CD2 
205  N N   . ARG A 25  ? 0.2643 0.2363 0.2636 -0.0013 -0.0466 -0.0316 26  ARG A N   
206  C CA  . ARG A 25  ? 0.2804 0.2477 0.2698 -0.0042 -0.0488 -0.0305 26  ARG A CA  
207  C C   . ARG A 25  ? 0.3490 0.3045 0.3262 0.0029  -0.0626 -0.0307 26  ARG A C   
208  O O   . ARG A 25  ? 0.3409 0.3044 0.3208 0.0042  -0.0694 -0.0354 26  ARG A O   
209  C CB  . ARG A 25  ? 0.2971 0.2522 0.2724 -0.0117 -0.0399 -0.0237 26  ARG A CB  
210  C CG  . ARG A 25  ? 0.3687 0.3187 0.3334 -0.0156 -0.0411 -0.0237 26  ARG A CG  
211  C CD  . ARG A 25  ? 0.3818 0.3228 0.3366 -0.0228 -0.0310 -0.0192 26  ARG A CD  
212  N NE  . ARG A 25  ? 0.3763 0.3005 0.3154 -0.0239 -0.0300 -0.0143 26  ARG A NE  
213  C CZ  . ARG A 25  ? 0.5498 0.4579 0.4692 -0.0287 -0.0289 -0.0119 26  ARG A CZ  
214  N NH1 . ARG A 25  ? 0.4731 0.3795 0.3854 -0.0317 -0.0302 -0.0136 26  ARG A NH1 
215  N NH2 . ARG A 25  ? 0.4348 0.3279 0.3404 -0.0317 -0.0257 -0.0085 26  ARG A NH2 
216  N N   A SER A 26  ? 0.3352 0.2707 0.2973 0.0070  -0.0668 -0.0257 27  SER A N   
217  N N   B SER A 26  ? 0.3334 0.2689 0.2955 0.0070  -0.0668 -0.0257 27  SER A N   
218  N N   C SER A 26  ? 0.3294 0.2650 0.2917 0.0071  -0.0668 -0.0257 27  SER A N   
219  C CA  A SER A 26  ? 0.3680 0.2854 0.3126 0.0147  -0.0804 -0.0239 27  SER A CA  
220  C CA  B SER A 26  ? 0.3652 0.2823 0.3095 0.0147  -0.0804 -0.0239 27  SER A CA  
221  C CA  C SER A 26  ? 0.3593 0.2759 0.3035 0.0148  -0.0803 -0.0237 27  SER A CA  
222  C C   A SER A 26  ? 0.4156 0.3497 0.3776 0.0257  -0.0932 -0.0325 27  SER A C   
223  C C   B SER A 26  ? 0.4198 0.3519 0.3806 0.0263  -0.0937 -0.0321 27  SER A C   
224  C C   C SER A 26  ? 0.4165 0.3478 0.3769 0.0264  -0.0937 -0.0319 27  SER A C   
225  O O   A SER A 26  ? 0.4271 0.3590 0.3814 0.0304  -0.1050 -0.0341 27  SER A O   
226  O O   B SER A 26  ? 0.4388 0.3647 0.3893 0.0326  -0.1068 -0.0328 27  SER A O   
227  O O   C SER A 26  ? 0.4347 0.3586 0.3839 0.0329  -0.1069 -0.0322 27  SER A O   
228  C CB  A SER A 26  ? 0.4349 0.3278 0.3633 0.0174  -0.0810 -0.0184 27  SER A CB  
229  C CB  B SER A 26  ? 0.4280 0.3182 0.3525 0.0158  -0.0801 -0.0173 27  SER A CB  
230  C CB  C SER A 26  ? 0.4173 0.3084 0.3436 0.0160  -0.0796 -0.0176 27  SER A CB  
231  O OG  A SER A 26  ? 0.5492 0.4259 0.4597 0.0069  -0.0703 -0.0119 27  SER A OG  
232  O OG  B SER A 26  ? 0.5069 0.4020 0.4455 0.0219  -0.0804 -0.0205 27  SER A OG  
233  O OG  C SER A 26  ? 0.5289 0.3957 0.4329 0.0238  -0.0927 -0.0143 27  SER A OG  
234  N N   . ARG A 27  ? 0.3539 0.3067 0.3403 0.0291  -0.0905 -0.0392 28  ARG A N   
235  C CA  . ARG A 27  ? 0.3658 0.3384 0.3740 0.0396  -0.1010 -0.0499 28  ARG A CA  
236  C C   . ARG A 27  ? 0.3786 0.3812 0.4086 0.0339  -0.0973 -0.0595 28  ARG A C   
237  O O   . ARG A 27  ? 0.3809 0.4057 0.4330 0.0405  -0.1041 -0.0710 28  ARG A O   
238  C CB  . ARG A 27  ? 0.3928 0.3683 0.4144 0.0455  -0.0991 -0.0536 28  ARG A CB  
239  C CG  . ARG A 27  ? 0.5442 0.4873 0.5425 0.0502  -0.1023 -0.0449 28  ARG A CG  
240  C CD  . ARG A 27  ? 0.6391 0.5842 0.6497 0.0536  -0.0978 -0.0488 28  ARG A CD  
241  N NE  . ARG A 27  ? 0.8439 0.8034 0.8755 0.0672  -0.1085 -0.0597 28  ARG A NE  
242  C CZ  . ARG A 27  ? 1.0273 1.0075 1.0839 0.0685  -0.1030 -0.0696 28  ARG A CZ  
243  N NH1 . ARG A 27  ? 0.8879 0.8826 0.9653 0.0815  -0.1129 -0.0812 28  ARG A NH1 
244  N NH2 . ARG A 27  ? 0.8475 0.8346 0.9083 0.0569  -0.0878 -0.0687 28  ARG A NH2 
245  N N   . ASP A 28  ? 0.3096 0.3122 0.3332 0.0217  -0.0863 -0.0556 29  ASP A N   
246  C CA  . ASP A 28  ? 0.3073 0.3319 0.3460 0.0134  -0.0800 -0.0633 29  ASP A CA  
247  C C   . ASP A 28  ? 0.3503 0.3980 0.4146 0.0112  -0.0718 -0.0726 29  ASP A C   
248  O O   . ASP A 28  ? 0.3464 0.4172 0.4296 0.0089  -0.0718 -0.0843 29  ASP A O   
249  C CB  . ASP A 28  ? 0.3400 0.3741 0.3803 0.0170  -0.0927 -0.0704 29  ASP A CB  
250  C CG  . ASP A 28  ? 0.4323 0.4817 0.4802 0.0055  -0.0847 -0.0765 29  ASP A CG  
251  O OD1 . ASP A 28  ? 0.4252 0.4651 0.4640 -0.0048 -0.0713 -0.0702 29  ASP A OD1 
252  O OD2 . ASP A 28  ? 0.4787 0.5496 0.5420 0.0069  -0.0919 -0.0884 29  ASP A OD2 
253  N N   . ILE A 29  ? 0.2781 0.3194 0.3420 0.0110  -0.0647 -0.0683 30  ILE A N   
254  C CA  . ILE A 29  ? 0.2520 0.3115 0.3354 0.0080  -0.0561 -0.0762 30  ILE A CA  
255  C C   . ILE A 29  ? 0.2840 0.3438 0.3638 -0.0047 -0.0410 -0.0727 30  ILE A C   
256  O O   . ILE A 29  ? 0.2527 0.2959 0.3165 -0.0078 -0.0357 -0.0619 30  ILE A O   
257  C CB  . ILE A 29  ? 0.2888 0.3424 0.3741 0.0151  -0.0575 -0.0753 30  ILE A CB  
258  C CG1 . ILE A 29  ? 0.3097 0.3624 0.4004 0.0297  -0.0733 -0.0804 30  ILE A CG1 
259  C CG2 . ILE A 29  ? 0.2599 0.3304 0.3615 0.0094  -0.0462 -0.0828 30  ILE A CG2 
260  C CD1 . ILE A 29  ? 0.3258 0.3615 0.4096 0.0367  -0.0751 -0.0763 30  ILE A CD1 
261  N N   A LEU A 30  ? 0.2493 0.3277 0.3436 -0.0121 -0.0340 -0.0825 31  LEU A N   
262  N N   B LEU A 30  ? 0.2569 0.3354 0.3513 -0.0120 -0.0341 -0.0825 31  LEU A N   
263  C CA  A LEU A 30  ? 0.2482 0.3250 0.3378 -0.0241 -0.0194 -0.0802 31  LEU A CA  
264  C CA  B LEU A 30  ? 0.2599 0.3373 0.3500 -0.0241 -0.0196 -0.0806 31  LEU A CA  
265  C C   A LEU A 30  ? 0.2807 0.3411 0.3527 -0.0291 -0.0160 -0.0708 31  LEU A C   
266  C C   B LEU A 30  ? 0.2889 0.3494 0.3611 -0.0291 -0.0160 -0.0710 31  LEU A C   
267  O O   A LEU A 30  ? 0.2574 0.3094 0.3208 -0.0363 -0.0053 -0.0657 31  LEU A O   
268  O O   B LEU A 30  ? 0.2690 0.3213 0.3327 -0.0362 -0.0053 -0.0658 31  LEU A O   
269  C CB  A LEU A 30  ? 0.2498 0.3222 0.3362 -0.0258 -0.0115 -0.0760 31  LEU A CB  
270  C CB  B LEU A 30  ? 0.2651 0.3392 0.3529 -0.0261 -0.0113 -0.0771 31  LEU A CB  
271  C CG  A LEU A 30  ? 0.3054 0.3956 0.4095 -0.0254 -0.0091 -0.0874 31  LEU A CG  
272  C CG  B LEU A 30  ? 0.3283 0.4212 0.4321 -0.0320 -0.0036 -0.0894 31  LEU A CG  
273  C CD1 A LEU A 30  ? 0.2878 0.3737 0.3844 -0.0328 0.0028  -0.0841 31  LEU A CD1 
274  C CD1 B LEU A 30  ? 0.3290 0.4313 0.4458 -0.0238 -0.0086 -0.0958 31  LEU A CD1 
275  C CD2 A LEU A 30  ? 0.3296 0.4425 0.4532 -0.0300 -0.0073 -0.1028 31  LEU A CD2 
276  C CD2 B LEU A 30  ? 0.3567 0.4417 0.4488 -0.0428 0.0104  -0.0848 31  LEU A CD2 
277  N N   . THR A 31  ? 0.2507 0.3060 0.3168 -0.0255 -0.0250 -0.0695 32  THR A N   
278  C CA  . THR A 31  ? 0.2520 0.2934 0.3030 -0.0308 -0.0212 -0.0631 32  THR A CA  
279  C C   . THR A 31  ? 0.3108 0.3629 0.3696 -0.0412 -0.0126 -0.0717 32  THR A C   
280  O O   . THR A 31  ? 0.3026 0.3746 0.3782 -0.0425 -0.0147 -0.0840 32  THR A O   
281  C CB  . THR A 31  ? 0.3289 0.3634 0.3706 -0.0258 -0.0327 -0.0615 32  THR A CB  
282  O OG1 . THR A 31  ? 0.3354 0.3875 0.3911 -0.0215 -0.0428 -0.0724 32  THR A OG1 
283  C CG2 . THR A 31  ? 0.3117 0.3296 0.3402 -0.0183 -0.0385 -0.0520 32  THR A CG2 
284  N N   . ASP A 32  ? 0.2739 0.3128 0.3214 -0.0485 -0.0019 -0.0662 33  ASP A N   
285  C CA  . ASP A 32  ? 0.2714 0.3143 0.3222 -0.0598 0.0088  -0.0733 33  ASP A CA  
286  C C   . ASP A 32  ? 0.3056 0.3358 0.3450 -0.0659 0.0135  -0.0715 33  ASP A C   
287  O O   . ASP A 32  ? 0.3017 0.3280 0.3388 -0.0761 0.0245  -0.0754 33  ASP A O   
288  C CB  . ASP A 32  ? 0.2862 0.3229 0.3333 -0.0641 0.0201  -0.0696 33  ASP A CB  
289  C CG  . ASP A 32  ? 0.3873 0.4044 0.4190 -0.0591 0.0219  -0.0556 33  ASP A CG  
290  O OD1 . ASP A 32  ? 0.3438 0.3509 0.3675 -0.0546 0.0175  -0.0494 33  ASP A OD1 
291  O OD2 . ASP A 32  ? 0.4865 0.4995 0.5142 -0.0598 0.0274  -0.0518 33  ASP A OD2 
292  N N   . VAL A 33  ? 0.2603 0.2819 0.2906 -0.0607 0.0061  -0.0662 34  VAL A N   
293  C CA  . VAL A 33  ? 0.2613 0.2712 0.2807 -0.0665 0.0104  -0.0658 34  VAL A CA  
294  C C   . VAL A 33  ? 0.3099 0.3184 0.3227 -0.0617 -0.0009 -0.0649 34  VAL A C   
295  O O   . VAL A 33  ? 0.3116 0.3186 0.3219 -0.0530 -0.0098 -0.0597 34  VAL A O   
296  C CB  . VAL A 33  ? 0.3036 0.2916 0.3098 -0.0674 0.0211  -0.0557 34  VAL A CB  
297  C CG1 . VAL A 33  ? 0.2883 0.2671 0.2871 -0.0584 0.0165  -0.0456 34  VAL A CG1 
298  C CG2 . VAL A 33  ? 0.3148 0.2905 0.3123 -0.0754 0.0293  -0.0581 34  VAL A CG2 
299  N N   A VAL A 34  ? 0.2831 0.2896 0.2905 -0.0683 0.0003  -0.0701 35  VAL A N   
300  N N   B VAL A 34  ? 0.2817 0.2884 0.2891 -0.0682 0.0001  -0.0702 35  VAL A N   
301  C CA  A VAL A 34  ? 0.2842 0.2854 0.2797 -0.0663 -0.0085 -0.0693 35  VAL A CA  
302  C CA  B VAL A 34  ? 0.2826 0.2834 0.2779 -0.0657 -0.0088 -0.0688 35  VAL A CA  
303  C C   A VAL A 34  ? 0.3294 0.3109 0.3107 -0.0716 0.0022  -0.0645 35  VAL A C   
304  C C   B VAL A 34  ? 0.3319 0.3140 0.3130 -0.0716 0.0015  -0.0648 35  VAL A C   
305  O O   A VAL A 34  ? 0.3351 0.3127 0.3173 -0.0796 0.0131  -0.0683 35  VAL A O   
306  O O   B VAL A 34  ? 0.3398 0.3189 0.3220 -0.0800 0.0119  -0.0694 35  VAL A O   
307  C CB  A VAL A 34  ? 0.3383 0.3563 0.3397 -0.0698 -0.0173 -0.0815 35  VAL A CB  
308  C CB  B VAL A 34  ? 0.3358 0.3537 0.3365 -0.0658 -0.0214 -0.0793 35  VAL A CB  
309  C CG1 A VAL A 34  ? 0.3479 0.3572 0.3318 -0.0685 -0.0265 -0.0798 35  VAL A CG1 
310  C CG1 B VAL A 34  ? 0.3387 0.3668 0.3464 -0.0775 -0.0147 -0.0912 35  VAL A CG1 
311  C CG2 A VAL A 34  ? 0.3325 0.3727 0.3519 -0.0632 -0.0279 -0.0882 35  VAL A CG2 
312  C CG2 B VAL A 34  ? 0.3475 0.3547 0.3299 -0.0617 -0.0322 -0.0752 35  VAL A CG2 
313  N N   . ILE A 35  ? 0.2869 0.2552 0.2549 -0.0674 0.0000  -0.0569 36  ILE A N   
314  C CA  . ILE A 35  ? 0.2876 0.2394 0.2436 -0.0716 0.0094  -0.0541 36  ILE A CA  
315  C C   . ILE A 35  ? 0.3591 0.3087 0.3020 -0.0758 0.0033  -0.0587 36  ILE A C   
316  O O   . ILE A 35  ? 0.3536 0.3027 0.2876 -0.0714 -0.0079 -0.0563 36  ILE A O   
317  C CB  . ILE A 35  ? 0.3087 0.2494 0.2599 -0.0659 0.0130  -0.0448 36  ILE A CB  
318  C CG1 . ILE A 35  ? 0.2975 0.2423 0.2602 -0.0606 0.0161  -0.0401 36  ILE A CG1 
319  C CG2 . ILE A 35  ? 0.3380 0.2646 0.2805 -0.0698 0.0234  -0.0445 36  ILE A CG2 
320  C CD1 . ILE A 35  ? 0.3073 0.2502 0.2762 -0.0645 0.0261  -0.0421 36  ILE A CD1 
321  N N   . VAL A 36  ? 0.3251 0.2713 0.2647 -0.0846 0.0105  -0.0653 37  VAL A N   
322  C CA  . VAL A 36  ? 0.3390 0.2833 0.2647 -0.0904 0.0056  -0.0710 37  VAL A CA  
323  C C   . VAL A 36  ? 0.4069 0.3323 0.3173 -0.0937 0.0151  -0.0679 37  VAL A C   
324  O O   . VAL A 36  ? 0.3975 0.3141 0.3112 -0.0967 0.0284  -0.0684 37  VAL A O   
325  C CB  . VAL A 36  ? 0.3900 0.3458 0.3225 -0.0996 0.0069  -0.0831 37  VAL A CB  
326  C CG1 . VAL A 36  ? 0.4043 0.3591 0.3212 -0.1059 0.0010  -0.0897 37  VAL A CG1 
327  C CG2 . VAL A 36  ? 0.3858 0.3639 0.3365 -0.0967 -0.0017 -0.0885 37  VAL A CG2 
328  N N   . VAL A 37  ? 0.3764 0.2947 0.2691 -0.0934 0.0083  -0.0654 38  VAL A N   
329  C CA  . VAL A 37  ? 0.3867 0.2886 0.2640 -0.0976 0.0173  -0.0638 38  VAL A CA  
330  C C   . VAL A 37  ? 0.4611 0.3590 0.3173 -0.1046 0.0105  -0.0690 38  VAL A C   
331  O O   . VAL A 37  ? 0.4437 0.3395 0.2857 -0.1015 -0.0022 -0.0655 38  VAL A O   
332  C CB  . VAL A 37  ? 0.4309 0.3259 0.3049 -0.0913 0.0176  -0.0550 38  VAL A CB  
333  C CG1 . VAL A 37  ? 0.4400 0.3218 0.3044 -0.0962 0.0303  -0.0556 38  VAL A CG1 
334  C CG2 . VAL A 37  ? 0.4046 0.3078 0.2991 -0.0831 0.0192  -0.0500 38  VAL A CG2 
335  N N   A SER A 38  ? 0.4642 0.3559 0.3132 -0.1143 0.0198  -0.0764 39  SER A N   
336  N N   B SER A 38  ? 0.4194 0.3201 0.2776 -0.1129 0.0160  -0.0782 39  SER A N   
337  C CA  A SER A 38  ? 0.4939 0.3808 0.3197 -0.1224 0.0141  -0.0819 39  SER A CA  
338  C CA  B SER A 38  ? 0.4285 0.3297 0.2711 -0.1218 0.0112  -0.0867 39  SER A CA  
339  C C   A SER A 38  ? 0.5526 0.4514 0.3734 -0.1182 -0.0066 -0.0826 39  SER A C   
340  C C   B SER A 38  ? 0.4609 0.3775 0.3035 -0.1174 -0.0084 -0.0885 39  SER A C   
341  O O   A SER A 38  ? 0.5615 0.4511 0.3585 -0.1176 -0.0170 -0.0792 39  SER A O   
342  O O   B SER A 38  ? 0.4236 0.3576 0.2871 -0.1153 -0.0115 -0.0930 39  SER A O   
343  C CB  A SER A 38  ? 0.5716 0.4402 0.3745 -0.1259 0.0196  -0.0783 39  SER A CB  
344  C CB  B SER A 38  ? 0.4987 0.3819 0.3160 -0.1282 0.0166  -0.0862 39  SER A CB  
345  O OG  A SER A 38  ? 0.7149 0.5749 0.5220 -0.1308 0.0379  -0.0816 39  SER A OG  
346  O OG  B SER A 38  ? 0.5708 0.4445 0.3943 -0.1319 0.0351  -0.0883 39  SER A OG  
347  N N   A ARG A 39  ? 0.4976 0.4159 0.3408 -0.1148 -0.0122 -0.0869 40  ARG A N   
348  N N   B ARG A 39  ? 0.4408 0.3506 0.2606 -0.1152 -0.0217 -0.0851 40  ARG A N   
349  C CA  A ARG A 39  ? 0.4988 0.4344 0.3461 -0.1089 -0.0314 -0.0900 40  ARG A CA  
350  C CA  B ARG A 39  ? 0.4482 0.3725 0.2690 -0.1082 -0.0422 -0.0870 40  ARG A CA  
351  C C   A ARG A 39  ? 0.5305 0.4617 0.3718 -0.0964 -0.0448 -0.0797 40  ARG A C   
352  C C   B ARG A 39  ? 0.4970 0.4286 0.3352 -0.0952 -0.0490 -0.0797 40  ARG A C   
353  O O   A ARG A 39  ? 0.5447 0.4801 0.3762 -0.0906 -0.0631 -0.0803 40  ARG A O   
354  O O   B ARG A 39  ? 0.4875 0.4406 0.3485 -0.0906 -0.0557 -0.0852 40  ARG A O   
355  C CB  A ARG A 39  ? 0.5209 0.4611 0.3520 -0.1160 -0.0413 -0.0994 40  ARG A CB  
356  C CB  B ARG A 39  ? 0.4797 0.3919 0.2669 -0.1096 -0.0560 -0.0860 40  ARG A CB  
357  C CG  A ARG A 39  ? 0.6594 0.6097 0.5010 -0.1282 -0.0311 -0.1125 40  ARG A CG  
358  C CG  B ARG A 39  ? 0.5690 0.4821 0.3433 -0.1226 -0.0529 -0.0968 40  ARG A CG  
359  C CD  A ARG A 39  ? 0.7461 0.7105 0.5787 -0.1325 -0.0463 -0.1233 40  ARG A CD  
360  C CD  B ARG A 39  ? 0.5825 0.4870 0.3232 -0.1234 -0.0699 -0.0971 40  ARG A CD  
361  N NE  A ARG A 39  ? 0.8264 0.7963 0.6624 -0.1471 -0.0353 -0.1366 40  ARG A NE  
362  N NE  B ARG A 39  ? 0.6054 0.5098 0.3323 -0.1374 -0.0651 -0.1078 40  ARG A NE  
363  C CZ  A ARG A 39  ? 0.9894 0.9430 0.8038 -0.1580 -0.0263 -0.1397 40  ARG A CZ  
364  C CZ  B ARG A 39  ? 0.7691 0.6947 0.5033 -0.1410 -0.0749 -0.1202 40  ARG A CZ  
365  N NH1 A ARG A 39  ? 0.8081 0.7395 0.5963 -0.1567 -0.0257 -0.1306 40  ARG A NH1 
366  N NH1 B ARG A 39  ? 0.5830 0.5339 0.3408 -0.1313 -0.0899 -0.1243 40  ARG A NH1 
367  N NH2 A ARG A 39  ? 0.8195 0.7782 0.6383 -0.1714 -0.0162 -0.1529 40  ARG A NH2 
368  N NH2 B ARG A 39  ? 0.6823 0.6055 0.4016 -0.1548 -0.0691 -0.1301 40  ARG A NH2 
369  N N   A GLU A 40  ? 0.4391 0.3609 0.2855 -0.0920 -0.0360 -0.0708 41  GLU A N   
370  N N   B GLU A 40  ? 0.4280 0.3428 0.2578 -0.0909 -0.0443 -0.0689 41  GLU A N   
371  C CA  A GLU A 40  ? 0.4325 0.3496 0.2767 -0.0812 -0.0451 -0.0617 41  GLU A CA  
372  C CA  B GLU A 40  ? 0.4047 0.3222 0.2461 -0.0796 -0.0498 -0.0616 41  GLU A CA  
373  C C   A GLU A 40  ? 0.4352 0.3668 0.3090 -0.0762 -0.0394 -0.0613 41  GLU A C   
374  C C   B GLU A 40  ? 0.4104 0.3449 0.2835 -0.0768 -0.0421 -0.0636 41  GLU A C   
375  O O   A GLU A 40  ? 0.3993 0.3304 0.2838 -0.0808 -0.0243 -0.0619 41  GLU A O   
376  O O   B GLU A 40  ? 0.3629 0.2992 0.2463 -0.0835 -0.0279 -0.0670 41  GLU A O   
377  C CB  A GLU A 40  ? 0.4641 0.3573 0.2862 -0.0830 -0.0382 -0.0529 41  GLU A CB  
378  C CB  B GLU A 40  ? 0.4295 0.3245 0.2530 -0.0786 -0.0443 -0.0512 41  GLU A CB  
379  C CG  A GLU A 40  ? 0.6562 0.5320 0.4442 -0.0892 -0.0437 -0.0529 41  GLU A CG  
380  C CG  B GLU A 40  ? 0.6400 0.5138 0.4288 -0.0861 -0.0449 -0.0498 41  GLU A CG  
381  C CD  A GLU A 40  ? 1.0982 0.9566 0.8611 -0.0829 -0.0571 -0.0447 41  GLU A CD  
382  C CD  B GLU A 40  ? 1.1134 0.9699 0.8740 -0.0807 -0.0602 -0.0430 41  GLU A CD  
383  O OE1 A GLU A 40  ? 1.1433 0.9792 0.8815 -0.0887 -0.0500 -0.0394 41  GLU A OE1 
384  O OE1 B GLU A 40  ? 1.1183 0.9835 0.8839 -0.0704 -0.0775 -0.0431 41  GLU A OE1 
385  O OE2 A GLU A 40  ? 1.0846 0.9510 0.8521 -0.0725 -0.0742 -0.0441 41  GLU A OE2 
386  O OE2 B GLU A 40  ? 1.1472 0.9801 0.8795 -0.0871 -0.0546 -0.0382 41  GLU A OE2 
387  N N   . GLN A 41  ? 0.3787 0.3228 0.2648 -0.0666 -0.0517 -0.0612 42  GLN A N   
388  C CA  . GLN A 41  ? 0.3597 0.3195 0.2729 -0.0632 -0.0467 -0.0628 42  GLN A CA  
389  C C   . GLN A 41  ? 0.3954 0.3485 0.3103 -0.0546 -0.0479 -0.0538 42  GLN A C   
390  O O   . GLN A 41  ? 0.4062 0.3513 0.3086 -0.0476 -0.0599 -0.0495 42  GLN A O   
391  C CB  . GLN A 41  ? 0.3819 0.3661 0.3128 -0.0605 -0.0579 -0.0733 42  GLN A CB  
392  C CG  . GLN A 41  ? 0.5730 0.5677 0.5073 -0.0713 -0.0538 -0.0846 42  GLN A CG  
393  C CD  . GLN A 41  ? 0.7988 0.8221 0.7555 -0.0706 -0.0621 -0.0975 42  GLN A CD  
394  O OE1 . GLN A 41  ? 0.6972 0.7348 0.6707 -0.0617 -0.0697 -0.0990 42  GLN A OE1 
395  N NE2 . GLN A 41  ? 0.8435 0.8768 0.8019 -0.0808 -0.0599 -0.1087 42  GLN A NE2 
396  N N   . PHE A 42  ? 0.3151 0.2700 0.2438 -0.0551 -0.0357 -0.0509 43  PHE A N   
397  C CA  . PHE A 42  ? 0.3202 0.2705 0.2519 -0.0482 -0.0355 -0.0434 43  PHE A CA  
398  C C   . PHE A 42  ? 0.3606 0.3272 0.3157 -0.0457 -0.0321 -0.0462 43  PHE A C   
399  O O   . PHE A 42  ? 0.3577 0.3273 0.3211 -0.0511 -0.0208 -0.0479 43  PHE A O   
400  C CB  . PHE A 42  ? 0.3431 0.2781 0.2653 -0.0518 -0.0234 -0.0368 43  PHE A CB  
401  C CG  . PHE A 42  ? 0.3813 0.2994 0.2793 -0.0566 -0.0236 -0.0351 43  PHE A CG  
402  C CD1 . PHE A 42  ? 0.4013 0.3159 0.2925 -0.0648 -0.0168 -0.0396 43  PHE A CD1 
403  C CD2 . PHE A 42  ? 0.4176 0.3210 0.2977 -0.0541 -0.0292 -0.0294 43  PHE A CD2 
404  C CE1 . PHE A 42  ? 0.4437 0.3424 0.3110 -0.0705 -0.0160 -0.0388 43  PHE A CE1 
405  C CE2 . PHE A 42  ? 0.4731 0.3587 0.3274 -0.0604 -0.0281 -0.0280 43  PHE A CE2 
406  C CZ  . PHE A 42  ? 0.4490 0.3332 0.2973 -0.0687 -0.0213 -0.0329 43  PHE A CZ  
407  N N   . ARG A 43  ? 0.3095 0.2844 0.2734 -0.0376 -0.0414 -0.0467 44  ARG A N   
408  C CA  . ARG A 43  ? 0.2802 0.2706 0.2651 -0.0360 -0.0376 -0.0502 44  ARG A CA  
409  C C   . ARG A 43  ? 0.3326 0.3142 0.3165 -0.0342 -0.0300 -0.0419 44  ARG A C   
410  O O   . ARG A 43  ? 0.3230 0.2915 0.2947 -0.0307 -0.0329 -0.0354 44  ARG A O   
411  C CB  . ARG A 43  ? 0.2997 0.3057 0.2975 -0.0281 -0.0506 -0.0569 44  ARG A CB  
412  C CG  . ARG A 43  ? 0.3985 0.4191 0.4015 -0.0293 -0.0596 -0.0674 44  ARG A CG  
413  C CD  . ARG A 43  ? 0.5128 0.5586 0.5401 -0.0238 -0.0670 -0.0786 44  ARG A CD  
414  N NE  . ARG A 43  ? 0.6491 0.7045 0.6927 -0.0284 -0.0540 -0.0810 44  ARG A NE  
415  C CZ  . ARG A 43  ? 0.7791 0.8473 0.8344 -0.0388 -0.0433 -0.0892 44  ARG A CZ  
416  N NH1 . ARG A 43  ? 0.6932 0.7703 0.7503 -0.0456 -0.0443 -0.0978 44  ARG A NH1 
417  N NH2 . ARG A 43  ? 0.5427 0.6142 0.6069 -0.0431 -0.0315 -0.0896 44  ARG A NH2 
418  N N   . ALA A 44  ? 0.2747 0.2625 0.2695 -0.0372 -0.0202 -0.0423 45  ALA A N   
419  C CA  . ALA A 44  ? 0.2750 0.2566 0.2689 -0.0351 -0.0141 -0.0352 45  ALA A CA  
420  C C   . ALA A 44  ? 0.2797 0.2714 0.2861 -0.0366 -0.0078 -0.0376 45  ALA A C   
421  O O   . ALA A 44  ? 0.2640 0.2668 0.2798 -0.0406 -0.0065 -0.0452 45  ALA A O   
422  C CB  . ALA A 44  ? 0.2882 0.2565 0.2714 -0.0385 -0.0060 -0.0298 45  ALA A CB  
423  N N   . HIS A 45  ? 0.2367 0.2247 0.2423 -0.0346 -0.0035 -0.0318 46  HIS A N   
424  C CA  . HIS A 45  ? 0.2224 0.2157 0.2342 -0.0364 0.0031  -0.0322 46  HIS A CA  
425  C C   . HIS A 45  ? 0.2724 0.2541 0.2760 -0.0393 0.0119  -0.0270 46  HIS A C   
426  O O   . HIS A 45  ? 0.2700 0.2436 0.2673 -0.0362 0.0124  -0.0213 46  HIS A O   
427  C CB  . HIS A 45  ? 0.2134 0.2097 0.2278 -0.0316 0.0008  -0.0293 46  HIS A CB  
428  C CG  . HIS A 45  ? 0.2521 0.2558 0.2733 -0.0270 -0.0080 -0.0339 46  HIS A CG  
429  N ND1 . HIS A 45  ? 0.2765 0.2720 0.2908 -0.0224 -0.0148 -0.0306 46  HIS A ND1 
430  C CD2 . HIS A 45  ? 0.2544 0.2718 0.2883 -0.0263 -0.0108 -0.0422 46  HIS A CD2 
431  C CE1 . HIS A 45  ? 0.2649 0.2667 0.2863 -0.0175 -0.0226 -0.0358 46  HIS A CE1 
432  N NE2 . HIS A 45  ? 0.2510 0.2681 0.2864 -0.0191 -0.0207 -0.0435 46  HIS A NE2 
433  N N   . LYS A 46  ? 0.2485 0.2288 0.2520 -0.0452 0.0190  -0.0299 47  LYS A N   
434  C CA  . LYS A 46  ? 0.2587 0.2242 0.2527 -0.0468 0.0272  -0.0248 47  LYS A CA  
435  C C   . LYS A 46  ? 0.2901 0.2508 0.2799 -0.0403 0.0271  -0.0169 47  LYS A C   
436  O O   . LYS A 46  ? 0.2703 0.2216 0.2550 -0.0367 0.0287  -0.0124 47  LYS A O   
437  C CB  . LYS A 46  ? 0.2854 0.2474 0.2771 -0.0548 0.0357  -0.0285 47  LYS A CB  
438  C CG  . LYS A 46  ? 0.2958 0.2614 0.2910 -0.0627 0.0378  -0.0374 47  LYS A CG  
439  C CD  . LYS A 46  ? 0.2996 0.2621 0.2925 -0.0728 0.0478  -0.0425 47  LYS A CD  
440  C CE  . LYS A 46  ? 0.3468 0.3185 0.3468 -0.0818 0.0495  -0.0540 47  LYS A CE  
441  N NZ  . LYS A 46  ? 0.3675 0.3364 0.3653 -0.0941 0.0613  -0.0607 47  LYS A NZ  
442  N N   . THR A 47  ? 0.2597 0.2284 0.2527 -0.0388 0.0251  -0.0164 48  THR A N   
443  C CA  . THR A 47  ? 0.2591 0.2251 0.2479 -0.0331 0.0243  -0.0098 48  THR A CA  
444  C C   . THR A 47  ? 0.2596 0.2276 0.2508 -0.0275 0.0196  -0.0073 48  THR A C   
445  O O   . THR A 47  ? 0.2457 0.2096 0.2340 -0.0229 0.0203  -0.0030 48  THR A O   
446  C CB  . THR A 47  ? 0.3235 0.2977 0.3140 -0.0338 0.0235  -0.0107 48  THR A CB  
447  O OG1 . THR A 47  ? 0.3161 0.3026 0.3169 -0.0336 0.0184  -0.0161 48  THR A OG1 
448  C CG2 . THR A 47  ? 0.3621 0.3310 0.3461 -0.0407 0.0309  -0.0124 48  THR A CG2 
449  N N   . VAL A 48  ? 0.2268 0.2004 0.2226 -0.0280 0.0150  -0.0106 49  VAL A N   
450  C CA  . VAL A 48  ? 0.2236 0.1966 0.2188 -0.0252 0.0124  -0.0091 49  VAL A CA  
451  C C   . VAL A 48  ? 0.2564 0.2208 0.2476 -0.0256 0.0165  -0.0082 49  VAL A C   
452  O O   . VAL A 48  ? 0.2440 0.2080 0.2358 -0.0226 0.0180  -0.0066 49  VAL A O   
453  C CB  . VAL A 48  ? 0.2525 0.2275 0.2483 -0.0260 0.0066  -0.0119 49  VAL A CB  
454  C CG1 . VAL A 48  ? 0.2573 0.2275 0.2482 -0.0259 0.0063  -0.0106 49  VAL A CG1 
455  C CG2 . VAL A 48  ? 0.2454 0.2285 0.2466 -0.0244 0.0031  -0.0136 49  VAL A CG2 
456  N N   . LEU A 49  ? 0.2325 0.1914 0.2210 -0.0296 0.0186  -0.0109 50  LEU A N   
457  C CA  . LEU A 49  ? 0.2414 0.1909 0.2256 -0.0306 0.0236  -0.0112 50  LEU A CA  
458  C C   . LEU A 49  ? 0.2761 0.2198 0.2600 -0.0258 0.0282  -0.0076 50  LEU A C   
459  O O   . LEU A 49  ? 0.2605 0.2019 0.2455 -0.0225 0.0305  -0.0074 50  LEU A O   
460  C CB  . LEU A 49  ? 0.2436 0.1886 0.2247 -0.0367 0.0257  -0.0155 50  LEU A CB  
461  C CG  . LEU A 49  ? 0.2746 0.2253 0.2553 -0.0401 0.0192  -0.0199 50  LEU A CG  
462  C CD1 . LEU A 49  ? 0.2833 0.2323 0.2626 -0.0466 0.0217  -0.0257 50  LEU A CD1 
463  C CD2 . LEU A 49  ? 0.3017 0.2483 0.2757 -0.0397 0.0165  -0.0191 50  LEU A CD2 
464  N N   . MET A 50  ? 0.2418 0.1832 0.2238 -0.0250 0.0293  -0.0050 51  MET A N   
465  C CA  . MET A 50  ? 0.2525 0.1849 0.2303 -0.0189 0.0319  -0.0002 51  MET A CA  
466  C C   . MET A 50  ? 0.2793 0.2211 0.2628 -0.0112 0.0274  0.0020  51  MET A C   
467  O O   . MET A 50  ? 0.2764 0.2145 0.2611 -0.0044 0.0283  0.0033  51  MET A O   
468  C CB  . MET A 50  ? 0.2820 0.2079 0.2520 -0.0212 0.0339  0.0024  51  MET A CB  
469  C CG  . MET A 50  ? 0.3223 0.2389 0.2872 -0.0300 0.0402  -0.0014 51  MET A CG  
470  S SD  . MET A 50  ? 0.3687 0.2829 0.3261 -0.0359 0.0434  -0.0008 51  MET A SD  
471  C CE  . MET A 50  ? 0.3464 0.2353 0.2863 -0.0308 0.0478  0.0072  51  MET A CE  
472  N N   . ALA A 51  ? 0.2456 0.2005 0.2337 -0.0122 0.0227  0.0013  52  ALA A N   
473  C CA  . ALA A 51  ? 0.2450 0.2113 0.2392 -0.0069 0.0188  0.0018  52  ALA A CA  
474  C C   . ALA A 51  ? 0.2754 0.2461 0.2764 -0.0059 0.0202  -0.0019 52  ALA A C   
475  O O   . ALA A 51  ? 0.2761 0.2564 0.2840 -0.0008 0.0185  -0.0029 52  ALA A O   
476  C CB  . ALA A 51  ? 0.2418 0.2185 0.2383 -0.0102 0.0149  0.0006  52  ALA A CB  
477  N N   . CYS A 52  ? 0.2358 0.2007 0.2345 -0.0115 0.0235  -0.0048 53  CYS A N   
478  C CA  . CYS A 52  ? 0.2420 0.2091 0.2440 -0.0134 0.0266  -0.0092 53  CYS A CA  
479  C C   . CYS A 52  ? 0.2816 0.2407 0.2839 -0.0116 0.0323  -0.0114 53  CYS A C   
480  O O   . CYS A 52  ? 0.2695 0.2329 0.2765 -0.0126 0.0360  -0.0162 53  CYS A O   
481  C CB  . CYS A 52  ? 0.2510 0.2153 0.2465 -0.0213 0.0258  -0.0111 53  CYS A CB  
482  S SG  . CYS A 52  ? 0.2808 0.2527 0.2767 -0.0227 0.0198  -0.0101 53  CYS A SG  
483  N N   . SER A 53  ? 0.2582 0.2050 0.2546 -0.0111 0.0344  -0.0092 54  SER A N   
484  C CA  . SER A 53  ? 0.2543 0.1903 0.2490 -0.0113 0.0408  -0.0122 54  SER A CA  
485  C C   . SER A 53  ? 0.3152 0.2385 0.3069 -0.0045 0.0427  -0.0087 54  SER A C   
486  O O   . SER A 53  ? 0.2962 0.2118 0.2802 -0.0066 0.0418  -0.0048 54  SER A O   
487  C CB  . SER A 53  ? 0.2768 0.2059 0.2628 -0.0212 0.0426  -0.0146 54  SER A CB  
488  O OG  . SER A 53  ? 0.3196 0.2352 0.3005 -0.0234 0.0486  -0.0168 54  SER A OG  
489  N N   . GLY A 54  ? 0.3060 0.2257 0.3030 0.0032  0.0458  -0.0108 55  GLY A N   
490  C CA  . GLY A 54  ? 0.3220 0.2242 0.3135 0.0110  0.0476  -0.0072 55  GLY A CA  
491  C C   . GLY A 54  ? 0.3627 0.2456 0.3420 0.0028  0.0541  -0.0076 55  GLY A C   
492  O O   . GLY A 54  ? 0.3648 0.2303 0.3331 0.0042  0.0555  -0.0028 55  GLY A O   
493  N N   . LEU A 55  ? 0.3241 0.2092 0.3033 -0.0072 0.0584  -0.0137 56  LEU A N   
494  C CA  . LEU A 55  ? 0.3237 0.1940 0.2926 -0.0165 0.0642  -0.0160 56  LEU A CA  
495  C C   . LEU A 55  ? 0.3450 0.2165 0.3077 -0.0233 0.0613  -0.0130 56  LEU A C   
496  O O   . LEU A 55  ? 0.3417 0.1974 0.2953 -0.0264 0.0658  -0.0117 56  LEU A O   
497  C CB  . LEU A 55  ? 0.3193 0.1933 0.2880 -0.0256 0.0678  -0.0236 56  LEU A CB  
498  C CG  . LEU A 55  ? 0.3918 0.2518 0.3508 -0.0354 0.0741  -0.0279 56  LEU A CG  
499  C CD1 . LEU A 55  ? 0.4124 0.2508 0.3677 -0.0309 0.0828  -0.0291 56  LEU A CD1 
500  C CD2 . LEU A 55  ? 0.3910 0.2575 0.3471 -0.0450 0.0746  -0.0346 56  LEU A CD2 
501  N N   . PHE A 56  ? 0.3066 0.1956 0.2741 -0.0259 0.0546  -0.0126 57  PHE A N   
502  C CA  . PHE A 56  ? 0.2911 0.1845 0.2560 -0.0317 0.0519  -0.0117 57  PHE A CA  
503  C C   . PHE A 56  ? 0.3391 0.2256 0.2994 -0.0269 0.0518  -0.0056 57  PHE A C   
504  O O   . PHE A 56  ? 0.3210 0.2014 0.2750 -0.0333 0.0549  -0.0059 57  PHE A O   
505  C CB  . PHE A 56  ? 0.2905 0.2018 0.2613 -0.0341 0.0445  -0.0132 57  PHE A CB  
506  C CG  . PHE A 56  ? 0.2923 0.2060 0.2615 -0.0408 0.0440  -0.0190 57  PHE A CG  
507  C CD1 . PHE A 56  ? 0.3168 0.2259 0.2818 -0.0489 0.0471  -0.0241 57  PHE A CD1 
508  C CD2 . PHE A 56  ? 0.2978 0.2178 0.2677 -0.0401 0.0404  -0.0197 57  PHE A CD2 
509  C CE1 . PHE A 56  ? 0.3284 0.2398 0.2900 -0.0547 0.0453  -0.0296 57  PHE A CE1 
510  C CE2 . PHE A 56  ? 0.3296 0.2489 0.2933 -0.0465 0.0391  -0.0242 57  PHE A CE2 
511  C CZ  . PHE A 56  ? 0.3061 0.2215 0.2657 -0.0531 0.0408  -0.0290 57  PHE A CZ  
512  N N   . TYR A 57  ? 0.3095 0.1968 0.2723 -0.0163 0.0486  -0.0008 58  TYR A N   
513  C CA  . TYR A 57  ? 0.3273 0.2053 0.2818 -0.0107 0.0474  0.0058  58  TYR A CA  
514  C C   . TYR A 57  ? 0.3911 0.2421 0.3308 -0.0129 0.0552  0.0075  58  TYR A C   
515  O O   . TYR A 57  ? 0.3829 0.2232 0.3106 -0.0180 0.0580  0.0103  58  TYR A O   
516  C CB  . TYR A 57  ? 0.3474 0.2316 0.3077 0.0023  0.0415  0.0092  58  TYR A CB  
517  C CG  . TYR A 57  ? 0.3985 0.2705 0.3469 0.0095  0.0387  0.0167  58  TYR A CG  
518  C CD1 . TYR A 57  ? 0.4140 0.2914 0.3565 0.0058  0.0356  0.0198  58  TYR A CD1 
519  C CD2 . TYR A 57  ? 0.4711 0.3247 0.4124 0.0204  0.0389  0.0206  58  TYR A CD2 
520  C CE1 . TYR A 57  ? 0.4536 0.3175 0.3808 0.0115  0.0331  0.0271  58  TYR A CE1 
521  C CE2 . TYR A 57  ? 0.5221 0.3607 0.4480 0.0277  0.0351  0.0285  58  TYR A CE2 
522  C CZ  . TYR A 57  ? 0.6151 0.4588 0.5327 0.0227  0.0322  0.0320  58  TYR A CZ  
523  O OH  . TYR A 57  ? 0.7143 0.5411 0.6130 0.0294  0.0284  0.0401  58  TYR A OH  
524  N N   A SER A 58  ? 0.3742 0.2130 0.3139 -0.0100 0.0599  0.0051  59  SER A N   
525  N N   B SER A 58  ? 0.3743 0.2132 0.3140 -0.0099 0.0598  0.0051  59  SER A N   
526  C CA  A SER A 58  ? 0.4009 0.2110 0.3261 -0.0120 0.0683  0.0059  59  SER A CA  
527  C CA  B SER A 58  ? 0.4013 0.2116 0.3267 -0.0120 0.0683  0.0058  59  SER A CA  
528  C C   A SER A 58  ? 0.4617 0.2677 0.3807 -0.0284 0.0756  0.0006  59  SER A C   
529  C C   B SER A 58  ? 0.4570 0.2639 0.3762 -0.0284 0.0752  0.0008  59  SER A C   
530  O O   A SER A 58  ? 0.4840 0.2688 0.3874 -0.0337 0.0820  0.0028  59  SER A O   
531  O O   B SER A 58  ? 0.4734 0.2605 0.3771 -0.0336 0.0810  0.0033  59  SER A O   
532  C CB  A SER A 58  ? 0.4381 0.2395 0.3680 -0.0055 0.0718  0.0023  59  SER A CB  
533  C CB  B SER A 58  ? 0.4438 0.2461 0.3741 -0.0066 0.0722  0.0017  59  SER A CB  
534  O OG  A SER A 58  ? 0.4376 0.2411 0.3733 0.0106  0.0657  0.0063  59  SER A OG  
535  O OG  B SER A 58  ? 0.5035 0.2753 0.4187 -0.0090 0.0811  0.0019  59  SER A OG  
536  N N   . ILE A 59  ? 0.4018 0.2280 0.3321 -0.0366 0.0742  -0.0067 60  ILE A N   
537  C CA  . ILE A 59  ? 0.3949 0.2241 0.3237 -0.0513 0.0790  -0.0139 60  ILE A CA  
538  C C   . ILE A 59  ? 0.4175 0.2519 0.3433 -0.0571 0.0787  -0.0128 60  ILE A C   
539  O O   . ILE A 59  ? 0.4374 0.2585 0.3532 -0.0674 0.0872  -0.0157 60  ILE A O   
540  C CB  . ILE A 59  ? 0.4037 0.2547 0.3444 -0.0562 0.0744  -0.0214 60  ILE A CB  
541  C CG1 . ILE A 59  ? 0.4078 0.2511 0.3482 -0.0549 0.0780  -0.0249 60  ILE A CG1 
542  C CG2 . ILE A 59  ? 0.3868 0.2483 0.3298 -0.0695 0.0757  -0.0297 60  ILE A CG2 
543  C CD1 . ILE A 59  ? 0.4171 0.2793 0.3649 -0.0577 0.0720  -0.0300 60  ILE A CD1 
544  N N   . PHE A 60  ? 0.3528 0.2061 0.2867 -0.0519 0.0702  -0.0097 61  PHE A N   
545  C CA  . PHE A 60  ? 0.3487 0.2100 0.2819 -0.0584 0.0706  -0.0109 61  PHE A CA  
546  C C   . PHE A 60  ? 0.4125 0.2544 0.3289 -0.0562 0.0742  -0.0031 61  PHE A C   
547  O O   . PHE A 60  ? 0.4295 0.2751 0.3425 -0.0635 0.0769  -0.0048 61  PHE A O   
548  C CB  . PHE A 60  ? 0.3392 0.2280 0.2876 -0.0557 0.0610  -0.0130 61  PHE A CB  
549  C CG  . PHE A 60  ? 0.3351 0.2387 0.2948 -0.0589 0.0572  -0.0204 61  PHE A CG  
550  C CD1 . PHE A 60  ? 0.3708 0.2780 0.3327 -0.0698 0.0612  -0.0295 61  PHE A CD1 
551  C CD2 . PHE A 60  ? 0.3413 0.2546 0.3077 -0.0518 0.0495  -0.0188 61  PHE A CD2 
552  C CE1 . PHE A 60  ? 0.3776 0.2978 0.3475 -0.0719 0.0559  -0.0360 61  PHE A CE1 
553  C CE2 . PHE A 60  ? 0.3693 0.2921 0.3409 -0.0548 0.0455  -0.0246 61  PHE A CE2 
554  C CZ  . PHE A 60  ? 0.3477 0.2738 0.3205 -0.0640 0.0478  -0.0328 61  PHE A CZ  
555  N N   . THR A 61  ? 0.4024 0.2222 0.3072 -0.0466 0.0748  0.0046  62  THR A N   
556  C CA  . THR A 61  ? 0.4215 0.2165 0.3045 -0.0444 0.0779  0.0127  62  THR A CA  
557  C C   . THR A 61  ? 0.5272 0.2908 0.3919 -0.0533 0.0901  0.0116  62  THR A C   
558  O O   . THR A 61  ? 0.5399 0.2763 0.3812 -0.0550 0.0953  0.0177  62  THR A O   
559  C CB  . THR A 61  ? 0.5147 0.3039 0.3939 -0.0272 0.0692  0.0221  62  THR A CB  
560  O OG1 . THR A 61  ? 0.4743 0.2586 0.3605 -0.0183 0.0682  0.0215  62  THR A OG1 
561  C CG2 . THR A 61  ? 0.4450 0.2626 0.3377 -0.0216 0.0588  0.0231  62  THR A CG2 
562  N N   . ASP A 62  ? 0.4700 0.2359 0.3431 -0.0604 0.0953  0.0033  63  ASP A N   
563  C CA  . ASP A 62  ? 0.4985 0.2357 0.3552 -0.0712 0.1082  0.0001  63  ASP A CA  
564  C C   . ASP A 62  ? 0.5872 0.3297 0.4401 -0.0891 0.1162  -0.0068 63  ASP A C   
565  O O   . ASP A 62  ? 0.5497 0.3242 0.4222 -0.0952 0.1128  -0.0153 63  ASP A O   
566  C CB  . ASP A 62  ? 0.4982 0.2390 0.3658 -0.0741 0.1111  -0.0081 63  ASP A CB  
567  C CG  . ASP A 62  ? 0.6722 0.3852 0.5237 -0.0879 0.1254  -0.0133 63  ASP A CG  
568  O OD1 . ASP A 62  ? 0.7389 0.4170 0.5722 -0.0822 0.1307  -0.0074 63  ASP A OD1 
569  O OD2 . ASP A 62  ? 0.6685 0.3943 0.5253 -0.1044 0.1314  -0.0238 63  ASP A OD2 
570  N N   . GLN A 63  ? 0.6201 0.3301 0.4472 -0.0976 0.1274  -0.0038 64  GLN A N   
571  C CA  . GLN A 63  ? 0.6436 0.3549 0.4638 -0.1163 0.1378  -0.0109 64  GLN A CA  
572  C C   . GLN A 63  ? 0.6904 0.4251 0.5293 -0.1325 0.1439  -0.0273 64  GLN A C   
573  O O   . GLN A 63  ? 0.7083 0.4626 0.5549 -0.1449 0.1478  -0.0361 64  GLN A O   
574  C CB  . GLN A 63  ? 0.7175 0.3822 0.5013 -0.1233 0.1503  -0.0043 64  GLN A CB  
575  C CG  . GLN A 63  ? 0.9822 0.6280 0.7452 -0.1098 0.1433  0.0109  64  GLN A CG  
576  N N   . LEU A 64  ? 0.5947 0.3284 0.4411 -0.1328 0.1448  -0.0326 65  LEU A N   
577  C CA  . LEU A 64  ? 0.5690 0.3277 0.4337 -0.1470 0.1482  -0.0487 65  LEU A CA  
578  C C   . LEU A 64  ? 0.5839 0.3822 0.4761 -0.1381 0.1333  -0.0525 65  LEU A C   
579  O O   . LEU A 64  ? 0.6001 0.4288 0.5104 -0.1464 0.1310  -0.0641 65  LEU A O   
580  C CB  . LEU A 64  ? 0.5918 0.3278 0.4476 -0.1546 0.1580  -0.0541 65  LEU A CB  
581  C CG  . LEU A 64  ? 0.7034 0.4042 0.5347 -0.1715 0.1763  -0.0573 65  LEU A CG  
582  C CD1 . LEU A 64  ? 0.7173 0.3968 0.5418 -0.1766 0.1844  -0.0624 65  LEU A CD1 
583  C CD2 . LEU A 64  ? 0.7478 0.4695 0.5869 -0.1925 0.1850  -0.0718 65  LEU A CD2 
584  N N   . LYS A 65  ? 0.4781 0.2752 0.3733 -0.1217 0.1234  -0.0437 66  LYS A N   
585  C CA  . LYS A 65  ? 0.4452 0.2734 0.3613 -0.1144 0.1105  -0.0467 66  LYS A CA  
586  C C   . LYS A 65  ? 0.4963 0.3499 0.4249 -0.1083 0.1005  -0.0445 66  LYS A C   
587  O O   . LYS A 65  ? 0.4725 0.3531 0.4181 -0.1067 0.0913  -0.0502 66  LYS A O   
588  C CB  . LYS A 65  ? 0.4588 0.2776 0.3737 -0.1013 0.1056  -0.0400 66  LYS A CB  
589  C CG  . LYS A 65  ? 0.4716 0.2697 0.3780 -0.1072 0.1147  -0.0448 66  LYS A CG  
590  C CD  . LYS A 65  ? 0.4500 0.2449 0.3591 -0.0941 0.1095  -0.0401 66  LYS A CD  
591  C CE  . LYS A 65  ? 0.5209 0.2892 0.4193 -0.0971 0.1197  -0.0432 66  LYS A CE  
592  N NZ  . LYS A 65  ? 0.5561 0.2893 0.4369 -0.0915 0.1271  -0.0350 66  LYS A NZ  
593  N N   . CYS A 66  ? 0.5080 0.3513 0.4265 -0.1049 0.1020  -0.0365 67  CYS A N   
594  C CA  . CYS A 66  ? 0.4952 0.3604 0.4240 -0.0999 0.0939  -0.0349 67  CYS A CA  
595  C C   . CYS A 66  ? 0.5392 0.4328 0.4854 -0.1103 0.0937  -0.0483 67  CYS A C   
596  O O   . CYS A 66  ? 0.5315 0.4484 0.4921 -0.1047 0.0846  -0.0497 67  CYS A O   
597  C CB  . CYS A 66  ? 0.5265 0.3733 0.4376 -0.0980 0.0977  -0.0257 67  CYS A CB  
598  S SG  . CYS A 66  ? 0.6160 0.4426 0.5083 -0.1172 0.1149  -0.0312 67  CYS A SG  
599  N N   . ASN A 67  ? 0.4980 0.3892 0.4431 -0.1253 0.1040  -0.0591 68  ASN A N   
600  C CA  . ASN A 67  ? 0.4964 0.4159 0.4596 -0.1364 0.1050  -0.0746 68  ASN A CA  
601  C C   . ASN A 67  ? 0.5180 0.4600 0.4988 -0.1363 0.0967  -0.0845 68  ASN A C   
602  O O   . ASN A 67  ? 0.4927 0.4619 0.4915 -0.1432 0.0949  -0.0985 68  ASN A O   
603  C CB  . ASN A 67  ? 0.5300 0.4367 0.4825 -0.1550 0.1221  -0.0826 68  ASN A CB  
604  C CG  . ASN A 67  ? 0.7201 0.6102 0.6558 -0.1565 0.1290  -0.0750 68  ASN A CG  
605  O OD1 . ASN A 67  ? 0.7448 0.6043 0.6567 -0.1663 0.1425  -0.0719 68  ASN A OD1 
606  N ND2 . ASN A 67  ? 0.5895 0.4966 0.5344 -0.1469 0.1200  -0.0712 68  ASN A ND2 
607  N N   . LEU A 68  ? 0.4752 0.4073 0.4510 -0.1281 0.0910  -0.0781 69  LEU A N   
608  C CA  . LEU A 68  ? 0.4518 0.4019 0.4392 -0.1283 0.0826  -0.0865 69  LEU A CA  
609  C C   . LEU A 68  ? 0.4550 0.4290 0.4569 -0.1163 0.0666  -0.0854 69  LEU A C   
610  O O   . LEU A 68  ? 0.4378 0.4063 0.4363 -0.1051 0.0617  -0.0742 69  LEU A O   
611  C CB  . LEU A 68  ? 0.4609 0.3898 0.4354 -0.1253 0.0841  -0.0808 69  LEU A CB  
612  C CG  . LEU A 68  ? 0.5352 0.4373 0.4945 -0.1367 0.0995  -0.0830 69  LEU A CG  
613  C CD1 . LEU A 68  ? 0.5431 0.4255 0.4919 -0.1310 0.1001  -0.0773 69  LEU A CD1 
614  C CD2 . LEU A 68  ? 0.5390 0.4549 0.5058 -0.1539 0.1059  -0.1000 69  LEU A CD2 
615  N N   . SER A 69  ? 0.3924 0.3919 0.4095 -0.1184 0.0581  -0.0973 70  SER A N   
616  C CA  A SER A 69  ? 0.3729 0.3926 0.4019 -0.1068 0.0418  -0.0974 70  SER A CA  
617  C CA  B SER A 69  ? 0.3784 0.3973 0.4070 -0.1064 0.0418  -0.0967 70  SER A CA  
618  C C   . SER A 69  ? 0.3893 0.4030 0.4100 -0.1007 0.0324  -0.0931 70  SER A C   
619  O O   . SER A 69  ? 0.3345 0.3559 0.3577 -0.0905 0.0193  -0.0900 70  SER A O   
620  C CB  A SER A 69  ? 0.4104 0.4613 0.4607 -0.1110 0.0365  -0.1136 70  SER A CB  
621  C CB  B SER A 69  ? 0.4251 0.4752 0.4752 -0.1097 0.0364  -0.1121 70  SER A CB  
622  O OG  A SER A 69  ? 0.4708 0.5290 0.5294 -0.1176 0.0460  -0.1189 70  SER A OG  
623  O OG  B SER A 69  ? 0.5106 0.5714 0.5655 -0.1196 0.0371  -0.1250 70  SER A OG  
624  N N   . VAL A 70  ? 0.3592 0.3577 0.3683 -0.1082 0.0400  -0.0940 71  VAL A N   
625  C CA  . VAL A 70  ? 0.3548 0.3460 0.3536 -0.1052 0.0338  -0.0915 71  VAL A CA  
626  C C   . VAL A 70  ? 0.3855 0.3490 0.3688 -0.1065 0.0454  -0.0834 71  VAL A C   
627  O O   . VAL A 70  ? 0.3899 0.3410 0.3691 -0.1154 0.0583  -0.0863 71  VAL A O   
628  C CB  . VAL A 70  ? 0.4160 0.4223 0.4188 -0.1136 0.0292  -0.1053 71  VAL A CB  
629  C CG1 . VAL A 70  ? 0.4263 0.4226 0.4143 -0.1119 0.0236  -0.1026 71  VAL A CG1 
630  C CG2 . VAL A 70  ? 0.4087 0.4453 0.4299 -0.1104 0.0163  -0.1150 71  VAL A CG2 
631  N N   . ILE A 71  ? 0.3117 0.2649 0.2863 -0.0980 0.0412  -0.0743 72  ILE A N   
632  C CA  . ILE A 71  ? 0.3194 0.2496 0.2823 -0.0972 0.0506  -0.0682 72  ILE A CA  
633  C C   . ILE A 71  ? 0.3806 0.3080 0.3344 -0.0981 0.0467  -0.0702 72  ILE A C   
634  O O   . ILE A 71  ? 0.3719 0.3064 0.3241 -0.0923 0.0361  -0.0672 72  ILE A O   
635  C CB  . ILE A 71  ? 0.3386 0.2593 0.3005 -0.0867 0.0520  -0.0564 72  ILE A CB  
636  C CG1 . ILE A 71  ? 0.3481 0.2691 0.3148 -0.0868 0.0564  -0.0541 72  ILE A CG1 
637  C CG2 . ILE A 71  ? 0.3707 0.2711 0.3236 -0.0838 0.0600  -0.0519 72  ILE A CG2 
638  C CD1 . ILE A 71  ? 0.4041 0.3086 0.3642 -0.0961 0.0699  -0.0574 72  ILE A CD1 
639  N N   . ASN A 72  ? 0.3487 0.2633 0.2947 -0.1058 0.0559  -0.0753 73  ASN A N   
640  C CA  . ASN A 72  ? 0.3569 0.2672 0.2922 -0.1086 0.0542  -0.0783 73  ASN A CA  
641  C C   . ASN A 72  ? 0.4045 0.2967 0.3331 -0.1034 0.0622  -0.0720 73  ASN A C   
642  O O   . ASN A 72  ? 0.3945 0.2712 0.3226 -0.1040 0.0737  -0.0715 73  ASN A O   
643  C CB  . ASN A 72  ? 0.4091 0.3186 0.3403 -0.1216 0.0596  -0.0903 73  ASN A CB  
644  C CG  . ASN A 72  ? 0.6336 0.5647 0.5744 -0.1275 0.0522  -0.0996 73  ASN A CG  
645  O OD1 . ASN A 72  ? 0.5035 0.4519 0.4472 -0.1235 0.0380  -0.1006 73  ASN A OD1 
646  N ND2 . ASN A 72  ? 0.5828 0.5131 0.5285 -0.1373 0.0620  -0.1072 73  ASN A ND2 
647  N N   . LEU A 73  ? 0.3475 0.2409 0.2706 -0.0986 0.0564  -0.0679 74  LEU A N   
648  C CA  . LEU A 73  ? 0.3415 0.2220 0.2610 -0.0945 0.0643  -0.0645 74  LEU A CA  
649  C C   . LEU A 73  ? 0.3937 0.2629 0.3026 -0.1029 0.0728  -0.0723 74  LEU A C   
650  O O   . LEU A 73  ? 0.4060 0.2788 0.3074 -0.1120 0.0699  -0.0796 74  LEU A O   
651  C CB  . LEU A 73  ? 0.3371 0.2223 0.2546 -0.0882 0.0577  -0.0583 74  LEU A CB  
652  C CG  . LEU A 73  ? 0.3627 0.2581 0.2900 -0.0797 0.0499  -0.0508 74  LEU A CG  
653  C CD1 . LEU A 73  ? 0.3589 0.2546 0.2838 -0.0747 0.0477  -0.0458 74  LEU A CD1 
654  C CD2 . LEU A 73  ? 0.3635 0.2567 0.3018 -0.0750 0.0553  -0.0475 74  LEU A CD2 
655  N N   . ASP A 74  ? 0.3599 0.2169 0.2693 -0.0994 0.0829  -0.0718 75  ASP A N   
656  C CA  . ASP A 74  ? 0.3823 0.2272 0.2831 -0.1063 0.0932  -0.0800 75  ASP A CA  
657  C C   . ASP A 74  ? 0.4499 0.3000 0.3359 -0.1143 0.0873  -0.0839 75  ASP A C   
658  O O   . ASP A 74  ? 0.4195 0.2763 0.3026 -0.1106 0.0798  -0.0786 75  ASP A O   
659  C CB  . ASP A 74  ? 0.4060 0.2418 0.3134 -0.0980 0.1026  -0.0786 75  ASP A CB  
660  C CG  . ASP A 74  ? 0.5453 0.3677 0.4467 -0.1036 0.1151  -0.0880 75  ASP A CG  
661  O OD1 . ASP A 74  ? 0.5578 0.3820 0.4479 -0.1117 0.1159  -0.0935 75  ASP A OD1 
662  O OD2 . ASP A 74  ? 0.5633 0.3718 0.4702 -0.0994 0.1243  -0.0897 75  ASP A OD2 
663  N N   . PRO A 75  ? 0.4656 0.3115 0.3401 -0.1255 0.0903  -0.0931 76  PRO A N   
664  C CA  . PRO A 75  ? 0.4811 0.3300 0.3372 -0.1330 0.0833  -0.0963 76  PRO A CA  
665  C C   . PRO A 75  ? 0.5288 0.3712 0.3749 -0.1327 0.0876  -0.0948 76  PRO A C   
666  O O   . PRO A 75  ? 0.5472 0.3900 0.3753 -0.1375 0.0801  -0.0943 76  PRO A O   
667  C CB  . PRO A 75  ? 0.5207 0.3648 0.3674 -0.1454 0.0885  -0.1077 76  PRO A CB  
668  C CG  . PRO A 75  ? 0.5791 0.4117 0.4377 -0.1444 0.1028  -0.1109 76  PRO A CG  
669  C CD  . PRO A 75  ? 0.4915 0.3281 0.3669 -0.1326 0.1000  -0.1012 76  PRO A CD  
670  N N   . GLU A 76  ? 0.4829 0.3193 0.3400 -0.1273 0.0995  -0.0947 77  GLU A N   
671  C CA  . GLU A 76  ? 0.5019 0.3353 0.3531 -0.1281 0.1055  -0.0955 77  GLU A CA  
672  C C   . GLU A 76  ? 0.4966 0.3381 0.3495 -0.1215 0.0962  -0.0861 77  GLU A C   
673  O O   . GLU A 76  ? 0.4915 0.3307 0.3351 -0.1248 0.0995  -0.0866 77  GLU A O   
674  C CB  . GLU A 76  ? 0.5340 0.3619 0.4002 -0.1231 0.1206  -0.1005 77  GLU A CB  
675  C CG  . GLU A 76  ? 0.7979 0.6140 0.6570 -0.1319 0.1329  -0.1120 77  GLU A CG  
676  C CD  . GLU A 76  ? 1.2053 1.0172 1.0455 -0.1435 0.1394  -0.1197 77  GLU A CD  
677  O OE1 . GLU A 76  ? 1.2018 1.0151 1.0483 -0.1414 0.1483  -0.1227 77  GLU A OE1 
678  O OE2 . GLU A 76  ? 1.2097 1.0178 1.0286 -0.1552 0.1356  -0.1234 77  GLU A OE2 
679  N N   . ILE A 77  ? 0.4204 0.2705 0.2845 -0.1135 0.0859  -0.0785 78  ILE A N   
680  C CA  . ILE A 77  ? 0.4008 0.2578 0.2673 -0.1073 0.0775  -0.0701 78  ILE A CA  
681  C C   . ILE A 77  ? 0.4659 0.3203 0.3101 -0.1129 0.0665  -0.0678 78  ILE A C   
682  O O   . ILE A 77  ? 0.4525 0.3085 0.2888 -0.1156 0.0572  -0.0689 78  ILE A O   
683  C CB  . ILE A 77  ? 0.4155 0.2819 0.3012 -0.0968 0.0714  -0.0634 78  ILE A CB  
684  C CG1 . ILE A 77  ? 0.4223 0.2867 0.3257 -0.0901 0.0818  -0.0646 78  ILE A CG1 
685  C CG2 . ILE A 77  ? 0.3683 0.2414 0.2555 -0.0911 0.0627  -0.0557 78  ILE A CG2 
686  C CD1 . ILE A 77  ? 0.5167 0.3810 0.4278 -0.0861 0.0914  -0.0669 78  ILE A CD1 
687  N N   . ASN A 78  ? 0.4687 0.3190 0.3034 -0.1140 0.0673  -0.0649 79  ASN A N   
688  C CA  . ASN A 78  ? 0.4943 0.3360 0.3034 -0.1188 0.0580  -0.0613 79  ASN A CA  
689  C C   . ASN A 78  ? 0.4806 0.3285 0.2949 -0.1097 0.0434  -0.0528 79  ASN A C   
690  O O   . ASN A 78  ? 0.4354 0.2904 0.2669 -0.1027 0.0450  -0.0487 79  ASN A O   
691  C CB  . ASN A 78  ? 0.5460 0.3782 0.3422 -0.1256 0.0685  -0.0628 79  ASN A CB  
692  C CG  . ASN A 78  ? 0.7307 0.5483 0.4965 -0.1308 0.0603  -0.0576 79  ASN A CG  
693  O OD1 . ASN A 78  ? 0.5917 0.4077 0.3574 -0.1273 0.0572  -0.0517 79  ASN A OD1 
694  N ND2 . ASN A 78  ? 0.6682 0.4730 0.4054 -0.1393 0.0564  -0.0598 79  ASN A ND2 
695  N N   . PRO A 79  ? 0.4605 0.3069 0.2612 -0.1091 0.0286  -0.0508 80  PRO A N   
696  C CA  . PRO A 79  ? 0.4457 0.2986 0.2534 -0.0993 0.0148  -0.0441 80  PRO A CA  
697  C C   . PRO A 79  ? 0.4822 0.3259 0.2819 -0.0971 0.0145  -0.0374 80  PRO A C   
698  O O   . PRO A 79  ? 0.4574 0.3096 0.2735 -0.0888 0.0105  -0.0331 80  PRO A O   
699  C CB  . PRO A 79  ? 0.4926 0.3433 0.2828 -0.0998 -0.0006 -0.0452 80  PRO A CB  
700  C CG  . PRO A 79  ? 0.5589 0.4101 0.3442 -0.1089 0.0058  -0.0537 80  PRO A CG  
701  C CD  . PRO A 79  ? 0.5104 0.3511 0.2905 -0.1164 0.0231  -0.0557 80  PRO A CD  
702  N N   . GLU A 80  ? 0.4641 0.2900 0.2376 -0.1058 0.0197  -0.0372 81  GLU A N   
703  C CA  . GLU A 80  ? 0.4671 0.2822 0.2311 -0.1060 0.0213  -0.0318 81  GLU A CA  
704  C C   . GLU A 80  ? 0.4699 0.2986 0.2615 -0.1035 0.0333  -0.0332 81  GLU A C   
705  O O   . GLU A 80  ? 0.4499 0.2818 0.2500 -0.0977 0.0297  -0.0286 81  GLU A O   
706  C CB  . GLU A 80  ? 0.5230 0.3141 0.2504 -0.1182 0.0263  -0.0320 81  GLU A CB  
707  C CG  . GLU A 80  ? 0.6342 0.4105 0.3477 -0.1192 0.0265  -0.0262 81  GLU A CG  
708  C CD  . GLU A 80  ? 0.9792 0.7302 0.6571 -0.1337 0.0361  -0.0269 81  GLU A CD  
709  O OE1 . GLU A 80  ? 0.9382 0.6676 0.5911 -0.1348 0.0307  -0.0203 81  GLU A OE1 
710  O OE2 . GLU A 80  ? 0.9154 0.6666 0.5896 -0.1443 0.0501  -0.0345 81  GLU A OE2 
711  N N   . GLY A 81  ? 0.4363 0.2728 0.2413 -0.1071 0.0465  -0.0400 82  GLY A N   
712  C CA  . GLY A 81  ? 0.4117 0.2629 0.2442 -0.1027 0.0561  -0.0422 82  GLY A CA  
713  C C   . GLY A 81  ? 0.4148 0.2802 0.2704 -0.0907 0.0477  -0.0376 82  GLY A C   
714  O O   . GLY A 81  ? 0.3830 0.2567 0.2526 -0.0857 0.0482  -0.0351 82  GLY A O   
715  N N   . PHE A 82  ? 0.3643 0.2332 0.2232 -0.0873 0.0401  -0.0371 83  PHE A N   
716  C CA  . PHE A 82  ? 0.3319 0.2136 0.2107 -0.0778 0.0333  -0.0336 83  PHE A CA  
717  C C   . PHE A 82  ? 0.3719 0.2530 0.2470 -0.0733 0.0230  -0.0278 83  PHE A C   
718  O O   . PHE A 82  ? 0.3443 0.2348 0.2355 -0.0671 0.0224  -0.0252 83  PHE A O   
719  C CB  . PHE A 82  ? 0.3461 0.2322 0.2286 -0.0772 0.0282  -0.0362 83  PHE A CB  
720  C CG  . PHE A 82  ? 0.3330 0.2318 0.2359 -0.0694 0.0245  -0.0337 83  PHE A CG  
721  C CD1 . PHE A 82  ? 0.3572 0.2608 0.2763 -0.0658 0.0327  -0.0337 83  PHE A CD1 
722  C CD2 . PHE A 82  ? 0.3334 0.2382 0.2380 -0.0653 0.0127  -0.0317 83  PHE A CD2 
723  C CE1 . PHE A 82  ? 0.3535 0.2660 0.2870 -0.0598 0.0299  -0.0309 83  PHE A CE1 
724  C CE2 . PHE A 82  ? 0.3391 0.2556 0.2615 -0.0595 0.0108  -0.0304 83  PHE A CE2 
725  C CZ  . PHE A 82  ? 0.3253 0.2447 0.2604 -0.0576 0.0198  -0.0297 83  PHE A CZ  
726  N N   . CYS A 83  ? 0.3878 0.2568 0.2409 -0.0759 0.0143  -0.0260 84  CYS A N   
727  C CA  . CYS A 83  ? 0.4099 0.2738 0.2563 -0.0708 0.0037  -0.0206 84  CYS A CA  
728  C C   . CYS A 83  ? 0.4253 0.2865 0.2739 -0.0718 0.0107  -0.0183 84  CYS A C   
729  O O   . CYS A 83  ? 0.3966 0.2641 0.2567 -0.0654 0.0064  -0.0154 84  CYS A O   
730  C CB  . CYS A 83  ? 0.4700 0.3157 0.2867 -0.0735 -0.0061 -0.0189 84  CYS A CB  
731  S SG  . CYS A 83  ? 0.5475 0.3827 0.3540 -0.0649 -0.0211 -0.0123 84  CYS A SG  
732  N N   . ILE A 84  ? 0.3868 0.2405 0.2259 -0.0807 0.0225  -0.0211 85  ILE A N   
733  C CA  . ILE A 84  ? 0.3642 0.2178 0.2063 -0.0841 0.0310  -0.0216 85  ILE A CA  
734  C C   . ILE A 84  ? 0.3549 0.2305 0.2283 -0.0765 0.0338  -0.0227 85  ILE A C   
735  O O   . ILE A 84  ? 0.3449 0.2253 0.2258 -0.0741 0.0331  -0.0211 85  ILE A O   
736  C CB  . ILE A 84  ? 0.4133 0.2582 0.2419 -0.0961 0.0445  -0.0272 85  ILE A CB  
737  C CG1 . ILE A 84  ? 0.4558 0.2731 0.2458 -0.1048 0.0413  -0.0245 85  ILE A CG1 
738  C CG2 . ILE A 84  ? 0.4035 0.2581 0.2458 -0.0997 0.0560  -0.0316 85  ILE A CG2 
739  C CD1 . ILE A 84  ? 0.5474 0.3554 0.3208 -0.1178 0.0541  -0.0309 85  ILE A CD1 
740  N N   . LEU A 85  ? 0.3211 0.2083 0.2104 -0.0732 0.0370  -0.0255 86  LEU A N   
741  C CA  . LEU A 85  ? 0.3029 0.2076 0.2179 -0.0653 0.0388  -0.0257 86  LEU A CA  
742  C C   . LEU A 85  ? 0.3401 0.2509 0.2632 -0.0577 0.0288  -0.0209 86  LEU A C   
743  O O   . LEU A 85  ? 0.3022 0.2236 0.2391 -0.0529 0.0286  -0.0197 86  LEU A O   
744  C CB  . LEU A 85  ? 0.3143 0.2242 0.2403 -0.0637 0.0455  -0.0296 86  LEU A CB  
745  C CG  . LEU A 85  ? 0.3879 0.2971 0.3134 -0.0697 0.0575  -0.0365 86  LEU A CG  
746  C CD1 . LEU A 85  ? 0.3995 0.3096 0.3329 -0.0677 0.0635  -0.0407 86  LEU A CD1 
747  C CD2 . LEU A 85  ? 0.3935 0.3159 0.3343 -0.0675 0.0619  -0.0391 86  LEU A CD2 
748  N N   . LEU A 86  ? 0.3091 0.2149 0.2242 -0.0567 0.0203  -0.0193 87  LEU A N   
749  C CA  . LEU A 86  ? 0.2984 0.2116 0.2225 -0.0500 0.0114  -0.0167 87  LEU A CA  
750  C C   . LEU A 86  ? 0.3384 0.2479 0.2583 -0.0486 0.0074  -0.0139 87  LEU A C   
751  O O   . LEU A 86  ? 0.3033 0.2226 0.2362 -0.0437 0.0057  -0.0127 87  LEU A O   
752  C CB  . LEU A 86  ? 0.2980 0.2091 0.2160 -0.0497 0.0031  -0.0179 87  LEU A CB  
753  C CG  . LEU A 86  ? 0.3479 0.2700 0.2784 -0.0433 -0.0051 -0.0179 87  LEU A CG  
754  C CD1 . LEU A 86  ? 0.3242 0.2587 0.2729 -0.0413 0.0008  -0.0186 87  LEU A CD1 
755  C CD2 . LEU A 86  ? 0.3843 0.3071 0.3097 -0.0430 -0.0145 -0.0213 87  LEU A CD2 
756  N N   . ASP A 87  ? 0.3267 0.2201 0.2262 -0.0536 0.0067  -0.0129 88  ASP A N   
757  C CA  . ASP A 87  ? 0.3220 0.2069 0.2138 -0.0538 0.0047  -0.0106 88  ASP A CA  
758  C C   . ASP A 87  ? 0.3403 0.2369 0.2468 -0.0551 0.0132  -0.0124 88  ASP A C   
759  O O   . ASP A 87  ? 0.3380 0.2390 0.2515 -0.0517 0.0104  -0.0114 88  ASP A O   
760  C CB  . ASP A 87  ? 0.3748 0.2359 0.2377 -0.0613 0.0054  -0.0093 88  ASP A CB  
761  C CG  . ASP A 87  ? 0.5516 0.3987 0.3966 -0.0576 -0.0073 -0.0064 88  ASP A CG  
762  O OD1 . ASP A 87  ? 0.5338 0.3920 0.3922 -0.0487 -0.0168 -0.0064 88  ASP A OD1 
763  O OD2 . ASP A 87  ? 0.5911 0.4166 0.4084 -0.0636 -0.0079 -0.0049 88  ASP A OD2 
764  N N   . PHE A 88  ? 0.3039 0.2067 0.2160 -0.0596 0.0231  -0.0162 89  PHE A N   
765  C CA  . PHE A 88  ? 0.2806 0.1986 0.2096 -0.0596 0.0300  -0.0195 89  PHE A CA  
766  C C   . PHE A 88  ? 0.2886 0.2230 0.2372 -0.0503 0.0253  -0.0176 89  PHE A C   
767  O O   . PHE A 88  ? 0.2631 0.2068 0.2207 -0.0487 0.0252  -0.0182 89  PHE A O   
768  C CB  . PHE A 88  ? 0.2891 0.2129 0.2236 -0.0636 0.0403  -0.0251 89  PHE A CB  
769  C CG  . PHE A 88  ? 0.2764 0.2205 0.2329 -0.0601 0.0448  -0.0293 89  PHE A CG  
770  C CD1 . PHE A 88  ? 0.2975 0.2473 0.2566 -0.0653 0.0491  -0.0334 89  PHE A CD1 
771  C CD2 . PHE A 88  ? 0.2939 0.2508 0.2676 -0.0510 0.0435  -0.0289 89  PHE A CD2 
772  C CE1 . PHE A 88  ? 0.2816 0.2533 0.2624 -0.0612 0.0513  -0.0382 89  PHE A CE1 
773  C CE2 . PHE A 88  ? 0.3137 0.2889 0.3063 -0.0456 0.0450  -0.0322 89  PHE A CE2 
774  C CZ  . PHE A 88  ? 0.2878 0.2723 0.2851 -0.0504 0.0482  -0.0372 89  PHE A CZ  
775  N N   . MET A 89  ? 0.2475 0.1850 0.2016 -0.0454 0.0224  -0.0160 90  MET A N   
776  C CA  . MET A 89  ? 0.2251 0.1748 0.1936 -0.0382 0.0191  -0.0141 90  MET A CA  
777  C C   . MET A 89  ? 0.2784 0.2298 0.2475 -0.0361 0.0130  -0.0124 90  MET A C   
778  O O   . MET A 89  ? 0.2636 0.2258 0.2429 -0.0330 0.0128  -0.0122 90  MET A O   
779  C CB  . MET A 89  ? 0.2347 0.1825 0.2038 -0.0361 0.0172  -0.0132 90  MET A CB  
780  C CG  . MET A 89  ? 0.2619 0.2078 0.2323 -0.0370 0.0239  -0.0153 90  MET A CG  
781  S SD  . MET A 89  ? 0.3000 0.2433 0.2711 -0.0361 0.0225  -0.0149 90  MET A SD  
782  C CE  . MET A 89  ? 0.3030 0.2380 0.2700 -0.0395 0.0311  -0.0186 90  MET A CE  
783  N N   . TYR A 90  ? 0.2519 0.1920 0.2094 -0.0374 0.0075  -0.0115 91  TYR A N   
784  C CA  . TYR A 90  ? 0.2504 0.1902 0.2087 -0.0342 0.0013  -0.0107 91  TYR A CA  
785  C C   . TYR A 90  ? 0.3048 0.2369 0.2555 -0.0377 0.0027  -0.0110 91  TYR A C   
786  O O   . TYR A 90  ? 0.2886 0.2191 0.2400 -0.0349 -0.0017 -0.0110 91  TYR A O   
787  C CB  . TYR A 90  ? 0.2726 0.2045 0.2237 -0.0315 -0.0069 -0.0104 91  TYR A CB  
788  C CG  . TYR A 90  ? 0.2728 0.2167 0.2361 -0.0281 -0.0091 -0.0120 91  TYR A CG  
789  C CD1 . TYR A 90  ? 0.2916 0.2364 0.2547 -0.0304 -0.0062 -0.0129 91  TYR A CD1 
790  C CD2 . TYR A 90  ? 0.2763 0.2302 0.2510 -0.0238 -0.0126 -0.0138 91  TYR A CD2 
791  C CE1 . TYR A 90  ? 0.2806 0.2348 0.2535 -0.0293 -0.0067 -0.0154 91  TYR A CE1 
792  C CE2 . TYR A 90  ? 0.2737 0.2381 0.2585 -0.0228 -0.0132 -0.0168 91  TYR A CE2 
793  C CZ  . TYR A 90  ? 0.3159 0.2801 0.2994 -0.0260 -0.0099 -0.0174 91  TYR A CZ  
794  O OH  . TYR A 90  ? 0.2769 0.2504 0.2694 -0.0269 -0.0091 -0.0214 91  TYR A OH  
795  N N   . THR A 91  ? 0.2683 0.1949 0.2115 -0.0445 0.0097  -0.0125 92  THR A N   
796  C CA  . THR A 91  ? 0.2801 0.1965 0.2134 -0.0503 0.0125  -0.0137 92  THR A CA  
797  C C   . THR A 91  ? 0.3064 0.2341 0.2476 -0.0567 0.0220  -0.0186 92  THR A C   
798  O O   . THR A 91  ? 0.3090 0.2311 0.2446 -0.0625 0.0252  -0.0210 92  THR A O   
799  C CB  . THR A 91  ? 0.3579 0.2478 0.2650 -0.0557 0.0117  -0.0116 92  THR A CB  
800  O OG1 . THR A 91  ? 0.3598 0.2476 0.2607 -0.0621 0.0187  -0.0134 92  THR A OG1 
801  C CG2 . THR A 91  ? 0.3464 0.2244 0.2441 -0.0485 0.0003  -0.0077 92  THR A CG2 
802  N N   . SER A 92  ? 0.2577 0.1990 0.2103 -0.0562 0.0267  -0.0211 93  SER A N   
803  C CA  . SER A 92  ? 0.2510 0.2061 0.2139 -0.0613 0.0354  -0.0278 93  SER A CA  
804  C C   . SER A 92  ? 0.3074 0.2476 0.2537 -0.0731 0.0442  -0.0316 93  SER A C   
805  O O   . SER A 92  ? 0.2984 0.2504 0.2533 -0.0789 0.0529  -0.0391 93  SER A O   
806  C CB  . SER A 92  ? 0.2689 0.2371 0.2421 -0.0623 0.0358  -0.0314 93  SER A CB  
807  O OG  . SER A 92  ? 0.3167 0.2956 0.3006 -0.0531 0.0283  -0.0280 93  SER A OG  
808  N N   A ARG A 93  ? 0.2997 0.2149 0.2221 -0.0763 0.0415  -0.0269 94  ARG A N   
809  N N   B ARG A 93  ? 0.2915 0.2063 0.2135 -0.0767 0.0417  -0.0270 94  ARG A N   
810  C CA  A ARG A 93  ? 0.3243 0.2190 0.2235 -0.0885 0.0492  -0.0290 94  ARG A CA  
811  C CA  B ARG A 93  ? 0.3111 0.2071 0.2113 -0.0891 0.0501  -0.0297 94  ARG A CA  
812  C C   A ARG A 93  ? 0.3764 0.2667 0.2691 -0.0893 0.0512  -0.0290 94  ARG A C   
813  C C   B ARG A 93  ? 0.3716 0.2611 0.2635 -0.0898 0.0514  -0.0290 94  ARG A C   
814  O O   A ARG A 93  ? 0.3554 0.2407 0.2444 -0.0822 0.0426  -0.0237 94  ARG A O   
815  O O   B ARG A 93  ? 0.3550 0.2383 0.2420 -0.0827 0.0423  -0.0234 94  ARG A O   
816  C CB  A ARG A 93  ? 0.3787 0.2440 0.2505 -0.0910 0.0438  -0.0232 94  ARG A CB  
817  C CB  B ARG A 93  ? 0.3461 0.2133 0.2190 -0.0944 0.0475  -0.0255 94  ARG A CB  
818  C CG  A ARG A 93  ? 0.4581 0.3238 0.3338 -0.0908 0.0425  -0.0237 94  ARG A CG  
819  C CG  B ARG A 93  ? 0.3521 0.2233 0.2305 -0.0987 0.0512  -0.0292 94  ARG A CG  
820  C CD  A ARG A 93  ? 0.5671 0.4019 0.4170 -0.0895 0.0350  -0.0173 94  ARG A CD  
821  C CD  B ARG A 93  ? 0.5098 0.3529 0.3656 -0.0984 0.0451  -0.0235 94  ARG A CD  
822  N NE  A ARG A 93  ? 0.6413 0.4449 0.4577 -0.1006 0.0403  -0.0160 94  ARG A NE  
823  N NE  B ARG A 93  ? 0.5948 0.4423 0.4572 -0.1028 0.0492  -0.0279 94  ARG A NE  
824  C CZ  A ARG A 93  ? 0.8031 0.5901 0.6027 -0.1140 0.0507  -0.0195 94  ARG A CZ  
825  C CZ  B ARG A 93  ? 0.7556 0.5757 0.5947 -0.1110 0.0525  -0.0275 94  ARG A CZ  
826  N NH1 A ARG A 93  ? 0.6625 0.4181 0.4277 -0.1247 0.0558  -0.0177 94  ARG A NH1 
827  N NH1 B ARG A 93  ? 0.6079 0.4343 0.4550 -0.1155 0.0568  -0.0327 94  ARG A NH1 
828  N NH2 A ARG A 93  ? 0.6140 0.4149 0.4294 -0.1179 0.0566  -0.0253 94  ARG A NH2 
829  N NH2 B ARG A 93  ? 0.6262 0.4105 0.4316 -0.1150 0.0515  -0.0219 94  ARG A NH2 
830  N N   . LEU A 94  ? 0.3418 0.2346 0.2334 -0.0990 0.0632  -0.0363 95  LEU A N   
831  C CA  . LEU A 94  ? 0.3442 0.2328 0.2295 -0.1014 0.0672  -0.0381 95  LEU A CA  
832  C C   . LEU A 94  ? 0.4240 0.2866 0.2770 -0.1159 0.0747  -0.0394 95  LEU A C   
833  O O   . LEU A 94  ? 0.4183 0.2799 0.2672 -0.1279 0.0865  -0.0464 95  LEU A O   
834  C CB  . LEU A 94  ? 0.3311 0.2459 0.2444 -0.0990 0.0753  -0.0467 95  LEU A CB  
835  C CG  . LEU A 94  ? 0.3824 0.2954 0.2939 -0.1002 0.0804  -0.0500 95  LEU A CG  
836  C CD1 . LEU A 94  ? 0.3664 0.2772 0.2798 -0.0894 0.0699  -0.0428 95  LEU A CD1 
837  C CD2 . LEU A 94  ? 0.3898 0.3255 0.3263 -0.0998 0.0908  -0.0610 95  LEU A CD2 
838  N N   . ASN A 95  ? 0.4296 0.2708 0.2582 -0.1156 0.0678  -0.0333 96  ASN A N   
839  C CA  . ASN A 95  ? 0.4651 0.2769 0.2565 -0.1289 0.0731  -0.0329 96  ASN A CA  
840  C C   . ASN A 95  ? 0.5187 0.3356 0.3101 -0.1376 0.0856  -0.0413 96  ASN A C   
841  O O   . ASN A 95  ? 0.5301 0.3390 0.3096 -0.1368 0.0820  -0.0395 96  ASN A O   
842  C CB  . ASN A 95  ? 0.5272 0.3141 0.2911 -0.1235 0.0581  -0.0229 96  ASN A CB  
843  C CG  . ASN A 95  ? 0.7690 0.5207 0.4884 -0.1364 0.0614  -0.0208 96  ASN A CG  
844  O OD1 . ASN A 95  ? 0.7083 0.4478 0.4124 -0.1508 0.0749  -0.0253 96  ASN A OD1 
845  N ND2 . ASN A 95  ? 0.6908 0.4252 0.3874 -0.1321 0.0491  -0.0145 96  ASN A ND2 
846  N N   . LEU A 96  ? 0.4694 0.3032 0.2783 -0.1449 0.0999  -0.0517 97  LEU A N   
847  C CA  . LEU A 96  ? 0.4819 0.3251 0.2973 -0.1526 0.1137  -0.0624 97  LEU A CA  
848  C C   . LEU A 96  ? 0.5615 0.3793 0.3415 -0.1723 0.1263  -0.0666 97  LEU A C   
849  O O   . LEU A 96  ? 0.5518 0.3616 0.3216 -0.1831 0.1338  -0.0693 97  LEU A O   
850  C CB  . LEU A 96  ? 0.4675 0.3452 0.3235 -0.1483 0.1213  -0.0729 97  LEU A CB  
851  C CG  . LEU A 96  ? 0.5347 0.4312 0.4119 -0.1477 0.1315  -0.0840 97  LEU A CG  
852  C CD1 . LEU A 96  ? 0.5295 0.4238 0.4092 -0.1362 0.1226  -0.0782 97  LEU A CD1 
853  C CD2 . LEU A 96  ? 0.5209 0.4516 0.4383 -0.1404 0.1350  -0.0932 97  LEU A CD2 
854  N N   . ARG A 97  ? 0.5373 0.3398 0.2950 -0.1781 0.1288  -0.0671 98  ARG A N   
855  C CA  . ARG A 97  ? 0.5936 0.3674 0.3107 -0.1978 0.1405  -0.0702 98  ARG A CA  
856  C C   . ARG A 97  ? 0.6071 0.3891 0.3279 -0.2056 0.1539  -0.0817 98  ARG A C   
857  O O   . ARG A 97  ? 0.5612 0.3609 0.3054 -0.1941 0.1493  -0.0830 98  ARG A O   
858  C CB  . ARG A 97  ? 0.6533 0.3900 0.3258 -0.1977 0.1264  -0.0566 98  ARG A CB  
859  C CG  . ARG A 97  ? 0.7548 0.4790 0.4204 -0.1896 0.1131  -0.0456 98  ARG A CG  
860  C CD  . ARG A 97  ? 0.9706 0.6605 0.5959 -0.1856 0.0966  -0.0327 98  ARG A CD  
861  N NE  . ARG A 97  ? 1.2293 0.8818 0.8040 -0.2031 0.1044  -0.0321 98  ARG A NE  
862  C CZ  . ARG A 97  ? 1.4942 1.1160 1.0361 -0.2157 0.1112  -0.0299 98  ARG A CZ  
863  N NH1 . ARG A 97  ? 1.3733 0.9588 0.8658 -0.2323 0.1187  -0.0291 98  ARG A NH1 
864  N NH2 . ARG A 97  ? 1.3462 0.9715 0.9020 -0.2126 0.1112  -0.0286 98  ARG A NH2 
865  N N   . GLU A 98  ? 0.5974 0.3643 0.2931 -0.2262 0.1715  -0.0905 99  GLU A N   
866  C CA  . GLU A 98  ? 0.5993 0.3724 0.2964 -0.2353 0.1859  -0.1029 99  GLU A CA  
867  C C   . GLU A 98  ? 0.6584 0.4219 0.3428 -0.2276 0.1744  -0.0963 99  GLU A C   
868  O O   . GLU A 98  ? 0.6473 0.4297 0.3555 -0.2230 0.1794  -0.1047 99  GLU A O   
869  C CB  . GLU A 98  ? 0.6638 0.4123 0.3223 -0.2610 0.2050  -0.1109 99  GLU A CB  
870  C CG  . GLU A 98  ? 0.7893 0.5468 0.4518 -0.2724 0.2232  -0.1267 99  GLU A CG  
871  C CD  . GLU A 98  ? 1.2305 0.9624 0.8520 -0.2998 0.2434  -0.1352 99  GLU A CD  
872  O OE1 . GLU A 98  ? 1.2086 0.8997 0.7775 -0.3095 0.2383  -0.1236 99  GLU A OE1 
873  O OE2 . GLU A 98  ? 1.2605 1.0129 0.9021 -0.3114 0.2646  -0.1541 99  GLU A OE2 
874  N N   . GLY A 99  ? 0.6542 0.3891 0.3024 -0.2257 0.1589  -0.0823 100 GLY A N   
875  C CA  . GLY A 99  ? 0.6714 0.3966 0.3041 -0.2197 0.1463  -0.0763 100 GLY A CA  
876  C C   . GLY A 99  ? 0.6698 0.4191 0.3388 -0.1993 0.1320  -0.0722 100 GLY A C   
877  O O   . GLY A 99  ? 0.6647 0.4122 0.3282 -0.1956 0.1249  -0.0711 100 GLY A O   
878  N N   . ASN A 100 ? 0.5877 0.3594 0.2929 -0.1869 0.1283  -0.0707 101 ASN A N   
879  C CA  . ASN A 100 ? 0.5456 0.3372 0.2817 -0.1688 0.1156  -0.0665 101 ASN A CA  
880  C C   . ASN A 100 ? 0.5539 0.3763 0.3353 -0.1603 0.1235  -0.0745 101 ASN A C   
881  O O   . ASN A 100 ? 0.5163 0.3525 0.3210 -0.1467 0.1152  -0.0717 101 ASN A O   
882  C CB  . ASN A 100 ? 0.5440 0.3301 0.2767 -0.1578 0.0974  -0.0537 101 ASN A CB  
883  C CG  . ASN A 100 ? 0.6250 0.4190 0.3725 -0.1556 0.0992  -0.0525 101 ASN A CG  
884  O OD1 . ASN A 100 ? 0.4867 0.3021 0.2626 -0.1555 0.1100  -0.0606 101 ASN A OD1 
885  N ND2 . ASN A 100 ? 0.5565 0.3345 0.2866 -0.1527 0.0878  -0.0429 101 ASN A ND2 
886  N N   . ILE A 101 ? 0.5187 0.3517 0.3123 -0.1679 0.1388  -0.0848 102 ILE A N   
887  C CA  . ILE A 101 ? 0.4847 0.3482 0.3219 -0.1579 0.1441  -0.0925 102 ILE A CA  
888  C C   . ILE A 101 ? 0.4991 0.3741 0.3573 -0.1487 0.1456  -0.0974 102 ILE A C   
889  O O   . ILE A 101 ? 0.4471 0.3396 0.3351 -0.1334 0.1395  -0.0955 102 ILE A O   
890  C CB  . ILE A 101 ? 0.5268 0.4027 0.3746 -0.1687 0.1607  -0.1055 102 ILE A CB  
891  C CG1 . ILE A 101 ? 0.5077 0.4177 0.4025 -0.1549 0.1619  -0.1126 102 ILE A CG1 
892  C CG2 . ILE A 101 ? 0.5317 0.3975 0.3607 -0.1863 0.1783  -0.1174 102 ILE A CG2 
893  C CD1 . ILE A 101 ? 0.5233 0.4505 0.4331 -0.1617 0.1711  -0.1221 102 ILE A CD1 
894  N N   . MET A 102 ? 0.4857 0.3487 0.3266 -0.1581 0.1538  -0.1034 103 MET A N   
895  C CA  . MET A 102 ? 0.4851 0.3555 0.3440 -0.1501 0.1561  -0.1085 103 MET A CA  
896  C C   . MET A 102 ? 0.5014 0.3690 0.3631 -0.1375 0.1400  -0.0971 103 MET A C   
897  O O   . MET A 102 ? 0.4617 0.3417 0.3503 -0.1245 0.1385  -0.0979 103 MET A O   
898  C CB  . MET A 102 ? 0.5504 0.4079 0.3887 -0.1643 0.1691  -0.1185 103 MET A CB  
899  C CG  . MET A 102 ? 0.6303 0.4934 0.4696 -0.1778 0.1881  -0.1328 103 MET A CG  
900  S SD  . MET A 102 ? 0.6785 0.5765 0.5692 -0.1663 0.1967  -0.1450 103 MET A SD  
901  C CE  . MET A 102 ? 0.6329 0.5378 0.5482 -0.1535 0.2003  -0.1526 103 MET A CE  
902  N N   . ALA A 103 ? 0.4747 0.3257 0.3086 -0.1408 0.1278  -0.0870 104 ALA A N   
903  C CA  . ALA A 103 ? 0.4642 0.3147 0.3010 -0.1305 0.1128  -0.0779 104 ALA A CA  
904  C C   . ALA A 103 ? 0.4665 0.3321 0.3288 -0.1169 0.1049  -0.0714 104 ALA A C   
905  O O   . ALA A 103 ? 0.4299 0.3033 0.3105 -0.1063 0.1002  -0.0691 104 ALA A O   
906  C CB  . ALA A 103 ? 0.4985 0.3313 0.3024 -0.1362 0.1010  -0.0702 104 ALA A CB  
907  N N   . VAL A 104 ? 0.3963 0.2648 0.2582 -0.1184 0.1045  -0.0692 105 VAL A N   
908  C CA  . VAL A 104 ? 0.3678 0.2510 0.2524 -0.1066 0.0973  -0.0638 105 VAL A CA  
909  C C   . VAL A 104 ? 0.3889 0.2907 0.3055 -0.0967 0.1031  -0.0695 105 VAL A C   
910  O O   . VAL A 104 ? 0.3674 0.2762 0.2992 -0.0848 0.0952  -0.0640 105 VAL A O   
911  C CB  . VAL A 104 ? 0.4101 0.2917 0.2870 -0.1115 0.0967  -0.0615 105 VAL A CB  
912  C CG1 . VAL A 104 ? 0.3739 0.2735 0.2764 -0.1003 0.0912  -0.0583 105 VAL A CG1 
913  C CG2 . VAL A 104 ? 0.4287 0.2889 0.2740 -0.1165 0.0868  -0.0531 105 VAL A CG2 
914  N N   A MET A 105 ? 0.3653 0.2744 0.2915 -0.1010 0.1166  -0.0808 106 MET A N   
915  N N   B MET A 105 ? 0.3669 0.2760 0.2931 -0.1010 0.1166  -0.0808 106 MET A N   
916  C CA  A MET A 105 ? 0.3625 0.2889 0.3197 -0.0893 0.1208  -0.0870 106 MET A CA  
917  C CA  B MET A 105 ? 0.3622 0.2887 0.3193 -0.0894 0.1209  -0.0871 106 MET A CA  
918  C C   A MET A 105 ? 0.4102 0.3299 0.3715 -0.0809 0.1183  -0.0849 106 MET A C   
919  C C   B MET A 105 ? 0.4137 0.3334 0.3750 -0.0810 0.1183  -0.0849 106 MET A C   
920  O O   A MET A 105 ? 0.3786 0.3056 0.3584 -0.0673 0.1130  -0.0814 106 MET A O   
921  O O   B MET A 105 ? 0.3887 0.3159 0.3685 -0.0673 0.1130  -0.0814 106 MET A O   
922  C CB  A MET A 105 ? 0.4032 0.3399 0.3711 -0.0956 0.1361  -0.1018 106 MET A CB  
923  C CB  B MET A 105 ? 0.4036 0.3401 0.3711 -0.0959 0.1364  -0.1019 106 MET A CB  
924  C CG  A MET A 105 ? 0.4370 0.3942 0.4396 -0.0808 0.1382  -0.1087 106 MET A CG  
925  C CG  B MET A 105 ? 0.4392 0.3964 0.4412 -0.0814 0.1385  -0.1089 106 MET A CG  
926  S SD  A MET A 105 ? 0.4962 0.4728 0.5173 -0.0879 0.1556  -0.1286 106 MET A SD  
927  S SD  B MET A 105 ? 0.5037 0.4769 0.5228 -0.0883 0.1570  -0.1293 106 MET A SD  
928  C CE  A MET A 105 ? 0.4801 0.4397 0.4880 -0.0959 0.1685  -0.1373 106 MET A CE  
929  C CE  B MET A 105 ? 0.4563 0.4413 0.5081 -0.0666 0.1554  -0.1340 106 MET A CE  
930  N N   . ALA A 106 ? 0.3957 0.2998 0.3376 -0.0899 0.1223  -0.0871 107 ALA A N   
931  C CA  . ALA A 106 ? 0.3995 0.2947 0.3423 -0.0850 0.1214  -0.0864 107 ALA A CA  
932  C C   . ALA A 106 ? 0.4017 0.2951 0.3448 -0.0772 0.1080  -0.0748 107 ALA A C   
933  O O   . ALA A 106 ? 0.3771 0.2699 0.3328 -0.0673 0.1069  -0.0730 107 ALA A O   
934  C CB  . ALA A 106 ? 0.4361 0.3162 0.3551 -0.0984 0.1269  -0.0912 107 ALA A CB  
935  N N   . THR A 107 ? 0.3540 0.2457 0.2830 -0.0814 0.0984  -0.0674 108 THR A N   
936  C CA  . THR A 107 ? 0.3435 0.2360 0.2741 -0.0750 0.0864  -0.0582 108 THR A CA  
937  C C   . THR A 107 ? 0.3724 0.2772 0.3242 -0.0628 0.0833  -0.0542 108 THR A C   
938  O O   . THR A 107 ? 0.3388 0.2429 0.2975 -0.0554 0.0792  -0.0499 108 THR A O   
939  C CB  . THR A 107 ? 0.4255 0.3130 0.3368 -0.0811 0.0766  -0.0527 108 THR A CB  
940  O OG1 . THR A 107 ? 0.4211 0.2966 0.3102 -0.0923 0.0794  -0.0569 108 THR A OG1 
941  C CG2 . THR A 107 ? 0.4014 0.2909 0.3152 -0.0757 0.0653  -0.0461 108 THR A CG2 
942  N N   . ALA A 108 ? 0.3204 0.2362 0.2812 -0.0616 0.0856  -0.0564 109 ALA A N   
943  C CA  . ALA A 108 ? 0.2942 0.2238 0.2745 -0.0502 0.0817  -0.0536 109 ALA A CA  
944  C C   . ALA A 108 ? 0.3298 0.2607 0.3259 -0.0394 0.0856  -0.0566 109 ALA A C   
945  O O   . ALA A 108 ? 0.3066 0.2400 0.3112 -0.0288 0.0795  -0.0508 109 ALA A O   
946  C CB  . ALA A 108 ? 0.2951 0.2377 0.2819 -0.0533 0.0846  -0.0580 109 ALA A CB  
947  N N   . MET A 109 ? 0.3067 0.2333 0.3044 -0.0418 0.0957  -0.0654 110 MET A N   
948  C CA  . MET A 109 ? 0.3069 0.2307 0.3182 -0.0303 0.0992  -0.0683 110 MET A CA  
949  C C   . MET A 109 ? 0.3514 0.2582 0.3532 -0.0274 0.0952  -0.0608 110 MET A C   
950  O O   . MET A 109 ? 0.3584 0.2619 0.3675 -0.0155 0.0914  -0.0561 110 MET A O   
951  C CB  . MET A 109 ? 0.3532 0.2750 0.3678 -0.0345 0.1119  -0.0806 110 MET A CB  
952  C CG  . MET A 109 ? 0.4078 0.3494 0.4385 -0.0348 0.1175  -0.0903 110 MET A CG  
953  S SD  . MET A 109 ? 0.4993 0.4384 0.5301 -0.0444 0.1345  -0.1065 110 MET A SD  
954  C CE  . MET A 109 ? 0.4716 0.4036 0.5196 -0.0267 0.1366  -0.1099 110 MET A CE  
955  N N   . TYR A 110 ? 0.3443 0.2404 0.3287 -0.0388 0.0956  -0.0600 111 TYR A N   
956  C CA  . TYR A 110 ? 0.3523 0.2344 0.3274 -0.0398 0.0932  -0.0553 111 TYR A CA  
957  C C   . TYR A 110 ? 0.3688 0.2553 0.3458 -0.0342 0.0831  -0.0455 111 TYR A C   
958  O O   . TYR A 110 ? 0.3505 0.2276 0.3279 -0.0283 0.0824  -0.0414 111 TYR A O   
959  C CB  . TYR A 110 ? 0.3680 0.2441 0.3258 -0.0539 0.0938  -0.0581 111 TYR A CB  
960  C CG  . TYR A 110 ? 0.3729 0.2407 0.3224 -0.0576 0.0900  -0.0549 111 TYR A CG  
961  C CD1 . TYR A 110 ? 0.4092 0.2623 0.3568 -0.0582 0.0970  -0.0581 111 TYR A CD1 
962  C CD2 . TYR A 110 ? 0.3618 0.2363 0.3054 -0.0616 0.0804  -0.0502 111 TYR A CD2 
963  C CE1 . TYR A 110 ? 0.3793 0.2261 0.3196 -0.0641 0.0951  -0.0571 111 TYR A CE1 
964  C CE2 . TYR A 110 ? 0.3574 0.2282 0.2959 -0.0663 0.0776  -0.0500 111 TYR A CE2 
965  C CZ  . TYR A 110 ? 0.3954 0.2529 0.3322 -0.0685 0.0855  -0.0538 111 TYR A CZ  
966  O OH  . TYR A 110 ? 0.3787 0.2341 0.3112 -0.0752 0.0842  -0.0554 111 TYR A OH  
967  N N   . LEU A 111 ? 0.3105 0.2095 0.2872 -0.0365 0.0762  -0.0422 112 LEU A N   
968  C CA  . LEU A 111 ? 0.2880 0.1926 0.2665 -0.0322 0.0674  -0.0344 112 LEU A CA  
969  C C   . LEU A 111 ? 0.3317 0.2428 0.3229 -0.0199 0.0652  -0.0312 112 LEU A C   
970  O O   . LEU A 111 ? 0.3167 0.2303 0.3081 -0.0159 0.0588  -0.0248 112 LEU A O   
971  C CB  . LEU A 111 ? 0.2661 0.1796 0.2394 -0.0382 0.0610  -0.0327 112 LEU A CB  
972  C CG  . LEU A 111 ? 0.3098 0.2171 0.2685 -0.0484 0.0589  -0.0342 112 LEU A CG  
973  C CD1 . LEU A 111 ? 0.3136 0.2265 0.2661 -0.0513 0.0511  -0.0314 112 LEU A CD1 
974  C CD2 . LEU A 111 ? 0.3345 0.2362 0.2908 -0.0496 0.0570  -0.0330 112 LEU A CD2 
975  N N   . GLN A 112 ? 0.3041 0.2202 0.3063 -0.0139 0.0698  -0.0366 113 GLN A N   
976  C CA  . GLN A 112 ? 0.3124 0.2377 0.3284 -0.0007 0.0662  -0.0352 113 GLN A CA  
977  C C   . GLN A 112 ? 0.3301 0.2729 0.3508 -0.0012 0.0591  -0.0325 113 GLN A C   
978  O O   . GLN A 112 ? 0.3012 0.2459 0.3212 0.0042  0.0520  -0.0257 113 GLN A O   
979  C CB  . GLN A 112 ? 0.3391 0.2493 0.3512 0.0091  0.0637  -0.0286 113 GLN A CB  
980  C CG  . GLN A 112 ? 0.3702 0.2598 0.3769 0.0097  0.0718  -0.0318 113 GLN A CG  
981  C CD  . GLN A 112 ? 0.4973 0.3660 0.4923 0.0143  0.0703  -0.0240 113 GLN A CD  
982  O OE1 . GLN A 112 ? 0.4191 0.2883 0.4134 0.0227  0.0634  -0.0170 113 GLN A OE1 
983  N NE2 . GLN A 112 ? 0.4691 0.3181 0.4527 0.0073  0.0773  -0.0254 113 GLN A NE2 
984  N N   . MET A 113 ? 0.2848 0.2382 0.3077 -0.0091 0.0621  -0.0383 114 MET A N   
985  C CA  . MET A 113 ? 0.2748 0.2429 0.3010 -0.0121 0.0577  -0.0377 114 MET A CA  
986  C C   . MET A 113 ? 0.3351 0.3200 0.3776 -0.0102 0.0627  -0.0474 114 MET A C   
987  O O   . MET A 113 ? 0.3145 0.3015 0.3548 -0.0203 0.0702  -0.0547 114 MET A O   
988  C CB  . MET A 113 ? 0.2939 0.2547 0.3042 -0.0248 0.0578  -0.0364 114 MET A CB  
989  C CG  . MET A 113 ? 0.3104 0.2600 0.3093 -0.0257 0.0519  -0.0290 114 MET A CG  
990  S SD  . MET A 113 ? 0.3428 0.2839 0.3237 -0.0376 0.0498  -0.0284 114 MET A SD  
991  C CE  . MET A 113 ? 0.3042 0.2557 0.2875 -0.0382 0.0444  -0.0263 114 MET A CE  
992  N N   . GLU A 114 ? 0.3294 0.3254 0.3877 0.0030  0.0589  -0.0484 115 GLU A N   
993  C CA  . GLU A 114 ? 0.3435 0.3589 0.4228 0.0084  0.0628  -0.0595 115 GLU A CA  
994  C C   . GLU A 114 ? 0.3509 0.3850 0.4371 -0.0019 0.0666  -0.0677 115 GLU A C   
995  O O   . GLU A 114 ? 0.3404 0.3849 0.4378 -0.0058 0.0757  -0.0795 115 GLU A O   
996  C CB  . GLU A 114 ? 0.3774 0.4021 0.4711 0.0264  0.0543  -0.0578 115 GLU A CB  
997  C CG  . GLU A 114 ? 0.5559 0.5582 0.6415 0.0367  0.0525  -0.0510 115 GLU A CG  
998  N N   . HIS A 115 ? 0.2952 0.3331 0.3750 -0.0070 0.0611  -0.0626 116 HIS A N   
999  C CA  . HIS A 115 ? 0.3115 0.3640 0.3958 -0.0181 0.0659  -0.0708 116 HIS A CA  
1000 C C   . HIS A 115 ? 0.3400 0.3783 0.4077 -0.0344 0.0764  -0.0743 116 HIS A C   
1001 O O   . HIS A 115 ? 0.3468 0.3958 0.4208 -0.0436 0.0860  -0.0856 116 HIS A O   
1002 C CB  . HIS A 115 ? 0.3304 0.3886 0.4115 -0.0194 0.0580  -0.0653 116 HIS A CB  
1003 C CG  . HIS A 115 ? 0.3806 0.4559 0.4775 -0.0051 0.0483  -0.0642 116 HIS A CG  
1004 N ND1 . HIS A 115 ? 0.4102 0.5113 0.5309 0.0015  0.0486  -0.0752 116 HIS A ND1 
1005 C CD2 . HIS A 115 ? 0.4022 0.4724 0.4930 0.0030  0.0381  -0.0539 116 HIS A CD2 
1006 C CE1 . HIS A 115 ? 0.4019 0.5113 0.5286 0.0146  0.0371  -0.0703 116 HIS A CE1 
1007 N NE2 . HIS A 115 ? 0.4020 0.4925 0.5099 0.0151  0.0312  -0.0573 116 HIS A NE2 
1008 N N   . VAL A 116 ? 0.2848 0.2995 0.3309 -0.0382 0.0749  -0.0656 117 VAL A N   
1009 C CA  . VAL A 116 ? 0.2973 0.2955 0.3235 -0.0524 0.0830  -0.0678 117 VAL A CA  
1010 C C   . VAL A 116 ? 0.3649 0.3659 0.3987 -0.0543 0.0942  -0.0785 117 VAL A C   
1011 O O   . VAL A 116 ? 0.3421 0.3431 0.3703 -0.0671 0.1049  -0.0873 117 VAL A O   
1012 C CB  . VAL A 116 ? 0.3342 0.3098 0.3376 -0.0546 0.0769  -0.0572 117 VAL A CB  
1013 C CG1 . VAL A 116 ? 0.3431 0.3015 0.3244 -0.0681 0.0840  -0.0599 117 VAL A CG1 
1014 C CG2 . VAL A 116 ? 0.3265 0.3004 0.3235 -0.0540 0.0673  -0.0490 117 VAL A CG2 
1015 N N   . VAL A 117 ? 0.3155 0.3175 0.3613 -0.0420 0.0928  -0.0785 118 VAL A N   
1016 C CA  . VAL A 117 ? 0.3229 0.3277 0.3787 -0.0416 0.1034  -0.0896 118 VAL A CA  
1017 C C   . VAL A 117 ? 0.3818 0.4117 0.4589 -0.0440 0.1113  -0.1040 118 VAL A C   
1018 O O   . VAL A 117 ? 0.3741 0.4044 0.4488 -0.0558 0.1241  -0.1149 118 VAL A O   
1019 C CB  . VAL A 117 ? 0.3563 0.3564 0.4221 -0.0258 0.0997  -0.0870 118 VAL A CB  
1020 C CG1 . VAL A 117 ? 0.3625 0.3653 0.4403 -0.0244 0.1112  -0.0999 118 VAL A CG1 
1021 C CG2 . VAL A 117 ? 0.3518 0.3283 0.3965 -0.0268 0.0944  -0.0753 118 VAL A CG2 
1022 N N   A ASP A 118 ? 0.3470 0.3986 0.4454 -0.0332 0.1040  -0.1051 119 ASP A N   
1023 N N   B ASP A 118 ? 0.3353 0.3859 0.4310 -0.0352 0.1039  -0.1043 119 ASP A N   
1024 C CA  A ASP A 118 ? 0.3485 0.4296 0.4723 -0.0338 0.1096  -0.1201 119 ASP A CA  
1025 C CA  B ASP A 118 ? 0.3275 0.4069 0.4468 -0.0371 0.1094  -0.1187 119 ASP A CA  
1026 C C   A ASP A 118 ? 0.4050 0.4881 0.5188 -0.0550 0.1214  -0.1285 119 ASP A C   
1027 C C   B ASP A 118 ? 0.3630 0.4410 0.4690 -0.0588 0.1210  -0.1258 119 ASP A C   
1028 O O   A ASP A 118 ? 0.4109 0.5104 0.5395 -0.0616 0.1336  -0.1446 119 ASP A O   
1029 O O   B ASP A 118 ? 0.3548 0.4451 0.4716 -0.0670 0.1341  -0.1411 119 ASP A O   
1030 C CB  A ASP A 118 ? 0.3617 0.4639 0.5043 -0.0201 0.0969  -0.1177 119 ASP A CB  
1031 C CB  B ASP A 118 ? 0.3404 0.4401 0.4770 -0.0245 0.0968  -0.1158 119 ASP A CB  
1032 C CG  A ASP A 118 ? 0.5157 0.6229 0.6751 0.0021  0.0878  -0.1156 119 ASP A CG  
1033 C CG  B ASP A 118 ? 0.5004 0.6350 0.6663 -0.0240 0.1007  -0.1324 119 ASP A CG  
1034 O OD1 A ASP A 118 ? 0.5568 0.6663 0.7289 0.0084  0.0941  -0.1244 119 ASP A OD1 
1035 O OD1 B ASP A 118 ? 0.5240 0.6742 0.7123 -0.0168 0.1060  -0.1450 119 ASP A OD1 
1036 O OD2 A ASP A 118 ? 0.5869 0.6942 0.7454 0.0133  0.0747  -0.1053 119 ASP A OD2 
1037 O OD2 B ASP A 118 ? 0.5644 0.7116 0.7320 -0.0307 0.0984  -0.1338 119 ASP A OD2 
1038 N N   A THR A 119 ? 0.3562 0.4212 0.4439 -0.0658 0.1183  -0.1181 120 THR A N   
1039 N N   B THR A 119 ? 0.3115 0.3729 0.3931 -0.0685 0.1169  -0.1154 120 THR A N   
1040 C CA  A THR A 119 ? 0.3656 0.4244 0.4364 -0.0864 0.1287  -0.1235 120 THR A CA  
1041 C CA  B THR A 119 ? 0.3255 0.3794 0.3894 -0.0892 0.1279  -0.1210 120 THR A CA  
1042 C C   A THR A 119 ? 0.4078 0.4460 0.4567 -0.0998 0.1408  -0.1269 120 THR A C   
1043 C C   B THR A 119 ? 0.3879 0.4207 0.4297 -0.1023 0.1398  -0.1242 120 THR A C   
1044 O O   A THR A 119 ? 0.4125 0.4554 0.4599 -0.1150 0.1552  -0.1397 120 THR A O   
1045 O O   B THR A 119 ? 0.3884 0.4198 0.4211 -0.1194 0.1532  -0.1342 120 THR A O   
1046 C CB  A THR A 119 ? 0.4582 0.5031 0.5093 -0.0903 0.1200  -0.1111 120 THR A CB  
1047 C CB  B THR A 119 ? 0.3541 0.3936 0.3973 -0.0949 0.1204  -0.1097 120 THR A CB  
1048 O OG1 A THR A 119 ? 0.4296 0.4974 0.5037 -0.0783 0.1106  -0.1109 120 THR A OG1 
1049 O OG1 B THR A 119 ? 0.3563 0.3937 0.3887 -0.1137 0.1322  -0.1182 120 THR A OG1 
1050 C CG2 A THR A 119 ? 0.4669 0.5016 0.4983 -0.1107 0.1302  -0.1158 120 THR A CG2 
1051 C CG2 B THR A 119 ? 0.2758 0.2841 0.2893 -0.0948 0.1130  -0.0946 120 THR A CG2 
1052 N N   . CYS A 120 ? 0.3565 0.3721 0.3876 -0.0956 0.1355  -0.1164 121 CYS A N   
1053 C CA  . CYS A 120 ? 0.3809 0.3765 0.3899 -0.1075 0.1456  -0.1195 121 CYS A CA  
1054 C C   . CYS A 120 ? 0.4512 0.4650 0.4818 -0.1096 0.1602  -0.1374 121 CYS A C   
1055 O O   . CYS A 120 ? 0.4467 0.4546 0.4638 -0.1270 0.1747  -0.1473 121 CYS A O   
1056 C CB  . CYS A 120 ? 0.3788 0.3557 0.3751 -0.0993 0.1368  -0.1083 121 CYS A CB  
1057 S SG  . CYS A 120 ? 0.4286 0.3815 0.3943 -0.1014 0.1227  -0.0905 121 CYS A SG  
1058 N N   . ARG A 121 ? 0.4155 0.4511 0.4795 -0.0917 0.1562  -0.1421 122 ARG A N   
1059 C CA  . ARG A 121 ? 0.4227 0.4801 0.5145 -0.0890 0.1680  -0.1605 122 ARG A CA  
1060 C C   . ARG A 121 ? 0.4674 0.5461 0.5701 -0.1037 0.1807  -0.1765 122 ARG A C   
1061 O O   . ARG A 121 ? 0.4623 0.5459 0.5676 -0.1157 0.1974  -0.1921 122 ARG A O   
1062 C CB  . ARG A 121 ? 0.4269 0.5037 0.5517 -0.0645 0.1576  -0.1608 122 ARG A CB  
1063 C CG  . ARG A 121 ? 0.6405 0.6971 0.7586 -0.0519 0.1516  -0.1515 122 ARG A CG  
1064 C CD  . ARG A 121 ? 0.8159 0.8881 0.9655 -0.0335 0.1523  -0.1616 122 ARG A CD  
1065 N NE  . ARG A 121 ? 0.9226 0.9934 1.0804 -0.0123 0.1360  -0.1496 122 ARG A NE  
1066 C CZ  . ARG A 121 ? 1.0496 1.0958 1.1943 -0.0036 0.1303  -0.1382 122 ARG A CZ  
1067 N NH1 . ARG A 121 ? 0.8253 0.8485 0.9499 -0.0137 0.1387  -0.1378 122 ARG A NH1 
1068 N NH2 . ARG A 121 ? 0.8866 0.9303 1.0364 0.0141  0.1166  -0.1278 122 ARG A NH2 
1069 N N   . LYS A 122 ? 0.4319 0.5227 0.5397 -0.1041 0.1739  -0.1733 123 LYS A N   
1070 C CA  . LYS A 122 ? 0.4401 0.5515 0.5582 -0.1190 0.1853  -0.1883 123 LYS A CA  
1071 C C   . LYS A 122 ? 0.5045 0.5902 0.5857 -0.1453 0.1998  -0.1897 123 LYS A C   
1072 O O   . LYS A 122 ? 0.5047 0.6026 0.5922 -0.1609 0.2174  -0.2076 123 LYS A O   
1073 C CB  . LYS A 122 ? 0.4492 0.5765 0.5788 -0.1130 0.1733  -0.1833 123 LYS A CB  
1074 C CG  . LYS A 122 ? 0.6472 0.8057 0.8155 -0.0891 0.1610  -0.1864 123 LYS A CG  
1075 C CD  . LYS A 122 ? 0.7789 0.9584 0.9603 -0.0868 0.1521  -0.1864 123 LYS A CD  
1076 C CE  . LYS A 122 ? 0.8920 1.0879 1.0957 -0.0614 0.1336  -0.1798 123 LYS A CE  
1077 N NZ  . LYS A 122 ? 0.9747 1.1999 1.2152 -0.0456 0.1338  -0.1945 123 LYS A NZ  
1078 N N   . PHE A 123 ? 0.4666 0.5165 0.5086 -0.1503 0.1925  -0.1715 124 PHE A N   
1079 C CA  . PHE A 123 ? 0.4938 0.5127 0.4941 -0.1734 0.2033  -0.1699 124 PHE A CA  
1080 C C   . PHE A 123 ? 0.5571 0.5665 0.5467 -0.1831 0.2178  -0.1795 124 PHE A C   
1081 O O   . PHE A 123 ? 0.5652 0.5653 0.5354 -0.2049 0.2347  -0.1896 124 PHE A O   
1082 C CB  . PHE A 123 ? 0.5187 0.5040 0.4834 -0.1718 0.1888  -0.1485 124 PHE A CB  
1083 C CG  . PHE A 123 ? 0.5394 0.5215 0.4972 -0.1746 0.1822  -0.1416 124 PHE A CG  
1084 C CD1 . PHE A 123 ? 0.5552 0.5683 0.5473 -0.1642 0.1766  -0.1459 124 PHE A CD1 
1085 C CD2 . PHE A 123 ? 0.5935 0.5400 0.5095 -0.1862 0.1802  -0.1305 124 PHE A CD2 
1086 C CE1 . PHE A 123 ? 0.5601 0.5697 0.5453 -0.1676 0.1712  -0.1405 124 PHE A CE1 
1087 C CE2 . PHE A 123 ? 0.6185 0.5598 0.5280 -0.1881 0.1745  -0.1245 124 PHE A CE2 
1088 C CZ  . PHE A 123 ? 0.5643 0.5374 0.5087 -0.1796 0.1708  -0.1300 124 PHE A CZ  
1089 N N   . ILE A 124 ? 0.4922 0.5041 0.4944 -0.1679 0.2125  -0.1777 125 ILE A N   
1090 C CA  . ILE A 124 ? 0.5146 0.5197 0.5102 -0.1758 0.2264  -0.1883 125 ILE A CA  
1091 C C   . ILE A 124 ? 0.5844 0.6205 0.6115 -0.1824 0.2449  -0.2129 125 ILE A C   
1092 O O   . ILE A 124 ? 0.6040 0.6318 0.6142 -0.2023 0.2632  -0.2249 125 ILE A O   
1093 C CB  . ILE A 124 ? 0.5405 0.5381 0.5408 -0.1585 0.2164  -0.1803 125 ILE A CB  
1094 C CG1 . ILE A 124 ? 0.5424 0.5075 0.5054 -0.1591 0.2027  -0.1600 125 ILE A CG1 
1095 C CG2 . ILE A 124 ? 0.5789 0.5764 0.5825 -0.1640 0.2320  -0.1952 125 ILE A CG2 
1096 C CD1 . ILE A 124 ? 0.5929 0.5543 0.5644 -0.1403 0.1891  -0.1498 125 ILE A CD1 
1097 N N   . LYS A 125 ? 0.5368 0.6092 0.6088 -0.1661 0.2399  -0.2209 126 LYS A N   
1098 C CA  . LYS A 125 ? 0.5436 0.6531 0.6541 -0.1683 0.2546  -0.2459 126 LYS A CA  
1099 C C   . LYS A 125 ? 0.6095 0.7233 0.7088 -0.1950 0.2720  -0.2589 126 LYS A C   
1100 O O   . LYS A 125 ? 0.6041 0.7343 0.7165 -0.2080 0.2919  -0.2807 126 LYS A O   
1101 C CB  . LYS A 125 ? 0.5595 0.7050 0.7165 -0.1432 0.2408  -0.2488 126 LYS A CB  
1102 C CG  . LYS A 125 ? 0.7599 0.9453 0.9631 -0.1367 0.2516  -0.2743 126 LYS A CG  
1103 C CD  . LYS A 125 ? 0.8928 1.1151 1.1382 -0.1148 0.2369  -0.2778 126 LYS A CD  
1104 C CE  . LYS A 125 ? 1.0478 1.3143 1.3414 -0.1091 0.2471  -0.3056 126 LYS A CE  
1105 N NZ  . LYS A 125 ? 1.1579 1.4622 1.4903 -0.0895 0.2317  -0.3098 126 LYS A NZ  
1106 N N   . ALA A 126 ? 0.5652 0.6624 0.6390 -0.2040 0.2658  -0.2461 127 ALA A N   
1107 C CA  . ALA A 126 ? 0.5898 0.6834 0.6462 -0.2306 0.2819  -0.2558 127 ALA A CA  
1108 C C   . ALA A 126 ? 0.6947 0.7541 0.7066 -0.2559 0.3001  -0.2587 127 ALA A C   
1109 O O   . ALA A 126 ? 0.7075 0.7709 0.7133 -0.2795 0.3207  -0.2752 127 ALA A O   
1110 C CB  . ALA A 126 ? 0.5893 0.6670 0.6256 -0.2316 0.2691  -0.2391 127 ALA A CB  
1111 N N   . SER A 127 ? 0.6944 0.7204 0.6743 -0.2521 0.2928  -0.2432 128 SER A N   
1112 C CA  . SER A 127 ? 0.7532 0.7436 0.6861 -0.2742 0.3068  -0.2435 128 SER A CA  
1113 C C   . SER A 127 ? 0.8392 0.8433 0.7873 -0.2795 0.3247  -0.2635 128 SER A C   
1114 O O   . SER A 127 ? 0.8880 0.8683 0.8000 -0.3025 0.3414  -0.2694 128 SER A O   
1115 C CB  . SER A 127 ? 0.8289 0.7784 0.7194 -0.2684 0.2895  -0.2186 128 SER A CB  
1116 O OG  . SER A 127 ? 0.9984 0.9220 0.8561 -0.2757 0.2817  -0.2039 128 SER A OG  
1117 N N   . GLU A 128 ? 0.7597 0.8004 0.7590 -0.2585 0.3215  -0.2742 129 GLU A N   
1118 C CA  . GLU A 128 ? 1.0053 1.0613 1.0246 -0.2603 0.3378  -0.2944 129 GLU A CA  
1119 C C   . GLU A 128 ? 1.5267 1.6132 1.5700 -0.2784 0.3622  -0.3230 129 GLU A C   
1120 O O   . GLU A 128 ? 1.1335 1.2053 1.1466 -0.3049 0.3766  -0.3272 129 GLU A O   
1121 C CB  . GLU A 128 ? 0.9912 1.0680 1.0516 -0.2295 0.3241  -0.2936 129 GLU A CB  
1122 C CG  . GLU A 128 ? 1.0802 1.2045 1.1990 -0.2112 0.3202  -0.3072 129 GLU A CG  
1123 C CD  . GLU A 128 ? 1.3144 1.4527 1.4677 -0.1788 0.3032  -0.3021 129 GLU A CD  
1124 O OE1 . GLU A 128 ? 1.1981 1.3080 1.3297 -0.1690 0.2914  -0.2842 129 GLU A OE1 
1125 O OE2 . GLU A 128 ? 1.2166 1.3942 1.4181 -0.1632 0.3015  -0.3165 129 GLU A OE2 
1129 N N   A TRP B 2   ? 0.2025 0.4353 0.2973 -0.0652 -0.0150 -0.0787 1   TRP D N   
1130 N N   B TRP B 2   ? 0.2059 0.4387 0.3007 -0.0652 -0.0150 -0.0787 1   TRP D N   
1131 C CA  A TRP B 2   ? 0.1918 0.4249 0.2873 -0.0651 -0.0142 -0.0792 1   TRP D CA  
1132 C CA  B TRP B 2   ? 0.1955 0.4286 0.2910 -0.0651 -0.0142 -0.0792 1   TRP D CA  
1133 C C   A TRP B 2   ? 0.2409 0.4738 0.3375 -0.0655 -0.0141 -0.0784 1   TRP D C   
1134 C C   B TRP B 2   ? 0.2356 0.4685 0.3322 -0.0655 -0.0141 -0.0784 1   TRP D C   
1135 O O   A TRP B 2   ? 0.2523 0.4845 0.3491 -0.0656 -0.0147 -0.0779 1   TRP D O   
1136 O O   B TRP B 2   ? 0.2327 0.4650 0.3295 -0.0657 -0.0146 -0.0779 1   TRP D O   
1137 C CB  A TRP B 2   ? 0.1739 0.4066 0.2690 -0.0647 -0.0150 -0.0801 1   TRP D CB  
1138 C CB  B TRP B 2   ? 0.1773 0.4101 0.2726 -0.0647 -0.0151 -0.0800 1   TRP D CB  
1139 C CG  A TRP B 2   ? 0.1781 0.4111 0.2721 -0.0644 -0.0151 -0.0820 1   TRP D CG  
1140 C CG  B TRP B 2   ? 0.1869 0.4196 0.2835 -0.0646 -0.0162 -0.0796 1   TRP D CG  
1141 C CD1 A TRP B 2   ? 0.2113 0.4440 0.3051 -0.0641 -0.0165 -0.0831 1   TRP D CD1 
1142 C CD1 B TRP B 2   ? 0.2251 0.4580 0.3229 -0.0644 -0.0178 -0.0799 1   TRP D CD1 
1143 C CD2 A TRP B 2   ? 0.1755 0.4091 0.2688 -0.0645 -0.0137 -0.0835 1   TRP D CD2 
1144 C CD2 B TRP B 2   ? 0.1827 0.4158 0.2802 -0.0645 -0.0160 -0.0791 1   TRP D CD2 
1145 N NE1 A TRP B 2   ? 0.2028 0.4359 0.2954 -0.0637 -0.0160 -0.0857 1   TRP D NE1 
1146 N NE1 B TRP B 2   ? 0.2179 0.4517 0.3179 -0.0642 -0.0182 -0.0798 1   TRP D NE1 
1147 C CE2 A TRP B 2   ? 0.2167 0.4505 0.3090 -0.0641 -0.0142 -0.0860 1   TRP D CE2 
1148 C CE2 B TRP B 2   ? 0.2321 0.4660 0.3316 -0.0641 -0.0171 -0.0793 1   TRP D CE2 
1149 C CE3 A TRP B 2   ? 0.1844 0.4182 0.2779 -0.0648 -0.0123 -0.0831 1   TRP D CE3 
1150 C CE3 B TRP B 2   ? 0.1953 0.4279 0.2925 -0.0645 -0.0153 -0.0787 1   TRP D CE3 
1151 C CZ2 A TRP B 2   ? 0.2061 0.4403 0.2973 -0.0640 -0.0128 -0.0886 1   TRP D CZ2 
1152 C CZ2 B TRP B 2   ? 0.2196 0.4546 0.3207 -0.0635 -0.0169 -0.0794 1   TRP D CZ2 
1153 C CZ3 A TRP B 2   ? 0.1922 0.4263 0.2848 -0.0650 -0.0110 -0.0850 1   TRP D CZ3 
1154 C CZ3 B TRP B 2   ? 0.2154 0.4484 0.3136 -0.0640 -0.0156 -0.0785 1   TRP D CZ3 
1155 C CH2 A TRP B 2   ? 0.2040 0.4384 0.2954 -0.0646 -0.0110 -0.0879 1   TRP D CH2 
1156 C CH2 B TRP B 2   ? 0.2203 0.4547 0.3203 -0.0634 -0.0162 -0.0790 1   TRP D CH2 
1157 N N   . VAL B 3   ? 0.1831 0.4165 0.2808 -0.0656 -0.0134 -0.0787 2   VAL D N   
1158 C CA  . VAL B 3   ? 0.1797 0.4128 0.2786 -0.0659 -0.0136 -0.0789 2   VAL D CA  
1159 C C   . VAL B 3   ? 0.2007 0.4329 0.3002 -0.0654 -0.0138 -0.0788 2   VAL D C   
1160 O O   . VAL B 3   ? 0.2000 0.4322 0.2990 -0.0653 -0.0135 -0.0786 2   VAL D O   
1161 C CB  . VAL B 3   ? 0.2170 0.4522 0.3178 -0.0670 -0.0131 -0.0798 2   VAL D CB  
1162 C CG1 . VAL B 3   ? 0.2101 0.4462 0.3097 -0.0679 -0.0129 -0.0793 2   VAL D CG1 
1163 C CG2 . VAL B 3   ? 0.2124 0.4498 0.3155 -0.0671 -0.0124 -0.0805 2   VAL D CG2 
1164 N N   . ILE B 4   ? 0.1743 0.4057 0.2747 -0.0652 -0.0144 -0.0793 3   ILE D N   
1165 C CA  . ILE B 4   ? 0.1902 0.4205 0.2912 -0.0649 -0.0152 -0.0791 3   ILE D CA  
1166 C C   . ILE B 4   ? 0.2307 0.4622 0.3349 -0.0656 -0.0152 -0.0803 3   ILE D C   
1167 O O   . ILE B 4   ? 0.2301 0.4626 0.3360 -0.0662 -0.0155 -0.0820 3   ILE D O   
1168 C CB  . ILE B 4   ? 0.2157 0.4447 0.3165 -0.0640 -0.0160 -0.0797 3   ILE D CB  
1169 C CG1 . ILE B 4   ? 0.1989 0.4286 0.2984 -0.0632 -0.0159 -0.0791 3   ILE D CG1 
1170 C CG2 . ILE B 4   ? 0.2382 0.4656 0.3395 -0.0636 -0.0173 -0.0794 3   ILE D CG2 
1171 C CD1 . ILE B 4   ? 0.2325 0.4629 0.3304 -0.0634 -0.0159 -0.0777 3   ILE D CD1 
1172 N N   . PRO B 5   ? 0.2173 0.4492 0.3227 -0.0658 -0.0149 -0.0799 4   PRO D N   
1173 C CA  . PRO B 5   ? 0.2213 0.4556 0.3315 -0.0665 -0.0150 -0.0815 4   PRO D CA  
1174 C C   . PRO B 5   ? 0.2740 0.5073 0.3871 -0.0665 -0.0170 -0.0828 4   PRO D C   
1175 O O   . PRO B 5   ? 0.2697 0.4996 0.3809 -0.0658 -0.0182 -0.0816 4   PRO D O   
1176 C CB  . PRO B 5   ? 0.2395 0.4744 0.3507 -0.0664 -0.0140 -0.0808 4   PRO D CB  
1177 C CG  . PRO B 5   ? 0.2890 0.5203 0.3957 -0.0659 -0.0141 -0.0788 4   PRO D CG  
1178 C CD  . PRO B 5   ? 0.2354 0.4661 0.3387 -0.0656 -0.0143 -0.0785 4   PRO D CD  
1179 N N   . ALA B 6   ? 0.2406 0.4772 0.3588 -0.0675 -0.0176 -0.0854 5   ALA D N   
# 
