data_9DAQ
# 
_entry.id   9DAQ 
# 
_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   9DAQ         pdb_00009daq 10.2210/pdb9daq/pdb 
WWPDB D_1000287598 ?            ?                   
# 
_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.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DAQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 jjez@wustl.edu      Joseph  Jez       M 'principal investigator/group leader' 0000-0001-7911-9108 
4 wencewicz@wustl.edu Timothy Wencewicz A 'principal investigator/group leader' 0000-0002-5839-6672 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Berkovich, D.A.' 1 ? 
'Jez, J.M.'       2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Infect Dis.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2373-8227 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Expanding the Landscape of Dual Action Antifolate Antibacterials through 2,4-Diamino-1,6-dihydro-1,3,5-triazines.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsinfecdis.4c00768 
_citation.pdbx_database_id_PubMed   39950956 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Georgiades, J.D.' 1  0009-0008-4783-1553 
primary 'Berkovich, D.A.'  2  0000-0002-4890-5971 
primary 'McKee, S.R.'      3  ?                   
primary 'Smith, A.R.'      4  ?                   
primary 'Sankaran, B.'     5  ?                   
primary 'Flentie, K.N.'    6  ?                   
primary 'Castaneda, C.H.'  7  ?                   
primary 'Grohmann, D.G.'   8  ?                   
primary 'Rohatgi, R.'      9  ?                   
primary 'Lasky, C.'        10 ?                   
primary 'Mason, T.A.'      11 ?                   
primary 'Champine, J.E.'   12 ?                   
primary 'Miller, P.A.'     13 ?                   
primary 'Mollmann, U.'     14 ?                   
primary 'Moraski, G.C.'    15 0000-0002-6992-5584 
primary 'Franzblau, S.G.'  16 0000-0002-8698-0243 
primary 'Miller, M.J.'     17 0000-0002-3704-8214 
primary 'Stallings, C.L.'  18 ?                   
primary 'Jez, J.M.'        19 ?                   
primary 'Hathaway, B.A.'   20 ?                   
primary 'Wencewicz, T.A.'  21 0000-0002-5839-6672 
# 
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 'Dihydrofolate reductase'                                                18244.568 1  1.5.1.3 ? ? ? 
2 non-polymer syn '(6S)-1-(4-chlorophenyl)-6-ethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine' 251.715   1  ?       ? ? ? 
3 water       nat water                                                                    18.015    16 ?       ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SHMISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSV
DEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILER
R
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SHMISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSV
DEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILER
R
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(6S)-1-(4-chlorophenyl)-6-ethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine' A1A3E 
3 water                                                                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   HIS n 
1 3   MET n 
1 4   ILE n 
1 5   SER n 
1 6   LEU n 
1 7   ILE n 
1 8   ALA n 
1 9   ALA n 
1 10  LEU n 
1 11  ALA n 
1 12  VAL n 
1 13  ASP n 
1 14  ARG n 
1 15  VAL n 
1 16  ILE n 
1 17  GLY n 
1 18  MET n 
1 19  GLU n 
1 20  ASN n 
1 21  ALA n 
1 22  MET n 
1 23  PRO n 
1 24  TRP n 
1 25  ASN n 
1 26  LEU n 
1 27  PRO n 
1 28  ALA n 
1 29  ASP n 
1 30  LEU n 
1 31  ALA n 
1 32  TRP n 
1 33  PHE n 
1 34  LYS n 
1 35  ARG n 
1 36  ASN n 
1 37  THR n 
1 38  LEU n 
1 39  ASN n 
1 40  LYS n 
1 41  PRO n 
1 42  VAL n 
1 43  ILE n 
1 44  MET n 
1 45  GLY n 
1 46  ARG n 
1 47  HIS n 
1 48  THR n 
1 49  TRP n 
1 50  GLU n 
1 51  SER n 
1 52  ILE n 
1 53  GLY n 
1 54  ARG n 
1 55  PRO n 
1 56  LEU n 
1 57  PRO n 
1 58  GLY n 
1 59  ARG n 
1 60  LYS n 
1 61  ASN n 
1 62  ILE n 
1 63  ILE n 
1 64  LEU n 
1 65  SER n 
1 66  SER n 
1 67  GLN n 
1 68  PRO n 
1 69  GLY n 
1 70  THR n 
1 71  ASP n 
1 72  ASP n 
1 73  ARG n 
1 74  VAL n 
1 75  THR n 
1 76  TRP n 
1 77  VAL n 
1 78  LYS n 
1 79  SER n 
1 80  VAL n 
1 81  ASP n 
1 82  GLU n 
1 83  ALA n 
1 84  ILE n 
1 85  ALA n 
1 86  ALA n 
1 87  CYS n 
1 88  GLY n 
1 89  ASP n 
1 90  VAL n 
1 91  PRO n 
1 92  GLU n 
1 93  ILE n 
1 94  MET n 
1 95  VAL n 
1 96  ILE n 
1 97  GLY n 
1 98  GLY n 
1 99  GLY n 
1 100 ARG n 
1 101 VAL n 
1 102 TYR n 
1 103 GLU n 
1 104 GLN n 
1 105 PHE n 
1 106 LEU n 
1 107 PRO n 
1 108 LYS n 
1 109 ALA n 
1 110 GLN n 
1 111 LYS n 
1 112 LEU n 
1 113 TYR n 
1 114 LEU n 
1 115 THR n 
1 116 HIS n 
1 117 ILE n 
1 118 ASP n 
1 119 ALA n 
1 120 GLU n 
1 121 VAL n 
1 122 GLU n 
1 123 GLY n 
1 124 ASP n 
1 125 THR n 
1 126 HIS n 
1 127 PHE n 
1 128 PRO n 
1 129 ASP n 
1 130 TYR n 
1 131 GLU n 
1 132 PRO n 
1 133 ASP n 
1 134 ASP n 
1 135 TRP n 
1 136 GLU n 
1 137 SER n 
1 138 VAL n 
1 139 PHE n 
1 140 SER n 
1 141 GLU n 
1 142 PHE n 
1 143 HIS n 
1 144 ASP n 
1 145 ALA n 
1 146 ASP n 
1 147 ALA n 
1 148 GLN n 
1 149 ASN n 
1 150 SER n 
1 151 HIS n 
1 152 SER n 
1 153 TYR n 
1 154 CYS n 
1 155 PHE n 
1 156 GLU n 
1 157 ILE n 
1 158 LEU n 
1 159 GLU n 
1 160 ARG n 
1 161 ARG 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                   161 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'folA, c0058' 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_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               ? 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_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_
_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 
A1A3E non-polymer         . '(6S)-1-(4-chlorophenyl)-6-ethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine' ? 'C11 H14 Cl N5'  251.715 
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 
CYS   'L-peptide linking' y CYSTEINE                                                                 ? 'C3 H7 N O2 S'   121.158 
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   SER 1   -1  -1  SER SER A . n 
A 1 2   HIS 2   0   0   HIS HIS A . n 
A 1 3   MET 3   1   1   MET MET A . n 
A 1 4   ILE 4   2   2   ILE ILE A . n 
A 1 5   SER 5   3   3   SER SER A . n 
A 1 6   LEU 6   4   4   LEU LEU A . n 
A 1 7   ILE 7   5   5   ILE ILE A . n 
A 1 8   ALA 8   6   6   ALA ALA A . n 
A 1 9   ALA 9   7   7   ALA ALA A . n 
A 1 10  LEU 10  8   8   LEU LEU A . n 
A 1 11  ALA 11  9   9   ALA ALA A . n 
A 1 12  VAL 12  10  10  VAL VAL A . n 
A 1 13  ASP 13  11  11  ASP ASP A . n 
A 1 14  ARG 14  12  12  ARG ARG A . n 
A 1 15  VAL 15  13  13  VAL VAL A . n 
A 1 16  ILE 16  14  14  ILE ILE A . n 
A 1 17  GLY 17  15  15  GLY GLY A . n 
A 1 18  MET 18  16  16  MET MET A . n 
A 1 19  GLU 19  17  17  GLU GLU A . n 
A 1 20  ASN 20  18  ?   ?   ?   A . n 
A 1 21  ALA 21  19  ?   ?   ?   A . n 
A 1 22  MET 22  20  ?   ?   ?   A . n 
A 1 23  PRO 23  21  ?   ?   ?   A . n 
A 1 24  TRP 24  22  ?   ?   ?   A . n 
A 1 25  ASN 25  23  ?   ?   ?   A . n 
A 1 26  LEU 26  24  24  LEU LEU A . n 
A 1 27  PRO 27  25  25  PRO PRO A . n 
A 1 28  ALA 28  26  26  ALA ALA A . n 
A 1 29  ASP 29  27  27  ASP ASP A . n 
A 1 30  LEU 30  28  28  LEU LEU A . n 
A 1 31  ALA 31  29  29  ALA ALA A . n 
A 1 32  TRP 32  30  30  TRP TRP A . n 
A 1 33  PHE 33  31  31  PHE PHE A . n 
A 1 34  LYS 34  32  32  LYS LYS A . n 
A 1 35  ARG 35  33  33  ARG ARG A . n 
A 1 36  ASN 36  34  34  ASN ASN A . n 
A 1 37  THR 37  35  35  THR THR A . n 
A 1 38  LEU 38  36  36  LEU LEU A . n 
A 1 39  ASN 39  37  37  ASN ASN A . n 
A 1 40  LYS 40  38  38  LYS LYS A . n 
A 1 41  PRO 41  39  39  PRO PRO A . n 
A 1 42  VAL 42  40  40  VAL VAL A . n 
A 1 43  ILE 43  41  41  ILE ILE A . n 
A 1 44  MET 44  42  42  MET MET A . n 
A 1 45  GLY 45  43  43  GLY GLY A . n 
A 1 46  ARG 46  44  44  ARG ARG A . n 
A 1 47  HIS 47  45  45  HIS HIS A . n 
A 1 48  THR 48  46  46  THR THR A . n 
A 1 49  TRP 49  47  47  TRP TRP A . n 
A 1 50  GLU 50  48  48  GLU GLU A . n 
A 1 51  SER 51  49  49  SER SER A . n 
A 1 52  ILE 52  50  50  ILE ILE A . n 
A 1 53  GLY 53  51  51  GLY GLY A . n 
A 1 54  ARG 54  52  52  ARG ARG A . n 
A 1 55  PRO 55  53  53  PRO PRO A . n 
A 1 56  LEU 56  54  54  LEU LEU A . n 
A 1 57  PRO 57  55  55  PRO PRO A . n 
A 1 58  GLY 58  56  56  GLY GLY A . n 
A 1 59  ARG 59  57  57  ARG ARG A . n 
A 1 60  LYS 60  58  58  LYS LYS A . n 
A 1 61  ASN 61  59  59  ASN ASN A . n 
A 1 62  ILE 62  60  60  ILE ILE A . n 
A 1 63  ILE 63  61  61  ILE ILE A . n 
A 1 64  LEU 64  62  62  LEU LEU A . n 
A 1 65  SER 65  63  63  SER SER A . n 
A 1 66  SER 66  64  64  SER SER A . n 
A 1 67  GLN 67  65  65  GLN GLN A . n 
A 1 68  PRO 68  66  66  PRO PRO A . n 
A 1 69  GLY 69  67  67  GLY GLY A . n 
A 1 70  THR 70  68  68  THR THR A . n 
A 1 71  ASP 71  69  69  ASP ASP A . n 
A 1 72  ASP 72  70  70  ASP ASP A . n 
A 1 73  ARG 73  71  71  ARG ARG A . n 
A 1 74  VAL 74  72  72  VAL VAL A . n 
A 1 75  THR 75  73  73  THR THR A . n 
A 1 76  TRP 76  74  74  TRP TRP A . n 
A 1 77  VAL 77  75  75  VAL VAL A . n 
A 1 78  LYS 78  76  76  LYS LYS A . n 
A 1 79  SER 79  77  77  SER SER A . n 
A 1 80  VAL 80  78  78  VAL VAL A . n 
A 1 81  ASP 81  79  79  ASP ASP A . n 
A 1 82  GLU 82  80  80  GLU GLU A . n 
A 1 83  ALA 83  81  81  ALA ALA A . n 
A 1 84  ILE 84  82  82  ILE ILE A . n 
A 1 85  ALA 85  83  83  ALA ALA A . n 
A 1 86  ALA 86  84  84  ALA ALA A . n 
A 1 87  CYS 87  85  85  CYS CYS A . n 
A 1 88  GLY 88  86  86  GLY GLY A . n 
A 1 89  ASP 89  87  87  ASP ASP A . n 
A 1 90  VAL 90  88  88  VAL VAL A . n 
A 1 91  PRO 91  89  89  PRO PRO A . n 
A 1 92  GLU 92  90  90  GLU GLU A . n 
A 1 93  ILE 93  91  91  ILE ILE A . n 
A 1 94  MET 94  92  92  MET MET A . n 
A 1 95  VAL 95  93  93  VAL VAL A . n 
A 1 96  ILE 96  94  94  ILE ILE A . n 
A 1 97  GLY 97  95  95  GLY GLY A . n 
A 1 98  GLY 98  96  96  GLY GLY A . n 
A 1 99  GLY 99  97  97  GLY GLY A . n 
A 1 100 ARG 100 98  98  ARG ARG A . n 
A 1 101 VAL 101 99  99  VAL VAL A . n 
A 1 102 TYR 102 100 100 TYR TYR A . n 
A 1 103 GLU 103 101 101 GLU GLU A . n 
A 1 104 GLN 104 102 102 GLN GLN A . n 
A 1 105 PHE 105 103 103 PHE PHE A . n 
A 1 106 LEU 106 104 104 LEU LEU A . n 
A 1 107 PRO 107 105 105 PRO PRO A . n 
A 1 108 LYS 108 106 106 LYS LYS A . n 
A 1 109 ALA 109 107 107 ALA ALA A . n 
A 1 110 GLN 110 108 108 GLN GLN A . n 
A 1 111 LYS 111 109 109 LYS LYS A . n 
A 1 112 LEU 112 110 110 LEU LEU A . n 
A 1 113 TYR 113 111 111 TYR TYR A . n 
A 1 114 LEU 114 112 112 LEU LEU A . n 
A 1 115 THR 115 113 113 THR THR A . n 
A 1 116 HIS 116 114 114 HIS HIS A . n 
A 1 117 ILE 117 115 115 ILE ILE A . n 
A 1 118 ASP 118 116 116 ASP ASP A . n 
A 1 119 ALA 119 117 117 ALA ALA A . n 
A 1 120 GLU 120 118 118 GLU GLU A . n 
A 1 121 VAL 121 119 119 VAL VAL A . n 
A 1 122 GLU 122 120 120 GLU GLU A . n 
A 1 123 GLY 123 121 121 GLY GLY A . n 
A 1 124 ASP 124 122 122 ASP ASP A . n 
A 1 125 THR 125 123 123 THR THR A . n 
A 1 126 HIS 126 124 124 HIS HIS A . n 
A 1 127 PHE 127 125 125 PHE PHE A . n 
A 1 128 PRO 128 126 126 PRO PRO A . n 
A 1 129 ASP 129 127 127 ASP ASP A . n 
A 1 130 TYR 130 128 128 TYR TYR A . n 
A 1 131 GLU 131 129 129 GLU GLU A . n 
A 1 132 PRO 132 130 130 PRO PRO A . n 
A 1 133 ASP 133 131 131 ASP ASP A . n 
A 1 134 ASP 134 132 132 ASP ASP A . n 
A 1 135 TRP 135 133 133 TRP TRP A . n 
A 1 136 GLU 136 134 134 GLU GLU A . n 
A 1 137 SER 137 135 135 SER SER A . n 
A 1 138 VAL 138 136 136 VAL VAL A . n 
A 1 139 PHE 139 137 137 PHE PHE A . n 
A 1 140 SER 140 138 138 SER SER A . n 
A 1 141 GLU 141 139 139 GLU GLU A . n 
A 1 142 PHE 142 140 140 PHE PHE A . n 
A 1 143 HIS 143 141 141 HIS HIS A . n 
A 1 144 ASP 144 142 142 ASP ASP A . n 
A 1 145 ALA 145 143 143 ALA ALA A . n 
A 1 146 ASP 146 144 144 ASP ASP A . n 
A 1 147 ALA 147 145 145 ALA ALA A . n 
A 1 148 GLN 148 146 146 GLN GLN A . n 
A 1 149 ASN 149 147 147 ASN ASN A . n 
A 1 150 SER 150 148 148 SER SER A . n 
A 1 151 HIS 151 149 149 HIS HIS A . n 
A 1 152 SER 152 150 150 SER SER A . n 
A 1 153 TYR 153 151 151 TYR TYR A . n 
A 1 154 CYS 154 152 152 CYS CYS A . n 
A 1 155 PHE 155 153 153 PHE PHE A . n 
A 1 156 GLU 156 154 154 GLU GLU A . n 
A 1 157 ILE 157 155 155 ILE ILE A . n 
A 1 158 LEU 158 156 156 LEU LEU A . n 
A 1 159 GLU 159 157 157 GLU GLU A . n 
A 1 160 ARG 160 158 158 ARG ARG A . n 
A 1 161 ARG 161 159 159 ARG ARG A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A3E 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A3E 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
B 2 A1A3E 1  201 201 A1A3E E3D A . 
C 3 HOH   1  301 312 HOH   HOH A . 
C 3 HOH   2  302 304 HOH   HOH A . 
C 3 HOH   3  303 301 HOH   HOH A . 
C 3 HOH   4  304 314 HOH   HOH A . 
C 3 HOH   5  305 305 HOH   HOH A . 
C 3 HOH   6  306 306 HOH   HOH A . 
C 3 HOH   7  307 313 HOH   HOH A . 
C 3 HOH   8  308 307 HOH   HOH A . 
C 3 HOH   9  309 302 HOH   HOH A . 
C 3 HOH   10 310 309 HOH   HOH A . 
C 3 HOH   11 311 315 HOH   HOH A . 
C 3 HOH   12 312 316 HOH   HOH A . 
C 3 HOH   13 313 310 HOH   HOH A . 
C 3 HOH   14 314 311 HOH   HOH A . 
C 3 HOH   15 315 308 HOH   HOH A . 
C 3 HOH   16 316 303 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.18.2_3874: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DAQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.032 
_cell.length_a_esd                 ? 
_cell.length_b                     67.032 
_cell.length_b_esd                 ? 
_cell.length_c                     216.062 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DAQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 61 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DAQ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.84 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          67.97 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '2.0 M ammonium sulfate, 0.1 M sodium acetate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.920 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.920 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DAQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.35 
_reflns.d_resolution_low                               34.7 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     8096 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           94.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                22.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.033 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.35 
_reflns_shell.d_res_low                                     2.59 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             406 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               22.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.445 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.802 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          81.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DAQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.35 
_refine.ls_d_res_low                             34.66 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     8092 
_refine.ls_number_reflns_R_free                  388 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    63.64 
_refine.ls_percent_reflns_R_free                 4.79 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2366 
_refine.ls_R_factor_R_free                       0.2554 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2356 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 32.26 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.28 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.35 
_refine_hist.d_res_low                        34.66 
_refine_hist.number_atoms_solvent             16 
_refine_hist.number_atoms_total               1267 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1234 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         17 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  ? 1292 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.508  ? 1757 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 31.578 ? 173  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.072  ? 187  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 229  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.35 2.69  . . 27  690  17.00  . . . . 0.3324 . . . . . . . . . . . 0.5201 
'X-RAY DIFFRACTION' 2.69 3.39  . . 138 2798 71.00  . . . . 0.2947 . . . . . . . . . . . 0.3326 
'X-RAY DIFFRACTION' 3.40 34.66 . . 223 4216 100.00 . . . . 0.2148 . . . . . . . . . . . 0.2282 
# 
_struct.entry_id                     9DAQ 
_struct.title                        
'Structure of E. coli dihydrofolate reductase (DHFR) in an occluded conformation and in complex with a cycloguanil derivative' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9DAQ 
_struct_keywords.text            'dihydrofolate reductase, occluded, cycloguanil, DHFR, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DYR_ECOL6 
_struct_ref.pdbx_db_accession          P0ABQ5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDE
AIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DAQ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 161 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0ABQ5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  159 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       159 
# 
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 9DAQ SER A 1 ? UNP P0ABQ5 ? ? 'expression tag' -1 1 
1 9DAQ HIS A 2 ? UNP P0ABQ5 ? ? 'expression tag' 0  2 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 ALA A 11  ? VAL A 15  ? ALA A 9   VAL A 13  5 ? 5  
HELX_P HELX_P2 AA2 PRO A 27  ? LEU A 38  ? PRO A 25  LEU A 36  1 ? 12 
HELX_P HELX_P3 AA3 ARG A 46  ? GLY A 53  ? ARG A 44  GLY A 51  1 ? 8  
HELX_P HELX_P4 AA4 SER A 79  ? GLY A 88  ? SER A 77  GLY A 86  1 ? 10 
HELX_P HELX_P5 AA5 GLY A 98  ? LEU A 106 ? GLY A 96  LEU A 104 1 ? 9  
HELX_P HELX_P6 AA6 GLU A 131 ? ASP A 133 ? GLU A 129 ASP A 131 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-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 THR A 75  ? VAL A 77  ? THR A 73  VAL A 75  
AA1 2 ASN A 61  ? LEU A 64  ? ASN A 59  LEU A 62  
AA1 3 VAL A 42  ? GLY A 45  ? VAL A 40  GLY A 43  
AA1 4 GLU A 92  ? GLY A 97  ? GLU A 90  GLY A 95  
AA1 5 MET A 3   ? LEU A 10  ? MET A 1   LEU A 8   
AA1 6 ALA A 109 ? ILE A 117 ? ALA A 107 ILE A 115 
AA1 7 TYR A 153 ? ARG A 160 ? TYR A 151 ARG A 158 
AA1 8 TRP A 135 ? HIS A 143 ? TRP A 133 HIS A 141 
# 
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 THR A 75  ? O THR A 73  N ILE A 63  ? N ILE A 61  
AA1 2 3 O LEU A 64  ? O LEU A 62  N MET A 44  ? N MET A 42  
AA1 3 4 N ILE A 43  ? N ILE A 41  O ILE A 96  ? O ILE A 94  
AA1 4 5 O ILE A 93  ? O ILE A 91  N MET A 3   ? N MET A 1   
AA1 5 6 N LEU A 6   ? N LEU A 4   O TYR A 113 ? O TYR A 111 
AA1 6 7 N HIS A 116 ? N HIS A 114 O CYS A 154 ? O CYS A 152 
AA1 7 8 O GLU A 159 ? O GLU A 157 N GLU A 136 ? N GLU A 134 
# 
_pdbx_entry_details.entry_id                   9DAQ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              127 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              127 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              127 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                111.19 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            -7.11 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
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 ALA A 9   ? ? -104.29 -169.65 
2 1 MET A 16  ? ? -105.88 -62.54  
3 1 ASP A 144 ? ? -129.24 -163.75 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     312 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_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[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -22.1483 23.5246 -6.2575 0.3808 ? 0.0183 ? 0.0160 ? 0.3555 ? -0.1507 ? 0.2717 ? 4.5844 ? 0.6875 ? 
1.1844 ? 6.5250 ? -1.0879 ? 5.8953 ? -0.1232 ? -0.1069 ? 0.0122  ? -0.3525 ? 0.2731 ? 0.0766 ? 0.2987 ? 0.2908 ? -0.1406 ? 
2 'X-RAY DIFFRACTION' ? refined -21.0130 22.6403 -1.0411 0.3257 ? 0.1435 ? 0.0880 ? 0.2073 ? -0.1638 ? 0.3298 ? 3.1727 ? 0.8906 ? 
2.2364 ? 0.7437 ? 0.5918  ? 5.6660 ? 0.1338  ? 0.0362  ? -0.0076 ? 0.0792  ? 0.1972 ? 0.0722 ? 0.4591 ? 0.2272 ? -0.2278 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid -1 through 35 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 36 through 159 )
;
# 
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 ASN 18 ? A ASN 20 
2 1 Y 1 A ALA 19 ? A ALA 21 
3 1 Y 1 A MET 20 ? A MET 22 
4 1 Y 1 A PRO 21 ? A PRO 23 
5 1 Y 1 A TRP 22 ? A TRP 24 
6 1 Y 1 A ASN 23 ? A ASN 25 
# 
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 
A1A3E C1   C  N N 1   
A1A3E C2   C  N N 2   
A1A3E C3   C  N S 3   
A1A3E C4   C  N N 4   
A1A3E C5   C  N N 5   
A1A3E C6   C  Y N 6   
A1A3E C7   C  Y N 7   
A1A3E C8   C  Y N 8   
A1A3E C9   C  Y N 9   
A1A3E N1   N  N N 10  
A1A3E N2   N  N N 11  
A1A3E CL1  CL N N 12  
A1A3E C10  C  Y N 13  
A1A3E C11  C  Y N 14  
A1A3E N3   N  N N 15  
A1A3E N4   N  N N 16  
A1A3E N5   N  N N 17  
A1A3E H3   H  N N 18  
A1A3E H4   H  N N 19  
A1A3E H5   H  N N 20  
A1A3E H6   H  N N 21  
A1A3E H7   H  N N 22  
A1A3E H8   H  N N 23  
A1A3E H9   H  N N 24  
A1A3E H10  H  N N 25  
A1A3E H11  H  N N 26  
A1A3E H12  H  N N 27  
A1A3E H16  H  N N 28  
A1A3E H17  H  N N 29  
A1A3E H18  H  N N 30  
A1A3E H19  H  N N 31  
ALA   N    N  N N 32  
ALA   CA   C  N S 33  
ALA   C    C  N N 34  
ALA   O    O  N N 35  
ALA   CB   C  N N 36  
ALA   OXT  O  N N 37  
ALA   H    H  N N 38  
ALA   H2   H  N N 39  
ALA   HA   H  N N 40  
ALA   HB1  H  N N 41  
ALA   HB2  H  N N 42  
ALA   HB3  H  N N 43  
ALA   HXT  H  N N 44  
ARG   N    N  N N 45  
ARG   CA   C  N S 46  
ARG   C    C  N N 47  
ARG   O    O  N N 48  
ARG   CB   C  N N 49  
ARG   CG   C  N N 50  
ARG   CD   C  N N 51  
ARG   NE   N  N N 52  
ARG   CZ   C  N N 53  
ARG   NH1  N  N N 54  
ARG   NH2  N  N N 55  
ARG   OXT  O  N N 56  
ARG   H    H  N N 57  
ARG   H2   H  N N 58  
ARG   HA   H  N N 59  
ARG   HB2  H  N N 60  
ARG   HB3  H  N N 61  
ARG   HG2  H  N N 62  
ARG   HG3  H  N N 63  
ARG   HD2  H  N N 64  
ARG   HD3  H  N N 65  
ARG   HE   H  N N 66  
ARG   HH11 H  N N 67  
ARG   HH12 H  N N 68  
ARG   HH21 H  N N 69  
ARG   HH22 H  N N 70  
ARG   HXT  H  N N 71  
ASN   N    N  N N 72  
ASN   CA   C  N S 73  
ASN   C    C  N N 74  
ASN   O    O  N N 75  
ASN   CB   C  N N 76  
ASN   CG   C  N N 77  
ASN   OD1  O  N N 78  
ASN   ND2  N  N N 79  
ASN   OXT  O  N N 80  
ASN   H    H  N N 81  
ASN   H2   H  N N 82  
ASN   HA   H  N N 83  
ASN   HB2  H  N N 84  
ASN   HB3  H  N N 85  
ASN   HD21 H  N N 86  
ASN   HD22 H  N N 87  
ASN   HXT  H  N N 88  
ASP   N    N  N N 89  
ASP   CA   C  N S 90  
ASP   C    C  N N 91  
ASP   O    O  N N 92  
ASP   CB   C  N N 93  
ASP   CG   C  N N 94  
ASP   OD1  O  N N 95  
ASP   OD2  O  N N 96  
ASP   OXT  O  N N 97  
ASP   H    H  N N 98  
ASP   H2   H  N N 99  
ASP   HA   H  N N 100 
ASP   HB2  H  N N 101 
ASP   HB3  H  N N 102 
ASP   HD2  H  N N 103 
ASP   HXT  H  N N 104 
CYS   N    N  N N 105 
CYS   CA   C  N R 106 
CYS   C    C  N N 107 
CYS   O    O  N N 108 
CYS   CB   C  N N 109 
CYS   SG   S  N N 110 
CYS   OXT  O  N N 111 
CYS   H    H  N N 112 
CYS   H2   H  N N 113 
CYS   HA   H  N N 114 
CYS   HB2  H  N N 115 
CYS   HB3  H  N N 116 
CYS   HG   H  N N 117 
CYS   HXT  H  N N 118 
GLN   N    N  N N 119 
GLN   CA   C  N S 120 
GLN   C    C  N N 121 
GLN   O    O  N N 122 
GLN   CB   C  N N 123 
GLN   CG   C  N N 124 
GLN   CD   C  N N 125 
GLN   OE1  O  N N 126 
GLN   NE2  N  N N 127 
GLN   OXT  O  N N 128 
GLN   H    H  N N 129 
GLN   H2   H  N N 130 
GLN   HA   H  N N 131 
GLN   HB2  H  N N 132 
GLN   HB3  H  N N 133 
GLN   HG2  H  N N 134 
GLN   HG3  H  N N 135 
GLN   HE21 H  N N 136 
GLN   HE22 H  N N 137 
GLN   HXT  H  N N 138 
GLU   N    N  N N 139 
GLU   CA   C  N S 140 
GLU   C    C  N N 141 
GLU   O    O  N N 142 
GLU   CB   C  N N 143 
GLU   CG   C  N N 144 
GLU   CD   C  N N 145 
GLU   OE1  O  N N 146 
GLU   OE2  O  N N 147 
GLU   OXT  O  N N 148 
GLU   H    H  N N 149 
GLU   H2   H  N N 150 
GLU   HA   H  N N 151 
GLU   HB2  H  N N 152 
GLU   HB3  H  N N 153 
GLU   HG2  H  N N 154 
GLU   HG3  H  N N 155 
GLU   HE2  H  N N 156 
GLU   HXT  H  N N 157 
GLY   N    N  N N 158 
GLY   CA   C  N N 159 
GLY   C    C  N N 160 
GLY   O    O  N N 161 
GLY   OXT  O  N N 162 
GLY   H    H  N N 163 
GLY   H2   H  N N 164 
GLY   HA2  H  N N 165 
GLY   HA3  H  N N 166 
GLY   HXT  H  N N 167 
HIS   N    N  N N 168 
HIS   CA   C  N S 169 
HIS   C    C  N N 170 
HIS   O    O  N N 171 
HIS   CB   C  N N 172 
HIS   CG   C  Y N 173 
HIS   ND1  N  Y N 174 
HIS   CD2  C  Y N 175 
HIS   CE1  C  Y N 176 
HIS   NE2  N  Y N 177 
HIS   OXT  O  N N 178 
HIS   H    H  N N 179 
HIS   H2   H  N N 180 
HIS   HA   H  N N 181 
HIS   HB2  H  N N 182 
HIS   HB3  H  N N 183 
HIS   HD1  H  N N 184 
HIS   HD2  H  N N 185 
HIS   HE1  H  N N 186 
HIS   HE2  H  N N 187 
HIS   HXT  H  N N 188 
HOH   O    O  N N 189 
HOH   H1   H  N N 190 
HOH   H2   H  N N 191 
ILE   N    N  N N 192 
ILE   CA   C  N S 193 
ILE   C    C  N N 194 
ILE   O    O  N N 195 
ILE   CB   C  N S 196 
ILE   CG1  C  N N 197 
ILE   CG2  C  N N 198 
ILE   CD1  C  N N 199 
ILE   OXT  O  N N 200 
ILE   H    H  N N 201 
ILE   H2   H  N N 202 
ILE   HA   H  N N 203 
ILE   HB   H  N N 204 
ILE   HG12 H  N N 205 
ILE   HG13 H  N N 206 
ILE   HG21 H  N N 207 
ILE   HG22 H  N N 208 
ILE   HG23 H  N N 209 
ILE   HD11 H  N N 210 
ILE   HD12 H  N N 211 
ILE   HD13 H  N N 212 
ILE   HXT  H  N N 213 
LEU   N    N  N N 214 
LEU   CA   C  N S 215 
LEU   C    C  N N 216 
LEU   O    O  N N 217 
LEU   CB   C  N N 218 
LEU   CG   C  N N 219 
LEU   CD1  C  N N 220 
LEU   CD2  C  N N 221 
LEU   OXT  O  N N 222 
LEU   H    H  N N 223 
LEU   H2   H  N N 224 
LEU   HA   H  N N 225 
LEU   HB2  H  N N 226 
LEU   HB3  H  N N 227 
LEU   HG   H  N N 228 
LEU   HD11 H  N N 229 
LEU   HD12 H  N N 230 
LEU   HD13 H  N N 231 
LEU   HD21 H  N N 232 
LEU   HD22 H  N N 233 
LEU   HD23 H  N N 234 
LEU   HXT  H  N N 235 
LYS   N    N  N N 236 
LYS   CA   C  N S 237 
LYS   C    C  N N 238 
LYS   O    O  N N 239 
LYS   CB   C  N N 240 
LYS   CG   C  N N 241 
LYS   CD   C  N N 242 
LYS   CE   C  N N 243 
LYS   NZ   N  N N 244 
LYS   OXT  O  N N 245 
LYS   H    H  N N 246 
LYS   H2   H  N N 247 
LYS   HA   H  N N 248 
LYS   HB2  H  N N 249 
LYS   HB3  H  N N 250 
LYS   HG2  H  N N 251 
LYS   HG3  H  N N 252 
LYS   HD2  H  N N 253 
LYS   HD3  H  N N 254 
LYS   HE2  H  N N 255 
LYS   HE3  H  N N 256 
LYS   HZ1  H  N N 257 
LYS   HZ2  H  N N 258 
LYS   HZ3  H  N N 259 
LYS   HXT  H  N N 260 
MET   N    N  N N 261 
MET   CA   C  N S 262 
MET   C    C  N N 263 
MET   O    O  N N 264 
MET   CB   C  N N 265 
MET   CG   C  N N 266 
MET   SD   S  N N 267 
MET   CE   C  N N 268 
MET   OXT  O  N N 269 
MET   H    H  N N 270 
MET   H2   H  N N 271 
MET   HA   H  N N 272 
MET   HB2  H  N N 273 
MET   HB3  H  N N 274 
MET   HG2  H  N N 275 
MET   HG3  H  N N 276 
MET   HE1  H  N N 277 
MET   HE2  H  N N 278 
MET   HE3  H  N N 279 
MET   HXT  H  N N 280 
PHE   N    N  N N 281 
PHE   CA   C  N S 282 
PHE   C    C  N N 283 
PHE   O    O  N N 284 
PHE   CB   C  N N 285 
PHE   CG   C  Y N 286 
PHE   CD1  C  Y N 287 
PHE   CD2  C  Y N 288 
PHE   CE1  C  Y N 289 
PHE   CE2  C  Y N 290 
PHE   CZ   C  Y N 291 
PHE   OXT  O  N N 292 
PHE   H    H  N N 293 
PHE   H2   H  N N 294 
PHE   HA   H  N N 295 
PHE   HB2  H  N N 296 
PHE   HB3  H  N N 297 
PHE   HD1  H  N N 298 
PHE   HD2  H  N N 299 
PHE   HE1  H  N N 300 
PHE   HE2  H  N N 301 
PHE   HZ   H  N N 302 
PHE   HXT  H  N N 303 
PRO   N    N  N N 304 
PRO   CA   C  N S 305 
PRO   C    C  N N 306 
PRO   O    O  N N 307 
PRO   CB   C  N N 308 
PRO   CG   C  N N 309 
PRO   CD   C  N N 310 
PRO   OXT  O  N N 311 
PRO   H    H  N N 312 
PRO   HA   H  N N 313 
PRO   HB2  H  N N 314 
PRO   HB3  H  N N 315 
PRO   HG2  H  N N 316 
PRO   HG3  H  N N 317 
PRO   HD2  H  N N 318 
PRO   HD3  H  N N 319 
PRO   HXT  H  N N 320 
SER   N    N  N N 321 
SER   CA   C  N S 322 
SER   C    C  N N 323 
SER   O    O  N N 324 
SER   CB   C  N N 325 
SER   OG   O  N N 326 
SER   OXT  O  N N 327 
SER   H    H  N N 328 
SER   H2   H  N N 329 
SER   HA   H  N N 330 
SER   HB2  H  N N 331 
SER   HB3  H  N N 332 
SER   HG   H  N N 333 
SER   HXT  H  N N 334 
THR   N    N  N N 335 
THR   CA   C  N S 336 
THR   C    C  N N 337 
THR   O    O  N N 338 
THR   CB   C  N R 339 
THR   OG1  O  N N 340 
THR   CG2  C  N N 341 
THR   OXT  O  N N 342 
THR   H    H  N N 343 
THR   H2   H  N N 344 
THR   HA   H  N N 345 
THR   HB   H  N N 346 
THR   HG1  H  N N 347 
THR   HG21 H  N N 348 
THR   HG22 H  N N 349 
THR   HG23 H  N N 350 
THR   HXT  H  N N 351 
TRP   N    N  N N 352 
TRP   CA   C  N S 353 
TRP   C    C  N N 354 
TRP   O    O  N N 355 
TRP   CB   C  N N 356 
TRP   CG   C  Y N 357 
TRP   CD1  C  Y N 358 
TRP   CD2  C  Y N 359 
TRP   NE1  N  Y N 360 
TRP   CE2  C  Y N 361 
TRP   CE3  C  Y N 362 
TRP   CZ2  C  Y N 363 
TRP   CZ3  C  Y N 364 
TRP   CH2  C  Y N 365 
TRP   OXT  O  N N 366 
TRP   H    H  N N 367 
TRP   H2   H  N N 368 
TRP   HA   H  N N 369 
TRP   HB2  H  N N 370 
TRP   HB3  H  N N 371 
TRP   HD1  H  N N 372 
TRP   HE1  H  N N 373 
TRP   HE3  H  N N 374 
TRP   HZ2  H  N N 375 
TRP   HZ3  H  N N 376 
TRP   HH2  H  N N 377 
TRP   HXT  H  N N 378 
TYR   N    N  N N 379 
TYR   CA   C  N S 380 
TYR   C    C  N N 381 
TYR   O    O  N N 382 
TYR   CB   C  N N 383 
TYR   CG   C  Y N 384 
TYR   CD1  C  Y N 385 
TYR   CD2  C  Y N 386 
TYR   CE1  C  Y N 387 
TYR   CE2  C  Y N 388 
TYR   CZ   C  Y N 389 
TYR   OH   O  N N 390 
TYR   OXT  O  N N 391 
TYR   H    H  N N 392 
TYR   H2   H  N N 393 
TYR   HA   H  N N 394 
TYR   HB2  H  N N 395 
TYR   HB3  H  N N 396 
TYR   HD1  H  N N 397 
TYR   HD2  H  N N 398 
TYR   HE1  H  N N 399 
TYR   HE2  H  N N 400 
TYR   HH   H  N N 401 
TYR   HXT  H  N N 402 
VAL   N    N  N N 403 
VAL   CA   C  N S 404 
VAL   C    C  N N 405 
VAL   O    O  N N 406 
VAL   CB   C  N N 407 
VAL   CG1  C  N N 408 
VAL   CG2  C  N N 409 
VAL   OXT  O  N N 410 
VAL   H    H  N N 411 
VAL   H2   H  N N 412 
VAL   HA   H  N N 413 
VAL   HB   H  N N 414 
VAL   HG11 H  N N 415 
VAL   HG12 H  N N 416 
VAL   HG13 H  N N 417 
VAL   HG21 H  N N 418 
VAL   HG22 H  N N 419 
VAL   HG23 H  N N 420 
VAL   HXT  H  N N 421 
# 
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 
A1A3E C5  C4   sing N N 1   
A1A3E C4  C3   sing N N 2   
A1A3E N4  C3   sing N N 3   
A1A3E N4  C2   doub N N 4   
A1A3E N3  C2   sing N N 5   
A1A3E C3  N5   sing N N 6   
A1A3E C2  N2   sing N N 7   
A1A3E N2  C1   doub N N 8   
A1A3E N5  C1   sing N N 9   
A1A3E N5  C6   sing N N 10  
A1A3E C1  N1   sing N N 11  
A1A3E C6  C7   doub Y N 12  
A1A3E C6  C11  sing Y N 13  
A1A3E C7  C8   sing Y N 14  
A1A3E C11 C10  doub Y N 15  
A1A3E C8  C9   doub Y N 16  
A1A3E C10 C9   sing Y N 17  
A1A3E C9  CL1  sing N N 18  
A1A3E C3  H3   sing N N 19  
A1A3E C4  H4   sing N N 20  
A1A3E C4  H5   sing N N 21  
A1A3E C5  H6   sing N N 22  
A1A3E C5  H7   sing N N 23  
A1A3E C5  H8   sing N N 24  
A1A3E C7  H9   sing N N 25  
A1A3E C8  H10  sing N N 26  
A1A3E N1  H11  sing N N 27  
A1A3E N1  H12  sing N N 28  
A1A3E C10 H16  sing N N 29  
A1A3E C11 H17  sing N N 30  
A1A3E N3  H18  sing N N 31  
A1A3E N3  H19  sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
THR   N   CA   sing N N 322 
THR   N   H    sing N N 323 
THR   N   H2   sing N N 324 
THR   CA  C    sing N N 325 
THR   CA  CB   sing N N 326 
THR   CA  HA   sing N N 327 
THR   C   O    doub N N 328 
THR   C   OXT  sing N N 329 
THR   CB  OG1  sing N N 330 
THR   CB  CG2  sing N N 331 
THR   CB  HB   sing N N 332 
THR   OG1 HG1  sing N N 333 
THR   CG2 HG21 sing N N 334 
THR   CG2 HG22 sing N N 335 
THR   CG2 HG23 sing N N 336 
THR   OXT HXT  sing N N 337 
TRP   N   CA   sing N N 338 
TRP   N   H    sing N N 339 
TRP   N   H2   sing N N 340 
TRP   CA  C    sing N N 341 
TRP   CA  CB   sing N N 342 
TRP   CA  HA   sing N N 343 
TRP   C   O    doub N N 344 
TRP   C   OXT  sing N N 345 
TRP   CB  CG   sing N N 346 
TRP   CB  HB2  sing N N 347 
TRP   CB  HB3  sing N N 348 
TRP   CG  CD1  doub Y N 349 
TRP   CG  CD2  sing Y N 350 
TRP   CD1 NE1  sing Y N 351 
TRP   CD1 HD1  sing N N 352 
TRP   CD2 CE2  doub Y N 353 
TRP   CD2 CE3  sing Y N 354 
TRP   NE1 CE2  sing Y N 355 
TRP   NE1 HE1  sing N N 356 
TRP   CE2 CZ2  sing Y N 357 
TRP   CE3 CZ3  doub Y N 358 
TRP   CE3 HE3  sing N N 359 
TRP   CZ2 CH2  doub Y N 360 
TRP   CZ2 HZ2  sing N N 361 
TRP   CZ3 CH2  sing Y N 362 
TRP   CZ3 HZ3  sing N N 363 
TRP   CH2 HH2  sing N N 364 
TRP   OXT HXT  sing N N 365 
TYR   N   CA   sing N N 366 
TYR   N   H    sing N N 367 
TYR   N   H2   sing N N 368 
TYR   CA  C    sing N N 369 
TYR   CA  CB   sing N N 370 
TYR   CA  HA   sing N N 371 
TYR   C   O    doub N N 372 
TYR   C   OXT  sing N N 373 
TYR   CB  CG   sing N N 374 
TYR   CB  HB2  sing N N 375 
TYR   CB  HB3  sing N N 376 
TYR   CG  CD1  doub Y N 377 
TYR   CG  CD2  sing Y N 378 
TYR   CD1 CE1  sing Y N 379 
TYR   CD1 HD1  sing N N 380 
TYR   CD2 CE2  doub Y N 381 
TYR   CD2 HD2  sing N N 382 
TYR   CE1 CZ   doub Y N 383 
TYR   CE1 HE1  sing N N 384 
TYR   CE2 CZ   sing Y N 385 
TYR   CE2 HE2  sing N N 386 
TYR   CZ  OH   sing N N 387 
TYR   OH  HH   sing N N 388 
TYR   OXT HXT  sing N N 389 
VAL   N   CA   sing N N 390 
VAL   N   H    sing N N 391 
VAL   N   H2   sing N N 392 
VAL   CA  C    sing N N 393 
VAL   CA  CB   sing N N 394 
VAL   CA  HA   sing N N 395 
VAL   C   O    doub N N 396 
VAL   C   OXT  sing N N 397 
VAL   CB  CG1  sing N N 398 
VAL   CB  CG2  sing N N 399 
VAL   CB  HB   sing N N 400 
VAL   CG1 HG11 sing N N 401 
VAL   CG1 HG12 sing N N 402 
VAL   CG1 HG13 sing N N 403 
VAL   CG2 HG21 sing N N 404 
VAL   CG2 HG22 sing N N 405 
VAL   CG2 HG23 sing N N 406 
VAL   OXT HXT  sing N N 407 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)'        'United States' 1P30GM124169 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 1R01AI171514 2 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 2U01AI123394 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1DDR 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DAQ 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.014918 
_atom_sites.fract_transf_matrix[1][2]   0.008613 
_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]   0.017226 
_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]   0.004628 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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   . SER   A 1 1   ? -34.453 29.278 9.723   1.00 93.03  ? -1  SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? -34.648 27.986 10.378  1.00 106.43 ? -1  SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? -33.384 27.120 10.356  1.00 112.19 ? -1  SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? -33.428 25.956 10.779  1.00 118.45 ? -1  SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? -35.806 27.215 9.725   1.00 108.43 ? -1  SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? -37.005 27.974 9.697   1.00 111.46 ? -1  SER   A OG  1 
ATOM   7    N  N   . HIS   A 1 2   ? -32.273 27.694 9.871   1.00 116.71 ? 0   HIS   A N   1 
ATOM   8    C  CA  . HIS   A 1 2   ? -30.960 27.032 9.844   1.00 112.58 ? 0   HIS   A CA  1 
ATOM   9    C  C   . HIS   A 1 2   ? -31.013 25.748 9.035   1.00 104.84 ? 0   HIS   A C   1 
ATOM   10   O  O   . HIS   A 1 2   ? -30.536 24.692 9.458   1.00 111.63 ? 0   HIS   A O   1 
ATOM   11   C  CB  . HIS   A 1 2   ? -30.442 26.757 11.253  1.00 119.52 ? 0   HIS   A CB  1 
ATOM   12   C  CG  . HIS   A 1 2   ? -30.437 27.970 12.119  1.00 121.11 ? 0   HIS   A CG  1 
ATOM   13   N  ND1 . HIS   A 1 2   ? -31.180 28.067 13.278  1.00 129.12 ? 0   HIS   A ND1 1 
ATOM   14   C  CD2 . HIS   A 1 2   ? -29.813 29.160 11.969  1.00 119.07 ? 0   HIS   A CD2 1 
ATOM   15   C  CE1 . HIS   A 1 2   ? -30.995 29.259 13.816  1.00 134.54 ? 0   HIS   A CE1 1 
ATOM   16   N  NE2 . HIS   A 1 2   ? -30.172 29.942 13.040  1.00 125.92 ? 0   HIS   A NE2 1 
ATOM   17   N  N   . MET   A 1 3   ? -31.669 25.838 7.892   1.00 77.91  ? 1   MET   A N   1 
ATOM   18   C  CA  . MET   A 1 3   ? -31.512 24.837 6.859   1.00 68.66  ? 1   MET   A CA  1 
ATOM   19   C  C   . MET   A 1 3   ? -30.076 24.792 6.376   1.00 54.77  ? 1   MET   A C   1 
ATOM   20   O  O   . MET   A 1 3   ? -29.495 25.826 6.029   1.00 50.63  ? 1   MET   A O   1 
ATOM   21   C  CB  . MET   A 1 3   ? -32.451 25.162 5.708   1.00 67.23  ? 1   MET   A CB  1 
ATOM   22   C  CG  . MET   A 1 3   ? -32.352 24.243 4.528   1.00 57.88  ? 1   MET   A CG  1 
ATOM   23   S  SD  . MET   A 1 3   ? -33.577 24.727 3.294   1.00 61.87  ? 1   MET   A SD  1 
ATOM   24   C  CE  . MET   A 1 3   ? -32.975 26.301 2.693   1.00 53.57  ? 1   MET   A CE  1 
ATOM   25   N  N   . ILE   A 1 4   ? -29.513 23.589 6.345   1.00 50.27  ? 2   ILE   A N   1 
ATOM   26   C  CA  . ILE   A 1 4   ? -28.201 23.352 5.764   1.00 48.73  ? 2   ILE   A CA  1 
ATOM   27   C  C   . ILE   A 1 4   ? -28.402 22.808 4.363   1.00 45.55  ? 2   ILE   A C   1 
ATOM   28   O  O   . ILE   A 1 4   ? -29.233 21.914 4.143   1.00 46.30  ? 2   ILE   A O   1 
ATOM   29   C  CB  . ILE   A 1 4   ? -27.351 22.375 6.599   1.00 45.46  ? 2   ILE   A CB  1 
ATOM   30   C  CG1 . ILE   A 1 4   ? -26.995 22.954 7.968   1.00 44.04  ? 2   ILE   A CG1 1 
ATOM   31   C  CG2 . ILE   A 1 4   ? -26.093 22.000 5.838   1.00 44.03  ? 2   ILE   A CG2 1 
ATOM   32   C  CD1 . ILE   A 1 4   ? -27.976 22.595 9.010   1.00 51.94  ? 2   ILE   A CD1 1 
ATOM   33   N  N   . SER   A 1 5   ? -27.648 23.352 3.413   1.00 40.39  ? 3   SER   A N   1 
ATOM   34   C  CA  . SER   A 1 5   ? -27.670 22.896 2.038   1.00 37.70  ? 3   SER   A CA  1 
ATOM   35   C  C   . SER   A 1 5   ? -26.250 22.577 1.622   1.00 37.88  ? 3   SER   A C   1 
ATOM   36   O  O   . SER   A 1 5   ? -25.278 23.062 2.215   1.00 38.85  ? 3   SER   A O   1 
ATOM   37   C  CB  . SER   A 1 5   ? -28.234 23.940 1.082   1.00 34.24  ? 3   SER   A CB  1 
ATOM   38   O  OG  . SER   A 1 5   ? -29.499 24.385 1.521   1.00 38.34  ? 3   SER   A OG  1 
ATOM   39   N  N   . LEU   A 1 6   ? -26.149 21.759 0.583   1.00 37.19  ? 4   LEU   A N   1 
ATOM   40   C  CA  . LEU   A 1 6   ? -24.879 21.384 -0.014  1.00 36.70  ? 4   LEU   A CA  1 
ATOM   41   C  C   . LEU   A 1 6   ? -24.923 21.838 -1.465  1.00 35.06  ? 4   LEU   A C   1 
ATOM   42   O  O   . LEU   A 1 6   ? -25.941 21.639 -2.140  1.00 36.92  ? 4   LEU   A O   1 
ATOM   43   C  CB  . LEU   A 1 6   ? -24.661 19.868 0.090   1.00 35.81  ? 4   LEU   A CB  1 
ATOM   44   C  CG  . LEU   A 1 6   ? -23.985 19.293 1.341   1.00 34.39  ? 4   LEU   A CG  1 
ATOM   45   C  CD1 . LEU   A 1 6   ? -24.701 19.723 2.601   1.00 33.97  ? 4   LEU   A CD1 1 
ATOM   46   C  CD2 . LEU   A 1 6   ? -23.981 17.782 1.254   1.00 35.04  ? 4   LEU   A CD2 1 
ATOM   47   N  N   . ILE   A 1 7   ? -23.859 22.504 -1.926  1.00 35.16  ? 5   ILE   A N   1 
ATOM   48   C  CA  . ILE   A 1 7   ? -23.718 22.899 -3.329  1.00 39.74  ? 5   ILE   A CA  1 
ATOM   49   C  C   . ILE   A 1 7   ? -22.419 22.318 -3.872  1.00 40.68  ? 5   ILE   A C   1 
ATOM   50   O  O   . ILE   A 1 7   ? -21.353 22.500 -3.270  1.00 37.57  ? 5   ILE   A O   1 
ATOM   51   C  CB  . ILE   A 1 7   ? -23.773 24.429 -3.507  1.00 37.71  ? 5   ILE   A CB  1 
ATOM   52   C  CG1 . ILE   A 1 7   ? -23.726 24.792 -4.989  1.00 34.91  ? 5   ILE   A CG1 1 
ATOM   53   C  CG2 . ILE   A 1 7   ? -22.749 25.147 -2.630  1.00 39.33  ? 5   ILE   A CG2 1 
ATOM   54   C  CD1 . ILE   A 1 7   ? -24.455 26.067 -5.310  1.00 37.73  ? 5   ILE   A CD1 1 
ATOM   55   N  N   . ALA   A 1 8   ? -22.512 21.599 -4.995  1.00 39.02  ? 6   ALA   A N   1 
ATOM   56   C  CA  . ALA   A 1 8   ? -21.381 20.829 -5.509  1.00 39.71  ? 6   ALA   A CA  1 
ATOM   57   C  C   . ALA   A 1 8   ? -21.450 20.739 -7.027  1.00 40.85  ? 6   ALA   A C   1 
ATOM   58   O  O   . ALA   A 1 8   ? -22.533 20.858 -7.617  1.00 38.81  ? 6   ALA   A O   1 
ATOM   59   C  CB  . ALA   A 1 8   ? -21.348 19.418 -4.914  1.00 35.75  ? 6   ALA   A CB  1 
ATOM   60   N  N   . ALA   A 1 9   ? -20.285 20.518 -7.650  1.00 40.93  ? 7   ALA   A N   1 
ATOM   61   C  CA  . ALA   A 1 9   ? -20.188 20.179 -9.067  1.00 37.71  ? 7   ALA   A CA  1 
ATOM   62   C  C   . ALA   A 1 9   ? -19.679 18.753 -9.207  1.00 43.64  ? 7   ALA   A C   1 
ATOM   63   O  O   . ALA   A 1 9   ? -18.636 18.409 -8.641  1.00 47.87  ? 7   ALA   A O   1 
ATOM   64   C  CB  . ALA   A 1 9   ? -19.258 21.130 -9.812  1.00 33.98  ? 7   ALA   A CB  1 
ATOM   65   N  N   . LEU   A 1 10  ? -20.401 17.928 -9.971  1.00 43.53  ? 8   LEU   A N   1 
ATOM   66   C  CA  . LEU   A 1 10  ? -20.068 16.519 -10.099 1.00 41.91  ? 8   LEU   A CA  1 
ATOM   67   C  C   . LEU   A 1 10  ? -19.801 16.178 -11.551 1.00 50.47  ? 8   LEU   A C   1 
ATOM   68   O  O   . LEU   A 1 10  ? -20.502 16.652 -12.452 1.00 53.24  ? 8   LEU   A O   1 
ATOM   69   C  CB  . LEU   A 1 10  ? -21.189 15.591 -9.623  1.00 44.41  ? 8   LEU   A CB  1 
ATOM   70   C  CG  . LEU   A 1 10  ? -21.935 15.782 -8.314  1.00 45.36  ? 8   LEU   A CG  1 
ATOM   71   C  CD1 . LEU   A 1 10  ? -22.782 14.532 -7.999  1.00 43.48  ? 8   LEU   A CD1 1 
ATOM   72   C  CD2 . LEU   A 1 10  ? -21.023 16.194 -7.183  1.00 46.88  ? 8   LEU   A CD2 1 
ATOM   73   N  N   . ALA   A 1 11  ? -18.824 15.303 -11.744 1.00 57.18  ? 9   ALA   A N   1 
ATOM   74   C  CA  . ALA   A 1 11  ? -18.604 14.755 -13.088 1.00 53.55  ? 9   ALA   A CA  1 
ATOM   75   C  C   . ALA   A 1 11  ? -19.178 13.347 -12.996 1.00 62.31  ? 9   ALA   A C   1 
ATOM   76   O  O   . ALA   A 1 11  ? -19.825 13.040 -11.989 1.00 64.60  ? 9   ALA   A O   1 
ATOM   77   C  CB  . ALA   A 1 11  ? -17.143 14.740 -13.410 1.00 53.27  ? 9   ALA   A CB  1 
ATOM   78   N  N   . VAL   A 1 12  ? -18.942 12.518 -13.997 1.00 68.48  ? 10  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 12  ? -19.542 11.158 -14.016 1.00 70.78  ? 10  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 12  ? -18.913 10.351 -12.880 1.00 78.74  ? 10  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 12  ? -17.758 10.652 -12.528 1.00 78.02  ? 10  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 12  ? -19.341 10.503 -15.395 1.00 75.34  ? 10  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 12  ? -20.117 11.236 -16.477 1.00 73.26  ? 10  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 12  ? -17.871 10.403 -15.772 1.00 73.41  ? 10  VAL   A CG2 1 
ATOM   85   N  N   . ASP   A 1 13  ? -19.660 9.403  -12.312 1.00 87.64  ? 11  ASP   A N   1 
ATOM   86   C  CA  . ASP   A 1 13  ? -19.174 8.594  -11.160 1.00 88.87  ? 11  ASP   A CA  1 
ATOM   87   C  C   . ASP   A 1 13  ? -19.164 9.458  -9.896  1.00 89.37  ? 11  ASP   A C   1 
ATOM   88   O  O   . ASP   A 1 13  ? -18.445 9.086  -8.957  1.00 86.06  ? 11  ASP   A O   1 
ATOM   89   C  CB  . ASP   A 1 13  ? -17.857 7.873  -11.452 1.00 84.00  ? 11  ASP   A CB  1 
ATOM   90   C  CG  . ASP   A 1 13  ? -18.037 6.554  -12.182 1.00 99.66  ? 11  ASP   A CG  1 
ATOM   91   O  OD1 . ASP   A 1 13  ? -19.108 5.940  -12.022 1.00 106.56 ? 11  ASP   A OD1 1 
ATOM   92   O  OD2 . ASP   A 1 13  ? -17.103 6.154  -12.903 1.00 108.90 ? 11  ASP   A OD2 1 
ATOM   93   N  N   . ARG   A 1 14  ? -19.880 10.587 -9.901  1.00 78.23  ? 12  ARG   A N   1 
ATOM   94   C  CA  . ARG   A 1 14  ? -20.010 11.458 -8.702  1.00 67.61  ? 12  ARG   A CA  1 
ATOM   95   C  C   . ARG   A 1 14  ? -18.641 12.029 -8.353  1.00 64.10  ? 12  ARG   A C   1 
ATOM   96   O  O   . ARG   A 1 14  ? -18.467 12.467 -7.219  1.00 62.96  ? 12  ARG   A O   1 
ATOM   97   C  CB  . ARG   A 1 14  ? -20.629 10.700 -7.523  1.00 65.60  ? 12  ARG   A CB  1 
ATOM   98   C  CG  . ARG   A 1 14  ? -22.134 10.869 -7.380  1.00 69.61  ? 12  ARG   A CG  1 
ATOM   99   C  CD  . ARG   A 1 14  ? -22.861 9.542  -7.468  1.00 84.25  ? 12  ARG   A CD  1 
ATOM   100  N  NE  . ARG   A 1 14  ? -23.716 9.263  -6.322  1.00 97.06  ? 12  ARG   A NE  1 
ATOM   101  C  CZ  . ARG   A 1 14  ? -25.044 9.252  -6.362  1.00 92.79  ? 12  ARG   A CZ  1 
ATOM   102  N  NH1 . ARG   A 1 14  ? -25.739 8.980  -5.271  1.00 84.85  ? 12  ARG   A NH1 1 
ATOM   103  N  NH2 . ARG   A 1 14  ? -25.673 9.516  -7.493  1.00 88.05  ? 12  ARG   A NH2 1 
ATOM   104  N  N   . VAL   A 1 15  ? -17.715 12.030 -9.307  1.00 66.06  ? 13  VAL   A N   1 
ATOM   105  C  CA  . VAL   A 1 15  ? -16.341 12.489 -8.981  1.00 64.43  ? 13  VAL   A CA  1 
ATOM   106  C  C   . VAL   A 1 15  ? -16.390 13.998 -8.777  1.00 61.50  ? 13  VAL   A C   1 
ATOM   107  O  O   . VAL   A 1 15  ? -17.060 14.677 -9.561  1.00 59.11  ? 13  VAL   A O   1 
ATOM   108  C  CB  . VAL   A 1 15  ? -15.308 12.055 -10.036 1.00 62.56  ? 13  VAL   A CB  1 
ATOM   109  C  CG1 . VAL   A 1 15  ? -13.920 12.593 -9.735  1.00 62.44  ? 13  VAL   A CG1 1 
ATOM   110  C  CG2 . VAL   A 1 15  ? -15.266 10.544 -10.179 1.00 65.57  ? 13  VAL   A CG2 1 
ATOM   111  N  N   . ILE   A 1 16  ? -15.708 14.480 -7.742  1.00 61.41  ? 14  ILE   A N   1 
ATOM   112  C  CA  . ILE   A 1 16  ? -15.675 15.935 -7.450  1.00 61.10  ? 14  ILE   A CA  1 
ATOM   113  C  C   . ILE   A 1 16  ? -14.223 16.394 -7.412  1.00 65.68  ? 14  ILE   A C   1 
ATOM   114  O  O   . ILE   A 1 16  ? -13.336 15.535 -7.321  1.00 62.93  ? 14  ILE   A O   1 
ATOM   115  C  CB  . ILE   A 1 16  ? -16.443 16.288 -6.157  1.00 57.79  ? 14  ILE   A CB  1 
ATOM   116  C  CG1 . ILE   A 1 16  ? -15.623 16.054 -4.890  1.00 60.24  ? 14  ILE   A CG1 1 
ATOM   117  C  CG2 . ILE   A 1 16  ? -17.773 15.563 -6.088  1.00 53.40  ? 14  ILE   A CG2 1 
ATOM   118  C  CD1 . ILE   A 1 16  ? -16.472 15.817 -3.668  1.00 57.79  ? 14  ILE   A CD1 1 
ATOM   119  N  N   . GLY   A 1 17  ? -14.007 17.699 -7.500  1.00 82.58  ? 15  GLY   A N   1 
ATOM   120  C  CA  . GLY   A 1 17  ? -12.680 18.304 -7.481  1.00 86.96  ? 15  GLY   A CA  1 
ATOM   121  C  C   . GLY   A 1 17  ? -12.774 19.798 -7.235  1.00 98.35  ? 15  GLY   A C   1 
ATOM   122  O  O   . GLY   A 1 17  ? -13.862 20.385 -7.209  1.00 99.69  ? 15  GLY   A O   1 
ATOM   123  N  N   . MET   A 1 18  ? -11.603 20.419 -7.079  1.00 93.71  ? 16  MET   A N   1 
ATOM   124  C  CA  . MET   A 1 18  ? -11.555 21.811 -6.639  1.00 92.73  ? 16  MET   A CA  1 
ATOM   125  C  C   . MET   A 1 18  ? -11.194 22.758 -7.784  1.00 89.00  ? 16  MET   A C   1 
ATOM   126  O  O   . MET   A 1 18  ? -11.992 23.634 -8.158  1.00 79.15  ? 16  MET   A O   1 
ATOM   127  C  CB  . MET   A 1 18  ? -10.575 21.916 -5.472  1.00 86.97  ? 16  MET   A CB  1 
ATOM   128  C  CG  . MET   A 1 18  ? -10.872 20.816 -4.455  1.00 87.37  ? 16  MET   A CG  1 
ATOM   129  S  SD  . MET   A 1 18  ? -10.069 20.913 -2.845  1.00 75.75  ? 16  MET   A SD  1 
ATOM   130  C  CE  . MET   A 1 18  ? -11.153 19.868 -1.851  1.00 71.20  ? 16  MET   A CE  1 
ATOM   131  N  N   . GLU   A 1 19  ? -9.997  22.590 -8.339  1.00 87.79  ? 17  GLU   A N   1 
ATOM   132  C  CA  . GLU   A 1 19  ? -9.689  23.153 -9.645  1.00 90.89  ? 17  GLU   A CA  1 
ATOM   133  C  C   . GLU   A 1 19  ? -9.506  22.021 -10.649 1.00 80.96  ? 17  GLU   A C   1 
ATOM   134  O  O   . GLU   A 1 19  ? -8.433  21.435 -10.744 1.00 80.04  ? 17  GLU   A O   1 
ATOM   135  C  CB  . GLU   A 1 19  ? -8.442  24.043 -9.605  1.00 96.11  ? 17  GLU   A CB  1 
ATOM   136  C  CG  . GLU   A 1 19  ? -8.150  24.742 -10.947 1.00 101.42 ? 17  GLU   A CG  1 
ATOM   137  C  CD  . GLU   A 1 19  ? -9.218  25.762 -11.347 1.00 106.36 ? 17  GLU   A CD  1 
ATOM   138  O  OE1 . GLU   A 1 19  ? -9.856  26.343 -10.439 1.00 111.75 ? 17  GLU   A OE1 1 
ATOM   139  O  OE2 . GLU   A 1 19  ? -9.428  25.963 -12.570 1.00 109.82 ? 17  GLU   A OE2 1 
ATOM   140  N  N   . LEU   A 1 26  ? -15.660 26.619 -16.191 1.00 55.70  ? 24  LEU   A N   1 
ATOM   141  C  CA  . LEU   A 1 26  ? -17.032 26.462 -16.696 1.00 57.21  ? 24  LEU   A CA  1 
ATOM   142  C  C   . LEU   A 1 26  ? -17.885 27.618 -16.166 1.00 47.12  ? 24  LEU   A C   1 
ATOM   143  O  O   . LEU   A 1 26  ? -18.472 27.510 -15.088 1.00 46.42  ? 24  LEU   A O   1 
ATOM   144  C  CB  . LEU   A 1 26  ? -17.625 25.107 -16.272 1.00 56.44  ? 24  LEU   A CB  1 
ATOM   145  C  CG  . LEU   A 1 26  ? -18.911 24.626 -16.960 1.00 53.07  ? 24  LEU   A CG  1 
ATOM   146  C  CD1 . LEU   A 1 26  ? -18.594 24.335 -18.393 1.00 48.11  ? 24  LEU   A CD1 1 
ATOM   147  C  CD2 . LEU   A 1 26  ? -19.485 23.370 -16.322 1.00 50.13  ? 24  LEU   A CD2 1 
ATOM   148  N  N   . PRO   A 1 27  ? -17.925 28.719 -16.925 1.00 47.27  ? 25  PRO   A N   1 
ATOM   149  C  CA  . PRO   A 1 27  ? -18.487 29.979 -16.388 1.00 44.96  ? 25  PRO   A CA  1 
ATOM   150  C  C   . PRO   A 1 27  ? -19.880 29.851 -15.792 1.00 47.53  ? 25  PRO   A C   1 
ATOM   151  O  O   . PRO   A 1 27  ? -20.106 30.263 -14.645 1.00 50.69  ? 25  PRO   A O   1 
ATOM   152  C  CB  . PRO   A 1 27  ? -18.493 30.890 -17.625 1.00 49.66  ? 25  PRO   A CB  1 
ATOM   153  C  CG  . PRO   A 1 27  ? -17.337 30.405 -18.443 1.00 50.18  ? 25  PRO   A CG  1 
ATOM   154  C  CD  . PRO   A 1 27  ? -17.367 28.894 -18.279 1.00 54.65  ? 25  PRO   A CD  1 
ATOM   155  N  N   . ALA   A 1 28  ? -20.819 29.281 -16.556 1.00 46.94  ? 26  ALA   A N   1 
ATOM   156  C  CA  . ALA   A 1 28  ? -22.219 29.228 -16.149 1.00 39.97  ? 26  ALA   A CA  1 
ATOM   157  C  C   . ALA   A 1 28  ? -22.378 28.602 -14.780 1.00 41.80  ? 26  ALA   A C   1 
ATOM   158  O  O   . ALA   A 1 28  ? -23.220 29.035 -13.985 1.00 51.88  ? 26  ALA   A O   1 
ATOM   159  C  CB  . ALA   A 1 28  ? -23.030 28.445 -17.172 1.00 39.81  ? 26  ALA   A CB  1 
ATOM   160  N  N   . ASP   A 1 29  ? -21.567 27.596 -14.473 1.00 39.00  ? 27  ASP   A N   1 
ATOM   161  C  CA  . ASP   A 1 29  ? -21.641 27.009 -13.142 1.00 42.00  ? 27  ASP   A CA  1 
ATOM   162  C  C   . ASP   A 1 29  ? -21.150 27.983 -12.078 1.00 47.74  ? 27  ASP   A C   1 
ATOM   163  O  O   . ASP   A 1 29  ? -21.595 27.912 -10.926 1.00 49.22  ? 27  ASP   A O   1 
ATOM   164  C  CB  . ASP   A 1 29  ? -20.845 25.706 -13.094 1.00 40.72  ? 27  ASP   A CB  1 
ATOM   165  C  CG  . ASP   A 1 29  ? -20.772 25.120 -11.707 1.00 41.20  ? 27  ASP   A CG  1 
ATOM   166  O  OD1 . ASP   A 1 29  ? -21.795 24.618 -11.206 1.00 43.96  ? 27  ASP   A OD1 1 
ATOM   167  O  OD2 . ASP   A 1 29  ? -19.692 25.193 -11.096 1.00 48.49  ? 27  ASP   A OD2 1 
ATOM   168  N  N   . LEU   A 1 30  ? -20.254 28.910 -12.438 1.00 47.90  ? 28  LEU   A N   1 
ATOM   169  C  CA  . LEU   A 1 30  ? -19.797 29.887 -11.453 1.00 42.48  ? 28  LEU   A CA  1 
ATOM   170  C  C   . LEU   A 1 30  ? -20.891 30.895 -11.143 1.00 39.62  ? 28  LEU   A C   1 
ATOM   171  O  O   . LEU   A 1 30  ? -21.055 31.301 -9.986  1.00 46.59  ? 28  LEU   A O   1 
ATOM   172  C  CB  . LEU   A 1 30  ? -18.534 30.587 -11.949 1.00 44.86  ? 28  LEU   A CB  1 
ATOM   173  C  CG  . LEU   A 1 30  ? -17.358 29.612 -12.127 1.00 54.48  ? 28  LEU   A CG  1 
ATOM   174  C  CD1 . LEU   A 1 30  ? -16.008 30.328 -12.105 1.00 58.76  ? 28  LEU   A CD1 1 
ATOM   175  C  CD2 . LEU   A 1 30  ? -17.374 28.462 -11.098 1.00 53.81  ? 28  LEU   A CD2 1 
ATOM   176  N  N   . ALA   A 1 31  ? -21.654 31.301 -12.164 1.00 43.34  ? 29  ALA   A N   1 
ATOM   177  C  CA  . ALA   A 1 31  ? -22.788 32.195 -11.948 1.00 44.86  ? 29  ALA   A CA  1 
ATOM   178  C  C   . ALA   A 1 31  ? -23.833 31.534 -11.069 1.00 45.65  ? 29  ALA   A C   1 
ATOM   179  O  O   . ALA   A 1 31  ? -24.374 32.166 -10.151 1.00 50.77  ? 29  ALA   A O   1 
ATOM   180  C  CB  . ALA   A 1 31  ? -23.411 32.603 -13.285 1.00 40.06  ? 29  ALA   A CB  1 
ATOM   181  N  N   . TRP   A 1 32  ? -24.121 30.256 -11.339 1.00 44.55  ? 30  TRP   A N   1 
ATOM   182  C  CA  . TRP   A 1 32  ? -25.052 29.485 -10.517 1.00 44.93  ? 30  TRP   A CA  1 
ATOM   183  C  C   . TRP   A 1 32  ? -24.551 29.370 -9.082  1.00 43.67  ? 30  TRP   A C   1 
ATOM   184  O  O   . TRP   A 1 32  ? -25.276 29.671 -8.123  1.00 44.09  ? 30  TRP   A O   1 
ATOM   185  C  CB  . TRP   A 1 32  ? -25.244 28.104 -11.143 1.00 42.65  ? 30  TRP   A CB  1 
ATOM   186  C  CG  . TRP   A 1 32  ? -25.793 27.040 -10.243 1.00 40.62  ? 30  TRP   A CG  1 
ATOM   187  C  CD1 . TRP   A 1 32  ? -25.084 26.245 -9.395  1.00 39.14  ? 30  TRP   A CD1 1 
ATOM   188  C  CD2 . TRP   A 1 32  ? -27.155 26.595 -10.164 1.00 39.14  ? 30  TRP   A CD2 1 
ATOM   189  N  NE1 . TRP   A 1 32  ? -25.920 25.355 -8.768  1.00 38.98  ? 30  TRP   A NE1 1 
ATOM   190  C  CE2 . TRP   A 1 32  ? -27.197 25.545 -9.225  1.00 37.22  ? 30  TRP   A CE2 1 
ATOM   191  C  CE3 . TRP   A 1 32  ? -28.343 26.989 -10.790 1.00 41.27  ? 30  TRP   A CE3 1 
ATOM   192  C  CZ2 . TRP   A 1 32  ? -28.379 24.876 -8.896  1.00 37.92  ? 30  TRP   A CZ2 1 
ATOM   193  C  CZ3 . TRP   A 1 32  ? -29.520 26.321 -10.465 1.00 36.40  ? 30  TRP   A CZ3 1 
ATOM   194  C  CH2 . TRP   A 1 32  ? -29.527 25.277 -9.522  1.00 36.39  ? 30  TRP   A CH2 1 
ATOM   195  N  N   . PHE   A 1 33  ? -23.300 28.950 -8.914  1.00 41.84  ? 31  PHE   A N   1 
ATOM   196  C  CA  . PHE   A 1 33  ? -22.734 28.930 -7.576  1.00 40.84  ? 31  PHE   A CA  1 
ATOM   197  C  C   . PHE   A 1 33  ? -22.836 30.292 -6.910  1.00 43.25  ? 31  PHE   A C   1 
ATOM   198  O  O   . PHE   A 1 33  ? -23.191 30.386 -5.729  1.00 49.02  ? 31  PHE   A O   1 
ATOM   199  C  CB  . PHE   A 1 33  ? -21.282 28.486 -7.617  1.00 39.50  ? 31  PHE   A CB  1 
ATOM   200  C  CG  . PHE   A 1 33  ? -20.622 28.551 -6.285  1.00 43.50  ? 31  PHE   A CG  1 
ATOM   201  C  CD1 . PHE   A 1 33  ? -20.715 27.487 -5.404  1.00 45.86  ? 31  PHE   A CD1 1 
ATOM   202  C  CD2 . PHE   A 1 33  ? -19.937 29.692 -5.887  1.00 43.44  ? 31  PHE   A CD2 1 
ATOM   203  C  CE1 . PHE   A 1 33  ? -20.100 27.547 -4.148  1.00 45.55  ? 31  PHE   A CE1 1 
ATOM   204  C  CE2 . PHE   A 1 33  ? -19.338 29.764 -4.628  1.00 46.36  ? 31  PHE   A CE2 1 
ATOM   205  C  CZ  . PHE   A 1 33  ? -19.414 28.686 -3.761  1.00 40.74  ? 31  PHE   A CZ  1 
ATOM   206  N  N   . LYS   A 1 34  ? -22.508 31.366 -7.639  1.00 43.67  ? 32  LYS   A N   1 
ATOM   207  C  CA  . LYS   A 1 34  ? -22.506 32.671 -6.990  1.00 45.18  ? 32  LYS   A CA  1 
ATOM   208  C  C   . LYS   A 1 34  ? -23.928 33.105 -6.619  1.00 45.72  ? 32  LYS   A C   1 
ATOM   209  O  O   . LYS   A 1 34  ? -24.143 33.660 -5.534  1.00 41.63  ? 32  LYS   A O   1 
ATOM   210  C  CB  . LYS   A 1 34  ? -21.795 33.718 -7.863  1.00 43.23  ? 32  LYS   A CB  1 
ATOM   211  C  CG  . LYS   A 1 34  ? -21.919 35.153 -7.285  1.00 53.63  ? 32  LYS   A CG  1 
ATOM   212  C  CD  . LYS   A 1 34  ? -20.700 36.041 -7.610  1.00 65.64  ? 32  LYS   A CD  1 
ATOM   213  C  CE  . LYS   A 1 34  ? -20.936 37.537 -7.300  1.00 64.11  ? 32  LYS   A CE  1 
ATOM   214  N  NZ  . LYS   A 1 34  ? -22.215 38.071 -7.883  1.00 71.33  ? 32  LYS   A NZ  1 
ATOM   215  N  N   . ARG   A 1 35  ? -24.928 32.816 -7.463  1.00 43.12  ? 33  ARG   A N   1 
ATOM   216  C  CA  . ARG   A 1 35  ? -26.249 33.335 -7.129  1.00 43.92  ? 33  ARG   A CA  1 
ATOM   217  C  C   . ARG   A 1 35  ? -26.860 32.560 -5.964  1.00 43.26  ? 33  ARG   A C   1 
ATOM   218  O  O   . ARG   A 1 35  ? -27.624 33.137 -5.185  1.00 49.58  ? 33  ARG   A O   1 
ATOM   219  C  CB  . ARG   A 1 35  ? -27.212 33.308 -8.329  1.00 42.77  ? 33  ARG   A CB  1 
ATOM   220  C  CG  . ARG   A 1 35  ? -27.804 31.949 -8.551  1.00 53.46  ? 33  ARG   A CG  1 
ATOM   221  C  CD  . ARG   A 1 35  ? -28.671 31.731 -9.803  1.00 61.67  ? 33  ARG   A CD  1 
ATOM   222  N  NE  . ARG   A 1 35  ? -27.838 31.782 -11.003 1.00 74.44  ? 33  ARG   A NE  1 
ATOM   223  C  CZ  . ARG   A 1 35  ? -28.254 31.504 -12.236 1.00 74.73  ? 33  ARG   A CZ  1 
ATOM   224  N  NH1 . ARG   A 1 35  ? -27.398 31.610 -13.252 1.00 66.08  ? 33  ARG   A NH1 1 
ATOM   225  N  NH2 . ARG   A 1 35  ? -29.481 31.018 -12.436 1.00 75.45  ? 33  ARG   A NH2 1 
ATOM   226  N  N   . ASN   A 1 36  ? -26.535 31.270 -5.804  1.00 43.99  ? 34  ASN   A N   1 
ATOM   227  C  CA  . ASN   A 1 36  ? -27.115 30.463 -4.724  1.00 40.59  ? 34  ASN   A CA  1 
ATOM   228  C  C   . ASN   A 1 36  ? -26.356 30.527 -3.401  1.00 42.03  ? 34  ASN   A C   1 
ATOM   229  O  O   . ASN   A 1 36  ? -26.810 29.918 -2.429  1.00 45.18  ? 34  ASN   A O   1 
ATOM   230  C  CB  . ASN   A 1 36  ? -27.237 29.001 -5.144  1.00 37.76  ? 34  ASN   A CB  1 
ATOM   231  C  CG  . ASN   A 1 36  ? -28.328 28.783 -6.159  1.00 43.63  ? 34  ASN   A CG  1 
ATOM   232  O  OD1 . ASN   A 1 36  ? -29.508 28.751 -5.805  1.00 50.36  ? 34  ASN   A OD1 1 
ATOM   233  N  ND2 . ASN   A 1 36  ? -27.952 28.603 -7.427  1.00 42.69  ? 34  ASN   A ND2 1 
ATOM   234  N  N   . THR   A 1 37  ? -25.215 31.219 -3.336  1.00 44.12  ? 35  THR   A N   1 
ATOM   235  C  CA  . THR   A 1 37  ? -24.518 31.451 -2.077  1.00 40.41  ? 35  THR   A CA  1 
ATOM   236  C  C   . THR   A 1 37  ? -24.421 32.922 -1.712  1.00 43.56  ? 35  THR   A C   1 
ATOM   237  O  O   . THR   A 1 37  ? -23.854 33.246 -0.658  1.00 45.19  ? 35  THR   A O   1 
ATOM   238  C  CB  . THR   A 1 37  ? -23.099 30.867 -2.119  1.00 40.76  ? 35  THR   A CB  1 
ATOM   239  O  OG1 . THR   A 1 37  ? -22.415 31.352 -3.283  1.00 38.16  ? 35  THR   A OG1 1 
ATOM   240  C  CG2 . THR   A 1 37  ? -23.128 29.347 -2.135  1.00 39.81  ? 35  THR   A CG2 1 
ATOM   241  N  N   . LEU   A 1 38  ? -24.943 33.820 -2.546  1.00 47.55  ? 36  LEU   A N   1 
ATOM   242  C  CA  . LEU   A 1 38  ? -24.818 35.252 -2.290  1.00 48.52  ? 36  LEU   A CA  1 
ATOM   243  C  C   . LEU   A 1 38  ? -25.507 35.606 -0.989  1.00 48.13  ? 36  LEU   A C   1 
ATOM   244  O  O   . LEU   A 1 38  ? -26.654 35.210 -0.757  1.00 51.11  ? 36  LEU   A O   1 
ATOM   245  C  CB  . LEU   A 1 38  ? -25.438 36.067 -3.423  1.00 51.25  ? 36  LEU   A CB  1 
ATOM   246  C  CG  . LEU   A 1 38  ? -24.970 37.518 -3.509  1.00 52.49  ? 36  LEU   A CG  1 
ATOM   247  C  CD1 . LEU   A 1 38  ? -23.619 37.577 -4.224  1.00 53.85  ? 36  LEU   A CD1 1 
ATOM   248  C  CD2 . LEU   A 1 38  ? -26.030 38.418 -4.172  1.00 46.50  ? 36  LEU   A CD2 1 
ATOM   249  N  N   . ASN   A 1 39  ? -24.802 36.337 -0.132  1.00 47.37  ? 37  ASN   A N   1 
ATOM   250  C  CA  . ASN   A 1 39  ? -25.346 36.761 1.152   1.00 47.83  ? 37  ASN   A CA  1 
ATOM   251  C  C   . ASN   A 1 39  ? -25.740 35.578 2.052   1.00 47.75  ? 37  ASN   A C   1 
ATOM   252  O  O   . ASN   A 1 39  ? -26.595 35.717 2.936   1.00 51.70  ? 37  ASN   A O   1 
ATOM   253  C  CB  . ASN   A 1 39  ? -26.542 37.696 0.937   1.00 51.89  ? 37  ASN   A CB  1 
ATOM   254  C  CG  . ASN   A 1 39  ? -26.209 38.851 0.007   1.00 55.77  ? 37  ASN   A CG  1 
ATOM   255  O  OD1 . ASN   A 1 39  ? -25.239 39.585 0.235   1.00 57.65  ? 37  ASN   A OD1 1 
ATOM   256  N  ND2 . ASN   A 1 39  ? -27.015 39.024 -1.045  1.00 55.46  ? 37  ASN   A ND2 1 
ATOM   257  N  N   . LYS   A 1 40  ? -25.143 34.404 1.857   1.00 44.49  ? 38  LYS   A N   1 
ATOM   258  C  CA  . LYS   A 1 40  ? -25.342 33.309 2.782   1.00 39.30  ? 38  LYS   A CA  1 
ATOM   259  C  C   . LYS   A 1 40  ? -23.997 32.921 3.379   1.00 41.65  ? 38  LYS   A C   1 
ATOM   260  O  O   . LYS   A 1 40  ? -22.985 32.974 2.681   1.00 47.78  ? 38  LYS   A O   1 
ATOM   261  C  CB  . LYS   A 1 40  ? -25.950 32.100 2.064   1.00 41.76  ? 38  LYS   A CB  1 
ATOM   262  C  CG  . LYS   A 1 40  ? -27.376 32.295 1.569   1.00 40.20  ? 38  LYS   A CG  1 
ATOM   263  C  CD  . LYS   A 1 40  ? -27.833 31.115 0.685   1.00 38.03  ? 38  LYS   A CD  1 
ATOM   264  C  CE  . LYS   A 1 40  ? -28.585 31.630 -0.540  1.00 40.10  ? 38  LYS   A CE  1 
ATOM   265  N  NZ  . LYS   A 1 40  ? -29.306 30.573 -1.300  1.00 37.73  ? 38  LYS   A NZ  1 
ATOM   266  N  N   . PRO   A 1 41  ? -23.937 32.538 4.645   1.00 39.87  ? 39  PRO   A N   1 
ATOM   267  C  CA  . PRO   A 1 41  ? -22.656 32.082 5.198   1.00 38.77  ? 39  PRO   A CA  1 
ATOM   268  C  C   . PRO   A 1 41  ? -22.285 30.738 4.597   1.00 41.48  ? 39  PRO   A C   1 
ATOM   269  O  O   . PRO   A 1 41  ? -23.152 29.879 4.416   1.00 44.04  ? 39  PRO   A O   1 
ATOM   270  C  CB  . PRO   A 1 41  ? -22.941 31.966 6.698   1.00 36.98  ? 39  PRO   A CB  1 
ATOM   271  C  CG  . PRO   A 1 41  ? -24.407 31.696 6.764   1.00 40.12  ? 39  PRO   A CG  1 
ATOM   272  C  CD  . PRO   A 1 41  ? -25.007 32.538 5.654   1.00 43.28  ? 39  PRO   A CD  1 
ATOM   273  N  N   . VAL   A 1 42  ? -20.993 30.547 4.284   1.00 39.44  ? 40  VAL   A N   1 
ATOM   274  C  CA  . VAL   A 1 42  ? -20.522 29.313 3.650   1.00 37.91  ? 40  VAL   A CA  1 
ATOM   275  C  C   . VAL   A 1 42  ? -19.493 28.602 4.536   1.00 37.51  ? 40  VAL   A C   1 
ATOM   276  O  O   . VAL   A 1 42  ? -18.683 29.246 5.219   1.00 37.90  ? 40  VAL   A O   1 
ATOM   277  C  CB  . VAL   A 1 42  ? -19.935 29.572 2.245   1.00 38.23  ? 40  VAL   A CB  1 
ATOM   278  C  CG1 . VAL   A 1 42  ? -21.004 30.153 1.329   1.00 39.97  ? 40  VAL   A CG1 1 
ATOM   279  C  CG2 . VAL   A 1 42  ? -18.723 30.463 2.312   1.00 35.11  ? 40  VAL   A CG2 1 
ATOM   280  N  N   . ILE   A 1 43  ? -19.524 27.260 4.498   1.00 33.54  ? 41  ILE   A N   1 
ATOM   281  C  CA  . ILE   A 1 43  ? -18.667 26.378 5.290   1.00 32.33  ? 41  ILE   A CA  1 
ATOM   282  C  C   . ILE   A 1 43  ? -17.860 25.500 4.331   1.00 40.10  ? 41  ILE   A C   1 
ATOM   283  O  O   . ILE   A 1 43  ? -18.419 24.996 3.350   1.00 40.48  ? 41  ILE   A O   1 
ATOM   284  C  CB  . ILE   A 1 43  ? -19.517 25.509 6.246   1.00 34.44  ? 41  ILE   A CB  1 
ATOM   285  C  CG1 . ILE   A 1 43  ? -20.355 26.370 7.192   1.00 31.40  ? 41  ILE   A CG1 1 
ATOM   286  C  CG2 . ILE   A 1 43  ? -18.659 24.557 7.049   1.00 38.13  ? 41  ILE   A CG2 1 
ATOM   287  C  CD1 . ILE   A 1 43  ? -21.346 25.569 8.021   1.00 26.45  ? 41  ILE   A CD1 1 
ATOM   288  N  N   . MET   A 1 44  ? -16.554 25.310 4.605   1.00 40.56  ? 42  MET   A N   1 
ATOM   289  C  CA  . MET   A 1 44  ? -15.652 24.596 3.689   1.00 34.94  ? 42  MET   A CA  1 
ATOM   290  C  C   . MET   A 1 44  ? -14.484 24.007 4.470   1.00 38.82  ? 42  MET   A C   1 
ATOM   291  O  O   . MET   A 1 44  ? -14.165 24.463 5.575   1.00 40.34  ? 42  MET   A O   1 
ATOM   292  C  CB  . MET   A 1 44  ? -15.082 25.521 2.620   1.00 35.71  ? 42  MET   A CB  1 
ATOM   293  C  CG  . MET   A 1 44  ? -14.180 26.574 3.227   1.00 33.78  ? 42  MET   A CG  1 
ATOM   294  S  SD  . MET   A 1 44  ? -13.726 27.916 2.102   1.00 33.68  ? 42  MET   A SD  1 
ATOM   295  C  CE  . MET   A 1 44  ? -14.969 29.111 2.604   1.00 27.40  ? 42  MET   A CE  1 
ATOM   296  N  N   . GLY   A 1 45  ? -13.810 23.004 3.858   1.00 31.86  ? 43  GLY   A N   1 
ATOM   297  C  CA  . GLY   A 1 45  ? -12.615 22.433 4.455   1.00 35.37  ? 43  GLY   A CA  1 
ATOM   298  C  C   . GLY   A 1 45  ? -11.373 23.282 4.196   1.00 37.56  ? 43  GLY   A C   1 
ATOM   299  O  O   . GLY   A 1 45  ? -11.449 24.235 3.422   1.00 36.91  ? 43  GLY   A O   1 
ATOM   300  N  N   . ARG   A 1 46  ? -10.270 22.951 4.902   1.00 41.18  ? 44  ARG   A N   1 
ATOM   301  C  CA  . ARG   A 1 46  ? -8.960  23.536 4.586   1.00 40.48  ? 44  ARG   A CA  1 
ATOM   302  C  C   . ARG   A 1 46  ? -8.685  23.494 3.100   1.00 44.65  ? 44  ARG   A C   1 
ATOM   303  O  O   . ARG   A 1 46  ? -8.336  24.507 2.486   1.00 47.38  ? 44  ARG   A O   1 
ATOM   304  C  CB  . ARG   A 1 46  ? -7.799  22.775 5.218   1.00 45.31  ? 44  ARG   A CB  1 
ATOM   305  C  CG  . ARG   A 1 46  ? -7.306  23.049 6.567   1.00 55.59  ? 44  ARG   A CG  1 
ATOM   306  C  CD  . ARG   A 1 46  ? -6.641  21.751 7.106   1.00 62.35  ? 44  ARG   A CD  1 
ATOM   307  N  NE  . ARG   A 1 46  ? -7.615  20.797 7.665   1.00 56.65  ? 44  ARG   A NE  1 
ATOM   308  C  CZ  . ARG   A 1 46  ? -7.323  19.555 8.024   1.00 41.02  ? 44  ARG   A CZ  1 
ATOM   309  N  NH1 . ARG   A 1 46  ? -6.104  19.107 7.853   1.00 50.01  ? 44  ARG   A NH1 1 
ATOM   310  N  NH2 . ARG   A 1 46  ? -8.240  18.767 8.540   1.00 35.56  ? 44  ARG   A NH2 1 
ATOM   311  N  N   . HIS   A 1 47  ? -8.702  22.275 2.552   1.00 43.58  ? 45  HIS   A N   1 
ATOM   312  C  CA  A HIS   A 1 47  ? -8.299  22.124 1.162   0.31 44.78  ? 45  HIS   A CA  1 
ATOM   313  C  CA  B HIS   A 1 47  ? -8.408  22.012 1.145   0.69 42.47  ? 45  HIS   A CA  1 
ATOM   314  C  C   . HIS   A 1 47  ? -9.102  23.044 0.257   1.00 45.32  ? 45  HIS   A C   1 
ATOM   315  O  O   . HIS   A 1 47  ? -8.511  23.683 -0.624  1.00 47.11  ? 45  HIS   A O   1 
ATOM   316  C  CB  A HIS   A 1 47  ? -8.399  20.662 0.736   0.31 44.07  ? 45  HIS   A CB  1 
ATOM   317  C  CB  B HIS   A 1 47  ? -8.887  20.577 0.808   0.69 45.51  ? 45  HIS   A CB  1 
ATOM   318  C  CG  A HIS   A 1 47  ? -7.362  19.802 1.374   0.31 36.10  ? 45  HIS   A CG  1 
ATOM   319  C  CG  B HIS   A 1 47  ? -10.146 20.144 1.534   0.69 38.30  ? 45  HIS   A CG  1 
ATOM   320  N  ND1 A HIS   A 1 47  ? -6.088  20.257 1.624   0.31 37.40  ? 45  HIS   A ND1 1 
ATOM   321  N  ND1 B HIS   A 1 47  ? -11.356 20.785 1.394   0.69 30.22  ? 45  HIS   A ND1 1 
ATOM   322  C  CD2 A HIS   A 1 47  ? -7.412  18.536 1.844   0.31 37.32  ? 45  HIS   A CD2 1 
ATOM   323  C  CD2 B HIS   A 1 47  ? -10.384 19.099 2.359   0.69 36.08  ? 45  HIS   A CD2 1 
ATOM   324  C  CE1 A HIS   A 1 47  ? -5.391  19.301 2.207   0.31 39.33  ? 45  HIS   A CE1 1 
ATOM   325  C  CE1 B HIS   A 1 47  ? -12.259 20.196 2.143   0.69 29.70  ? 45  HIS   A CE1 1 
ATOM   326  N  NE2 A HIS   A 1 47  ? -6.172  18.247 2.353   0.31 39.34  ? 45  HIS   A NE2 1 
ATOM   327  N  NE2 B HIS   A 1 47  ? -11.707 19.151 2.715   0.69 31.14  ? 45  HIS   A NE2 1 
ATOM   328  N  N   . THR   A 1 48  ? -10.400 23.189 0.502   1.00 44.83  ? 46  THR   A N   1 
ATOM   329  C  CA  . THR   A 1 48  ? -11.244 24.074 -0.286  1.00 41.35  ? 46  THR   A CA  1 
ATOM   330  C  C   . THR   A 1 48  ? -10.874 25.537 -0.037  1.00 43.15  ? 46  THR   A C   1 
ATOM   331  O  O   . THR   A 1 48  ? -10.769 26.329 -0.976  1.00 44.65  ? 46  THR   A O   1 
ATOM   332  C  CB  . THR   A 1 48  ? -12.705 23.739 0.058   1.00 42.53  ? 46  THR   A CB  1 
ATOM   333  O  OG1 . THR   A 1 48  ? -12.938 22.343 -0.208  1.00 42.72  ? 46  THR   A OG1 1 
ATOM   334  C  CG2 . THR   A 1 48  ? -13.714 24.585 -0.668  1.00 36.36  ? 46  THR   A CG2 1 
ATOM   335  N  N   . TRP   A 1 49  ? -10.631 25.909 1.217   1.00 46.04  ? 47  TRP   A N   1 
ATOM   336  C  CA  . TRP   A 1 49  ? -10.129 27.253 1.490   1.00 46.55  ? 47  TRP   A CA  1 
ATOM   337  C  C   . TRP   A 1 49  ? -8.803  27.505 0.769   1.00 45.70  ? 47  TRP   A C   1 
ATOM   338  O  O   . TRP   A 1 49  ? -8.573  28.594 0.225   1.00 43.92  ? 47  TRP   A O   1 
ATOM   339  C  CB  . TRP   A 1 49  ? -9.968  27.449 3.003   1.00 45.85  ? 47  TRP   A CB  1 
ATOM   340  C  CG  . TRP   A 1 49  ? -9.093  28.622 3.397   1.00 44.01  ? 47  TRP   A CG  1 
ATOM   341  C  CD1 . TRP   A 1 49  ? -7.863  28.568 3.975   1.00 39.00  ? 47  TRP   A CD1 1 
ATOM   342  C  CD2 . TRP   A 1 49  ? -9.404  30.014 3.241   1.00 41.58  ? 47  TRP   A CD2 1 
ATOM   343  N  NE1 . TRP   A 1 49  ? -7.380  29.842 4.192   1.00 38.19  ? 47  TRP   A NE1 1 
ATOM   344  C  CE2 . TRP   A 1 49  ? -8.306  30.745 3.741   1.00 39.60  ? 47  TRP   A CE2 1 
ATOM   345  C  CE3 . TRP   A 1 49  ? -10.500 30.709 2.720   1.00 38.15  ? 47  TRP   A CE3 1 
ATOM   346  C  CZ2 . TRP   A 1 49  ? -8.278  32.140 3.747   1.00 42.00  ? 47  TRP   A CZ2 1 
ATOM   347  C  CZ3 . TRP   A 1 49  ? -10.467 32.096 2.720   1.00 42.51  ? 47  TRP   A CZ3 1 
ATOM   348  C  CH2 . TRP   A 1 49  ? -9.364  32.796 3.231   1.00 43.72  ? 47  TRP   A CH2 1 
ATOM   349  N  N   . GLU   A 1 50  ? -7.916  26.508 0.752   1.00 47.32  ? 48  GLU   A N   1 
ATOM   350  C  CA  . GLU   A 1 50  ? -6.581  26.750 0.230   1.00 42.57  ? 48  GLU   A CA  1 
ATOM   351  C  C   . GLU   A 1 50  ? -6.609  26.990 -1.269  1.00 44.75  ? 48  GLU   A C   1 
ATOM   352  O  O   . GLU   A 1 50  ? -5.738  27.688 -1.799  1.00 45.05  ? 48  GLU   A O   1 
ATOM   353  C  CB  . GLU   A 1 50  ? -5.663  25.584 0.580   1.00 41.51  ? 48  GLU   A CB  1 
ATOM   354  C  CG  . GLU   A 1 50  ? -5.145  25.654 1.992   1.00 44.92  ? 48  GLU   A CG  1 
ATOM   355  C  CD  . GLU   A 1 50  ? -4.452  24.373 2.456   1.00 49.21  ? 48  GLU   A CD  1 
ATOM   356  O  OE1 . GLU   A 1 50  ? -3.921  23.624 1.601   1.00 47.65  ? 48  GLU   A OE1 1 
ATOM   357  O  OE2 . GLU   A 1 50  ? -4.429  24.129 3.691   1.00 54.30  ? 48  GLU   A OE2 1 
ATOM   358  N  N   . SER   A 1 51  ? -7.617  26.458 -1.961  1.00 45.89  ? 49  SER   A N   1 
ATOM   359  C  CA  . SER   A 1 51  ? -7.653  26.587 -3.411  1.00 48.68  ? 49  SER   A CA  1 
ATOM   360  C  C   . SER   A 1 51  ? -8.280  27.908 -3.875  1.00 49.90  ? 49  SER   A C   1 
ATOM   361  O  O   . SER   A 1 51  ? -7.980  28.366 -4.986  1.00 58.77  ? 49  SER   A O   1 
ATOM   362  C  CB  . SER   A 1 51  ? -8.359  25.363 -4.020  1.00 46.98  ? 49  SER   A CB  1 
ATOM   363  O  OG  . SER   A 1 51  ? -9.752  25.373 -3.794  1.00 52.69  ? 49  SER   A OG  1 
ATOM   364  N  N   . ILE   A 1 52  ? -9.112  28.556 -3.056  1.00 45.38  ? 50  ILE   A N   1 
ATOM   365  C  CA  . ILE   A 1 52  ? -9.639  29.861 -3.451  1.00 46.10  ? 50  ILE   A CA  1 
ATOM   366  C  C   . ILE   A 1 52  ? -8.699  30.987 -3.011  1.00 52.22  ? 50  ILE   A C   1 
ATOM   367  O  O   . ILE   A 1 52  ? -8.519  31.978 -3.728  1.00 56.02  ? 50  ILE   A O   1 
ATOM   368  C  CB  . ILE   A 1 52  ? -11.075 30.071 -2.914  1.00 42.42  ? 50  ILE   A CB  1 
ATOM   369  C  CG1 . ILE   A 1 52  ? -11.149 29.923 -1.410  1.00 48.16  ? 50  ILE   A CG1 1 
ATOM   370  C  CG2 . ILE   A 1 52  ? -12.029 29.067 -3.477  1.00 49.73  ? 50  ILE   A CG2 1 
ATOM   371  C  CD1 . ILE   A 1 52  ? -12.512 30.305 -0.875  1.00 49.28  ? 50  ILE   A CD1 1 
ATOM   372  N  N   . GLY   A 1 53  ? -8.089  30.872 -1.843  1.00 57.27  ? 51  GLY   A N   1 
ATOM   373  C  CA  . GLY   A 1 53  ? -7.184  31.940 -1.405  1.00 56.04  ? 51  GLY   A CA  1 
ATOM   374  C  C   . GLY   A 1 53  ? -7.786  33.172 -0.742  1.00 61.26  ? 51  GLY   A C   1 
ATOM   375  O  O   . GLY   A 1 53  ? -7.317  33.592 0.323   1.00 61.01  ? 51  GLY   A O   1 
ATOM   376  N  N   . ARG   A 1 54  ? -8.817  33.768 -1.354  1.00 57.31  ? 52  ARG   A N   1 
ATOM   377  C  CA  . ARG   A 1 54  ? -9.611  34.934 -0.964  1.00 52.91  ? 52  ARG   A CA  1 
ATOM   378  C  C   . ARG   A 1 54  ? -10.850 34.494 -0.186  1.00 48.42  ? 52  ARG   A C   1 
ATOM   379  O  O   . ARG   A 1 54  ? -11.434 33.452 -0.490  1.00 48.52  ? 52  ARG   A O   1 
ATOM   380  C  CB  . ARG   A 1 54  ? -10.053 35.700 -2.203  1.00 62.55  ? 52  ARG   A CB  1 
ATOM   381  C  CG  . ARG   A 1 54  ? -9.198  36.876 -2.601  1.00 65.53  ? 52  ARG   A CG  1 
ATOM   382  C  CD  . ARG   A 1 54  ? -9.733  37.390 -3.935  1.00 77.45  ? 52  ARG   A CD  1 
ATOM   383  N  NE  . ARG   A 1 54  ? -9.128  36.671 -5.069  1.00 87.50  ? 52  ARG   A NE  1 
ATOM   384  C  CZ  . ARG   A 1 54  ? -7.819  36.637 -5.363  1.00 95.85  ? 52  ARG   A CZ  1 
ATOM   385  N  NH1 . ARG   A 1 54  ? -6.938  37.320 -4.633  1.00 91.70  ? 52  ARG   A NH1 1 
ATOM   386  N  NH2 . ARG   A 1 54  ? -7.383  35.939 -6.415  1.00 91.54  ? 52  ARG   A NH2 1 
ATOM   387  N  N   . PRO   A 1 55  ? -11.279 35.224 0.837   1.00 49.56  ? 53  PRO   A N   1 
ATOM   388  C  CA  . PRO   A 1 55  ? -12.653 35.053 1.318   1.00 43.46  ? 53  PRO   A CA  1 
ATOM   389  C  C   . PRO   A 1 55  ? -13.649 35.261 0.180   1.00 46.91  ? 53  PRO   A C   1 
ATOM   390  O  O   . PRO   A 1 55  ? -13.419 36.052 -0.739  1.00 50.72  ? 53  PRO   A O   1 
ATOM   391  C  CB  . PRO   A 1 55  ? -12.796 36.143 2.391   1.00 40.96  ? 53  PRO   A CB  1 
ATOM   392  C  CG  . PRO   A 1 55  ? -11.400 36.493 2.810   1.00 45.47  ? 53  PRO   A CG  1 
ATOM   393  C  CD  . PRO   A 1 55  ? -10.419 35.910 1.818   1.00 49.92  ? 53  PRO   A CD  1 
ATOM   394  N  N   . LEU   A 1 56  ? -14.758 34.536 0.232   1.00 48.85  ? 54  LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 56  ? -15.842 34.797 -0.712  1.00 41.77  ? 54  LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 56  ? -16.533 36.086 -0.308  1.00 41.85  ? 54  LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 56  ? -17.051 36.171 0.814   1.00 45.96  ? 54  LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 56  ? -16.845 33.659 -0.735  1.00 41.10  ? 54  LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 56  ? -16.209 32.361 -1.184  1.00 34.07  ? 54  LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 56  ? -17.234 31.248 -1.225  1.00 37.71  ? 54  LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 56  ? -15.630 32.607 -2.533  1.00 37.44  ? 54  LEU   A CD2 1 
ATOM   402  N  N   . PRO   A 1 57  ? -16.626 37.103 -1.200  1.00 44.68  ? 55  PRO   A N   1 
ATOM   403  C  CA  . PRO   A 1 57  ? -17.183 38.391 -0.829  1.00 43.05  ? 55  PRO   A CA  1 
ATOM   404  C  C   . PRO   A 1 57  ? -18.608 38.410 -0.278  1.00 47.63  ? 55  PRO   A C   1 
ATOM   405  O  O   . PRO   A 1 57  ? -19.438 37.703 -0.792  1.00 48.31  ? 55  PRO   A O   1 
ATOM   406  C  CB  . PRO   A 1 57  ? -17.196 39.170 -2.144  1.00 40.19  ? 55  PRO   A CB  1 
ATOM   407  C  CG  . PRO   A 1 57  ? -17.178 38.124 -3.209  1.00 46.63  ? 55  PRO   A CG  1 
ATOM   408  C  CD  . PRO   A 1 57  ? -16.220 37.119 -2.625  1.00 45.63  ? 55  PRO   A CD  1 
ATOM   409  N  N   . GLY   A 1 58  ? -18.842 39.224 0.751   1.00 47.74  ? 56  GLY   A N   1 
ATOM   410  C  CA  . GLY   A 1 58  ? -20.201 39.402 1.289   1.00 52.71  ? 56  GLY   A CA  1 
ATOM   411  C  C   . GLY   A 1 58  ? -20.798 38.115 1.786   1.00 57.67  ? 56  GLY   A C   1 
ATOM   412  O  O   . GLY   A 1 58  ? -22.020 37.951 1.654   1.00 52.31  ? 56  GLY   A O   1 
ATOM   413  N  N   . ARG   A 1 59  ? -19.965 37.226 2.314   1.00 57.27  ? 57  ARG   A N   1 
ATOM   414  C  CA  . ARG   A 1 59  ? -20.471 35.970 2.907   1.00 50.04  ? 57  ARG   A CA  1 
ATOM   415  C  C   . ARG   A 1 59  ? -19.627 35.710 4.144   1.00 48.70  ? 57  ARG   A C   1 
ATOM   416  O  O   . ARG   A 1 59  ? -18.447 36.071 4.120   1.00 57.14  ? 57  ARG   A O   1 
ATOM   417  C  CB  . ARG   A 1 59  ? -20.325 34.818 1.914   1.00 39.82  ? 57  ARG   A CB  1 
ATOM   418  C  CG  . ARG   A 1 59  ? -21.240 34.901 0.702   1.00 43.77  ? 57  ARG   A CG  1 
ATOM   419  C  CD  . ARG   A 1 59  ? -20.674 34.161 -0.490  1.00 43.40  ? 57  ARG   A CD  1 
ATOM   420  N  NE  . ARG   A 1 59  ? -20.429 35.066 -1.600  1.00 46.08  ? 57  ARG   A NE  1 
ATOM   421  C  CZ  . ARG   A 1 59  ? -20.348 34.690 -2.866  1.00 51.61  ? 57  ARG   A CZ  1 
ATOM   422  N  NH1 . ARG   A 1 59  ? -20.120 35.585 -3.811  1.00 59.75  ? 57  ARG   A NH1 1 
ATOM   423  N  NH2 . ARG   A 1 59  ? -20.494 33.418 -3.186  1.00 53.35  ? 57  ARG   A NH2 1 
ATOM   424  N  N   . LYS   A 1 60  ? -20.214 35.146 5.191   1.00 45.51  ? 58  LYS   A N   1 
ATOM   425  C  CA  . LYS   A 1 60  ? -19.364 34.770 6.338   1.00 41.18  ? 58  LYS   A CA  1 
ATOM   426  C  C   . LYS   A 1 60  ? -18.688 33.473 5.938   1.00 40.92  ? 58  LYS   A C   1 
ATOM   427  O  O   . LYS   A 1 60  ? -19.391 32.483 5.741   1.00 38.93  ? 58  LYS   A O   1 
ATOM   428  C  CB  . LYS   A 1 60  ? -20.133 34.628 7.651   1.00 36.69  ? 58  LYS   A CB  1 
ATOM   429  C  CG  . LYS   A 1 60  ? -19.313 34.090 8.814   1.00 37.59  ? 58  LYS   A CG  1 
ATOM   430  C  CD  . LYS   A 1 60  ? -20.025 34.170 10.139  1.00 38.28  ? 58  LYS   A CD  1 
ATOM   431  C  CE  . LYS   A 1 60  ? -19.099 34.549 11.273  1.00 40.74  ? 58  LYS   A CE  1 
ATOM   432  N  NZ  . LYS   A 1 60  ? -19.074 33.518 12.334  1.00 48.09  ? 58  LYS   A NZ  1 
ATOM   433  N  N   . ASN   A 1 61  ? -17.381 33.521 5.755   1.00 42.82  ? 59  ASN   A N   1 
ATOM   434  C  CA  . ASN   A 1 61  ? -16.606 32.331 5.413   1.00 37.55  ? 59  ASN   A CA  1 
ATOM   435  C  C   . ASN   A 1 61  ? -16.233 31.608 6.699   1.00 36.12  ? 59  ASN   A C   1 
ATOM   436  O  O   . ASN   A 1 61  ? -15.653 32.219 7.609   1.00 36.15  ? 59  ASN   A O   1 
ATOM   437  C  CB  . ASN   A 1 61  ? -15.322 32.700 4.672   1.00 38.07  ? 59  ASN   A CB  1 
ATOM   438  C  CG  . ASN   A 1 61  ? -15.557 33.096 3.242   1.00 39.32  ? 59  ASN   A CG  1 
ATOM   439  O  OD1 . ASN   A 1 61  ? -15.130 34.147 2.806   1.00 46.62  ? 59  ASN   A OD1 1 
ATOM   440  N  ND2 . ASN   A 1 61  ? -16.209 32.247 2.499   1.00 44.97  ? 59  ASN   A ND2 1 
ATOM   441  N  N   . ILE   A 1 62  ? -16.540 30.310 6.768   1.00 35.16  ? 60  ILE   A N   1 
ATOM   442  C  CA  . ILE   A 1 62  ? -16.266 29.492 7.951   1.00 35.59  ? 60  ILE   A CA  1 
ATOM   443  C  C   . ILE   A 1 62  ? -15.500 28.251 7.524   1.00 37.69  ? 60  ILE   A C   1 
ATOM   444  O  O   . ILE   A 1 62  ? -15.948 27.517 6.632   1.00 34.78  ? 60  ILE   A O   1 
ATOM   445  C  CB  . ILE   A 1 62  ? -17.557 29.072 8.664   1.00 33.67  ? 60  ILE   A CB  1 
ATOM   446  C  CG1 . ILE   A 1 62  ? -18.289 30.286 9.213   1.00 31.51  ? 60  ILE   A CG1 1 
ATOM   447  C  CG2 . ILE   A 1 62  ? -17.249 28.055 9.738   1.00 34.05  ? 60  ILE   A CG2 1 
ATOM   448  C  CD1 . ILE   A 1 62  ? -19.701 29.957 9.581   1.00 35.75  ? 60  ILE   A CD1 1 
ATOM   449  N  N   . ILE   A 1 63  ? -14.368 27.992 8.175   1.00 37.46  ? 61  ILE   A N   1 
ATOM   450  C  CA  . ILE   A 1 63  ? -13.443 26.951 7.731   1.00 39.53  ? 61  ILE   A CA  1 
ATOM   451  C  C   . ILE   A 1 63  ? -13.437 25.831 8.763   1.00 36.61  ? 61  ILE   A C   1 
ATOM   452  O  O   . ILE   A 1 63  ? -13.263 26.086 9.959   1.00 39.19  ? 61  ILE   A O   1 
ATOM   453  C  CB  . ILE   A 1 63  ? -12.028 27.512 7.521   1.00 36.18  ? 61  ILE   A CB  1 
ATOM   454  C  CG1 . ILE   A 1 63  ? -12.100 28.831 6.753   1.00 32.92  ? 61  ILE   A CG1 1 
ATOM   455  C  CG2 . ILE   A 1 63  ? -11.162 26.495 6.793   1.00 36.08  ? 61  ILE   A CG2 1 
ATOM   456  C  CD1 . ILE   A 1 63  ? -12.813 28.742 5.462   1.00 34.55  ? 61  ILE   A CD1 1 
ATOM   457  N  N   . LEU   A 1 64  ? -13.637 24.598 8.315   1.00 37.62  ? 62  LEU   A N   1 
ATOM   458  C  CA  . LEU   A 1 64  ? -13.775 23.470 9.232   1.00 38.98  ? 62  LEU   A CA  1 
ATOM   459  C  C   . LEU   A 1 64  ? -12.484 22.664 9.190   1.00 39.28  ? 62  LEU   A C   1 
ATOM   460  O  O   . LEU   A 1 64  ? -12.199 22.013 8.183   1.00 43.01  ? 62  LEU   A O   1 
ATOM   461  C  CB  . LEU   A 1 64  ? -14.981 22.596 8.872   1.00 36.59  ? 62  LEU   A CB  1 
ATOM   462  C  CG  . LEU   A 1 64  ? -15.165 21.365 9.781   1.00 34.34  ? 62  LEU   A CG  1 
ATOM   463  C  CD1 . LEU   A 1 64  ? -15.361 21.789 11.209  1.00 40.26  ? 62  LEU   A CD1 1 
ATOM   464  C  CD2 . LEU   A 1 64  ? -16.329 20.487 9.352   1.00 36.85  ? 62  LEU   A CD2 1 
ATOM   465  N  N   . SER   A 1 65  ? -11.722 22.674 10.290  1.00 40.48  ? 63  SER   A N   1 
ATOM   466  C  CA  . SER   A 1 65  ? -10.430 21.997 10.307  1.00 44.84  ? 63  SER   A CA  1 
ATOM   467  C  C   . SER   A 1 65  ? -9.962  21.707 11.731  1.00 47.85  ? 63  SER   A C   1 
ATOM   468  O  O   . SER   A 1 65  ? -10.198 22.488 12.665  1.00 51.81  ? 63  SER   A O   1 
ATOM   469  C  CB  . SER   A 1 65  ? -9.381  22.831 9.568   1.00 44.79  ? 63  SER   A CB  1 
ATOM   470  O  OG  . SER   A 1 65  ? -8.090  22.284 9.741   1.00 53.74  ? 63  SER   A OG  1 
ATOM   471  N  N   . SER   A 1 66  ? -9.304  20.548 11.859  1.00 50.85  ? 64  SER   A N   1 
ATOM   472  C  CA  . SER   A 1 66  ? -8.622  20.135 13.078  1.00 50.73  ? 64  SER   A CA  1 
ATOM   473  C  C   . SER   A 1 66  ? -7.379  20.995 13.363  1.00 56.48  ? 64  SER   A C   1 
ATOM   474  O  O   . SER   A 1 66  ? -7.042  21.189 14.543  1.00 67.33  ? 64  SER   A O   1 
ATOM   475  C  CB  . SER   A 1 66  ? -8.218  18.663 12.954  1.00 54.13  ? 64  SER   A CB  1 
ATOM   476  O  OG  . SER   A 1 66  ? -7.193  18.598 11.981  1.00 57.46  ? 64  SER   A OG  1 
ATOM   477  N  N   . GLN   A 1 67  ? -6.676  21.469 12.297  1.00 60.30  ? 65  GLN   A N   1 
ATOM   478  C  CA  . GLN   A 1 67  ? -5.442  22.260 12.331  1.00 55.35  ? 65  GLN   A CA  1 
ATOM   479  C  C   . GLN   A 1 67  ? -5.772  23.745 12.555  1.00 56.69  ? 65  GLN   A C   1 
ATOM   480  O  O   . GLN   A 1 67  ? -6.884  24.217 12.257  1.00 57.40  ? 65  GLN   A O   1 
ATOM   481  C  CB  . GLN   A 1 67  ? -4.668  21.968 11.038  1.00 60.89  ? 65  GLN   A CB  1 
ATOM   482  C  CG  . GLN   A 1 67  ? -3.345  22.632 10.687  1.00 73.45  ? 65  GLN   A CG  1 
ATOM   483  C  CD  . GLN   A 1 67  ? -2.840  21.940 9.487   1.00 79.75  ? 65  GLN   A CD  1 
ATOM   484  O  OE1 . GLN   A 1 67  ? -3.532  20.995 9.009   1.00 83.76  ? 65  GLN   A OE1 1 
ATOM   485  N  NE2 . GLN   A 1 67  ? -1.672  22.295 9.015   1.00 87.10  ? 65  GLN   A NE2 1 
ATOM   486  N  N   . PRO   A 1 68  ? -4.851  24.481 13.168  1.00 55.84  ? 66  PRO   A N   1 
ATOM   487  C  CA  . PRO   A 1 68  ? -5.155  25.825 13.665  1.00 49.58  ? 66  PRO   A CA  1 
ATOM   488  C  C   . PRO   A 1 68  ? -5.224  26.891 12.568  1.00 50.12  ? 66  PRO   A C   1 
ATOM   489  O  O   . PRO   A 1 68  ? -4.705  26.737 11.455  1.00 53.36  ? 66  PRO   A O   1 
ATOM   490  C  CB  . PRO   A 1 68  ? -3.980  26.108 14.621  1.00 43.58  ? 66  PRO   A CB  1 
ATOM   491  C  CG  . PRO   A 1 68  ? -3.344  24.770 14.936  1.00 47.87  ? 66  PRO   A CG  1 
ATOM   492  C  CD  . PRO   A 1 68  ? -3.519  24.035 13.605  1.00 56.09  ? 66  PRO   A CD  1 
ATOM   493  N  N   . GLY   A 1 69  ? -5.812  28.029 12.948  1.00 47.53  ? 67  GLY   A N   1 
ATOM   494  C  CA  . GLY   A 1 69  ? -6.117  29.068 11.975  1.00 44.29  ? 67  GLY   A CA  1 
ATOM   495  C  C   . GLY   A 1 69  ? -4.879  29.764 11.432  1.00 47.20  ? 67  GLY   A C   1 
ATOM   496  O  O   . GLY   A 1 69  ? -3.875  29.923 12.117  1.00 56.51  ? 67  GLY   A O   1 
ATOM   497  N  N   . THR   A 1 70  ? -4.944  30.174 10.158  1.00 46.79  ? 68  THR   A N   1 
ATOM   498  C  CA  . THR   A 1 70  ? -3.855  30.925 9.543   1.00 40.79  ? 68  THR   A CA  1 
ATOM   499  C  C   . THR   A 1 70  ? -4.264  32.258 8.906   1.00 44.29  ? 68  THR   A C   1 
ATOM   500  O  O   . THR   A 1 70  ? -3.418  32.875 8.253   1.00 48.23  ? 68  THR   A O   1 
ATOM   501  C  CB  . THR   A 1 70  ? -3.151  30.070 8.475   1.00 39.83  ? 68  THR   A CB  1 
ATOM   502  O  OG1 . THR   A 1 70  ? -3.947  30.048 7.279   1.00 60.29  ? 68  THR   A OG1 1 
ATOM   503  C  CG2 . THR   A 1 70  ? -2.951  28.645 8.948   1.00 43.81  ? 68  THR   A CG2 1 
ATOM   504  N  N   . ASP   A 1 71  ? -5.507  32.734 9.081   1.00 40.74  ? 69  ASP   A N   1 
ATOM   505  C  CA  . ASP   A 1 71  ? -6.003  33.904 8.342   1.00 39.83  ? 69  ASP   A CA  1 
ATOM   506  C  C   . ASP   A 1 71  ? -7.185  34.514 9.087   1.00 38.24  ? 69  ASP   A C   1 
ATOM   507  O  O   . ASP   A 1 71  ? -8.210  33.844 9.226   1.00 41.80  ? 69  ASP   A O   1 
ATOM   508  C  CB  . ASP   A 1 71  ? -6.426  33.476 6.932   1.00 41.12  ? 69  ASP   A CB  1 
ATOM   509  C  CG  . ASP   A 1 71  ? -6.641  34.652 5.975   1.00 41.77  ? 69  ASP   A CG  1 
ATOM   510  O  OD1 . ASP   A 1 71  ? -7.478  35.522 6.304   1.00 43.68  ? 69  ASP   A OD1 1 
ATOM   511  O  OD2 . ASP   A 1 71  ? -6.024  34.675 4.874   1.00 42.01  ? 69  ASP   A OD2 1 
ATOM   512  N  N   . ASP   A 1 72  ? -7.092  35.790 9.519   1.00 41.36  ? 70  ASP   A N   1 
ATOM   513  C  CA  . ASP   A 1 72  ? -8.163  36.343 10.362  1.00 43.76  ? 70  ASP   A CA  1 
ATOM   514  C  C   . ASP   A 1 72  ? -9.420  36.729 9.590   1.00 45.84  ? 70  ASP   A C   1 
ATOM   515  O  O   . ASP   A 1 72  ? -10.453 36.992 10.217  1.00 56.12  ? 70  ASP   A O   1 
ATOM   516  C  CB  . ASP   A 1 72  ? -7.742  37.599 11.144  1.00 38.71  ? 70  ASP   A CB  1 
ATOM   517  C  CG  . ASP   A 1 72  ? -7.498  38.834 10.254  1.00 50.87  ? 70  ASP   A CG  1 
ATOM   518  O  OD1 . ASP   A 1 72  ? -7.612  38.779 9.009   1.00 56.05  ? 70  ASP   A OD1 1 
ATOM   519  O  OD2 . ASP   A 1 72  ? -7.207  39.906 10.826  1.00 58.25  ? 70  ASP   A OD2 1 
ATOM   520  N  N   . ARG   A 1 73  ? -9.357  36.817 8.268   1.00 39.41  ? 71  ARG   A N   1 
ATOM   521  C  CA  . ARG   A 1 73  ? -10.517 37.252 7.505   1.00 44.72  ? 71  ARG   A CA  1 
ATOM   522  C  C   . ARG   A 1 73  ? -11.662 36.250 7.538   1.00 49.22  ? 71  ARG   A C   1 
ATOM   523  O  O   . ARG   A 1 73  ? -12.753 36.570 7.035   1.00 47.37  ? 71  ARG   A O   1 
ATOM   524  C  CB  . ARG   A 1 73  ? -10.100 37.528 6.058   1.00 45.07  ? 71  ARG   A CB  1 
ATOM   525  C  CG  . ARG   A 1 73  ? -9.070  38.649 5.957   1.00 48.15  ? 71  ARG   A CG  1 
ATOM   526  C  CD  . ARG   A 1 73  ? -8.445  38.743 4.568   1.00 49.16  ? 71  ARG   A CD  1 
ATOM   527  N  NE  . ARG   A 1 73  ? -7.907  37.454 4.156   1.00 48.90  ? 71  ARG   A NE  1 
ATOM   528  C  CZ  . ARG   A 1 73  ? -7.424  37.198 2.950   1.00 43.13  ? 71  ARG   A CZ  1 
ATOM   529  N  NH1 . ARG   A 1 73  ? -7.393  38.150 2.033   1.00 48.55  ? 71  ARG   A NH1 1 
ATOM   530  N  NH2 . ARG   A 1 73  ? -6.958  35.993 2.669   1.00 43.41  ? 71  ARG   A NH2 1 
ATOM   531  N  N   . VAL   A 1 74  ? -11.444 35.058 8.106   1.00 41.78  ? 72  VAL   A N   1 
ATOM   532  C  CA  . VAL   A 1 74  ? -12.428 33.986 8.069   1.00 44.15  ? 72  VAL   A CA  1 
ATOM   533  C  C   . VAL   A 1 74  ? -12.479 33.310 9.439   1.00 45.04  ? 72  VAL   A C   1 
ATOM   534  O  O   . VAL   A 1 74  ? -11.501 33.317 10.194  1.00 46.90  ? 72  VAL   A O   1 
ATOM   535  C  CB  . VAL   A 1 74  ? -12.090 32.974 6.959   1.00 43.58  ? 72  VAL   A CB  1 
ATOM   536  C  CG1 . VAL   A 1 74  ? -12.134 33.644 5.564   1.00 38.50  ? 72  VAL   A CG1 1 
ATOM   537  C  CG2 . VAL   A 1 74  ? -10.736 32.347 7.233   1.00 41.81  ? 72  VAL   A CG2 1 
ATOM   538  N  N   . THR   A 1 75  ? -13.636 32.734 9.767   1.00 41.73  ? 73  THR   A N   1 
ATOM   539  C  CA  . THR   A 1 75  ? -13.826 32.036 11.033  1.00 35.02  ? 73  THR   A CA  1 
ATOM   540  C  C   . THR   A 1 75  ? -13.401 30.577 10.925  1.00 36.60  ? 73  THR   A C   1 
ATOM   541  O  O   . THR   A 1 75  ? -13.763 29.895 9.959   1.00 39.82  ? 73  THR   A O   1 
ATOM   542  C  CB  . THR   A 1 75  ? -15.287 32.127 11.442  1.00 33.63  ? 73  THR   A CB  1 
ATOM   543  O  OG1 . THR   A 1 75  ? -15.681 33.510 11.470  1.00 40.86  ? 73  THR   A OG1 1 
ATOM   544  C  CG2 . THR   A 1 75  ? -15.504 31.480 12.762  1.00 28.97  ? 73  THR   A CG2 1 
ATOM   545  N  N   . TRP   A 1 76  ? -12.656 30.095 11.925  1.00 37.44  ? 74  TRP   A N   1 
ATOM   546  C  CA  . TRP   A 1 76  ? -12.144 28.723 11.973  1.00 34.53  ? 74  TRP   A CA  1 
ATOM   547  C  C   . TRP   A 1 76  ? -12.841 27.935 13.082  1.00 33.96  ? 74  TRP   A C   1 
ATOM   548  O  O   . TRP   A 1 76  ? -13.025 28.453 14.182  1.00 37.89  ? 74  TRP   A O   1 
ATOM   549  C  CB  . TRP   A 1 76  ? -10.633 28.723 12.234  1.00 31.02  ? 74  TRP   A CB  1 
ATOM   550  C  CG  . TRP   A 1 76  ? -9.840  29.367 11.138  1.00 37.48  ? 74  TRP   A CG  1 
ATOM   551  C  CD1 . TRP   A 1 76  ? -9.652  30.707 10.950  1.00 38.39  ? 74  TRP   A CD1 1 
ATOM   552  C  CD2 . TRP   A 1 76  ? -9.112  28.708 10.078  1.00 39.22  ? 74  TRP   A CD2 1 
ATOM   553  N  NE1 . TRP   A 1 76  ? -8.861  30.922 9.836   1.00 43.10  ? 74  TRP   A NE1 1 
ATOM   554  C  CE2 . TRP   A 1 76  ? -8.519  29.715 9.286   1.00 37.41  ? 74  TRP   A CE2 1 
ATOM   555  C  CE3 . TRP   A 1 76  ? -8.912  27.371 9.723   1.00 40.33  ? 74  TRP   A CE3 1 
ATOM   556  C  CZ2 . TRP   A 1 76  ? -7.739  29.428 8.169   1.00 38.40  ? 74  TRP   A CZ2 1 
ATOM   557  C  CZ3 . TRP   A 1 76  ? -8.134  27.081 8.593   1.00 41.12  ? 74  TRP   A CZ3 1 
ATOM   558  C  CH2 . TRP   A 1 76  ? -7.562  28.106 7.834   1.00 39.12  ? 74  TRP   A CH2 1 
ATOM   559  N  N   . VAL   A 1 77  ? -13.218 26.675 12.810  1.00 35.55  ? 75  VAL   A N   1 
ATOM   560  C  CA  . VAL   A 1 77  ? -13.915 25.832 13.784  1.00 32.99  ? 75  VAL   A CA  1 
ATOM   561  C  C   . VAL   A 1 77  ? -13.367 24.411 13.695  1.00 39.67  ? 75  VAL   A C   1 
ATOM   562  O  O   . VAL   A 1 77  ? -12.820 24.001 12.670  1.00 39.18  ? 75  VAL   A O   1 
ATOM   563  C  CB  . VAL   A 1 77  ? -15.440 25.792 13.550  1.00 35.87  ? 75  VAL   A CB  1 
ATOM   564  C  CG1 . VAL   A 1 77  ? -16.064 27.152 13.774  1.00 33.21  ? 75  VAL   A CG1 1 
ATOM   565  C  CG2 . VAL   A 1 77  ? -15.725 25.287 12.148  1.00 34.54  ? 75  VAL   A CG2 1 
ATOM   566  N  N   . LYS   A 1 78  ? -13.548 23.631 14.768  1.00 38.55  ? 76  LYS   A N   1 
ATOM   567  C  CA  . LYS   A 1 78  ? -13.007 22.273 14.782  1.00 40.89  ? 76  LYS   A CA  1 
ATOM   568  C  C   . LYS   A 1 78  ? -14.107 21.205 14.805  1.00 40.86  ? 76  LYS   A C   1 
ATOM   569  O  O   . LYS   A 1 78  ? -13.811 20.015 14.986  1.00 41.48  ? 76  LYS   A O   1 
ATOM   570  C  CB  . LYS   A 1 78  ? -12.065 22.107 15.987  1.00 34.95  ? 76  LYS   A CB  1 
ATOM   571  C  CG  . LYS   A 1 78  ? -10.843 23.005 15.880  1.00 46.90  ? 76  LYS   A CG  1 
ATOM   572  C  CD  . LYS   A 1 78  ? -9.846  23.031 17.034  1.00 48.68  ? 76  LYS   A CD  1 
ATOM   573  C  CE  . LYS   A 1 78  ? -9.040  21.774 17.066  1.00 63.48  ? 76  LYS   A CE  1 
ATOM   574  N  NZ  . LYS   A 1 78  ? -7.941  21.910 18.064  1.00 80.82  ? 76  LYS   A NZ  1 
ATOM   575  N  N   . SER   A 1 79  ? -15.367 21.602 14.640  1.00 35.56  ? 77  SER   A N   1 
ATOM   576  C  CA  . SER   A 1 79  ? -16.516 20.766 14.954  1.00 33.34  ? 77  SER   A CA  1 
ATOM   577  C  C   . SER   A 1 79  ? -17.646 21.097 13.994  1.00 40.37  ? 77  SER   A C   1 
ATOM   578  O  O   . SER   A 1 79  ? -17.859 22.272 13.668  1.00 43.02  ? 77  SER   A O   1 
ATOM   579  C  CB  . SER   A 1 79  ? -16.999 21.005 16.383  1.00 41.04  ? 77  SER   A CB  1 
ATOM   580  O  OG  . SER   A 1 79  ? -18.257 20.383 16.590  1.00 49.93  ? 77  SER   A OG  1 
ATOM   581  N  N   . VAL   A 1 80  ? -18.376 20.069 13.550  1.00 36.98  ? 78  VAL   A N   1 
ATOM   582  C  CA  . VAL   A 1 80  ? -19.573 20.342 12.759  1.00 37.26  ? 78  VAL   A CA  1 
ATOM   583  C  C   . VAL   A 1 80  ? -20.488 21.323 13.503  1.00 41.10  ? 78  VAL   A C   1 
ATOM   584  O  O   . VAL   A 1 80  ? -21.016 22.276 12.912  1.00 43.17  ? 78  VAL   A O   1 
ATOM   585  C  CB  . VAL   A 1 80  ? -20.298 19.027 12.405  1.00 35.70  ? 78  VAL   A CB  1 
ATOM   586  C  CG1 . VAL   A 1 80  ? -21.601 19.315 11.687  1.00 33.98  ? 78  VAL   A CG1 1 
ATOM   587  C  CG2 . VAL   A 1 80  ? -19.419 18.148 11.543  1.00 38.82  ? 78  VAL   A CG2 1 
ATOM   588  N  N   . ASP   A 1 81  ? -20.651 21.140 14.822  1.00 39.74  ? 79  ASP   A N   1 
ATOM   589  C  CA  . ASP   A 1 81  ? -21.585 21.994 15.554  1.00 42.09  ? 79  ASP   A CA  1 
ATOM   590  C  C   . ASP   A 1 81  ? -21.015 23.392 15.790  1.00 40.78  ? 79  ASP   A C   1 
ATOM   591  O  O   . ASP   A 1 81  ? -21.774 24.371 15.880  1.00 38.83  ? 79  ASP   A O   1 
ATOM   592  C  CB  . ASP   A 1 81  ? -21.975 21.345 16.888  1.00 41.17  ? 79  ASP   A CB  1 
ATOM   593  C  CG  . ASP   A 1 81  ? -22.835 20.095 16.700  1.00 49.35  ? 79  ASP   A CG  1 
ATOM   594  O  OD1 . ASP   A 1 81  ? -23.614 20.012 15.715  1.00 48.49  ? 79  ASP   A OD1 1 
ATOM   595  O  OD2 . ASP   A 1 81  ? -22.737 19.195 17.557  1.00 56.59  ? 79  ASP   A OD2 1 
ATOM   596  N  N   . GLU   A 1 82  ? -19.693 23.506 15.925  1.00 39.06  ? 80  GLU   A N   1 
ATOM   597  C  CA  . GLU   A 1 82  ? -19.086 24.829 16.003  1.00 35.87  ? 80  GLU   A CA  1 
ATOM   598  C  C   . GLU   A 1 82  ? -19.297 25.597 14.698  1.00 40.18  ? 80  GLU   A C   1 
ATOM   599  O  O   . GLU   A 1 82  ? -19.588 26.803 14.716  1.00 38.41  ? 80  GLU   A O   1 
ATOM   600  C  CB  . GLU   A 1 82  ? -17.604 24.681 16.341  1.00 35.38  ? 80  GLU   A CB  1 
ATOM   601  C  CG  . GLU   A 1 82  ? -17.360 24.261 17.790  1.00 38.00  ? 80  GLU   A CG  1 
ATOM   602  C  CD  . GLU   A 1 82  ? -15.886 24.079 18.086  1.00 36.91  ? 80  GLU   A CD  1 
ATOM   603  O  OE1 . GLU   A 1 82  ? -15.128 24.007 17.111  1.00 42.55  ? 80  GLU   A OE1 1 
ATOM   604  O  OE2 . GLU   A 1 82  ? -15.471 24.000 19.266  1.00 44.44  ? 80  GLU   A OE2 1 
ATOM   605  N  N   . ALA   A 1 83  ? -19.195 24.902 13.558  1.00 36.84  ? 81  ALA   A N   1 
ATOM   606  C  CA  . ALA   A 1 83  ? -19.438 25.553 12.273  1.00 34.08  ? 81  ALA   A CA  1 
ATOM   607  C  C   . ALA   A 1 83  ? -20.879 26.023 12.149  1.00 33.67  ? 81  ALA   A C   1 
ATOM   608  O  O   . ALA   A 1 83  ? -21.134 27.134 11.667  1.00 37.11  ? 81  ALA   A O   1 
ATOM   609  C  CB  . ALA   A 1 83  ? -19.108 24.615 11.122  1.00 35.98  ? 81  ALA   A CB  1 
ATOM   610  N  N   . ILE   A 1 84  ? -21.842 25.194 12.551  1.00 35.62  ? 82  ILE   A N   1 
ATOM   611  C  CA  . ILE   A 1 84  ? -23.230 25.599 12.357  1.00 37.51  ? 82  ILE   A CA  1 
ATOM   612  C  C   . ILE   A 1 84  ? -23.560 26.784 13.241  1.00 37.56  ? 82  ILE   A C   1 
ATOM   613  O  O   . ILE   A 1 84  ? -24.238 27.725 12.808  1.00 38.34  ? 82  ILE   A O   1 
ATOM   614  C  CB  . ILE   A 1 84  ? -24.190 24.427 12.595  1.00 30.01  ? 82  ILE   A CB  1 
ATOM   615  C  CG1 . ILE   A 1 84  ? -23.863 23.325 11.600  1.00 32.09  ? 82  ILE   A CG1 1 
ATOM   616  C  CG2 . ILE   A 1 84  ? -25.607 24.891 12.426  1.00 30.84  ? 82  ILE   A CG2 1 
ATOM   617  C  CD1 . ILE   A 1 84  ? -24.633 22.081 11.812  1.00 39.98  ? 82  ILE   A CD1 1 
ATOM   618  N  N   . ALA   A 1 85  ? -23.073 26.763 14.488  1.00 37.56  ? 83  ALA   A N   1 
ATOM   619  C  CA  . ALA   A 1 85  ? -23.335 27.855 15.417  1.00 32.23  ? 83  ALA   A CA  1 
ATOM   620  C  C   . ALA   A 1 85  ? -22.674 29.144 14.955  1.00 37.59  ? 83  ALA   A C   1 
ATOM   621  O  O   . ALA   A 1 85  ? -23.178 30.234 15.245  1.00 43.34  ? 83  ALA   A O   1 
ATOM   622  C  CB  . ALA   A 1 85  ? -22.846 27.482 16.813  1.00 33.40  ? 83  ALA   A CB  1 
ATOM   623  N  N   . ALA   A 1 86  ? -21.557 29.045 14.226  1.00 35.68  ? 84  ALA   A N   1 
ATOM   624  C  CA  . ALA   A 1 86  ? -20.876 30.246 13.767  1.00 32.82  ? 84  ALA   A CA  1 
ATOM   625  C  C   . ALA   A 1 86  ? -21.670 30.969 12.691  1.00 35.90  ? 84  ALA   A C   1 
ATOM   626  O  O   . ALA   A 1 86  ? -21.471 32.171 12.492  1.00 40.07  ? 84  ALA   A O   1 
ATOM   627  C  CB  . ALA   A 1 86  ? -19.481 29.885 13.254  1.00 34.82  ? 84  ALA   A CB  1 
ATOM   628  N  N   . CYS   A 1 87  ? -22.559 30.261 11.992  1.00 38.36  ? 85  CYS   A N   1 
ATOM   629  C  CA  . CYS   A 1 87  ? -23.414 30.881 10.987  1.00 40.23  ? 85  CYS   A CA  1 
ATOM   630  C  C   . CYS   A 1 87  ? -24.484 31.769 11.612  1.00 40.96  ? 85  CYS   A C   1 
ATOM   631  O  O   . CYS   A 1 87  ? -24.995 32.674 10.936  1.00 45.09  ? 85  CYS   A O   1 
ATOM   632  C  CB  . CYS   A 1 87  ? -24.069 29.795 10.118  1.00 45.38  ? 85  CYS   A CB  1 
ATOM   633  S  SG  . CYS   A 1 87  ? -22.864 28.756 9.208   1.00 37.28  ? 85  CYS   A SG  1 
ATOM   634  N  N   . GLY   A 1 88  ? -24.835 31.535 12.876  1.00 36.19  ? 86  GLY   A N   1 
ATOM   635  C  CA  . GLY   A 1 88  ? -25.808 32.422 13.474  1.00 37.77  ? 86  GLY   A CA  1 
ATOM   636  C  C   . GLY   A 1 88  ? -27.212 32.153 12.956  1.00 53.17  ? 86  GLY   A C   1 
ATOM   637  O  O   . GLY   A 1 88  ? -27.508 31.088 12.398  1.00 63.11  ? 86  GLY   A O   1 
ATOM   638  N  N   . ASP   A 1 89  ? -28.085 33.154 13.138  1.00 55.60  ? 87  ASP   A N   1 
ATOM   639  C  CA  . ASP   A 1 89  ? -29.505 33.043 12.779  1.00 61.76  ? 87  ASP   A CA  1 
ATOM   640  C  C   . ASP   A 1 89  ? -29.722 33.453 11.333  1.00 59.32  ? 87  ASP   A C   1 
ATOM   641  O  O   . ASP   A 1 89  ? -30.076 34.597 11.039  1.00 60.56  ? 87  ASP   A O   1 
ATOM   642  C  CB  . ASP   A 1 89  ? -30.384 33.876 13.703  1.00 64.07  ? 87  ASP   A CB  1 
ATOM   643  C  CG  . ASP   A 1 89  ? -31.832 33.407 13.690  1.00 72.84  ? 87  ASP   A CG  1 
ATOM   644  O  OD1 . ASP   A 1 89  ? -32.095 32.347 13.072  1.00 79.06  ? 87  ASP   A OD1 1 
ATOM   645  O  OD2 . ASP   A 1 89  ? -32.701 34.083 14.299  1.00 70.17  ? 87  ASP   A OD2 1 
ATOM   646  N  N   . VAL   A 1 90  ? -29.548 32.492 10.428  1.00 58.95  ? 88  VAL   A N   1 
ATOM   647  C  CA  . VAL   A 1 90  ? -29.714 32.714 8.998   1.00 49.47  ? 88  VAL   A CA  1 
ATOM   648  C  C   . VAL   A 1 90  ? -30.685 31.656 8.484   1.00 55.40  ? 88  VAL   A C   1 
ATOM   649  O  O   . VAL   A 1 90  ? -30.790 30.572 9.080   1.00 62.21  ? 88  VAL   A O   1 
ATOM   650  C  CB  . VAL   A 1 90  ? -28.364 32.645 8.262   1.00 53.33  ? 88  VAL   A CB  1 
ATOM   651  C  CG1 . VAL   A 1 90  ? -27.457 33.771 8.721   1.00 53.90  ? 88  VAL   A CG1 1 
ATOM   652  C  CG2 . VAL   A 1 90  ? -27.685 31.281 8.434   1.00 51.10  ? 88  VAL   A CG2 1 
ATOM   653  N  N   . PRO   A 1 91  ? -31.412 31.921 7.394   1.00 51.10  ? 89  PRO   A N   1 
ATOM   654  C  CA  . PRO   A 1 91  ? -32.357 30.910 6.887   1.00 51.24  ? 89  PRO   A CA  1 
ATOM   655  C  C   . PRO   A 1 91  ? -31.672 29.706 6.294   1.00 56.51  ? 89  PRO   A C   1 
ATOM   656  O  O   . PRO   A 1 91  ? -32.171 28.583 6.430   1.00 63.84  ? 89  PRO   A O   1 
ATOM   657  C  CB  . PRO   A 1 91  ? -33.146 31.673 5.816   1.00 44.09  ? 89  PRO   A CB  1 
ATOM   658  C  CG  . PRO   A 1 91  ? -32.977 33.102 6.179   1.00 43.12  ? 89  PRO   A CG  1 
ATOM   659  C  CD  . PRO   A 1 91  ? -31.567 33.200 6.692   1.00 46.74  ? 89  PRO   A CD  1 
ATOM   660  N  N   . GLU   A 1 92  ? -30.544 29.910 5.624   1.00 48.39  ? 90  GLU   A N   1 
ATOM   661  C  CA  . GLU   A 1 92  ? -29.893 28.830 4.905   1.00 48.03  ? 90  GLU   A CA  1 
ATOM   662  C  C   . GLU   A 1 92  ? -28.377 28.953 5.012   1.00 46.96  ? 90  GLU   A C   1 
ATOM   663  O  O   . GLU   A 1 92  ? -27.808 30.038 4.813   1.00 41.59  ? 90  GLU   A O   1 
ATOM   664  C  CB  . GLU   A 1 92  ? -30.317 28.826 3.439   1.00 43.84  ? 90  GLU   A CB  1 
ATOM   665  C  CG  . GLU   A 1 92  ? -29.607 27.783 2.622   1.00 40.85  ? 90  GLU   A CG  1 
ATOM   666  C  CD  . GLU   A 1 92  ? -30.098 27.759 1.208   1.00 43.20  ? 90  GLU   A CD  1 
ATOM   667  O  OE1 . GLU   A 1 92  ? -30.422 28.862 0.701   1.00 41.86  ? 90  GLU   A OE1 1 
ATOM   668  O  OE2 . GLU   A 1 92  ? -30.117 26.662 0.595   1.00 47.09  ? 90  GLU   A OE2 1 
ATOM   669  N  N   . ILE   A 1 93  ? -27.745 27.819 5.312   1.00 41.88  ? 91  ILE   A N   1 
ATOM   670  C  CA  . ILE   A 1 93  ? -26.302 27.681 5.442   1.00 41.24  ? 91  ILE   A CA  1 
ATOM   671  C  C   . ILE   A 1 93  ? -25.817 26.903 4.226   1.00 39.39  ? 91  ILE   A C   1 
ATOM   672  O  O   . ILE   A 1 93  ? -26.403 25.872 3.876   1.00 44.22  ? 91  ILE   A O   1 
ATOM   673  C  CB  . ILE   A 1 93  ? -25.941 26.964 6.763   1.00 40.18  ? 91  ILE   A CB  1 
ATOM   674  C  CG1 . ILE   A 1 93  ? -26.182 27.875 7.976   1.00 40.84  ? 91  ILE   A CG1 1 
ATOM   675  C  CG2 . ILE   A 1 93  ? -24.505 26.451 6.767   1.00 38.09  ? 91  ILE   A CG2 1 
ATOM   676  C  CD1 . ILE   A 1 93  ? -26.440 27.118 9.244   1.00 46.50  ? 91  ILE   A CD1 1 
ATOM   677  N  N   . MET   A 1 94  ? -24.763 27.381 3.570   1.00 37.83  ? 92  MET   A N   1 
ATOM   678  C  CA  . MET   A 1 94  ? -24.294 26.746 2.336   1.00 36.54  ? 92  MET   A CA  1 
ATOM   679  C  C   . MET   A 1 94  ? -22.998 25.998 2.627   1.00 37.47  ? 92  MET   A C   1 
ATOM   680  O  O   . MET   A 1 94  ? -21.981 26.618 2.973   1.00 39.88  ? 92  MET   A O   1 
ATOM   681  C  CB  . MET   A 1 94  ? -24.083 27.773 1.224   1.00 33.60  ? 92  MET   A CB  1 
ATOM   682  C  CG  . MET   A 1 94  ? -25.352 28.501 0.805   1.00 37.39  ? 92  MET   A CG  1 
ATOM   683  S  SD  . MET   A 1 94  ? -26.611 27.384 0.175   1.00 36.05  ? 92  MET   A SD  1 
ATOM   684  C  CE  . MET   A 1 94  ? -25.860 26.894 -1.386  1.00 32.01  ? 92  MET   A CE  1 
ATOM   685  N  N   . VAL   A 1 95  ? -23.026 24.674 2.490   1.00 31.12  ? 93  VAL   A N   1 
ATOM   686  C  CA  . VAL   A 1 95  ? -21.822 23.860 2.611   1.00 32.40  ? 93  VAL   A CA  1 
ATOM   687  C  C   . VAL   A 1 95  ? -21.247 23.681 1.211   1.00 36.95  ? 93  VAL   A C   1 
ATOM   688  O  O   . VAL   A 1 95  ? -21.906 23.109 0.336   1.00 40.16  ? 93  VAL   A O   1 
ATOM   689  C  CB  . VAL   A 1 95  ? -22.132 22.504 3.247   1.00 29.88  ? 93  VAL   A CB  1 
ATOM   690  C  CG1 . VAL   A 1 95  ? -20.932 21.619 3.111   1.00 30.83  ? 93  VAL   A CG1 1 
ATOM   691  C  CG2 . VAL   A 1 95  ? -22.565 22.673 4.698   1.00 28.98  ? 93  VAL   A CG2 1 
ATOM   692  N  N   . ILE   A 1 96  ? -20.035 24.175 0.981   1.00 31.82  ? 94  ILE   A N   1 
ATOM   693  C  CA  . ILE   A 1 96  ? -19.545 24.358 -0.385  1.00 32.54  ? 94  ILE   A CA  1 
ATOM   694  C  C   . ILE   A 1 96  ? -18.398 23.439 -0.728  1.00 36.88  ? 94  ILE   A C   1 
ATOM   695  O  O   . ILE   A 1 96  ? -17.966 23.435 -1.892  1.00 47.72  ? 94  ILE   A O   1 
ATOM   696  C  CB  . ILE   A 1 96  ? -19.125 25.818 -0.659  1.00 34.46  ? 94  ILE   A CB  1 
ATOM   697  C  CG1 . ILE   A 1 96  ? -17.889 26.165 0.166   1.00 34.36  ? 94  ILE   A CG1 1 
ATOM   698  C  CG2 . ILE   A 1 96  ? -20.274 26.804 -0.380  1.00 39.16  ? 94  ILE   A CG2 1 
ATOM   699  C  CD1 . ILE   A 1 96  ? -17.162 27.360 -0.344  1.00 32.74  ? 94  ILE   A CD1 1 
ATOM   700  N  N   . GLY   A 1 97  ? -17.863 22.677 0.208   1.00 35.87  ? 95  GLY   A N   1 
ATOM   701  C  CA  . GLY   A 1 97  ? -16.742 21.910 -0.263  1.00 40.33  ? 95  GLY   A CA  1 
ATOM   702  C  C   . GLY   A 1 97  ? -15.836 21.221 0.715   1.00 39.15  ? 95  GLY   A C   1 
ATOM   703  O  O   . GLY   A 1 97  ? -15.682 21.612 1.876   1.00 38.69  ? 95  GLY   A O   1 
ATOM   704  N  N   . GLY   A 1 98  ? -15.128 20.251 0.148   1.00 50.69  ? 96  GLY   A N   1 
ATOM   705  C  CA  . GLY   A 1 98  ? -14.576 19.131 0.855   1.00 46.06  ? 96  GLY   A CA  1 
ATOM   706  C  C   . GLY   A 1 98  ? -15.455 17.936 0.604   1.00 44.75  ? 96  GLY   A C   1 
ATOM   707  O  O   . GLY   A 1 98  ? -16.646 17.962 0.927   1.00 49.04  ? 96  GLY   A O   1 
ATOM   708  N  N   . GLY   A 1 99  ? -14.908 16.902 -0.022  1.00 43.31  ? 97  GLY   A N   1 
ATOM   709  C  CA  . GLY   A 1 99  ? -15.590 15.627 0.028   1.00 45.47  ? 97  GLY   A CA  1 
ATOM   710  C  C   . GLY   A 1 99  ? -15.868 15.223 1.460   1.00 44.10  ? 97  GLY   A C   1 
ATOM   711  O  O   . GLY   A 1 99  ? -16.989 14.840 1.807   1.00 43.46  ? 97  GLY   A O   1 
ATOM   712  N  N   . ARG   A 1 100 ? -14.850 15.339 2.325   1.00 44.30  ? 98  ARG   A N   1 
ATOM   713  C  CA  . ARG   A 1 100 ? -15.052 14.994 3.729   1.00 49.65  ? 98  ARG   A CA  1 
ATOM   714  C  C   . ARG   A 1 100 ? -16.097 15.909 4.371   1.00 48.12  ? 98  ARG   A C   1 
ATOM   715  O  O   . ARG   A 1 100 ? -16.950 15.439 5.135   1.00 47.84  ? 98  ARG   A O   1 
ATOM   716  C  CB  . ARG   A 1 100 ? -13.718 15.039 4.492   1.00 44.53  ? 98  ARG   A CB  1 
ATOM   717  C  CG  . ARG   A 1 100 ? -13.768 14.573 5.975   1.00 54.86  ? 98  ARG   A CG  1 
ATOM   718  C  CD  . ARG   A 1 100 ? -14.756 13.408 6.253   1.00 64.38  ? 98  ARG   A CD  1 
ATOM   719  N  NE  . ARG   A 1 100 ? -14.850 13.062 7.681   1.00 71.08  ? 98  ARG   A NE  1 
ATOM   720  C  CZ  . ARG   A 1 100 ? -15.756 12.228 8.202   1.00 72.56  ? 98  ARG   A CZ  1 
ATOM   721  N  NH1 . ARG   A 1 100 ? -15.768 11.995 9.512   1.00 78.68  ? 98  ARG   A NH1 1 
ATOM   722  N  NH2 . ARG   A 1 100 ? -16.651 11.622 7.420   1.00 66.09  ? 98  ARG   A NH2 1 
ATOM   723  N  N   . VAL   A 1 101 ? -16.096 17.196 4.040   1.00 46.22  ? 99  VAL   A N   1 
ATOM   724  C  CA  . VAL   A 1 101 ? -17.076 18.153 4.635   1.00 40.39  ? 99  VAL   A CA  1 
ATOM   725  C  C   . VAL   A 1 101 ? -18.492 17.815 4.156   1.00 43.23  ? 99  VAL   A C   1 
ATOM   726  O  O   . VAL   A 1 101 ? -19.417 17.908 4.968   1.00 42.13  ? 99  VAL   A O   1 
ATOM   727  C  CB  . VAL   A 1 101 ? -16.671 19.615 4.380   1.00 36.80  ? 99  VAL   A CB  1 
ATOM   728  C  CG1 . VAL   A 1 101 ? -17.770 20.600 4.736   1.00 37.70  ? 99  VAL   A CG1 1 
ATOM   729  C  CG2 . VAL   A 1 101 ? -15.389 19.965 5.112   1.00 38.86  ? 99  VAL   A CG2 1 
ATOM   730  N  N   . TYR   A 1 102 ? -18.650 17.401 2.898   1.00 38.06  ? 100 TYR   A N   1 
ATOM   731  C  CA  . TYR   A 1 102 ? -19.979 17.019 2.358   1.00 36.76  ? 100 TYR   A CA  1 
ATOM   732  C  C   . TYR   A 1 102 ? -20.513 15.793 3.092   1.00 38.60  ? 100 TYR   A C   1 
ATOM   733  O  O   . TYR   A 1 102 ? -21.719 15.721 3.324   1.00 41.43  ? 100 TYR   A O   1 
ATOM   734  C  CB  . TYR   A 1 102 ? -19.890 16.683 0.871   1.00 44.16  ? 100 TYR   A CB  1 
ATOM   735  C  CG  . TYR   A 1 102 ? -19.700 17.824 -0.094  1.00 40.86  ? 100 TYR   A CG  1 
ATOM   736  C  CD1 . TYR   A 1 102 ? -20.356 19.030 0.068   1.00 39.85  ? 100 TYR   A CD1 1 
ATOM   737  C  CD2 . TYR   A 1 102 ? -18.885 17.675 -1.201  1.00 36.36  ? 100 TYR   A CD2 1 
ATOM   738  C  CE1 . TYR   A 1 102 ? -20.189 20.065 -0.834  1.00 38.46  ? 100 TYR   A CE1 1 
ATOM   739  C  CE2 . TYR   A 1 102 ? -18.701 18.701 -2.108  1.00 37.41  ? 100 TYR   A CE2 1 
ATOM   740  C  CZ  . TYR   A 1 102 ? -19.357 19.901 -1.926  1.00 40.73  ? 100 TYR   A CZ  1 
ATOM   741  O  OH  . TYR   A 1 102 ? -19.177 20.911 -2.822  1.00 37.49  ? 100 TYR   A OH  1 
ATOM   742  N  N   . GLU   A 1 103 ? -19.646 14.831 3.385   1.00 40.67  ? 101 GLU   A N   1 
ATOM   743  C  CA  . GLU   A 1 103 ? -20.049 13.607 4.126   1.00 46.22  ? 101 GLU   A CA  1 
ATOM   744  C  C   . GLU   A 1 103 ? -20.495 13.966 5.542   1.00 43.19  ? 101 GLU   A C   1 
ATOM   745  O  O   . GLU   A 1 103 ? -21.451 13.356 6.022   1.00 42.36  ? 101 GLU   A O   1 
ATOM   746  C  CB  . GLU   A 1 103 ? -18.879 12.627 4.184   1.00 45.30  ? 101 GLU   A CB  1 
ATOM   747  C  CG  . GLU   A 1 103 ? -19.180 11.277 3.567   1.00 58.44  ? 101 GLU   A CG  1 
ATOM   748  C  CD  . GLU   A 1 103 ? -18.093 10.789 2.626   1.00 84.41  ? 101 GLU   A CD  1 
ATOM   749  O  OE1 . GLU   A 1 103 ? -16.904 10.974 2.956   1.00 82.11  ? 101 GLU   A OE1 1 
ATOM   750  O  OE2 . GLU   A 1 103 ? -18.437 10.233 1.563   1.00 98.24  ? 101 GLU   A OE2 1 
ATOM   751  N  N   . GLN   A 1 104 ? -19.799 14.903 6.181   1.00 46.14  ? 102 GLN   A N   1 
ATOM   752  C  CA  . GLN   A 1 104 ? -20.114 15.295 7.576   1.00 39.54  ? 102 GLN   A CA  1 
ATOM   753  C  C   . GLN   A 1 104 ? -21.427 16.075 7.618   1.00 39.83  ? 102 GLN   A C   1 
ATOM   754  O  O   . GLN   A 1 104 ? -22.095 16.021 8.654   1.00 37.97  ? 102 GLN   A O   1 
ATOM   755  C  CB  . GLN   A 1 104 ? -18.966 16.119 8.146   1.00 38.60  ? 102 GLN   A CB  1 
ATOM   756  C  CG  . GLN   A 1 104 ? -17.762 15.294 8.559   1.00 45.77  ? 102 GLN   A CG  1 
ATOM   757  C  CD  . GLN   A 1 104 ? -16.608 16.172 8.968   1.00 48.88  ? 102 GLN   A CD  1 
ATOM   758  O  OE1 . GLN   A 1 104 ? -16.058 16.920 8.166   1.00 47.07  ? 102 GLN   A OE1 1 
ATOM   759  N  NE2 . GLN   A 1 104 ? -16.233 16.090 10.232  1.00 56.80  ? 102 GLN   A NE2 1 
ATOM   760  N  N   . PHE   A 1 105 ? -21.795 16.754 6.529   1.00 39.55  ? 103 PHE   A N   1 
ATOM   761  C  CA  . PHE   A 1 105 ? -22.995 17.580 6.597   1.00 36.56  ? 103 PHE   A CA  1 
ATOM   762  C  C   . PHE   A 1 105 ? -24.212 17.036 5.854   1.00 38.59  ? 103 PHE   A C   1 
ATOM   763  O  O   . PHE   A 1 105 ? -25.311 17.580 6.045   1.00 40.86  ? 103 PHE   A O   1 
ATOM   764  C  CB  . PHE   A 1 105 ? -22.693 18.996 6.081   1.00 39.34  ? 103 PHE   A CB  1 
ATOM   765  C  CG  . PHE   A 1 105 ? -22.003 19.868 7.093   1.00 37.63  ? 103 PHE   A CG  1 
ATOM   766  C  CD1 . PHE   A 1 105 ? -20.609 19.866 7.206   1.00 38.33  ? 103 PHE   A CD1 1 
ATOM   767  C  CD2 . PHE   A 1 105 ? -22.744 20.675 7.941   1.00 32.71  ? 103 PHE   A CD2 1 
ATOM   768  C  CE1 . PHE   A 1 105 ? -19.966 20.670 8.151   1.00 39.84  ? 103 PHE   A CE1 1 
ATOM   769  C  CE2 . PHE   A 1 105 ? -22.116 21.481 8.900   1.00 38.42  ? 103 PHE   A CE2 1 
ATOM   770  C  CZ  . PHE   A 1 105 ? -20.727 21.484 9.003   1.00 41.82  ? 103 PHE   A CZ  1 
ATOM   771  N  N   . LEU   A 1 106 ? -24.065 16.001 5.014   1.00 39.24  ? 104 LEU   A N   1 
ATOM   772  C  CA  . LEU   A 1 106 ? -25.239 15.442 4.347   1.00 37.47  ? 104 LEU   A CA  1 
ATOM   773  C  C   . LEU   A 1 106 ? -26.315 15.005 5.334   1.00 41.98  ? 104 LEU   A C   1 
ATOM   774  O  O   . LEU   A 1 106 ? -27.486 15.368 5.141   1.00 44.82  ? 104 LEU   A O   1 
ATOM   775  C  CB  . LEU   A 1 106 ? -24.828 14.298 3.416   1.00 39.05  ? 104 LEU   A CB  1 
ATOM   776  C  CG  . LEU   A 1 106 ? -25.914 13.781 2.447   1.00 41.73  ? 104 LEU   A CG  1 
ATOM   777  C  CD1 . LEU   A 1 106 ? -26.301 14.818 1.388   1.00 43.22  ? 104 LEU   A CD1 1 
ATOM   778  C  CD2 . LEU   A 1 106 ? -25.502 12.462 1.753   1.00 44.50  ? 104 LEU   A CD2 1 
ATOM   779  N  N   . PRO   A 1 107 ? -25.997 14.284 6.417   1.00 42.77  ? 105 PRO   A N   1 
ATOM   780  C  CA  . PRO   A 1 107 ? -27.052 13.913 7.369   1.00 37.41  ? 105 PRO   A CA  1 
ATOM   781  C  C   . PRO   A 1 107 ? -27.755 15.095 7.995   1.00 42.99  ? 105 PRO   A C   1 
ATOM   782  O  O   . PRO   A 1 107 ? -28.808 14.895 8.608   1.00 51.37  ? 105 PRO   A O   1 
ATOM   783  C  CB  . PRO   A 1 107 ? -26.289 13.124 8.436   1.00 39.01  ? 105 PRO   A CB  1 
ATOM   784  C  CG  . PRO   A 1 107 ? -25.112 12.617 7.725   1.00 38.84  ? 105 PRO   A CG  1 
ATOM   785  C  CD  . PRO   A 1 107 ? -24.700 13.761 6.866   1.00 41.19  ? 105 PRO   A CD  1 
ATOM   786  N  N   . LYS   A 1 108 ? -27.219 16.312 7.899   1.00 42.32  ? 106 LYS   A N   1 
ATOM   787  C  CA  . LYS   A 1 108 ? -27.878 17.450 8.528   1.00 44.91  ? 106 LYS   A CA  1 
ATOM   788  C  C   . LYS   A 1 108 ? -28.462 18.418 7.505   1.00 47.62  ? 106 LYS   A C   1 
ATOM   789  O  O   . LYS   A 1 108 ? -28.859 19.534 7.870   1.00 47.06  ? 106 LYS   A O   1 
ATOM   790  C  CB  . LYS   A 1 108 ? -26.922 18.168 9.488   1.00 42.95  ? 106 LYS   A CB  1 
ATOM   791  C  CG  . LYS   A 1 108 ? -26.500 17.264 10.648  1.00 45.31  ? 106 LYS   A CG  1 
ATOM   792  C  CD  . LYS   A 1 108 ? -25.589 17.923 11.675  1.00 45.28  ? 106 LYS   A CD  1 
ATOM   793  C  CE  . LYS   A 1 108 ? -26.394 18.903 12.535  1.00 55.13  ? 106 LYS   A CE  1 
ATOM   794  N  NZ  . LYS   A 1 108 ? -27.347 18.266 13.495  1.00 49.23  ? 106 LYS   A NZ  1 
ATOM   795  N  N   . ALA   A 1 109 ? -28.559 17.993 6.241   1.00 46.30  ? 107 ALA   A N   1 
ATOM   796  C  CA  . ALA   A 1 109 ? -28.908 18.864 5.126   1.00 45.94  ? 107 ALA   A CA  1 
ATOM   797  C  C   . ALA   A 1 109 ? -30.290 18.532 4.585   1.00 45.80  ? 107 ALA   A C   1 
ATOM   798  O  O   . ALA   A 1 109 ? -30.671 17.360 4.510   1.00 44.11  ? 107 ALA   A O   1 
ATOM   799  C  CB  . ALA   A 1 109 ? -27.887 18.735 3.999   1.00 41.21  ? 107 ALA   A CB  1 
ATOM   800  N  N   . GLN   A 1 110 ? -31.032 19.569 4.184   1.00 45.43  ? 108 GLN   A N   1 
ATOM   801  C  CA  . GLN   A 1 110 ? -32.339 19.370 3.578   1.00 45.64  ? 108 GLN   A CA  1 
ATOM   802  C  C   . GLN   A 1 110 ? -32.376 19.703 2.106   1.00 46.44  ? 108 GLN   A C   1 
ATOM   803  O  O   . GLN   A 1 110 ? -33.320 19.292 1.429   1.00 52.66  ? 108 GLN   A O   1 
ATOM   804  C  CB  . GLN   A 1 110 ? -33.415 20.211 4.282   1.00 57.78  ? 108 GLN   A CB  1 
ATOM   805  C  CG  . GLN   A 1 110 ? -33.677 19.835 5.755   1.00 71.12  ? 108 GLN   A CG  1 
ATOM   806  C  CD  . GLN   A 1 110 ? -32.703 20.494 6.732   1.00 70.43  ? 108 GLN   A CD  1 
ATOM   807  O  OE1 . GLN   A 1 110 ? -32.694 21.716 6.881   1.00 75.85  ? 108 GLN   A OE1 1 
ATOM   808  N  NE2 . GLN   A 1 110 ? -31.876 19.684 7.394   1.00 70.53  ? 108 GLN   A NE2 1 
ATOM   809  N  N   . LYS   A 1 111 ? -31.382 20.422 1.593   1.00 45.74  ? 109 LYS   A N   1 
ATOM   810  C  CA  . LYS   A 1 111 ? -31.377 20.872 0.210   1.00 39.41  ? 109 LYS   A CA  1 
ATOM   811  C  C   . LYS   A 1 111 ? -30.035 20.566 -0.437  1.00 41.57  ? 109 LYS   A C   1 
ATOM   812  O  O   . LYS   A 1 111 ? -28.986 20.682 0.206   1.00 38.47  ? 109 LYS   A O   1 
ATOM   813  C  CB  . LYS   A 1 111 ? -31.664 22.380 0.120   1.00 41.65  ? 109 LYS   A CB  1 
ATOM   814  C  CG  . LYS   A 1 111 ? -32.388 22.799 -1.142  1.00 39.58  ? 109 LYS   A CG  1 
ATOM   815  C  CD  . LYS   A 1 111 ? -32.873 24.239 -1.078  1.00 41.49  ? 109 LYS   A CD  1 
ATOM   816  C  CE  . LYS   A 1 111 ? -33.519 24.647 -2.403  1.00 40.96  ? 109 LYS   A CE  1 
ATOM   817  N  NZ  . LYS   A 1 111 ? -33.673 26.122 -2.556  1.00 45.85  ? 109 LYS   A NZ  1 
ATOM   818  N  N   . LEU   A 1 112 ? -30.076 20.208 -1.724  1.00 41.85  ? 110 LEU   A N   1 
ATOM   819  C  CA  . LEU   A 1 112 ? -28.888 19.876 -2.502  1.00 39.62  ? 110 LEU   A CA  1 
ATOM   820  C  C   . LEU   A 1 112 ? -28.901 20.705 -3.786  1.00 40.22  ? 110 LEU   A C   1 
ATOM   821  O  O   . LEU   A 1 112 ? -29.919 20.749 -4.487  1.00 39.44  ? 110 LEU   A O   1 
ATOM   822  C  CB  . LEU   A 1 112 ? -28.867 18.385 -2.847  1.00 42.01  ? 110 LEU   A CB  1 
ATOM   823  C  CG  . LEU   A 1 112 ? -28.454 17.405 -1.749  1.00 43.28  ? 110 LEU   A CG  1 
ATOM   824  C  CD1 . LEU   A 1 112 ? -28.268 15.990 -2.315  1.00 42.13  ? 110 LEU   A CD1 1 
ATOM   825  C  CD2 . LEU   A 1 112 ? -27.233 17.884 -1.030  1.00 43.84  ? 110 LEU   A CD2 1 
ATOM   826  N  N   . TYR   A 1 113 ? -27.789 21.379 -4.085  1.00 39.23  ? 111 TYR   A N   1 
ATOM   827  C  CA  . TYR   A 1 113 ? -27.632 22.124 -5.332  1.00 38.28  ? 111 TYR   A CA  1 
ATOM   828  C  C   . TYR   A 1 113 ? -26.506 21.474 -6.128  1.00 40.33  ? 111 TYR   A C   1 
ATOM   829  O  O   . TYR   A 1 113 ? -25.324 21.681 -5.819  1.00 41.16  ? 111 TYR   A O   1 
ATOM   830  C  CB  . TYR   A 1 113 ? -27.308 23.591 -5.085  1.00 37.15  ? 111 TYR   A CB  1 
ATOM   831  C  CG  . TYR   A 1 113 ? -28.317 24.382 -4.296  1.00 36.12  ? 111 TYR   A CG  1 
ATOM   832  C  CD1 . TYR   A 1 113 ? -28.362 24.282 -2.916  1.00 38.69  ? 111 TYR   A CD1 1 
ATOM   833  C  CD2 . TYR   A 1 113 ? -29.166 25.294 -4.918  1.00 34.02  ? 111 TYR   A CD2 1 
ATOM   834  C  CE1 . TYR   A 1 113 ? -29.260 25.034 -2.165  1.00 39.72  ? 111 TYR   A CE1 1 
ATOM   835  C  CE2 . TYR   A 1 113 ? -30.062 26.048 -4.177  1.00 37.89  ? 111 TYR   A CE2 1 
ATOM   836  C  CZ  . TYR   A 1 113 ? -30.105 25.908 -2.797  1.00 38.33  ? 111 TYR   A CZ  1 
ATOM   837  O  OH  . TYR   A 1 113 ? -30.982 26.639 -2.032  1.00 35.44  ? 111 TYR   A OH  1 
ATOM   838  N  N   . LEU   A 1 114 ? -26.867 20.727 -7.168  1.00 35.63  ? 112 LEU   A N   1 
ATOM   839  C  CA  . LEU   A 1 114 ? -25.920 19.941 -7.941  1.00 35.62  ? 112 LEU   A CA  1 
ATOM   840  C  C   . LEU   A 1 114 ? -25.761 20.487 -9.356  1.00 38.97  ? 112 LEU   A C   1 
ATOM   841  O  O   . LEU   A 1 114 ? -26.747 20.862 -10.005 1.00 40.24  ? 112 LEU   A O   1 
ATOM   842  C  CB  . LEU   A 1 114 ? -26.385 18.484 -8.019  1.00 35.70  ? 112 LEU   A CB  1 
ATOM   843  C  CG  . LEU   A 1 114 ? -26.573 17.766 -6.687  1.00 40.05  ? 112 LEU   A CG  1 
ATOM   844  C  CD1 . LEU   A 1 114 ? -26.973 16.310 -6.915  1.00 36.28  ? 112 LEU   A CD1 1 
ATOM   845  C  CD2 . LEU   A 1 114 ? -25.319 17.885 -5.822  1.00 39.87  ? 112 LEU   A CD2 1 
ATOM   846  N  N   . THR   A 1 115 ? -24.526 20.485 -9.860  1.00 37.56  ? 113 THR   A N   1 
ATOM   847  C  CA  . THR   A 1 115 ? -24.274 20.702 -11.275 1.00 36.22  ? 113 THR   A CA  1 
ATOM   848  C  C   . THR   A 1 115 ? -23.720 19.418 -11.874 1.00 39.08  ? 113 THR   A C   1 
ATOM   849  O  O   . THR   A 1 115 ? -22.626 18.977 -11.504 1.00 39.89  ? 113 THR   A O   1 
ATOM   850  C  CB  . THR   A 1 115 ? -23.308 21.853 -11.506 1.00 36.38  ? 113 THR   A CB  1 
ATOM   851  O  OG1 . THR   A 1 115 ? -23.890 23.058 -10.993 1.00 36.58  ? 113 THR   A OG1 1 
ATOM   852  C  CG2 . THR   A 1 115 ? -23.075 22.014 -12.997 1.00 36.69  ? 113 THR   A CG2 1 
ATOM   853  N  N   . HIS   A 1 116 ? -24.484 18.818 -12.783 1.00 39.50  ? 114 HIS   A N   1 
ATOM   854  C  CA  . HIS   A 1 116 ? -24.090 17.594 -13.471 1.00 42.65  ? 114 HIS   A CA  1 
ATOM   855  C  C   . HIS   A 1 116 ? -23.357 17.985 -14.741 1.00 42.70  ? 114 HIS   A C   1 
ATOM   856  O  O   . HIS   A 1 116 ? -23.968 18.526 -15.671 1.00 41.19  ? 114 HIS   A O   1 
ATOM   857  C  CB  . HIS   A 1 116 ? -25.310 16.754 -13.825 1.00 46.45  ? 114 HIS   A CB  1 
ATOM   858  C  CG  . HIS   A 1 116 ? -26.016 16.173 -12.644 1.00 42.73  ? 114 HIS   A CG  1 
ATOM   859  N  ND1 . HIS   A 1 116 ? -25.521 15.098 -11.937 1.00 49.80  ? 114 HIS   A ND1 1 
ATOM   860  C  CD2 . HIS   A 1 116 ? -27.194 16.498 -12.064 1.00 37.50  ? 114 HIS   A CD2 1 
ATOM   861  C  CE1 . HIS   A 1 116 ? -26.361 14.792 -10.963 1.00 46.45  ? 114 HIS   A CE1 1 
ATOM   862  N  NE2 . HIS   A 1 116 ? -27.382 15.629 -11.016 1.00 43.17  ? 114 HIS   A NE2 1 
ATOM   863  N  N   . ILE   A 1 117 ? -22.060 17.700 -14.798 1.00 44.65  ? 115 ILE   A N   1 
ATOM   864  C  CA  . ILE   A 1 117 ? -21.232 18.072 -15.936 1.00 51.21  ? 115 ILE   A CA  1 
ATOM   865  C  C   . ILE   A 1 117 ? -20.935 16.821 -16.744 1.00 51.10  ? 115 ILE   A C   1 
ATOM   866  O  O   . ILE   A 1 117 ? -20.590 15.777 -16.176 1.00 47.15  ? 115 ILE   A O   1 
ATOM   867  C  CB  . ILE   A 1 117 ? -19.946 18.786 -15.489 1.00 50.01  ? 115 ILE   A CB  1 
ATOM   868  C  CG1 . ILE   A 1 117 ? -20.282 19.845 -14.440 1.00 43.72  ? 115 ILE   A CG1 1 
ATOM   869  C  CG2 . ILE   A 1 117 ? -19.246 19.418 -16.669 1.00 46.03  ? 115 ILE   A CG2 1 
ATOM   870  C  CD1 . ILE   A 1 117 ? -19.077 20.350 -13.734 1.00 41.73  ? 115 ILE   A CD1 1 
ATOM   871  N  N   . ASP   A 1 118 ? -21.100 16.922 -18.066 1.00 51.31  ? 116 ASP   A N   1 
ATOM   872  C  CA  . ASP   A 1 118 ? -20.904 15.785 -18.963 1.00 57.78  ? 116 ASP   A CA  1 
ATOM   873  C  C   . ASP   A 1 118 ? -19.421 15.724 -19.332 1.00 61.83  ? 116 ASP   A C   1 
ATOM   874  O  O   . ASP   A 1 118 ? -18.990 16.117 -20.418 1.00 63.80  ? 116 ASP   A O   1 
ATOM   875  C  CB  . ASP   A 1 118 ? -21.824 15.894 -20.182 1.00 57.00  ? 116 ASP   A CB  1 
ATOM   876  C  CG  . ASP   A 1 118 ? -23.316 15.600 -19.832 1.00 70.09  ? 116 ASP   A CG  1 
ATOM   877  O  OD1 . ASP   A 1 118 ? -23.643 14.472 -19.376 1.00 72.55  ? 116 ASP   A OD1 1 
ATOM   878  O  OD2 . ASP   A 1 118 ? -24.173 16.508 -19.982 1.00 63.83  ? 116 ASP   A OD2 1 
ATOM   879  N  N   . ALA   A 1 119 ? -18.633 15.233 -18.366 1.00 61.09  ? 117 ALA   A N   1 
ATOM   880  C  CA  . ALA   A 1 119 ? -17.182 15.155 -18.485 1.00 56.79  ? 117 ALA   A CA  1 
ATOM   881  C  C   . ALA   A 1 119 ? -16.626 14.004 -17.657 1.00 64.95  ? 117 ALA   A C   1 
ATOM   882  O  O   . ALA   A 1 119 ? -17.067 13.744 -16.536 1.00 68.39  ? 117 ALA   A O   1 
ATOM   883  C  CB  . ALA   A 1 119 ? -16.491 16.450 -18.042 1.00 55.86  ? 117 ALA   A CB  1 
ATOM   884  N  N   . GLU   A 1 120 ? -15.636 13.341 -18.231 1.00 71.65  ? 118 GLU   A N   1 
ATOM   885  C  CA  . GLU   A 1 120 ? -14.845 12.323 -17.566 1.00 70.98  ? 118 GLU   A CA  1 
ATOM   886  C  C   . GLU   A 1 120 ? -13.818 13.007 -16.680 1.00 73.70  ? 118 GLU   A C   1 
ATOM   887  O  O   . GLU   A 1 120 ? -13.103 13.903 -17.140 1.00 74.10  ? 118 GLU   A O   1 
ATOM   888  C  CB  . GLU   A 1 120 ? -14.138 11.502 -18.635 1.00 84.61  ? 118 GLU   A CB  1 
ATOM   889  C  CG  . GLU   A 1 120 ? -13.777 10.093 -18.318 1.00 94.31  ? 118 GLU   A CG  1 
ATOM   890  C  CD  . GLU   A 1 120 ? -13.513 9.314  -19.605 1.00 106.05 ? 118 GLU   A CD  1 
ATOM   891  O  OE1 . GLU   A 1 120 ? -12.640 9.752  -20.390 1.00 104.48 ? 118 GLU   A OE1 1 
ATOM   892  O  OE2 . GLU   A 1 120 ? -14.200 8.301  -19.868 1.00 103.11 ? 118 GLU   A OE2 1 
ATOM   893  N  N   . VAL   A 1 121 ? -13.733 12.606 -15.415 1.00 78.10  ? 119 VAL   A N   1 
ATOM   894  C  CA  . VAL   A 1 121 ? -12.689 13.147 -14.551 1.00 74.33  ? 119 VAL   A CA  1 
ATOM   895  C  C   . VAL   A 1 121 ? -12.090 12.035 -13.713 1.00 85.40  ? 119 VAL   A C   1 
ATOM   896  O  O   . VAL   A 1 121 ? -12.810 11.269 -13.061 1.00 89.38  ? 119 VAL   A O   1 
ATOM   897  C  CB  . VAL   A 1 121 ? -13.178 14.287 -13.644 1.00 67.51  ? 119 VAL   A CB  1 
ATOM   898  C  CG1 . VAL   A 1 121 ? -12.183 14.501 -12.522 1.00 76.57  ? 119 VAL   A CG1 1 
ATOM   899  C  CG2 . VAL   A 1 121 ? -13.336 15.560 -14.455 1.00 62.43  ? 119 VAL   A CG2 1 
ATOM   900  N  N   . GLU   A 1 122 ? -10.763 11.980 -13.727 1.00 98.59  ? 120 GLU   A N   1 
ATOM   901  C  CA  . GLU   A 1 122 ? -9.962  10.991 -13.028 1.00 98.22  ? 120 GLU   A CA  1 
ATOM   902  C  C   . GLU   A 1 122 ? -9.679  11.548 -11.634 1.00 100.04 ? 120 GLU   A C   1 
ATOM   903  O  O   . GLU   A 1 122 ? -8.966  12.546 -11.490 1.00 104.22 ? 120 GLU   A O   1 
ATOM   904  C  CB  . GLU   A 1 122 ? -8.685  10.737 -13.830 1.00 103.57 ? 120 GLU   A CB  1 
ATOM   905  C  CG  . GLU   A 1 122 ? -7.922  9.446  -13.567 1.00 110.06 ? 120 GLU   A CG  1 
ATOM   906  C  CD  . GLU   A 1 122 ? -7.083  9.512  -12.305 1.00 124.24 ? 120 GLU   A CD  1 
ATOM   907  O  OE1 . GLU   A 1 122 ? -6.844  10.632 -11.797 1.00 122.27 ? 120 GLU   A OE1 1 
ATOM   908  O  OE2 . GLU   A 1 122 ? -6.594  8.447  -11.866 1.00 132.44 ? 120 GLU   A OE2 1 
ATOM   909  N  N   . GLY   A 1 123 ? -10.271 10.937 -10.610 1.00 98.02  ? 121 GLY   A N   1 
ATOM   910  C  CA  . GLY   A 1 123 ? -9.941  11.265 -9.221  1.00 93.34  ? 121 GLY   A CA  1 
ATOM   911  C  C   . GLY   A 1 123 ? -10.657 10.312 -8.261  1.00 88.77  ? 121 GLY   A C   1 
ATOM   912  O  O   . GLY   A 1 123 ? -11.649 9.704  -8.702  1.00 88.31  ? 121 GLY   A O   1 
ATOM   913  N  N   . ASP   A 1 124 ? -10.230 10.118 -6.986  1.00 85.12  ? 122 ASP   A N   1 
ATOM   914  C  CA  . ASP   A 1 124 ? -11.116 9.419  -6.049  1.00 85.47  ? 122 ASP   A CA  1 
ATOM   915  C  C   . ASP   A 1 124 ? -11.734 10.345 -5.020  1.00 79.59  ? 122 ASP   A C   1 
ATOM   916  O  O   . ASP   A 1 124 ? -11.811 9.968  -3.852  1.00 86.56  ? 122 ASP   A O   1 
ATOM   917  C  CB  . ASP   A 1 124 ? -10.483 8.315  -5.193  1.00 88.54  ? 122 ASP   A CB  1 
ATOM   918  C  CG  . ASP   A 1 124 ? -10.007 7.102  -5.987  1.00 96.17  ? 122 ASP   A CG  1 
ATOM   919  O  OD1 . ASP   A 1 124 ? -10.524 6.896  -7.098  1.00 95.54  ? 122 ASP   A OD1 1 
ATOM   920  O  OD2 . ASP   A 1 124 ? -9.255  6.219  -5.447  1.00 108.03 ? 122 ASP   A OD2 1 
ATOM   921  N  N   . THR   A 1 125 ? -12.117 11.551 -5.364  1.00 75.62  ? 123 THR   A N   1 
ATOM   922  C  CA  . THR   A 1 125 ? -12.904 12.343 -4.432  1.00 68.13  ? 123 THR   A CA  1 
ATOM   923  C  C   . THR   A 1 125 ? -14.333 12.328 -4.967  1.00 65.15  ? 123 THR   A C   1 
ATOM   924  O  O   . THR   A 1 125 ? -14.618 12.879 -6.038  1.00 66.20  ? 123 THR   A O   1 
ATOM   925  C  CB  . THR   A 1 125 ? -12.302 13.734 -4.299  1.00 68.75  ? 123 THR   A CB  1 
ATOM   926  O  OG1 . THR   A 1 125 ? -10.948 13.561 -3.881  1.00 76.80  ? 123 THR   A OG1 1 
ATOM   927  C  CG2 . THR   A 1 125 ? -12.994 14.535 -3.179  1.00 66.41  ? 123 THR   A CG2 1 
ATOM   928  N  N   . HIS   A 1 126 ? -15.215 11.643 -4.246  1.00 65.66  ? 124 HIS   A N   1 
ATOM   929  C  CA  . HIS   A 1 126 ? -16.570 11.386 -4.703  1.00 60.49  ? 124 HIS   A CA  1 
ATOM   930  C  C   . HIS   A 1 126 ? -17.563 12.089 -3.790  1.00 57.08  ? 124 HIS   A C   1 
ATOM   931  O  O   . HIS   A 1 126 ? -17.318 12.286 -2.593  1.00 50.89  ? 124 HIS   A O   1 
ATOM   932  C  CB  . HIS   A 1 126 ? -16.873 9.882  -4.757  1.00 61.61  ? 124 HIS   A CB  1 
ATOM   933  C  CG  . HIS   A 1 126 ? -15.911 9.096  -5.600  1.00 73.25  ? 124 HIS   A CG  1 
ATOM   934  N  ND1 . HIS   A 1 126 ? -16.120 8.862  -6.946  1.00 76.96  ? 124 HIS   A ND1 1 
ATOM   935  C  CD2 . HIS   A 1 126 ? -14.751 8.467  -5.289  1.00 74.46  ? 124 HIS   A CD2 1 
ATOM   936  C  CE1 . HIS   A 1 126 ? -15.127 8.135  -7.428  1.00 75.40  ? 124 HIS   A CE1 1 
ATOM   937  N  NE2 . HIS   A 1 126 ? -14.282 7.882  -6.444  1.00 79.60  ? 124 HIS   A NE2 1 
ATOM   938  N  N   . PHE   A 1 127 ? -18.662 12.518 -4.388  1.00 58.62  ? 125 PHE   A N   1 
ATOM   939  C  CA  . PHE   A 1 127 ? -19.758 13.062 -3.621  1.00 51.45  ? 125 PHE   A CA  1 
ATOM   940  C  C   . PHE   A 1 127 ? -20.472 11.925 -2.902  1.00 52.52  ? 125 PHE   A C   1 
ATOM   941  O  O   . PHE   A 1 127 ? -20.531 10.801 -3.412  1.00 59.91  ? 125 PHE   A O   1 
ATOM   942  C  CB  . PHE   A 1 127 ? -20.725 13.785 -4.541  1.00 47.32  ? 125 PHE   A CB  1 
ATOM   943  C  CG  . PHE   A 1 127 ? -21.748 14.613 -3.828  1.00 46.44  ? 125 PHE   A CG  1 
ATOM   944  C  CD1 . PHE   A 1 127 ? -21.419 15.858 -3.313  1.00 47.25  ? 125 PHE   A CD1 1 
ATOM   945  C  CD2 . PHE   A 1 127 ? -23.041 14.148 -3.667  1.00 44.59  ? 125 PHE   A CD2 1 
ATOM   946  C  CE1 . PHE   A 1 127 ? -22.362 16.634 -2.653  1.00 40.39  ? 125 PHE   A CE1 1 
ATOM   947  C  CE2 . PHE   A 1 127 ? -23.986 14.915 -3.020  1.00 45.97  ? 125 PHE   A CE2 1 
ATOM   948  C  CZ  . PHE   A 1 127 ? -23.642 16.166 -2.501  1.00 42.09  ? 125 PHE   A CZ  1 
ATOM   949  N  N   . PRO   A 1 128 ? -21.015 12.192 -1.716  1.00 53.98  ? 126 PRO   A N   1 
ATOM   950  C  CA  . PRO   A 1 128 ? -21.687 11.134 -0.958  1.00 54.95  ? 126 PRO   A CA  1 
ATOM   951  C  C   . PRO   A 1 128 ? -22.925 10.605 -1.667  1.00 63.23  ? 126 PRO   A C   1 
ATOM   952  O  O   . PRO   A 1 128 ? -23.737 11.351 -2.234  1.00 64.95  ? 126 PRO   A O   1 
ATOM   953  C  CB  . PRO   A 1 128 ? -22.052 11.821 0.364   1.00 52.20  ? 126 PRO   A CB  1 
ATOM   954  C  CG  . PRO   A 1 128 ? -21.013 12.854 0.504   1.00 49.26  ? 126 PRO   A CG  1 
ATOM   955  C  CD  . PRO   A 1 128 ? -20.832 13.394 -0.892  1.00 49.55  ? 126 PRO   A CD  1 
ATOM   956  N  N   . ASP   A 1 129 ? -23.033 9.286  -1.634  1.00 67.90  ? 127 ASP   A N   1 
ATOM   957  C  CA  . ASP   A 1 129 ? -24.287 8.608  -1.913  1.00 75.45  ? 127 ASP   A CA  1 
ATOM   958  C  C   . ASP   A 1 129 ? -25.463 9.127  -1.105  1.00 73.84  ? 127 ASP   A C   1 
ATOM   959  O  O   . ASP   A 1 129 ? -25.420 9.178  0.126   1.00 72.19  ? 127 ASP   A O   1 
ATOM   960  C  CB  . ASP   A 1 129 ? -24.051 7.121  -1.746  1.00 77.74  ? 127 ASP   A CB  1 
ATOM   961  C  CG  . ASP   A 1 129 ? -23.378 6.597  -2.953  1.00 92.00  ? 127 ASP   A CG  1 
ATOM   962  O  OD1 . ASP   A 1 129 ? -23.792 7.175  -3.992  1.00 89.62  ? 127 ASP   A OD1 1 
ATOM   963  O  OD2 . ASP   A 1 129 ? -22.389 5.851  -2.870  1.00 103.43 ? 127 ASP   A OD2 1 
ATOM   964  N  N   . TYR   A 1 130 ? -26.495 9.546  -1.850  1.00 79.04  ? 128 TYR   A N   1 
ATOM   965  C  CA  . TYR   A 1 130 ? -27.794 10.041 -1.408  1.00 76.05  ? 128 TYR   A CA  1 
ATOM   966  C  C   . TYR   A 1 130 ? -28.752 9.125  -2.136  1.00 87.80  ? 128 TYR   A C   1 
ATOM   967  O  O   . TYR   A 1 130 ? -28.976 9.231  -3.343  1.00 89.15  ? 128 TYR   A O   1 
ATOM   968  C  CB  . TYR   A 1 130 ? -28.010 11.479 -1.738  1.00 70.11  ? 128 TYR   A CB  1 
ATOM   969  C  CG  . TYR   A 1 130 ? -27.801 11.830 -3.213  1.00 70.43  ? 128 TYR   A CG  1 
ATOM   970  C  CD1 . TYR   A 1 130 ? -26.516 12.040 -3.735  1.00 71.62  ? 128 TYR   A CD1 1 
ATOM   971  C  CD2 . TYR   A 1 130 ? -28.885 12.045 -4.063  1.00 63.82  ? 128 TYR   A CD2 1 
ATOM   972  C  CE1 . TYR   A 1 130 ? -26.325 12.390 -5.083  1.00 68.92  ? 128 TYR   A CE1 1 
ATOM   973  C  CE2 . TYR   A 1 130 ? -28.701 12.406 -5.389  1.00 59.63  ? 128 TYR   A CE2 1 
ATOM   974  C  CZ  . TYR   A 1 130 ? -27.419 12.580 -5.893  1.00 65.06  ? 128 TYR   A CZ  1 
ATOM   975  O  OH  . TYR   A 1 130 ? -27.185 12.941 -7.205  1.00 59.64  ? 128 TYR   A OH  1 
ATOM   976  N  N   . GLU   A 1 131 ? -29.145 8.121  -1.436  1.00 92.13  ? 129 GLU   A N   1 
ATOM   977  C  CA  . GLU   A 1 131 ? -30.187 7.195  -1.825  1.00 91.78  ? 129 GLU   A CA  1 
ATOM   978  C  C   . GLU   A 1 131 ? -31.480 7.919  -2.247  1.00 91.36  ? 129 GLU   A C   1 
ATOM   979  O  O   . GLU   A 1 131 ? -32.007 8.814  -1.558  1.00 88.45  ? 129 GLU   A O   1 
ATOM   980  C  CB  . GLU   A 1 131 ? -30.291 6.247  -0.629  1.00 93.07  ? 129 GLU   A CB  1 
ATOM   981  C  CG  . GLU   A 1 131 ? -30.950 6.840  0.676   1.00 99.89  ? 129 GLU   A CG  1 
ATOM   982  C  CD  . GLU   A 1 131 ? -30.048 7.851  1.432   1.00 107.66 ? 129 GLU   A CD  1 
ATOM   983  O  OE1 . GLU   A 1 131 ? -29.206 8.458  0.703   1.00 103.59 ? 129 GLU   A OE1 1 
ATOM   984  O  OE2 . GLU   A 1 131 ? -30.008 7.842  2.687   1.00 120.17 ? 129 GLU   A OE2 1 
ATOM   985  N  N   . PRO   A 1 132 ? -32.033 7.558  -3.401  1.00 93.16  ? 130 PRO   A N   1 
ATOM   986  C  CA  . PRO   A 1 132 ? -33.150 8.338  -3.915  1.00 88.48  ? 130 PRO   A CA  1 
ATOM   987  C  C   . PRO   A 1 132 ? -34.372 8.225  -3.038  1.00 92.87  ? 130 PRO   A C   1 
ATOM   988  O  O   . PRO   A 1 132 ? -35.272 9.048  -3.194  1.00 90.97  ? 130 PRO   A O   1 
ATOM   989  C  CB  . PRO   A 1 132 ? -33.375 7.753  -5.306  1.00 83.48  ? 130 PRO   A CB  1 
ATOM   990  C  CG  . PRO   A 1 132 ? -32.680 6.394  -5.310  1.00 87.94  ? 130 PRO   A CG  1 
ATOM   991  C  CD  . PRO   A 1 132 ? -31.937 6.224  -4.024  1.00 93.71  ? 130 PRO   A CD  1 
ATOM   992  N  N   . ASP   A 1 133 ? -34.380 7.283  -2.077  1.00 102.91 ? 131 ASP   A N   1 
ATOM   993  C  CA  . ASP   A 1 133 ? -35.574 6.980  -1.290  1.00 98.03  ? 131 ASP   A CA  1 
ATOM   994  C  C   . ASP   A 1 133 ? -36.037 8.190  -0.499  1.00 100.37 ? 131 ASP   A C   1 
ATOM   995  O  O   . ASP   A 1 133 ? -37.240 8.418  -0.332  1.00 104.63 ? 131 ASP   A O   1 
ATOM   996  C  CB  . ASP   A 1 133 ? -35.276 5.824  -0.338  1.00 101.80 ? 131 ASP   A CB  1 
ATOM   997  C  CG  . ASP   A 1 133 ? -34.754 4.601  -1.061  1.00 108.84 ? 131 ASP   A CG  1 
ATOM   998  O  OD1 . ASP   A 1 133 ? -34.994 4.481  -2.286  1.00 110.13 ? 131 ASP   A OD1 1 
ATOM   999  O  OD2 . ASP   A 1 133 ? -34.095 3.766  -0.395  1.00 113.61 ? 131 ASP   A OD2 1 
ATOM   1000 N  N   . ASP   A 1 134 ? -35.102 8.966  0.010   1.00 97.43  ? 132 ASP   A N   1 
ATOM   1001 C  CA  . ASP   A 1 134 ? -35.454 10.080 0.872   1.00 89.39  ? 132 ASP   A CA  1 
ATOM   1002 C  C   . ASP   A 1 134 ? -34.900 11.392 0.333   1.00 82.87  ? 132 ASP   A C   1 
ATOM   1003 O  O   . ASP   A 1 134 ? -34.631 12.321 1.099   1.00 87.01  ? 132 ASP   A O   1 
ATOM   1004 C  CB  . ASP   A 1 134 ? -35.013 9.794  2.310   1.00 95.85  ? 132 ASP   A CB  1 
ATOM   1005 C  CG  . ASP   A 1 134 ? -33.591 9.270  2.394   1.00 98.28  ? 132 ASP   A CG  1 
ATOM   1006 O  OD1 . ASP   A 1 134 ? -32.942 9.150  1.333   1.00 101.57 ? 132 ASP   A OD1 1 
ATOM   1007 O  OD2 . ASP   A 1 134 ? -33.141 8.933  3.513   1.00 92.51  ? 132 ASP   A OD2 1 
ATOM   1008 N  N   . TRP   A 1 135 ? -34.760 11.488 -0.992  1.00 78.33  ? 133 TRP   A N   1 
ATOM   1009 C  CA  . TRP   A 1 135 ? -34.487 12.749 -1.670  1.00 68.93  ? 133 TRP   A CA  1 
ATOM   1010 C  C   . TRP   A 1 135 ? -35.414 12.869 -2.867  1.00 63.65  ? 133 TRP   A C   1 
ATOM   1011 O  O   . TRP   A 1 135 ? -35.497 11.949 -3.686  1.00 68.20  ? 133 TRP   A O   1 
ATOM   1012 C  CB  . TRP   A 1 135 ? -33.014 12.868 -2.109  1.00 61.83  ? 133 TRP   A CB  1 
ATOM   1013 C  CG  . TRP   A 1 135 ? -32.082 13.113 -0.956  1.00 60.15  ? 133 TRP   A CG  1 
ATOM   1014 C  CD1 . TRP   A 1 135 ? -31.429 12.167 -0.207  1.00 64.48  ? 133 TRP   A CD1 1 
ATOM   1015 C  CD2 . TRP   A 1 135 ? -31.716 14.387 -0.403  1.00 57.47  ? 133 TRP   A CD2 1 
ATOM   1016 N  NE1 . TRP   A 1 135 ? -30.683 12.774 0.777   1.00 55.27  ? 133 TRP   A NE1 1 
ATOM   1017 C  CE2 . TRP   A 1 135 ? -30.836 14.136 0.678   1.00 54.18  ? 133 TRP   A CE2 1 
ATOM   1018 C  CE3 . TRP   A 1 135 ? -32.046 15.715 -0.713  1.00 51.82  ? 133 TRP   A CE3 1 
ATOM   1019 C  CZ2 . TRP   A 1 135 ? -30.276 15.170 1.447   1.00 43.37  ? 133 TRP   A CZ2 1 
ATOM   1020 C  CZ3 . TRP   A 1 135 ? -31.489 16.741 0.054   1.00 48.60  ? 133 TRP   A CZ3 1 
ATOM   1021 C  CH2 . TRP   A 1 135 ? -30.616 16.459 1.121   1.00 45.94  ? 133 TRP   A CH2 1 
ATOM   1022 N  N   . GLU   A 1 136 ? -36.110 13.999 -2.956  1.00 55.25  ? 134 GLU   A N   1 
ATOM   1023 C  CA  . GLU   A 1 136 ? -36.981 14.311 -4.073  1.00 50.10  ? 134 GLU   A CA  1 
ATOM   1024 C  C   . GLU   A 1 136 ? -36.324 15.373 -4.934  1.00 51.86  ? 134 GLU   A C   1 
ATOM   1025 O  O   . GLU   A 1 136 ? -35.779 16.354 -4.415  1.00 53.99  ? 134 GLU   A O   1 
ATOM   1026 C  CB  . GLU   A 1 136 ? -38.349 14.807 -3.592  1.00 56.98  ? 134 GLU   A CB  1 
ATOM   1027 C  CG  . GLU   A 1 136 ? -39.403 14.910 -4.703  1.00 59.14  ? 134 GLU   A CG  1 
ATOM   1028 C  CD  . GLU   A 1 136 ? -40.681 15.668 -4.302  1.00 60.69  ? 134 GLU   A CD  1 
ATOM   1029 O  OE1 . GLU   A 1 136 ? -40.901 15.956 -3.092  1.00 53.74  ? 134 GLU   A OE1 1 
ATOM   1030 O  OE2 . GLU   A 1 136 ? -41.474 15.968 -5.226  1.00 65.07  ? 134 GLU   A OE2 1 
ATOM   1031 N  N   . SER   A 1 137 ? -36.375 15.180 -6.248  1.00 50.26  ? 135 SER   A N   1 
ATOM   1032 C  CA  . SER   A 1 137 ? -35.846 16.172 -7.172  1.00 46.94  ? 135 SER   A CA  1 
ATOM   1033 C  C   . SER   A 1 137 ? -36.943 17.161 -7.537  1.00 49.39  ? 135 SER   A C   1 
ATOM   1034 O  O   . SER   A 1 137 ? -38.024 16.762 -7.990  1.00 57.56  ? 135 SER   A O   1 
ATOM   1035 C  CB  . SER   A 1 137 ? -35.295 15.507 -8.427  1.00 41.47  ? 135 SER   A CB  1 
ATOM   1036 O  OG  . SER   A 1 137 ? -34.903 16.495 -9.372  1.00 44.38  ? 135 SER   A OG  1 
ATOM   1037 N  N   . VAL   A 1 138 ? -36.668 18.447 -7.342  1.00 49.33  ? 136 VAL   A N   1 
ATOM   1038 C  CA  . VAL   A 1 138 ? -37.666 19.477 -7.600  1.00 49.80  ? 136 VAL   A CA  1 
ATOM   1039 C  C   . VAL   A 1 138 ? -37.315 20.381 -8.776  1.00 48.62  ? 136 VAL   A C   1 
ATOM   1040 O  O   . VAL   A 1 138 ? -38.230 20.994 -9.349  1.00 51.39  ? 136 VAL   A O   1 
ATOM   1041 C  CB  . VAL   A 1 138 ? -37.940 20.328 -6.344  1.00 40.64  ? 136 VAL   A CB  1 
ATOM   1042 C  CG1 . VAL   A 1 138 ? -38.230 19.427 -5.178  1.00 47.12  ? 136 VAL   A CG1 1 
ATOM   1043 C  CG2 . VAL   A 1 138 ? -36.751 21.233 -6.049  1.00 40.35  ? 136 VAL   A CG2 1 
ATOM   1044 N  N   . PHE   A 1 139 ? -36.038 20.479 -9.168  1.00 46.16  ? 137 PHE   A N   1 
ATOM   1045 C  CA  . PHE   A 1 139 ? -35.639 21.399 -10.233 1.00 45.42  ? 137 PHE   A CA  1 
ATOM   1046 C  C   . PHE   A 1 139 ? -34.539 20.799 -11.101 1.00 42.56  ? 137 PHE   A C   1 
ATOM   1047 O  O   . PHE   A 1 139 ? -33.694 20.034 -10.628 1.00 43.25  ? 137 PHE   A O   1 
ATOM   1048 C  CB  . PHE   A 1 139 ? -35.152 22.733 -9.667  1.00 44.14  ? 137 PHE   A CB  1 
ATOM   1049 C  CG  . PHE   A 1 139 ? -34.773 23.722 -10.720 1.00 42.19  ? 137 PHE   A CG  1 
ATOM   1050 C  CD1 . PHE   A 1 139 ? -35.749 24.391 -11.446 1.00 44.14  ? 137 PHE   A CD1 1 
ATOM   1051 C  CD2 . PHE   A 1 139 ? -33.436 23.945 -11.027 1.00 40.49  ? 137 PHE   A CD2 1 
ATOM   1052 C  CE1 . PHE   A 1 139 ? -35.394 25.308 -12.429 1.00 41.97  ? 137 PHE   A CE1 1 
ATOM   1053 C  CE2 . PHE   A 1 139 ? -33.073 24.846 -12.016 1.00 41.85  ? 137 PHE   A CE2 1 
ATOM   1054 C  CZ  . PHE   A 1 139 ? -34.053 25.531 -12.721 1.00 42.49  ? 137 PHE   A CZ  1 
ATOM   1055 N  N   . SER   A 1 140 ? -34.509 21.213 -12.362 1.00 41.37  ? 138 SER   A N   1 
ATOM   1056 C  CA  . SER   A 1 140 ? -33.735 20.482 -13.353 1.00 36.38  ? 138 SER   A CA  1 
ATOM   1057 C  C   . SER   A 1 140 ? -33.544 21.359 -14.582 1.00 41.06  ? 138 SER   A C   1 
ATOM   1058 O  O   . SER   A 1 140 ? -34.533 21.802 -15.166 1.00 50.37  ? 138 SER   A O   1 
ATOM   1059 C  CB  . SER   A 1 140 ? -34.495 19.213 -13.683 1.00 35.73  ? 138 SER   A CB  1 
ATOM   1060 O  OG  . SER   A 1 140 ? -33.816 18.471 -14.650 1.00 43.55  ? 138 SER   A OG  1 
ATOM   1061 N  N   . GLU   A 1 141 ? -32.297 21.613 -14.992 1.00 39.64  ? 139 GLU   A N   1 
ATOM   1062 C  CA  . GLU   A 1 141 ? -32.056 22.540 -16.107 1.00 39.05  ? 139 GLU   A CA  1 
ATOM   1063 C  C   . GLU   A 1 141 ? -30.823 22.142 -16.906 1.00 42.17  ? 139 GLU   A C   1 
ATOM   1064 O  O   . GLU   A 1 141 ? -29.697 22.388 -16.459 1.00 41.56  ? 139 GLU   A O   1 
ATOM   1065 C  CB  . GLU   A 1 141 ? -31.900 23.965 -15.610 1.00 39.60  ? 139 GLU   A CB  1 
ATOM   1066 C  CG  . GLU   A 1 141 ? -32.353 24.975 -16.615 1.00 41.98  ? 139 GLU   A CG  1 
ATOM   1067 C  CD  . GLU   A 1 141 ? -32.033 26.391 -16.202 1.00 43.24  ? 139 GLU   A CD  1 
ATOM   1068 O  OE1 . GLU   A 1 141 ? -32.994 27.133 -15.893 1.00 49.33  ? 139 GLU   A OE1 1 
ATOM   1069 O  OE2 . GLU   A 1 141 ? -30.831 26.758 -16.202 1.00 37.57  ? 139 GLU   A OE2 1 
ATOM   1070 N  N   . PHE   A 1 142 ? -31.031 21.591 -18.107 1.00 44.53  ? 140 PHE   A N   1 
ATOM   1071 C  CA  . PHE   A 1 142 ? -29.936 21.160 -18.970 1.00 43.54  ? 140 PHE   A CA  1 
ATOM   1072 C  C   . PHE   A 1 142 ? -29.464 22.326 -19.829 1.00 42.68  ? 140 PHE   A C   1 
ATOM   1073 O  O   . PHE   A 1 142 ? -30.255 23.206 -20.187 1.00 40.87  ? 140 PHE   A O   1 
ATOM   1074 C  CB  . PHE   A 1 142 ? -30.376 19.996 -19.866 1.00 38.77  ? 140 PHE   A CB  1 
ATOM   1075 C  CG  . PHE   A 1 142 ? -29.284 19.439 -20.766 1.00 40.73  ? 140 PHE   A CG  1 
ATOM   1076 C  CD1 . PHE   A 1 142 ? -28.420 18.447 -20.310 1.00 44.26  ? 140 PHE   A CD1 1 
ATOM   1077 C  CD2 . PHE   A 1 142 ? -29.125 19.902 -22.063 1.00 40.96  ? 140 PHE   A CD2 1 
ATOM   1078 C  CE1 . PHE   A 1 142 ? -27.418 17.928 -21.128 1.00 42.06  ? 140 PHE   A CE1 1 
ATOM   1079 C  CE2 . PHE   A 1 142 ? -28.120 19.388 -22.890 1.00 40.79  ? 140 PHE   A CE2 1 
ATOM   1080 C  CZ  . PHE   A 1 142 ? -27.270 18.397 -22.421 1.00 42.18  ? 140 PHE   A CZ  1 
ATOM   1081 N  N   . HIS   A 1 143 ? -28.166 22.311 -20.169 1.00 42.70  ? 141 HIS   A N   1 
ATOM   1082 C  CA  . HIS   A 1 143 ? -27.537 23.323 -21.018 1.00 42.98  ? 141 HIS   A CA  1 
ATOM   1083 C  C   . HIS   A 1 143 ? -26.561 22.668 -21.980 1.00 42.27  ? 141 HIS   A C   1 
ATOM   1084 O  O   . HIS   A 1 143 ? -25.725 21.861 -21.558 1.00 43.65  ? 141 HIS   A O   1 
ATOM   1085 C  CB  . HIS   A 1 143 ? -26.800 24.365 -20.169 1.00 40.46  ? 141 HIS   A CB  1 
ATOM   1086 C  CG  . HIS   A 1 143 ? -27.721 25.284 -19.429 1.00 41.52  ? 141 HIS   A CG  1 
ATOM   1087 N  ND1 . HIS   A 1 143 ? -28.253 26.423 -19.999 1.00 40.15  ? 141 HIS   A ND1 1 
ATOM   1088 C  CD2 . HIS   A 1 143 ? -28.274 25.188 -18.196 1.00 41.27  ? 141 HIS   A CD2 1 
ATOM   1089 C  CE1 . HIS   A 1 143 ? -29.060 27.012 -19.132 1.00 41.93  ? 141 HIS   A CE1 1 
ATOM   1090 N  NE2 . HIS   A 1 143 ? -29.085 26.287 -18.027 1.00 41.12  ? 141 HIS   A NE2 1 
ATOM   1091 N  N   . ASP   A 1 144 ? -26.649 23.010 -23.265 1.00 41.63  ? 142 ASP   A N   1 
ATOM   1092 C  CA  . ASP   A 1 144 ? -25.605 22.536 -24.158 1.00 44.03  ? 142 ASP   A CA  1 
ATOM   1093 C  C   . ASP   A 1 144 ? -24.282 23.256 -23.880 1.00 42.73  ? 142 ASP   A C   1 
ATOM   1094 O  O   . ASP   A 1 144 ? -24.229 24.302 -23.224 1.00 44.87  ? 142 ASP   A O   1 
ATOM   1095 C  CB  . ASP   A 1 144 ? -25.983 22.747 -25.619 1.00 41.28  ? 142 ASP   A CB  1 
ATOM   1096 C  CG  . ASP   A 1 144 ? -27.160 21.913 -26.032 1.00 42.09  ? 142 ASP   A CG  1 
ATOM   1097 O  OD1 . ASP   A 1 144 ? -27.127 20.699 -25.753 1.00 49.17  ? 142 ASP   A OD1 1 
ATOM   1098 O  OD2 . ASP   A 1 144 ? -28.076 22.443 -26.704 1.00 39.97  ? 142 ASP   A OD2 1 
ATOM   1099 N  N   . ALA   A 1 145 ? -23.201 22.689 -24.397 1.00 43.65  ? 143 ALA   A N   1 
ATOM   1100 C  CA  . ALA   A 1 145 ? -21.946 23.424 -24.424 1.00 45.35  ? 143 ALA   A CA  1 
ATOM   1101 C  C   . ALA   A 1 145 ? -22.029 24.547 -25.445 1.00 48.46  ? 143 ALA   A C   1 
ATOM   1102 O  O   . ALA   A 1 145 ? -22.611 24.397 -26.521 1.00 52.03  ? 143 ALA   A O   1 
ATOM   1103 C  CB  . ALA   A 1 145 ? -20.783 22.496 -24.766 1.00 47.23  ? 143 ALA   A CB  1 
ATOM   1104 N  N   . ASP   A 1 146 ? -21.444 25.698 -25.092 1.00 49.87  ? 144 ASP   A N   1 
ATOM   1105 C  CA  . ASP   A 1 146 ? -21.388 26.849 -25.983 1.00 53.41  ? 144 ASP   A CA  1 
ATOM   1106 C  C   . ASP   A 1 146 ? -19.938 27.327 -26.044 1.00 58.93  ? 144 ASP   A C   1 
ATOM   1107 O  O   . ASP   A 1 146 ? -18.999 26.619 -25.659 1.00 60.13  ? 144 ASP   A O   1 
ATOM   1108 C  CB  . ASP   A 1 146 ? -22.347 27.975 -25.552 1.00 50.96  ? 144 ASP   A CB  1 
ATOM   1109 C  CG  . ASP   A 1 146 ? -22.213 28.350 -24.079 1.00 58.33  ? 144 ASP   A CG  1 
ATOM   1110 O  OD1 . ASP   A 1 146 ? -21.093 28.707 -23.640 1.00 62.64  ? 144 ASP   A OD1 1 
ATOM   1111 O  OD2 . ASP   A 1 146 ? -23.248 28.323 -23.363 1.00 59.30  ? 144 ASP   A OD2 1 
ATOM   1112 N  N   . ALA   A 1 147 ? -19.742 28.554 -26.532 1.00 63.75  ? 145 ALA   A N   1 
ATOM   1113 C  CA  . ALA   A 1 147 ? -18.392 29.084 -26.690 1.00 62.33  ? 145 ALA   A CA  1 
ATOM   1114 C  C   . ALA   A 1 147 ? -17.683 29.229 -25.348 1.00 64.67  ? 145 ALA   A C   1 
ATOM   1115 O  O   . ALA   A 1 147 ? -16.486 28.937 -25.238 1.00 71.58  ? 145 ALA   A O   1 
ATOM   1116 C  CB  . ALA   A 1 147 ? -18.442 30.424 -27.423 1.00 62.45  ? 145 ALA   A CB  1 
ATOM   1117 N  N   . GLN   A 1 148 ? -18.404 29.665 -24.310 1.00 68.33  ? 146 GLN   A N   1 
ATOM   1118 C  CA  . GLN   A 1 148 ? -17.776 29.909 -23.011 1.00 68.36  ? 146 GLN   A CA  1 
ATOM   1119 C  C   . GLN   A 1 148 ? -17.682 28.643 -22.158 1.00 69.68  ? 146 GLN   A C   1 
ATOM   1120 O  O   . GLN   A 1 148 ? -16.817 28.563 -21.270 1.00 72.30  ? 146 GLN   A O   1 
ATOM   1121 C  CB  . GLN   A 1 148 ? -18.551 30.981 -22.234 1.00 72.47  ? 146 GLN   A CB  1 
ATOM   1122 C  CG  . GLN   A 1 148 ? -18.675 32.320 -22.939 1.00 70.54  ? 146 GLN   A CG  1 
ATOM   1123 C  CD  . GLN   A 1 148 ? -19.828 32.333 -23.931 1.00 73.86  ? 146 GLN   A CD  1 
ATOM   1124 O  OE1 . GLN   A 1 148 ? -19.630 32.476 -25.141 1.00 84.11  ? 146 GLN   A OE1 1 
ATOM   1125 N  NE2 . GLN   A 1 148 ? -21.045 32.170 -23.418 1.00 80.49  ? 146 GLN   A NE2 1 
ATOM   1126 N  N   . ASN   A 1 149 ? -18.550 27.656 -22.405 1.00 62.74  ? 147 ASN   A N   1 
ATOM   1127 C  CA  . ASN   A 1 149 ? -18.675 26.472 -21.560 1.00 60.34  ? 147 ASN   A CA  1 
ATOM   1128 C  C   . ASN   A 1 149 ? -18.398 25.226 -22.389 1.00 56.76  ? 147 ASN   A C   1 
ATOM   1129 O  O   . ASN   A 1 149 ? -19.139 24.921 -23.331 1.00 54.76  ? 147 ASN   A O   1 
ATOM   1130 C  CB  . ASN   A 1 149 ? -20.063 26.416 -20.937 1.00 58.48  ? 147 ASN   A CB  1 
ATOM   1131 C  CG  . ASN   A 1 149 ? -20.407 27.690 -20.213 1.00 54.02  ? 147 ASN   A CG  1 
ATOM   1132 O  OD1 . ASN   A 1 149 ? -20.203 27.807 -19.001 1.00 52.77  ? 147 ASN   A OD1 1 
ATOM   1133 N  ND2 . ASN   A 1 149 ? -20.901 28.673 -20.961 1.00 55.29  ? 147 ASN   A ND2 1 
ATOM   1134 N  N   . SER   A 1 150 ? -17.343 24.502 -22.025 1.00 59.79  ? 148 SER   A N   1 
ATOM   1135 C  CA  . SER   A 1 150 ? -16.783 23.470 -22.894 1.00 61.20  ? 148 SER   A CA  1 
ATOM   1136 C  C   . SER   A 1 150 ? -17.511 22.132 -22.823 1.00 59.17  ? 148 SER   A C   1 
ATOM   1137 O  O   . SER   A 1 150 ? -17.207 21.243 -23.626 1.00 54.56  ? 148 SER   A O   1 
ATOM   1138 C  CB  . SER   A 1 150 ? -15.290 23.293 -22.562 1.00 65.70  ? 148 SER   A CB  1 
ATOM   1139 O  OG  . SER   A 1 150 ? -15.091 22.427 -21.447 1.00 68.61  ? 148 SER   A OG  1 
ATOM   1140 N  N   . HIS   A 1 151 ? -18.452 21.958 -21.897 1.00 56.68  ? 149 HIS   A N   1 
ATOM   1141 C  CA  . HIS   A 1 151 ? -19.161 20.696 -21.765 1.00 53.66  ? 149 HIS   A CA  1 
ATOM   1142 C  C   . HIS   A 1 151 ? -20.618 21.004 -21.469 1.00 47.98  ? 149 HIS   A C   1 
ATOM   1143 O  O   . HIS   A 1 151 ? -20.930 22.037 -20.868 1.00 46.85  ? 149 HIS   A O   1 
ATOM   1144 C  CB  . HIS   A 1 151 ? -18.552 19.819 -20.653 1.00 53.22  ? 149 HIS   A CB  1 
ATOM   1145 C  CG  . HIS   A 1 151 ? -17.262 19.152 -21.042 1.00 65.50  ? 149 HIS   A CG  1 
ATOM   1146 N  ND1 . HIS   A 1 151 ? -17.210 17.899 -21.620 1.00 78.42  ? 149 HIS   A ND1 1 
ATOM   1147 C  CD2 . HIS   A 1 151 ? -15.974 19.559 -20.922 1.00 67.64  ? 149 HIS   A CD2 1 
ATOM   1148 C  CE1 . HIS   A 1 151 ? -15.949 17.572 -21.858 1.00 77.68  ? 149 HIS   A CE1 1 
ATOM   1149 N  NE2 . HIS   A 1 151 ? -15.179 18.561 -21.440 1.00 72.50  ? 149 HIS   A NE2 1 
ATOM   1150 N  N   . SER   A 1 152 ? -21.515 20.128 -21.917 1.00 47.98  ? 150 SER   A N   1 
ATOM   1151 C  CA  . SER   A 1 152 ? -22.906 20.287 -21.513 1.00 49.02  ? 150 SER   A CA  1 
ATOM   1152 C  C   . SER   A 1 152 ? -23.015 19.990 -20.024 1.00 46.75  ? 150 SER   A C   1 
ATOM   1153 O  O   . SER   A 1 152 ? -22.175 19.291 -19.448 1.00 50.44  ? 150 SER   A O   1 
ATOM   1154 C  CB  . SER   A 1 152 ? -23.846 19.373 -22.311 1.00 48.91  ? 150 SER   A CB  1 
ATOM   1155 O  OG  . SER   A 1 152 ? -23.411 18.018 -22.293 1.00 58.99  ? 150 SER   A OG  1 
ATOM   1156 N  N   . TYR   A 1 153 ? -24.047 20.546 -19.397 1.00 40.89  ? 151 TYR   A N   1 
ATOM   1157 C  CA  . TYR   A 1 153 ? -24.184 20.465 -17.951 1.00 43.34  ? 151 TYR   A CA  1 
ATOM   1158 C  C   . TYR   A 1 153 ? -25.645 20.665 -17.583 1.00 43.57  ? 151 TYR   A C   1 
ATOM   1159 O  O   . TYR   A 1 153 ? -26.429 21.227 -18.354 1.00 44.24  ? 151 TYR   A O   1 
ATOM   1160 C  CB  . TYR   A 1 153 ? -23.317 21.517 -17.244 1.00 45.87  ? 151 TYR   A CB  1 
ATOM   1161 C  CG  . TYR   A 1 153 ? -23.570 22.901 -17.792 1.00 43.09  ? 151 TYR   A CG  1 
ATOM   1162 C  CD1 . TYR   A 1 153 ? -22.979 23.319 -18.979 1.00 46.62  ? 151 TYR   A CD1 1 
ATOM   1163 C  CD2 . TYR   A 1 153 ? -24.423 23.779 -17.138 1.00 40.25  ? 151 TYR   A CD2 1 
ATOM   1164 C  CE1 . TYR   A 1 153 ? -23.232 24.576 -19.493 1.00 47.49  ? 151 TYR   A CE1 1 
ATOM   1165 C  CE2 . TYR   A 1 153 ? -24.676 25.032 -17.637 1.00 42.98  ? 151 TYR   A CE2 1 
ATOM   1166 C  CZ  . TYR   A 1 153 ? -24.082 25.428 -18.814 1.00 44.82  ? 151 TYR   A CZ  1 
ATOM   1167 O  OH  . TYR   A 1 153 ? -24.352 26.676 -19.317 1.00 47.49  ? 151 TYR   A OH  1 
ATOM   1168 N  N   . CYS   A 1 154 ? -25.999 20.235 -16.375 1.00 40.89  ? 152 CYS   A N   1 
ATOM   1169 C  CA  . CYS   A 1 154 ? -27.389 20.258 -15.946 1.00 36.38  ? 152 CYS   A CA  1 
ATOM   1170 C  C   . CYS   A 1 154 ? -27.476 20.595 -14.469 1.00 39.83  ? 152 CYS   A C   1 
ATOM   1171 O  O   . CYS   A 1 154 ? -26.965 19.840 -13.638 1.00 41.63  ? 152 CYS   A O   1 
ATOM   1172 C  CB  . CYS   A 1 154 ? -28.051 18.914 -16.210 1.00 37.99  ? 152 CYS   A CB  1 
ATOM   1173 S  SG  . CYS   A 1 154 ? -29.834 19.042 -16.074 1.00 42.75  ? 152 CYS   A SG  1 
ATOM   1174 N  N   . PHE   A 1 155 ? -28.144 21.702 -14.137 1.00 36.28  ? 153 PHE   A N   1 
ATOM   1175 C  CA  . PHE   A 1 155 ? -28.365 22.053 -12.744 1.00 34.36  ? 153 PHE   A CA  1 
ATOM   1176 C  C   . PHE   A 1 155 ? -29.519 21.247 -12.177 1.00 36.94  ? 153 PHE   A C   1 
ATOM   1177 O  O   . PHE   A 1 155 ? -30.529 21.029 -12.848 1.00 41.60  ? 153 PHE   A O   1 
ATOM   1178 C  CB  . PHE   A 1 155 ? -28.656 23.544 -12.600 1.00 31.74  ? 153 PHE   A CB  1 
ATOM   1179 C  CG  . PHE   A 1 155 ? -27.573 24.404 -13.160 1.00 37.73  ? 153 PHE   A CG  1 
ATOM   1180 C  CD1 . PHE   A 1 155 ? -26.258 24.229 -12.746 1.00 42.03  ? 153 PHE   A CD1 1 
ATOM   1181 C  CD2 . PHE   A 1 155 ? -27.849 25.369 -14.112 1.00 39.57  ? 153 PHE   A CD2 1 
ATOM   1182 C  CE1 . PHE   A 1 155 ? -25.234 25.000 -13.269 1.00 41.83  ? 153 PHE   A CE1 1 
ATOM   1183 C  CE2 . PHE   A 1 155 ? -26.834 26.146 -14.644 1.00 39.77  ? 153 PHE   A CE2 1 
ATOM   1184 C  CZ  . PHE   A 1 155 ? -25.524 25.965 -14.219 1.00 42.11  ? 153 PHE   A CZ  1 
ATOM   1185 N  N   . GLU   A 1 156 ? -29.376 20.818 -10.931 1.00 35.07  ? 154 GLU   A N   1 
ATOM   1186 C  CA  . GLU   A 1 156 ? -30.447 20.099 -10.261 1.00 38.15  ? 154 GLU   A CA  1 
ATOM   1187 C  C   . GLU   A 1 156 ? -30.534 20.535 -8.804  1.00 39.14  ? 154 GLU   A C   1 
ATOM   1188 O  O   . GLU   A 1 156 ? -29.504 20.765 -8.161  1.00 39.87  ? 154 GLU   A O   1 
ATOM   1189 C  CB  . GLU   A 1 156 ? -30.230 18.584 -10.356 1.00 33.64  ? 154 GLU   A CB  1 
ATOM   1190 C  CG  . GLU   A 1 156 ? -31.441 17.807 -9.894  1.00 38.36  ? 154 GLU   A CG  1 
ATOM   1191 C  CD  . GLU   A 1 156 ? -31.184 16.320 -9.709  1.00 41.36  ? 154 GLU   A CD  1 
ATOM   1192 O  OE1 . GLU   A 1 156 ? -30.006 15.884 -9.827  1.00 40.86  ? 154 GLU   A OE1 1 
ATOM   1193 O  OE2 . GLU   A 1 156 ? -32.176 15.597 -9.428  1.00 37.50  ? 154 GLU   A OE2 1 
ATOM   1194 N  N   . ILE   A 1 157 ? -31.759 20.653 -8.283  1.00 38.20  ? 155 ILE   A N   1 
ATOM   1195 C  CA  . ILE   A 1 157 ? -31.991 20.927 -6.867  1.00 38.06  ? 155 ILE   A CA  1 
ATOM   1196 C  C   . ILE   A 1 157 ? -32.857 19.812 -6.298  1.00 39.48  ? 155 ILE   A C   1 
ATOM   1197 O  O   . ILE   A 1 157 ? -33.903 19.476 -6.863  1.00 39.64  ? 155 ILE   A O   1 
ATOM   1198 C  CB  . ILE   A 1 157 ? -32.650 22.301 -6.633  1.00 38.84  ? 155 ILE   A CB  1 
ATOM   1199 C  CG1 . ILE   A 1 157 ? -31.899 23.405 -7.379  1.00 35.67  ? 155 ILE   A CG1 1 
ATOM   1200 C  CG2 . ILE   A 1 157 ? -32.681 22.618 -5.158  1.00 37.24  ? 155 ILE   A CG2 1 
ATOM   1201 C  CD1 . ILE   A 1 157 ? -32.534 24.763 -7.261  1.00 31.08  ? 155 ILE   A CD1 1 
ATOM   1202 N  N   . LEU   A 1 158 ? -32.420 19.232 -5.189  1.00 44.13  ? 156 LEU   A N   1 
ATOM   1203 C  CA  . LEU   A 1 158 ? -33.183 18.180 -4.543  1.00 42.74  ? 156 LEU   A CA  1 
ATOM   1204 C  C   . LEU   A 1 158 ? -33.562 18.654 -3.154  1.00 42.19  ? 156 LEU   A C   1 
ATOM   1205 O  O   . LEU   A 1 158 ? -32.836 19.425 -2.527  1.00 45.10  ? 156 LEU   A O   1 
ATOM   1206 C  CB  . LEU   A 1 158 ? -32.406 16.868 -4.419  1.00 42.19  ? 156 LEU   A CB  1 
ATOM   1207 C  CG  . LEU   A 1 158 ? -32.110 16.080 -5.693  1.00 42.41  ? 156 LEU   A CG  1 
ATOM   1208 C  CD1 . LEU   A 1 158 ? -30.894 16.687 -6.373  1.00 38.58  ? 156 LEU   A CD1 1 
ATOM   1209 C  CD2 . LEU   A 1 158 ? -31.943 14.589 -5.466  1.00 45.70  ? 156 LEU   A CD2 1 
ATOM   1210 N  N   . GLU   A 1 159 ? -34.705 18.190 -2.685  1.00 46.00  ? 157 GLU   A N   1 
ATOM   1211 C  CA  . GLU   A 1 159 ? -35.191 18.465 -1.345  1.00 48.36  ? 157 GLU   A CA  1 
ATOM   1212 C  C   . GLU   A 1 159 ? -35.257 17.127 -0.622  1.00 52.28  ? 157 GLU   A C   1 
ATOM   1213 O  O   . GLU   A 1 159 ? -35.607 16.110 -1.232  1.00 54.51  ? 157 GLU   A O   1 
ATOM   1214 C  CB  . GLU   A 1 159 ? -36.597 19.091 -1.390  1.00 53.15  ? 157 GLU   A CB  1 
ATOM   1215 C  CG  . GLU   A 1 159 ? -36.801 20.456 -2.085  1.00 49.45  ? 157 GLU   A CG  1 
ATOM   1216 C  CD  . GLU   A 1 159 ? -36.348 21.623 -1.258  1.00 43.72  ? 157 GLU   A CD  1 
ATOM   1217 O  OE1 . GLU   A 1 159 ? -36.352 21.461 -0.030  1.00 56.33  ? 157 GLU   A OE1 1 
ATOM   1218 O  OE2 . GLU   A 1 159 ? -36.081 22.719 -1.811  1.00 41.04  ? 157 GLU   A OE2 1 
ATOM   1219 N  N   . ARG   A 1 160 ? -34.932 17.113 0.666   1.00 52.43  ? 158 ARG   A N   1 
ATOM   1220 C  CA  . ARG   A 1 160 ? -35.081 15.887 1.435   1.00 54.24  ? 158 ARG   A CA  1 
ATOM   1221 C  C   . ARG   A 1 160 ? -36.554 15.556 1.633   1.00 59.94  ? 158 ARG   A C   1 
ATOM   1222 O  O   . ARG   A 1 160 ? -37.322 16.371 2.155   1.00 60.95  ? 158 ARG   A O   1 
ATOM   1223 C  CB  . ARG   A 1 160 ? -34.396 16.002 2.794   1.00 56.39  ? 158 ARG   A CB  1 
ATOM   1224 C  CG  . ARG   A 1 160 ? -34.149 14.632 3.428   1.00 55.06  ? 158 ARG   A CG  1 
ATOM   1225 C  CD  . ARG   A 1 160 ? -33.621 14.713 4.854   1.00 57.82  ? 158 ARG   A CD  1 
ATOM   1226 N  NE  . ARG   A 1 160 ? -32.161 14.773 4.915   1.00 52.12  ? 158 ARG   A NE  1 
ATOM   1227 C  CZ  . ARG   A 1 160 ? -31.343 13.724 4.782   1.00 54.04  ? 158 ARG   A CZ  1 
ATOM   1228 N  NH1 . ARG   A 1 160 ? -31.818 12.496 4.545   1.00 56.84  ? 158 ARG   A NH1 1 
ATOM   1229 N  NH2 . ARG   A 1 160 ? -30.026 13.912 4.866   1.00 51.81  ? 158 ARG   A NH2 1 
ATOM   1230 N  N   . ARG   A 1 161 ? -36.950 14.355 1.228   1.00 62.28  ? 159 ARG   A N   1 
ATOM   1231 C  CA  . ARG   A 1 161 ? -38.315 13.924 1.468   1.00 68.36  ? 159 ARG   A CA  1 
ATOM   1232 C  C   . ARG   A 1 161 ? -38.521 13.804 2.962   1.00 71.71  ? 159 ARG   A C   1 
ATOM   1233 O  O   . ARG   A 1 161 ? -37.948 12.910 3.590   1.00 75.58  ? 159 ARG   A O   1 
ATOM   1234 C  CB  . ARG   A 1 161 ? -38.621 12.599 0.760   1.00 75.97  ? 159 ARG   A CB  1 
ATOM   1235 C  CG  . ARG   A 1 161 ? -38.490 12.643 -0.768  1.00 76.09  ? 159 ARG   A CG  1 
ATOM   1236 C  CD  . ARG   A 1 161 ? -39.300 11.518 -1.412  1.00 80.17  ? 159 ARG   A CD  1 
ATOM   1237 N  NE  . ARG   A 1 161 ? -40.656 11.419 -0.847  1.00 95.35  ? 159 ARG   A NE  1 
ATOM   1238 C  CZ  . ARG   A 1 161 ? -41.639 12.311 -1.018  1.00 99.00  ? 159 ARG   A CZ  1 
ATOM   1239 N  NH1 . ARG   A 1 161 ? -42.826 12.108 -0.444  1.00 93.83  ? 159 ARG   A NH1 1 
ATOM   1240 N  NH2 . ARG   A 1 161 ? -41.453 13.395 -1.775  1.00 98.03  ? 159 ARG   A NH2 1 
ATOM   1241 O  OXT . ARG   A 1 161 ? -39.243 14.611 3.563   1.00 73.35  ? 159 ARG   A OXT 1 
HETATM 1242 C  C1  . A1A3E B 2 .   ? -19.156 23.935 -5.987  1.00 52.70  ? 201 A1A3E A C1  1 
HETATM 1243 C  C2  . A1A3E B 2 .   ? -20.502 24.462 -7.756  1.00 44.80  ? 201 A1A3E A C2  1 
HETATM 1244 C  C3  . A1A3E B 2 .   ? -18.130 25.021 -8.000  1.00 51.33  ? 201 A1A3E A C3  1 
HETATM 1245 C  C4  . A1A3E B 2 .   ? -17.143 24.189 -8.840  1.00 58.66  ? 201 A1A3E A C4  1 
HETATM 1246 C  C5  . A1A3E B 2 .   ? -16.782 24.563 -10.279 1.00 51.37  ? 201 A1A3E A C5  1 
HETATM 1247 C  C6  . A1A3E B 2 .   ? -16.863 24.679 -5.877  1.00 61.02  ? 201 A1A3E A C6  1 
HETATM 1248 C  C7  . A1A3E B 2 .   ? -15.957 23.628 -5.891  1.00 67.47  ? 201 A1A3E A C7  1 
HETATM 1249 C  C8  . A1A3E B 2 .   ? -14.747 23.735 -5.232  1.00 75.27  ? 201 A1A3E A C8  1 
HETATM 1250 C  C9  . A1A3E B 2 .   ? -14.459 24.894 -4.549  1.00 83.66  ? 201 A1A3E A C9  1 
HETATM 1251 N  N1  . A1A3E B 2 .   ? -18.915 23.267 -4.874  1.00 58.03  ? 201 A1A3E A N1  1 
HETATM 1252 N  N2  . A1A3E B 2 .   ? -20.394 23.992 -6.488  1.00 52.44  ? 201 A1A3E A N2  1 
HETATM 1253 CL CL1 . A1A3E B 2 .   ? -12.919 24.998 -3.742  1.00 127.54 ? 201 A1A3E A CL1 1 
HETATM 1254 C  C10 . A1A3E B 2 .   ? -15.349 25.954 -4.507  1.00 54.76  ? 201 A1A3E A C10 1 
HETATM 1255 C  C11 . A1A3E B 2 .   ? -16.558 25.841 -5.180  1.00 53.54  ? 201 A1A3E A C11 1 
HETATM 1256 N  N3  . A1A3E B 2 .   ? -21.725 24.465 -8.282  1.00 37.72  ? 201 A1A3E A N3  1 
HETATM 1257 N  N4  . A1A3E B 2 .   ? -19.500 24.936 -8.502  1.00 50.26  ? 201 A1A3E A N4  1 
HETATM 1258 N  N5  . A1A3E B 2 .   ? -18.100 24.545 -6.596  1.00 56.61  ? 201 A1A3E A N5  1 
HETATM 1259 O  O   . HOH   C 3 .   ? -16.272 19.982 -7.806  1.00 54.39  ? 301 HOH   A O   1 
HETATM 1260 O  O   . HOH   C 3 .   ? -18.862 20.408 19.128  1.00 37.14  ? 302 HOH   A O   1 
HETATM 1261 O  O   . HOH   C 3 .   ? -29.258 32.247 4.664   1.00 43.24  ? 303 HOH   A O   1 
HETATM 1262 O  O   . HOH   C 3 .   ? -24.296 23.208 -8.309  1.00 38.60  ? 304 HOH   A O   1 
HETATM 1263 O  O   . HOH   C 3 .   ? -24.212 34.886 -10.534 1.00 46.37  ? 305 HOH   A O   1 
HETATM 1264 O  O   . HOH   C 3 .   ? -30.701 29.582 -3.467  1.00 40.37  ? 306 HOH   A O   1 
HETATM 1265 O  O   . HOH   C 3 .   ? -13.106 26.959 -17.167 1.00 56.10  ? 307 HOH   A O   1 
HETATM 1266 O  O   . HOH   C 3 .   ? -34.990 19.012 -17.278 1.00 35.09  ? 308 HOH   A O   1 
HETATM 1267 O  O   . HOH   C 3 .   ? -27.827 34.549 5.362   1.00 41.36  ? 309 HOH   A O   1 
HETATM 1268 O  O   . HOH   C 3 .   ? -7.863  28.989 14.962  1.00 38.82  ? 310 HOH   A O   1 
HETATM 1269 O  O   . HOH   C 3 .   ? -38.730 22.152 -12.114 1.00 34.42  ? 311 HOH   A O   1 
HETATM 1270 O  O   . HOH   C 3 .   ? -26.371 15.225 -18.005 0.50 53.48  ? 312 HOH   A O   1 
HETATM 1271 O  O   . HOH   C 3 .   ? -12.351 36.723 12.720  1.00 46.16  ? 313 HOH   A O   1 
HETATM 1272 O  O   . HOH   C 3 .   ? -13.947 36.817 10.921  1.00 45.61  ? 314 HOH   A O   1 
HETATM 1273 O  O   . HOH   C 3 .   ? -29.082 36.788 6.312   1.00 41.71  ? 315 HOH   A O   1 
HETATM 1274 O  O   . HOH   C 3 .   ? -30.948 33.148 2.442   1.00 42.62  ? 316 HOH   A 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   . SER A 1   ? 1.1165 1.3636 1.0547 0.1804  0.3643  -0.1954 -1  SER A N   
2    C CA  . SER A 1   ? 1.2809 1.5674 1.1957 0.1579  0.3813  -0.1716 -1  SER A CA  
3    C C   . SER A 1   ? 1.3853 1.6432 1.2341 0.1380  0.3471  -0.1614 -1  SER A C   
4    O O   . SER A 1   ? 1.4646 1.7472 1.2887 0.1194  0.3547  -0.1351 -1  SER A O   
5    C CB  . SER A 1   ? 1.2487 1.6142 1.2570 0.1501  0.3947  -0.1397 -1  SER A CB  
6    O OG  . SER A 1   ? 1.2475 1.6547 1.3328 0.1678  0.4208  -0.1505 -1  SER A OG  
7    N N   . HIS A 2   ? 1.4678 1.6750 1.2918 0.1407  0.3095  -0.1806 0   HIS A N   
8    C CA  . HIS A 2   ? 1.4424 1.6227 1.2125 0.1238  0.2743  -0.1770 0   HIS A CA  
9    C C   . HIS A 2   ? 1.3204 1.5398 1.1232 0.1093  0.2632  -0.1486 0   HIS A C   
10   O O   . HIS A 2   ? 1.4224 1.6370 1.1821 0.0935  0.2545  -0.1278 0   HIS A O   
11   C CB  . HIS A 2   ? 1.5681 1.7242 1.2489 0.1156  0.2810  -0.1793 0   HIS A CB  
12   C CG  . HIS A 2   ? 1.6144 1.7319 1.2553 0.1259  0.2950  -0.2097 0   HIS A CG  
13   N ND1 . HIS A 2   ? 1.7246 1.8503 1.3309 0.1276  0.3354  -0.2151 0   HIS A ND1 
14   C CD2 . HIS A 2   ? 1.6077 1.6784 1.2381 0.1328  0.2759  -0.2374 0   HIS A CD2 
15   C CE1 . HIS A 2   ? 1.8179 1.9021 1.3919 0.1361  0.3395  -0.2482 0   HIS A CE1 
16   N NE2 . HIS A 2   ? 1.7167 1.7643 1.3033 0.1393  0.3038  -0.2606 0   HIS A NE2 
17   N N   . MET A 3   ? 0.9459 1.1853 0.8291 0.1089  0.2574  -0.1396 1   MET A N   
18   C CA  . MET A 3   ? 0.8194 1.0529 0.7363 0.0865  0.2277  -0.1120 1   MET A CA  
19   C C   . MET A 3   ? 0.6706 0.8579 0.5525 0.0815  0.1899  -0.1234 1   MET A C   
20   O O   . MET A 3   ? 0.6259 0.7916 0.5061 0.0921  0.1773  -0.1500 1   MET A O   
21   C CB  . MET A 3   ? 0.7651 1.0213 0.7679 0.0873  0.2231  -0.1044 1   MET A CB  
22   C CG  . MET A 3   ? 0.6413 0.8845 0.6735 0.0641  0.1906  -0.0811 1   MET A CG  
23   S SD  . MET A 3   ? 0.6498 0.9234 0.7777 0.0646  0.1824  -0.0712 1   MET A SD  
24   C CE  . MET A 3   ? 0.5562 0.7963 0.6831 0.0879  0.1676  -0.1049 1   MET A CE  
25   N N   . ILE A 4   ? 0.6264 0.7990 0.4845 0.0654  0.1723  -0.1019 2   ILE A N   
26   C CA  . ILE A 4   ? 0.6245 0.7629 0.4641 0.0620  0.1386  -0.1081 2   ILE A CA  
27   C C   . ILE A 4   ? 0.5714 0.7010 0.4584 0.0504  0.1201  -0.0942 2   ILE A C   
28   O O   . ILE A 4   ? 0.5700 0.7086 0.4804 0.0367  0.1238  -0.0689 2   ILE A O   
29   C CB  . ILE A 4   ? 0.6073 0.7300 0.3898 0.0574  0.1280  -0.0952 2   ILE A CB  
30   C CG1 . ILE A 4   ? 0.6091 0.7339 0.3304 0.0669  0.1392  -0.1112 2   ILE A CG1 
31   C CG2 . ILE A 4   ? 0.5979 0.6945 0.3805 0.0568  0.0953  -0.0983 2   ILE A CG2 
32   C CD1 . ILE A 4   ? 0.7108 0.8567 0.4060 0.0640  0.1719  -0.0949 2   ILE A CD1 
33   N N   . SER A 5   ? 0.5088 0.6194 0.4064 0.0531  0.1000  -0.1103 3   SER A N   
34   C CA  . SER A 5   ? 0.4703 0.5653 0.3969 0.0427  0.0815  -0.1015 3   SER A CA  
35   C C   . SER A 5   ? 0.4893 0.5590 0.3908 0.0442  0.0619  -0.1097 3   SER A C   
36   O O   . SER A 5   ? 0.5095 0.5800 0.3867 0.0527  0.0592  -0.1249 3   SER A O   
37   C CB  . SER A 5   ? 0.4113 0.5108 0.3788 0.0444  0.0787  -0.1104 3   SER A CB  
38   O OG  . SER A 5   ? 0.4418 0.5724 0.4425 0.0494  0.0984  -0.1054 3   SER A OG  
39   N N   . LEU A 6   ? 0.4850 0.5336 0.3942 0.0359  0.0481  -0.1004 4   LEU A N   
40   C CA  . LEU A 6   ? 0.4909 0.5189 0.3846 0.0403  0.0340  -0.1082 4   LEU A CA  
41   C C   . LEU A 6   ? 0.4685 0.4844 0.3794 0.0338  0.0267  -0.1154 4   LEU A C   
42   O O   . LEU A 6   ? 0.4892 0.4976 0.4160 0.0225  0.0230  -0.1052 4   LEU A O   
43   C CB  . LEU A 6   ? 0.4942 0.4974 0.3689 0.0396  0.0263  -0.0922 4   LEU A CB  
44   C CG  . LEU A 6   ? 0.4851 0.4900 0.3313 0.0497  0.0248  -0.0850 4   LEU A CG  
45   C CD1 . LEU A 6   ? 0.4755 0.5047 0.3104 0.0470  0.0398  -0.0787 4   LEU A CD1 
46   C CD2 . LEU A 6   ? 0.5104 0.4791 0.3418 0.0481  0.0150  -0.0658 4   LEU A CD2 
47   N N   . ILE A 7   ? 0.4704 0.4871 0.3784 0.0383  0.0236  -0.1309 5   ILE A N   
48   C CA  . ILE A 7   ? 0.5316 0.5340 0.4444 0.0308  0.0182  -0.1358 5   ILE A CA  
49   C C   . ILE A 7   ? 0.5511 0.5453 0.4490 0.0369  0.0170  -0.1430 5   ILE A C   
50   O O   . ILE A 7   ? 0.5044 0.5187 0.4043 0.0460  0.0189  -0.1507 5   ILE A O   
51   C CB  . ILE A 7   ? 0.4977 0.5098 0.4254 0.0277  0.0197  -0.1451 5   ILE A CB  
52   C CG1 . ILE A 7   ? 0.4692 0.4625 0.3946 0.0169  0.0129  -0.1443 5   ILE A CG1 
53   C CG2 . ILE A 7   ? 0.5133 0.5428 0.4381 0.0338  0.0228  -0.1590 5   ILE A CG2 
54   C CD1 . ILE A 7   ? 0.5000 0.4904 0.4434 0.0118  0.0087  -0.1428 5   ILE A CD1 
55   N N   . ALA A 8   ? 0.5445 0.5103 0.4279 0.0326  0.0134  -0.1411 6   ALA A N   
56   C CA  . ALA A 8   ? 0.5619 0.5169 0.4301 0.0438  0.0169  -0.1492 6   ALA A CA  
57   C C   . ALA A 8   ? 0.5936 0.5196 0.4390 0.0350  0.0173  -0.1542 6   ALA A C   
58   O O   . ALA A 8   ? 0.5775 0.4824 0.4147 0.0193  0.0074  -0.1472 6   ALA A O   
59   C CB  . ALA A 8   ? 0.5224 0.4567 0.3791 0.0558  0.0125  -0.1423 6   ALA A CB  
60   N N   . ALA A 9   ? 0.5974 0.5253 0.4326 0.0456  0.0288  -0.1659 7   ALA A N   
61   C CA  . ALA A 9   ? 0.5798 0.4744 0.3786 0.0414  0.0338  -0.1737 7   ALA A CA  
62   C C   . ALA A 9   ? 0.6724 0.5359 0.4499 0.0618  0.0381  -0.1829 7   ALA A C   
63   O O   . ALA A 9   ? 0.7105 0.5991 0.5094 0.0843  0.0477  -0.1878 7   ALA A O   
64   C CB  . ALA A 9   ? 0.5233 0.4444 0.3232 0.0372  0.0503  -0.1806 7   ALA A CB  
65   N N   . LEU A 10  ? 0.7037 0.5102 0.4400 0.0544  0.0283  -0.1853 8   LEU A N   
66   C CA  . LEU A 10  ? 0.7066 0.4678 0.4179 0.0731  0.0290  -0.1948 8   LEU A CA  
67   C C   . LEU A 10  ? 0.8333 0.5713 0.5129 0.0682  0.0382  -0.2059 8   LEU A C   
68   O O   . LEU A 10  ? 0.8811 0.6061 0.5356 0.0451  0.0293  -0.2033 8   LEU A O   
69   C CB  . LEU A 10  ? 0.7575 0.4718 0.4580 0.0623  0.0055  -0.1827 8   LEU A CB  
70   C CG  . LEU A 10  ? 0.7472 0.4900 0.4861 0.0524  -0.0060 -0.1603 8   LEU A CG  
71   C CD1 . LEU A 10  ? 0.7465 0.4356 0.4698 0.0430  -0.0244 -0.1484 8   LEU A CD1 
72   C CD2 . LEU A 10  ? 0.7365 0.5328 0.5117 0.0724  0.0051  -0.1574 8   LEU A CD2 
73   N N   . ALA A 11  ? 0.9208 0.6521 0.5998 0.0922  0.0541  -0.2183 9   ALA A N   
74   C CA  . ALA A 11  ? 0.8991 0.5955 0.5401 0.0926  0.0609  -0.2326 9   ALA A CA  
75   C C   . ALA A 11  ? 1.0438 0.6681 0.6557 0.0935  0.0400  -0.2328 9   ALA A C   
76   O O   . ALA A 11  ? 1.0775 0.6804 0.6967 0.0885  0.0198  -0.2194 9   ALA A O   
77   C CB  . ALA A 11  ? 0.8784 0.6087 0.5368 0.1186  0.0930  -0.2484 9   ALA A CB  
78   N N   . VAL A 12  ? 1.1483 0.7310 0.7227 0.0983  0.0446  -0.2485 10  VAL A N   
79   C CA  . VAL A 12  ? 1.2115 0.7202 0.7575 0.1014  0.0264  -0.2511 10  VAL A CA  
80   C C   . VAL A 12  ? 1.3036 0.8074 0.8806 0.1331  0.0299  -0.2485 10  VAL A C   
81   O O   . VAL A 12  ? 1.2630 0.8211 0.8803 0.1580  0.0510  -0.2505 10  VAL A O   
82   C CB  . VAL A 12  ? 1.2992 0.7662 0.7971 0.1053  0.0346  -0.2732 10  VAL A CB  
83   C CG1 . VAL A 12  ? 1.2852 0.7521 0.7462 0.0741  0.0249  -0.2715 10  VAL A CG1 
84   C CG2 . VAL A 12  ? 1.2569 0.7608 0.7716 0.1386  0.0719  -0.2937 10  VAL A CG2 
85   N N   . ASP A 13  ? 1.4454 0.8814 1.0031 0.1310  0.0065  -0.2417 11  ASP A N   
86   C CA  . ASP A 13  ? 1.4601 0.8774 1.0393 0.1591  0.0016  -0.2334 11  ASP A CA  
87   C C   . ASP A 13  ? 1.4325 0.9100 1.0530 0.1639  0.0021  -0.2171 11  ASP A C   
88   O O   . ASP A 13  ? 1.3698 0.8765 1.0235 0.1970  0.0104  -0.2148 11  ASP A O   
89   C CB  . ASP A 13  ? 1.3961 0.8101 0.9856 0.2001  0.0231  -0.2513 11  ASP A CB  
90   C CG  . ASP A 13  ? 1.6379 0.9660 1.1828 0.2029  0.0146  -0.2653 11  ASP A CG  
91   O OD1 . ASP A 13  ? 1.7559 1.0197 1.2734 0.1810  -0.0142 -0.2531 11  ASP A OD1 
92   O OD2 . ASP A 13  ? 1.7573 1.0843 1.2962 0.2257  0.0376  -0.2888 11  ASP A OD2 
93   N N   . ARG A 14  ? 1.2849 0.7832 0.9045 0.1311  -0.0083 -0.2061 12  ARG A N   
94   C CA  . ARG A 14  ? 1.1212 0.6744 0.7732 0.1318  -0.0080 -0.1939 12  ARG A CA  
95   C C   . ARG A 14  ? 1.0381 0.6655 0.7319 0.1618  0.0151  -0.2008 12  ARG A C   
96   O O   . ARG A 14  ? 0.9905 0.6768 0.7248 0.1602  0.0128  -0.1846 12  ARG A O   
97   C CB  . ARG A 14  ? 1.0927 0.6361 0.7636 0.1260  -0.0268 -0.1658 12  ARG A CB  
98   C CG  . ARG A 14  ? 1.1503 0.6743 0.8202 0.0865  -0.0482 -0.1392 12  ARG A CG  
99   C CD  . ARG A 14  ? 1.3809 0.8091 1.0111 0.0720  -0.0698 -0.1359 12  ARG A CD  
100  N NE  . ARG A 14  ? 1.5364 0.9672 1.1844 0.0403  -0.0853 -0.1021 12  ARG A NE  
101  C CZ  . ARG A 14  ? 1.4724 0.9198 1.1334 0.0000  -0.0956 -0.0876 12  ARG A CZ  
102  N NH1 . ARG A 14  ? 1.3622 0.8175 1.0443 -0.0262 -0.1042 -0.0545 12  ARG A NH1 
103  N NH2 . ARG A 14  ? 1.4133 0.8668 1.0653 -0.0142 -0.0980 -0.1041 12  ARG A NH2 
104  N N   . VAL A 15  ? 1.0535 0.7014 0.7551 0.1759  0.0377  -0.2161 13  VAL A N   
105  C CA  . VAL A 15  ? 0.9930 0.7122 0.7429 0.2020  0.0570  -0.2192 13  VAL A CA  
106  C C   . VAL A 15  ? 0.9256 0.7119 0.6993 0.1814  0.0623  -0.2139 13  VAL A C   
107  O O   . VAL A 15  ? 0.9038 0.6864 0.6559 0.1511  0.0634  -0.2144 13  VAL A O   
108  C CB  . VAL A 15  ? 0.9662 0.6909 0.7198 0.2196  0.0835  -0.2370 13  VAL A CB  
109  C CG1 . VAL A 15  ? 0.9176 0.7263 0.7284 0.2394  0.1059  -0.2382 13  VAL A CG1 
110  C CG2 . VAL A 15  ? 1.0302 0.6917 0.7694 0.2470  0.0771  -0.2427 13  VAL A CG2 
111  N N   . ILE A 16  ? 0.8896 0.7357 0.7079 0.1976  0.0611  -0.2082 14  ILE A N   
112  C CA  . ILE A 16  ? 0.8538 0.7658 0.7018 0.1765  0.0640  -0.2028 14  ILE A CA  
113  C C   . ILE A 16  ? 0.8712 0.8551 0.7691 0.1957  0.0810  -0.2093 14  ILE A C   
114  O O   . ILE A 16  ? 0.8261 0.8181 0.7468 0.2276  0.0872  -0.2128 14  ILE A O   
115  C CB  . ILE A 16  ? 0.8025 0.7288 0.6644 0.1601  0.0420  -0.1828 14  ILE A CB  
116  C CG1 . ILE A 16  ? 0.8215 0.7605 0.7068 0.1858  0.0293  -0.1725 14  ILE A CG1 
117  C CG2 . ILE A 16  ? 0.7772 0.6481 0.6037 0.1391  0.0283  -0.1731 14  ILE A CG2 
118  C CD1 . ILE A 16  ? 0.7837 0.7391 0.6731 0.1711  0.0115  -0.1543 14  ILE A CD1 
119  N N   . GLY A 17  ? 1.0602 1.0965 0.9810 0.1725  0.0868  -0.2071 15  GLY A N   
120  C CA  . GLY A 17  ? 1.0724 1.1845 1.0471 0.1803  0.1011  -0.2101 15  GLY A CA  
121  C C   . GLY A 17  ? 1.1974 1.3492 1.1902 0.1462  0.0961  -0.2033 15  GLY A C   
122  O O   . GLY A 17  ? 1.2352 1.3548 1.1978 0.1210  0.0856  -0.1983 15  GLY A O   
123  N N   . MET A 18  ? 1.0971 1.3198 1.1438 0.1458  0.1034  -0.2030 16  MET A N   
124  C CA  . MET A 18  ? 1.0661 1.3230 1.1341 0.1137  0.0930  -0.1968 16  MET A CA  
125  C C   . MET A 18  ? 1.0110 1.2888 1.0819 0.0893  0.1170  -0.1983 16  MET A C   
126  O O   . MET A 18  ? 0.9075 1.1531 0.9466 0.0611  0.1139  -0.1947 16  MET A O   
127  C CB  . MET A 18  ? 0.9540 1.2718 1.0787 0.1220  0.0744  -0.1920 16  MET A CB  
128  C CG  . MET A 18  ? 0.9717 1.2633 1.0846 0.1489  0.0525  -0.1871 16  MET A CG  
129  S SD  . MET A 18  ? 0.7929 1.1368 0.9484 0.1554  0.0178  -0.1777 16  MET A SD  
130  C CE  . MET A 18  ? 0.7763 1.0525 0.8762 0.1709  -0.0034 -0.1678 16  MET A CE  
131  N N   . GLU A 19  ? 0.9641 1.2970 1.0747 0.1005  0.1416  -0.2014 17  GLU A N   
132  C CA  . GLU A 19  ? 1.0035 1.3478 1.1021 0.0820  0.1735  -0.2021 17  GLU A CA  
133  C C   . GLU A 19  ? 0.8945 1.2184 0.9632 0.1123  0.2043  -0.2149 17  GLU A C   
134  O O   . GLU A 19  ? 0.8553 1.2198 0.9659 0.1374  0.2211  -0.2143 17  GLU A O   
135  C CB  . GLU A 19  ? 1.0180 1.4481 1.1859 0.0634  0.1844  -0.1945 17  GLU A CB  
136  C CG  . GLU A 19  ? 1.0870 1.5287 1.2378 0.0371  0.2195  -0.1900 17  GLU A CG  
137  C CD  . GLU A 19  ? 1.1902 1.5688 1.2824 -0.0006 0.2068  -0.1813 17  GLU A CD  
138  O OE1 . GLU A 19  ? 1.2666 1.6200 1.3594 -0.0140 0.1726  -0.1776 17  GLU A OE1 
139  O OE2 . GLU A 19  ? 1.2590 1.6116 1.3020 -0.0144 0.2309  -0.1784 17  GLU A OE2 
140  N N   . LEU A 26  ? 0.8184 0.7989 0.4990 -0.0788 0.1556  -0.1517 24  LEU A N   
141  C CA  . LEU A 26  ? 0.8771 0.7930 0.5038 -0.0853 0.1265  -0.1460 24  LEU A CA  
142  C C   . LEU A 26  ? 0.7436 0.6472 0.3994 -0.1013 0.0945  -0.1276 24  LEU A C   
143  O O   . LEU A 26  ? 0.7190 0.6274 0.4174 -0.0884 0.0752  -0.1313 24  LEU A O   
144  C CB  . LEU A 26  ? 0.8771 0.7698 0.4977 -0.0600 0.1146  -0.1630 24  LEU A CB  
145  C CG  . LEU A 26  ? 0.8752 0.7044 0.4367 -0.0676 0.0869  -0.1605 24  LEU A CG  
146  C CD1 . LEU A 26  ? 0.8448 0.6475 0.3358 -0.0739 0.1016  -0.1623 24  LEU A CD1 
147  C CD2 . LEU A 26  ? 0.8392 0.6516 0.4139 -0.0468 0.0716  -0.1720 24  LEU A CD2 
148  N N   . PRO A 27  ? 0.7597 0.6459 0.3905 -0.1282 0.0910  -0.1076 25  PRO A N   
149  C CA  . PRO A 27  ? 0.7223 0.5977 0.3882 -0.1407 0.0651  -0.0911 25  PRO A CA  
150  C C   . PRO A 27  ? 0.7573 0.6074 0.4410 -0.1274 0.0313  -0.0907 25  PRO A C   
151  O O   . PRO A 27  ? 0.7744 0.6399 0.5119 -0.1175 0.0217  -0.0949 25  PRO A O   
152  C CB  . PRO A 27  ? 0.8105 0.6525 0.4239 -0.1705 0.0632  -0.0667 25  PRO A CB  
153  C CG  . PRO A 27  ? 0.8212 0.6878 0.3977 -0.1772 0.1034  -0.0721 25  PRO A CG  
154  C CD  . PRO A 27  ? 0.8782 0.7528 0.4454 -0.1478 0.1136  -0.0986 25  PRO A CD  
155  N N   . ALA A 28  ? 0.7772 0.5904 0.4159 -0.1281 0.0133  -0.0858 26  ALA A N   
156  C CA  . ALA A 28  ? 0.6872 0.4827 0.3486 -0.1198 -0.0198 -0.0800 26  ALA A CA  
157  C C   . ALA A 28  ? 0.6816 0.5084 0.3980 -0.0970 -0.0164 -0.0963 26  ALA A C   
158  O O   . ALA A 28  ? 0.7928 0.6247 0.5535 -0.0887 -0.0328 -0.0920 26  ALA A O   
159  C CB  . ALA A 28  ? 0.7166 0.4748 0.3214 -0.1265 -0.0394 -0.0754 26  ALA A CB  
160  N N   . ASP A 29  ? 0.6401 0.4880 0.3536 -0.0851 0.0062  -0.1142 27  ASP A N   
161  C CA  . ASP A 29  ? 0.6539 0.5287 0.4131 -0.0650 0.0085  -0.1260 27  ASP A CA  
162  C C   . ASP A 29  ? 0.7005 0.6059 0.5075 -0.0619 0.0139  -0.1282 27  ASP A C   
163  O O   . ASP A 29  ? 0.7028 0.6226 0.5446 -0.0489 0.0083  -0.1330 27  ASP A O   
164  C CB  . ASP A 29  ? 0.6396 0.5238 0.3838 -0.0506 0.0278  -0.1424 27  ASP A CB  
165  C CG  . ASP A 29  ? 0.6230 0.5334 0.4091 -0.0312 0.0293  -0.1507 27  ASP A CG  
166  O OD1 . ASP A 29  ? 0.6586 0.5574 0.4541 -0.0269 0.0138  -0.1470 27  ASP A OD1 
167  O OD2 . ASP A 29  ? 0.6953 0.6407 0.5062 -0.0221 0.0449  -0.1587 27  ASP A OD2 
168  N N   . LEU A 30  ? 0.7003 0.6136 0.5059 -0.0764 0.0243  -0.1246 28  LEU A N   
169  C CA  . LEU A 30  ? 0.6113 0.5449 0.4578 -0.0781 0.0242  -0.1280 28  LEU A CA  
170  C C   . LEU A 30  ? 0.5795 0.4850 0.4410 -0.0790 0.0026  -0.1199 28  LEU A C   
171  O O   . LEU A 30  ? 0.6543 0.5689 0.5471 -0.0686 -0.0013 -0.1294 28  LEU A O   
172  C CB  . LEU A 30  ? 0.6363 0.5863 0.4818 -0.0984 0.0399  -0.1240 28  LEU A CB  
173  C CG  . LEU A 30  ? 0.7444 0.7354 0.5902 -0.0914 0.0658  -0.1341 28  LEU A CG  
174  C CD1 . LEU A 30  ? 0.7760 0.8068 0.6497 -0.1093 0.0816  -0.1319 28  LEU A CD1 
175  C CD2 . LEU A 30  ? 0.7215 0.7344 0.5887 -0.0636 0.0655  -0.1496 28  LEU A CD2 
176  N N   . ALA A 31  ? 0.6465 0.5164 0.4837 -0.0893 -0.0122 -0.1026 29  ALA A N   
177  C CA  . ALA A 31  ? 0.6674 0.5114 0.5256 -0.0842 -0.0344 -0.0932 29  ALA A CA  
178  C C   . ALA A 31  ? 0.6620 0.5219 0.5504 -0.0616 -0.0400 -0.1006 29  ALA A C   
179  O O   . ALA A 31  ? 0.7148 0.5765 0.6378 -0.0478 -0.0437 -0.1061 29  ALA A O   
180  C CB  . ALA A 31  ? 0.6304 0.4358 0.4560 -0.0987 -0.0539 -0.0695 29  ALA A CB  
181  N N   . TRP A 32  ? 0.6501 0.5193 0.5234 -0.0585 -0.0389 -0.1013 30  TRP A N   
182  C CA  . TRP A 32  ? 0.6393 0.5269 0.5408 -0.0426 -0.0418 -0.1049 30  TRP A CA  
183  C C   . TRP A 32  ? 0.6061 0.5224 0.5309 -0.0281 -0.0245 -0.1220 30  TRP A C   
184  O O   . TRP A 32  ? 0.5970 0.5252 0.5531 -0.0144 -0.0242 -0.1252 30  TRP A O   
185  C CB  . TRP A 32  ? 0.6219 0.5040 0.4947 -0.0475 -0.0451 -0.1029 30  TRP A CB  
186  C CG  . TRP A 32  ? 0.5825 0.4840 0.4768 -0.0363 -0.0422 -0.1072 30  TRP A CG  
187  C CD1 . TRP A 32  ? 0.5584 0.4768 0.4517 -0.0264 -0.0251 -0.1197 30  TRP A CD1 
188  C CD2 . TRP A 32  ? 0.5538 0.4600 0.4735 -0.0368 -0.0583 -0.0951 30  TRP A CD2 
189  N NE1 . TRP A 32  ? 0.5479 0.4751 0.4582 -0.0218 -0.0284 -0.1152 30  TRP A NE1 
190  C CE2 . TRP A 32  ? 0.5204 0.4438 0.4500 -0.0295 -0.0472 -0.1003 30  TRP A CE2 
191  C CE3 . TRP A 32  ? 0.5760 0.4767 0.5154 -0.0437 -0.0829 -0.0777 30  TRP A CE3 
192  C CZ2 . TRP A 32  ? 0.5155 0.4516 0.4738 -0.0324 -0.0566 -0.0885 30  TRP A CZ2 
193  C CZ3 . TRP A 32  ? 0.4959 0.4160 0.4712 -0.0447 -0.0938 -0.0671 30  TRP A CZ3 
194  C CH2 . TRP A 32  ? 0.4867 0.4248 0.4712 -0.0407 -0.0789 -0.0724 30  TRP A CH2 
195  N N   . PHE A 33  ? 0.5836 0.5133 0.4928 -0.0301 -0.0098 -0.1328 31  PHE A N   
196  C CA  . PHE A 33  ? 0.5567 0.5119 0.4832 -0.0188 0.0006  -0.1471 31  PHE A CA  
197  C C   . PHE A 33  ? 0.5833 0.5320 0.5281 -0.0176 -0.0028 -0.1534 31  PHE A C   
198  O O   . PHE A 33  ? 0.6483 0.6077 0.6064 -0.0040 0.0007  -0.1634 31  PHE A O   
199  C CB  . PHE A 33  ? 0.5366 0.5114 0.4529 -0.0219 0.0124  -0.1551 31  PHE A CB  
200  C CG  . PHE A 33  ? 0.5731 0.5742 0.5056 -0.0133 0.0161  -0.1677 31  PHE A CG  
201  C CD1 . PHE A 33  ? 0.5980 0.6142 0.5303 0.0020  0.0185  -0.1706 31  PHE A CD1 
202  C CD2 . PHE A 33  ? 0.5671 0.5727 0.5106 -0.0229 0.0135  -0.1751 31  PHE A CD2 
203  C CE1 . PHE A 33  ? 0.5845 0.6228 0.5234 0.0090  0.0179  -0.1804 31  PHE A CE1 
204  C CE2 . PHE A 33  ? 0.5942 0.6212 0.5461 -0.0174 0.0115  -0.1878 31  PHE A CE2 
205  C CZ  . PHE A 33  ? 0.5186 0.5633 0.4663 -0.0007 0.0134  -0.1901 31  PHE A CZ  
206  N N   . LYS A 34  ? 0.5976 0.5238 0.5378 -0.0324 -0.0089 -0.1482 32  LYS A N   
207  C CA  . LYS A 34  ? 0.6182 0.5268 0.5719 -0.0318 -0.0140 -0.1567 32  LYS A CA  
208  C C   . LYS A 34  ? 0.6233 0.5167 0.5973 -0.0130 -0.0205 -0.1555 32  LYS A C   
209  O O   . LYS A 34  ? 0.5690 0.4593 0.5536 0.0008  -0.0166 -0.1716 32  LYS A O   
210  C CB  . LYS A 34  ? 0.6056 0.4878 0.5494 -0.0554 -0.0202 -0.1479 32  LYS A CB  
211  C CG  . LYS A 34  ? 0.7455 0.5920 0.7001 -0.0559 -0.0303 -0.1563 32  LYS A CG  
212  C CD  . LYS A 34  ? 0.9046 0.7368 0.8524 -0.0854 -0.0333 -0.1540 32  LYS A CD  
213  C CE  . LYS A 34  ? 0.9026 0.6790 0.8544 -0.0893 -0.0485 -0.1589 32  LYS A CE  
214  N NZ  . LYS A 34  ? 1.0071 0.7408 0.9624 -0.0745 -0.0610 -0.1444 32  LYS A NZ  
215  N N   . ARG A 35  ? 0.5903 0.4773 0.5709 -0.0108 -0.0300 -0.1377 33  ARG A N   
216  C CA  . ARG A 35  ? 0.5912 0.4726 0.6048 0.0089  -0.0361 -0.1348 33  ARG A CA  
217  C C   . ARG A 35  ? 0.5643 0.4826 0.5969 0.0277  -0.0205 -0.1449 33  ARG A C   
218  O O   . ARG A 35  ? 0.6347 0.5559 0.6933 0.0483  -0.0139 -0.1532 33  ARG A O   
219  C CB  . ARG A 35  ? 0.5773 0.4469 0.6008 0.0052  -0.0566 -0.1101 33  ARG A CB  
220  C CG  . ARG A 35  ? 0.7019 0.6006 0.7287 0.0034  -0.0576 -0.1011 33  ARG A CG  
221  C CD  . ARG A 35  ? 0.8091 0.6969 0.8372 -0.0066 -0.0837 -0.0769 33  ARG A CD  
222  N NE  . ARG A 35  ? 0.9990 0.8549 0.9744 -0.0296 -0.0924 -0.0690 33  ARG A NE  
223  C CZ  . ARG A 35  ? 1.0176 0.8544 0.9675 -0.0447 -0.1152 -0.0502 33  ARG A CZ  
224  N NH1 . ARG A 35  ? 0.9365 0.7442 0.8298 -0.0651 -0.1163 -0.0451 33  ARG A NH1 
225  N NH2 . ARG A 35  ? 1.0127 0.8632 0.9908 -0.0418 -0.1357 -0.0371 33  ARG A NH2 
226  N N   . ASN A 36  ? 0.5698 0.5138 0.5878 0.0221  -0.0125 -0.1441 34  ASN A N   
227  C CA  . ASN A 36  ? 0.5118 0.4879 0.5427 0.0355  0.0021  -0.1481 34  ASN A CA  
228  C C   . ASN A 36  ? 0.5334 0.5185 0.5451 0.0430  0.0173  -0.1686 34  ASN A C   
229  O O   . ASN A 36  ? 0.5645 0.5736 0.5784 0.0532  0.0311  -0.1705 34  ASN A O   
230  C CB  . ASN A 36  ? 0.4742 0.4642 0.4965 0.0255  -0.0003 -0.1348 34  ASN A CB  
231  C CG  . ASN A 36  ? 0.5422 0.5296 0.5860 0.0188  -0.0174 -0.1149 34  ASN A CG  
232  O OD1 . ASN A 36  ? 0.6063 0.6170 0.6900 0.0275  -0.0163 -0.1062 34  ASN A OD1 
233  N ND2 . ASN A 36  ? 0.5474 0.5099 0.5648 0.0024  -0.0332 -0.1069 34  ASN A ND2 
234  N N   . THR A 37  ? 0.5723 0.5400 0.5639 0.0351  0.0136  -0.1817 35  THR A N   
235  C CA  . THR A 37  ? 0.5304 0.5028 0.5023 0.0399  0.0209  -0.2022 35  THR A CA  
236  C C   . THR A 37  ? 0.5819 0.5220 0.5513 0.0430  0.0171  -0.2203 35  THR A C   
237  O O   . THR A 37  ? 0.6114 0.5477 0.5578 0.0448  0.0193  -0.2405 35  THR A O   
238  C CB  . THR A 37  ? 0.5367 0.5221 0.4898 0.0259  0.0161  -0.2038 35  THR A CB  
239  O OG1 . THR A 37  ? 0.5073 0.4786 0.4640 0.0083  0.0070  -0.1974 35  THR A OG1 
240  C CG2 . THR A 37  ? 0.5182 0.5276 0.4667 0.0288  0.0209  -0.1913 35  THR A CG2 
241  N N   . LEU A 38  ? 0.6262 0.4845 0.6960 0.1136  0.0623  -0.1048 36  LEU A N   
242  C CA  . LEU A 38  ? 0.6505 0.4742 0.7188 0.1175  0.0557  -0.1096 36  LEU A CA  
243  C C   . LEU A 38  ? 0.6480 0.4750 0.7057 0.1319  0.0576  -0.1132 36  LEU A C   
244  O O   . LEU A 38  ? 0.6777 0.5247 0.7394 0.1426  0.0618  -0.1104 36  LEU A O   
245  C CB  . LEU A 38  ? 0.6909 0.4846 0.7719 0.1205  0.0468  -0.1045 36  LEU A CB  
246  C CG  . LEU A 38  ? 0.7254 0.4671 0.8019 0.1168  0.0344  -0.1066 36  LEU A CG  
247  C CD1 . LEU A 38  ? 0.7467 0.4708 0.8286 0.0917  0.0339  -0.1068 36  LEU A CD1 
248  C CD2 . LEU A 38  ? 0.6577 0.3688 0.7403 0.1287  0.0207  -0.0988 36  LEU A CD2 
249  N N   . ASN A 39  ? 0.6477 0.4571 0.6951 0.1306  0.0568  -0.1206 37  ASN A N   
250  C CA  . ASN A 39  ? 0.6551 0.4665 0.6958 0.1424  0.0621  -0.1258 37  ASN A CA  
251  C C   . ASN A 39  ? 0.6415 0.4931 0.6796 0.1443  0.0716  -0.1226 37  ASN A C   
252  O O   . ASN A 39  ? 0.6861 0.5498 0.7284 0.1539  0.0788  -0.1259 37  ASN A O   
253  C CB  . ASN A 39  ? 0.7083 0.5031 0.7603 0.1572  0.0601  -0.1273 37  ASN A CB  
254  C CG  . ASN A 39  ? 0.7727 0.5193 0.8268 0.1541  0.0465  -0.1276 37  ASN A CG  
255  O OD1 . ASN A 39  ? 0.8108 0.5249 0.8546 0.1446  0.0405  -0.1335 37  ASN A OD1 
256  N ND2 . ASN A 39  ? 0.7667 0.5060 0.8343 0.1604  0.0394  -0.1206 37  ASN A ND2 
257  N N   . LYS A 40  ? 0.5945 0.4665 0.6293 0.1342  0.0719  -0.1174 38  LYS A N   
258  C CA  . LYS A 40  ? 0.5215 0.4203 0.5513 0.1337  0.0782  -0.1145 38  LYS A CA  
259  C C   . LYS A 40  ? 0.5542 0.4550 0.5734 0.1250  0.0776  -0.1157 38  LYS A C   
260  O O   . LYS A 40  ? 0.6341 0.5279 0.6535 0.1169  0.0736  -0.1163 38  LYS A O   
261  C CB  . LYS A 40  ? 0.5444 0.4621 0.5802 0.1309  0.0785  -0.1077 38  LYS A CB  
262  C CG  . LYS A 40  ? 0.5172 0.4426 0.5675 0.1397  0.0810  -0.1068 38  LYS A CG  
263  C CD  . LYS A 40  ? 0.4819 0.4232 0.5399 0.1338  0.0805  -0.1020 38  LYS A CD  
264  C CE  . LYS A 40  ? 0.5045 0.4411 0.5779 0.1388  0.0774  -0.1003 38  LYS A CE  
265  N NZ  . LYS A 40  ? 0.4644 0.4194 0.5497 0.1341  0.0797  -0.0971 38  LYS A NZ  
266  N N   . PRO A 41  ? 0.5278 0.4417 0.5454 0.1250  0.0833  -0.1191 39  PRO A N   
267  C CA  . PRO A 41  ? 0.5150 0.4327 0.5257 0.1175  0.0831  -0.1204 39  PRO A CA  
268  C C   . PRO A 41  ? 0.5472 0.4739 0.5548 0.1127  0.0813  -0.1133 39  PRO A C   
269  O O   . PRO A 41  ? 0.5767 0.5113 0.5853 0.1146  0.0821  -0.1089 39  PRO A O   
270  C CB  . PRO A 41  ? 0.4886 0.4179 0.4984 0.1200  0.0899  -0.1255 39  PRO A CB  
271  C CG  . PRO A 41  ? 0.5220 0.4637 0.5388 0.1261  0.0949  -0.1238 39  PRO A CG  
272  C CD  . PRO A 41  ? 0.5645 0.4925 0.5875 0.1319  0.0912  -0.1227 39  PRO A CD  
273  N N   . VAL A 42  ? 0.5234 0.4486 0.5264 0.1073  0.0793  -0.1134 40  VAL A N   
274  C CA  . VAL A 42  ? 0.5044 0.4341 0.5020 0.1057  0.0780  -0.1083 40  VAL A CA  
275  C C   . VAL A 42  ? 0.5009 0.4343 0.4900 0.1048  0.0805  -0.1090 40  VAL A C   
276  O O   . VAL A 42  ? 0.5054 0.4407 0.4940 0.1030  0.0827  -0.1145 40  VAL A O   
277  C CB  . VAL A 42  ? 0.5083 0.4362 0.5081 0.1021  0.0754  -0.1075 40  VAL A CB  
278  C CG1 . VAL A 42  ? 0.5291 0.4509 0.5386 0.1026  0.0728  -0.1062 40  VAL A CG1 
279  C CG2 . VAL A 42  ? 0.4678 0.3966 0.4697 0.0966  0.0771  -0.1149 40  VAL A CG2 
280  N N   . ILE A 43  ? 0.4538 0.3852 0.4355 0.1052  0.0799  -0.1036 41  ILE A N   
281  C CA  . ILE A 43  ? 0.4420 0.3701 0.4161 0.1041  0.0836  -0.1037 41  ILE A CA  
282  C C   . ILE A 43  ? 0.5411 0.4659 0.5165 0.1020  0.0845  -0.1035 41  ILE A C   
283  O O   . ILE A 43  ? 0.5482 0.4666 0.5232 0.1015  0.0828  -0.0996 41  ILE A O   
284  C CB  . ILE A 43  ? 0.4738 0.3953 0.4397 0.1047  0.0851  -0.1007 41  ILE A CB  
285  C CG1 . ILE A 43  ? 0.4301 0.3631 0.3997 0.1071  0.0866  -0.1047 41  ILE A CG1 
286  C CG2 . ILE A 43  ? 0.5231 0.4380 0.4876 0.0998  0.0904  -0.1041 41  ILE A CG2 
287  C CD1 . ILE A 43  ? 0.3675 0.3042 0.3332 0.1078  0.0900  -0.1074 41  ILE A CD1 
288  N N   . MET A 44  ? 0.5428 0.4766 0.5217 0.1020  0.0863  -0.1113 42  MET A N   
289  C CA  . MET A 44  ? 0.4666 0.4101 0.4508 0.1040  0.0830  -0.1175 42  MET A CA  
290  C C   . MET A 44  ? 0.5107 0.4687 0.4957 0.1089  0.0770  -0.1261 42  MET A C   
291  O O   . MET A 44  ? 0.5291 0.4914 0.5122 0.1081  0.0790  -0.1277 42  MET A O   
292  C CB  . MET A 44  ? 0.4696 0.4294 0.4577 0.1021  0.0829  -0.1192 42  MET A CB  
293  C CG  . MET A 44  ? 0.4392 0.4153 0.4291 0.0993  0.0839  -0.1244 42  MET A CG  
294  S SD  . MET A 44  ? 0.4300 0.4240 0.4258 0.0922  0.0849  -0.1296 42  MET A SD  
295  C CE  . MET A 44  ? 0.3584 0.3293 0.3534 0.0904  0.0849  -0.1260 42  MET A CE  
296  N N   . GLY A 45  ? 0.4193 0.3867 0.4044 0.1171  0.0671  -0.1325 43  GLY A N   
297  C CA  . GLY A 45  ? 0.4590 0.4436 0.4412 0.1279  0.0572  -0.1410 43  GLY A CA  
298  C C   . GLY A 45  ? 0.4726 0.4928 0.4615 0.1274  0.0575  -0.1480 43  GLY A C   
299  O O   . GLY A 45  ? 0.4599 0.4881 0.4542 0.1183  0.0645  -0.1463 43  GLY A O   
300  N N   . ARG A 46  ? 0.5119 0.5533 0.4993 0.1368  0.0495  -0.1559 44  ARG A N   
301  C CA  . ARG A 46  ? 0.4863 0.5709 0.4809 0.1373  0.0476  -0.1653 44  ARG A CA  
302  C C   . ARG A 46  ? 0.5302 0.6362 0.5299 0.1380  0.0455  -0.1698 44  ARG A C   
303  O O   . ARG A 46  ? 0.5549 0.6843 0.5612 0.1264  0.0525  -0.1717 44  ARG A O   
304  C CB  . ARG A 46  ? 0.5399 0.6499 0.5317 0.1538  0.0347  -0.1752 44  ARG A CB  
305  C CG  . ARG A 46  ? 0.6681 0.7862 0.6579 0.1545  0.0345  -0.1774 44  ARG A CG  
306  C CD  . ARG A 46  ? 0.7542 0.8798 0.7349 0.1791  0.0163  -0.1854 44  ARG A CD  
307  N NE  . ARG A 46  ? 0.7022 0.7815 0.6686 0.1862  0.0113  -0.1785 44  ARG A NE  
308  C CZ  . ARG A 46  ? 0.5128 0.5819 0.4640 0.2099  -0.0076 -0.1839 44  ARG A CZ  
309  N NH1 . ARG A 46  ? 0.6155 0.7188 0.5657 0.2301  -0.0226 -0.1963 44  ARG A NH1 
310  N NH2 . ARG A 46  ? 0.4640 0.4890 0.3982 0.2152  -0.0136 -0.1781 44  ARG A NH2 
311  N N   . HIS A 47  ? 0.5196 0.6218 0.5146 0.1530  0.0342  -0.1738 45  HIS A N   
312  C CA  A HIS A 47  ? 0.5240 0.6541 0.5233 0.1563  0.0305  -0.1813 45  HIS A CA  
313  C CA  B HIS A 47  ? 0.4965 0.6221 0.4949 0.1571  0.0299  -0.1807 45  HIS A CA  
314  C C   . HIS A 47  ? 0.5326 0.6532 0.5363 0.1386  0.0436  -0.1734 45  HIS A C   
315  O O   . HIS A 47  ? 0.5406 0.6985 0.5510 0.1319  0.0463  -0.1794 45  HIS A O   
316  C CB  A HIS A 47  ? 0.5223 0.6398 0.5125 0.1759  0.0156  -0.1867 45  HIS A CB  
317  C CB  B HIS A 47  ? 0.5474 0.6465 0.5351 0.1734  0.0176  -0.1823 45  HIS A CB  
318  C CG  A HIS A 47  ? 0.4174 0.5526 0.4016 0.1979  -0.0006 -0.1978 45  HIS A CG  
319  C CG  B HIS A 47  ? 0.4767 0.5231 0.4552 0.1694  0.0202  -0.1704 45  HIS A CG  
320  N ND1 A HIS A 47  ? 0.4144 0.6002 0.4064 0.2014  -0.0033 -0.2078 45  HIS A ND1 
321  N ND1 B HIS A 47  ? 0.3817 0.4031 0.3633 0.1522  0.0338  -0.1588 45  HIS A ND1 
322  C CD2 A HIS A 47  ? 0.4468 0.5549 0.4161 0.2177  -0.0161 -0.2004 45  HIS A CD2 
323  C CD2 B HIS A 47  ? 0.4629 0.4799 0.4282 0.1808  0.0099  -0.1693 45  HIS A CD2 
324  C CE1 A HIS A 47  ? 0.4398 0.6314 0.4232 0.2245  -0.0198 -0.2167 45  HIS A CE1 
325  C CE1 B HIS A 47  ? 0.3898 0.3753 0.3633 0.1517  0.0331  -0.1519 45  HIS A CE1 
326  N NE2 A HIS A 47  ? 0.4616 0.6033 0.4298 0.2353  -0.0283 -0.2122 45  HIS A NE2 
327  N NE2 B HIS A 47  ? 0.4137 0.3935 0.3761 0.1679  0.0186  -0.1576 45  HIS A NE2 
328  N N   . THR A 48  ? 0.5421 0.6191 0.5420 0.1308  0.0511  -0.1612 46  THR A N   
329  C CA  . THR A 48  ? 0.5015 0.5661 0.5036 0.1173  0.0620  -0.1532 46  THR A CA  
330  C C   . THR A 48  ? 0.5171 0.5986 0.5240 0.1054  0.0696  -0.1542 46  THR A C   
331  O O   . THR A 48  ? 0.5262 0.6314 0.5390 0.0969  0.0726  -0.1595 46  THR A O   
332  C CB  . THR A 48  ? 0.5330 0.5531 0.5299 0.1154  0.0655  -0.1420 46  THR A CB  
333  O OG1 . THR A 48  ? 0.5409 0.5496 0.5325 0.1258  0.0559  -0.1450 46  THR A OG1 
334  C CG2 . THR A 48  ? 0.4599 0.4646 0.4570 0.1057  0.0744  -0.1329 46  THR A CG2 
335  N N   . TRP A 49  ? 0.5560 0.6320 0.5615 0.1041  0.0712  -0.1535 47  TRP A N   
336  C CA  . TRP A 49  ? 0.5530 0.6518 0.5640 0.0931  0.0754  -0.1607 47  TRP A CA  
337  C C   . TRP A 49  ? 0.5190 0.6790 0.5384 0.0885  0.0720  -0.1759 47  TRP A C   
338  O O   . TRP A 49  ? 0.4852 0.6732 0.5102 0.0722  0.0773  -0.1840 47  TRP A O   
339  C CB  . TRP A 49  ? 0.5491 0.6365 0.5564 0.0940  0.0761  -0.1596 47  TRP A CB  
340  C CG  . TRP A 49  ? 0.5129 0.6334 0.5260 0.0826  0.0781  -0.1723 47  TRP A CG  
341  C CD1 . TRP A 49  ? 0.4354 0.5950 0.4515 0.0831  0.0741  -0.1826 47  TRP A CD1 
342  C CD2 . TRP A 49  ? 0.4816 0.6000 0.4983 0.0670  0.0845  -0.1790 47  TRP A CD2 
343  N NE1 . TRP A 49  ? 0.4156 0.5999 0.4357 0.0657  0.0789  -0.1942 47  TRP A NE1 
344  C CE2 . TRP A 49  ? 0.4426 0.5995 0.4626 0.0546  0.0856  -0.1937 47  TRP A CE2 
345  C CE3 . TRP A 49  ? 0.4479 0.5360 0.4658 0.0612  0.0886  -0.1762 47  TRP A CE3 
346  C CZ2 . TRP A 49  ? 0.4716 0.6318 0.4923 0.0324  0.0926  -0.2073 47  TRP A CZ2 
347  C CZ3 . TRP A 49  ? 0.5018 0.5899 0.5236 0.0426  0.0942  -0.1906 47  TRP A CZ3 
348  C CH2 . TRP A 49  ? 0.5066 0.6272 0.5274 0.0264  0.0969  -0.2067 47  TRP A CH2 
349  N N   . GLU A 50  ? 0.5303 0.7172 0.5504 0.1010  0.0629  -0.1817 48  GLU A N   
350  C CA  . GLU A 50  ? 0.4445 0.7005 0.4726 0.0970  0.0585  -0.1966 48  GLU A CA  
351  C C   . GLU A 50  ? 0.4603 0.7473 0.4926 0.0879  0.0604  -0.2009 48  GLU A C   
352  O O   . GLU A 50  ? 0.4414 0.7904 0.4797 0.0720  0.0617  -0.2112 48  GLU A O   
353  C CB  . GLU A 50  ? 0.4233 0.7025 0.4513 0.1173  0.0454  -0.2038 48  GLU A CB  
354  C CG  . GLU A 50  ? 0.4667 0.7468 0.4935 0.1210  0.0432  -0.2054 48  GLU A CG  
355  C CD  . GLU A 50  ? 0.5181 0.8097 0.5418 0.1453  0.0284  -0.2119 48  GLU A CD  
356  O OE1 . GLU A 50  ? 0.4876 0.8099 0.5129 0.1588  0.0182  -0.2211 48  GLU A OE1 
357  O OE2 . GLU A 50  ? 0.5908 0.8630 0.6093 0.1519  0.0260  -0.2093 48  GLU A OE2 
358  N N   . SER A 51  ? 0.4887 0.7380 0.5168 0.0939  0.0611  -0.1928 49  SER A N   
359  C CA  . SER A 51  ? 0.5124 0.7936 0.5436 0.0862  0.0623  -0.1974 49  SER A CA  
360  C C   . SER A 51  ? 0.5277 0.8080 0.5602 0.0626  0.0741  -0.1952 49  SER A C   
361  O O   . SER A 51  ? 0.6235 0.9515 0.6579 0.0458  0.0769  -0.2010 49  SER A O   
362  C CB  . SER A 51  ? 0.5036 0.7519 0.5293 0.1027  0.0567  -0.1929 49  SER A CB  
363  O OG  . SER A 51  ? 0.5989 0.7843 0.6187 0.1017  0.0626  -0.1787 49  SER A OG  
364  N N   . ILE A 52  ? 0.4873 0.7192 0.5176 0.0588  0.0805  -0.1883 50  ILE A N   
365  C CA  . ILE A 52  ? 0.4963 0.7275 0.5277 0.0356  0.0912  -0.1915 50  ILE A CA  
366  C C   . ILE A 52  ? 0.5611 0.8324 0.5907 0.0100  0.0971  -0.2026 50  ILE A C   
367  O O   . ILE A 52  ? 0.6014 0.9035 0.6237 -0.0228 0.1056  -0.2070 50  ILE A O   
368  C CB  . ILE A 52  ? 0.4734 0.6339 0.5046 0.0436  0.0938  -0.1820 50  ILE A CB  
369  C CG1 . ILE A 52  ? 0.5586 0.6850 0.5863 0.0553  0.0905  -0.1756 50  ILE A CG1 
370  C CG2 . ILE A 52  ? 0.5770 0.7068 0.6057 0.0596  0.0894  -0.1698 50  ILE A CG2 
371  C CD1 . ILE A 52  ? 0.5918 0.6619 0.6185 0.0596  0.0916  -0.1658 50  ILE A CD1 
372  N N   . GLY A 53  ? 0.6250 0.8957 0.6554 0.0181  0.0930  -0.2046 51  GLY A N   
373  C CA  . GLY A 53  ? 0.5978 0.9078 0.6236 -0.0097 0.0985  -0.2155 51  GLY A CA  
374  C C   . GLY A 53  ? 0.6835 0.9439 0.7003 -0.0295 0.1051  -0.2176 51  GLY A C   
375  O O   . GLY A 53  ? 0.6822 0.9405 0.6956 -0.0345 0.1048  -0.2239 51  GLY A O   
376  N N   . ARG A 54  ? 0.6527 0.8576 0.6670 -0.0405 0.1011  -0.2013 52  ARG A N   
377  C CA  . ARG A 54  ? 0.6237 0.7552 0.6316 -0.0549 0.0945  -0.1897 52  ARG A CA  
378  C C   . ARG A 54  ? 0.5817 0.6585 0.5994 -0.0207 0.0980  -0.1939 52  ARG A C   
379  O O   . ARG A 54  ? 0.5788 0.6592 0.6055 0.0042  0.1027  -0.1955 52  ARG A O   
380  C CB  . ARG A 54  ? 0.7562 0.8645 0.7559 -0.0818 0.0858  -0.1697 52  ARG A CB  
381  C CG  . ARG A 54  ? 0.7964 0.9162 0.7773 -0.1294 0.0756  -0.1580 52  ARG A CG  
382  C CD  . ARG A 54  ? 0.9574 1.0559 0.9296 -0.1522 0.0661  -0.1360 52  ARG A CD  
383  N NE  . ARG A 54  ? 1.0574 1.2353 1.0318 -0.1607 0.0718  -0.1353 52  ARG A NE  
384  C CZ  . ARG A 54  ? 1.1380 1.3979 1.1058 -0.1863 0.0742  -0.1397 52  ARG A CZ  
385  N NH1 . ARG A 54  ? 1.0849 1.3573 1.0419 -0.2110 0.0707  -0.1425 52  ARG A NH1 
386  N NH2 . ARG A 54  ? 1.0572 1.3925 1.0285 -0.1885 0.0797  -0.1426 52  ARG A NH2 
387  N N   . PRO A 55  ? 0.6129 0.6423 0.6281 -0.0193 0.0955  -0.1968 53  PRO A N   
388  C CA  . PRO A 55  ? 0.5492 0.5290 0.5731 0.0068  0.0974  -0.1976 53  PRO A CA  
389  C C   . PRO A 55  ? 0.6016 0.5520 0.6287 0.0051  0.0922  -0.1825 53  PRO A C   
390  O O   . PRO A 55  ? 0.6553 0.5983 0.6734 -0.0211 0.0831  -0.1696 53  PRO A O   
391  C CB  . PRO A 55  ? 0.5336 0.4718 0.5510 0.0016  0.0925  -0.2043 53  PRO A CB  
392  C CG  . PRO A 55  ? 0.5830 0.5553 0.5893 -0.0210 0.0914  -0.2106 53  PRO A CG  
393  C CD  . PRO A 55  ? 0.6186 0.6536 0.6245 -0.0346 0.0935  -0.2056 53  PRO A CD  
394  N N   . LEU A 56  ? 0.6273 0.5631 0.6657 0.0308  0.0968  -0.1826 54  LEU A N   
395  C CA  . LEU A 56  ? 0.5459 0.4523 0.5888 0.0316  0.0913  -0.1691 54  LEU A CA  
396  C C   . LEU A 56  ? 0.5659 0.4176 0.6066 0.0301  0.0815  -0.1677 54  LEU A C   
397  O O   . LEU A 56  ? 0.6215 0.4640 0.6609 0.0472  0.0789  -0.1690 54  LEU A O   
398  C CB  . LEU A 56  ? 0.5334 0.4485 0.5796 0.0541  0.0897  -0.1557 54  LEU A CB  
399  C CG  . LEU A 56  ? 0.4324 0.3878 0.4743 0.0575  0.0920  -0.1528 54  LEU A CG  
400  C CD1 . LEU A 56  ? 0.4827 0.4334 0.5167 0.0728  0.0856  -0.1350 54  LEU A CD1 
401  C CD2 . LEU A 56  ? 0.4662 0.4420 0.5141 0.0407  0.0994  -0.1638 54  LEU A CD2 
402  N N   . PRO A 57  ? 0.6146 0.4370 0.6461 0.0096  0.0678  -0.1537 55  PRO A N   
403  C CA  . PRO A 57  ? 0.6164 0.3787 0.6406 0.0083  0.0535  -0.1545 55  PRO A CA  
404  C C   . PRO A 57  ? 0.6780 0.4146 0.7171 0.0421  0.0543  -0.1622 55  PRO A C   
405  O O   . PRO A 57  ? 0.6762 0.4355 0.7237 0.0567  0.0576  -0.1518 55  PRO A O   
406  C CB  . PRO A 57  ? 0.5932 0.3303 0.6034 -0.0192 0.0367  -0.1328 55  PRO A CB  
407  C CG  . PRO A 57  ? 0.6571 0.4387 0.6760 -0.0193 0.0453  -0.1225 55  PRO A CG  
408  C CD  . PRO A 57  ? 0.6228 0.4630 0.6479 -0.0129 0.0626  -0.1362 55  PRO A CD  
409  N N   . GLY A 58  ? 0.6929 0.4023 0.7188 0.0512  0.0437  -0.1661 56  GLY A N   
410  C CA  . GLY A 58  ? 0.7606 0.4635 0.7789 0.0780  0.0393  -0.1603 56  GLY A CA  
411  C C   . GLY A 58  ? 0.8036 0.5601 0.8274 0.0936  0.0512  -0.1524 56  GLY A C   
412  O O   . GLY A 58  ? 0.7308 0.4957 0.7610 0.1030  0.0515  -0.1429 56  GLY A O   
413  N N   . ARG A 59  ? 0.7891 0.5781 0.8087 0.0933  0.0589  -0.1555 57  ARG A N   
414  C CA  . ARG A 59  ? 0.6835 0.5151 0.7026 0.1001  0.0665  -0.1458 57  ARG A CA  
415  C C   . ARG A 59  ? 0.6627 0.5132 0.6744 0.0971  0.0711  -0.1501 57  ARG A C   
416  O O   . ARG A 59  ? 0.7674 0.6218 0.7817 0.0847  0.0725  -0.1580 57  ARG A O   
417  C CB  . ARG A 59  ? 0.5443 0.3962 0.5724 0.0931  0.0692  -0.1387 57  ARG A CB  
418  C CG  . ARG A 59  ? 0.5925 0.4445 0.6261 0.1003  0.0672  -0.1295 57  ARG A CG  
419  C CD  . ARG A 59  ? 0.5806 0.4448 0.6236 0.0914  0.0700  -0.1258 57  ARG A CD  
420  N NE  . ARG A 59  ? 0.6193 0.4575 0.6739 0.0794  0.0696  -0.1322 57  ARG A NE  
421  C CZ  . ARG A 59  ? 0.6854 0.5247 0.7509 0.0717  0.0735  -0.1299 57  ARG A CZ  
422  N NH1 . ARG A 59  ? 0.7968 0.6106 0.8629 0.0533  0.0690  -0.1280 57  ARG A NH1 
423  N NH2 . ARG A 59  ? 0.6982 0.5653 0.7636 0.0774  0.0762  -0.1222 57  ARG A NH2 
424  N N   . LYS A 60  ? 0.6206 0.4841 0.6246 0.1066  0.0748  -0.1463 58  LYS A N   
425  C CA  . LYS A 60  ? 0.5615 0.4439 0.5594 0.1031  0.0788  -0.1475 58  LYS A CA  
426  C C   . LYS A 60  ? 0.5511 0.4544 0.5493 0.0986  0.0800  -0.1386 58  LYS A C   
427  O O   . LYS A 60  ? 0.5231 0.4345 0.5216 0.1027  0.0803  -0.1289 58  LYS A O   
428  C CB  . LYS A 60  ? 0.5020 0.3950 0.4971 0.1112  0.0841  -0.1471 58  LYS A CB  
429  C CG  . LYS A 60  ? 0.5103 0.4168 0.5014 0.1068  0.0873  -0.1521 58  LYS A CG  
430  C CD  . LYS A 60  ? 0.5144 0.4324 0.5076 0.1121  0.0930  -0.1578 58  LYS A CD  
431  C CE  . LYS A 60  ? 0.5445 0.4718 0.5318 0.1073  0.0949  -0.1651 58  LYS A CE  
432  N NZ  . LYS A 60  ? 0.6298 0.5802 0.6172 0.1079  0.1008  -0.1653 58  LYS A NZ  
433  N N   . ASN A 61  ? 0.5715 0.4835 0.5719 0.0895  0.0811  -0.1451 59  ASN A N   
434  C CA  . ASN A 61  ? 0.4990 0.4308 0.4968 0.0882  0.0828  -0.1389 59  ASN A CA  
435  C C   . ASN A 61  ? 0.4813 0.4220 0.4691 0.0919  0.0853  -0.1358 59  ASN A C   
436  O O   . ASN A 61  ? 0.4807 0.4246 0.4684 0.0884  0.0866  -0.1453 59  ASN A O   
437  C CB  . ASN A 61  ? 0.4981 0.4435 0.5048 0.0766  0.0848  -0.1509 59  ASN A CB  
438  C CG  . ASN A 61  ? 0.5123 0.4521 0.5298 0.0700  0.0852  -0.1542 59  ASN A CG  
439  O OD1 . ASN A 61  ? 0.6050 0.5360 0.6303 0.0563  0.0876  -0.1689 59  ASN A OD1 
440  N ND2 . ASN A 61  ? 0.5836 0.5250 0.5999 0.0767  0.0836  -0.1424 59  ASN A ND2 
441  N N   . ILE A 62  ? 0.4681 0.4139 0.4539 0.0963  0.0864  -0.1283 60  ILE A N   
442  C CA  . ILE A 62  ? 0.4734 0.4250 0.4539 0.0981  0.0893  -0.1285 60  ILE A CA  
443  C C   . ILE A 62  ? 0.4995 0.4552 0.4774 0.0991  0.0895  -0.1253 60  ILE A C   
444  O O   . ILE A 62  ? 0.4651 0.4137 0.4426 0.1010  0.0888  -0.1196 60  ILE A O   
445  C CB  . ILE A 62  ? 0.4514 0.3985 0.4292 0.1023  0.0914  -0.1251 60  ILE A CB  
446  C CG1 . ILE A 62  ? 0.4224 0.3691 0.4057 0.1027  0.0923  -0.1315 60  ILE A CG1 
447  C CG2 . ILE A 62  ? 0.4582 0.4077 0.4277 0.1030  0.0949  -0.1249 60  ILE A CG2 
448  C CD1 . ILE A 62  ? 0.4747 0.4242 0.4593 0.1068  0.0955  -0.1291 60  ILE A CD1 
449  N N   . ILE A 63  ? 0.4926 0.4607 0.4700 0.0981  0.0897  -0.1310 61  ILE A N   
450  C CA  . ILE A 63  ? 0.5144 0.4933 0.4942 0.1005  0.0867  -0.1332 61  ILE A CA  
451  C C   . ILE A 63  ? 0.4803 0.4554 0.4552 0.1046  0.0853  -0.1343 61  ILE A C   
452  O O   . ILE A 63  ? 0.5131 0.4922 0.4836 0.1039  0.0870  -0.1375 61  ILE A O   
453  C CB  . ILE A 63  ? 0.4616 0.4669 0.4462 0.0980  0.0844  -0.1419 61  ILE A CB  
454  C CG1 . ILE A 63  ? 0.4188 0.4254 0.4065 0.0907  0.0866  -0.1437 61  ILE A CG1 
455  C CG2 . ILE A 63  ? 0.4525 0.4769 0.4413 0.1041  0.0780  -0.1460 61  ILE A CG2 
456  C CD1 . ILE A 63  ? 0.4426 0.4385 0.4318 0.0910  0.0866  -0.1374 61  ILE A CD1 
457  N N   . LEU A 64  ? 0.4959 0.4630 0.4705 0.1090  0.0808  -0.1332 62  LEU A N   
458  C CA  . LEU A 64  ? 0.5181 0.4774 0.4856 0.1141  0.0759  -0.1360 62  LEU A CA  
459  C C   . LEU A 64  ? 0.5172 0.4929 0.4823 0.1277  0.0616  -0.1439 62  LEU A C   
460  O O   . LEU A 64  ? 0.5640 0.5399 0.5301 0.1346  0.0538  -0.1446 62  LEU A O   
461  C CB  . LEU A 64  ? 0.4957 0.4341 0.4604 0.1143  0.0740  -0.1333 62  LEU A CB  
462  C CG  . LEU A 64  ? 0.4767 0.4041 0.4242 0.1263  0.0604  -0.1397 62  LEU A CG  
463  C CD1 . LEU A 64  ? 0.5515 0.4868 0.4912 0.1242  0.0656  -0.1438 62  LEU A CD1 
464  C CD2 . LEU A 64  ? 0.5206 0.4221 0.4573 0.1283  0.0542  -0.1379 62  LEU A CD2 
465  N N   . SER A 65  ? 0.5291 0.5201 0.4890 0.1341  0.0568  -0.1505 63  SER A N   
466  C CA  . SER A 65  ? 0.5788 0.5902 0.5350 0.1511  0.0416  -0.1587 63  SER A CA  
467  C C   . SER A 65  ? 0.6180 0.6379 0.5621 0.1617  0.0340  -0.1652 63  SER A C   
468  O O   . SER A 65  ? 0.6662 0.6915 0.6109 0.1509  0.0440  -0.1656 63  SER A O   
469  C CB  . SER A 65  ? 0.5629 0.6067 0.5322 0.1468  0.0446  -0.1626 63  SER A CB  
470  O OG  . SER A 65  ? 0.6668 0.7409 0.6342 0.1640  0.0303  -0.1730 63  SER A OG  
471  N N   . SER A 66  ? 0.6610 0.6801 0.5909 0.1854  0.0141  -0.1708 64  SER A N   
472  C CA  . SER A 66  ? 0.6613 0.6904 0.5756 0.2026  0.0017  -0.1780 64  SER A CA  
473  C C   . SER A 66  ? 0.7130 0.7907 0.6424 0.1995  0.0054  -0.1857 64  SER A C   
474  O O   . SER A 66  ? 0.8479 0.9404 0.7701 0.2023  0.0044  -0.1905 64  SER A O   
475  C CB  . SER A 66  ? 0.7196 0.7269 0.6103 0.2334  -0.0248 -0.1817 64  SER A CB  
476  O OG  . SER A 66  ? 0.7467 0.7848 0.6517 0.2416  -0.0309 -0.1879 64  SER A OG  
477  N N   . GLN A 67  ? 0.7463 0.8512 0.6934 0.1945  0.0082  -0.1882 65  GLN A N   
478  C CA  . GLN A 67  ? 0.6626 0.8178 0.6228 0.1913  0.0094  -0.1971 65  GLN A CA  
479  C C   . GLN A 67  ? 0.6753 0.8330 0.6456 0.1639  0.0285  -0.1939 65  GLN A C   
480  O O   . GLN A 67  ? 0.6952 0.8196 0.6663 0.1489  0.0408  -0.1846 65  GLN A O   
481  C CB  . GLN A 67  ? 0.7208 0.9029 0.6898 0.2004  0.0013  -0.2029 65  GLN A CB  
482  C CG  . GLN A 67  ? 0.8545 1.0985 0.8377 0.1984  -0.0002 -0.2145 65  GLN A CG  
483  C CD  . GLN A 67  ? 0.9269 1.1905 0.9128 0.2133  -0.0115 -0.2209 65  GLN A CD  
484  O OE1 . GLN A 67  ? 0.9942 1.2183 0.9700 0.2242  -0.0177 -0.2160 65  GLN A OE1 
485  N NE2 . GLN A 67  ? 0.9955 1.3209 0.9929 0.2150  -0.0158 -0.2331 65  GLN A NE2 
486  N N   . PRO A 68  ? 0.6498 0.8461 0.6257 0.1589  0.0295  -0.2025 66  PRO A N   
487  C CA  . PRO A 68  ? 0.5704 0.7638 0.5497 0.1365  0.0437  -0.2020 66  PRO A CA  
488  C C   . PRO A 68  ? 0.5732 0.7688 0.5626 0.1197  0.0525  -0.2015 66  PRO A C   
489  O O   . PRO A 68  ? 0.6043 0.8218 0.6013 0.1225  0.0484  -0.2042 66  PRO A O   
490  C CB  . PRO A 68  ? 0.4782 0.7185 0.4590 0.1382  0.0384  -0.2140 66  PRO A CB  
491  C CG  . PRO A 68  ? 0.5290 0.7871 0.5030 0.1655  0.0213  -0.2182 66  PRO A CG  
492  C CD  . PRO A 68  ? 0.6368 0.8812 0.6132 0.1763  0.0153  -0.2143 66  PRO A CD  
493  N N   . GLY A 69  ? 0.5467 0.7244 0.5348 0.1033  0.0631  -0.2007 67  GLY A N   
494  C CA  . GLY A 69  ? 0.5062 0.6769 0.4999 0.0893  0.0700  -0.2010 67  GLY A CA  
495  C C   . GLY A 69  ? 0.5222 0.7455 0.5255 0.0784  0.0683  -0.2149 67  GLY A C   
496  O O   . GLY A 69  ? 0.6260 0.8897 0.6313 0.0756  0.0649  -0.2252 67  GLY A O   
497  N N   . THR A 70  ? 0.5133 0.7424 0.5222 0.0703  0.0710  -0.2159 68  THR A N   
498  C CA  . THR A 70  ? 0.4158 0.7017 0.4323 0.0531  0.0714  -0.2301 68  THR A CA  
499  C C   . THR A 70  ? 0.4640 0.7399 0.4788 0.0281  0.0807  -0.2373 68  THR A C   
500  O O   . THR A 70  ? 0.4966 0.8225 0.5136 0.0065  0.0827  -0.2484 68  THR A O   
501  C CB  . THR A 70  ? 0.3875 0.7142 0.4117 0.0633  0.0638  -0.2303 68  THR A CB  
502  O OG1 . THR A 70  ? 0.6550 0.9562 0.6796 0.0622  0.0674  -0.2233 68  THR A OG1 
503  C CG2 . THR A 70  ? 0.4399 0.7626 0.4623 0.0904  0.0529  -0.2252 68  THR A CG2 
504  N N   . ASP A 71  ? 0.4406 0.6574 0.4498 0.0280  0.0857  -0.2324 69  ASP A N   
505  C CA  . ASP A 71  ? 0.4368 0.6340 0.4427 0.0069  0.0925  -0.2413 69  ASP A CA  
506  C C   . ASP A 71  ? 0.4391 0.5743 0.4394 0.0106  0.0941  -0.2395 69  ASP A C   
507  O O   . ASP A 71  ? 0.4952 0.5966 0.4963 0.0309  0.0921  -0.2228 69  ASP A O   
508  C CB  . ASP A 71  ? 0.4518 0.6476 0.4629 0.0112  0.0930  -0.2334 69  ASP A CB  
509  C CG  . ASP A 71  ? 0.4650 0.6531 0.4691 -0.0174 0.1001  -0.2461 69  ASP A CG  
510  O OD1 . ASP A 71  ? 0.5103 0.6421 0.5073 -0.0241 0.1017  -0.2514 69  ASP A OD1 
511  O OD2 . ASP A 71  ? 0.4533 0.6871 0.4557 -0.0339 0.1023  -0.2496 69  ASP A OD2 
512  N N   . ASP A 72  ? 0.4875 0.6058 0.4782 -0.0109 0.0963  -0.2565 70  ASP A N   
513  C CA  . ASP A 72  ? 0.5377 0.6009 0.5240 -0.0020 0.0944  -0.2547 70  ASP A CA  
514  C C   . ASP A 72  ? 0.5802 0.5933 0.5683 0.0037  0.0931  -0.2483 70  ASP A C   
515  O O   . ASP A 72  ? 0.7232 0.7000 0.7091 0.0177  0.0899  -0.2421 70  ASP A O   
516  C CB  . ASP A 72  ? 0.4837 0.5311 0.4560 -0.0238 0.0926  -0.2743 70  ASP A CB  
517  C CG  . ASP A 72  ? 0.6529 0.6709 0.6091 -0.0590 0.0889  -0.2892 70  ASP A CG  
518  O OD1 . ASP A 72  ? 0.7185 0.7347 0.6765 -0.0679 0.0882  -0.2811 70  ASP A OD1 
519  O OD2 . ASP A 72  ? 0.7616 0.7512 0.7004 -0.0810 0.0816  -0.3012 70  ASP A OD2 
520  N N   . ARG A 73  ? 0.4975 0.5120 0.4877 -0.0078 0.0949  -0.2504 71  ARG A N   
521  C CA  . ARG A 73  ? 0.5806 0.5456 0.5728 -0.0036 0.0920  -0.2446 71  ARG A CA  
522  C C   . ARG A 73  ? 0.6364 0.5964 0.6372 0.0261  0.0907  -0.2212 71  ARG A C   
523  O O   . ARG A 73  ? 0.6240 0.5493 0.6266 0.0332  0.0872  -0.2141 71  ARG A O   
524  C CB  . ARG A 73  ? 0.5843 0.5553 0.5731 -0.0283 0.0921  -0.2460 71  ARG A CB  
525  C CG  . ARG A 73  ? 0.6294 0.6007 0.5995 -0.0684 0.0816  -0.2439 71  ARG A CG  
526  C CD  . ARG A 73  ? 0.6337 0.6353 0.5988 -0.0970 0.0767  -0.2275 71  ARG A CD  
527  N NE  . ARG A 73  ? 0.6015 0.6762 0.5802 -0.0821 0.0876  -0.2292 71  ARG A NE  
528  C CZ  . ARG A 73  ? 0.5138 0.6322 0.4929 -0.0973 0.0872  -0.2193 71  ARG A CZ  
529  N NH1 . ARG A 73  ? 0.5937 0.6917 0.5592 -0.1326 0.0766  -0.2034 71  ARG A NH1 
530  N NH2 . ARG A 73  ? 0.4920 0.6744 0.4831 -0.0772 0.0956  -0.2259 71  ARG A NH2 
531  N N   . VAL A 74  ? 0.5323 0.5219 0.5335 0.0401  0.0914  -0.2086 72  VAL A N   
532  C CA  . VAL A 74  ? 0.5657 0.5468 0.5649 0.0587  0.0896  -0.1871 72  VAL A CA  
533  C C   . VAL A 74  ? 0.5781 0.5644 0.5689 0.0681  0.0897  -0.1801 72  VAL A C   
534  O O   . VAL A 74  ? 0.5950 0.6022 0.5849 0.0635  0.0904  -0.1888 72  VAL A O   
535  C CB  . VAL A 74  ? 0.5506 0.5517 0.5536 0.0614  0.0898  -0.1789 72  VAL A CB  
536  C CG1 . VAL A 74  ? 0.4842 0.4829 0.4958 0.0497  0.0916  -0.1873 72  VAL A CG1 
537  C CG2 . VAL A 74  ? 0.5153 0.5547 0.5185 0.0598  0.0898  -0.1839 72  VAL A CG2 
538  N N   . THR A 75  ? 0.5435 0.5139 0.5282 0.0790  0.0898  -0.1662 73  THR A N   
539  C CA  . THR A 75  ? 0.4597 0.4342 0.4367 0.0846  0.0920  -0.1616 73  THR A CA  
540  C C   . THR A 75  ? 0.4775 0.4616 0.4514 0.0887  0.0923  -0.1526 73  THR A C   
541  O O   . THR A 75  ? 0.5193 0.4982 0.4953 0.0917  0.0914  -0.1449 73  THR A O   
542  C CB  . THR A 75  ? 0.4468 0.4082 0.4227 0.0906  0.0935  -0.1575 73  THR A CB  
543  O OG1 . THR A 75  ? 0.5432 0.4894 0.5199 0.0898  0.0922  -0.1665 73  THR A OG1 
544  C CG2 . THR A 75  ? 0.3856 0.3577 0.3575 0.0928  0.0971  -0.1583 73  THR A CG2 
545  N N   . TRP A 76  ? 0.4844 0.4830 0.4552 0.0889  0.0927  -0.1569 74  TRP A N   
546  C CA  . TRP A 76  ? 0.4456 0.4520 0.4145 0.0938  0.0909  -0.1534 74  TRP A CA  
547  C C   . TRP A 76  ? 0.4429 0.4430 0.4042 0.0972  0.0929  -0.1516 74  TRP A C   
548  O O   . TRP A 76  ? 0.4918 0.4978 0.4500 0.0950  0.0952  -0.1573 74  TRP A O   
549  C CB  . TRP A 76  ? 0.3895 0.4266 0.3626 0.0930  0.0864  -0.1643 74  TRP A CB  
550  C CG  . TRP A 76  ? 0.4624 0.5176 0.4442 0.0877  0.0846  -0.1704 74  TRP A CG  
551  C CD1 . TRP A 76  ? 0.4703 0.5316 0.4567 0.0769  0.0866  -0.1803 74  TRP A CD1 
552  C CD2 . TRP A 76  ? 0.4759 0.5507 0.4637 0.0917  0.0800  -0.1710 74  TRP A CD2 
553  N NE1 . TRP A 76  ? 0.5188 0.6053 0.5134 0.0711  0.0851  -0.1872 74  TRP A NE1 
554  C CE2 . TRP A 76  ? 0.4427 0.5404 0.4385 0.0813  0.0809  -0.1809 74  TRP A CE2 
555  C CE3 . TRP A 76  ? 0.4892 0.5667 0.4765 0.1029  0.0741  -0.1673 74  TRP A CE3 
556  C CZ2 . TRP A 76  ? 0.4423 0.5715 0.4454 0.0815  0.0774  -0.1855 74  TRP A CZ2 
557  C CZ3 . TRP A 76  ? 0.4880 0.5919 0.4824 0.1062  0.0688  -0.1720 74  TRP A CZ3 
558  C CH2 . TRP A 76  ? 0.4506 0.5828 0.4529 0.0954  0.0711  -0.1803 74  TRP A CH2 
559  N N   . VAL A 77  ? 0.4669 0.4581 0.4257 0.1017  0.0914  -0.1470 75  VAL A N   
560  C CA  . VAL A 77  ? 0.4379 0.4270 0.3886 0.1042  0.0917  -0.1495 75  VAL A CA  
561  C C   . VAL A 77  ? 0.5234 0.5144 0.4694 0.1139  0.0808  -0.1535 75  VAL A C   
562  O O   . VAL A 77  ? 0.5159 0.5053 0.4675 0.1185  0.0746  -0.1516 75  VAL A O   
563  C CB  . VAL A 77  ? 0.4801 0.4540 0.4289 0.1023  0.0975  -0.1435 75  VAL A CB  
564  C CG1 . VAL A 77  ? 0.4446 0.4208 0.3964 0.0998  0.1021  -0.1423 75  VAL A CG1 
565  C CG2 . VAL A 77  ? 0.4670 0.4247 0.4205 0.1031  0.0960  -0.1359 75  VAL A CG2 
566  N N   . LYS A 78  ? 0.5131 0.5079 0.4438 0.1206  0.0752  -0.1601 76  LYS A N   
567  C CA  . LYS A 78  ? 0.5504 0.5385 0.4647 0.1390  0.0574  -0.1637 76  LYS A CA  
568  C C   . LYS A 78  ? 0.5680 0.5267 0.4576 0.1465  0.0498  -0.1626 76  LYS A C   
569  O O   . LYS A 78  ? 0.5949 0.5279 0.4535 0.1665  0.0300  -0.1639 76  LYS A O   
570  C CB  . LYS A 78  ? 0.4733 0.4813 0.3733 0.1491  0.0492  -0.1719 76  LYS A CB  
571  C CG  . LYS A 78  ? 0.6088 0.6451 0.5280 0.1445  0.0524  -0.1745 76  LYS A CG  
572  C CD  . LYS A 78  ? 0.6248 0.6894 0.5352 0.1519  0.0459  -0.1834 76  LYS A CD  
573  C CE  . LYS A 78  ? 0.8182 0.8825 0.7113 0.1792  0.0244  -0.1874 76  LYS A CE  
574  N NZ  . LYS A 78  ? 1.0279 1.1271 0.9158 0.1872  0.0180  -0.1962 76  LYS A NZ  
575  N N   . SER A 79  ? 0.5001 0.4555 0.3953 0.1334  0.0626  -0.1600 77  SER A N   
576  C CA  . SER A 79  ? 0.4908 0.4240 0.3518 0.1377  0.0580  -0.1610 77  SER A CA  
577  C C   . SER A 79  ? 0.5745 0.5046 0.4547 0.1266  0.0687  -0.1565 77  SER A C   
578  O O   . SER A 79  ? 0.5906 0.5403 0.5036 0.1132  0.0843  -0.1535 77  SER A O   
579  C CB  . SER A 79  ? 0.5847 0.5440 0.4309 0.1236  0.0646  -0.1604 77  SER A CB  
580  O OG  . SER A 79  ? 0.7059 0.6560 0.5352 0.1021  0.0617  -0.1422 77  SER A OG  
581  N N   . VAL A 80  ? 0.5518 0.4465 0.4069 0.1263  0.0573  -0.1470 78  VAL A N   
582  C CA  . VAL A 80  ? 0.5494 0.4469 0.4192 0.1155  0.0675  -0.1433 78  VAL A CA  
583  C C   . VAL A 80  ? 0.5776 0.5203 0.4637 0.1012  0.0867  -0.1474 78  VAL A C   
584  O O   . VAL A 80  ? 0.5887 0.5485 0.5030 0.1016  0.1006  -0.1534 78  VAL A O   
585  C CB  . VAL A 80  ? 0.5528 0.4096 0.3942 0.1025  0.0500  -0.1232 78  VAL A CB  
586  C CG1 . VAL A 80  ? 0.5219 0.3906 0.3786 0.0886  0.0610  -0.1186 78  VAL A CG1 
587  C CG2 . VAL A 80  ? 0.6123 0.4229 0.4397 0.1225  0.0303  -0.1249 78  VAL A CG2 
588  N N   . ASP A 81  ? 0.5596 0.5222 0.4283 0.0874  0.0860  -0.1418 79  ASP A N   
589  C CA  . ASP A 81  ? 0.5679 0.5805 0.4508 0.0755  0.1035  -0.1487 79  ASP A CA  
590  C C   . ASP A 81  ? 0.5356 0.5684 0.4453 0.0880  0.1155  -0.1651 79  ASP A C   
591  O O   . ASP A 81  ? 0.4979 0.5500 0.4274 0.0848  0.1231  -0.1629 79  ASP A O   
592  C CB  . ASP A 81  ? 0.5593 0.5920 0.4129 0.0525  0.0982  -0.1349 79  ASP A CB  
593  C CG  . ASP A 81  ? 0.6799 0.6901 0.5052 0.0287  0.0838  -0.1088 79  ASP A CG  
594  O OD1 . ASP A 81  ? 0.6680 0.6704 0.5040 0.0258  0.0859  -0.1051 79  ASP A OD1 
595  O OD2 . ASP A 81  ? 0.7872 0.7862 0.5769 0.0104  0.0688  -0.0909 79  ASP A OD2 
596  N N   . GLU A 82  ? 0.5204 0.5352 0.4286 0.0953  0.1084  -0.1637 80  GLU A N   
597  C CA  . GLU A 82  ? 0.4738 0.4881 0.4010 0.0957  0.1111  -0.1590 80  GLU A CA  
598  C C   . GLU A 82  ? 0.5300 0.5238 0.4729 0.0987  0.1111  -0.1481 80  GLU A C   
599  O O   . GLU A 82  ? 0.5026 0.5012 0.4557 0.0990  0.1133  -0.1469 80  GLU A O   
600  C CB  . GLU A 82  ? 0.4713 0.4803 0.3929 0.0993  0.1044  -0.1613 80  GLU A CB  
601  C CG  . GLU A 82  ? 0.5021 0.5372 0.4045 0.0976  0.1030  -0.1714 80  GLU A CG  
602  C CD  . GLU A 82  ? 0.4903 0.5244 0.3877 0.1045  0.0939  -0.1742 80  GLU A CD  
603  O OE1 . GLU A 82  ? 0.5639 0.5806 0.4722 0.1102  0.0882  -0.1694 80  GLU A OE1 
604  O OE2 . GLU A 82  ? 0.5829 0.6397 0.4658 0.1036  0.0922  -0.1811 80  GLU A OE2 
605  N N   . ALA A 83  ? 0.4954 0.4670 0.4374 0.1011  0.1071  -0.1419 81  ALA A N   
606  C CA  . ALA A 83  ? 0.4620 0.4200 0.4129 0.1034  0.1060  -0.1312 81  ALA A CA  
607  C C   . ALA A 83  ? 0.4496 0.4210 0.4087 0.1040  0.1091  -0.1313 81  ALA A C   
608  O O   . ALA A 83  ? 0.4907 0.4611 0.4583 0.1064  0.1080  -0.1277 81  ALA A O   
609  C CB  . ALA A 83  ? 0.4924 0.4314 0.4435 0.1025  0.1008  -0.1258 81  ALA A CB  
610  N N   . ILE A 84  ? 0.4696 0.4569 0.4268 0.1004  0.1132  -0.1382 82  ILE A N   
611  C CA  . ILE A 84  ? 0.4819 0.4907 0.4527 0.0987  0.1185  -0.1396 82  ILE A CA  
612  C C   . ILE A 84  ? 0.4724 0.5021 0.4527 0.0993  0.1233  -0.1447 82  ILE A C   
613  O O   . ILE A 84  ? 0.4774 0.5089 0.4702 0.1040  0.1239  -0.1436 82  ILE A O   
614  C CB  . ILE A 84  ? 0.3812 0.4131 0.3461 0.0888  0.1249  -0.1482 82  ILE A CB  
615  C CG1 . ILE A 84  ? 0.4224 0.4209 0.3761 0.0896  0.1184  -0.1470 82  ILE A CG1 
616  C CG2 . ILE A 84  ? 0.3749 0.4397 0.3570 0.0852  0.1324  -0.1495 82  ILE A CG2 
617  C CD1 . ILE A 84  ? 0.5304 0.5277 0.4609 0.0694  0.1135  -0.1357 82  ILE A CD1 
618  N N   . ALA A 85  ? 0.4699 0.5143 0.4429 0.0955  0.1257  -0.1521 83  ALA A N   
619  C CA  . ALA A 85  ? 0.3934 0.4572 0.3738 0.0966  0.1292  -0.1601 83  ALA A CA  
620  C C   . ALA A 85  ? 0.4695 0.5049 0.4537 0.1039  0.1242  -0.1572 83  ALA A C   
621  O O   . ALA A 85  ? 0.5376 0.5792 0.5300 0.1084  0.1259  -0.1646 83  ALA A O   
622  C CB  . ALA A 85  ? 0.4043 0.4914 0.3732 0.0897  0.1317  -0.1686 83  ALA A CB  
623  N N   . ALA A 86  ? 0.4569 0.4648 0.4339 0.1046  0.1179  -0.1487 84  ALA A N   
624  C CA  . ALA A 86  ? 0.4254 0.4162 0.4054 0.1071  0.1131  -0.1500 84  ALA A CA  
625  C C   . ALA A 86  ? 0.4637 0.4458 0.4545 0.1119  0.1109  -0.1492 84  ALA A C   
626  O O   . ALA A 86  ? 0.5188 0.4899 0.5140 0.1143  0.1080  -0.1564 84  ALA A O   
627  C CB  . ALA A 86  ? 0.4572 0.4350 0.4309 0.1043  0.1076  -0.1452 84  ALA A CB  
628  N N   . CYS A 87  ? 0.4935 0.4778 0.4863 0.1134  0.1121  -0.1411 85  CYS A N   
629  C CA  . CYS A 87  ? 0.5156 0.4942 0.5187 0.1185  0.1105  -0.1400 85  CYS A CA  
630  C C   . CYS A 87  ? 0.5166 0.5092 0.5305 0.1249  0.1158  -0.1508 85  CYS A C   
631  O O   . CYS A 87  ? 0.5696 0.5520 0.5918 0.1318  0.1135  -0.1537 85  CYS A O   
632  C CB  . CYS A 87  ? 0.5806 0.5612 0.5824 0.1180  0.1104  -0.1292 85  CYS A CB  
633  S SG  . CYS A 87  ? 0.4879 0.4510 0.4775 0.1140  0.1021  -0.1199 85  CYS A SG  
634  N N   . GLY A 88  ? 0.4481 0.4653 0.4619 0.1234  0.1223  -0.1580 86  GLY A N   
635  C CA  . GLY A 88  ? 0.4576 0.4940 0.4833 0.1310  0.1260  -0.1717 86  GLY A CA  
636  C C   . GLY A 88  ? 0.6407 0.6994 0.6803 0.1350  0.1297  -0.1708 86  GLY A C   
637  O O   . GLY A 88  ? 0.7634 0.8309 0.8038 0.1288  0.1309  -0.1620 86  GLY A O   
638  N N   . ASP A 89  ? 0.6631 0.7340 0.7156 0.1464  0.1302  -0.1833 87  ASP A N   
639  C CA  . ASP A 89  ? 0.7240 0.8282 0.7944 0.1523  0.1326  -0.1875 87  ASP A CA  
640  C C   . ASP A 89  ? 0.7013 0.7756 0.7771 0.1591  0.1280  -0.1785 87  ASP A C   
641  O O   . ASP A 89  ? 0.7187 0.7799 0.8025 0.1724  0.1239  -0.1866 87  ASP A O   
642  C CB  . ASP A 89  ? 0.7374 0.8772 0.8199 0.1641  0.1335  -0.2082 87  ASP A CB  
643  C CG  . ASP A 89  ? 0.8237 1.0210 0.9229 0.1662  0.1365  -0.2143 87  ASP A CG  
644  O OD1 . ASP A 89  ? 0.8984 1.1072 0.9983 0.1553  0.1391  -0.2021 87  ASP A OD1 
645  O OD2 . ASP A 89  ? 0.7736 1.0081 0.8844 0.1787  0.1355  -0.2324 87  ASP A OD2 
646  N N   . VAL A 90  ? 0.7008 0.7665 0.7726 0.1505  0.1277  -0.1636 88  VAL A N   
647  C CA  . VAL A 90  ? 0.5875 0.6292 0.6629 0.1547  0.1231  -0.1540 88  VAL A CA  
648  C C   . VAL A 90  ? 0.6478 0.7220 0.7350 0.1501  0.1265  -0.1501 88  VAL A C   
649  O O   . VAL A 90  ? 0.7256 0.8280 0.8102 0.1393  0.1314  -0.1509 88  VAL A O   
650  C CB  . VAL A 90  ? 0.6571 0.6564 0.7127 0.1487  0.1166  -0.1415 88  VAL A CB  
651  C CG1 . VAL A 90  ? 0.6742 0.6501 0.7238 0.1515  0.1120  -0.1508 88  VAL A CG1 
652  C CG2 . VAL A 90  ? 0.6313 0.6356 0.6748 0.1369  0.1169  -0.1338 88  VAL A CG2 
653  N N   . PRO A 91  ? 0.5893 0.6630 0.6894 0.1569  0.1238  -0.1471 89  PRO A N   
654  C CA  . PRO A 91  ? 0.5749 0.6844 0.6874 0.1512  0.1271  -0.1447 89  PRO A CA  
655  C C   . PRO A 91  ? 0.6516 0.7450 0.7505 0.1382  0.1265  -0.1336 89  PRO A C   
656  O O   . PRO A 91  ? 0.7323 0.8589 0.8344 0.1270  0.1318  -0.1352 89  PRO A O   
657  C CB  . PRO A 91  ? 0.4796 0.5867 0.6090 0.1640  0.1224  -0.1444 89  PRO A CB  
658  C CG  . PRO A 91  ? 0.4743 0.5594 0.6045 0.1781  0.1181  -0.1530 89  PRO A CG  
659  C CD  . PRO A 91  ? 0.5403 0.5885 0.6471 0.1705  0.1178  -0.1490 89  PRO A CD  
660  N N   . GLU A 92  ? 0.5694 0.6174 0.6517 0.1384  0.1189  -0.1245 90  GLU A N   
661  C CA  . GLU A 92  ? 0.5737 0.6071 0.6442 0.1291  0.1143  -0.1172 90  GLU A CA  
662  C C   . GLU A 92  ? 0.5782 0.5790 0.6271 0.1270  0.1062  -0.1130 90  GLU A C   
663  O O   . GLU A 92  ? 0.5190 0.4990 0.5623 0.1323  0.1011  -0.1118 90  GLU A O   
664  C CB  . GLU A 92  ? 0.5196 0.5472 0.5988 0.1309  0.1093  -0.1122 90  GLU A CB  
665  C CG  . GLU A 92  ? 0.4907 0.5011 0.5602 0.1208  0.1034  -0.1081 90  GLU A CG  
666  C CD  . GLU A 92  ? 0.5173 0.5255 0.5987 0.1205  0.1003  -0.1047 90  GLU A CD  
667  O OE1 . GLU A 92  ? 0.4991 0.5036 0.5879 0.1303  0.0968  -0.1031 90  GLU A OE1 
668  O OE2 . GLU A 92  ? 0.5673 0.5722 0.6498 0.1105  0.1020  -0.1042 90  GLU A OE2 
669  N N   . ILE A 93  ? 0.5180 0.5167 0.5565 0.1187  0.1053  -0.1127 91  ILE A N   
670  C CA  . ILE A 93  ? 0.5231 0.4999 0.5439 0.1168  0.0977  -0.1096 91  ILE A CA  
671  C C   . ILE A 93  ? 0.5058 0.4688 0.5222 0.1129  0.0893  -0.1056 91  ILE A C   
672  O O   . ILE A 93  ? 0.5643 0.5306 0.5854 0.1079  0.0918  -0.1076 91  ILE A O   
673  C CB  . ILE A 93  ? 0.5099 0.4940 0.5228 0.1128  0.1032  -0.1144 91  ILE A CB  
674  C CG1 . ILE A 93  ? 0.5124 0.5102 0.5294 0.1156  0.1106  -0.1199 91  ILE A CG1 
675  C CG2 . ILE A 93  ? 0.4957 0.4596 0.4919 0.1114  0.0953  -0.1111 91  ILE A CG2 
676  C CD1 . ILE A 93  ? 0.5762 0.5982 0.5924 0.1089  0.1192  -0.1283 91  ILE A CD1 
677  N N   . MET A 94  ? 0.4930 0.4420 0.5024 0.1124  0.0812  -0.1013 92  MET A N   
678  C CA  . MET A 94  ? 0.4804 0.4209 0.4871 0.1090  0.0749  -0.0984 92  MET A CA  
679  C C   . MET A 94  ? 0.5001 0.4325 0.4909 0.1077  0.0709  -0.0965 92  MET A C   
680  O O   . MET A 94  ? 0.5317 0.4629 0.5206 0.1072  0.0727  -0.0974 92  MET A O   
681  C CB  . MET A 94  ? 0.4425 0.3783 0.4558 0.1090  0.0725  -0.0971 92  MET A CB  
682  C CG  . MET A 94  ? 0.4841 0.4238 0.5129 0.1121  0.0752  -0.0977 92  MET A CG  
683  S SD  . MET A 94  ? 0.4600 0.4095 0.5002 0.1093  0.0789  -0.0970 92  MET A SD  
684  C CE  . MET A 94  ? 0.4138 0.3517 0.4508 0.1035  0.0737  -0.0942 92  MET A CE  
685  N N   . VAL A 95  ? 0.4248 0.3493 0.4082 0.1073  0.0681  -0.0976 93  VAL A N   
686  C CA  . VAL A 95  ? 0.4529 0.3607 0.4176 0.1077  0.0679  -0.0931 93  VAL A CA  
687  C C   . VAL A 95  ? 0.5137 0.4134 0.4767 0.1047  0.0704  -0.0884 93  VAL A C   
688  O O   . VAL A 95  ? 0.5560 0.4508 0.5189 0.1052  0.0663  -0.0900 93  VAL A O   
689  C CB  . VAL A 95  ? 0.4308 0.3195 0.3851 0.1071  0.0695  -0.0969 93  VAL A CB  
690  C CG1 . VAL A 95  ? 0.4321 0.3189 0.4204 0.0891  0.0797  -0.1080 93  VAL A CG1 
691  C CG2 . VAL A 95  ? 0.4117 0.3172 0.3722 0.1094  0.0685  -0.1073 93  VAL A CG2 
692  N N   . ILE A 96  ? 0.4441 0.3501 0.4149 0.1018  0.0764  -0.0910 94  ILE A N   
693  C CA  . ILE A 96  ? 0.4491 0.3619 0.4254 0.1007  0.0770  -0.0932 94  ILE A CA  
694  C C   . ILE A 96  ? 0.5003 0.4173 0.4837 0.0992  0.0800  -0.1030 94  ILE A C   
695  O O   . ILE A 96  ? 0.6337 0.5605 0.6191 0.1005  0.0798  -0.1075 94  ILE A O   
696  C CB  . ILE A 96  ? 0.4661 0.3943 0.4490 0.1015  0.0757  -0.0963 94  ILE A CB  
697  C CG1 . ILE A 96  ? 0.4618 0.3977 0.4462 0.1006  0.0800  -0.1019 94  ILE A CG1 
698  C CG2 . ILE A 96  ? 0.5227 0.4523 0.5130 0.1025  0.0709  -0.0959 94  ILE A CG2 
699  C CD1 . ILE A 96  ? 0.4342 0.3845 0.4253 0.0977  0.0814  -0.1085 94  ILE A CD1 
700  N N   . GLY A 97  ? 0.4875 0.4025 0.4727 0.1012  0.0785  -0.1099 95  GLY A N   
701  C CA  . GLY A 97  ? 0.5395 0.4678 0.5250 0.1089  0.0701  -0.1207 95  GLY A CA  
702  C C   . GLY A 97  ? 0.5241 0.4572 0.5061 0.1174  0.0611  -0.1276 95  GLY A C   
703  O O   . GLY A 97  ? 0.5182 0.4514 0.5005 0.1157  0.0643  -0.1262 95  GLY A O   
704  N N   . GLY A 98  ? 0.6700 0.6096 0.6463 0.1293  0.0486  -0.1361 96  GLY A N   
705  C CA  . GLY A 98  ? 0.6180 0.5490 0.5832 0.1430  0.0345  -0.1418 96  GLY A CA  
706  C C   . GLY A 98  ? 0.6168 0.5139 0.5696 0.1459  0.0258  -0.1405 96  GLY A C   
707  O O   . GLY A 98  ? 0.6782 0.5540 0.6310 0.1350  0.0317  -0.1335 96  GLY A O   
708  N N   . GLY A 99  ? 0.6039 0.4969 0.5450 0.1615  0.0101  -0.1489 97  GLY A N   
709  C CA  . GLY A 99  ? 0.6521 0.5032 0.5724 0.1682  -0.0049 -0.1488 97  GLY A CA  
710  C C   . GLY A 99  ? 0.6499 0.4718 0.5539 0.1713  -0.0136 -0.1445 97  GLY A C   
711  O O   . GLY A 99  ? 0.6587 0.4447 0.5478 0.1646  -0.0176 -0.1382 97  GLY A O   
712  N N   . ARG A 100 ? 0.6476 0.4845 0.5511 0.1814  -0.0176 -0.1481 98  ARG A N   
713  C CA  . ARG A 100 ? 0.7311 0.5400 0.6153 0.1858  -0.0268 -0.1445 98  ARG A CA  
714  C C   . ARG A 100 ? 0.7079 0.5183 0.6021 0.1665  -0.0088 -0.1367 98  ARG A C   
715  O O   . ARG A 100 ? 0.7255 0.4970 0.5952 0.1652  -0.0170 -0.1319 98  ARG A O   
716  C CB  . ARG A 100 ? 0.6593 0.4899 0.5427 0.2013  -0.0339 -0.1513 98  ARG A CB  
717  C CG  . ARG A 100 ? 0.8099 0.6081 0.6666 0.2104  -0.0477 -0.1488 98  ARG A CG  
718  C CD  . ARG A 100 ? 0.9673 0.6953 0.7835 0.2129  -0.0686 -0.1418 98  ARG A CD  
719  N NE  . ARG A 100 ? 1.0762 0.7652 0.8592 0.2186  -0.0826 -0.1372 98  ARG A NE  
720  C CZ  . ARG A 100 ? 1.1338 0.7510 0.8719 0.2133  -0.1018 -0.1267 98  ARG A CZ  
721  N NH1 . ARG A 100 ? 1.2364 0.8141 0.9391 0.2161  -0.1153 -0.1211 98  ARG A NH1 
722  N NH2 . ARG A 100 ? 1.0691 0.6491 0.7929 0.2019  -0.1092 -0.1202 98  ARG A NH2 
723  N N   . VAL A 101 ? 0.6608 0.5101 0.5853 0.1517  0.0135  -0.1352 99  VAL A N   
724  C CA  . VAL A 101 ? 0.5816 0.4357 0.5174 0.1359  0.0297  -0.1303 99  VAL A CA  
725  C C   . VAL A 101 ? 0.6285 0.4574 0.5568 0.1292  0.0287  -0.1267 99  VAL A C   
726  O O   . VAL A 101 ? 0.6205 0.4387 0.5414 0.1238  0.0324  -0.1251 99  VAL A O   
727  C CB  . VAL A 101 ? 0.5160 0.4044 0.4777 0.1232  0.0495  -0.1279 99  VAL A CB  
728  C CG1 . VAL A 101 ? 0.5233 0.4132 0.4959 0.1093  0.0650  -0.1230 99  VAL A CG1 
729  C CG2 . VAL A 101 ? 0.5349 0.4435 0.4980 0.1280  0.0497  -0.1313 99  VAL A CG2 
730  N N   . TYR A 102 ? 0.5668 0.3864 0.4930 0.1306  0.0228  -0.1268 100 TYR A N   
731  C CA  . TYR A 102 ? 0.5620 0.3564 0.4785 0.1240  0.0203  -0.1237 100 TYR A CA  
732  C C   . TYR A 102 ? 0.6196 0.3555 0.4916 0.1279  -0.0002 -0.1201 100 TYR A C   
733  O O   . TYR A 102 ? 0.6701 0.3809 0.5231 0.1183  0.0016  -0.1156 100 TYR A O   
734  C CB  . TYR A 102 ? 0.6535 0.4502 0.5743 0.1253  0.0174  -0.1258 100 TYR A CB  
735  C CG  . TYR A 102 ? 0.5895 0.4243 0.5388 0.1169  0.0356  -0.1255 100 TYR A CG  
736  C CD1 . TYR A 102 ? 0.5645 0.4167 0.5331 0.1051  0.0523  -0.1208 100 TYR A CD1 
737  C CD2 . TYR A 102 ? 0.5278 0.3755 0.4784 0.1225  0.0335  -0.1299 100 TYR A CD2 
738  C CE1 . TYR A 102 ? 0.5361 0.4079 0.5172 0.0991  0.0650  -0.1161 100 TYR A CE1 
739  C CE2 . TYR A 102 ? 0.5277 0.4007 0.4930 0.1155  0.0470  -0.1279 100 TYR A CE2 
740  C CZ  . TYR A 102 ? 0.5632 0.4435 0.5408 0.1042  0.0622  -0.1197 100 TYR A CZ  
741  O OH  . TYR A 102 ? 0.5158 0.4114 0.4972 0.1014  0.0706  -0.1156 100 TYR A OH  
742  N N   . GLU A 103 ? 0.6645 0.3694 0.5114 0.1403  -0.0218 -0.1211 101 GLU A N   
743  C CA  . GLU A 103 ? 0.7717 0.4141 0.5703 0.1432  -0.0452 -0.1150 101 GLU A CA  
744  C C   . GLU A 103 ? 0.7411 0.3748 0.5251 0.1371  -0.0389 -0.1115 101 GLU A C   
745  O O   . GLU A 103 ? 0.7632 0.3418 0.5046 0.1204  -0.0496 -0.1007 101 GLU A O   
746  C CB  . GLU A 103 ? 0.7702 0.3974 0.5538 0.1630  -0.0673 -0.1193 101 GLU A CB  
747  C CG  . GLU A 103 ? 0.9562 0.5453 0.7191 0.1637  -0.0859 -0.1186 101 GLU A CG  
748  C CD  . GLU A 103 ? 1.2877 0.8753 1.0440 0.1872  -0.1046 -0.1286 101 GLU A CD  
749  O OE1 . GLU A 103 ? 1.2329 0.8717 1.0154 0.2018  -0.0954 -0.1382 101 GLU A OE1 
750  O OE2 . GLU A 103 ? 1.4969 1.0227 1.2131 0.1890  -0.1323 -0.1247 101 GLU A OE2 
751  N N   . GLN A 104 ? 0.7516 0.4365 0.5648 0.1438  -0.0228 -0.1182 102 GLN A N   
752  C CA  . GLN A 104 ? 0.6791 0.3528 0.4705 0.1399  -0.0175 -0.1176 102 GLN A CA  
753  C C   . GLN A 104 ? 0.6680 0.3712 0.4742 0.1129  0.0024  -0.1080 102 GLN A C   
754  O O   . GLN A 104 ? 0.6463 0.3574 0.4389 0.0892  0.0028  -0.0928 102 GLN A O   
755  C CB  . GLN A 104 ? 0.6378 0.3678 0.4611 0.1484  -0.0048 -0.1252 102 GLN A CB  
756  C CG  . GLN A 104 ? 0.7380 0.4540 0.5471 0.1665  -0.0255 -0.1269 102 GLN A CG  
757  C CD  . GLN A 104 ? 0.7524 0.5188 0.5861 0.1720  -0.0145 -0.1338 102 GLN A CD  
758  O OE1 . GLN A 104 ? 0.7006 0.5154 0.5726 0.1682  -0.0014 -0.1371 102 GLN A OE1 
759  N NE2 . GLN A 104 ? 0.8686 0.6167 0.6728 0.1784  -0.0209 -0.1354 102 GLN A NE2 
760  N N   . PHE A 105 ? 0.6473 0.3736 0.4820 0.1141  0.0174  -0.1148 103 PHE A N   
761  C CA  . PHE A 105 ? 0.5885 0.3550 0.4457 0.0940  0.0367  -0.1083 103 PHE A CA  
762  C C   . PHE A 105 ? 0.6213 0.3747 0.4701 0.0736  0.0320  -0.0952 103 PHE A C   
763  O O   . PHE A 105 ? 0.6323 0.4236 0.4965 0.0559  0.0455  -0.0885 103 PHE A O   
764  C CB  . PHE A 105 ? 0.5956 0.4046 0.4944 0.1074  0.0573  -0.1236 103 PHE A CB  
765  C CG  . PHE A 105 ? 0.5536 0.4017 0.4746 0.1079  0.0659  -0.1292 103 PHE A CG  
766  C CD1 . PHE A 105 ? 0.5556 0.4124 0.4883 0.1113  0.0606  -0.1300 103 PHE A CD1 
767  C CD2 . PHE A 105 ? 0.4808 0.3556 0.4063 0.1038  0.0819  -0.1327 103 PHE A CD2 
768  C CE1 . PHE A 105 ? 0.5627 0.4443 0.5068 0.1089  0.0699  -0.1329 103 PHE A CE1 
769  C CE2 . PHE A 105 ? 0.5365 0.4427 0.4807 0.1014  0.0885  -0.1385 103 PHE A CE2 
770  C CZ  . PHE A 105 ? 0.5799 0.4809 0.5283 0.1030  0.0839  -0.1360 103 PHE A CZ  
771  N N   . LEU A 106 ? 0.6538 0.3582 0.4790 0.0765  0.0129  -0.0931 104 LEU A N   
772  C CA  . LEU A 106 ? 0.6395 0.3304 0.4536 0.0533  0.0071  -0.0798 104 LEU A CA  
773  C C   . LEU A 106 ? 0.7014 0.3994 0.4943 0.0182  0.0035  -0.0585 104 LEU A C   
774  O O   . LEU A 106 ? 0.7197 0.4561 0.5273 -0.0021 0.0151  -0.0508 104 LEU A O   
775  C CB  . LEU A 106 ? 0.6898 0.3190 0.4750 0.0623  -0.0166 -0.0829 104 LEU A CB  
776  C CG  . LEU A 106 ? 0.7321 0.3460 0.5077 0.0409  -0.0228 -0.0732 104 LEU A CG  
777  C CD1 . LEU A 106 ? 0.7211 0.3833 0.5378 0.0466  -0.0015 -0.0816 104 LEU A CD1 
778  C CD2 . LEU A 106 ? 0.8047 0.3450 0.5411 0.0484  -0.0520 -0.0769 104 LEU A CD2 
779  N N   . PRO A 107 ? 0.7320 0.4018 0.4913 0.0088  -0.0120 -0.0481 105 PRO A N   
780  C CA  . PRO A 107 ? 0.6656 0.3522 0.4035 -0.0303 -0.0146 -0.0260 105 PRO A CA  
781  C C   . PRO A 107 ? 0.6967 0.4665 0.4703 -0.0379 0.0132  -0.0294 105 PRO A C   
782  O O   . PRO A 107 ? 0.7955 0.5981 0.5580 -0.0715 0.0149  -0.0135 105 PRO A O   
783  C CB  . PRO A 107 ? 0.7135 0.3564 0.4122 -0.0320 -0.0357 -0.0171 105 PRO A CB  
784  C CG  . PRO A 107 ? 0.7349 0.3178 0.4233 0.0021  -0.0533 -0.0310 105 PRO A CG  
785  C CD  . PRO A 107 ? 0.7338 0.3601 0.4714 0.0314  -0.0292 -0.0545 105 PRO A CD  
786  N N   . LYS A 108 ? 0.6625 0.4692 0.4764 -0.0092 0.0336  -0.0499 106 LYS A N   
787  C CA  . LYS A 108 ? 0.6604 0.5400 0.5058 -0.0123 0.0570  -0.0565 106 LYS A CA  
788  C C   . LYS A 108 ? 0.6703 0.5835 0.5554 -0.0001 0.0730  -0.0676 106 LYS A C   
789  O O   . LYS A 108 ? 0.6349 0.6023 0.5507 0.0078  0.0911  -0.0789 106 LYS A O   
790  C CB  . LYS A 108 ? 0.6267 0.5229 0.4824 0.0066  0.0657  -0.0704 106 LYS A CB  
791  C CG  . LYS A 108 ? 0.6775 0.5503 0.4937 -0.0085 0.0499  -0.0570 106 LYS A CG  
792  C CD  . LYS A 108 ? 0.6676 0.5611 0.4916 0.0072  0.0578  -0.0698 106 LYS A CD  
793  C CE  . LYS A 108 ? 0.7602 0.7281 0.6065 -0.0022 0.0792  -0.0770 106 LYS A CE  
794  N NZ  . LYS A 108 ? 0.6843 0.6821 0.5040 -0.0389 0.0752  -0.0581 106 LYS A NZ  
795  N N   . ALA A 109 ? 0.6651 0.5460 0.5482 0.0017  0.0648  -0.0648 107 ALA A N   
796  C CA  . ALA A 109 ? 0.6418 0.5445 0.5594 0.0157  0.0765  -0.0742 107 ALA A CA  
797  C C   . ALA A 109 ? 0.6324 0.5576 0.5501 -0.0078 0.0755  -0.0615 107 ALA A C   
798  O O   . ALA A 109 ? 0.6317 0.5279 0.5164 -0.0328 0.0599  -0.0456 107 ALA A O   
799  C CB  . ALA A 109 ? 0.5965 0.4549 0.5142 0.0366  0.0692  -0.0828 107 ALA A CB  
800  N N   . GLN A 110 ? 0.5994 0.5740 0.5528 0.0003  0.0902  -0.0685 108 GLN A N   
801  C CA  . GLN A 110 ? 0.5899 0.5953 0.5489 -0.0186 0.0901  -0.0583 108 GLN A CA  
802  C C   . GLN A 110 ? 0.5984 0.5909 0.5752 -0.0054 0.0896  -0.0618 108 GLN A C   
803  O O   . GLN A 110 ? 0.6736 0.6790 0.6482 -0.0229 0.0854  -0.0516 108 GLN A O   
804  C CB  . GLN A 110 ? 0.7086 0.7930 0.6939 -0.0207 0.1050  -0.0629 108 GLN A CB  
805  C CG  . GLN A 110 ? 0.8729 0.9895 0.8397 -0.0416 0.1067  -0.0575 108 GLN A CG  
806  C CD  . GLN A 110 ? 0.8633 0.9769 0.8357 -0.0205 0.1140  -0.0724 108 GLN A CD  
807  O OE1 . GLN A 110 ? 0.9104 1.0565 0.9150 0.0050  0.1270  -0.0909 108 GLN A OE1 
808  N NE2 . GLN A 110 ? 0.8898 0.9610 0.8290 -0.0307 0.1035  -0.0645 108 GLN A NE2 
809  N N   . LYS A 111 ? 0.5916 0.5622 0.5841 0.0217  0.0931  -0.0747 109 LYS A N   
810  C CA  . LYS A 111 ? 0.5078 0.4719 0.5176 0.0330  0.0931  -0.0774 109 LYS A CA  
811  C C   . LYS A 111 ? 0.5560 0.4707 0.5530 0.0459  0.0858  -0.0840 109 LYS A C   
812  O O   . LYS A 111 ? 0.5237 0.4226 0.5154 0.0580  0.0865  -0.0925 109 LYS A O   
813  C CB  . LYS A 111 ? 0.5112 0.5129 0.5586 0.0529  0.1053  -0.0872 109 LYS A CB  
814  C CG  . LYS A 111 ? 0.4740 0.4900 0.5398 0.0550  0.1043  -0.0831 109 LYS A CG  
815  C CD  . LYS A 111 ? 0.4753 0.5263 0.5748 0.0749  0.1121  -0.0915 109 LYS A CD  
816  C CE  . LYS A 111 ? 0.4601 0.5204 0.5757 0.0779  0.1080  -0.0854 109 LYS A CE  
817  N NZ  . LYS A 111 ? 0.5087 0.5811 0.6524 0.1019  0.1099  -0.0937 109 LYS A NZ  
818  N N   . LEU A 112 ? 0.5664 0.4640 0.5596 0.0439  0.0790  -0.0816 110 LEU A N   
819  C CA  . LEU A 112 ? 0.5539 0.4159 0.5358 0.0565  0.0719  -0.0902 110 LEU A CA  
820  C C   . LEU A 112 ? 0.5487 0.4267 0.5530 0.0641  0.0765  -0.0927 110 LEU A C   
821  O O   . LEU A 112 ? 0.5306 0.4252 0.5427 0.0535  0.0761  -0.0841 110 LEU A O   
822  C CB  . LEU A 112 ? 0.6102 0.4297 0.5562 0.0447  0.0547  -0.0862 110 LEU A CB  
823  C CG  . LEU A 112 ? 0.6487 0.4330 0.5628 0.0400  0.0431  -0.0842 110 LEU A CG  
824  C CD1 . LEU A 112 ? 0.6653 0.3941 0.5413 0.0341  0.0213  -0.0836 110 LEU A CD1 
825  C CD2 . LEU A 112 ? 0.6539 0.4377 0.5742 0.0615  0.0480  -0.0962 110 LEU A CD2 
826  N N   . TYR A 113 ? 0.5334 0.4100 0.5470 0.0799  0.0802  -0.1031 111 TYR A N   
827  C CA  . TYR A 113 ? 0.5120 0.4033 0.5392 0.0826  0.0797  -0.1015 111 TYR A CA  
828  C C   . TYR A 113 ? 0.5487 0.4283 0.5555 0.0870  0.0682  -0.1070 111 TYR A C   
829  O O   . TYR A 113 ? 0.5615 0.4461 0.5564 0.0951  0.0620  -0.1068 111 TYR A O   
830  C CB  . TYR A 113 ? 0.4851 0.3998 0.5267 0.0877  0.0793  -0.0963 111 TYR A CB  
831  C CG  . TYR A 113 ? 0.4602 0.3915 0.5206 0.0892  0.0865  -0.0937 111 TYR A CG  
832  C CD1 . TYR A 113 ? 0.4929 0.4286 0.5487 0.0907  0.0884  -0.0960 111 TYR A CD1 
833  C CD2 . TYR A 113 ? 0.4213 0.3668 0.5045 0.0918  0.0904  -0.0902 111 TYR A CD2 
834  C CE1 . TYR A 113 ? 0.4927 0.4513 0.5651 0.0947  0.0949  -0.0967 111 TYR A CE1 
835  C CE2 . TYR A 113 ? 0.4582 0.4239 0.5576 0.0984  0.0940  -0.0903 111 TYR A CE2 
836  C CZ  . TYR A 113 ? 0.4629 0.4373 0.5560 0.0999  0.0965  -0.0944 111 TYR A CZ  
837  O OH  . TYR A 113 ? 0.4128 0.4135 0.5201 0.1082  0.1001  -0.0972 111 TYR A OH  
838  N N   . LEU A 114 ? 0.4961 0.3612 0.4964 0.0824  0.0675  -0.1120 112 LEU A N   
839  C CA  . LEU A 114 ? 0.5072 0.3611 0.4851 0.0891  0.0569  -0.1207 112 LEU A CA  
840  C C   . LEU A 114 ? 0.5373 0.4153 0.5282 0.0873  0.0607  -0.1247 112 LEU A C   
841  O O   . LEU A 114 ? 0.5455 0.4356 0.5478 0.0754  0.0626  -0.1137 112 LEU A O   
842  C CB  . LEU A 114 ? 0.5294 0.3453 0.4816 0.0840  0.0446  -0.1257 112 LEU A CB  
843  C CG  . LEU A 114 ? 0.6008 0.3860 0.5347 0.0811  0.0381  -0.1215 112 LEU A CG  
844  C CD1 . LEU A 114 ? 0.5801 0.3200 0.4784 0.0715  0.0192  -0.1207 112 LEU A CD1 
845  C CD2 . LEU A 114 ? 0.5888 0.3903 0.5358 0.0882  0.0405  -0.1242 112 LEU A CD2 
846  N N   . THR A 115 ? 0.5182 0.4090 0.4998 0.0928  0.0595  -0.1287 113 THR A N   
847  C CA  . THR A 115 ? 0.4908 0.4075 0.4780 0.0914  0.0596  -0.1384 113 THR A CA  
848  C C   . THR A 115 ? 0.5381 0.4451 0.5017 0.0965  0.0495  -0.1498 113 THR A C   
849  O O   . THR A 115 ? 0.5502 0.4587 0.5066 0.1023  0.0470  -0.1520 113 THR A O   
850  C CB  . THR A 115 ? 0.4769 0.4277 0.4776 0.0905  0.0667  -0.1379 113 THR A CB  
851  O OG1 . THR A 115 ? 0.4714 0.4237 0.4947 0.0850  0.0745  -0.1279 113 THR A OG1 
852  C CG2 . THR A 115 ? 0.4688 0.4537 0.4716 0.0848  0.0671  -0.1472 113 THR A CG2 
853  N N   . HIS A 116 ? 0.5493 0.4479 0.5036 0.0940  0.0425  -0.1587 114 HIS A N   
854  C CA  . HIS A 116 ? 0.6011 0.4876 0.5318 0.0989  0.0306  -0.1707 114 HIS A CA  
855  C C   . HIS A 116 ? 0.5844 0.5184 0.5198 0.1007  0.0337  -0.1817 114 HIS A C   
856  O O   . HIS A 116 ? 0.5546 0.5128 0.4975 0.0897  0.0375  -0.1808 114 HIS A O   
857  C CB  . HIS A 116 ? 0.6677 0.5177 0.5795 0.0915  0.0190  -0.1735 114 HIS A CB  
858  C CG  . HIS A 116 ? 0.6401 0.4437 0.5399 0.0855  0.0124  -0.1625 114 HIS A CG  
859  N ND1 . HIS A 116 ? 0.7465 0.5172 0.6284 0.0909  0.0014  -0.1646 114 HIS A ND1 
860  C CD2 . HIS A 116 ? 0.5714 0.3722 0.4810 0.0661  0.0169  -0.1401 114 HIS A CD2 
861  C CE1 . HIS A 116 ? 0.7212 0.4536 0.5901 0.0813  -0.0046 -0.1545 114 HIS A CE1 
862  N NE2 . HIS A 116 ? 0.6654 0.4218 0.5530 0.0643  0.0065  -0.1381 114 HIS A NE2 
863  N N   . ILE A 117 ? 0.6034 0.5568 0.5364 0.1097  0.0316  -0.1876 115 ILE A N   
864  C CA  . ILE A 117 ? 0.6667 0.6744 0.6044 0.1103  0.0340  -0.1987 115 ILE A CA  
865  C C   . ILE A 117 ? 0.6725 0.6767 0.5925 0.1200  0.0216  -0.2145 115 ILE A C   
866  O O   . ILE A 117 ? 0.6371 0.6084 0.5461 0.1316  0.0112  -0.2177 115 ILE A O   
867  C CB  . ILE A 117 ? 0.6353 0.6784 0.5865 0.1126  0.0396  -0.1965 115 ILE A CB  
868  C CG1 . ILE A 117 ? 0.5551 0.5859 0.5201 0.1052  0.0493  -0.1808 115 ILE A CG1 
869  C CG2 . ILE A 117 ? 0.5605 0.6699 0.5185 0.1062  0.0439  -0.2061 115 ILE A CG2 
870  C CD1 . ILE A 117 ? 0.5205 0.5715 0.4934 0.1074  0.0520  -0.1787 115 ILE A CD1 
871  N N   . ASP A 118 ? 0.6644 0.7038 0.5815 0.1145  0.0221  -0.2249 116 ASP A N   
872  C CA  . ASP A 118 ? 0.7522 0.7904 0.6526 0.1235  0.0103  -0.2417 116 ASP A CA  
873  C C   . ASP A 118 ? 0.7831 0.8737 0.6926 0.1358  0.0087  -0.2535 116 ASP A C   
874  O O   . ASP A 118 ? 0.7858 0.9367 0.7014 0.1306  0.0124  -0.2623 116 ASP A O   
875  C CB  . ASP A 118 ? 0.7397 0.7943 0.6317 0.1098  0.0110  -0.2475 116 ASP A CB  
876  C CG  . ASP A 118 ? 0.9288 0.9266 0.8078 0.0999  0.0062  -0.2410 116 ASP A CG  
877  O OD1 . ASP A 118 ? 0.9858 0.9251 0.8457 0.1058  -0.0069 -0.2426 116 ASP A OD1 
878  O OD2 . ASP A 118 ? 0.8404 0.8530 0.7319 0.0807  0.0146  -0.2257 116 ASP A OD2 
879  N N   . ALA A 119 ? 0.7794 0.8512 0.6904 0.1508  0.0026  -0.2535 117 ALA A N   
880  C CA  . ALA A 119 ? 0.7049 0.8264 0.6265 0.1647  -0.0012 -0.2656 117 ALA A CA  
881  C C   . ALA A 119 ? 0.8235 0.9081 0.7363 0.1866  -0.0158 -0.2719 117 ALA A C   
882  O O   . ALA A 119 ? 0.8871 0.9181 0.7933 0.1857  -0.0179 -0.2595 117 ALA A O   
883  C CB  . ALA A 119 ? 0.6717 0.8376 0.6129 0.1542  0.0106  -0.2559 117 ALA A CB  
884  N N   . GLU A 120 ? 0.8962 1.0161 0.8099 0.2062  -0.0268 -0.2923 118 GLU A N   
885  C CA  . GLU A 120 ? 0.8961 0.9973 0.8035 0.2313  -0.0434 -0.3026 118 GLU A CA  
886  C C   . GLU A 120 ? 0.9137 1.0488 0.8377 0.2332  -0.0393 -0.2973 118 GLU A C   
887  O O   . GLU A 120 ? 0.8901 1.0934 0.8319 0.2263  -0.0308 -0.3008 118 GLU A O   
888  C CB  . GLU A 120 ? 1.0570 1.1957 0.9621 0.2535  -0.0568 -0.3295 118 GLU A CB  
889  C CG  . GLU A 120 ? 1.1986 1.2981 1.0867 0.2827  -0.0799 -0.3447 118 GLU A CG  
890  C CD  . GLU A 120 ? 1.3402 1.4668 1.2226 0.3010  -0.0916 -0.3714 118 GLU A CD  
891  O OE1 . GLU A 120 ? 1.2864 1.4956 1.1877 0.3060  -0.0879 -0.3862 118 GLU A OE1 
892  O OE2 . GLU A 120 ? 1.3299 1.3987 1.1890 0.3082  -0.1045 -0.3779 118 GLU A OE2 
893  N N   . VAL A 121 ? 0.9864 1.0774 0.9039 0.2405  -0.0459 -0.2891 119 VAL A N   
894  C CA  . VAL A 121 ? 0.9235 1.0464 0.8544 0.2442  -0.0442 -0.2867 119 VAL A CA  
895  C C   . VAL A 121 ? 1.0771 1.1716 0.9960 0.2700  -0.0640 -0.2952 119 VAL A C   
896  O O   . VAL A 121 ? 1.1560 1.1835 1.0567 0.2721  -0.0725 -0.2876 119 VAL A O   
897  C CB  . VAL A 121 ? 0.8395 0.9470 0.7786 0.2202  -0.0269 -0.2631 119 VAL A CB  
898  C CG1 . VAL A 121 ? 0.9472 1.0689 0.8933 0.2274  -0.0296 -0.2614 119 VAL A CG1 
899  C CG2 . VAL A 121 ? 0.7552 0.9086 0.7083 0.1992  -0.0106 -0.2584 119 VAL A CG2 
900  N N   . GLU A 122 ? 1.2227 1.3720 1.1512 0.2889  -0.0728 -0.3115 120 GLU A N   
901  C CA  . GLU A 122 ? 1.2253 1.3634 1.1433 0.3193  -0.0956 -0.3249 120 GLU A CA  
902  C C   . GLU A 122 ? 1.2498 1.3793 1.1720 0.3126  -0.0912 -0.3102 120 GLU A C   
903  O O   . GLU A 122 ? 1.2781 1.4629 1.2190 0.3034  -0.0803 -0.3087 120 GLU A O   
904  C CB  . GLU A 122 ? 1.2642 1.4786 1.1925 0.3444  -0.1081 -0.3530 120 GLU A CB  
905  C CG  . GLU A 122 ? 1.3546 1.5597 1.2676 0.3849  -0.1381 -0.3758 120 GLU A CG  
906  C CD  . GLU A 122 ? 1.5320 1.7434 1.4450 0.3970  -0.1468 -0.3746 120 GLU A CD  
907  O OE1 . GLU A 122 ? 1.4910 1.7339 1.4209 0.3755  -0.1292 -0.3610 120 GLU A OE1 
908  O OE2 . GLU A 122 ? 1.6498 1.8375 1.5447 0.4293  -0.1729 -0.3894 120 GLU A OE2 
909  N N   . GLY A 123 ? 1.2531 1.3139 1.1572 0.3145  -0.0992 -0.2987 121 GLY A N   
910  C CA  . GLY A 123 ? 1.1968 1.2478 1.1017 0.3126  -0.0985 -0.2877 121 GLY A CA  
911  C C   . GLY A 123 ? 1.1737 1.1459 1.0532 0.3169  -0.1119 -0.2780 121 GLY A C   
912  O O   . GLY A 123 ? 1.1885 1.1134 1.0534 0.3112  -0.1150 -0.2741 121 GLY A O   
913  N N   . ASP A 124 ? 1.1361 1.0909 1.0074 0.3255  -0.1209 -0.2738 122 ASP A N   
914  C CA  . ASP A 124 ? 1.1733 1.0532 1.0210 0.3202  -0.1293 -0.2594 122 ASP A CA  
915  C C   . ASP A 124 ? 1.0987 0.9689 0.9564 0.2931  -0.1089 -0.2372 122 ASP A C   
916  O O   . ASP A 124 ? 1.2038 1.0380 1.0470 0.2950  -0.1172 -0.2293 122 ASP A O   
917  C CB  . ASP A 124 ? 1.2322 1.0779 1.0541 0.3477  -0.1578 -0.2677 122 ASP A CB  
918  C CG  . ASP A 124 ? 1.3394 1.1731 1.1417 0.3795  -0.1858 -0.2904 122 ASP A CG  
919  O OD1 . ASP A 124 ? 1.3321 1.1629 1.1349 0.3760  -0.1837 -0.2957 122 ASP A OD1 
920  O OD2 . ASP A 124 ? 1.5028 1.3176 1.2841 0.4085  -0.2127 -0.3027 122 ASP A OD2 
921  N N   . THR A 125 ? 1.0303 0.9319 0.9110 0.2694  -0.0839 -0.2279 123 THR A N   
922  C CA  . THR A 125 ? 0.9385 0.8236 0.8264 0.2448  -0.0663 -0.2081 123 THR A CA  
923  C C   . THR A 125 ? 0.9127 0.7651 0.7977 0.2246  -0.0566 -0.1975 123 THR A C   
924  O O   . THR A 125 ? 0.9141 0.7900 0.8112 0.2150  -0.0447 -0.1989 123 THR A O   
925  C CB  . THR A 125 ? 0.9204 0.8588 0.8330 0.2340  -0.0481 -0.2057 123 THR A CB  
926  O OG1 . THR A 125 ? 1.0117 0.9817 0.9247 0.2547  -0.0604 -0.2183 123 THR A OG1 
927  C CG2 . THR A 125 ? 0.8943 0.8159 0.8133 0.2131  -0.0325 -0.1880 123 THR A CG2 
928  N N   . HIS A 126 ? 0.9438 0.7423 0.8088 0.2207  -0.0662 -0.1888 124 HIS A N   
929  C CA  . HIS A 126 ? 0.8933 0.6564 0.7486 0.2058  -0.0648 -0.1816 124 HIS A CA  
930  C C   . HIS A 126 ? 0.8522 0.6032 0.7134 0.1844  -0.0509 -0.1655 124 HIS A C   
931  O O   . HIS A 126 ? 0.7751 0.5229 0.6355 0.1847  -0.0509 -0.1599 124 HIS A O   
932  C CB  . HIS A 126 ? 0.9391 0.6431 0.7588 0.2183  -0.0931 -0.1861 124 HIS A CB  
933  C CG  . HIS A 126 ? 1.0861 0.7992 0.8980 0.2439  -0.1102 -0.2050 124 HIS A CG  
934  N ND1 . HIS A 126 ? 1.1303 0.8510 0.9429 0.2458  -0.1106 -0.2152 124 HIS A ND1 
935  C CD2 . HIS A 126 ? 1.1035 0.8199 0.9055 0.2705  -0.1293 -0.2175 124 HIS A CD2 
936  C CE1 . HIS A 126 ? 1.1099 0.8402 0.9146 0.2729  -0.1285 -0.2338 124 HIS A CE1 
937  N NE2 . HIS A 126 ? 1.1660 0.8942 0.9643 0.2890  -0.1407 -0.2358 124 HIS A NE2 
938  N N   . PHE A 127 ? 0.8703 0.6188 0.7381 0.1672  -0.0394 -0.1598 125 PHE A N   
939  C CA  . PHE A 127 ? 0.7832 0.5180 0.6536 0.1495  -0.0298 -0.1472 125 PHE A CA  
940  C C   . PHE A 127 ? 0.8300 0.5018 0.6636 0.1480  -0.0516 -0.1412 125 PHE A C   
941  O O   . PHE A 127 ? 0.9447 0.5792 0.7523 0.1544  -0.0719 -0.1452 125 PHE A O   
942  C CB  . PHE A 127 ? 0.7214 0.4704 0.6063 0.1346  -0.0150 -0.1446 125 PHE A CB  
943  C CG  . PHE A 127 ? 0.7070 0.4561 0.6015 0.1197  -0.0027 -0.1346 125 PHE A CG  
944  C CD1 . PHE A 127 ? 0.6958 0.4826 0.6170 0.1157  0.0157  -0.1313 125 PHE A CD1 
945  C CD2 . PHE A 127 ? 0.7045 0.4127 0.5771 0.1090  -0.0112 -0.1287 125 PHE A CD2 
946  C CE1 . PHE A 127 ? 0.6046 0.3944 0.5356 0.1055  0.0259  -0.1251 125 PHE A CE1 
947  C CE2 . PHE A 127 ? 0.7198 0.4295 0.5975 0.0980  -0.0007 -0.1218 125 PHE A CE2 
948  C CZ  . PHE A 127 ? 0.6450 0.3993 0.5549 0.0990  0.0180  -0.1215 125 PHE A CZ  
949  N N   . PRO A 128 ? 0.8566 0.5115 0.6828 0.1383  -0.0498 -0.1311 126 PRO A N   
950  C CA  . PRO A 128 ? 0.9065 0.4933 0.6881 0.1313  -0.0732 -0.1217 126 PRO A CA  
951  C C   . PRO A 128 ? 1.0319 0.5794 0.7911 0.1131  -0.0819 -0.1157 126 PRO A C   
952  O O   . PRO A 128 ? 1.0409 0.6095 0.8172 0.1004  -0.0657 -0.1146 126 PRO A O   
953  C CB  . PRO A 128 ? 0.8721 0.4586 0.6527 0.1216  -0.0641 -0.1130 126 PRO A CB  
954  C CG  . PRO A 128 ? 0.8000 0.4503 0.6212 0.1338  -0.0442 -0.1211 126 PRO A CG  
955  C CD  . PRO A 128 ? 0.7790 0.4725 0.6314 0.1343  -0.0299 -0.1282 126 PRO A CD  
956  N N   . ASP A 129 ? 1.1246 0.6127 0.8425 0.1114  -0.1099 -0.1115 127 ASP A N   
957  C CA  . ASP A 129 ? 1.2491 0.6849 0.9325 0.0848  -0.1243 -0.0995 127 ASP A CA  
958  C C   . ASP A 129 ? 1.2381 0.6589 0.9085 0.0525  -0.1172 -0.0825 127 ASP A C   
959  O O   . ASP A 129 ? 1.2286 0.6319 0.8825 0.0450  -0.1209 -0.0727 127 ASP A O   
960  C CB  . ASP A 129 ? 1.3146 0.6865 0.9525 0.0873  -0.1585 -0.0956 127 ASP A CB  
961  C CG  . ASP A 129 ? 1.4893 0.8710 1.1353 0.1108  -0.1650 -0.1133 127 ASP A CG  
962  O OD1 . ASP A 129 ? 1.4394 0.8555 1.1104 0.1062  -0.1474 -0.1197 127 ASP A OD1 
963  O OD2 . ASP A 129 ? 1.6432 1.0097 1.2767 0.1351  -0.1833 -0.1225 127 ASP A OD2 
964  N N   . TYR A 130 ? 1.2986 0.7289 0.9756 0.0324  -0.1066 -0.0798 128 TYR A N   
965  C CA  . TYR A 130 ? 1.2631 0.6943 0.9320 -0.0051 -0.0973 -0.0631 128 TYR A CA  
966  C C   . TYR A 130 ? 1.4362 0.8270 1.0730 -0.0353 -0.1158 -0.0527 128 TYR A C   
967  O O   . TYR A 130 ? 1.4450 0.8479 1.0945 -0.0310 -0.1115 -0.0626 128 TYR A O   
968  C CB  . TYR A 130 ? 1.1410 0.6571 0.8656 0.0022  -0.0635 -0.0682 128 TYR A CB  
969  C CG  . TYR A 130 ? 1.1323 0.6653 0.8785 0.0203  -0.0564 -0.0853 128 TYR A CG  
970  C CD1 . TYR A 130 ? 1.1328 0.6868 0.9015 0.0552  -0.0526 -0.1047 128 TYR A CD1 
971  C CD2 . TYR A 130 ? 1.0353 0.5960 0.7937 -0.0012 -0.0490 -0.0771 128 TYR A CD2 
972  C CE1 . TYR A 130 ? 1.0785 0.6676 0.8724 0.0653  -0.0438 -0.1158 128 TYR A CE1 
973  C CE2 . TYR A 130 ? 0.9696 0.5495 0.7468 0.0131  -0.0425 -0.0909 128 TYR A CE2 
974  C CZ  . TYR A 130 ? 1.0349 0.6157 0.8214 0.0476  -0.0416 -0.1133 128 TYR A CZ  
975  O OH  . TYR A 130 ? 0.9480 0.5619 0.7559 0.0579  -0.0342 -0.1245 128 TYR A OH  
976  N N   . GLU A 131 ? 1.5229 0.8624 1.1151 -0.0633 -0.1396 -0.0337 129 GLU A N   
977  C CA  . GLU A 131 ? 1.5402 0.8486 1.0984 -0.1023 -0.1583 -0.0164 129 GLU A CA  
978  C C   . GLU A 131 ? 1.5046 0.8775 1.0891 -0.1353 -0.1363 -0.0052 129 GLU A C   
979  O O   . GLU A 131 ? 1.4316 0.8802 1.0492 -0.1468 -0.1118 0.0052  129 GLU A O   
980  C CB  . GLU A 131 ? 1.5868 0.8502 1.0991 -0.1273 -0.1827 0.0061  129 GLU A CB  
981  C CG  . GLU A 131 ? 1.6616 0.9595 1.1742 -0.1649 -0.1695 0.0288  129 GLU A CG  
982  C CD  . GLU A 131 ? 1.7300 1.0782 1.2823 -0.1287 -0.1461 0.0161  129 GLU A CD  
983  O OE1 . GLU A 131 ? 1.6619 1.0258 1.2482 -0.0847 -0.1330 -0.0099 129 GLU A OE1 
984  O OE2 . GLU A 131 ? 1.8900 1.2458 1.4300 -0.1429 -0.1475 0.0306  129 GLU A OE2 
985  N N   . PRO A 132 ? 1.5341 0.8946 1.1109 -0.1470 -0.1433 -0.0080 130 PRO A N   
986  C CA  . PRO A 132 ? 1.4351 0.8775 1.0492 -0.1677 -0.1196 0.0002  130 PRO A CA  
987  C C   . PRO A 132 ? 1.4819 0.9609 1.0856 -0.2176 -0.1181 0.0285  130 PRO A C   
988  O O   . PRO A 132 ? 1.4170 0.9806 1.0589 -0.2295 -0.0952 0.0342  130 PRO A O   
989  C CB  . PRO A 132 ? 1.3888 0.7967 0.9864 -0.1710 -0.1336 -0.0090 130 PRO A CB  
990  C CG  . PRO A 132 ? 1.4913 0.8102 1.0397 -0.1603 -0.1667 -0.0141 130 PRO A CG  
991  C CD  . PRO A 132 ? 1.5755 0.8728 1.1121 -0.1475 -0.1731 -0.0094 130 PRO A CD  
992  N N   . ASP A 133 ? 1.6445 1.0672 1.1986 -0.2451 -0.1419 0.0456  131 ASP A N   
993  C CA  . ASP A 133 ? 1.5784 1.0337 1.1125 -0.3016 -0.1449 0.0749  131 ASP A CA  
994  C C   . ASP A 133 ? 1.5542 1.1206 1.1388 -0.3006 -0.1111 0.0783  131 ASP A C   
995  O O   . ASP A 133 ? 1.5798 1.2197 1.1758 -0.3367 -0.1004 0.0933  131 ASP A O   
996  C CB  . ASP A 133 ? 1.6749 1.0469 1.1461 -0.3258 -0.1777 0.0922  131 ASP A CB  
997  C CG  . ASP A 133 ? 1.8035 1.0945 1.2373 -0.3042 -0.2089 0.0825  131 ASP A CG  
998  O OD1 . ASP A 133 ? 1.8185 1.1064 1.2595 -0.2972 -0.2092 0.0715  131 ASP A OD1 
999  O OD2 . ASP A 133 ? 1.8952 1.1288 1.2927 -0.2942 -0.2331 0.0859  131 ASP A OD2 
1000 N N   . ASP A 134 ? 1.5018 1.0841 1.1161 -0.2592 -0.0953 0.0630  132 ASP A N   
1001 C CA  . ASP A 134 ? 1.3541 1.0316 1.0109 -0.2557 -0.0665 0.0634  132 ASP A CA  
1002 C C   . ASP A 134 ? 1.2373 0.9593 0.9522 -0.2057 -0.0402 0.0387  132 ASP A C   
1003 O O   . ASP A 134 ? 1.2631 1.0341 1.0089 -0.1864 -0.0208 0.0313  132 ASP A O   
1004 C CB  . ASP A 134 ? 1.4498 1.1112 1.0809 -0.2652 -0.0737 0.0737  132 ASP A CB  
1005 C CG  . ASP A 134 ? 1.5198 1.0892 1.1250 -0.2330 -0.0929 0.0629  132 ASP A CG  
1006 O OD1 . ASP A 134 ? 1.5754 1.0994 1.1843 -0.2021 -0.0992 0.0453  132 ASP A OD1 
1007 O OD2 . ASP A 134 ? 1.4635 1.0087 1.0429 -0.2393 -0.1031 0.0721  132 ASP A OD2 
1008 N N   . TRP A 135 ? 1.1809 0.8867 0.9087 -0.1874 -0.0405 0.0266  133 TRP A N   
1009 C CA  . TRP A 135 ? 1.0281 0.7823 0.8087 -0.1503 -0.0172 0.0085  133 TRP A CA  
1010 C C   . TRP A 135 ? 0.9463 0.7306 0.7415 -0.1620 -0.0144 0.0109  133 TRP A C   
1011 O O   . TRP A 135 ? 1.0308 0.7648 0.7955 -0.1761 -0.0330 0.0134  133 TRP A O   
1012 C CB  . TRP A 135 ? 0.9537 0.6587 0.7370 -0.1084 -0.0200 -0.0121 133 TRP A CB  
1013 C CG  . TRP A 135 ? 0.9353 0.6319 0.7182 -0.0900 -0.0167 -0.0175 133 TRP A CG  
1014 C CD1 . TRP A 135 ? 1.0244 0.6594 0.7663 -0.0935 -0.0369 -0.0134 133 TRP A CD1 
1015 C CD2 . TRP A 135 ? 0.8701 0.6198 0.6936 -0.0662 0.0063  -0.0275 133 TRP A CD2 
1016 N NE1 . TRP A 135 ? 0.8969 0.5497 0.6532 -0.0738 -0.0263 -0.0199 133 TRP A NE1 
1017 C CE2 . TRP A 135 ? 0.8436 0.5657 0.6493 -0.0575 0.0004  -0.0293 133 TRP A CE2 
1018 C CE3 . TRP A 135 ? 0.7616 0.5749 0.6324 -0.0512 0.0288  -0.0351 133 TRP A CE3 
1019 C CZ2 . TRP A 135 ? 0.6846 0.4441 0.5189 -0.0362 0.0180  -0.0394 133 TRP A CZ2 
1020 C CZ3 . TRP A 135 ? 0.7022 0.5453 0.5991 -0.0292 0.0443  -0.0453 133 TRP A CZ3 
1021 C CH2 . TRP A 135 ? 0.6830 0.5008 0.5617 -0.0231 0.0396  -0.0478 133 TRP A CH2 
1022 N N   . GLU A 136 ? 0.7979 0.6628 0.6384 -0.1550 0.0070  0.0093  134 GLU A N   
1023 C CA  . GLU A 136 ? 0.7127 0.6167 0.5742 -0.1609 0.0113  0.0112  134 GLU A CA  
1024 C C   . GLU A 136 ? 0.7197 0.6327 0.6180 -0.1208 0.0236  -0.0054 134 GLU A C   
1025 O O   . GLU A 136 ? 0.7307 0.6644 0.6564 -0.0935 0.0375  -0.0151 134 GLU A O   
1026 C CB  . GLU A 136 ? 0.7623 0.7557 0.6472 -0.1817 0.0233  0.0218  134 GLU A CB  
1027 C CG  . GLU A 136 ? 0.7704 0.8060 0.6705 -0.1948 0.0235  0.0272  134 GLU A CG  
1028 C CD  . GLU A 136 ? 0.7438 0.8833 0.6787 -0.2025 0.0378  0.0318  134 GLU A CD  
1029 O OE1 . GLU A 136 ? 0.6388 0.8219 0.5810 -0.2055 0.0467  0.0322  134 GLU A OE1 
1030 O OE2 . GLU A 136 ? 0.7786 0.9599 0.7338 -0.2045 0.0394  0.0339  134 GLU A OE2 
1031 N N   . SER A 137 ? 0.7052 0.6028 0.6018 -0.1200 0.0173  -0.0079 135 SER A N   
1032 C CA  . SER A 137 ? 0.6481 0.5588 0.5764 -0.0888 0.0273  -0.0199 135 SER A CA  
1033 C C   . SER A 137 ? 0.6424 0.6253 0.6089 -0.0888 0.0389  -0.0138 135 SER A C   
1034 O O   . SER A 137 ? 0.7383 0.7480 0.7007 -0.1137 0.0339  -0.0030 135 SER A O   
1035 C CB  . SER A 137 ? 0.6017 0.4653 0.5087 -0.0865 0.0147  -0.0273 135 SER A CB  
1036 O OG  . SER A 137 ? 0.6210 0.5075 0.5578 -0.0630 0.0242  -0.0354 135 SER A OG  
1037 N N   . VAL A 138 ? 0.6199 0.6327 0.6219 -0.0605 0.0524  -0.0212 136 VAL A N   
1038 C CA  . VAL A 138 ? 0.5921 0.6692 0.6309 -0.0534 0.0607  -0.0176 136 VAL A CA  
1039 C C   . VAL A 138 ? 0.5704 0.6463 0.6305 -0.0318 0.0618  -0.0214 136 VAL A C   
1040 O O   . VAL A 138 ? 0.5830 0.7031 0.6665 -0.0296 0.0626  -0.0157 136 VAL A O   
1041 C CB  . VAL A 138 ? 0.4538 0.5737 0.5165 -0.0394 0.0724  -0.0224 136 VAL A CB  
1042 C CG1 . VAL A 138 ? 0.5425 0.6669 0.5810 -0.0645 0.0710  -0.0169 136 VAL A CG1 
1043 C CG2 . VAL A 138 ? 0.4553 0.5475 0.5302 -0.0085 0.0788  -0.0352 136 VAL A CG2 
1044 N N   . PHE A 139 ? 0.5571 0.5880 0.6088 -0.0173 0.0608  -0.0301 137 PHE A N   
1045 C CA  . PHE A 139 ? 0.5413 0.5740 0.6106 -0.0011 0.0615  -0.0317 137 PHE A CA  
1046 C C   . PHE A 139 ? 0.5265 0.5179 0.5726 -0.0020 0.0555  -0.0386 137 PHE A C   
1047 O O   . PHE A 139 ? 0.5551 0.5102 0.5781 -0.0014 0.0529  -0.0474 137 PHE A O   
1048 C CB  . PHE A 139 ? 0.5147 0.5540 0.6086 0.0238  0.0694  -0.0376 137 PHE A CB  
1049 C CG  . PHE A 139 ? 0.4859 0.5235 0.5936 0.0354  0.0671  -0.0355 137 PHE A CG  
1050 C CD1 . PHE A 139 ? 0.4936 0.5624 0.6210 0.0374  0.0631  -0.0257 137 PHE A CD1 
1051 C CD2 . PHE A 139 ? 0.4773 0.4850 0.5761 0.0422  0.0675  -0.0424 137 PHE A CD2 
1052 C CE1 . PHE A 139 ? 0.4654 0.5281 0.6012 0.0450  0.0581  -0.0207 137 PHE A CE1 
1053 C CE2 . PHE A 139 ? 0.4916 0.4998 0.5989 0.0466  0.0641  -0.0377 137 PHE A CE2 
1054 C CZ  . PHE A 139 ? 0.4861 0.5179 0.6105 0.0472  0.0586  -0.0257 137 PHE A CZ  
1055 N N   . SER A 140 ? 0.5060 0.5067 0.5590 -0.0009 0.0527  -0.0356 138 SER A N   
1056 C CA  . SER A 140 ? 0.4591 0.4345 0.4888 -0.0056 0.0461  -0.0431 138 SER A CA  
1057 C C   . SER A 140 ? 0.5072 0.5023 0.5505 -0.0018 0.0459  -0.0390 138 SER A C   
1058 O O   . SER A 140 ? 0.6108 0.6346 0.6686 -0.0083 0.0436  -0.0264 138 SER A O   
1059 C CB  . SER A 140 ? 0.4620 0.4278 0.4677 -0.0278 0.0364  -0.0402 138 SER A CB  
1060 O OG  . SER A 140 ? 0.5772 0.5183 0.5590 -0.0299 0.0285  -0.0509 138 SER A OG  
1061 N N   . GLU A 141 ? 0.4946 0.4791 0.5324 0.0071  0.0473  -0.0484 139 GLU A N   
1062 C CA  . GLU A 141 ? 0.4767 0.4821 0.5249 0.0063  0.0464  -0.0416 139 GLU A CA  
1063 C C   . GLU A 141 ? 0.5234 0.5258 0.5531 0.0061  0.0452  -0.0552 139 GLU A C   
1064 O O   . GLU A 141 ? 0.5185 0.5142 0.5465 0.0164  0.0496  -0.0655 139 GLU A O   
1065 C CB  . GLU A 141 ? 0.4743 0.4850 0.5453 0.0177  0.0505  -0.0340 139 GLU A CB  
1066 C CG  . GLU A 141 ? 0.4937 0.5237 0.5775 0.0131  0.0447  -0.0180 139 GLU A CG  
1067 C CD  . GLU A 141 ? 0.5069 0.5295 0.6065 0.0239  0.0443  -0.0116 139 GLU A CD  
1068 O OE1 . GLU A 141 ? 0.5760 0.6040 0.6945 0.0330  0.0405  -0.0022 139 GLU A OE1 
1069 O OE2 . GLU A 141 ? 0.4410 0.4536 0.5329 0.0235  0.0464  -0.0169 139 GLU A OE2 
1070 N N   . PHE A 142 ? 0.5536 0.5680 0.5703 -0.0056 0.0391  -0.0562 140 PHE A N   
1071 C CA  . PHE A 142 ? 0.5444 0.5667 0.5431 -0.0050 0.0376  -0.0724 140 PHE A CA  
1072 C C   . PHE A 142 ? 0.5190 0.5743 0.5282 -0.0114 0.0395  -0.0623 140 PHE A C   
1073 O O   . PHE A 142 ? 0.4870 0.5546 0.5113 -0.0198 0.0371  -0.0412 140 PHE A O   
1074 C CB  . PHE A 142 ? 0.4921 0.5121 0.4689 -0.0150 0.0291  -0.0808 140 PHE A CB  
1075 C CG  . PHE A 142 ? 0.5192 0.5521 0.4762 -0.0107 0.0266  -0.1032 140 PHE A CG  
1076 C CD1 . PHE A 142 ? 0.5792 0.5862 0.5164 0.0059  0.0232  -0.1288 140 PHE A CD1 
1077 C CD2 . PHE A 142 ? 0.5083 0.5824 0.4656 -0.0221 0.0264  -0.0996 140 PHE A CD2 
1078 C CE1 . PHE A 142 ? 0.5505 0.5766 0.4708 0.0148  0.0202  -0.1538 140 PHE A CE1 
1079 C CE2 . PHE A 142 ? 0.5043 0.6016 0.4438 -0.0177 0.0250  -0.1231 140 PHE A CE2 
1080 C CZ  . PHE A 142 ? 0.5351 0.6103 0.4572 0.0027  0.0221  -0.1520 140 PHE A CZ  
1081 N N   . HIS A 143 ? 0.5172 0.5885 0.5166 -0.0080 0.0422  -0.0772 141 HIS A N   
1082 C CA  . HIS A 143 ? 0.5078 0.6145 0.5107 -0.0199 0.0431  -0.0680 141 HIS A CA  
1083 C C   . HIS A 143 ? 0.4936 0.6350 0.4775 -0.0223 0.0430  -0.0890 141 HIS A C   
1084 O O   . HIS A 143 ? 0.5160 0.6531 0.4894 -0.0060 0.0450  -0.1143 141 HIS A O   
1085 C CB  . HIS A 143 ? 0.4739 0.5749 0.4886 -0.0154 0.0481  -0.0628 141 HIS A CB  
1086 C CG  . HIS A 143 ? 0.4896 0.5646 0.5235 -0.0130 0.0465  -0.0425 141 HIS A CG  
1087 N ND1 . HIS A 143 ? 0.4675 0.5475 0.5105 -0.0248 0.0396  -0.0187 141 HIS A ND1 
1088 C CD2 . HIS A 143 ? 0.4925 0.5385 0.5371 0.0010  0.0493  -0.0436 141 HIS A CD2 
1089 C CE1 . HIS A 143 ? 0.4928 0.5476 0.5527 -0.0140 0.0380  -0.0089 141 HIS A CE1 
1090 N NE2 . HIS A 143 ? 0.4874 0.5257 0.5493 0.0007  0.0451  -0.0240 141 HIS A NE2 
1091 N N   . ASP A 144 ? 0.4746 0.6534 0.4536 -0.0411 0.0397  -0.0798 142 ASP A N   
1092 C CA  . ASP A 144 ? 0.4953 0.7199 0.4575 -0.0435 0.0411  -0.1016 142 ASP A CA  
1093 C C   . ASP A 144 ? 0.4679 0.7224 0.4331 -0.0445 0.0474  -0.1057 142 ASP A C   
1094 O O   . ASP A 144 ? 0.4960 0.7347 0.4741 -0.0499 0.0490  -0.0866 142 ASP A O   
1095 C CB  . ASP A 144 ? 0.4497 0.7148 0.4040 -0.0666 0.0363  -0.0903 142 ASP A CB  
1096 C CG  . ASP A 144 ? 0.4685 0.7140 0.4166 -0.0676 0.0297  -0.0905 142 ASP A CG  
1097 O OD1 . ASP A 144 ? 0.5700 0.7928 0.5054 -0.0513 0.0279  -0.1160 142 ASP A OD1 
1098 O OD2 . ASP A 144 ? 0.4372 0.6912 0.3901 -0.0856 0.0244  -0.0660 142 ASP A OD2 
1099 N N   . ALA A 145 ? 0.4685 0.7694 0.4206 -0.0394 0.0501  -0.1326 143 ALA A N   
1100 C CA  . ALA A 145 ? 0.4735 0.8231 0.4266 -0.0485 0.0557  -0.1348 143 ALA A CA  
1101 C C   . ALA A 145 ? 0.5008 0.8888 0.4518 -0.0846 0.0531  -0.1062 143 ALA A C   
1102 O O   . ALA A 145 ? 0.5422 0.9497 0.4850 -0.0989 0.0484  -0.0994 143 ALA A O   
1103 C CB  . ALA A 145 ? 0.4841 0.8859 0.4246 -0.0316 0.0588  -0.1740 143 ALA A CB  
1104 N N   . ASP A 146 ? 0.5145 0.9100 0.4704 -0.1015 0.0542  -0.0881 144 ASP A N   
1105 C CA  . ASP A 146 ? 0.5515 0.9774 0.5005 -0.1396 0.0483  -0.0581 144 ASP A CA  
1106 C C   . ASP A 146 ? 0.6036 1.0905 0.5449 -0.1571 0.0533  -0.0649 144 ASP A C   
1107 O O   . ASP A 146 ? 0.6074 1.1281 0.5491 -0.1373 0.0618  -0.0971 144 ASP A O   
1108 C CB  . ASP A 146 ? 0.5386 0.9005 0.4973 -0.1493 0.0387  -0.0213 144 ASP A CB  
1109 C CG  . ASP A 146 ? 0.6446 0.9547 0.6170 -0.1310 0.0416  -0.0225 144 ASP A CG  
1110 O OD1 . ASP A 146 ? 0.6930 1.0247 0.6626 -0.1370 0.0461  -0.0295 144 ASP A OD1 
1111 O OD2 . ASP A 146 ? 0.6715 0.9242 0.6574 -0.1123 0.0391  -0.0160 144 ASP A OD2 
1112 N N   . ALA A 147 ? 0.6625 1.1645 0.5952 -0.1957 0.0461  -0.0334 145 ALA A N   
1113 C CA  . ALA A 147 ? 0.6261 1.1940 0.5483 -0.2217 0.0495  -0.0355 145 ALA A CA  
1114 C C   . ALA A 147 ? 0.6597 1.2051 0.5924 -0.2047 0.0555  -0.0478 145 ALA A C   
1115 O O   . ALA A 147 ? 0.7264 1.3367 0.6567 -0.2035 0.0640  -0.0715 145 ALA A O   
1116 C CB  . ALA A 147 ? 0.6312 1.2044 0.5373 -0.2714 0.0364  0.0064  145 ALA A CB  
1117 N N   . GLN A 148 ? 0.7306 1.1901 0.6757 -0.1900 0.0512  -0.0337 146 GLN A N   
1118 C CA  . GLN A 148 ? 0.7360 1.1716 0.6898 -0.1768 0.0559  -0.0428 146 GLN A CA  
1119 C C   . GLN A 148 ? 0.7517 1.1780 0.7179 -0.1315 0.0661  -0.0784 146 GLN A C   
1120 O O   . GLN A 148 ? 0.7800 1.2163 0.7507 -0.1196 0.0721  -0.0949 146 GLN A O   
1121 C CB  . GLN A 148 ? 0.8144 1.1646 0.7743 -0.1804 0.0458  -0.0145 146 GLN A CB  
1122 C CG  . GLN A 148 ? 0.7989 1.1382 0.7430 -0.2231 0.0301  0.0233  146 GLN A CG  
1123 C CD  . GLN A 148 ? 0.8472 1.1707 0.7884 -0.2287 0.0202  0.0430  146 GLN A CD  
1124 O OE1 . GLN A 148 ? 0.9659 1.3391 0.8907 -0.2596 0.0153  0.0555  146 GLN A OE1 
1125 N NE2 . GLN A 148 ? 0.9471 1.2071 0.9042 -0.1997 0.0172  0.0456  146 GLN A NE2 
1126 N N   . ASN A 149 ? 0.6697 1.0751 0.6392 -0.1079 0.0663  -0.0895 147 ASN A N   
1127 C CA  . ASN A 149 ? 0.6463 1.0232 0.6231 -0.0675 0.0712  -0.1176 147 ASN A CA  
1128 C C   . ASN A 149 ? 0.5888 1.0122 0.5558 -0.0524 0.0728  -0.1475 147 ASN A C   
1129 O O   . ASN A 149 ? 0.5647 0.9907 0.5252 -0.0595 0.0688  -0.1425 147 ASN A O   
1130 C CB  . ASN A 149 ? 0.6457 0.9439 0.6326 -0.0540 0.0671  -0.1030 147 ASN A CB  
1131 C CG  . ASN A 149 ? 0.6008 0.8548 0.5968 -0.0659 0.0635  -0.0763 147 ASN A CG  
1132 O OD1 . ASN A 149 ? 0.5926 0.8158 0.5968 -0.0509 0.0669  -0.0819 147 ASN A OD1 
1133 N ND2 . ASN A 149 ? 0.6193 0.8692 0.6121 -0.0926 0.0549  -0.0477 147 ASN A ND2 
1134 N N   . SER A 150 ? 0.6159 1.0749 0.5810 -0.0294 0.0773  -0.1801 148 SER A N   
1135 C CA  . SER A 150 ? 0.6206 1.1218 0.5828 -0.0156 0.0707  -0.2040 148 SER A CA  
1136 C C   . SER A 150 ? 0.6143 1.0613 0.5727 0.0150  0.0634  -0.2196 148 SER A C   
1137 O O   . SER A 150 ? 0.5488 1.0188 0.5054 0.0259  0.0554  -0.2356 148 SER A O   
1138 C CB  . SER A 150 ? 0.6606 1.2002 0.6357 -0.0045 0.0652  -0.2172 148 SER A CB  
1139 O OG  . SER A 150 ? 0.7133 1.1989 0.6946 0.0305  0.0594  -0.2290 148 SER A OG  
1140 N N   . HIS A 151 ? 0.6065 0.9837 0.5635 0.0275  0.0649  -0.2152 149 HIS A N   
1141 C CA  . HIS A 151 ? 0.5896 0.9104 0.5388 0.0504  0.0557  -0.2263 149 HIS A CA  
1142 C C   . HIS A 151 ? 0.5350 0.8033 0.4847 0.0398  0.0574  -0.2061 149 HIS A C   
1143 O O   . HIS A 151 ? 0.5222 0.7714 0.4864 0.0259  0.0614  -0.1796 149 HIS A O   
1144 C CB  . HIS A 151 ? 0.5982 0.8731 0.5508 0.0787  0.0468  -0.2335 149 HIS A CB  
1145 C CG  . HIS A 151 ? 0.7395 1.0540 0.6950 0.0928  0.0385  -0.2496 149 HIS A CG  
1146 N ND1 . HIS A 151 ? 0.9095 1.2147 0.8552 0.1102  0.0271  -0.2663 149 HIS A ND1 
1147 C CD2 . HIS A 151 ? 0.7452 1.1116 0.7130 0.0925  0.0389  -0.2534 149 HIS A CD2 
1148 C CE1 . HIS A 151 ? 0.8814 1.2344 0.8356 0.1225  0.0213  -0.2806 149 HIS A CE1 
1149 N NE2 . HIS A 151 ? 0.7978 1.1908 0.7660 0.1114  0.0281  -0.2731 149 HIS A NE2 
1150 N N   . SER A 152 ? 0.5490 0.7870 0.4872 0.0436  0.0498  -0.2105 150 SER A N   
1151 C CA  . SER A 152 ? 0.5783 0.7609 0.5233 0.0335  0.0471  -0.1842 150 SER A CA  
1152 C C   . SER A 152 ? 0.5666 0.6941 0.5156 0.0512  0.0466  -0.1849 150 SER A C   
1153 O O   . SER A 152 ? 0.6188 0.7384 0.5591 0.0744  0.0442  -0.2090 150 SER A O   
1154 C CB  . SER A 152 ? 0.5876 0.7532 0.5174 0.0297  0.0382  -0.1885 150 SER A CB  
1155 O OG  . SER A 152 ? 0.7286 0.8759 0.6368 0.0536  0.0296  -0.2220 150 SER A OG  
1156 N N   . TYR A 153 ? 0.4993 0.5927 0.4616 0.0411  0.0481  -0.1589 151 TYR A N   
1157 C CA  . TYR A 153 ? 0.5427 0.5934 0.5107 0.0533  0.0493  -0.1563 151 TYR A CA  
1158 C C   . TYR A 153 ? 0.5528 0.5728 0.5299 0.0420  0.0481  -0.1329 151 TYR A C   
1159 O O   . TYR A 153 ? 0.5534 0.5891 0.5386 0.0256  0.0476  -0.1153 151 TYR A O   
1160 C CB  . TYR A 153 ? 0.5642 0.6317 0.5471 0.0550  0.0578  -0.1521 151 TYR A CB  
1161 C CG  . TYR A 153 ? 0.5159 0.6077 0.5136 0.0332  0.0615  -0.1280 151 TYR A CG  
1162 C CD1 . TYR A 153 ? 0.5458 0.6864 0.5391 0.0183  0.0618  -0.1279 151 TYR A CD1 
1163 C CD2 . TYR A 153 ? 0.4833 0.5490 0.4969 0.0277  0.0627  -0.1059 151 TYR A CD2 
1164 C CE1 . TYR A 153 ? 0.5494 0.7040 0.5512 -0.0042 0.0613  -0.1027 151 TYR A CE1 
1165 C CE2 . TYR A 153 ? 0.5106 0.5882 0.5342 0.0107  0.0616  -0.0842 151 TYR A CE2 
1166 C CZ  . TYR A 153 ? 0.5229 0.6407 0.5392 -0.0066 0.0599  -0.0809 151 TYR A CZ  
1167 O OH  . TYR A 153 ? 0.5536 0.6755 0.5754 -0.0261 0.0550  -0.0562 151 TYR A OH  
1168 N N   . CYS A 154 ? 0.5322 0.5135 0.5081 0.0506  0.0470  -0.1326 152 CYS A N   
1169 C CA  . CYS A 154 ? 0.4794 0.4404 0.4624 0.0402  0.0457  -0.1140 152 CYS A CA  
1170 C C   . CYS A 154 ? 0.5261 0.4677 0.5196 0.0476  0.0508  -0.1088 152 CYS A C   
1171 O O   . CYS A 154 ? 0.5621 0.4779 0.5417 0.0587  0.0479  -0.1211 152 CYS A O   
1172 C CB  . CYS A 154 ? 0.5166 0.4504 0.4763 0.0352  0.0348  -0.1200 152 CYS A CB  
1173 S SG  . CYS A 154 ? 0.5739 0.5064 0.5440 0.0152  0.0336  -0.0954 152 CYS A SG  
1174 N N   . PHE A 155 ? 0.4697 0.4227 0.4860 0.0428  0.0566  -0.0915 153 PHE A N   
1175 C CA  . PHE A 155 ? 0.4462 0.3864 0.4730 0.0496  0.0616  -0.0880 153 PHE A CA  
1176 C C   . PHE A 155 ? 0.4856 0.4121 0.5060 0.0421  0.0580  -0.0820 153 PHE A C   
1177 O O   . PHE A 155 ? 0.5411 0.4777 0.5619 0.0295  0.0539  -0.0724 153 PHE A O   
1178 C CB  . PHE A 155 ? 0.3993 0.3554 0.4512 0.0504  0.0667  -0.0754 153 PHE A CB  
1179 C CG  . PHE A 155 ? 0.4703 0.4385 0.5249 0.0505  0.0681  -0.0772 153 PHE A CG  
1180 C CD1 . PHE A 155 ? 0.5281 0.4949 0.5740 0.0579  0.0712  -0.0920 153 PHE A CD1 
1181 C CD2 . PHE A 155 ? 0.4854 0.4688 0.5494 0.0411  0.0648  -0.0632 153 PHE A CD2 
1182 C CE1 . PHE A 155 ? 0.5188 0.5050 0.5655 0.0531  0.0725  -0.0931 153 PHE A CE1 
1183 C CE2 . PHE A 155 ? 0.4845 0.4800 0.5465 0.0347  0.0644  -0.0621 153 PHE A CE2 
1184 C CZ  . PHE A 155 ? 0.5155 0.5154 0.5690 0.0393  0.0690  -0.0772 153 PHE A CZ  
1185 N N   . GLU A 156 ? 0.4707 0.3778 0.4839 0.0472  0.0590  -0.0863 154 GLU A N   
1186 C CA  . GLU A 156 ? 0.5154 0.4139 0.5201 0.0350  0.0554  -0.0784 154 GLU A CA  
1187 C C   . GLU A 156 ? 0.5233 0.4255 0.5382 0.0405  0.0626  -0.0768 154 GLU A C   
1188 O O   . GLU A 156 ? 0.5366 0.4278 0.5506 0.0538  0.0660  -0.0863 154 GLU A O   
1189 C CB  . GLU A 156 ? 0.4828 0.3429 0.4524 0.0286  0.0425  -0.0857 154 GLU A CB  
1190 C CG  . GLU A 156 ? 0.5498 0.4019 0.5057 0.0069  0.0359  -0.0734 154 GLU A CG  
1191 C CD  . GLU A 156 ? 0.6190 0.4184 0.5341 -0.0006 0.0192  -0.0790 154 GLU A CD  
1192 O OE1 . GLU A 156 ? 0.6281 0.3971 0.5273 0.0174  0.0126  -0.0954 154 GLU A OE1 
1193 O OE2 . GLU A 156 ? 0.5793 0.3686 0.4771 -0.0249 0.0109  -0.0670 154 GLU A OE2 
1194 N N   . ILE A 157 ? 0.5009 0.4250 0.5257 0.0301  0.0651  -0.0660 155 ILE A N   
1195 C CA  . ILE A 157 ? 0.4931 0.4282 0.5248 0.0326  0.0716  -0.0656 155 ILE A CA  
1196 C C   . ILE A 157 ? 0.5189 0.4517 0.5294 0.0101  0.0654  -0.0570 155 ILE A C   
1197 O O   . ILE A 157 ? 0.5151 0.4661 0.5248 -0.0072 0.0614  -0.0473 155 ILE A O   
1198 C CB  . ILE A 157 ? 0.4784 0.4535 0.5440 0.0432  0.0807  -0.0633 155 ILE A CB  
1199 C CG1 . ILE A 157 ? 0.4346 0.4051 0.5158 0.0589  0.0825  -0.0674 155 ILE A CG1 
1200 C CG2 . ILE A 157 ? 0.4520 0.4394 0.5235 0.0493  0.0880  -0.0682 155 ILE A CG2 
1201 C CD1 . ILE A 157 ? 0.3579 0.3548 0.4681 0.0716  0.0860  -0.0654 155 ILE A CD1 
1202 N N   . LEU A 158 ? 0.5915 0.5026 0.5829 0.0074  0.0631  -0.0591 156 LEU A N   
1203 C CA  . LEU A 158 ? 0.5840 0.4897 0.5501 -0.0189 0.0551  -0.0481 156 LEU A CA  
1204 C C   . LEU A 158 ? 0.5614 0.5028 0.5387 -0.0206 0.0649  -0.0461 156 LEU A C   
1205 O O   . LEU A 158 ? 0.5922 0.5373 0.5840 0.0001  0.0736  -0.0562 156 LEU A O   
1206 C CB  . LEU A 158 ? 0.6124 0.4543 0.5365 -0.0250 0.0384  -0.0498 156 LEU A CB  
1207 C CG  . LEU A 158 ? 0.6353 0.4374 0.5387 -0.0259 0.0247  -0.0543 156 LEU A CG  
1208 C CD1 . LEU A 158 ? 0.5835 0.3808 0.5017 0.0040  0.0298  -0.0711 156 LEU A CD1 
1209 C CD2 . LEU A 158 ? 0.7137 0.4532 0.5693 -0.0412 0.0027  -0.0516 156 LEU A CD2 
1210 N N   . GLU A 159 ? 0.6022 0.5740 0.5717 -0.0472 0.0632  -0.0338 157 GLU A N   
1211 C CA  . GLU A 159 ? 0.6156 0.6306 0.5911 -0.0544 0.0715  -0.0317 157 GLU A CA  
1212 C C   . GLU A 159 ? 0.6904 0.6742 0.6218 -0.0865 0.0577  -0.0183 157 GLU A C   
1213 O O   . GLU A 159 ? 0.7384 0.6911 0.6416 -0.1109 0.0428  -0.0073 157 GLU A O   
1214 C CB  . GLU A 159 ? 0.6406 0.7337 0.6449 -0.0613 0.0808  -0.0282 157 GLU A CB  
1215 C CG  . GLU A 159 ? 0.5684 0.6952 0.6155 -0.0307 0.0907  -0.0389 157 GLU A CG  
1216 C CD  . GLU A 159 ? 0.4818 0.6261 0.5533 -0.0017 0.1021  -0.0541 157 GLU A CD  
1217 O OE1 . GLU A 159 ? 0.6384 0.8005 0.7016 -0.0087 0.1064  -0.0561 157 GLU A OE1 
1218 O OE2 . GLU A 159 ? 0.4396 0.5826 0.5370 0.0256  0.1057  -0.0634 157 GLU A OE2 
1219 N N   . ARG A 160 ? 0.6938 0.6823 0.6161 -0.0885 0.0605  -0.0186 158 ARG A N   
1220 C CA  . ARG A 160 ? 0.7409 0.7016 0.6185 -0.1230 0.0452  -0.0023 158 ARG A CA  
1221 C C   . ARG A 160 ? 0.7951 0.8145 0.6678 -0.1623 0.0453  0.0139  158 ARG A C   
1222 O O   . ARG A 160 ? 0.7704 0.8720 0.6734 -0.1610 0.0618  0.0100  158 ARG A O   
1223 C CB  . ARG A 160 ? 0.7718 0.7301 0.6408 -0.1170 0.0482  -0.0052 158 ARG A CB  
1224 C CG  . ARG A 160 ? 0.7925 0.6926 0.6070 -0.1469 0.0257  0.0121  158 ARG A CG  
1225 C CD  . ARG A 160 ? 0.8287 0.7356 0.6327 -0.1467 0.0280  0.0127  158 ARG A CD  
1226 N NE  . ARG A 160 ? 0.7764 0.6270 0.5768 -0.1129 0.0231  -0.0006 158 ARG A NE  
1227 C CZ  . ARG A 160 ? 0.8413 0.6099 0.6022 -0.1118 -0.0007 0.0040  158 ARG A CZ  
1228 N NH1 . ARG A 160 ? 0.9075 0.6272 0.6249 -0.1438 -0.0243 0.0222  158 ARG A NH1 
1229 N NH2 . ARG A 160 ? 0.8230 0.5580 0.5874 -0.0775 -0.0025 -0.0111 158 ARG A NH2 
1230 N N   . ARG A 161 ? 0.8512 0.8307 0.6845 -0.1974 0.0258  0.0307  159 ARG A N   
1231 C CA  . ARG A 161 ? 0.9129 0.9490 0.7353 -0.2425 0.0237  0.0487  159 ARG A CA  
1232 C C   . ARG A 161 ? 0.9476 1.0215 0.7554 -0.2654 0.0266  0.0579  159 ARG A C   
1233 O O   . ARG A 161 ? 1.0325 1.0433 0.7957 -0.2835 0.0091  0.0697  159 ARG A O   
1234 C CB  . ARG A 161 ? 1.0456 1.0196 0.8214 -0.2798 -0.0014 0.0659  159 ARG A CB  
1235 C CG  . ARG A 161 ? 1.0539 0.9959 0.8413 -0.2609 -0.0048 0.0564  159 ARG A CG  
1236 C CD  . ARG A 161 ? 1.1271 1.0430 0.8760 -0.3063 -0.0254 0.0739  159 ARG A CD  
1237 N NE  . ARG A 161 ? 1.2923 1.2907 1.0400 -0.3518 -0.0214 0.0919  159 ARG A NE  
1238 C CZ  . ARG A 161 ? 1.2885 1.3916 1.0815 -0.3487 -0.0015 0.0884  159 ARG A CZ  
1239 N NH1 . ARG A 161 ? 1.1981 1.3810 0.9861 -0.3921 0.0006  0.1040  159 ARG A NH1 
1240 N NH2 . ARG A 161 ? 1.2510 1.3812 1.0925 -0.3034 0.0146  0.0697  159 ARG A NH2 
1241 O OXT . ARG A 161 ? 0.9262 1.0950 0.7658 -0.2643 0.0453  0.0526  159 ARG A OXT 
# 
