data_9GGT
# 
_entry.id   9GGT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9GGT         pdb_00009ggt 10.2210/pdb9ggt/pdb 
WWPDB D_1292140506 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-16 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GGT 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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_database_related.content_type 
_pdbx_database_related.db_id 
_pdbx_database_related.db_name 
_pdbx_database_related.details 
unspecified 9GGY PDB . 
unspecified 9GH2 PDB . 
unspecified 9GGZ PDB . 
unspecified 9GH0 PDB . 
unspecified 9GH1 PDB . 
unspecified 9GGW PDB . 
unspecified 9GGX PDB . 
unspecified 9GGU PDB . 
unspecified 9GGV PDB . 
unspecified 9G4B PDB . 
unspecified 9G0Y PDB . 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexander.schuettelkopf@cancer.org.uk 
_pdbx_contact_author.name_first         Alexander 
_pdbx_contact_author.name_last          Schuettelkopf 
_pdbx_contact_author.name_mi            W. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9424-8730 
# 
_audit_author.name               'Schuettelkopf, A.W.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-9424-8730 
# 
_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            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                9129 
_citation.page_last                 9161 
_citation.title                     
'Reversible Small Molecule Multivariant Ras Inhibitors Display Tunable Affinity for the Active and Inactive Forms of Ras.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02929 
_citation.pdbx_database_id_PubMed   40162713 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Parry, C.W.'        1  ? 
primary 'Pellicano, F.'      2  ? 
primary 'Schuttelkopf, A.W.' 3  ? 
primary 'Beyer, K.S.'        4  ? 
primary 'Bower, J.'          5  ? 
primary 'Bryson, A.'         6  ? 
primary 'Cameron, K.'        7  ? 
primary 'Cerutti, N.M.'      8  ? 
primary 'Clark, J.P.'        9  ? 
primary 'Davidson, S.C.'     10 ? 
primary 'Davies, K.'         11 ? 
primary 'Drysdale, M.J.'     12 ? 
primary 'Engelman, J.'       13 ? 
primary 'Estevan-Barber, A.' 14 ? 
primary 'Gohlke, A.'         15 ? 
primary 'Gray, C.H.'         16 ? 
primary 'Guthy, D.A.'        17 ? 
primary 'Hong, M.'           18 ? 
primary 'Hopkins, A.'        19 ? 
primary 'Hutchinson, L.D.'   20 ? 
primary 'Konczal, J.'        21 ? 
primary 'Maira, M.'          22 ? 
primary 'McArthur, D.'       23 ? 
primary 'Mezna, M.'          24 ? 
primary 'McKinnon, H.'       25 ? 
primary 'Nepravishta, R.'    26 ? 
primary 'Ostermann, N.'      27 ? 
primary 'Pasquali, C.C.'     28 ? 
primary 'Pollock, K.'        29 ? 
primary 'Pugliese, A.'       30 ? 
primary 'Rooney, N.'         31 ? 
primary 'Schmiedeberg, N.'   32 ? 
primary 'Shaw, P.'           33 ? 
primary 'Velez-Vega, C.'     34 ? 
primary 'West, C.'           35 ? 
primary 'West, R.'           36 ? 
primary 'Zecri, F.'          37 ? 
primary 'Taylor, J.B.'       38 ? 
# 
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 'GTPase KRas'                                                     19607.078 1   3.6.5.2 C118S ? ? 
2 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                                        443.201   1   ?       ?     ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                                   24.305    1   ?       ?     ? ? 
4 non-polymer syn 'N-(7-chloro-1,3-benzothiazol-2-yl)-3-hydroxy-benzenesulfonamide' 340.805   1   ?       ?     ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                    62.068    1   ?       ?     ? ? 
6 water       nat water                                                             18.015    166 ?       ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'K-Ras 2,Ki-Ras,c-K-ras,c-Ki-ras' 
# 
_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       
;GGSMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEG
FLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFY
TLVREIRQYRLK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GGSMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEG
FLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFY
TLVREIRQYRLK
;
_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 "GUANOSINE-5'-DIPHOSPHATE"                                        GDP   
3 'MAGNESIUM ION'                                                   MG    
4 'N-(7-chloro-1,3-benzothiazol-2-yl)-3-hydroxy-benzenesulfonamide' A1IK7 
5 1,2-ETHANEDIOL                                                    EDO   
6 water                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   GLY n 
1 3   SER n 
1 4   MET n 
1 5   THR n 
1 6   GLU n 
1 7   TYR n 
1 8   LYS n 
1 9   LEU n 
1 10  VAL n 
1 11  VAL n 
1 12  VAL n 
1 13  GLY n 
1 14  ALA n 
1 15  GLY n 
1 16  GLY n 
1 17  VAL n 
1 18  GLY n 
1 19  LYS n 
1 20  SER n 
1 21  ALA n 
1 22  LEU n 
1 23  THR n 
1 24  ILE n 
1 25  GLN n 
1 26  LEU n 
1 27  ILE n 
1 28  GLN n 
1 29  ASN n 
1 30  HIS n 
1 31  PHE n 
1 32  VAL n 
1 33  ASP n 
1 34  GLU n 
1 35  TYR n 
1 36  ASP n 
1 37  PRO n 
1 38  THR n 
1 39  ILE n 
1 40  GLU n 
1 41  ASP n 
1 42  SER n 
1 43  TYR n 
1 44  ARG n 
1 45  LYS n 
1 46  GLN n 
1 47  VAL n 
1 48  VAL n 
1 49  ILE n 
1 50  ASP n 
1 51  GLY n 
1 52  GLU n 
1 53  THR n 
1 54  CYS n 
1 55  LEU n 
1 56  LEU n 
1 57  ASP n 
1 58  ILE n 
1 59  LEU n 
1 60  ASP n 
1 61  THR n 
1 62  ALA n 
1 63  GLY n 
1 64  GLN n 
1 65  GLU n 
1 66  GLU n 
1 67  TYR n 
1 68  SER n 
1 69  ALA n 
1 70  MET n 
1 71  ARG n 
1 72  ASP n 
1 73  GLN n 
1 74  TYR n 
1 75  MET n 
1 76  ARG n 
1 77  THR n 
1 78  GLY n 
1 79  GLU n 
1 80  GLY n 
1 81  PHE n 
1 82  LEU n 
1 83  CYS n 
1 84  VAL n 
1 85  PHE n 
1 86  ALA n 
1 87  ILE n 
1 88  ASN n 
1 89  ASN n 
1 90  THR n 
1 91  LYS n 
1 92  SER n 
1 93  PHE n 
1 94  GLU n 
1 95  ASP n 
1 96  ILE n 
1 97  HIS n 
1 98  HIS n 
1 99  TYR n 
1 100 ARG n 
1 101 GLU n 
1 102 GLN n 
1 103 ILE n 
1 104 LYS n 
1 105 ARG n 
1 106 VAL n 
1 107 LYS n 
1 108 ASP n 
1 109 SER n 
1 110 GLU n 
1 111 ASP n 
1 112 VAL n 
1 113 PRO n 
1 114 MET n 
1 115 VAL n 
1 116 LEU n 
1 117 VAL n 
1 118 GLY n 
1 119 ASN n 
1 120 LYS n 
1 121 SER n 
1 122 ASP n 
1 123 LEU n 
1 124 PRO n 
1 125 SER n 
1 126 ARG n 
1 127 THR n 
1 128 VAL n 
1 129 ASP n 
1 130 THR n 
1 131 LYS n 
1 132 GLN n 
1 133 ALA n 
1 134 GLN n 
1 135 ASP n 
1 136 LEU n 
1 137 ALA n 
1 138 ARG n 
1 139 SER n 
1 140 TYR n 
1 141 GLY n 
1 142 ILE n 
1 143 PRO n 
1 144 PHE n 
1 145 ILE n 
1 146 GLU n 
1 147 THR n 
1 148 SER n 
1 149 ALA n 
1 150 LYS n 
1 151 THR n 
1 152 ARG n 
1 153 GLN n 
1 154 ARG n 
1 155 VAL n 
1 156 GLU n 
1 157 ASP n 
1 158 ALA n 
1 159 PHE n 
1 160 TYR n 
1 161 THR n 
1 162 LEU n 
1 163 VAL n 
1 164 ARG n 
1 165 GLU n 
1 166 ILE n 
1 167 ARG n 
1 168 GLN n 
1 169 TYR n 
1 170 ARG n 
1 171 LEU n 
1 172 LYS 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                   172 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'KRAS, KRAS2, RASK2' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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 
A1IK7 non-polymer         . 'N-(7-chloro-1,3-benzothiazol-2-yl)-3-hydroxy-benzenesulfonamide' ?                 
'C13 H9 Cl N2 O3 S2' 340.805 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL                                                    'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068  
GDP   'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE"                                        ?                 
'C10 H15 N5 O11 P2'  443.201 
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 
MG    non-polymer         . 'MAGNESIUM ION'                                                   ?                 'Mg 2' 24.305  
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 
TYR   'L-peptide linking' y TYROSINE                                                          ?                 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                            ?                 'C5 H11 N O2' 
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   GLY 2   -1  ?   ?   ?   A . n 
A 1 3   SER 3   0   0   SER SER A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   THR 5   2   2   THR THR A . n 
A 1 6   GLU 6   3   3   GLU GLU A . n 
A 1 7   TYR 7   4   4   TYR TYR A . n 
A 1 8   LYS 8   5   5   LYS LYS A . n 
A 1 9   LEU 9   6   6   LEU LEU A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  VAL 11  8   8   VAL VAL A . n 
A 1 12  VAL 12  9   9   VAL VAL A . n 
A 1 13  GLY 13  10  10  GLY GLY A . n 
A 1 14  ALA 14  11  11  ALA ALA A . n 
A 1 15  GLY 15  12  12  GLY GLY A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  VAL 17  14  14  VAL VAL A . n 
A 1 18  GLY 18  15  15  GLY GLY A . n 
A 1 19  LYS 19  16  16  LYS LYS A . n 
A 1 20  SER 20  17  17  SER SER A . n 
A 1 21  ALA 21  18  18  ALA ALA A . n 
A 1 22  LEU 22  19  19  LEU LEU A . n 
A 1 23  THR 23  20  20  THR THR A . n 
A 1 24  ILE 24  21  21  ILE ILE A . n 
A 1 25  GLN 25  22  22  GLN GLN A . n 
A 1 26  LEU 26  23  23  LEU LEU A . n 
A 1 27  ILE 27  24  24  ILE ILE A . n 
A 1 28  GLN 28  25  25  GLN GLN A . n 
A 1 29  ASN 29  26  26  ASN ASN A . n 
A 1 30  HIS 30  27  27  HIS HIS A . n 
A 1 31  PHE 31  28  28  PHE PHE A . n 
A 1 32  VAL 32  29  29  VAL VAL A . n 
A 1 33  ASP 33  30  30  ASP ASP A . n 
A 1 34  GLU 34  31  31  GLU GLU A . n 
A 1 35  TYR 35  32  32  TYR TYR A . n 
A 1 36  ASP 36  33  33  ASP ASP A . n 
A 1 37  PRO 37  34  34  PRO PRO A . n 
A 1 38  THR 38  35  35  THR THR A . n 
A 1 39  ILE 39  36  36  ILE ILE A . n 
A 1 40  GLU 40  37  37  GLU GLU A . n 
A 1 41  ASP 41  38  38  ASP ASP A . n 
A 1 42  SER 42  39  39  SER SER A . n 
A 1 43  TYR 43  40  40  TYR TYR A . n 
A 1 44  ARG 44  41  41  ARG ARG A . n 
A 1 45  LYS 45  42  42  LYS LYS A . n 
A 1 46  GLN 46  43  43  GLN GLN A . n 
A 1 47  VAL 47  44  44  VAL VAL A . n 
A 1 48  VAL 48  45  45  VAL VAL A . n 
A 1 49  ILE 49  46  46  ILE ILE A . n 
A 1 50  ASP 50  47  47  ASP ASP A . n 
A 1 51  GLY 51  48  48  GLY GLY A . n 
A 1 52  GLU 52  49  49  GLU GLU A . n 
A 1 53  THR 53  50  50  THR THR A . n 
A 1 54  CYS 54  51  51  CYS CYS A . n 
A 1 55  LEU 55  52  52  LEU LEU A . n 
A 1 56  LEU 56  53  53  LEU LEU A . n 
A 1 57  ASP 57  54  54  ASP ASP A . n 
A 1 58  ILE 58  55  55  ILE ILE A . n 
A 1 59  LEU 59  56  56  LEU LEU A . n 
A 1 60  ASP 60  57  57  ASP ASP A . n 
A 1 61  THR 61  58  58  THR THR A . n 
A 1 62  ALA 62  59  59  ALA ALA A . n 
A 1 63  GLY 63  60  60  GLY GLY A . n 
A 1 64  GLN 64  61  61  GLN GLN A . n 
A 1 65  GLU 65  62  62  GLU GLU A . n 
A 1 66  GLU 66  63  63  GLU GLU A . n 
A 1 67  TYR 67  64  64  TYR TYR A . n 
A 1 68  SER 68  65  65  SER SER A . n 
A 1 69  ALA 69  66  66  ALA ALA A . n 
A 1 70  MET 70  67  67  MET MET A . n 
A 1 71  ARG 71  68  68  ARG ARG A . n 
A 1 72  ASP 72  69  69  ASP ASP A . n 
A 1 73  GLN 73  70  70  GLN GLN A . n 
A 1 74  TYR 74  71  71  TYR TYR A . n 
A 1 75  MET 75  72  72  MET MET A . n 
A 1 76  ARG 76  73  73  ARG ARG A . n 
A 1 77  THR 77  74  74  THR THR A . n 
A 1 78  GLY 78  75  75  GLY GLY A . n 
A 1 79  GLU 79  76  76  GLU GLU A . n 
A 1 80  GLY 80  77  77  GLY GLY A . n 
A 1 81  PHE 81  78  78  PHE PHE A . n 
A 1 82  LEU 82  79  79  LEU LEU A . n 
A 1 83  CYS 83  80  80  CYS CYS A . n 
A 1 84  VAL 84  81  81  VAL VAL A . n 
A 1 85  PHE 85  82  82  PHE PHE A . n 
A 1 86  ALA 86  83  83  ALA ALA A . n 
A 1 87  ILE 87  84  84  ILE ILE A . n 
A 1 88  ASN 88  85  85  ASN ASN A . n 
A 1 89  ASN 89  86  86  ASN ASN A . n 
A 1 90  THR 90  87  87  THR THR A . n 
A 1 91  LYS 91  88  88  LYS LYS A . n 
A 1 92  SER 92  89  89  SER SER A . n 
A 1 93  PHE 93  90  90  PHE PHE A . n 
A 1 94  GLU 94  91  91  GLU GLU A . n 
A 1 95  ASP 95  92  92  ASP ASP A . n 
A 1 96  ILE 96  93  93  ILE ILE A . n 
A 1 97  HIS 97  94  94  HIS HIS A . n 
A 1 98  HIS 98  95  95  HIS HIS A . n 
A 1 99  TYR 99  96  96  TYR TYR A . n 
A 1 100 ARG 100 97  97  ARG ARG A . n 
A 1 101 GLU 101 98  98  GLU GLU A . n 
A 1 102 GLN 102 99  99  GLN GLN A . n 
A 1 103 ILE 103 100 100 ILE ILE A . n 
A 1 104 LYS 104 101 101 LYS LYS A . n 
A 1 105 ARG 105 102 102 ARG ARG A . n 
A 1 106 VAL 106 103 103 VAL VAL A . n 
A 1 107 LYS 107 104 104 LYS LYS A . n 
A 1 108 ASP 108 105 105 ASP ASP A . n 
A 1 109 SER 109 106 106 SER SER A . n 
A 1 110 GLU 110 107 107 GLU GLU A . n 
A 1 111 ASP 111 108 108 ASP ASP A . n 
A 1 112 VAL 112 109 109 VAL VAL A . n 
A 1 113 PRO 113 110 110 PRO PRO A . n 
A 1 114 MET 114 111 111 MET MET A . n 
A 1 115 VAL 115 112 112 VAL VAL A . n 
A 1 116 LEU 116 113 113 LEU LEU A . n 
A 1 117 VAL 117 114 114 VAL VAL A . n 
A 1 118 GLY 118 115 115 GLY GLY A . n 
A 1 119 ASN 119 116 116 ASN ASN A . n 
A 1 120 LYS 120 117 117 LYS LYS A . n 
A 1 121 SER 121 118 118 SER SER A . n 
A 1 122 ASP 122 119 119 ASP ASP A . n 
A 1 123 LEU 123 120 120 LEU LEU A . n 
A 1 124 PRO 124 121 121 PRO PRO A . n 
A 1 125 SER 125 122 122 SER SER A . n 
A 1 126 ARG 126 123 123 ARG ARG A . n 
A 1 127 THR 127 124 124 THR THR A . n 
A 1 128 VAL 128 125 125 VAL VAL A . n 
A 1 129 ASP 129 126 126 ASP ASP A . n 
A 1 130 THR 130 127 127 THR THR A . n 
A 1 131 LYS 131 128 128 LYS LYS A . n 
A 1 132 GLN 132 129 129 GLN GLN A . n 
A 1 133 ALA 133 130 130 ALA ALA A . n 
A 1 134 GLN 134 131 131 GLN GLN A . n 
A 1 135 ASP 135 132 132 ASP ASP A . n 
A 1 136 LEU 136 133 133 LEU LEU A . n 
A 1 137 ALA 137 134 134 ALA ALA A . n 
A 1 138 ARG 138 135 135 ARG ARG A . n 
A 1 139 SER 139 136 136 SER SER A . n 
A 1 140 TYR 140 137 137 TYR TYR A . n 
A 1 141 GLY 141 138 138 GLY GLY A . n 
A 1 142 ILE 142 139 139 ILE ILE A . n 
A 1 143 PRO 143 140 140 PRO PRO A . n 
A 1 144 PHE 144 141 141 PHE PHE A . n 
A 1 145 ILE 145 142 142 ILE ILE A . n 
A 1 146 GLU 146 143 143 GLU GLU A . n 
A 1 147 THR 147 144 144 THR THR A . n 
A 1 148 SER 148 145 145 SER SER A . n 
A 1 149 ALA 149 146 146 ALA ALA A . n 
A 1 150 LYS 150 147 147 LYS LYS A . n 
A 1 151 THR 151 148 148 THR THR A . n 
A 1 152 ARG 152 149 149 ARG ARG A . n 
A 1 153 GLN 153 150 150 GLN GLN A . n 
A 1 154 ARG 154 151 151 ARG ARG A . n 
A 1 155 VAL 155 152 152 VAL VAL A . n 
A 1 156 GLU 156 153 153 GLU GLU A . n 
A 1 157 ASP 157 154 154 ASP ASP A . n 
A 1 158 ALA 158 155 155 ALA ALA A . n 
A 1 159 PHE 159 156 156 PHE PHE A . n 
A 1 160 TYR 160 157 157 TYR TYR A . n 
A 1 161 THR 161 158 158 THR THR A . n 
A 1 162 LEU 162 159 159 LEU LEU A . n 
A 1 163 VAL 163 160 160 VAL VAL A . n 
A 1 164 ARG 164 161 161 ARG ARG A . n 
A 1 165 GLU 165 162 162 GLU GLU A . n 
A 1 166 ILE 166 163 163 ILE ILE A . n 
A 1 167 ARG 167 164 164 ARG ARG A . n 
A 1 168 GLN 168 165 165 GLN GLN A . n 
A 1 169 TYR 169 166 166 TYR TYR A . n 
A 1 170 ARG 170 167 167 ARG ARG A . n 
A 1 171 LEU 171 168 168 LEU LEU A . n 
A 1 172 LYS 172 169 169 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 GDP   1   201 1000 GDP   GDP A . 
C 3 MG    1   202 1001 MG    MG  A . 
D 4 A1IK7 1   203 1    A1IK7 DRG A . 
E 5 EDO   1   204 1    EDO   EDO A . 
F 6 HOH   1   301 144  HOH   HOH A . 
F 6 HOH   2   302 330  HOH   HOH A . 
F 6 HOH   3   303 168  HOH   HOH A . 
F 6 HOH   4   304 255  HOH   HOH A . 
F 6 HOH   5   305 7    HOH   HOH A . 
F 6 HOH   6   306 252  HOH   HOH A . 
F 6 HOH   7   307 6    HOH   HOH A . 
F 6 HOH   8   308 163  HOH   HOH A . 
F 6 HOH   9   309 324  HOH   HOH A . 
F 6 HOH   10  310 266  HOH   HOH A . 
F 6 HOH   11  311 136  HOH   HOH A . 
F 6 HOH   12  312 64   HOH   HOH A . 
F 6 HOH   13  313 48   HOH   HOH A . 
F 6 HOH   14  314 195  HOH   HOH A . 
F 6 HOH   15  315 49   HOH   HOH A . 
F 6 HOH   16  316 340  HOH   HOH A . 
F 6 HOH   17  317 3    HOH   HOH A . 
F 6 HOH   18  318 263  HOH   HOH A . 
F 6 HOH   19  319 336  HOH   HOH A . 
F 6 HOH   20  320 9    HOH   HOH A . 
F 6 HOH   21  321 217  HOH   HOH A . 
F 6 HOH   22  322 243  HOH   HOH A . 
F 6 HOH   23  323 134  HOH   HOH A . 
F 6 HOH   24  324 139  HOH   HOH A . 
F 6 HOH   25  325 212  HOH   HOH A . 
F 6 HOH   26  326 25   HOH   HOH A . 
F 6 HOH   27  327 135  HOH   HOH A . 
F 6 HOH   28  328 30   HOH   HOH A . 
F 6 HOH   29  329 242  HOH   HOH A . 
F 6 HOH   30  330 133  HOH   HOH A . 
F 6 HOH   31  331 148  HOH   HOH A . 
F 6 HOH   32  332 334  HOH   HOH A . 
F 6 HOH   33  333 154  HOH   HOH A . 
F 6 HOH   34  334 249  HOH   HOH A . 
F 6 HOH   35  335 231  HOH   HOH A . 
F 6 HOH   36  336 269  HOH   HOH A . 
F 6 HOH   37  337 44   HOH   HOH A . 
F 6 HOH   38  338 182  HOH   HOH A . 
F 6 HOH   39  339 259  HOH   HOH A . 
F 6 HOH   40  340 88   HOH   HOH A . 
F 6 HOH   41  341 80   HOH   HOH A . 
F 6 HOH   42  342 190  HOH   HOH A . 
F 6 HOH   43  343 151  HOH   HOH A . 
F 6 HOH   44  344 143  HOH   HOH A . 
F 6 HOH   45  345 175  HOH   HOH A . 
F 6 HOH   46  346 209  HOH   HOH A . 
F 6 HOH   47  347 132  HOH   HOH A . 
F 6 HOH   48  348 206  HOH   HOH A . 
F 6 HOH   49  349 233  HOH   HOH A . 
F 6 HOH   50  350 16   HOH   HOH A . 
F 6 HOH   51  351 214  HOH   HOH A . 
F 6 HOH   52  352 165  HOH   HOH A . 
F 6 HOH   53  353 253  HOH   HOH A . 
F 6 HOH   54  354 77   HOH   HOH A . 
F 6 HOH   55  355 302  HOH   HOH A . 
F 6 HOH   56  356 10   HOH   HOH A . 
F 6 HOH   57  357 170  HOH   HOH A . 
F 6 HOH   58  358 160  HOH   HOH A . 
F 6 HOH   59  359 31   HOH   HOH A . 
F 6 HOH   60  360 311  HOH   HOH A . 
F 6 HOH   61  361 156  HOH   HOH A . 
F 6 HOH   62  362 42   HOH   HOH A . 
F 6 HOH   63  363 68   HOH   HOH A . 
F 6 HOH   64  364 8    HOH   HOH A . 
F 6 HOH   65  365 260  HOH   HOH A . 
F 6 HOH   66  366 241  HOH   HOH A . 
F 6 HOH   67  367 147  HOH   HOH A . 
F 6 HOH   68  368 188  HOH   HOH A . 
F 6 HOH   69  369 155  HOH   HOH A . 
F 6 HOH   70  370 1    HOH   HOH A . 
F 6 HOH   71  371 171  HOH   HOH A . 
F 6 HOH   72  372 236  HOH   HOH A . 
F 6 HOH   73  373 17   HOH   HOH A . 
F 6 HOH   74  374 323  HOH   HOH A . 
F 6 HOH   75  375 267  HOH   HOH A . 
F 6 HOH   76  376 142  HOH   HOH A . 
F 6 HOH   77  377 161  HOH   HOH A . 
F 6 HOH   78  378 140  HOH   HOH A . 
F 6 HOH   79  379 40   HOH   HOH A . 
F 6 HOH   80  380 58   HOH   HOH A . 
F 6 HOH   81  381 205  HOH   HOH A . 
F 6 HOH   82  382 202  HOH   HOH A . 
F 6 HOH   83  383 207  HOH   HOH A . 
F 6 HOH   84  384 250  HOH   HOH A . 
F 6 HOH   85  385 29   HOH   HOH A . 
F 6 HOH   86  386 184  HOH   HOH A . 
F 6 HOH   87  387 248  HOH   HOH A . 
F 6 HOH   88  388 279  HOH   HOH A . 
F 6 HOH   89  389 166  HOH   HOH A . 
F 6 HOH   90  390 335  HOH   HOH A . 
F 6 HOH   91  391 19   HOH   HOH A . 
F 6 HOH   92  392 338  HOH   HOH A . 
F 6 HOH   93  393 185  HOH   HOH A . 
F 6 HOH   94  394 39   HOH   HOH A . 
F 6 HOH   95  395 152  HOH   HOH A . 
F 6 HOH   96  396 157  HOH   HOH A . 
F 6 HOH   97  397 149  HOH   HOH A . 
F 6 HOH   98  398 240  HOH   HOH A . 
F 6 HOH   99  399 297  HOH   HOH A . 
F 6 HOH   100 400 167  HOH   HOH A . 
F 6 HOH   101 401 20   HOH   HOH A . 
F 6 HOH   102 402 36   HOH   HOH A . 
F 6 HOH   103 403 59   HOH   HOH A . 
F 6 HOH   104 404 193  HOH   HOH A . 
F 6 HOH   105 405 191  HOH   HOH A . 
F 6 HOH   106 406 308  HOH   HOH A . 
F 6 HOH   107 407 200  HOH   HOH A . 
F 6 HOH   108 408 254  HOH   HOH A . 
F 6 HOH   109 409 177  HOH   HOH A . 
F 6 HOH   110 410 246  HOH   HOH A . 
F 6 HOH   111 411 194  HOH   HOH A . 
F 6 HOH   112 412 222  HOH   HOH A . 
F 6 HOH   113 413 244  HOH   HOH A . 
F 6 HOH   114 414 197  HOH   HOH A . 
F 6 HOH   115 415 257  HOH   HOH A . 
F 6 HOH   116 416 173  HOH   HOH A . 
F 6 HOH   117 417 337  HOH   HOH A . 
F 6 HOH   118 418 238  HOH   HOH A . 
F 6 HOH   119 419 145  HOH   HOH A . 
F 6 HOH   120 420 179  HOH   HOH A . 
F 6 HOH   121 421 153  HOH   HOH A . 
F 6 HOH   122 422 283  HOH   HOH A . 
F 6 HOH   123 423 215  HOH   HOH A . 
F 6 HOH   124 424 176  HOH   HOH A . 
F 6 HOH   125 425 34   HOH   HOH A . 
F 6 HOH   126 426 183  HOH   HOH A . 
F 6 HOH   127 427 33   HOH   HOH A . 
F 6 HOH   128 428 35   HOH   HOH A . 
F 6 HOH   129 429 339  HOH   HOH A . 
F 6 HOH   130 430 146  HOH   HOH A . 
F 6 HOH   131 431 313  HOH   HOH A . 
F 6 HOH   132 432 303  HOH   HOH A . 
F 6 HOH   133 433 199  HOH   HOH A . 
F 6 HOH   134 434 284  HOH   HOH A . 
F 6 HOH   135 435 211  HOH   HOH A . 
F 6 HOH   136 436 234  HOH   HOH A . 
F 6 HOH   137 437 282  HOH   HOH A . 
F 6 HOH   138 438 78   HOH   HOH A . 
F 6 HOH   139 439 304  HOH   HOH A . 
F 6 HOH   140 440 315  HOH   HOH A . 
F 6 HOH   141 441 291  HOH   HOH A . 
F 6 HOH   142 442 196  HOH   HOH A . 
F 6 HOH   143 443 322  HOH   HOH A . 
F 6 HOH   144 444 174  HOH   HOH A . 
F 6 HOH   145 445 172  HOH   HOH A . 
F 6 HOH   146 446 216  HOH   HOH A . 
F 6 HOH   147 447 312  HOH   HOH A . 
F 6 HOH   148 448 208  HOH   HOH A . 
F 6 HOH   149 449 326  HOH   HOH A . 
F 6 HOH   150 450 321  HOH   HOH A . 
F 6 HOH   151 451 318  HOH   HOH A . 
F 6 HOH   152 452 251  HOH   HOH A . 
F 6 HOH   153 453 309  HOH   HOH A . 
F 6 HOH   154 454 314  HOH   HOH A . 
F 6 HOH   155 455 223  HOH   HOH A . 
F 6 HOH   156 456 271  HOH   HOH A . 
F 6 HOH   157 457 220  HOH   HOH A . 
F 6 HOH   158 458 333  HOH   HOH A . 
F 6 HOH   159 459 307  HOH   HOH A . 
F 6 HOH   160 460 227  HOH   HOH A . 
F 6 HOH   161 461 258  HOH   HOH A . 
F 6 HOH   162 462 329  HOH   HOH A . 
F 6 HOH   163 463 328  HOH   HOH A . 
F 6 HOH   164 464 204  HOH   HOH A . 
F 6 HOH   165 465 332  HOH   HOH A . 
F 6 HOH   166 466 306  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        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0258 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? xia2        ? ? ? 0.3.6.3  2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.22     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GGT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.340 
_cell.length_a_esd                 ? 
_cell.length_b                     40.870 
_cell.length_b_esd                 ? 
_cell.length_c                     112.060 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9GGT 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9GGT 
_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             2.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.59 
_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               0.325 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.2 
_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    '25% PEG 8000, 300 mM LiCl, 100 mM bis-tris propane' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_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 PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-08-12 
_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   0.9163 
_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                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9163 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          9.206 
_reflns.entry_id                                       9GGT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.710 
_reflns.d_resolution_low                               37.340 
_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                                     19159 
_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                           99.500 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.100 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.600 
_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                                0.141 
_reflns.pdbx_Rpim_I_all                                0.057 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       116422 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.114 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_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 
_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 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_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 
1.710 1.750  ? 2.400  ? ? ? ? 1373 ? ? ? ? ? ? ? ? ? ? ? 6.100 ? ? ? 0.902 0.358 ? 1 1 ? ? ? 99.800 ? 0.727 ? ? ? ? ? ? ? ? ? 
7.650 37.340 ? 36.300 ? ? ? ? 270  ? ? ? ? ? ? ? ? ? ? ? 5.600 ? ? ? 0.047 0.020 ? 2 1 ? ? ? 99.100 ? 0.041 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -1.0100 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            -0.6800 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            1.6900 
_refine.B_iso_max                                48.340 
_refine.B_iso_mean                               19.0720 
_refine.B_iso_min                                7.350 
_refine.correlation_coeff_Fo_to_Fc               0.9430 
_refine.correlation_coeff_Fo_to_Fc_free          0.9110 
_refine.details                                  'U VALUES      : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9GGT 
_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                            1.7100 
_refine.ls_d_res_low                             35.4500 
_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                     18180 
_refine.ls_number_reflns_R_free                  931 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.3200 
_refine.ls_percent_reflns_R_free                 4.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2099 
_refine.ls_R_factor_R_free                       0.2628 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2073 
_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                    MASK 
_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                          0.000 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.1330 
_refine.pdbx_overall_ESU_R_Free                  0.1360 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_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                 ? 
_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                             7.0420 
_refine.overall_SU_ML                            0.1020 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.7100 
_refine_hist.d_res_low                        35.4500 
_refine_hist.number_atoms_solvent             166 
_refine_hist.number_atoms_total               1588 
_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       170 
_refine_hist.pdbx_B_iso_mean_ligand           23.11 
_refine_hist.pdbx_B_iso_mean_solvent          26.70 
_refine_hist.pdbx_number_atoms_protein        1368 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_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' ? 0.017  0.013  1454 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.035  0.018  1316 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 2.005  1.710  1971 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 2.385  1.616  3049 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 5.147  5.000  171  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 33.352 22.143 84   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 15.217 15.000 256  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 19.284 15.000 12   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.128  0.200  189  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  1617 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  313  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 0.926  1.124  684  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 0.926  1.124  683  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 1.513  1.679  855  ? r_mcangle_it           ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.7100 
_refine_ls_shell.d_res_low                        1.7540 
_refine_ls_shell.number_reflns_all                1368 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             71 
_refine_ls_shell.number_reflns_R_work             1297 
_refine_ls_shell.percent_reflns_obs               99.8500 
_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                  0.2890 
_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   20 
_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                  0.3770 
# 
_struct.entry_id                     9GGT 
_struct.title                        'Human KRas4A (GDP) in complex with compound 8' 
_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        9GGT 
_struct_keywords.text            'RAS, GTPase, inhibitor, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RASK_HUMAN 
_struct_ref.pdbx_db_accession          P01116 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLV
REIRQYRLK
;
_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              9GGT 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 172 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P01116 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  169 
_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       169 
# 
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 9GGT GLY A 1   ? UNP P01116 ?   ?   'expression tag'      -2  1 
1 9GGT GLY A 2   ? UNP P01116 ?   ?   'expression tag'      -1  2 
1 9GGT SER A 3   ? UNP P01116 ?   ?   'expression tag'      0   3 
1 9GGT SER A 121 ? UNP P01116 CYS 118 'engineered mutation' 118 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1010 ? 
1 MORE         -18  ? 
1 'SSA (A^2)'  8430 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 GLY A 18  ? ASN A 29  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2 AA2 SER A 68  ? GLY A 78  ? SER A 65  GLY A 75  1 ? 11 
HELX_P HELX_P3 AA3 ASN A 89  ? ASP A 108 ? ASN A 86  ASP A 105 1 ? 20 
HELX_P HELX_P4 AA4 ASP A 129 ? GLY A 141 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P5 AA5 ARG A 154 ? LEU A 171 ? ARG A 151 LEU A 168 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A SER 20 OG  ? ? ? 1_555 C MG  . MG ? ? A SER 17  A MG  202 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc2 metalc ? ? B GDP .  O1B ? ? ? 1_555 C MG  . MG ? ? A GDP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.211 ? ? 
metalc3 metalc ? ? C MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 305 1_555 ? ? ? ? ? ? ? 2.250 ? ? 
metalc4 metalc ? ? C MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 307 1_555 ? ? ? ? ? ? ? 1.994 ? ? 
metalc5 metalc ? ? C MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 360 1_555 ? ? ? ? ? ? ? 1.860 ? ? 
metalc6 metalc ? ? C MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 364 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O1B ? B GDP . ? A GDP 201 ? 1_555 89.0  ? 
2  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 305 ? 1_555 89.3  ? 
3  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 305 ? 1_555 82.6  ? 
4  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 307 ? 1_555 83.3  ? 
5  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 307 ? 1_555 92.9  ? 
6  O   ? F HOH .  ? A HOH 305 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 307 ? 1_555 171.5 ? 
7  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 360 ? 1_555 177.2 ? 
8  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 360 ? 1_555 90.7  ? 
9  O   ? F HOH .  ? A HOH 305 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 360 ? 1_555 93.4  ? 
10 O   ? F HOH .  ? A HOH 307 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 360 ? 1_555 93.9  ? 
11 OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 364 ? 1_555 92.3  ? 
12 O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 364 ? 1_555 166.6 ? 
13 O   ? F HOH .  ? A HOH 305 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 364 ? 1_555 84.1  ? 
14 O   ? F HOH .  ? A HOH 307 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 364 ? 1_555 100.5 ? 
15 O   ? F HOH .  ? A HOH 360 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 364 ? 1_555 88.6  ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   6 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? 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 ASP A 41  ? ILE A 49  ? ASP A 38  ILE A 46  
AA1 2 GLU A 52  ? ASP A 60  ? GLU A 49  ASP A 57  
AA1 3 THR A 5   ? VAL A 12  ? THR A 2   VAL A 9   
AA1 4 GLY A 80  ? ALA A 86  ? GLY A 77  ALA A 83  
AA1 5 MET A 114 ? ASN A 119 ? MET A 111 ASN A 116 
AA1 6 PHE A 144 ? GLU A 146 ? PHE A 141 GLU A 143 
# 
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 N VAL A 47  ? N VAL A 44  O CYS A 54  ? O CYS A 51  
AA1 2 3 O ASP A 57  ? O ASP A 54  N LEU A 9   ? N LEU A 6   
AA1 3 4 N VAL A 10  ? N VAL A 7   O LEU A 82  ? O LEU A 79  
AA1 4 5 N CYS A 83  ? N CYS A 80  O VAL A 115 ? O VAL A 112 
AA1 5 6 N LEU A 116 ? N LEU A 113 O ILE A 145 ? O ILE A 142 
# 
_pdbx_entry_details.entry_id                   9GGT 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              68 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              68 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              68 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                126.61 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            6.31 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ALA 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     59 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -99.53 
_pdbx_validate_torsion.psi             -83.92 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -1.1418 
_pdbx_refine_tls.origin_y         18.2656 
_pdbx_refine_tls.origin_z         11.9402 
_pdbx_refine_tls.T[1][1]          0.0183 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0015 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0069 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0150 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0088 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0167 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.4305 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0135 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.1998 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.7992 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.1329 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.9731 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0197 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1443 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0746 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0498 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0040 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0512 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0783 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0343 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0237 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
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 ? ? A 1 ? ? ? A 9999 ? ? ? 
2 'X-RAY DIFFRACTION' 1 ? ? L 1 ? ? ? L 9999 ? ? ? 
3 'X-RAY DIFFRACTION' 1 ? ? W 1 ? ? ? W 9999 ? ? ? 
4 'X-RAY DIFFRACTION' 1 ? ? X 1 ? ? ? X 9999 ? ? ? 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       466 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.81 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY -2 ? A GLY 1 
2 1 Y 1 A GLY -1 ? A GLY 2 
# 
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 
A1IK7 NAL    N  Y N 1   
A1IK7 CAM    C  Y N 2   
A1IK7 CAN    C  Y N 3   
A1IK7 CAO    C  Y N 4   
A1IK7 CAP    C  Y N 5   
A1IK7 CAQ    C  Y N 6   
A1IK7 CLAR   CL N N 7   
A1IK7 CAT    C  Y N 8   
A1IK7 SAU    S  Y N 9   
A1IK7 CAK    C  Y N 10  
A1IK7 NAJ    N  N N 11  
A1IK7 SAB    S  N N 12  
A1IK7 OAA    O  N N 13  
A1IK7 OAC    O  N N 14  
A1IK7 CAI    C  Y N 15  
A1IK7 CAS    C  Y N 16  
A1IK7 CAE    C  Y N 17  
A1IK7 OAD    O  N N 18  
A1IK7 CAF    C  Y N 19  
A1IK7 CAG    C  Y N 20  
A1IK7 CAH    C  Y N 21  
A1IK7 H1     H  N N 22  
A1IK7 H2     H  N N 23  
A1IK7 H3     H  N N 24  
A1IK7 H4     H  N N 25  
A1IK7 H5     H  N N 26  
A1IK7 H6     H  N N 27  
A1IK7 H7     H  N N 28  
A1IK7 H8     H  N N 29  
A1IK7 H9     H  N N 30  
ALA   N      N  N N 31  
ALA   CA     C  N S 32  
ALA   C      C  N N 33  
ALA   O      O  N N 34  
ALA   CB     C  N N 35  
ALA   OXT    O  N N 36  
ALA   H      H  N N 37  
ALA   H2     H  N N 38  
ALA   HA     H  N N 39  
ALA   HB1    H  N N 40  
ALA   HB2    H  N N 41  
ALA   HB3    H  N N 42  
ALA   HXT    H  N N 43  
ARG   N      N  N N 44  
ARG   CA     C  N S 45  
ARG   C      C  N N 46  
ARG   O      O  N N 47  
ARG   CB     C  N N 48  
ARG   CG     C  N N 49  
ARG   CD     C  N N 50  
ARG   NE     N  N N 51  
ARG   CZ     C  N N 52  
ARG   NH1    N  N N 53  
ARG   NH2    N  N N 54  
ARG   OXT    O  N N 55  
ARG   H      H  N N 56  
ARG   H2     H  N N 57  
ARG   HA     H  N N 58  
ARG   HB2    H  N N 59  
ARG   HB3    H  N N 60  
ARG   HG2    H  N N 61  
ARG   HG3    H  N N 62  
ARG   HD2    H  N N 63  
ARG   HD3    H  N N 64  
ARG   HE     H  N N 65  
ARG   HH11   H  N N 66  
ARG   HH12   H  N N 67  
ARG   HH21   H  N N 68  
ARG   HH22   H  N N 69  
ARG   HXT    H  N N 70  
ASN   N      N  N N 71  
ASN   CA     C  N S 72  
ASN   C      C  N N 73  
ASN   O      O  N N 74  
ASN   CB     C  N N 75  
ASN   CG     C  N N 76  
ASN   OD1    O  N N 77  
ASN   ND2    N  N N 78  
ASN   OXT    O  N N 79  
ASN   H      H  N N 80  
ASN   H2     H  N N 81  
ASN   HA     H  N N 82  
ASN   HB2    H  N N 83  
ASN   HB3    H  N N 84  
ASN   HD21   H  N N 85  
ASN   HD22   H  N N 86  
ASN   HXT    H  N N 87  
ASP   N      N  N N 88  
ASP   CA     C  N S 89  
ASP   C      C  N N 90  
ASP   O      O  N N 91  
ASP   CB     C  N N 92  
ASP   CG     C  N N 93  
ASP   OD1    O  N N 94  
ASP   OD2    O  N N 95  
ASP   OXT    O  N N 96  
ASP   H      H  N N 97  
ASP   H2     H  N N 98  
ASP   HA     H  N N 99  
ASP   HB2    H  N N 100 
ASP   HB3    H  N N 101 
ASP   HD2    H  N N 102 
ASP   HXT    H  N N 103 
CYS   N      N  N N 104 
CYS   CA     C  N R 105 
CYS   C      C  N N 106 
CYS   O      O  N N 107 
CYS   CB     C  N N 108 
CYS   SG     S  N N 109 
CYS   OXT    O  N N 110 
CYS   H      H  N N 111 
CYS   H2     H  N N 112 
CYS   HA     H  N N 113 
CYS   HB2    H  N N 114 
CYS   HB3    H  N N 115 
CYS   HG     H  N N 116 
CYS   HXT    H  N N 117 
EDO   C1     C  N N 118 
EDO   O1     O  N N 119 
EDO   C2     C  N N 120 
EDO   O2     O  N N 121 
EDO   H11    H  N N 122 
EDO   H12    H  N N 123 
EDO   HO1    H  N N 124 
EDO   H21    H  N N 125 
EDO   H22    H  N N 126 
EDO   HO2    H  N N 127 
GDP   PB     P  N N 128 
GDP   O1B    O  N N 129 
GDP   O2B    O  N N 130 
GDP   O3B    O  N N 131 
GDP   O3A    O  N N 132 
GDP   PA     P  N N 133 
GDP   O1A    O  N N 134 
GDP   O2A    O  N N 135 
GDP   "O5'"  O  N N 136 
GDP   "C5'"  C  N N 137 
GDP   "C4'"  C  N R 138 
GDP   "O4'"  O  N N 139 
GDP   "C3'"  C  N S 140 
GDP   "O3'"  O  N N 141 
GDP   "C2'"  C  N R 142 
GDP   "O2'"  O  N N 143 
GDP   "C1'"  C  N R 144 
GDP   N9     N  Y N 145 
GDP   C8     C  Y N 146 
GDP   N7     N  Y N 147 
GDP   C5     C  Y N 148 
GDP   C6     C  N N 149 
GDP   O6     O  N N 150 
GDP   N1     N  N N 151 
GDP   C2     C  N N 152 
GDP   N2     N  N N 153 
GDP   N3     N  N N 154 
GDP   C4     C  Y N 155 
GDP   HOB2   H  N N 156 
GDP   HOB3   H  N N 157 
GDP   HOA2   H  N N 158 
GDP   "H5'"  H  N N 159 
GDP   "H5''" H  N N 160 
GDP   "H4'"  H  N N 161 
GDP   "H3'"  H  N N 162 
GDP   "HO3'" H  N N 163 
GDP   "H2'"  H  N N 164 
GDP   "HO2'" H  N N 165 
GDP   "H1'"  H  N N 166 
GDP   H8     H  N N 167 
GDP   HN1    H  N N 168 
GDP   HN21   H  N N 169 
GDP   HN22   H  N N 170 
GLN   N      N  N N 171 
GLN   CA     C  N S 172 
GLN   C      C  N N 173 
GLN   O      O  N N 174 
GLN   CB     C  N N 175 
GLN   CG     C  N N 176 
GLN   CD     C  N N 177 
GLN   OE1    O  N N 178 
GLN   NE2    N  N N 179 
GLN   OXT    O  N N 180 
GLN   H      H  N N 181 
GLN   H2     H  N N 182 
GLN   HA     H  N N 183 
GLN   HB2    H  N N 184 
GLN   HB3    H  N N 185 
GLN   HG2    H  N N 186 
GLN   HG3    H  N N 187 
GLN   HE21   H  N N 188 
GLN   HE22   H  N N 189 
GLN   HXT    H  N N 190 
GLU   N      N  N N 191 
GLU   CA     C  N S 192 
GLU   C      C  N N 193 
GLU   O      O  N N 194 
GLU   CB     C  N N 195 
GLU   CG     C  N N 196 
GLU   CD     C  N N 197 
GLU   OE1    O  N N 198 
GLU   OE2    O  N N 199 
GLU   OXT    O  N N 200 
GLU   H      H  N N 201 
GLU   H2     H  N N 202 
GLU   HA     H  N N 203 
GLU   HB2    H  N N 204 
GLU   HB3    H  N N 205 
GLU   HG2    H  N N 206 
GLU   HG3    H  N N 207 
GLU   HE2    H  N N 208 
GLU   HXT    H  N N 209 
GLY   N      N  N N 210 
GLY   CA     C  N N 211 
GLY   C      C  N N 212 
GLY   O      O  N N 213 
GLY   OXT    O  N N 214 
GLY   H      H  N N 215 
GLY   H2     H  N N 216 
GLY   HA2    H  N N 217 
GLY   HA3    H  N N 218 
GLY   HXT    H  N N 219 
HIS   N      N  N N 220 
HIS   CA     C  N S 221 
HIS   C      C  N N 222 
HIS   O      O  N N 223 
HIS   CB     C  N N 224 
HIS   CG     C  Y N 225 
HIS   ND1    N  Y N 226 
HIS   CD2    C  Y N 227 
HIS   CE1    C  Y N 228 
HIS   NE2    N  Y N 229 
HIS   OXT    O  N N 230 
HIS   H      H  N N 231 
HIS   H2     H  N N 232 
HIS   HA     H  N N 233 
HIS   HB2    H  N N 234 
HIS   HB3    H  N N 235 
HIS   HD1    H  N N 236 
HIS   HD2    H  N N 237 
HIS   HE1    H  N N 238 
HIS   HE2    H  N N 239 
HIS   HXT    H  N N 240 
HOH   O      O  N N 241 
HOH   H1     H  N N 242 
HOH   H2     H  N N 243 
ILE   N      N  N N 244 
ILE   CA     C  N S 245 
ILE   C      C  N N 246 
ILE   O      O  N N 247 
ILE   CB     C  N S 248 
ILE   CG1    C  N N 249 
ILE   CG2    C  N N 250 
ILE   CD1    C  N N 251 
ILE   OXT    O  N N 252 
ILE   H      H  N N 253 
ILE   H2     H  N N 254 
ILE   HA     H  N N 255 
ILE   HB     H  N N 256 
ILE   HG12   H  N N 257 
ILE   HG13   H  N N 258 
ILE   HG21   H  N N 259 
ILE   HG22   H  N N 260 
ILE   HG23   H  N N 261 
ILE   HD11   H  N N 262 
ILE   HD12   H  N N 263 
ILE   HD13   H  N N 264 
ILE   HXT    H  N N 265 
LEU   N      N  N N 266 
LEU   CA     C  N S 267 
LEU   C      C  N N 268 
LEU   O      O  N N 269 
LEU   CB     C  N N 270 
LEU   CG     C  N N 271 
LEU   CD1    C  N N 272 
LEU   CD2    C  N N 273 
LEU   OXT    O  N N 274 
LEU   H      H  N N 275 
LEU   H2     H  N N 276 
LEU   HA     H  N N 277 
LEU   HB2    H  N N 278 
LEU   HB3    H  N N 279 
LEU   HG     H  N N 280 
LEU   HD11   H  N N 281 
LEU   HD12   H  N N 282 
LEU   HD13   H  N N 283 
LEU   HD21   H  N N 284 
LEU   HD22   H  N N 285 
LEU   HD23   H  N N 286 
LEU   HXT    H  N N 287 
LYS   N      N  N N 288 
LYS   CA     C  N S 289 
LYS   C      C  N N 290 
LYS   O      O  N N 291 
LYS   CB     C  N N 292 
LYS   CG     C  N N 293 
LYS   CD     C  N N 294 
LYS   CE     C  N N 295 
LYS   NZ     N  N N 296 
LYS   OXT    O  N N 297 
LYS   H      H  N N 298 
LYS   H2     H  N N 299 
LYS   HA     H  N N 300 
LYS   HB2    H  N N 301 
LYS   HB3    H  N N 302 
LYS   HG2    H  N N 303 
LYS   HG3    H  N N 304 
LYS   HD2    H  N N 305 
LYS   HD3    H  N N 306 
LYS   HE2    H  N N 307 
LYS   HE3    H  N N 308 
LYS   HZ1    H  N N 309 
LYS   HZ2    H  N N 310 
LYS   HZ3    H  N N 311 
LYS   HXT    H  N N 312 
MET   N      N  N N 313 
MET   CA     C  N S 314 
MET   C      C  N N 315 
MET   O      O  N N 316 
MET   CB     C  N N 317 
MET   CG     C  N N 318 
MET   SD     S  N N 319 
MET   CE     C  N N 320 
MET   OXT    O  N N 321 
MET   H      H  N N 322 
MET   H2     H  N N 323 
MET   HA     H  N N 324 
MET   HB2    H  N N 325 
MET   HB3    H  N N 326 
MET   HG2    H  N N 327 
MET   HG3    H  N N 328 
MET   HE1    H  N N 329 
MET   HE2    H  N N 330 
MET   HE3    H  N N 331 
MET   HXT    H  N N 332 
MG    MG     MG N N 333 
PHE   N      N  N N 334 
PHE   CA     C  N S 335 
PHE   C      C  N N 336 
PHE   O      O  N N 337 
PHE   CB     C  N N 338 
PHE   CG     C  Y N 339 
PHE   CD1    C  Y N 340 
PHE   CD2    C  Y N 341 
PHE   CE1    C  Y N 342 
PHE   CE2    C  Y N 343 
PHE   CZ     C  Y N 344 
PHE   OXT    O  N N 345 
PHE   H      H  N N 346 
PHE   H2     H  N N 347 
PHE   HA     H  N N 348 
PHE   HB2    H  N N 349 
PHE   HB3    H  N N 350 
PHE   HD1    H  N N 351 
PHE   HD2    H  N N 352 
PHE   HE1    H  N N 353 
PHE   HE2    H  N N 354 
PHE   HZ     H  N N 355 
PHE   HXT    H  N N 356 
PRO   N      N  N N 357 
PRO   CA     C  N S 358 
PRO   C      C  N N 359 
PRO   O      O  N N 360 
PRO   CB     C  N N 361 
PRO   CG     C  N N 362 
PRO   CD     C  N N 363 
PRO   OXT    O  N N 364 
PRO   H      H  N N 365 
PRO   HA     H  N N 366 
PRO   HB2    H  N N 367 
PRO   HB3    H  N N 368 
PRO   HG2    H  N N 369 
PRO   HG3    H  N N 370 
PRO   HD2    H  N N 371 
PRO   HD3    H  N N 372 
PRO   HXT    H  N N 373 
SER   N      N  N N 374 
SER   CA     C  N S 375 
SER   C      C  N N 376 
SER   O      O  N N 377 
SER   CB     C  N N 378 
SER   OG     O  N N 379 
SER   OXT    O  N N 380 
SER   H      H  N N 381 
SER   H2     H  N N 382 
SER   HA     H  N N 383 
SER   HB2    H  N N 384 
SER   HB3    H  N N 385 
SER   HG     H  N N 386 
SER   HXT    H  N N 387 
THR   N      N  N N 388 
THR   CA     C  N S 389 
THR   C      C  N N 390 
THR   O      O  N N 391 
THR   CB     C  N R 392 
THR   OG1    O  N N 393 
THR   CG2    C  N N 394 
THR   OXT    O  N N 395 
THR   H      H  N N 396 
THR   H2     H  N N 397 
THR   HA     H  N N 398 
THR   HB     H  N N 399 
THR   HG1    H  N N 400 
THR   HG21   H  N N 401 
THR   HG22   H  N N 402 
THR   HG23   H  N N 403 
THR   HXT    H  N N 404 
TYR   N      N  N N 405 
TYR   CA     C  N S 406 
TYR   C      C  N N 407 
TYR   O      O  N N 408 
TYR   CB     C  N N 409 
TYR   CG     C  Y N 410 
TYR   CD1    C  Y N 411 
TYR   CD2    C  Y N 412 
TYR   CE1    C  Y N 413 
TYR   CE2    C  Y N 414 
TYR   CZ     C  Y N 415 
TYR   OH     O  N N 416 
TYR   OXT    O  N N 417 
TYR   H      H  N N 418 
TYR   H2     H  N N 419 
TYR   HA     H  N N 420 
TYR   HB2    H  N N 421 
TYR   HB3    H  N N 422 
TYR   HD1    H  N N 423 
TYR   HD2    H  N N 424 
TYR   HE1    H  N N 425 
TYR   HE2    H  N N 426 
TYR   HH     H  N N 427 
TYR   HXT    H  N N 428 
VAL   N      N  N N 429 
VAL   CA     C  N S 430 
VAL   C      C  N N 431 
VAL   O      O  N N 432 
VAL   CB     C  N N 433 
VAL   CG1    C  N N 434 
VAL   CG2    C  N N 435 
VAL   OXT    O  N N 436 
VAL   H      H  N N 437 
VAL   H2     H  N N 438 
VAL   HA     H  N N 439 
VAL   HB     H  N N 440 
VAL   HG11   H  N N 441 
VAL   HG12   H  N N 442 
VAL   HG13   H  N N 443 
VAL   HG21   H  N N 444 
VAL   HG22   H  N N 445 
VAL   HG23   H  N N 446 
VAL   HXT    H  N N 447 
# 
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 
A1IK7 CAO   CAN    doub Y N 1   
A1IK7 CAO   CAP    sing Y N 2   
A1IK7 CAN   CAM    sing Y N 3   
A1IK7 CAP   CAQ    doub Y N 4   
A1IK7 CAM   NAL    sing Y N 5   
A1IK7 CAM   CAT    doub Y N 6   
A1IK7 NAL   CAK    doub Y N 7   
A1IK7 CAQ   CAT    sing Y N 8   
A1IK7 CAQ   CLAR   sing N N 9   
A1IK7 CAT   SAU    sing Y N 10  
A1IK7 CAK   NAJ    sing N N 11  
A1IK7 CAK   SAU    sing Y N 12  
A1IK7 NAJ   SAB    sing N N 13  
A1IK7 SAB   OAA    doub N N 14  
A1IK7 SAB   OAC    doub N N 15  
A1IK7 SAB   CAI    sing N N 16  
A1IK7 CAS   CAI    doub Y N 17  
A1IK7 CAS   CAE    sing Y N 18  
A1IK7 OAD   CAE    sing N N 19  
A1IK7 CAI   CAH    sing Y N 20  
A1IK7 CAE   CAF    doub Y N 21  
A1IK7 CAH   CAG    doub Y N 22  
A1IK7 CAF   CAG    sing Y N 23  
A1IK7 CAN   H1     sing N N 24  
A1IK7 CAO   H2     sing N N 25  
A1IK7 CAP   H3     sing N N 26  
A1IK7 NAJ   H4     sing N N 27  
A1IK7 CAS   H5     sing N N 28  
A1IK7 OAD   H6     sing N N 29  
A1IK7 CAF   H7     sing N N 30  
A1IK7 CAG   H8     sing N N 31  
A1IK7 CAH   H9     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 
EDO   C1    O1     sing N N 115 
EDO   C1    C2     sing N N 116 
EDO   C1    H11    sing N N 117 
EDO   C1    H12    sing N N 118 
EDO   O1    HO1    sing N N 119 
EDO   C2    O2     sing N N 120 
EDO   C2    H21    sing N N 121 
EDO   C2    H22    sing N N 122 
EDO   O2    HO2    sing N N 123 
GDP   PB    O1B    doub N N 124 
GDP   PB    O2B    sing N N 125 
GDP   PB    O3B    sing N N 126 
GDP   PB    O3A    sing N N 127 
GDP   O2B   HOB2   sing N N 128 
GDP   O3B   HOB3   sing N N 129 
GDP   O3A   PA     sing N N 130 
GDP   PA    O1A    doub N N 131 
GDP   PA    O2A    sing N N 132 
GDP   PA    "O5'"  sing N N 133 
GDP   O2A   HOA2   sing N N 134 
GDP   "O5'" "C5'"  sing N N 135 
GDP   "C5'" "C4'"  sing N N 136 
GDP   "C5'" "H5'"  sing N N 137 
GDP   "C5'" "H5''" sing N N 138 
GDP   "C4'" "O4'"  sing N N 139 
GDP   "C4'" "C3'"  sing N N 140 
GDP   "C4'" "H4'"  sing N N 141 
GDP   "O4'" "C1'"  sing N N 142 
GDP   "C3'" "O3'"  sing N N 143 
GDP   "C3'" "C2'"  sing N N 144 
GDP   "C3'" "H3'"  sing N N 145 
GDP   "O3'" "HO3'" sing N N 146 
GDP   "C2'" "O2'"  sing N N 147 
GDP   "C2'" "C1'"  sing N N 148 
GDP   "C2'" "H2'"  sing N N 149 
GDP   "O2'" "HO2'" sing N N 150 
GDP   "C1'" N9     sing N N 151 
GDP   "C1'" "H1'"  sing N N 152 
GDP   N9    C8     sing Y N 153 
GDP   N9    C4     sing Y N 154 
GDP   C8    N7     doub Y N 155 
GDP   C8    H8     sing N N 156 
GDP   N7    C5     sing Y N 157 
GDP   C5    C6     sing N N 158 
GDP   C5    C4     doub Y N 159 
GDP   C6    O6     doub N N 160 
GDP   C6    N1     sing N N 161 
GDP   N1    C2     sing N N 162 
GDP   N1    HN1    sing N N 163 
GDP   C2    N2     sing N N 164 
GDP   C2    N3     doub N N 165 
GDP   N2    HN21   sing N N 166 
GDP   N2    HN22   sing N N 167 
GDP   N3    C4     sing N N 168 
GLN   N     CA     sing N N 169 
GLN   N     H      sing N N 170 
GLN   N     H2     sing N N 171 
GLN   CA    C      sing N N 172 
GLN   CA    CB     sing N N 173 
GLN   CA    HA     sing N N 174 
GLN   C     O      doub N N 175 
GLN   C     OXT    sing N N 176 
GLN   CB    CG     sing N N 177 
GLN   CB    HB2    sing N N 178 
GLN   CB    HB3    sing N N 179 
GLN   CG    CD     sing N N 180 
GLN   CG    HG2    sing N N 181 
GLN   CG    HG3    sing N N 182 
GLN   CD    OE1    doub N N 183 
GLN   CD    NE2    sing N N 184 
GLN   NE2   HE21   sing N N 185 
GLN   NE2   HE22   sing N N 186 
GLN   OXT   HXT    sing N N 187 
GLU   N     CA     sing N N 188 
GLU   N     H      sing N N 189 
GLU   N     H2     sing N N 190 
GLU   CA    C      sing N N 191 
GLU   CA    CB     sing N N 192 
GLU   CA    HA     sing N N 193 
GLU   C     O      doub N N 194 
GLU   C     OXT    sing N N 195 
GLU   CB    CG     sing N N 196 
GLU   CB    HB2    sing N N 197 
GLU   CB    HB3    sing N N 198 
GLU   CG    CD     sing N N 199 
GLU   CG    HG2    sing N N 200 
GLU   CG    HG3    sing N N 201 
GLU   CD    OE1    doub N N 202 
GLU   CD    OE2    sing N N 203 
GLU   OE2   HE2    sing N N 204 
GLU   OXT   HXT    sing N N 205 
GLY   N     CA     sing N N 206 
GLY   N     H      sing N N 207 
GLY   N     H2     sing N N 208 
GLY   CA    C      sing N N 209 
GLY   CA    HA2    sing N N 210 
GLY   CA    HA3    sing N N 211 
GLY   C     O      doub N N 212 
GLY   C     OXT    sing N N 213 
GLY   OXT   HXT    sing N N 214 
HIS   N     CA     sing N N 215 
HIS   N     H      sing N N 216 
HIS   N     H2     sing N N 217 
HIS   CA    C      sing N N 218 
HIS   CA    CB     sing N N 219 
HIS   CA    HA     sing N N 220 
HIS   C     O      doub N N 221 
HIS   C     OXT    sing N N 222 
HIS   CB    CG     sing N N 223 
HIS   CB    HB2    sing N N 224 
HIS   CB    HB3    sing N N 225 
HIS   CG    ND1    sing Y N 226 
HIS   CG    CD2    doub Y N 227 
HIS   ND1   CE1    doub Y N 228 
HIS   ND1   HD1    sing N N 229 
HIS   CD2   NE2    sing Y N 230 
HIS   CD2   HD2    sing N N 231 
HIS   CE1   NE2    sing Y N 232 
HIS   CE1   HE1    sing N N 233 
HIS   NE2   HE2    sing N N 234 
HIS   OXT   HXT    sing N N 235 
HOH   O     H1     sing N N 236 
HOH   O     H2     sing N N 237 
ILE   N     CA     sing N N 238 
ILE   N     H      sing N N 239 
ILE   N     H2     sing N N 240 
ILE   CA    C      sing N N 241 
ILE   CA    CB     sing N N 242 
ILE   CA    HA     sing N N 243 
ILE   C     O      doub N N 244 
ILE   C     OXT    sing N N 245 
ILE   CB    CG1    sing N N 246 
ILE   CB    CG2    sing N N 247 
ILE   CB    HB     sing N N 248 
ILE   CG1   CD1    sing N N 249 
ILE   CG1   HG12   sing N N 250 
ILE   CG1   HG13   sing N N 251 
ILE   CG2   HG21   sing N N 252 
ILE   CG2   HG22   sing N N 253 
ILE   CG2   HG23   sing N N 254 
ILE   CD1   HD11   sing N N 255 
ILE   CD1   HD12   sing N N 256 
ILE   CD1   HD13   sing N N 257 
ILE   OXT   HXT    sing N N 258 
LEU   N     CA     sing N N 259 
LEU   N     H      sing N N 260 
LEU   N     H2     sing N N 261 
LEU   CA    C      sing N N 262 
LEU   CA    CB     sing N N 263 
LEU   CA    HA     sing N N 264 
LEU   C     O      doub N N 265 
LEU   C     OXT    sing N N 266 
LEU   CB    CG     sing N N 267 
LEU   CB    HB2    sing N N 268 
LEU   CB    HB3    sing N N 269 
LEU   CG    CD1    sing N N 270 
LEU   CG    CD2    sing N N 271 
LEU   CG    HG     sing N N 272 
LEU   CD1   HD11   sing N N 273 
LEU   CD1   HD12   sing N N 274 
LEU   CD1   HD13   sing N N 275 
LEU   CD2   HD21   sing N N 276 
LEU   CD2   HD22   sing N N 277 
LEU   CD2   HD23   sing N N 278 
LEU   OXT   HXT    sing N N 279 
LYS   N     CA     sing N N 280 
LYS   N     H      sing N N 281 
LYS   N     H2     sing N N 282 
LYS   CA    C      sing N N 283 
LYS   CA    CB     sing N N 284 
LYS   CA    HA     sing N N 285 
LYS   C     O      doub N N 286 
LYS   C     OXT    sing N N 287 
LYS   CB    CG     sing N N 288 
LYS   CB    HB2    sing N N 289 
LYS   CB    HB3    sing N N 290 
LYS   CG    CD     sing N N 291 
LYS   CG    HG2    sing N N 292 
LYS   CG    HG3    sing N N 293 
LYS   CD    CE     sing N N 294 
LYS   CD    HD2    sing N N 295 
LYS   CD    HD3    sing N N 296 
LYS   CE    NZ     sing N N 297 
LYS   CE    HE2    sing N N 298 
LYS   CE    HE3    sing N N 299 
LYS   NZ    HZ1    sing N N 300 
LYS   NZ    HZ2    sing N N 301 
LYS   NZ    HZ3    sing N N 302 
LYS   OXT   HXT    sing N N 303 
MET   N     CA     sing N N 304 
MET   N     H      sing N N 305 
MET   N     H2     sing N N 306 
MET   CA    C      sing N N 307 
MET   CA    CB     sing N N 308 
MET   CA    HA     sing N N 309 
MET   C     O      doub N N 310 
MET   C     OXT    sing N N 311 
MET   CB    CG     sing N N 312 
MET   CB    HB2    sing N N 313 
MET   CB    HB3    sing N N 314 
MET   CG    SD     sing N N 315 
MET   CG    HG2    sing N N 316 
MET   CG    HG3    sing N N 317 
MET   SD    CE     sing N N 318 
MET   CE    HE1    sing N N 319 
MET   CE    HE2    sing N N 320 
MET   CE    HE3    sing N N 321 
MET   OXT   HXT    sing N N 322 
PHE   N     CA     sing N N 323 
PHE   N     H      sing N N 324 
PHE   N     H2     sing N N 325 
PHE   CA    C      sing N N 326 
PHE   CA    CB     sing N N 327 
PHE   CA    HA     sing N N 328 
PHE   C     O      doub N N 329 
PHE   C     OXT    sing N N 330 
PHE   CB    CG     sing N N 331 
PHE   CB    HB2    sing N N 332 
PHE   CB    HB3    sing N N 333 
PHE   CG    CD1    doub Y N 334 
PHE   CG    CD2    sing Y N 335 
PHE   CD1   CE1    sing Y N 336 
PHE   CD1   HD1    sing N N 337 
PHE   CD2   CE2    doub Y N 338 
PHE   CD2   HD2    sing N N 339 
PHE   CE1   CZ     doub Y N 340 
PHE   CE1   HE1    sing N N 341 
PHE   CE2   CZ     sing Y N 342 
PHE   CE2   HE2    sing N N 343 
PHE   CZ    HZ     sing N N 344 
PHE   OXT   HXT    sing N N 345 
PRO   N     CA     sing N N 346 
PRO   N     CD     sing N N 347 
PRO   N     H      sing N N 348 
PRO   CA    C      sing N N 349 
PRO   CA    CB     sing N N 350 
PRO   CA    HA     sing N N 351 
PRO   C     O      doub N N 352 
PRO   C     OXT    sing N N 353 
PRO   CB    CG     sing N N 354 
PRO   CB    HB2    sing N N 355 
PRO   CB    HB3    sing N N 356 
PRO   CG    CD     sing N N 357 
PRO   CG    HG2    sing N N 358 
PRO   CG    HG3    sing N N 359 
PRO   CD    HD2    sing N N 360 
PRO   CD    HD3    sing N N 361 
PRO   OXT   HXT    sing N N 362 
SER   N     CA     sing N N 363 
SER   N     H      sing N N 364 
SER   N     H2     sing N N 365 
SER   CA    C      sing N N 366 
SER   CA    CB     sing N N 367 
SER   CA    HA     sing N N 368 
SER   C     O      doub N N 369 
SER   C     OXT    sing N N 370 
SER   CB    OG     sing N N 371 
SER   CB    HB2    sing N N 372 
SER   CB    HB3    sing N N 373 
SER   OG    HG     sing N N 374 
SER   OXT   HXT    sing N N 375 
THR   N     CA     sing N N 376 
THR   N     H      sing N N 377 
THR   N     H2     sing N N 378 
THR   CA    C      sing N N 379 
THR   CA    CB     sing N N 380 
THR   CA    HA     sing N N 381 
THR   C     O      doub N N 382 
THR   C     OXT    sing N N 383 
THR   CB    OG1    sing N N 384 
THR   CB    CG2    sing N N 385 
THR   CB    HB     sing N N 386 
THR   OG1   HG1    sing N N 387 
THR   CG2   HG21   sing N N 388 
THR   CG2   HG22   sing N N 389 
THR   CG2   HG23   sing N N 390 
THR   OXT   HXT    sing N N 391 
TYR   N     CA     sing N N 392 
TYR   N     H      sing N N 393 
TYR   N     H2     sing N N 394 
TYR   CA    C      sing N N 395 
TYR   CA    CB     sing N N 396 
TYR   CA    HA     sing N N 397 
TYR   C     O      doub N N 398 
TYR   C     OXT    sing N N 399 
TYR   CB    CG     sing N N 400 
TYR   CB    HB2    sing N N 401 
TYR   CB    HB3    sing N N 402 
TYR   CG    CD1    doub Y N 403 
TYR   CG    CD2    sing Y N 404 
TYR   CD1   CE1    sing Y N 405 
TYR   CD1   HD1    sing N N 406 
TYR   CD2   CE2    doub Y N 407 
TYR   CD2   HD2    sing N N 408 
TYR   CE1   CZ     doub Y N 409 
TYR   CE1   HE1    sing N N 410 
TYR   CE2   CZ     sing Y N 411 
TYR   CE2   HE2    sing N N 412 
TYR   CZ    OH     sing N N 413 
TYR   OH    HH     sing N N 414 
TYR   OXT   HXT    sing N N 415 
VAL   N     CA     sing N N 416 
VAL   N     H      sing N N 417 
VAL   N     H2     sing N N 418 
VAL   CA    C      sing N N 419 
VAL   CA    CB     sing N N 420 
VAL   CA    HA     sing N N 421 
VAL   C     O      doub N N 422 
VAL   C     OXT    sing N N 423 
VAL   CB    CG1    sing N N 424 
VAL   CB    CG2    sing N N 425 
VAL   CB    HB     sing N N 426 
VAL   CG1   HG11   sing N N 427 
VAL   CG1   HG12   sing N N 428 
VAL   CG1   HG13   sing N N 429 
VAL   CG2   HG21   sing N N 430 
VAL   CG2   HG22   sing N N 431 
VAL   CG2   HG23   sing N N 432 
VAL   OXT   HXT    sing N N 433 
# 
_pdbx_audit_support.funding_organization   'Cancer Research UK' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'unreleased crystal structure' 
# 
_atom_sites.entry_id                    9GGT 
_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]   0.026781 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.024468 
_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]   0.008924 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
MG 
N  
O  
P  
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 3   ? -18.904 22.943 -7.383 1.00 28.78 ? 0   SER   A N     1 
ATOM   2    C  CA    . SER   A 1 3   ? -18.425 21.558 -7.138 1.00 26.10 ? 0   SER   A CA    1 
ATOM   3    C  C     . SER   A 1 3   ? -17.116 21.581 -6.336 1.00 25.93 ? 0   SER   A C     1 
ATOM   4    O  O     . SER   A 1 3   ? -16.074 21.613 -6.937 1.00 25.82 ? 0   SER   A O     1 
ATOM   5    C  CB    . SER   A 1 3   ? -18.342 20.748 -8.395 1.00 26.84 ? 0   SER   A CB    1 
ATOM   6    O  OG    . SER   A 1 3   ? -17.706 19.513 -8.174 1.00 26.58 ? 0   SER   A OG    1 
ATOM   7    N  N     . MET   A 1 4   ? -17.235 21.621 -5.010 1.00 30.41 ? 1   MET   A N     1 
ATOM   8    C  CA    . MET   A 1 4   ? -16.096 21.727 -4.059 1.00 27.31 ? 1   MET   A CA    1 
ATOM   9    C  C     . MET   A 1 4   ? -16.560 21.267 -2.669 1.00 24.65 ? 1   MET   A C     1 
ATOM   10   O  O     . MET   A 1 4   ? -17.690 21.533 -2.298 1.00 23.95 ? 1   MET   A O     1 
ATOM   11   C  CB    . MET   A 1 4   ? -15.635 23.194 -4.042 1.00 28.73 ? 1   MET   A CB    1 
ATOM   12   C  CG    . MET   A 1 4   ? -14.640 23.613 -2.992 1.00 29.51 ? 1   MET   A CG    1 
ATOM   13   S  SD    . MET   A 1 4   ? -15.327 23.870 -1.314 1.00 32.26 ? 1   MET   A SD    1 
ATOM   14   C  CE    . MET   A 1 4   ? -15.831 25.591 -1.318 1.00 31.90 ? 1   MET   A CE    1 
ATOM   15   N  N     . THR   A 1 5   ? -15.641 20.733 -1.876 1.00 20.31 ? 2   THR   A N     1 
ATOM   16   C  CA    . THR   A 1 5   ? -15.980 20.229 -0.531 1.00 18.30 ? 2   THR   A CA    1 
ATOM   17   C  C     . THR   A 1 5   ? -15.013 20.884 0.454  1.00 16.63 ? 2   THR   A C     1 
ATOM   18   O  O     . THR   A 1 5   ? -13.881 20.982 0.115  1.00 15.85 ? 2   THR   A O     1 
ATOM   19   C  CB    . THR   A 1 5   ? -15.813 18.707 -0.507 1.00 17.91 ? 2   THR   A CB    1 
ATOM   20   O  OG1   . THR   A 1 5   ? -16.711 18.127 -1.446 1.00 17.57 ? 2   THR   A OG1   1 
ATOM   21   C  CG2   . THR   A 1 5   ? -16.009 18.103 0.855  1.00 17.82 ? 2   THR   A CG2   1 
ATOM   22   N  N     . GLU   A 1 6   ? -15.510 21.328 1.589  1.00 16.09 ? 3   GLU   A N     1 
ATOM   23   C  CA    . GLU   A 1 6   ? -14.642 22.001 2.563  1.00 15.67 ? 3   GLU   A CA    1 
ATOM   24   C  C     . GLU   A 1 6   ? -14.100 21.041 3.611  1.00 13.96 ? 3   GLU   A C     1 
ATOM   25   O  O     . GLU   A 1 6   ? -14.805 20.110 4.025  1.00 14.81 ? 3   GLU   A O     1 
ATOM   26   C  CB    . GLU   A 1 6   ? -15.409 23.089 3.287  1.00 17.26 ? 3   GLU   A CB    1 
ATOM   27   C  CG    . GLU   A 1 6   ? -15.905 24.220 2.410  1.00 19.99 ? 3   GLU   A CG    1 
ATOM   28   C  CD    . GLU   A 1 6   ? -16.941 25.106 3.110  1.00 23.72 ? 3   GLU   A CD    1 
ATOM   29   O  OE1   . GLU   A 1 6   ? -17.084 25.053 4.354  1.00 26.44 ? 3   GLU   A OE1   1 
ATOM   30   O  OE2   . GLU   A 1 6   ? -17.639 25.869 2.415  1.00 28.02 ? 3   GLU   A OE2   1 
ATOM   31   N  N     . TYR   A 1 7   ? -12.887 21.314 4.100  1.00 12.50 ? 4   TYR   A N     1 
ATOM   32   C  CA    . TYR   A 1 7   ? -12.270 20.557 5.213  1.00 11.69 ? 4   TYR   A CA    1 
ATOM   33   C  C     . TYR   A 1 7   ? -11.556 21.501 6.171  1.00 11.57 ? 4   TYR   A C     1 
ATOM   34   O  O     . TYR   A 1 7   ? -10.700 22.280 5.712  1.00 11.61 ? 4   TYR   A O     1 
ATOM   35   C  CB    . TYR   A 1 7   ? -11.213 19.593 4.653  1.00 10.90 ? 4   TYR   A CB    1 
ATOM   36   C  CG    . TYR   A 1 7   ? -11.791 18.506 3.771  1.00 10.97 ? 4   TYR   A CG    1 
ATOM   37   C  CD1   . TYR   A 1 7   ? -12.008 18.721 2.414  1.00 11.31 ? 4   TYR   A CD1   1 
ATOM   38   C  CD2   . TYR   A 1 7   ? -12.113 17.263 4.294  1.00 10.72 ? 4   TYR   A CD2   1 
ATOM   39   C  CE1   . TYR   A 1 7   ? -12.535 17.717 1.588  1.00 11.50 ? 4   TYR   A CE1   1 
ATOM   40   C  CE2   . TYR   A 1 7   ? -12.621 16.242 3.483  1.00 11.17 ? 4   TYR   A CE2   1 
ATOM   41   C  CZ    . TYR   A 1 7   ? -12.854 16.475 2.142  1.00 11.78 ? 4   TYR   A CZ    1 
ATOM   42   O  OH    . TYR   A 1 7   ? -13.392 15.452 1.363  1.00 12.00 ? 4   TYR   A OH    1 
ATOM   43   N  N     . LYS   A 1 8   ? -11.859 21.403 7.469  1.00 12.22 ? 5   LYS   A N     1 
ATOM   44   C  CA    . LYS   A 1 8   ? -11.240 22.264 8.502  1.00 12.59 ? 5   LYS   A CA    1 
ATOM   45   C  C     . LYS   A 1 8   ? -10.141 21.499 9.220  1.00 11.52 ? 5   LYS   A C     1 
ATOM   46   O  O     . LYS   A 1 8   ? -10.425 20.527 9.941  1.00 10.73 ? 5   LYS   A O     1 
ATOM   47   C  CB    . LYS   A 1 8   ? -12.275 22.736 9.530  1.00 14.21 ? 5   LYS   A CB    1 
ATOM   48   C  CG    . LYS   A 1 8   ? -13.284 23.717 8.975  1.00 16.36 ? 5   LYS   A CG    1 
ATOM   49   C  CD    . LYS   A 1 8   ? -14.629 23.564 9.638  1.00 18.56 ? 5   LYS   A CD    1 
ATOM   50   C  CE    . LYS   A 1 8   ? -15.329 24.878 9.850  1.00 21.05 ? 5   LYS   A CE    1 
ATOM   51   N  NZ    . LYS   A 1 8   ? -15.752 25.483 8.569  1.00 22.09 ? 5   LYS   A NZ    1 
ATOM   52   N  N     . LEU   A 1 9   ? -8.893  21.920 9.004  1.00 11.04 ? 6   LEU   A N     1 
ATOM   53   C  CA    . LEU   A 1 9   ? -7.717  21.238 9.546  1.00 11.16 ? 6   LEU   A CA    1 
ATOM   54   C  C     . LEU   A 1 9   ? -7.063  22.071 10.642 1.00 11.01 ? 6   LEU   A C     1 
ATOM   55   O  O     . LEU   A 1 9   ? -7.053  23.303 10.558 1.00 11.88 ? 6   LEU   A O     1 
ATOM   56   C  CB    . LEU   A 1 9   ? -6.680  20.909 8.452  1.00 11.06 ? 6   LEU   A CB    1 
ATOM   57   C  CG    . LEU   A 1 9   ? -7.165  20.260 7.127  1.00 11.86 ? 6   LEU   A CG    1 
ATOM   58   C  CD1   . LEU   A 1 9   ? -5.989  19.863 6.238  1.00 11.60 ? 6   LEU   A CD1   1 
ATOM   59   C  CD2   . LEU   A 1 9   ? -8.069  19.068 7.351  1.00 12.44 ? 6   LEU   A CD2   1 
ATOM   60   N  N     . VAL   A 1 10  ? -6.532  21.398 11.663 1.00 10.24 ? 7   VAL   A N     1 
ATOM   61   C  CA    . VAL   A 1 10  ? -5.854  22.077 12.780 1.00 10.95 ? 7   VAL   A CA    1 
ATOM   62   C  C     . VAL   A 1 10  ? -4.507  21.410 13.050 1.00 11.19 ? 7   VAL   A C     1 
ATOM   63   O  O     . VAL   A 1 10  ? -4.445  20.184 13.217 1.00 10.66 ? 7   VAL   A O     1 
ATOM   64   C  CB    . VAL   A 1 10  ? -6.688  22.042 14.089 1.00 11.01 ? 7   VAL   A CB    1 
ATOM   65   C  CG1   . VAL   A 1 10  ? -6.014  22.876 15.179 1.00 11.67 ? 7   VAL   A CG1   1 
ATOM   66   C  CG2   . VAL   A 1 10  ? -8.118  22.551 13.839 1.00 11.35 ? 7   VAL   A CG2   1 
ATOM   67   N  N     . VAL   A 1 11  ? -3.449  22.222 13.092 1.00 11.61 ? 8   VAL   A N     1 
ATOM   68   C  CA    . VAL   A 1 11  ? -2.081  21.751 13.274 1.00 12.49 ? 8   VAL   A CA    1 
ATOM   69   C  C     . VAL   A 1 11  ? -1.668  22.026 14.702 1.00 13.07 ? 8   VAL   A C     1 
ATOM   70   O  O     . VAL   A 1 11  ? -1.619  23.182 15.145 1.00 13.81 ? 8   VAL   A O     1 
ATOM   71   C  CB    . VAL   A 1 11  ? -1.125  22.440 12.257 1.00 12.67 ? 8   VAL   A CB    1 
ATOM   72   C  CG1   . VAL   A 1 11  ? 0.301   21.915 12.397 1.00 13.15 ? 8   VAL   A CG1   1 
ATOM   73   C  CG2   . VAL   A 1 11  ? -1.626  22.287 10.844 1.00 12.86 ? 8   VAL   A CG2   1 
ATOM   74   N  N     . VAL   A 1 12  ? -1.444  20.950 15.450 1.00 12.93 ? 9   VAL   A N     1 
ATOM   75   C  CA    . VAL   A 1 12  ? -1.076  21.044 16.883 1.00 14.27 ? 9   VAL   A CA    1 
ATOM   76   C  C     . VAL   A 1 12  ? 0.274   20.365 17.149 1.00 13.71 ? 9   VAL   A C     1 
ATOM   77   O  O     . VAL   A 1 12  ? 0.696   19.601 16.331 1.00 13.42 ? 9   VAL   A O     1 
ATOM   78   C  CB    . VAL   A 1 12  ? -2.160  20.423 17.786 1.00 14.87 ? 9   VAL   A CB    1 
ATOM   79   C  CG1   . VAL   A 1 12  ? -3.523  21.003 17.435 1.00 14.87 ? 9   VAL   A CG1   1 
ATOM   80   C  CG2   . VAL   A 1 12  ? -2.188  18.907 17.673 1.00 14.10 ? 9   VAL   A CG2   1 
ATOM   81   N  N     . GLY   A 1 13  ? 0.873   20.697 18.283 1.00 14.27 ? 10  GLY   A N     1 
ATOM   82   C  CA    . GLY   A 1 13  ? 2.133   20.078 18.703 1.00 14.54 ? 10  GLY   A CA    1 
ATOM   83   C  C     . GLY   A 1 13  ? 2.928   21.039 19.569 1.00 15.90 ? 10  GLY   A C     1 
ATOM   84   O  O     . GLY   A 1 13  ? 2.667   22.198 19.540 1.00 15.16 ? 10  GLY   A O     1 
ATOM   85   N  N     . ALA   A 1 14  ? 3.963   20.535 20.217 1.00 15.79 ? 11  ALA   A N     1 
ATOM   86   C  CA    . ALA   A 1 14  ? 4.755   21.417 21.083 1.00 16.11 ? 11  ALA   A CA    1 
ATOM   87   C  C     . ALA   A 1 14  ? 5.436   22.577 20.335 1.00 15.60 ? 11  ALA   A C     1 
ATOM   88   O  O     . ALA   A 1 14  ? 5.708   22.533 19.161 1.00 15.74 ? 11  ALA   A O     1 
ATOM   89   C  CB    . ALA   A 1 14  ? 5.735   20.580 21.872 1.00 17.11 ? 11  ALA   A CB    1 
ATOM   90   N  N     . GLY   A 1 15  ? 5.759   23.622 21.090 1.00 15.74 ? 12  GLY   A N     1 
ATOM   91   C  CA    . GLY   A 1 15  ? 6.561   24.709 20.535 1.00 15.87 ? 12  GLY   A CA    1 
ATOM   92   C  C     . GLY   A 1 15  ? 7.859   24.204 19.891 1.00 15.59 ? 12  GLY   A C     1 
ATOM   93   O  O     . GLY   A 1 15  ? 8.511   23.339 20.423 1.00 15.86 ? 12  GLY   A O     1 
ATOM   94   N  N     . GLY   A 1 16  ? 8.142   24.708 18.708 1.00 14.89 ? 13  GLY   A N     1 
ATOM   95   C  CA    . GLY   A 1 16  ? 9.373   24.430 17.985 1.00 14.96 ? 13  GLY   A CA    1 
ATOM   96   C  C     . GLY   A 1 16  ? 9.401   23.172 17.131 1.00 14.35 ? 13  GLY   A C     1 
ATOM   97   O  O     . GLY   A 1 16  ? 10.438  22.888 16.522 1.00 13.94 ? 13  GLY   A O     1 
ATOM   98   N  N     . VAL   A 1 17  ? 8.297   22.421 17.086 1.00 13.94 ? 14  VAL   A N     1 
ATOM   99   C  CA    . VAL   A 1 17  ? 8.258   21.187 16.262 1.00 13.20 ? 14  VAL   A CA    1 
ATOM   100  C  C     . VAL   A 1 17  ? 8.192   21.425 14.743 1.00 12.70 ? 14  VAL   A C     1 
ATOM   101  O  O     . VAL   A 1 17  ? 8.587   20.523 13.958 1.00 12.51 ? 14  VAL   A O     1 
ATOM   102  C  CB    . VAL   A 1 17  ? 7.143   20.169 16.697 1.00 13.10 ? 14  VAL   A CB    1 
ATOM   103  C  CG1   . VAL   A 1 17  ? 7.338   19.706 18.131 1.00 13.52 ? 14  VAL   A CG1   1 
ATOM   104  C  CG2   . VAL   A 1 17  ? 5.748   20.718 16.502 1.00 13.43 ? 14  VAL   A CG2   1 
ATOM   105  N  N     . GLY   A 1 18  ? 7.703   22.596 14.317 1.00 12.46 ? 15  GLY   A N     1 
ATOM   106  C  CA    . GLY   A 1 18  ? 7.557   22.939 12.920 1.00 12.22 ? 15  GLY   A CA    1 
ATOM   107  C  C     . GLY   A 1 18  ? 6.127   23.084 12.387 1.00 12.09 ? 15  GLY   A C     1 
ATOM   108  O  O     . GLY   A 1 18  ? 5.928   22.946 11.198 1.00 12.09 ? 15  GLY   A O     1 
ATOM   109  N  N     . LYS   A 1 19  ? 5.152   23.397 13.256 1.00 12.01 ? 16  LYS   A N     1 
ATOM   110  C  CA    . LYS   A 1 19  ? 3.754   23.646 12.834 1.00 11.73 ? 16  LYS   A CA    1 
ATOM   111  C  C     . LYS   A 1 19  ? 3.658   24.731 11.766 1.00 11.43 ? 16  LYS   A C     1 
ATOM   112  O  O     . LYS   A 1 19  ? 3.062   24.528 10.698 1.00 11.75 ? 16  LYS   A O     1 
ATOM   113  C  CB    . LYS   A 1 19  ? 2.866   24.061 14.021 1.00 12.54 ? 16  LYS   A CB    1 
ATOM   114  C  CG    . LYS   A 1 19  ? 2.706   23.016 15.110 1.00 13.02 ? 16  LYS   A CG    1 
ATOM   115  C  CD    . LYS   A 1 19  ? 1.886   23.537 16.302 1.00 13.39 ? 16  LYS   A CD    1 
ATOM   116  C  CE    . LYS   A 1 19  ? 2.521   24.697 17.041 1.00 14.15 ? 16  LYS   A CE    1 
ATOM   117  N  NZ    . LYS   A 1 19  ? 3.836   24.389 17.701 1.00 14.40 ? 16  LYS   A NZ    1 
ATOM   118  N  N     . SER   A 1 20  ? 4.266   25.874 12.062 1.00 11.85 ? 17  SER   A N     1 
ATOM   119  C  CA    . SER   A 1 20  ? 4.295   26.998 11.162 1.00 12.13 ? 17  SER   A CA    1 
ATOM   120  C  C     . SER   A 1 20  ? 5.063   26.694 9.886  1.00 12.05 ? 17  SER   A C     1 
ATOM   121  O  O     . SER   A 1 20  ? 4.580   27.013 8.796  1.00 11.73 ? 17  SER   A O     1 
ATOM   122  C  CB    . SER   A 1 20  ? 4.918   28.220 11.839 1.00 13.52 ? 17  SER   A CB    1 
ATOM   123  O  OG    . SER   A 1 20  ? 4.097   28.662 12.910 1.00 15.36 ? 17  SER   A OG    1 
ATOM   124  N  N     . ALA   A 1 21  ? 6.250   26.096 10.026 1.00 11.55 ? 18  ALA   A N     1 
ATOM   125  C  CA    . ALA   A 1 21  ? 7.074   25.768 8.859  1.00 11.64 ? 18  ALA   A CA    1 
ATOM   126  C  C     . ALA   A 1 21  ? 6.345   24.842 7.882  1.00 11.01 ? 18  ALA   A C     1 
ATOM   127  O  O     . ALA   A 1 21  ? 6.420   25.060 6.686  1.00 10.99 ? 18  ALA   A O     1 
ATOM   128  C  CB    . ALA   A 1 21  ? 8.434   25.168 9.240  1.00 11.58 ? 18  ALA   A CB    1 
ATOM   129  N  N     . LEU   A 1 22  ? 5.663   23.819 8.403  1.00 10.44 ? 19  LEU   A N     1 
ATOM   130  C  CA    . LEU   A 1 22  ? 4.853   22.900 7.561  1.00 10.83 ? 19  LEU   A CA    1 
ATOM   131  C  C     . LEU   A 1 22  ? 3.726   23.651 6.836  1.00 10.93 ? 19  LEU   A C     1 
ATOM   132  O  O     . LEU   A 1 22  ? 3.529   23.519 5.616  1.00 11.82 ? 19  LEU   A O     1 
ATOM   133  C  CB    . LEU   A 1 22  ? 4.272   21.771 8.423  1.00 10.15 ? 19  LEU   A CB    1 
ATOM   134  C  CG    . LEU   A 1 22  ? 5.267   20.673 8.841  1.00 10.22 ? 19  LEU   A CG    1 
ATOM   135  C  CD1   . LEU   A 1 22  ? 4.646   19.780 9.894  1.00 10.22 ? 19  LEU   A CD1   1 
ATOM   136  C  CD2   . LEU   A 1 22  ? 5.704   19.834 7.631  1.00 10.55 ? 19  LEU   A CD2   1 
ATOM   137  N  N     . THR   A 1 23  ? 2.974   24.415 7.610  1.00 11.68 ? 20  THR   A N     1 
ATOM   138  C  CA    . THR   A 1 23  ? 1.793   25.122 7.046  1.00 12.19 ? 20  THR   A CA    1 
ATOM   139  C  C     . THR   A 1 23  ? 2.239   26.118 5.969  1.00 12.24 ? 20  THR   A C     1 
ATOM   140  O  O     . THR   A 1 23  ? 1.629   26.198 4.966  1.00 12.52 ? 20  THR   A O     1 
ATOM   141  C  CB    . THR   A 1 23  ? 1.003   25.846 8.139  1.00 12.65 ? 20  THR   A CB    1 
ATOM   142  O  OG1   . THR   A 1 23  ? 0.635   24.951 9.177  1.00 12.70 ? 20  THR   A OG1   1 
ATOM   143  C  CG2   . THR   A 1 23  ? -0.225  26.535 7.593  1.00 12.94 ? 20  THR   A CG2   1 
ATOM   144  N  N     . ILE   A 1 24  ? 3.263   26.889 6.276  1.00 13.22 ? 21  ILE   A N     1 
ATOM   145  C  CA    . ILE   A 1 24  ? 3.763   27.924 5.330  1.00 13.76 ? 21  ILE   A CA    1 
ATOM   146  C  C     . ILE   A 1 24  ? 4.335   27.260 4.065  1.00 13.73 ? 21  ILE   A C     1 
ATOM   147  O  O     . ILE   A 1 24  ? 4.188   27.799 3.000  1.00 13.99 ? 21  ILE   A O     1 
ATOM   148  C  CB    . ILE   A 1 24  ? 4.680   28.928 6.062  1.00 15.19 ? 21  ILE   A CB    1 
ATOM   149  C  CG1   . ILE   A 1 24  ? 3.861   29.625 7.151  1.00 15.61 ? 21  ILE   A CG1   1 
ATOM   150  C  CG2   . ILE   A 1 24  ? 5.322   29.891 5.070  1.00 15.98 ? 21  ILE   A CG2   1 
ATOM   151  C  CD1   . ILE   A 1 24  ? 4.564   30.698 7.892  1.00 17.41 ? 21  ILE   A CD1   1 
ATOM   152  N  N     . GLN   A 1 25  ? 5.019   26.131 4.221  1.00 13.20 ? 22  GLN   A N     1 
ATOM   153  C  CA    . GLN   A 1 25  ? 5.494   25.421 3.016  1.00 13.59 ? 22  GLN   A CA    1 
ATOM   154  C  C     . GLN   A 1 25  ? 4.294   25.000 2.149  1.00 13.94 ? 22  GLN   A C     1 
ATOM   155  O  O     . GLN   A 1 25  ? 4.348   25.180 0.994  1.00 13.87 ? 22  GLN   A O     1 
ATOM   156  C  CB    . GLN   A 1 25  ? 6.282   24.179 3.406  1.00 13.89 ? 22  GLN   A CB    1 
ATOM   157  C  CG    . GLN   A 1 25  ? 7.775   24.422 3.416  1.00 15.11 ? 22  GLN   A CG    1 
ATOM   158  C  CD    . GLN   A 1 25  ? 8.474   24.521 2.077  1.00 16.03 ? 22  GLN   A CD    1 
ATOM   159  O  OE1   . GLN   A 1 25  ? 7.878   24.688 1.035  1.00 17.71 ? 22  GLN   A OE1   1 
ATOM   160  N  NE2   . GLN   A 1 25  ? 9.775   24.399 2.116  1.00 15.99 ? 22  GLN   A NE2   1 
ATOM   161  N  N     . LEU   A 1 26  ? 3.271   24.419 2.751  1.00 13.75 ? 23  LEU   A N     1 
ATOM   162  C  CA    . LEU   A 1 26  ? 2.108   23.978 1.945  1.00 13.31 ? 23  LEU   A CA    1 
ATOM   163  C  C     . LEU   A 1 26  ? 1.494   25.158 1.160  1.00 14.84 ? 23  LEU   A C     1 
ATOM   164  O  O     . LEU   A 1 26  ? 1.127   24.993 0.019  1.00 15.18 ? 23  LEU   A O     1 
ATOM   165  C  CB    . LEU   A 1 26  ? 1.058   23.360 2.873  1.00 13.34 ? 23  LEU   A CB    1 
ATOM   166  C  CG    . LEU   A 1 26  ? -0.201  22.887 2.157  1.00 14.41 ? 23  LEU   A CG    1 
ATOM   167  C  CD1   . LEU   A 1 26  ? 0.042   21.569 1.447  1.00 15.01 ? 23  LEU   A CD1   1 
ATOM   168  C  CD2   . LEU   A 1 26  ? -1.410  22.784 3.072  1.00 13.77 ? 23  LEU   A CD2   1 
ATOM   169  N  N     . ILE   A 1 27  ? 1.300   26.268 1.848  1.00 15.26 ? 24  ILE   A N     1 
ATOM   170  C  CA    . ILE   A 1 27  ? 0.604   27.460 1.294  1.00 16.85 ? 24  ILE   A CA    1 
ATOM   171  C  C     . ILE   A 1 27  ? 1.491   28.349 0.431  1.00 17.51 ? 24  ILE   A C     1 
ATOM   172  O  O     . ILE   A 1 27  ? 1.015   28.781 -0.582 1.00 18.66 ? 24  ILE   A O     1 
ATOM   173  C  CB    . ILE   A 1 27  ? 0.039   28.301 2.447  1.00 17.00 ? 24  ILE   A CB    1 
ATOM   174  C  CG1   . ILE   A 1 27  ? -0.861  27.483 3.362  1.00 16.81 ? 24  ILE   A CG1   1 
ATOM   175  C  CG2   . ILE   A 1 27  ? -0.696  29.499 1.908  1.00 18.51 ? 24  ILE   A CG2   1 
ATOM   176  C  CD1   . ILE   A 1 27  ? -2.109  27.060 2.695  1.00 16.75 ? 24  ILE   A CD1   1 
ATOM   177  N  N     . GLN   A 1 28  ? 2.699   28.655 0.903  1.00 18.23 ? 25  GLN   A N     1 
ATOM   178  C  CA    . GLN   A 1 28  ? 3.535   29.666 0.202  1.00 19.30 ? 25  GLN   A CA    1 
ATOM   179  C  C     . GLN   A 1 28  ? 4.801   29.129 -0.450 1.00 20.37 ? 25  GLN   A C     1 
ATOM   180  O  O     . GLN   A 1 28  ? 5.473   29.930 -1.093 1.00 20.05 ? 25  GLN   A O     1 
ATOM   181  C  CB    . GLN   A 1 28  ? 3.832   30.821 1.153  1.00 20.49 ? 25  GLN   A CB    1 
ATOM   182  C  CG    . GLN   A 1 28  ? 2.576   31.416 1.734  1.00 20.77 ? 25  GLN   A CG    1 
ATOM   183  C  CD    . GLN   A 1 28  ? 2.848   32.445 2.801  1.00 22.58 ? 25  GLN   A CD    1 
ATOM   184  O  OE1   . GLN   A 1 28  ? 3.969   32.817 3.026  1.00 23.79 ? 25  GLN   A OE1   1 
ATOM   185  N  NE2   . GLN   A 1 28  ? 1.815   32.904 3.467  1.00 24.05 ? 25  GLN   A NE2   1 
ATOM   186  N  N     . ASN   A 1 29  ? 5.097   27.840 -0.309 1.00 19.87 ? 26  ASN   A N     1 
ATOM   187  C  CA    . ASN   A 1 29  ? 6.262   27.250 -1.026 1.00 20.88 ? 26  ASN   A CA    1 
ATOM   188  C  C     . ASN   A 1 29  ? 7.606   27.924 -0.687 1.00 21.48 ? 26  ASN   A C     1 
ATOM   189  O  O     . ASN   A 1 29  ? 8.296   28.313 -1.577 1.00 23.00 ? 26  ASN   A O     1 
ATOM   190  C  CB    . ASN   A 1 29  ? 6.004   27.134 -2.528 1.00 23.20 ? 26  ASN   A CB    1 
ATOM   191  C  CG    . ASN   A 1 29  ? 7.060   26.366 -3.280 1.00 24.82 ? 26  ASN   A CG    1 
ATOM   192  O  OD1   . ASN   A 1 29  ? 7.595   25.400 -2.790 1.00 26.96 ? 26  ASN   A OD1   1 
ATOM   193  N  ND2   . ASN   A 1 29  ? 7.340   26.771 -4.501 1.00 28.20 ? 26  ASN   A ND2   1 
ATOM   194  N  N     . HIS   A 1 30  ? 7.878   28.096 0.595  1.00 18.93 ? 27  HIS   A N     1 
ATOM   195  C  CA    . HIS   A 1 30  ? 9.195   28.553 1.124  1.00 18.05 ? 27  HIS   A CA    1 
ATOM   196  C  C     . HIS   A 1 30  ? 9.361   28.017 2.549  1.00 16.58 ? 27  HIS   A C     1 
ATOM   197  O  O     . HIS   A 1 30  ? 8.389   27.712 3.136  1.00 15.41 ? 27  HIS   A O     1 
ATOM   198  C  CB    . HIS   A 1 30  ? 9.416   30.052 0.965  1.00 17.85 ? 27  HIS   A CB    1 
ATOM   199  C  CG    . HIS   A 1 30  ? 8.521   30.879 1.801  1.00 17.38 ? 27  HIS   A CG    1 
ATOM   200  N  ND1   . HIS   A 1 30  ? 8.950   31.484 2.922  1.00 18.43 ? 27  HIS   A ND1   1 
ATOM   201  C  CD2   . HIS   A 1 30  ? 7.226   31.190 1.681  1.00 17.80 ? 27  HIS   A CD2   1 
ATOM   202  C  CE1   . HIS   A 1 30  ? 7.955   32.112 3.494  1.00 19.10 ? 27  HIS   A CE1   1 
ATOM   203  N  NE2   . HIS   A 1 30  ? 6.890   31.953 2.746  1.00 18.33 ? 27  HIS   A NE2   1 
ATOM   204  N  N     . PHE   A 1 31  ? 10.582  28.022 3.064  1.00 16.51 ? 28  PHE   A N     1 
ATOM   205  C  CA    . PHE   A 1 31  ? 10.889  27.497 4.408  1.00 16.80 ? 28  PHE   A CA    1 
ATOM   206  C  C     . PHE   A 1 31  ? 11.175  28.675 5.328  1.00 18.59 ? 28  PHE   A C     1 
ATOM   207  O  O     . PHE   A 1 31  ? 12.110  29.442 5.063  1.00 19.39 ? 28  PHE   A O     1 
ATOM   208  C  CB    . PHE   A 1 31  ? 12.135  26.597 4.343  1.00 16.46 ? 28  PHE   A CB    1 
ATOM   209  C  CG    . PHE   A 1 31  ? 12.603  26.075 5.682  1.00 16.45 ? 28  PHE   A CG    1 
ATOM   210  C  CD1   . PHE   A 1 31  ? 11.720  25.435 6.563  1.00 14.65 ? 28  PHE   A CD1   1 
ATOM   211  C  CD2   . PHE   A 1 31  ? 13.926  26.223 6.063  1.00 15.98 ? 28  PHE   A CD2   1 
ATOM   212  C  CE1   . PHE   A 1 31  ? 12.159  24.959 7.786  1.00 14.84 ? 28  PHE   A CE1   1 
ATOM   213  C  CE2   . PHE   A 1 31  ? 14.371  25.749 7.283  1.00 16.17 ? 28  PHE   A CE2   1 
ATOM   214  C  CZ    . PHE   A 1 31  ? 13.488  25.113 8.148  1.00 14.77 ? 28  PHE   A CZ    1 
ATOM   215  N  N     . VAL   A 1 32  ? 10.394  28.813 6.390  1.00 19.49 ? 29  VAL   A N     1 
ATOM   216  C  CA    . VAL   A 1 32  ? 10.661  29.914 7.356  1.00 21.34 ? 29  VAL   A CA    1 
ATOM   217  C  C     . VAL   A 1 32  ? 11.563  29.390 8.461  1.00 23.06 ? 29  VAL   A C     1 
ATOM   218  O  O     . VAL   A 1 32  ? 11.298  28.373 9.017  1.00 22.69 ? 29  VAL   A O     1 
ATOM   219  C  CB    . VAL   A 1 32  ? 9.392   30.576 7.905  1.00 21.62 ? 29  VAL   A CB    1 
ATOM   220  C  CG1   . VAL   A 1 32  ? 8.695   31.352 6.827  1.00 21.95 ? 29  VAL   A CG1   1 
ATOM   221  C  CG2   . VAL   A 1 32  ? 8.450   29.559 8.511  1.00 21.37 ? 29  VAL   A CG2   1 
ATOM   222  N  N     . ASP   A 1 33  ? 12.602  30.162 8.769  1.00 26.73 ? 30  ASP   A N     1 
ATOM   223  C  CA    . ASP   A 1 33  ? 13.606  29.756 9.779  1.00 28.19 ? 30  ASP   A CA    1 
ATOM   224  C  C     . ASP   A 1 33  ? 13.340  30.338 11.161 1.00 28.52 ? 30  ASP   A C     1 
ATOM   225  O  O     . ASP   A 1 33  ? 13.822  29.774 12.119 1.00 29.39 ? 30  ASP   A O     1 
ATOM   226  C  CB    . ASP   A 1 33  ? 14.950  30.365 9.415  1.00 33.76 ? 30  ASP   A CB    1 
ATOM   227  C  CG    . ASP   A 1 33  ? 15.505  29.742 8.166  1.00 35.12 ? 30  ASP   A CG    1 
ATOM   228  O  OD1   . ASP   A 1 33  ? 15.675  28.558 8.190  1.00 34.54 ? 30  ASP   A OD1   1 
ATOM   229  O  OD2   . ASP   A 1 33  ? 15.661  30.468 7.163  1.00 38.97 ? 30  ASP   A OD2   1 
ATOM   230  N  N     . GLU   A 1 34  ? 12.744  31.507 11.257 1.00 28.66 ? 31  GLU   A N     1 
ATOM   231  C  CA    . GLU   A 1 34  ? 12.641  32.092 12.611 1.00 30.30 ? 31  GLU   A CA    1 
ATOM   232  C  C     . GLU   A 1 34  ? 11.236  32.630 12.864 1.00 27.11 ? 31  GLU   A C     1 
ATOM   233  O  O     . GLU   A 1 34  ? 11.099  33.675 13.465 1.00 25.96 ? 31  GLU   A O     1 
ATOM   234  C  CB    . GLU   A 1 34  ? 13.678  33.214 12.732 1.00 36.33 ? 31  GLU   A CB    1 
ATOM   235  C  CG    . GLU   A 1 34  ? 15.111  32.717 12.729 1.00 40.97 ? 31  GLU   A CG    1 
ATOM   236  C  CD    . GLU   A 1 34  ? 16.255  33.707 12.787 1.00 44.63 ? 31  GLU   A CD    1 
ATOM   237  O  OE1   . GLU   A 1 34  ? 16.270  34.620 11.958 1.00 46.54 ? 31  GLU   A OE1   1 
ATOM   238  O  OE2   . GLU   A 1 34  ? 17.131  33.527 13.670 1.00 48.01 ? 31  GLU   A OE2   1 
ATOM   239  N  N     . TYR   A 1 35  ? 10.221  31.856 12.563 1.00 23.53 ? 32  TYR   A N     1 
ATOM   240  C  CA    . TYR   A 1 35  ? 8.859   32.393 12.565 1.00 23.48 ? 32  TYR   A CA    1 
ATOM   241  C  C     . TYR   A 1 35  ? 8.371   32.631 13.994 1.00 23.40 ? 32  TYR   A C     1 
ATOM   242  O  O     . TYR   A 1 35  ? 8.351   31.718 14.810 1.00 22.62 ? 32  TYR   A O     1 
ATOM   243  C  CB    . TYR   A 1 35  ? 7.901   31.459 11.823 1.00 22.08 ? 32  TYR   A CB    1 
ATOM   244  C  CG    . TYR   A 1 35  ? 6.692   32.161 11.255 1.00 21.62 ? 32  TYR   A CG    1 
ATOM   245  C  CD1   . TYR   A 1 35  ? 6.814   33.064 10.199 1.00 22.70 ? 32  TYR   A CD1   1 
ATOM   246  C  CD2   . TYR   A 1 35  ? 5.423   31.926 11.777 1.00 21.23 ? 32  TYR   A CD2   1 
ATOM   247  C  CE1   . TYR   A 1 35  ? 5.708   33.706 9.678  1.00 23.58 ? 32  TYR   A CE1   1 
ATOM   248  C  CE2   . TYR   A 1 35  ? 4.309   32.559 11.265 1.00 22.15 ? 32  TYR   A CE2   1 
ATOM   249  C  CZ    . TYR   A 1 35  ? 4.449   33.445 10.217 1.00 23.66 ? 32  TYR   A CZ    1 
ATOM   250  O  OH    . TYR   A 1 35  ? 3.329   34.072 9.719  1.00 24.70 ? 32  TYR   A OH    1 
ATOM   251  N  N     . ASP   A 1 36  ? 7.979   33.872 14.282 1.00 23.79 ? 33  ASP   A N     1 
ATOM   252  C  CA    . ASP   A 1 36  ? 7.483   34.249 15.600 1.00 24.88 ? 33  ASP   A CA    1 
ATOM   253  C  C     . ASP   A 1 36  ? 6.576   33.138 16.113 1.00 23.85 ? 33  ASP   A C     1 
ATOM   254  O  O     . ASP   A 1 36  ? 5.598   32.783 15.437 1.00 23.60 ? 33  ASP   A O     1 
ATOM   255  C  CB    . ASP   A 1 36  ? 6.732   35.598 15.529 1.00 26.14 ? 33  ASP   A CB    1 
ATOM   256  C  CG    . ASP   A 1 36  ? 6.263   36.113 16.900 1.00 27.25 ? 33  ASP   A CG    1 
ATOM   257  O  OD1   . ASP   A 1 36  ? 6.097   35.325 17.872 1.00 26.63 ? 33  ASP   A OD1   1 
ATOM   258  O  OD2   . ASP   A 1 36  ? 6.053   37.339 16.994 1.00 28.27 ? 33  ASP   A OD2   1 
ATOM   259  N  N     . PRO   A 1 37  ? 6.907   32.566 17.285 1.00 23.60 ? 34  PRO   A N     1 
ATOM   260  C  CA    . PRO   A 1 37  ? 6.175   31.388 17.763 1.00 22.89 ? 34  PRO   A CA    1 
ATOM   261  C  C     . PRO   A 1 37  ? 4.812   31.691 18.371 1.00 23.92 ? 34  PRO   A C     1 
ATOM   262  O  O     . PRO   A 1 37  ? 4.083   30.760 18.702 1.00 23.78 ? 34  PRO   A O     1 
ATOM   263  C  CB    . PRO   A 1 37  ? 7.106   30.795 18.825 1.00 23.16 ? 34  PRO   A CB    1 
ATOM   264  C  CG    . PRO   A 1 37  ? 7.926   31.939 19.289 1.00 25.32 ? 34  PRO   A CG    1 
ATOM   265  C  CD    . PRO   A 1 37  ? 8.128   32.807 18.075 1.00 24.86 ? 34  PRO   A CD    1 
ATOM   266  N  N     . THR   A 1 38  ? 4.461   32.967 18.498 1.00 23.49 ? 35  THR   A N     1 
ATOM   267  C  CA    . THR   A 1 38  ? 3.156   33.347 19.046 1.00 24.00 ? 35  THR   A CA    1 
ATOM   268  C  C     . THR   A 1 38  ? 2.105   33.650 17.951 1.00 23.51 ? 35  THR   A C     1 
ATOM   269  O  O     . THR   A 1 38  ? 0.930   33.918 18.274 1.00 24.15 ? 35  THR   A O     1 
ATOM   270  C  CB    . THR   A 1 38  ? 3.312   34.534 20.023 1.00 25.46 ? 35  THR   A CB    1 
ATOM   271  O  OG1   . THR   A 1 38  ? 3.628   35.739 19.309 1.00 26.49 ? 35  THR   A OG1   1 
ATOM   272  C  CG2   . THR   A 1 38  ? 4.427   34.244 21.022 1.00 26.34 ? 35  THR   A CG2   1 
ATOM   273  N  N     . ILE   A 1 39  ? 2.510   33.642 16.674 1.00 22.13 ? 36  ILE   A N     1 
ATOM   274  C  CA    . ILE   A 1 39  ? 1.589   34.041 15.588 1.00 21.78 ? 36  ILE   A CA    1 
ATOM   275  C  C     . ILE   A 1 39  ? 0.677   32.859 15.275 1.00 20.41 ? 36  ILE   A C     1 
ATOM   276  O  O     . ILE   A 1 39  ? 1.148   31.739 15.020 1.00 19.44 ? 36  ILE   A O     1 
ATOM   277  C  CB    . ILE   A 1 39  ? 2.321   34.517 14.306 1.00 22.14 ? 36  ILE   A CB    1 
ATOM   278  C  CG1   . ILE   A 1 39  ? 3.156   35.766 14.595 1.00 23.13 ? 36  ILE   A CG1   1 
ATOM   279  C  CG2   . ILE   A 1 39  ? 1.328   34.808 13.175 1.00 22.56 ? 36  ILE   A CG2   1 
ATOM   280  C  CD1   . ILE   A 1 39  ? 3.789   36.376 13.356 1.00 23.60 ? 36  ILE   A CD1   1 
ATOM   281  N  N     . GLU   A 1 40  ? -0.626  33.102 15.331 1.00 20.10 ? 37  GLU   A N     1 
ATOM   282  C  CA    . GLU   A 1 40  ? -1.626  32.042 15.114 1.00 19.74 ? 37  GLU   A CA    1 
ATOM   283  C  C     . GLU   A 1 40  ? -2.560  32.535 14.026 1.00 19.85 ? 37  GLU   A C     1 
ATOM   284  O  O     . GLU   A 1 40  ? -3.286  33.458 14.293 1.00 21.42 ? 37  GLU   A O     1 
ATOM   285  C  CB    . GLU   A 1 40  ? -2.398  31.778 16.395 1.00 20.29 ? 37  GLU   A CB    1 
ATOM   286  C  CG    . GLU   A 1 40  ? -3.379  30.652 16.290 1.00 20.41 ? 37  GLU   A CG    1 
ATOM   287  C  CD    . GLU   A 1 40  ? -3.891  30.240 17.647 1.00 21.44 ? 37  GLU   A CD    1 
ATOM   288  O  OE1   . GLU   A 1 40  ? -3.190  29.548 18.342 1.00 20.65 ? 37  GLU   A OE1   1 
ATOM   289  O  OE2   . GLU   A 1 40  ? -5.000  30.670 17.970 1.00 24.05 ? 37  GLU   A OE2   1 
ATOM   290  N  N     . ASP   A 1 41  ? -2.482  31.931 12.853 1.00 19.02 ? 38  ASP   A N     1 
ATOM   291  C  CA    . ASP   A 1 41  ? -3.286  32.390 11.701 1.00 19.90 ? 38  ASP   A CA    1 
ATOM   292  C  C     . ASP   A 1 41  ? -3.916  31.190 10.996 1.00 18.12 ? 38  ASP   A C     1 
ATOM   293  O  O     . ASP   A 1 41  ? -3.476  30.094 11.208 1.00 17.66 ? 38  ASP   A O     1 
ATOM   294  C  CB    . ASP   A 1 41  ? -2.428  33.040 10.619 1.00 21.88 ? 38  ASP   A CB    1 
ATOM   295  C  CG    . ASP   A 1 41  ? -2.154  34.539 10.714 1.00 25.13 ? 38  ASP   A CG    1 
ATOM   296  O  OD1   . ASP   A 1 41  ? -3.095  35.286 11.046 1.00 26.33 ? 38  ASP   A OD1   1 
ATOM   297  O  OD2   . ASP   A 1 41  ? -1.002  34.940 10.457 1.00 27.54 ? 38  ASP   A OD2   1 
ATOM   298  N  N     . SER   A 1 42  ? -4.967  31.457 10.240 1.00 17.92 ? 39  SER   A N     1 
ATOM   299  C  CA    . SER   A 1 42  ? -5.601  30.424 9.405  1.00 16.96 ? 39  SER   A CA    1 
ATOM   300  C  C     . SER   A 1 42  ? -5.295  30.770 7.941  1.00 17.71 ? 39  SER   A C     1 
ATOM   301  O  O     . SER   A 1 42  ? -5.161  31.904 7.587  1.00 18.16 ? 39  SER   A O     1 
ATOM   302  C  CB    . SER   A 1 42  ? -7.066  30.305 9.669  1.00 17.73 ? 39  SER   A CB    1 
ATOM   303  O  OG    . SER   A 1 42  ? -7.738  31.474 9.273  1.00 19.84 ? 39  SER   A OG    1 
ATOM   304  N  N     . TYR   A 1 43  ? -5.226  29.750 7.110  1.00 16.72 ? 40  TYR   A N     1 
ATOM   305  C  CA    . TYR   A 1 43  ? -4.937  29.869 5.678  1.00 17.75 ? 40  TYR   A CA    1 
ATOM   306  C  C     . TYR   A 1 43  ? -5.955  29.028 4.919  1.00 17.30 ? 40  TYR   A C     1 
ATOM   307  O  O     . TYR   A 1 43  ? -6.297  27.940 5.362  1.00 16.41 ? 40  TYR   A O     1 
ATOM   308  C  CB    . TYR   A 1 43  ? -3.557  29.302 5.385  1.00 17.67 ? 40  TYR   A CB    1 
ATOM   309  C  CG    . TYR   A 1 43  ? -2.451  30.084 6.051  1.00 19.19 ? 40  TYR   A CG    1 
ATOM   310  C  CD1   . TYR   A 1 43  ? -2.025  29.771 7.333  1.00 19.15 ? 40  TYR   A CD1   1 
ATOM   311  C  CD2   . TYR   A 1 43  ? -1.829  31.130 5.373  1.00 22.00 ? 40  TYR   A CD2   1 
ATOM   312  C  CE1   . TYR   A 1 43  ? -1.002  30.487 7.936  1.00 21.68 ? 40  TYR   A CE1   1 
ATOM   313  C  CE2   . TYR   A 1 43  ? -0.812  31.860 5.972  1.00 23.88 ? 40  TYR   A CE2   1 
ATOM   314  C  CZ    . TYR   A 1 43  ? -0.402  31.527 7.248  1.00 24.10 ? 40  TYR   A CZ    1 
ATOM   315  O  OH    . TYR   A 1 43  ? 0.616   32.260 7.837  1.00 27.86 ? 40  TYR   A OH    1 
ATOM   316  N  N     . ARG   A 1 44  ? -6.436  29.530 3.797  1.00 19.01 ? 41  ARG   A N     1 
ATOM   317  C  CA    . ARG   A 1 44  ? -7.289  28.727 2.915  1.00 21.03 ? 41  ARG   A CA    1 
ATOM   318  C  C     . ARG   A 1 44  ? -6.501  28.328 1.669  1.00 21.00 ? 41  ARG   A C     1 
ATOM   319  O  O     . ARG   A 1 44  ? -5.675  29.086 1.171  1.00 22.36 ? 41  ARG   A O     1 
ATOM   320  C  CB    . ARG   A 1 44  ? -8.590  29.460 2.565  1.00 25.17 ? 41  ARG   A CB    1 
ATOM   321  C  CG    . ARG   A 1 44  ? -9.478  29.739 3.785  1.00 29.03 ? 41  ARG   A CG    1 
ATOM   322  C  CD    . ARG   A 1 44  ? -10.951 30.024 3.442  1.00 35.17 ? 41  ARG   A CD    1 
ATOM   323  N  NE    . ARG   A 1 44  ? -11.836 28.957 3.942  1.00 38.97 ? 41  ARG   A NE    1 
ATOM   324  C  CZ    . ARG   A 1 44  ? -13.170 28.939 3.869  1.00 38.60 ? 41  ARG   A CZ    1 
ATOM   325  N  NH1   . ARG   A 1 44  ? -13.825 27.890 4.373  1.00 38.19 ? 41  ARG   A NH1   1 
ATOM   326  N  NH2   . ARG   A 1 44  ? -13.853 29.928 3.288  1.00 35.62 ? 41  ARG   A NH2   1 
ATOM   327  N  N     . LYS   A 1 45  ? -6.725  27.111 1.187  1.00 19.40 ? 42  LYS   A N     1 
ATOM   328  C  CA    . LYS   A 1 45  ? -6.097  26.662 -0.052 1.00 20.33 ? 42  LYS   A CA    1 
ATOM   329  C  C     . LYS   A 1 45  ? -6.997  25.683 -0.782 1.00 19.10 ? 42  LYS   A C     1 
ATOM   330  O  O     . LYS   A 1 45  ? -7.516  24.753 -0.181 1.00 15.47 ? 42  LYS   A O     1 
ATOM   331  C  CB    . LYS   A 1 45  ? -4.767  25.986 0.233  1.00 23.09 ? 42  LYS   A CB    1 
ATOM   332  C  CG    . LYS   A 1 45  ? -4.123  25.409 -1.022 1.00 25.77 ? 42  LYS   A CG    1 
ATOM   333  C  CD    . LYS   A 1 45  ? -2.613  25.299 -0.944 1.00 27.61 ? 42  LYS   A CD    1 
ATOM   334  C  CE    . LYS   A 1 45  ? -1.995  25.368 -2.334 1.00 29.53 ? 42  LYS   A CE    1 
ATOM   335  N  NZ    . LYS   A 1 45  ? -0.971  24.311 -2.504 1.00 31.56 ? 42  LYS   A NZ    1 
ATOM   336  N  N     . GLN   A 1 46  ? -7.141  25.867 -2.092 1.00 18.56 ? 43  GLN   A N     1 
ATOM   337  C  CA    . GLN   A 1 46  ? -7.965  24.938 -2.916 1.00 17.78 ? 43  GLN   A CA    1 
ATOM   338  C  C     . GLN   A 1 46  ? -7.038  23.973 -3.659 1.00 16.60 ? 43  GLN   A C     1 
ATOM   339  O  O     . GLN   A 1 46  ? -6.133  24.420 -4.299 1.00 16.75 ? 43  GLN   A O     1 
ATOM   340  C  CB    . GLN   A 1 46  ? -8.819  25.728 -3.885 1.00 19.61 ? 43  GLN   A CB    1 
ATOM   341  C  CG    . GLN   A 1 46  ? -9.588  24.880 -4.862 1.00 21.25 ? 43  GLN   A CG    1 
ATOM   342  C  CD    . GLN   A 1 46  ? -10.532 25.784 -5.622 1.00 23.98 ? 43  GLN   A CD    1 
ATOM   343  O  OE1   . GLN   A 1 46  ? -11.570 26.178 -5.138 1.00 29.31 ? 43  GLN   A OE1   1 
ATOM   344  N  NE2   . GLN   A 1 46  ? -10.167 26.095 -6.821 1.00 25.45 ? 43  GLN   A NE2   1 
ATOM   345  N  N     . VAL   A 1 47  ? -7.270  22.666 -3.530 1.00 15.03 ? 44  VAL   A N     1 
ATOM   346  C  CA    . VAL   A 1 47  ? -6.452  21.591 -4.098 1.00 14.86 ? 44  VAL   A CA    1 
ATOM   347  C  C     . VAL   A 1 47  ? -7.355  20.470 -4.644 1.00 14.39 ? 44  VAL   A C     1 
ATOM   348  O  O     . VAL   A 1 47  ? -8.547  20.400 -4.306 1.00 14.79 ? 44  VAL   A O     1 
ATOM   349  C  CB    . VAL   A 1 47  ? -5.493  21.000 -3.043 1.00 15.10 ? 44  VAL   A CB    1 
ATOM   350  C  CG1   . VAL   A 1 47  ? -4.565  22.068 -2.503 1.00 17.19 ? 44  VAL   A CG1   1 
ATOM   351  C  CG2   . VAL   A 1 47  ? -6.265  20.369 -1.895 1.00 15.96 ? 44  VAL   A CG2   1 
ATOM   352  N  N     . VAL   A 1 48  ? -6.812  19.608 -5.498 1.00 14.28 ? 45  VAL   A N     1 
ATOM   353  C  CA    . VAL   A 1 48  ? -7.578  18.455 -6.019 1.00 14.44 ? 45  VAL   A CA    1 
ATOM   354  C  C     . VAL   A 1 48  ? -6.954  17.203 -5.413 1.00 13.60 ? 45  VAL   A C     1 
ATOM   355  O  O     . VAL   A 1 48  ? -5.752  16.956 -5.604 1.00 12.61 ? 45  VAL   A O     1 
ATOM   356  C  CB    . VAL   A 1 48  ? -7.588  18.358 -7.553 1.00 16.19 ? 45  VAL   A CB    1 
ATOM   357  C  CG1   . VAL   A 1 48  ? -8.284  17.085 -8.014 1.00 16.66 ? 45  VAL   A CG1   1 
ATOM   358  C  CG2   . VAL   A 1 48  ? -8.298  19.545 -8.173 1.00 17.24 ? 45  VAL   A CG2   1 
ATOM   359  N  N     . ILE   A 1 49  ? -7.772  16.451 -4.666 1.00 12.76 ? 46  ILE   A N     1 
ATOM   360  C  CA    . ILE   A 1 49  ? -7.384  15.191 -4.012 1.00 12.03 ? 46  ILE   A CA    1 
ATOM   361  C  C     . ILE   A 1 49  ? -8.402  14.111 -4.413 1.00 11.97 ? 46  ILE   A C     1 
ATOM   362  O  O     . ILE   A 1 49  ? -9.585  14.268 -4.152 1.00 11.28 ? 46  ILE   A O     1 
ATOM   363  C  CB    . ILE   A 1 49  ? -7.340  15.352 -2.483 1.00 12.48 ? 46  ILE   A CB    1 
ATOM   364  C  CG1   . ILE   A 1 49  ? -6.422  16.502 -2.046 1.00 12.39 ? 46  ILE   A CG1   1 
ATOM   365  C  CG2   . ILE   A 1 49  ? -6.872  14.081 -1.770 1.00 12.59 ? 46  ILE   A CG2   1 
ATOM   366  C  CD1   . ILE   A 1 49  ? -6.719  17.065 -0.663 1.00 11.83 ? 46  ILE   A CD1   1 
ATOM   367  N  N     . ASP   A 1 50  ? -7.948  13.043 -5.075 1.00 11.63 ? 47  ASP   A N     1 
ATOM   368  C  CA    . ASP   A 1 50  ? -8.829  11.919 -5.537 1.00 11.89 ? 47  ASP   A CA    1 
ATOM   369  C  C     . ASP   A 1 50  ? -10.010 12.372 -6.423 1.00 12.25 ? 47  ASP   A C     1 
ATOM   370  O  O     . ASP   A 1 50  ? -11.146 11.884 -6.322 1.00 12.00 ? 47  ASP   A O     1 
ATOM   371  C  CB    . ASP   A 1 50  ? -9.334  11.039 -4.348 1.00 12.13 ? 47  ASP   A CB    1 
ATOM   372  C  CG    . ASP   A 1 50  ? -8.189  10.500 -3.454 1.00 11.68 ? 47  ASP   A CG    1 
ATOM   373  O  OD1   . ASP   A 1 50  ? -7.309  9.765  -3.939 1.00 12.79 ? 47  ASP   A OD1   1 
ATOM   374  O  OD2   . ASP   A 1 50  ? -8.170  10.808 -2.261 1.00 11.09 ? 47  ASP   A OD2   1 
ATOM   375  N  N     . GLY   A 1 51  ? -9.723  13.347 -7.274 1.00 12.34 ? 48  GLY   A N     1 
ATOM   376  C  CA    . GLY   A 1 51  ? -10.713 13.861 -8.223 1.00 13.34 ? 48  GLY   A CA    1 
ATOM   377  C  C     . GLY   A 1 51  ? -11.667 14.864 -7.636 1.00 13.54 ? 48  GLY   A C     1 
ATOM   378  O  O     . GLY   A 1 51  ? -12.480 15.356 -8.378 1.00 14.34 ? 48  GLY   A O     1 
ATOM   379  N  N     . GLU   A 1 52  ? -11.491 15.201 -6.367 1.00 13.21 ? 49  GLU   A N     1 
ATOM   380  C  CA    . GLU   A 1 52  ? -12.389 16.161 -5.682 1.00 13.67 ? 49  GLU   A CA    1 
ATOM   381  C  C     . GLU   A 1 52  ? -11.705 17.522 -5.496 1.00 12.98 ? 49  GLU   A C     1 
ATOM   382  O  O     . GLU   A 1 52  ? -10.634 17.535 -4.993 1.00 12.14 ? 49  GLU   A O     1 
ATOM   383  C  CB    . GLU   A 1 52  ? -12.755 15.634 -4.313 1.00 13.51 ? 49  GLU   A CB    1 
ATOM   384  C  CG    . GLU   A 1 52  ? -13.853 16.401 -3.591 1.00 14.24 ? 49  GLU   A CG    1 
ATOM   385  C  CD    . GLU   A 1 52  ? -14.208 15.761 -2.255 1.00 14.10 ? 49  GLU   A CD    1 
ATOM   386  O  OE1   . GLU   A 1 52  ? -13.297 15.331 -1.566 1.00 13.80 ? 49  GLU   A OE1   1 
ATOM   387  O  OE2   . GLU   A 1 52  ? -15.360 15.665 -1.943 1.00 15.06 ? 49  GLU   A OE2   1 
ATOM   388  N  N     . THR   A 1 53  ? -12.344 18.596 -5.952 1.00 13.73 ? 50  THR   A N     1 
ATOM   389  C  CA    . THR   A 1 53  ? -11.823 19.943 -5.642 1.00 14.18 ? 50  THR   A CA    1 
ATOM   390  C  C     . THR   A 1 53  ? -12.129 20.222 -4.176 1.00 13.21 ? 50  THR   A C     1 
ATOM   391  O  O     . THR   A 1 53  ? -13.258 20.220 -3.847 1.00 13.74 ? 50  THR   A O     1 
ATOM   392  C  CB    . THR   A 1 53  ? -12.475 20.991 -6.553 1.00 15.21 ? 50  THR   A CB    1 
ATOM   393  O  OG1   . THR   A 1 53  ? -12.176 20.573 -7.871 1.00 15.61 ? 50  THR   A OG1   1 
ATOM   394  C  CG2   . THR   A 1 53  ? -12.006 22.398 -6.249 1.00 15.67 ? 50  THR   A CG2   1 
ATOM   395  N  N     . CYS   A 1 54  ? -11.102 20.401 -3.344 1.00 13.21 ? 51  CYS   A N     1 
ATOM   396  C  CA    . CYS   A 1 54  ? -11.273 20.557 -1.885 1.00 13.38 ? 51  CYS   A CA    1 
ATOM   397  C  C     . CYS   A 1 54  ? -10.833 21.986 -1.460 1.00 13.21 ? 51  CYS   A C     1 
ATOM   398  O  O     . CYS   A 1 54  ? -9.846  22.429 -1.949 1.00 13.41 ? 51  CYS   A O     1 
ATOM   399  C  CB    . CYS   A 1 54  ? -10.390 19.542 -1.138 1.00 12.88 ? 51  CYS   A CB    1 
ATOM   400  S  SG    . CYS   A 1 54  ? -10.656 17.793 -1.577 1.00 13.93 ? 51  CYS   A SG    1 
ATOM   401  N  N     . LEU   A 1 55  ? -11.603 22.636 -0.595 1.00 13.18 ? 52  LEU   A N     1 
ATOM   402  C  CA    . LEU   A 1 55  ? -11.170 23.889 0.051  1.00 14.22 ? 52  LEU   A CA    1 
ATOM   403  C  C     . LEU   A 1 55  ? -10.675 23.564 1.479  1.00 14.19 ? 52  LEU   A C     1 
ATOM   404  O  O     . LEU   A 1 55  ? -11.449 23.158 2.271  1.00 14.10 ? 52  LEU   A O     1 
ATOM   405  C  CB    . LEU   A 1 55  ? -12.295 24.927 0.055  1.00 15.52 ? 52  LEU   A CB    1 
ATOM   406  C  CG    . LEU   A 1 55  ? -11.909 26.275 0.664  1.00 16.88 ? 52  LEU   A CG    1 
ATOM   407  C  CD1   . LEU   A 1 55  ? -10.674 26.839 -0.022 1.00 16.87 ? 52  LEU   A CD1   1 
ATOM   408  C  CD2   . LEU   A 1 55  ? -13.071 27.242 0.560  1.00 18.02 ? 52  LEU   A CD2   1 
ATOM   409  N  N     . LEU   A 1 56  ? -9.367  23.705 1.706  1.00 13.96 ? 53  LEU   A N     1 
ATOM   410  C  CA    . LEU   A 1 56  ? -8.741  23.443 3.002  1.00 13.99 ? 53  LEU   A CA    1 
ATOM   411  C  C     . LEU   A 1 56  ? -8.713  24.747 3.786  1.00 14.36 ? 53  LEU   A C     1 
ATOM   412  O  O     . LEU   A 1 56  ? -8.276  25.772 3.268  1.00 15.00 ? 53  LEU   A O     1 
ATOM   413  C  CB    . LEU   A 1 56  ? -7.311  22.931 2.863  1.00 13.88 ? 53  LEU   A CB    1 
ATOM   414  C  CG    . LEU   A 1 56  ? -7.050  21.761 1.926  1.00 14.18 ? 53  LEU   A CG    1 
ATOM   415  C  CD1   . LEU   A 1 56  ? -5.577  21.389 2.027  1.00 13.81 ? 53  LEU   A CD1   1 
ATOM   416  C  CD2   . LEU   A 1 56  ? -7.974  20.602 2.264  1.00 14.95 ? 53  LEU   A CD2   1 
ATOM   417  N  N     . ASP   A 1 57  ? -9.222  24.710 5.001  1.00 13.92 ? 54  ASP   A N     1 
ATOM   418  C  CA    . ASP   A 1 57  ? -9.088  25.856 5.924  1.00 14.44 ? 54  ASP   A CA    1 
ATOM   419  C  C     . ASP   A 1 57  ? -8.195  25.355 7.035  1.00 13.18 ? 54  ASP   A C     1 
ATOM   420  O  O     . ASP   A 1 57  ? -8.584  24.450 7.770  1.00 13.06 ? 54  ASP   A O     1 
ATOM   421  C  CB    . ASP   A 1 57  ? -10.463 26.306 6.430  1.00 17.05 ? 54  ASP   A CB    1 
ATOM   422  C  CG    . ASP   A 1 57  ? -10.488 27.769 6.944  1.00 19.12 ? 54  ASP   A CG    1 
ATOM   423  O  OD1   . ASP   A 1 57  ? -9.432  28.432 7.046  1.00 21.00 ? 54  ASP   A OD1   1 
ATOM   424  O  OD2   . ASP   A 1 57  ? -11.601 28.265 7.234  1.00 22.23 ? 54  ASP   A OD2   1 
ATOM   425  N  N     . ILE   A 1 58  ? -6.979  25.888 7.118  1.00 12.10 ? 55  ILE   A N     1 
ATOM   426  C  CA    . ILE   A 1 58  ? -5.961  25.313 8.007  1.00 11.85 ? 55  ILE   A CA    1 
ATOM   427  C  C     . ILE   A 1 58  ? -5.604  26.304 9.127  1.00 12.09 ? 55  ILE   A C     1 
ATOM   428  O  O     . ILE   A 1 58  ? -5.236  27.429 8.834  1.00 12.32 ? 55  ILE   A O     1 
ATOM   429  C  CB    . ILE   A 1 58  ? -4.683  24.951 7.234  1.00 11.87 ? 55  ILE   A CB    1 
ATOM   430  C  CG1   . ILE   A 1 58  ? -4.994  23.981 6.090  1.00 12.08 ? 55  ILE   A CG1   1 
ATOM   431  C  CG2   . ILE   A 1 58  ? -3.631  24.397 8.197  1.00 11.36 ? 55  ILE   A CG2   1 
ATOM   432  C  CD1   . ILE   A 1 58  ? -3.909  23.893 5.036  1.00 12.23 ? 55  ILE   A CD1   1 
ATOM   433  N  N     . LEU   A 1 59  ? -5.679  25.859 10.376 1.00 11.58 ? 56  LEU   A N     1 
ATOM   434  C  CA    . LEU   A 1 59  ? -5.290  26.685 11.525 1.00 12.89 ? 56  LEU   A CA    1 
ATOM   435  C  C     . LEU   A 1 59  ? -3.934  26.270 12.091 1.00 12.39 ? 56  LEU   A C     1 
ATOM   436  O  O     . LEU   A 1 59  ? -3.776  25.171 12.632 1.00 11.75 ? 56  LEU   A O     1 
ATOM   437  C  CB    . LEU   A 1 59  ? -6.344  26.621 12.618 1.00 13.42 ? 56  LEU   A CB    1 
ATOM   438  C  CG    . LEU   A 1 59  ? -6.061  27.539 13.808 1.00 14.37 ? 56  LEU   A CG    1 
ATOM   439  C  CD1   . LEU   A 1 59  ? -6.193  28.997 13.371 1.00 15.45 ? 56  LEU   A CD1   1 
ATOM   440  C  CD2   . LEU   A 1 59  ? -7.000  27.229 14.959 1.00 14.88 ? 56  LEU   A CD2   1 
ATOM   441  N  N     . ASP   A 1 60  ? -2.982  27.182 11.980 1.00 13.37 ? 57  ASP   A N     1 
ATOM   442  C  CA    . ASP   A 1 60  ? -1.632  27.011 12.512 1.00 13.77 ? 57  ASP   A CA    1 
ATOM   443  C  C     . ASP   A 1 60  ? -1.603  27.554 13.920 1.00 15.08 ? 57  ASP   A C     1 
ATOM   444  O  O     . ASP   A 1 60  ? -1.562  28.779 14.124 1.00 15.08 ? 57  ASP   A O     1 
ATOM   445  C  CB    . ASP   A 1 60  ? -0.602  27.728 11.611 1.00 13.80 ? 57  ASP   A CB    1 
ATOM   446  C  CG    . ASP   A 1 60  ? 0.801   27.746 12.223 1.00 13.95 ? 57  ASP   A CG    1 
ATOM   447  O  OD1   . ASP   A 1 60  ? 1.080   26.839 13.042 1.00 13.56 ? 57  ASP   A OD1   1 
ATOM   448  O  OD2   . ASP   A 1 60  ? 1.583   28.676 11.877 1.00 15.45 ? 57  ASP   A OD2   1 
ATOM   449  N  N     . THR   A 1 61  ? -1.682  26.644 14.899 1.00 15.40 ? 58  THR   A N     1 
ATOM   450  C  CA    . THR   A 1 61  ? -1.861  27.053 16.280 1.00 16.91 ? 58  THR   A CA    1 
ATOM   451  C  C     . THR   A 1 61  ? -0.542  27.510 16.902 1.00 17.69 ? 58  THR   A C     1 
ATOM   452  O  O     . THR   A 1 61  ? 0.511   26.970 16.592 1.00 17.32 ? 58  THR   A O     1 
ATOM   453  C  CB    . THR   A 1 61  ? -2.555  25.958 17.147 1.00 17.63 ? 58  THR   A CB    1 
ATOM   454  O  OG1   . THR   A 1 61  ? -1.710  24.795 17.304 1.00 17.37 ? 58  THR   A OG1   1 
ATOM   455  C  CG2   . THR   A 1 61  ? -3.931  25.575 16.527 1.00 17.25 ? 58  THR   A CG2   1 
ATOM   456  N  N     . ALA   A 1 62  ? -0.628  28.540 17.741 1.00 20.09 ? 59  ALA   A N     1 
ATOM   457  C  CA    . ALA   A 1 62  ? 0.537   29.093 18.458 1.00 22.13 ? 59  ALA   A CA    1 
ATOM   458  C  C     . ALA   A 1 62  ? 0.564   28.553 19.881 1.00 22.91 ? 59  ALA   A C     1 
ATOM   459  O  O     . ALA   A 1 62  ? 1.230   27.578 20.136 1.00 22.04 ? 59  ALA   A O     1 
ATOM   460  C  CB    . ALA   A 1 62  ? 0.524   30.622 18.444 1.00 23.68 ? 59  ALA   A CB    1 
ATOM   461  N  N     . GLY   A 1 63  ? -0.176  29.173 20.789 1.00 25.52 ? 60  GLY   A N     1 
ATOM   462  C  CA    . GLY   A 1 63  ? -0.128  28.711 22.176 1.00 27.68 ? 60  GLY   A CA    1 
ATOM   463  C  C     . GLY   A 1 63  ? -0.684  27.314 22.358 1.00 28.71 ? 60  GLY   A C     1 
ATOM   464  O  O     . GLY   A 1 63  ? -1.713  27.039 21.786 1.00 27.94 ? 60  GLY   A O     1 
ATOM   465  N  N     . GLN   A 1 64  ? -0.033  26.490 23.182 1.00 28.30 ? 61  GLN   A N     1 
ATOM   466  C  CA    . GLN   A 1 64  ? -0.569  25.117 23.380 1.00 28.68 ? 61  GLN   A CA    1 
ATOM   467  C  C     . GLN   A 1 64  ? -1.096  24.983 24.806 1.00 31.96 ? 61  GLN   A C     1 
ATOM   468  O  O     . GLN   A 1 64  ? -1.057  23.871 25.335 1.00 34.38 ? 61  GLN   A O     1 
ATOM   469  C  CB    . GLN   A 1 64  ? 0.441   23.994 23.099 1.00 26.13 ? 61  GLN   A CB    1 
ATOM   470  C  CG    . GLN   A 1 64  ? 1.112   23.972 21.728 1.00 23.15 ? 61  GLN   A CG    1 
ATOM   471  C  CD    . GLN   A 1 64  ? 0.165   23.793 20.571 1.00 22.51 ? 61  GLN   A CD    1 
ATOM   472  O  OE1   . GLN   A 1 64  ? -0.411  22.739 20.375 1.00 20.89 ? 61  GLN   A OE1   1 
ATOM   473  N  NE2   . GLN   A 1 64  ? 0.029   24.850 19.791 1.00 20.60 ? 61  GLN   A NE2   1 
ATOM   474  N  N     . GLU   A 1 65  ? -1.566  26.075 25.412 1.00 34.37 ? 62  GLU   A N     1 
ATOM   475  C  CA    . GLU   A 1 65  ? -1.915  26.069 26.869 1.00 35.12 ? 62  GLU   A CA    1 
ATOM   476  C  C     . GLU   A 1 65  ? -3.090  25.146 27.224 1.00 34.82 ? 62  GLU   A C     1 
ATOM   477  O  O     . GLU   A 1 65  ? -4.036  25.049 26.471 1.00 32.08 ? 62  GLU   A O     1 
ATOM   478  C  CB    . GLU   A 1 65  ? -1.962  27.495 27.441 1.00 37.26 ? 62  GLU   A CB    1 
ATOM   479  C  CG    . GLU   A 1 65  ? -1.004  28.453 26.752 1.00 39.26 ? 62  GLU   A CG    1 
ATOM   480  C  CD    . GLU   A 1 65  ? -1.528  29.480 25.749 1.00 39.93 ? 62  GLU   A CD    1 
ATOM   481  O  OE1   . GLU   A 1 65  ? -2.505  29.205 25.048 1.00 37.92 ? 62  GLU   A OE1   1 
ATOM   482  O  OE2   . GLU   A 1 65  ? -0.937  30.561 25.663 1.00 39.54 ? 62  GLU   A OE2   1 
ATOM   483  N  N     . GLU   A 1 66  ? -2.991  24.482 28.380 1.00 37.86 ? 63  GLU   A N     1 
ATOM   484  C  CA    . GLU   A 1 66  ? -4.057  23.578 28.859 1.00 36.73 ? 63  GLU   A CA    1 
ATOM   485  C  C     . GLU   A 1 66  ? -5.344  24.374 29.042 1.00 33.43 ? 63  GLU   A C     1 
ATOM   486  O  O     . GLU   A 1 66  ? -6.312  23.972 28.481 1.00 34.32 ? 63  GLU   A O     1 
ATOM   487  C  CB    . GLU   A 1 66  ? -3.646  22.856 30.140 1.00 39.72 ? 63  GLU   A CB    1 
ATOM   488  C  CG    . GLU   A 1 66  ? -4.791  22.144 30.799 1.00 42.85 ? 63  GLU   A CG    1 
ATOM   489  C  CD    . GLU   A 1 66  ? -4.938  20.718 30.363 1.00 44.39 ? 63  GLU   A CD    1 
ATOM   490  O  OE1   . GLU   A 1 66  ? -4.072  20.283 29.625 1.00 48.34 ? 63  GLU   A OE1   1 
ATOM   491  O  OE2   . GLU   A 1 66  ? -5.932  20.070 30.741 1.00 48.27 ? 63  GLU   A OE2   1 
ATOM   492  N  N     . TYR   A 1 67  ? -5.296  25.475 29.787 1.00 30.63 ? 64  TYR   A N     1 
ATOM   493  C  CA    . TYR   A 1 67  ? -6.503  26.289 29.980 1.00 29.23 ? 64  TYR   A CA    1 
ATOM   494  C  C     . TYR   A 1 67  ? -6.567  27.443 28.975 1.00 26.94 ? 64  TYR   A C     1 
ATOM   495  O  O     . TYR   A 1 67  ? -5.885  28.465 29.139 1.00 27.36 ? 64  TYR   A O     1 
ATOM   496  C  CB    . TYR   A 1 67  ? -6.600  26.798 31.433 1.00 31.09 ? 64  TYR   A CB    1 
ATOM   497  C  CG    . TYR   A 1 67  ? -6.491  25.658 32.416 1.00 31.60 ? 64  TYR   A CG    1 
ATOM   498  C  CD1   . TYR   A 1 67  ? -7.525  24.726 32.529 1.00 32.25 ? 64  TYR   A CD1   1 
ATOM   499  C  CD2   . TYR   A 1 67  ? -5.338  25.472 33.191 1.00 31.54 ? 64  TYR   A CD2   1 
ATOM   500  C  CE1   . TYR   A 1 67  ? -7.432  23.654 33.397 1.00 32.85 ? 64  TYR   A CE1   1 
ATOM   501  C  CE2   . TYR   A 1 67  ? -5.239  24.405 34.074 1.00 32.95 ? 64  TYR   A CE2   1 
ATOM   502  C  CZ    . TYR   A 1 67  ? -6.290  23.496 34.167 1.00 34.21 ? 64  TYR   A CZ    1 
ATOM   503  O  OH    . TYR   A 1 67  ? -6.219  22.419 35.020 1.00 36.55 ? 64  TYR   A OH    1 
ATOM   504  N  N     . SER   A 1 68  ? -7.409  27.266 27.953 1.00 24.43 ? 65  SER   A N     1 
ATOM   505  C  CA    . SER   A 1 68  ? -7.647  28.287 26.943 1.00 23.95 ? 65  SER   A CA    1 
ATOM   506  C  C     . SER   A 1 68  ? -9.029  28.110 26.274 1.00 23.83 ? 65  SER   A C     1 
ATOM   507  O  O     . SER   A 1 68  ? -9.258  27.158 25.538 1.00 22.23 ? 65  SER   A O     1 
ATOM   508  C  CB    . SER   A 1 68  ? -6.524  28.230 25.906 1.00 22.88 ? 65  SER   A CB    1 
ATOM   509  O  OG    . SER   A 1 68  ? -6.835  28.959 24.725 1.00 23.11 ? 65  SER   A OG    1 
ATOM   510  N  N     . ALA   A 1 69  ? -9.947  29.038 26.538 1.00 25.26 ? 66  ALA   A N     1 
ATOM   511  C  CA    . ALA   A 1 69  ? -11.258 29.024 25.866 1.00 26.63 ? 66  ALA   A CA    1 
ATOM   512  C  C     . ALA   A 1 69  ? -11.144 28.982 24.334 1.00 25.46 ? 66  ALA   A C     1 
ATOM   513  O  O     . ALA   A 1 69  ? -11.945 28.331 23.668 1.00 24.41 ? 66  ALA   A O     1 
ATOM   514  C  CB    . ALA   A 1 69  ? -12.100 30.218 26.293 1.00 27.86 ? 66  ALA   A CB    1 
ATOM   515  N  N     . MET   A 1 70  ? -10.173 29.692 23.779 1.00 26.23 ? 67  MET   A N     1 
ATOM   516  C  CA    . MET   A 1 70  ? -10.023 29.748 22.306 1.00 27.84 ? 67  MET   A CA    1 
ATOM   517  C  C     . MET   A 1 70  ? -9.574  28.383 21.786 1.00 24.74 ? 67  MET   A C     1 
ATOM   518  O  O     . MET   A 1 70  ? -10.046 27.968 20.761 1.00 21.85 ? 67  MET   A O     1 
ATOM   519  C  CB    . MET   A 1 70  ? -9.078  30.853 21.847 1.00 31.29 ? 67  MET   A CB    1 
ATOM   520  C  CG    . MET   A 1 70  ? -9.723  32.230 21.931 1.00 37.10 ? 67  MET   A CG    1 
ATOM   521  S  SD    . MET   A 1 70  ? -10.315 32.906 20.366 1.00 47.45 ? 67  MET   A SD    1 
ATOM   522  C  CE    . MET   A 1 70  ? -11.985 32.275 20.249 1.00 43.85 ? 67  MET   A CE    1 
ATOM   523  N  N     . ARG   A 1 71  ? -8.697  27.723 22.526 1.00 23.42 ? 68  ARG   A N     1 
ATOM   524  C  CA    . ARG   A 1 71  ? -8.254  26.362 22.154 1.00 23.59 ? 68  ARG   A CA    1 
ATOM   525  C  C     . ARG   A 1 71  ? -9.456  25.415 22.210 1.00 22.57 ? 68  ARG   A C     1 
ATOM   526  O  O     . ARG   A 1 71  ? -9.580  24.580 21.370 1.00 20.35 ? 68  ARG   A O     1 
ATOM   527  C  CB    . ARG   A 1 71  ? -7.162  25.878 23.106 1.00 25.76 ? 68  ARG   A CB    1 
ATOM   528  C  CG    . ARG   A 1 71  ? -6.486  24.602 22.652 1.00 28.26 ? 68  ARG   A CG    1 
ATOM   529  C  CD    . ARG   A 1 71  ? -4.998  24.648 22.978 1.00 32.14 ? 68  ARG   A CD    1 
ATOM   530  N  NE    . ARG   A 1 71  ? -4.447  23.381 22.568 1.00 35.54 ? 68  ARG   A NE    1 
ATOM   531  C  CZ    . ARG   A 1 71  ? -3.543  23.187 21.616 1.00 37.18 ? 68  ARG   A CZ    1 
ATOM   532  N  NH1   . ARG   A 1 71  ? -2.978  24.102 20.885 1.00 37.54 ? 68  ARG   A NH1   1 
ATOM   533  N  NH2   . ARG   A 1 71  ? -3.174  22.009 21.390 1.00 38.20 ? 68  ARG   A NH2   1 
ATOM   534  N  N     . ASP   A 1 72  ? -10.302 25.558 23.215 1.00 23.17 ? 69  ASP   A N     1 
ATOM   535  C  CA    . ASP   A 1 72  ? -11.503 24.690 23.274 1.00 23.78 ? 69  ASP   A CA    1 
ATOM   536  C  C     . ASP   A 1 72  ? -12.401 24.958 22.061 1.00 22.60 ? 69  ASP   A C     1 
ATOM   537  O  O     . ASP   A 1 72  ? -12.924 24.011 21.512 1.00 21.42 ? 69  ASP   A O     1 
ATOM   538  C  CB    . ASP   A 1 72  ? -12.241 24.856 24.608 1.00 26.38 ? 69  ASP   A CB    1 
ATOM   539  C  CG    . ASP   A 1 72  ? -11.464 24.348 25.809 1.00 27.88 ? 69  ASP   A CG    1 
ATOM   540  O  OD1   . ASP   A 1 72  ? -10.681 23.383 25.686 1.00 28.14 ? 69  ASP   A OD1   1 
ATOM   541  O  OD2   . ASP   A 1 72  ? -11.653 24.931 26.860 1.00 31.96 ? 69  ASP   A OD2   1 
ATOM   542  N  N     . GLN   A 1 73  ? -12.530 26.217 21.668 1.00 22.54 ? 70  GLN   A N     1 
ATOM   543  C  CA    . GLN   A 1 73  ? -13.355 26.561 20.507 1.00 23.28 ? 70  GLN   A CA    1 
ATOM   544  C  C     . GLN   A 1 73  ? -12.789 25.972 19.206 1.00 21.37 ? 70  GLN   A C     1 
ATOM   545  O  O     . GLN   A 1 73  ? -13.537 25.431 18.398 1.00 20.61 ? 70  GLN   A O     1 
ATOM   546  C  CB    . GLN   A 1 73  ? -13.516 28.075 20.358 1.00 25.67 ? 70  GLN   A CB    1 
ATOM   547  C  CG    . GLN   A 1 73  ? -14.638 28.514 19.406 1.00 28.27 ? 70  GLN   A CG    1 
ATOM   548  C  CD    . GLN   A 1 73  ? -15.960 27.755 19.596 1.00 30.69 ? 70  GLN   A CD    1 
ATOM   549  O  OE1   . GLN   A 1 73  ? -16.493 27.663 20.710 1.00 36.79 ? 70  GLN   A OE1   1 
ATOM   550  N  NE2   . GLN   A 1 73  ? -16.497 27.216 18.509 1.00 32.20 ? 70  GLN   A NE2   1 
ATOM   551  N  N     . TYR   A 1 74  ? -11.485 26.076 18.976 1.00 20.22 ? 71  TYR   A N     1 
ATOM   552  C  CA    . TYR   A 1 74  ? -10.975 25.505 17.726 1.00 19.31 ? 71  TYR   A CA    1 
ATOM   553  C  C     . TYR   A 1 74  ? -10.884 23.974 17.716 1.00 17.69 ? 71  TYR   A C     1 
ATOM   554  O  O     . TYR   A 1 74  ? -10.942 23.354 16.649 1.00 16.35 ? 71  TYR   A O     1 
ATOM   555  C  CB    . TYR   A 1 74  ? -9.698  26.198 17.210 1.00 19.73 ? 71  TYR   A CB    1 
ATOM   556  C  CG    . TYR   A 1 74  ? -8.405  26.014 17.973 1.00 20.58 ? 71  TYR   A CG    1 
ATOM   557  C  CD1   . TYR   A 1 74  ? -7.835  24.751 18.167 1.00 20.32 ? 71  TYR   A CD1   1 
ATOM   558  C  CD2   . TYR   A 1 74  ? -7.699  27.126 18.423 1.00 21.86 ? 71  TYR   A CD2   1 
ATOM   559  C  CE1   . TYR   A 1 74  ? -6.626  24.606 18.819 1.00 21.38 ? 71  TYR   A CE1   1 
ATOM   560  C  CE2   . TYR   A 1 74  ? -6.495  26.990 19.077 1.00 22.00 ? 71  TYR   A CE2   1 
ATOM   561  C  CZ    . TYR   A 1 74  ? -5.961  25.737 19.275 1.00 22.09 ? 71  TYR   A CZ    1 
ATOM   562  O  OH    . TYR   A 1 74  ? -4.748  25.620 19.925 1.00 23.75 ? 71  TYR   A OH    1 
ATOM   563  N  N     . MET   A 1 75  ? -10.820 23.337 18.879 1.00 17.26 ? 72  MET   A N     1 
ATOM   564  C  CA    . MET   A 1 75  ? -10.962 21.886 18.869 1.00 18.15 ? 72  MET   A CA    1 
ATOM   565  C  C     . MET   A 1 75  ? -12.403 21.473 18.562 1.00 18.35 ? 72  MET   A C     1 
ATOM   566  O  O     . MET   A 1 75  ? -12.610 20.500 17.871 1.00 18.71 ? 72  MET   A O     1 
ATOM   567  C  CB    . MET   A 1 75  ? -10.444 21.257 20.152 1.00 17.98 ? 72  MET   A CB    1 
ATOM   568  C  CG    . MET   A 1 75  ? -8.939  21.416 20.291 1.00 18.76 ? 72  MET   A CG    1 
ATOM   569  S  SD    . MET   A 1 75  ? -8.309  20.539 21.724 1.00 20.43 ? 72  MET   A SD    1 
ATOM   570  C  CE    . MET   A 1 75  ? -6.554  20.812 21.521 1.00 21.00 ? 72  MET   A CE    1 
ATOM   571  N  N     . ARG   A 1 76  ? -13.384 22.235 19.045 1.00 19.09 ? 73  ARG   A N     1 
ATOM   572  C  CA    . ARG   A 1 76  ? -14.790 22.037 18.641 1.00 19.77 ? 73  ARG   A CA    1 
ATOM   573  C  C     . ARG   A 1 76  ? -15.029 22.254 17.145 1.00 18.82 ? 73  ARG   A C     1 
ATOM   574  O  O     . ARG   A 1 76  ? -15.706 21.454 16.481 1.00 18.13 ? 73  ARG   A O     1 
ATOM   575  C  CB    . ARG   A 1 76  ? -15.717 22.930 19.484 1.00 22.01 ? 73  ARG   A CB    1 
ATOM   576  C  CG    . ARG   A 1 76  ? -15.925 22.410 20.897 1.00 24.26 ? 73  ARG   A CG    1 
ATOM   577  C  CD    . ARG   A 1 76  ? -17.048 23.140 21.617 1.00 27.08 ? 73  ARG   A CD    1 
ATOM   578  N  NE    . ARG   A 1 76  ? -16.778 24.572 21.803 1.00 29.79 ? 73  ARG   A NE    1 
ATOM   579  C  CZ    . ARG   A 1 76  ? -16.264 25.132 22.903 1.00 31.46 ? 73  ARG   A CZ    1 
ATOM   580  N  NH1   . ARG   A 1 76  ? -15.919 24.397 23.967 1.00 31.72 ? 73  ARG   A NH1   1 
ATOM   581  N  NH2   . ARG   A 1 76  ? -16.085 26.452 22.944 1.00 32.29 ? 73  ARG   A NH2   1 
ATOM   582  N  N     . THR   A 1 77  ? -14.455 23.323 16.600 1.00 18.10 ? 74  THR   A N     1 
ATOM   583  C  CA    . THR   A 1 77  ? -14.662 23.668 15.186 1.00 17.06 ? 74  THR   A CA    1 
ATOM   584  C  C     . THR   A 1 77  ? -13.884 22.780 14.194 1.00 15.94 ? 74  THR   A C     1 
ATOM   585  O  O     . THR   A 1 77  ? -14.360 22.498 13.090 1.00 15.77 ? 74  THR   A O     1 
ATOM   586  C  CB    . THR   A 1 77  ? -14.320 25.144 14.957 1.00 17.72 ? 74  THR   A CB    1 
ATOM   587  O  OG1   . THR   A 1 77  ? -15.114 25.932 15.855 1.00 19.33 ? 74  THR   A OG1   1 
ATOM   588  C  CG2   . THR   A 1 77  ? -14.630 25.573 13.538 1.00 18.07 ? 74  THR   A CG2   1 
ATOM   589  N  N     . GLY   A 1 78  ? -12.690 22.345 14.573 1.00 13.97 ? 75  GLY   A N     1 
ATOM   590  C  CA    . GLY   A 1 78  ? -11.816 21.620 13.616 1.00 13.03 ? 75  GLY   A CA    1 
ATOM   591  C  C     . GLY   A 1 78  ? -12.327 20.229 13.329 1.00 12.50 ? 75  GLY   A C     1 
ATOM   592  O  O     . GLY   A 1 78  ? -12.880 19.573 14.219 1.00 13.79 ? 75  GLY   A O     1 
ATOM   593  N  N     . GLU   A 1 79  ? -12.111 19.766 12.106 1.00 11.81 ? 76  GLU   A N     1 
ATOM   594  C  CA    . GLU   A 1 79  ? -12.577 18.444 11.679 1.00 12.12 ? 76  GLU   A CA    1 
ATOM   595  C  C     . GLU   A 1 79  ? -11.496 17.362 11.761 1.00 11.26 ? 76  GLU   A C     1 
ATOM   596  O  O     . GLU   A 1 79  ? -11.799 16.229 12.152 1.00 11.31 ? 76  GLU   A O     1 
ATOM   597  C  CB    . GLU   A 1 79  ? -13.161 18.523 10.285 1.00 12.48 ? 76  GLU   A CB    1 
ATOM   598  C  CG    . GLU   A 1 79  ? -14.419 19.354 10.220 1.00 14.31 ? 76  GLU   A CG    1 
ATOM   599  C  CD    . GLU   A 1 79  ? -14.958 19.482 8.813  1.00 15.45 ? 76  GLU   A CD    1 
ATOM   600  O  OE1   . GLU   A 1 79  ? -14.217 19.887 7.904  1.00 15.20 ? 76  GLU   A OE1   1 
ATOM   601  O  OE2   . GLU   A 1 79  ? -16.149 19.132 8.599  1.00 20.18 ? 76  GLU   A OE2   1 
ATOM   602  N  N     . GLY   A 1 80  ? -10.254 17.712 11.407 1.00 10.52 ? 77  GLY   A N     1 
ATOM   603  C  CA    . GLY   A 1 80  ? -9.130  16.805 11.571 1.00 10.01 ? 77  GLY   A CA    1 
ATOM   604  C  C     . GLY   A 1 80  ? -7.895  17.510 12.125 1.00 9.77  ? 77  GLY   A C     1 
ATOM   605  O  O     . GLY   A 1 80  ? -7.695  18.728 11.947 1.00 10.06 ? 77  GLY   A O     1 
ATOM   606  N  N     . PHE   A 1 81  ? -7.062  16.703 12.769 1.00 9.82  ? 78  PHE   A N     1 
ATOM   607  C  CA    . PHE   A 1 81  ? -5.922  17.191 13.580 1.00 10.07 ? 78  PHE   A CA    1 
ATOM   608  C  C     . PHE   A 1 81  ? -4.602  16.566 13.110 1.00 10.17 ? 78  PHE   A C     1 
ATOM   609  O  O     . PHE   A 1 81  ? -4.446  15.335 13.083 1.00 10.54 ? 78  PHE   A O     1 
ATOM   610  C  CB    . PHE   A 1 81  ? -6.208  16.938 15.046 1.00 10.38 ? 78  PHE   A CB    1 
ATOM   611  C  CG    . PHE   A 1 81  ? -7.463  17.617 15.507 1.00 10.42 ? 78  PHE   A CG    1 
ATOM   612  C  CD1   . PHE   A 1 81  ? -8.693  17.023 15.309 1.00 10.67 ? 78  PHE   A CD1   1 
ATOM   613  C  CD2   . PHE   A 1 81  ? -7.409  18.897 16.066 1.00 10.89 ? 78  PHE   A CD2   1 
ATOM   614  C  CE1   . PHE   A 1 81  ? -9.852  17.669 15.672 1.00 11.28 ? 78  PHE   A CE1   1 
ATOM   615  C  CE2   . PHE   A 1 81  ? -8.574  19.547 16.451 1.00 11.71 ? 78  PHE   A CE2   1 
ATOM   616  C  CZ    . PHE   A 1 81  ? -9.792  18.929 16.241 1.00 11.69 ? 78  PHE   A CZ    1 
ATOM   617  N  N     . LEU   A 1 82  ? -3.688  17.463 12.738 1.00 9.94  ? 79  LEU   A N     1 
ATOM   618  C  CA    . LEU   A 1 82  ? -2.316  17.088 12.360 1.00 10.25 ? 79  LEU   A CA    1 
ATOM   619  C  C     . LEU   A 1 82  ? -1.540  17.163 13.673 1.00 10.62 ? 79  LEU   A C     1 
ATOM   620  O  O     . LEU   A 1 82  ? -1.440  18.209 14.219 1.00 10.13 ? 79  LEU   A O     1 
ATOM   621  C  CB    . LEU   A 1 82  ? -1.786  18.052 11.288 1.00 10.80 ? 79  LEU   A CB    1 
ATOM   622  C  CG    . LEU   A 1 82  ? -0.775  17.428 10.347 1.00 11.27 ? 79  LEU   A CG    1 
ATOM   623  C  CD1   . LEU   A 1 82  ? -1.471  16.450 9.434  1.00 11.91 ? 79  LEU   A CD1   1 
ATOM   624  C  CD2   . LEU   A 1 82  ? 0.017   18.449 9.555  1.00 11.44 ? 79  LEU   A CD2   1 
ATOM   625  N  N     . CYS   A 1 83  ? -1.127  16.012 14.172 1.00 10.77 ? 80  CYS   A N     1 
ATOM   626  C  CA    . CYS   A 1 83  ? -0.427  15.945 15.473 1.00 11.65 ? 80  CYS   A CA    1 
ATOM   627  C  C     . CYS   A 1 83  ? 1.064   15.842 15.188 1.00 11.62 ? 80  CYS   A C     1 
ATOM   628  O  O     . CYS   A 1 83  ? 1.470   14.798 14.773 1.00 11.04 ? 80  CYS   A O     1 
ATOM   629  C  CB    . CYS   A 1 83  ? -0.954  14.803 16.306 1.00 12.51 ? 80  CYS   A CB    1 
ATOM   630  S  SG    . CYS   A 1 83  ? -2.628  15.249 16.852 1.00 17.31 ? 80  CYS   A SG    1 
ATOM   631  N  N     . VAL   A 1 84  ? 1.782   16.921 15.514 1.00 11.17 ? 81  VAL   A N     1 
ATOM   632  C  CA    . VAL   A 1 84  ? 3.214   17.016 15.114 1.00 10.95 ? 81  VAL   A CA    1 
ATOM   633  C  C     . VAL   A 1 84  ? 4.207   16.945 16.292 1.00 11.00 ? 81  VAL   A C     1 
ATOM   634  O  O     . VAL   A 1 84  ? 4.044   17.626 17.236 1.00 10.78 ? 81  VAL   A O     1 
ATOM   635  C  CB    . VAL   A 1 84  ? 3.467   18.286 14.281 1.00 10.58 ? 81  VAL   A CB    1 
ATOM   636  C  CG1   . VAL   A 1 84  ? 4.842   18.348 13.652 1.00 11.00 ? 81  VAL   A CG1   1 
ATOM   637  C  CG2   . VAL   A 1 84  ? 2.395   18.535 13.247 1.00 10.48 ? 81  VAL   A CG2   1 
ATOM   638  N  N     . PHE   A 1 85  ? 5.208   16.082 16.124 1.00 10.72 ? 82  PHE   A N     1 
ATOM   639  C  CA    . PHE   A 1 85  ? 6.417   16.003 16.984 1.00 11.01 ? 82  PHE   A CA    1 
ATOM   640  C  C     . PHE   A 1 85  ? 7.645   16.119 16.048 1.00 10.97 ? 82  PHE   A C     1 
ATOM   641  O  O     . PHE   A 1 85  ? 7.515   15.985 14.870 1.00 11.17 ? 82  PHE   A O     1 
ATOM   642  C  CB    . PHE   A 1 85  ? 6.452   14.753 17.872 1.00 10.61 ? 82  PHE   A CB    1 
ATOM   643  C  CG    . PHE   A 1 85  ? 6.773   13.481 17.132 1.00 10.60 ? 82  PHE   A CG    1 
ATOM   644  C  CD1   . PHE   A 1 85  ? 5.782   12.730 16.539 1.00 10.40 ? 82  PHE   A CD1   1 
ATOM   645  C  CD2   . PHE   A 1 85  ? 8.074   13.037 17.001 1.00 10.69 ? 82  PHE   A CD2   1 
ATOM   646  C  CE1   . PHE   A 1 85  ? 6.082   11.584 15.831 1.00 10.12 ? 82  PHE   A CE1   1 
ATOM   647  C  CE2   . PHE   A 1 85  ? 8.361   11.891 16.302 1.00 10.31 ? 82  PHE   A CE2   1 
ATOM   648  C  CZ    . PHE   A 1 85  ? 7.370   11.168 15.701 1.00 10.46 ? 82  PHE   A CZ    1 
ATOM   649  N  N     . ALA   A 1 86  ? 8.792   16.417 16.639 1.00 10.78 ? 83  ALA   A N     1 
ATOM   650  C  CA    . ALA   A 1 86  ? 10.066  16.511 15.912 1.00 11.36 ? 83  ALA   A CA    1 
ATOM   651  C  C     . ALA   A 1 86  ? 10.902  15.269 16.204 1.00 11.85 ? 83  ALA   A C     1 
ATOM   652  O  O     . ALA   A 1 86  ? 11.000  14.846 17.385 1.00 11.88 ? 83  ALA   A O     1 
ATOM   653  C  CB    . ALA   A 1 86  ? 10.811  17.742 16.349 1.00 11.52 ? 83  ALA   A CB    1 
ATOM   654  N  N     . ILE   A 1 87  ? 11.506  14.671 15.175 1.00 11.86 ? 84  ILE   A N     1 
ATOM   655  C  CA    . ILE   A 1 87  ? 12.173  13.377 15.413 1.00 12.51 ? 84  ILE   A CA    1 
ATOM   656  C  C     . ILE   A 1 87  ? 13.448  13.462 16.264 1.00 13.45 ? 84  ILE   A C     1 
ATOM   657  O  O     . ILE   A 1 87  ? 13.995  12.428 16.671 1.00 13.77 ? 84  ILE   A O     1 
ATOM   658  C  CB    . ILE   A 1 87  ? 12.493  12.628 14.105 1.00 12.52 ? 84  ILE   A CB    1 
ATOM   659  C  CG1   . ILE   A 1 87  ? 13.517  13.414 13.264 1.00 13.17 ? 84  ILE   A CG1   1 
ATOM   660  C  CG2   . ILE   A 1 87  ? 11.202  12.365 13.345 1.00 12.51 ? 84  ILE   A CG2   1 
ATOM   661  C  CD1   . ILE   A 1 87  ? 14.267  12.564 12.290 1.00 13.87 ? 84  ILE   A CD1   1 
ATOM   662  N  N     . ASN   A 1 88  ? 13.904  14.684 16.543 1.00 14.18 ? 85  ASN   A N     1 
ATOM   663  C  CA    . ASN   A 1 88  ? 15.046  14.946 17.452 1.00 15.35 ? 85  ASN   A CA    1 
ATOM   664  C  C     . ASN   A 1 88  ? 14.654  15.501 18.833 1.00 16.08 ? 85  ASN   A C     1 
ATOM   665  O  O     . ASN   A 1 88  ? 15.504  16.060 19.559 1.00 18.23 ? 85  ASN   A O     1 
ATOM   666  C  CB    . ASN   A 1 88  ? 16.058  15.886 16.755 1.00 15.77 ? 85  ASN   A CB    1 
ATOM   667  C  CG    . ASN   A 1 88  ? 15.519  17.302 16.563 1.00 15.80 ? 85  ASN   A CG    1 
ATOM   668  O  OD1   . ASN   A 1 88  ? 14.312  17.512 16.427 1.00 15.69 ? 85  ASN   A OD1   1 
ATOM   669  N  ND2   . ASN   A 1 88  ? 16.417  18.290 16.567 1.00 15.26 ? 85  ASN   A ND2   1 
ATOM   670  N  N     . ASN   A 1 89  ? 13.387  15.351 19.222 1.00 15.69 ? 86  ASN   A N     1 
ATOM   671  C  CA    . ASN   A 1 89  ? 12.886  15.953 20.475 1.00 16.59 ? 86  ASN   A CA    1 
ATOM   672  C  C     . ASN   A 1 89  ? 11.945  14.925 21.100 1.00 16.20 ? 86  ASN   A C     1 
ATOM   673  O  O     . ASN   A 1 89  ? 10.753  14.877 20.776 1.00 14.85 ? 86  ASN   A O     1 
ATOM   674  C  CB    . ASN   A 1 89  ? 12.190  17.285 20.195 1.00 17.59 ? 86  ASN   A CB    1 
ATOM   675  C  CG    . ASN   A 1 89  ? 11.521  17.917 21.423 1.00 19.08 ? 86  ASN   A CG    1 
ATOM   676  O  OD1   . ASN   A 1 89  ? 11.378  17.329 22.486 1.00 19.93 ? 86  ASN   A OD1   1 
ATOM   677  N  ND2   . ASN   A 1 89  ? 11.071  19.155 21.242 1.00 21.58 ? 86  ASN   A ND2   1 
ATOM   678  N  N     . THR   A 1 90  ? 12.511  14.081 21.954 1.00 16.50 ? 87  THR   A N     1 
ATOM   679  C  CA    . THR   A 1 90  ? 11.736  13.050 22.628 1.00 17.04 ? 87  THR   A CA    1 
ATOM   680  C  C     . THR   A 1 90  ? 10.567  13.609 23.459 1.00 18.25 ? 87  THR   A C     1 
ATOM   681  O  O     . THR   A 1 90  ? 9.478   13.039 23.445 1.00 19.63 ? 87  THR   A O     1 
ATOM   682  C  CB    . THR   A 1 90  ? 12.643  12.165 23.483 1.00 18.06 ? 87  THR   A CB    1 
ATOM   683  O  OG1   . THR   A 1 90  ? 13.551  11.454 22.633 1.00 18.65 ? 87  THR   A OG1   1 
ATOM   684  C  CG2   . THR   A 1 90  ? 11.812  11.164 24.268 1.00 18.68 ? 87  THR   A CG2   1 
ATOM   685  N  N     . LYS   A 1 91  ? 10.769  14.734 24.139 1.00 18.27 ? 88  LYS   A N     1 
ATOM   686  C  CA    . LYS   A 1 91  ? 9.687   15.374 24.904 1.00 19.54 ? 88  LYS   A CA    1 
ATOM   687  C  C     . LYS   A 1 91  ? 8.454   15.673 24.036 1.00 18.14 ? 88  LYS   A C     1 
ATOM   688  O  O     . LYS   A 1 91  ? 7.306   15.460 24.467 1.00 18.35 ? 88  LYS   A O     1 
ATOM   689  C  CB    . LYS   A 1 91  ? 10.196  16.664 25.579 1.00 21.39 ? 88  LYS   A CB    1 
ATOM   690  C  CG    . LYS   A 1 91  ? 9.148   17.469 26.333 1.00 24.94 ? 88  LYS   A CG    1 
ATOM   691  C  CD    . LYS   A 1 91  ? 8.647   16.744 27.587 1.00 27.24 ? 88  LYS   A CD    1 
ATOM   692  C  CE    . LYS   A 1 91  ? 7.889   17.679 28.540 1.00 30.45 ? 88  LYS   A CE    1 
ATOM   693  N  NZ    . LYS   A 1 91  ? 6.772   18.448 27.897 1.00 32.26 ? 88  LYS   A NZ    1 
ATOM   694  N  N     . SER   A 1 92  ? 8.692   16.182 22.831 1.00 16.24 ? 89  SER   A N     1 
ATOM   695  C  CA    . SER   A 1 92  ? 7.624   16.487 21.878 1.00 15.26 ? 89  SER   A CA    1 
ATOM   696  C  C     . SER   A 1 92  ? 6.829   15.237 21.448 1.00 14.92 ? 89  SER   A C     1 
ATOM   697  O  O     . SER   A 1 92  ? 5.614   15.320 21.187 1.00 15.11 ? 89  SER   A O     1 
ATOM   698  C  CB    . SER   A 1 92  ? 8.199   17.236 20.659 1.00 14.73 ? 89  SER   A CB    1 
ATOM   699  O  OG    . SER   A 1 92  ? 8.874   16.373 19.743 1.00 12.76 ? 89  SER   A OG    1 
ATOM   700  N  N     . PHE   A 1 93  ? 7.497   14.094 21.375 1.00 14.48 ? 90  PHE   A N     1 
ATOM   701  C  CA    . PHE   A 1 93  ? 6.830   12.823 21.036 1.00 15.36 ? 90  PHE   A CA    1 
ATOM   702  C  C     . PHE   A 1 93  ? 5.986   12.334 22.236 1.00 16.55 ? 90  PHE   A C     1 
ATOM   703  O  O     . PHE   A 1 93  ? 4.873   11.800 22.080 1.00 15.51 ? 90  PHE   A O     1 
ATOM   704  C  CB    . PHE   A 1 93  ? 7.885   11.781 20.593 1.00 14.86 ? 90  PHE   A CB    1 
ATOM   705  C  CG    . PHE   A 1 93  ? 7.344   10.391 20.345 1.00 14.62 ? 90  PHE   A CG    1 
ATOM   706  C  CD1   . PHE   A 1 93  ? 6.493   10.131 19.281 1.00 14.19 ? 90  PHE   A CD1   1 
ATOM   707  C  CD2   . PHE   A 1 93  ? 7.704   9.327  21.202 1.00 15.89 ? 90  PHE   A CD2   1 
ATOM   708  C  CE1   . PHE   A 1 93  ? 6.031   8.850  19.051 1.00 14.46 ? 90  PHE   A CE1   1 
ATOM   709  C  CE2   . PHE   A 1 93  ? 7.229   8.044  20.979 1.00 16.02 ? 90  PHE   A CE2   1 
ATOM   710  C  CZ    . PHE   A 1 93  ? 6.397   7.804  19.908 1.00 15.26 ? 90  PHE   A CZ    1 
ATOM   711  N  N     . GLU   A 1 94  ? 6.522   12.541 23.439 1.00 18.26 ? 91  GLU   A N     1 
ATOM   712  C  CA    . GLU   A 1 94  ? 5.785   12.251 24.691 1.00 20.61 ? 91  GLU   A CA    1 
ATOM   713  C  C     . GLU   A 1 94  ? 4.604   13.180 24.927 1.00 21.18 ? 91  GLU   A C     1 
ATOM   714  O  O     . GLU   A 1 94  ? 3.626   12.775 25.558 1.00 23.25 ? 91  GLU   A O     1 
ATOM   715  C  CB    . GLU   A 1 94  ? 6.732   12.319 25.881 1.00 22.09 ? 91  GLU   A CB    1 
ATOM   716  C  CG    . GLU   A 1 94  ? 7.761   11.201 25.856 1.00 23.57 ? 91  GLU   A CG    1 
ATOM   717  C  CD    . GLU   A 1 94  ? 8.561   11.126 27.146 1.00 25.89 ? 91  GLU   A CD    1 
ATOM   718  O  OE1   . GLU   A 1 94  ? 8.156   11.776 28.130 1.00 30.39 ? 91  GLU   A OE1   1 
ATOM   719  O  OE2   . GLU   A 1 94  ? 9.587   10.422 27.192 1.00 26.15 ? 91  GLU   A OE2   1 
ATOM   720  N  N     . ASP   A 1 95  ? 4.676   14.408 24.422 1.00 21.28 ? 92  ASP   A N     1 
ATOM   721  C  CA    . ASP   A 1 95  ? 3.537   15.340 24.481 1.00 21.18 ? 92  ASP   A CA    1 
ATOM   722  C  C     . ASP   A 1 95  ? 2.300   14.853 23.692 1.00 19.60 ? 92  ASP   A C     1 
ATOM   723  O  O     . ASP   A 1 95  ? 1.180   15.259 24.027 1.00 18.62 ? 92  ASP   A O     1 
ATOM   724  C  CB    . ASP   A 1 95  ? 3.924   16.755 23.983 1.00 22.90 ? 92  ASP   A CB    1 
ATOM   725  C  CG    . ASP   A 1 95  ? 4.783   17.556 24.992 1.00 25.28 ? 92  ASP   A CG    1 
ATOM   726  O  OD1   . ASP   A 1 95  ? 4.966   17.141 26.169 1.00 26.07 ? 92  ASP   A OD1   1 
ATOM   727  O  OD2   . ASP   A 1 95  ? 5.288   18.628 24.584 1.00 27.34 ? 92  ASP   A OD2   1 
ATOM   728  N  N     . ILE   A 1 96  ? 2.497   14.011 22.655 1.00 16.77 ? 93  ILE   A N     1 
ATOM   729  C  CA    . ILE   A 1 96  ? 1.435   13.677 21.680 1.00 16.05 ? 93  ILE   A CA    1 
ATOM   730  C  C     . ILE   A 1 96  ? 0.200   13.120 22.370 1.00 16.65 ? 93  ILE   A C     1 
ATOM   731  O  O     . ILE   A 1 96  ? -0.937  13.448 22.013 1.00 16.39 ? 93  ILE   A O     1 
ATOM   732  C  CB    . ILE   A 1 96  ? 1.934   12.647 20.608 1.00 14.82 ? 93  ILE   A CB    1 
ATOM   733  C  CG1   . ILE   A 1 96  ? 2.958   13.295 19.654 1.00 13.44 ? 93  ILE   A CG1   1 
ATOM   734  C  CG2   . ILE   A 1 96  ? 0.786   12.001 19.814 1.00 15.32 ? 93  ILE   A CG2   1 
ATOM   735  C  CD1   . ILE   A 1 96  ? 2.464   14.428 18.760 1.00 13.09 ? 93  ILE   A CD1   1 
ATOM   736  N  N     . HIS   A 1 97  ? 0.442   12.253 23.347 1.00 17.95 ? 94  HIS   A N     1 
ATOM   737  C  CA    . HIS   A 1 97  ? -0.624  11.593 24.084 1.00 20.46 ? 94  HIS   A CA    1 
ATOM   738  C  C     . HIS   A 1 97  ? -1.593  12.630 24.669 1.00 20.01 ? 94  HIS   A C     1 
ATOM   739  O  O     . HIS   A 1 97  ? -2.813  12.452 24.604 1.00 20.31 ? 94  HIS   A O     1 
ATOM   740  C  CB    . HIS   A 1 97  ? 0.013   10.702 25.162 1.00 23.98 ? 94  HIS   A CB    1 
ATOM   741  C  CG    . HIS   A 1 97  ? -0.909  10.332 26.270 1.00 26.69 ? 94  HIS   A CG    1 
ATOM   742  N  ND1   . HIS   A 1 97  ? -1.736  9.230  26.207 1.00 30.35 ? 94  HIS   A ND1   1 
ATOM   743  C  CD2   . HIS   A 1 97  ? -1.145  10.917 27.466 1.00 28.30 ? 94  HIS   A CD2   1 
ATOM   744  C  CE1   . HIS   A 1 97  ? -2.457  9.162  27.313 1.00 29.91 ? 94  HIS   A CE1   1 
ATOM   745  N  NE2   . HIS   A 1 97  ? -2.121  10.178 28.090 1.00 31.02 ? 94  HIS   A NE2   1 
ATOM   746  N  N     . HIS   A 1 98  ? -1.058  13.716 25.213 1.00 18.87 ? 95  HIS   A N     1 
ATOM   747  C  CA    . HIS   A 1 98  ? -1.882  14.746 25.850 1.00 20.35 ? 95  HIS   A CA    1 
ATOM   748  C  C     . HIS   A 1 98  ? -2.768  15.525 24.869 1.00 20.09 ? 95  HIS   A C     1 
ATOM   749  O  O     . HIS   A 1 98  ? -3.933  15.855 25.197 1.00 19.36 ? 95  HIS   A O     1 
ATOM   750  C  CB    . HIS   A 1 98  ? -0.987  15.733 26.609 1.00 22.14 ? 95  HIS   A CB    1 
ATOM   751  C  CG    . HIS   A 1 98  ? -0.189  15.096 27.702 1.00 25.27 ? 95  HIS   A CG    1 
ATOM   752  N  ND1   . HIS   A 1 98  ? -0.752  14.259 28.645 1.00 28.91 ? 95  HIS   A ND1   1 
ATOM   753  C  CD2   . HIS   A 1 98  ? 1.131   15.169 28.003 1.00 27.00 ? 95  HIS   A CD2   1 
ATOM   754  C  CE1   . HIS   A 1 98  ? 0.183   13.857 29.491 1.00 29.97 ? 95  HIS   A CE1   1 
ATOM   755  N  NE2   . HIS   A 1 98  ? 1.334   14.394 29.122 1.00 28.39 ? 95  HIS   A NE2   1 
ATOM   756  N  N     . TYR   A 1 99  ? -2.224  15.845 23.689 1.00 19.48 ? 96  TYR   A N     1 
ATOM   757  C  CA    . TYR   A 1 99  ? -3.047  16.438 22.600 1.00 19.42 ? 96  TYR   A CA    1 
ATOM   758  C  C     . TYR   A 1 99  ? -4.195  15.521 22.176 1.00 18.83 ? 96  TYR   A C     1 
ATOM   759  O  O     . TYR   A 1 99  ? -5.331  15.973 22.013 1.00 17.99 ? 96  TYR   A O     1 
ATOM   760  C  CB    . TYR   A 1 99  ? -2.189  16.778 21.358 1.00 20.08 ? 96  TYR   A CB    1 
ATOM   761  C  CG    . TYR   A 1 99  ? -1.173  17.838 21.621 1.00 21.98 ? 96  TYR   A CG    1 
ATOM   762  C  CD1   . TYR   A 1 99  ? -1.565  19.080 22.098 1.00 24.32 ? 96  TYR   A CD1   1 
ATOM   763  C  CD2   . TYR   A 1 99  ? 0.181   17.614 21.425 1.00 23.01 ? 96  TYR   A CD2   1 
ATOM   764  C  CE1   . TYR   A 1 99  ? -0.642  20.072 22.380 1.00 26.00 ? 96  TYR   A CE1   1 
ATOM   765  C  CE2   . TYR   A 1 99  ? 1.126   18.599 21.709 1.00 23.90 ? 96  TYR   A CE2   1 
ATOM   766  C  CZ    . TYR   A 1 99  ? 0.706   19.838 22.189 1.00 26.02 ? 96  TYR   A CZ    1 
ATOM   767  O  OH    . TYR   A 1 99  ? 1.605   20.852 22.502 1.00 28.61 ? 96  TYR   A OH    1 
ATOM   768  N  N     . ARG   A 1 100 ? -3.909  14.240 21.976 1.00 19.04 ? 97  ARG   A N     1 
ATOM   769  C  CA    . ARG   A 1 100 ? -4.964  13.311 21.585 1.00 19.89 ? 97  ARG   A CA    1 
ATOM   770  C  C     . ARG   A 1 100 ? -6.069  13.177 22.659 1.00 20.95 ? 97  ARG   A C     1 
ATOM   771  O  O     . ARG   A 1 100 ? -7.262  13.141 22.320 1.00 20.63 ? 97  ARG   A O     1 
ATOM   772  C  CB    . ARG   A 1 100 ? -4.388  11.942 21.206 1.00 20.39 ? 97  ARG   A CB    1 
ATOM   773  C  CG    . ARG   A 1 100 ? -5.468  10.962 20.791 1.00 22.20 ? 97  ARG   A CG    1 
ATOM   774  C  CD    . ARG   A 1 100 ? -4.913  9.645  20.307 1.00 24.14 ? 97  ARG   A CD    1 
ATOM   775  N  NE    . ARG   A 1 100 ? -5.981  8.666  20.152 1.00 25.42 ? 97  ARG   A NE    1 
ATOM   776  C  CZ    . ARG   A 1 100 ? -6.779  8.559  19.089 1.00 25.57 ? 97  ARG   A CZ    1 
ATOM   777  N  NH1   . ARG   A 1 100 ? -6.643  9.373  18.043 1.00 25.97 ? 97  ARG   A NH1   1 
ATOM   778  N  NH2   . ARG   A 1 100 ? -7.731  7.622  19.075 1.00 27.42 ? 97  ARG   A NH2   1 
ATOM   779  N  N     . GLU   A 1 101 ? -5.682  13.110 23.930 1.00 21.96 ? 98  GLU   A N     1 
ATOM   780  C  CA    . GLU   A 1 101 ? -6.643  13.061 25.044 1.00 24.19 ? 98  GLU   A CA    1 
ATOM   781  C  C     . GLU   A 1 101 ? -7.474  14.342 25.191 1.00 23.85 ? 98  GLU   A C     1 
ATOM   782  O  O     . GLU   A 1 101 ? -8.665  14.258 25.541 1.00 23.72 ? 98  GLU   A O     1 
ATOM   783  C  CB    . GLU   A 1 101 ? -5.930  12.781 26.376 1.00 26.78 ? 98  GLU   A CB    1 
ATOM   784  C  CG    . GLU   A 1 101 ? -5.290  11.400 26.474 1.00 29.70 ? 98  GLU   A CG    1 
ATOM   785  C  CD    . GLU   A 1 101 ? -6.318  10.291 26.449 1.00 33.31 ? 98  GLU   A CD    1 
ATOM   786  O  OE1   . GLU   A 1 101 ? -7.101  10.230 27.416 1.00 37.17 ? 98  GLU   A OE1   1 
ATOM   787  O  OE2   . GLU   A 1 101 ? -6.363  9.501  25.467 1.00 36.91 ? 98  GLU   A OE2   1 
ATOM   788  N  N     . GLN   A 1 102 ? -6.852  15.501 24.930 1.00 23.82 ? 99  GLN   A N     1 
ATOM   789  C  CA    . GLN   A 1 102 ? -7.546  16.805 24.921 1.00 24.31 ? 99  GLN   A CA    1 
ATOM   790  C  C     . GLN   A 1 102 ? -8.620  16.834 23.819 1.00 22.11 ? 99  GLN   A C     1 
ATOM   791  O  O     . GLN   A 1 102 ? -9.749  17.235 24.063 1.00 20.51 ? 99  GLN   A O     1 
ATOM   792  C  CB    . GLN   A 1 102 ? -6.582  17.981 24.688 1.00 26.15 ? 99  GLN   A CB    1 
ATOM   793  C  CG    . GLN   A 1 102 ? -5.777  18.433 25.898 1.00 29.90 ? 99  GLN   A CG    1 
ATOM   794  C  CD    . GLN   A 1 102 ? -4.786  19.562 25.593 1.00 31.65 ? 99  GLN   A CD    1 
ATOM   795  O  OE1   . GLN   A 1 102 ? -4.557  19.937 24.429 1.00 34.41 ? 99  GLN   A OE1   1 
ATOM   796  N  NE2   . GLN   A 1 102 ? -4.184  20.111 26.654 1.00 35.82 ? 99  GLN   A NE2   1 
ATOM   797  N  N     . ILE   A 1 103 ? -8.252  16.415 22.618 1.00 19.71 ? 100 ILE   A N     1 
ATOM   798  C  CA    . ILE   A 1 103 ? -9.170  16.476 21.461 1.00 19.91 ? 100 ILE   A CA    1 
ATOM   799  C  C     . ILE   A 1 103 ? -10.359 15.526 21.680 1.00 19.94 ? 100 ILE   A C     1 
ATOM   800  O  O     . ILE   A 1 103 ? -11.511 15.887 21.410 1.00 19.58 ? 100 ILE   A O     1 
ATOM   801  C  CB    . ILE   A 1 103 ? -8.445  16.138 20.136 1.00 19.26 ? 100 ILE   A CB    1 
ATOM   802  C  CG1   . ILE   A 1 103 ? -7.362  17.186 19.800 1.00 19.09 ? 100 ILE   A CG1   1 
ATOM   803  C  CG2   . ILE   A 1 103 ? -9.438  16.050 18.974 1.00 20.17 ? 100 ILE   A CG2   1 
ATOM   804  C  CD1   . ILE   A 1 103 ? -6.291  16.700 18.834 1.00 19.60 ? 100 ILE   A CD1   1 
ATOM   805  N  N     . LYS   A 1 104 ? -10.072 14.324 22.181 1.00 19.66 ? 101 LYS   A N     1 
ATOM   806  C  CA    . LYS   A 1 104 ? -11.116 13.320 22.476 1.00 21.05 ? 101 LYS   A CA    1 
ATOM   807  C  C     . LYS   A 1 104 ? -12.131 13.783 23.501 1.00 21.79 ? 101 LYS   A C     1 
ATOM   808  O  O     . LYS   A 1 104 ? -13.340 13.558 23.336 1.00 20.80 ? 101 LYS   A O     1 
ATOM   809  C  CB    . LYS   A 1 104 ? -10.495 12.005 22.963 1.00 22.14 ? 101 LYS   A CB    1 
ATOM   810  C  CG    . LYS   A 1 104 ? -10.093 11.084 21.824 1.00 22.79 ? 101 LYS   A CG    1 
ATOM   811  C  CD    . LYS   A 1 104 ? -9.039  10.071 22.219 1.00 23.62 ? 101 LYS   A CD    1 
ATOM   812  C  CE    . LYS   A 1 104 ? -9.578  8.986  23.127 1.00 26.97 ? 101 LYS   A CE    1 
ATOM   813  N  NZ    . LYS   A 1 104 ? -8.527  8.587  24.113 1.00 28.64 ? 101 LYS   A NZ    1 
ATOM   814  N  N     . ARG   A 1 105 ? -11.618 14.406 24.565 1.00 21.91 ? 102 ARG   A N     1 
ATOM   815  C  CA    . ARG   A 1 105 ? -12.433 15.079 25.572 1.00 24.10 ? 102 ARG   A CA    1 
ATOM   816  C  C     . ARG   A 1 105 ? -13.404 16.123 24.988 1.00 23.00 ? 102 ARG   A C     1 
ATOM   817  O  O     . ARG   A 1 105 ? -14.610 16.090 25.251 1.00 22.67 ? 102 ARG   A O     1 
ATOM   818  C  CB    . ARG   A 1 105 ? -11.502 15.730 26.616 1.00 26.01 ? 102 ARG   A CB    1 
ATOM   819  C  CG    . ARG   A 1 105 ? -12.142 16.786 27.508 1.00 28.88 ? 102 ARG   A CG    1 
ATOM   820  C  CD    . ARG   A 1 105 ? -11.316 17.058 28.764 1.00 32.66 ? 102 ARG   A CD    1 
ATOM   821  N  NE    . ARG   A 1 105 ? -9.919  17.395 28.467 1.00 34.57 ? 102 ARG   A NE    1 
ATOM   822  C  CZ    . ARG   A 1 105 ? -8.846  16.653 28.785 1.00 37.57 ? 102 ARG   A CZ    1 
ATOM   823  N  NH1   . ARG   A 1 105 ? -8.959  15.492 29.437 1.00 37.80 ? 102 ARG   A NH1   1 
ATOM   824  N  NH2   . ARG   A 1 105 ? -7.628  17.080 28.441 1.00 37.05 ? 102 ARG   A NH2   1 
ATOM   825  N  N     . VAL   A 1 106 ? -12.867 17.063 24.226 1.00 21.69 ? 103 VAL   A N     1 
ATOM   826  C  CA    . VAL   A 1 106 ? -13.670 18.107 23.593 1.00 22.28 ? 103 VAL   A CA    1 
ATOM   827  C  C     . VAL   A 1 106 ? -14.732 17.503 22.637 1.00 22.02 ? 103 VAL   A C     1 
ATOM   828  O  O     . VAL   A 1 106 ? -15.894 17.922 22.675 1.00 23.21 ? 103 VAL   A O     1 
ATOM   829  C  CB    . VAL   A 1 106 ? -12.748 19.108 22.854 1.00 22.38 ? 103 VAL   A CB    1 
ATOM   830  C  CG1   . VAL   A 1 106 ? -13.536 19.988 21.882 1.00 23.14 ? 103 VAL   A CG1   1 
ATOM   831  C  CG2   . VAL   A 1 106 ? -11.984 19.969 23.849 1.00 23.03 ? 103 VAL   A CG2   1 
ATOM   832  N  N     . LYS   A 1 107 ? -14.345 16.512 21.833 1.00 20.84 ? 104 LYS   A N     1 
ATOM   833  C  CA    . LYS   A 1 107 ? -15.291 15.902 20.866 1.00 20.96 ? 104 LYS   A CA    1 
ATOM   834  C  C     . LYS   A 1 107 ? -16.231 14.900 21.551 1.00 22.70 ? 104 LYS   A C     1 
ATOM   835  O  O     . LYS   A 1 107 ? -17.144 14.435 20.864 1.00 24.03 ? 104 LYS   A O     1 
ATOM   836  C  CB    . LYS   A 1 107 ? -14.557 15.127 19.758 1.00 19.44 ? 104 LYS   A CB    1 
ATOM   837  C  CG    . LYS   A 1 107 ? -13.675 15.955 18.842 1.00 17.86 ? 104 LYS   A CG    1 
ATOM   838  C  CD    . LYS   A 1 107 ? -14.443 16.859 17.949 1.00 17.53 ? 104 LYS   A CD    1 
ATOM   839  C  CE    . LYS   A 1 107 ? -13.584 17.756 17.118 1.00 16.60 ? 104 LYS   A CE    1 
ATOM   840  N  NZ    . LYS   A 1 107 ? -14.382 18.700 16.311 1.00 16.84 ? 104 LYS   A NZ    1 
ATOM   841  N  N     . ASP   A 1 108 ? -15.921 14.477 22.779 1.00 22.66 ? 105 ASP   A N     1 
ATOM   842  C  CA    . ASP   A 1 108 ? -16.684 13.417 23.478 1.00 24.34 ? 105 ASP   A CA    1 
ATOM   843  C  C     . ASP   A 1 108 ? -16.732 12.209 22.533 1.00 25.06 ? 105 ASP   A C     1 
ATOM   844  O  O     . ASP   A 1 108 ? -17.764 11.641 22.391 1.00 26.23 ? 105 ASP   A O     1 
ATOM   845  C  CB    . ASP   A 1 108 ? -18.074 13.915 23.898 1.00 25.67 ? 105 ASP   A CB    1 
ATOM   846  C  CG    . ASP   A 1 108 ? -18.993 12.857 24.490 1.00 27.92 ? 105 ASP   A CG    1 
ATOM   847  O  OD1   . ASP   A 1 108 ? -18.511 12.068 25.293 1.00 27.83 ? 105 ASP   A OD1   1 
ATOM   848  O  OD2   . ASP   A 1 108 ? -20.184 12.809 24.086 1.00 27.58 ? 105 ASP   A OD2   1 
ATOM   849  N  N     . SER   A 1 109 ? -15.624 11.868 21.873 1.00 26.79 ? 106 SER   A N     1 
ATOM   850  C  CA    . SER   A 1 109 ? -15.712 10.803 20.843 1.00 28.88 ? 106 SER   A CA    1 
ATOM   851  C  C     . SER   A 1 109 ? -14.401 10.044 20.655 1.00 30.88 ? 106 SER   A C     1 
ATOM   852  O  O     . SER   A 1 109 ? -13.389 10.604 20.974 1.00 30.56 ? 106 SER   A O     1 
ATOM   853  C  CB    . SER   A 1 109 ? -16.092 11.429 19.516 1.00 29.35 ? 106 SER   A CB    1 
ATOM   854  O  OG    . SER   A 1 109 ? -16.196 10.440 18.508 1.00 30.97 ? 106 SER   A OG    1 
ATOM   855  N  N     . GLU   A 1 110 ? -14.478 8.799  20.173 1.00 32.44 ? 107 GLU   A N     1 
ATOM   856  C  CA    . GLU   A 1 110 ? -13.296 7.986  19.771 1.00 34.31 ? 107 GLU   A CA    1 
ATOM   857  C  C     . GLU   A 1 110 ? -13.047 8.239  18.292 1.00 32.24 ? 107 GLU   A C     1 
ATOM   858  O  O     . GLU   A 1 110 ? -11.960 8.009  17.776 1.00 33.14 ? 107 GLU   A O     1 
ATOM   859  C  CB    . GLU   A 1 110 ? -13.627 6.501  19.847 1.00 36.97 ? 107 GLU   A CB    1 
ATOM   860  C  CG    . GLU   A 1 110 ? -14.004 6.073  21.244 1.00 39.39 ? 107 GLU   A CG    1 
ATOM   861  C  CD    . GLU   A 1 110 ? -12.805 5.804  22.114 1.00 40.99 ? 107 GLU   A CD    1 
ATOM   862  O  OE1   . GLU   A 1 110 ? -12.984 5.429  23.257 1.00 44.60 ? 107 GLU   A OE1   1 
ATOM   863  O  OE2   . GLU   A 1 110 ? -11.714 5.978  21.648 1.00 41.21 ? 107 GLU   A OE2   1 
ATOM   864  N  N     . ASP   A 1 111 ? -14.115 8.598  17.617 1.00 32.92 ? 108 ASP   A N     1 
ATOM   865  C  CA    . ASP   A 1 111 ? -14.056 8.864  16.179 1.00 31.21 ? 108 ASP   A CA    1 
ATOM   866  C  C     . ASP   A 1 111 ? -13.394 10.209 16.027 1.00 27.42 ? 108 ASP   A C     1 
ATOM   867  O  O     . ASP   A 1 111 ? -14.133 11.138 15.845 1.00 28.33 ? 108 ASP   A O     1 
ATOM   868  C  CB    . ASP   A 1 111 ? -15.464 8.881  15.549 1.00 33.00 ? 108 ASP   A CB    1 
ATOM   869  C  CG    . ASP   A 1 111 ? -15.979 7.500  15.149 1.00 35.91 ? 108 ASP   A CG    1 
ATOM   870  O  OD1   . ASP   A 1 111 ? -15.323 6.490  15.505 1.00 35.01 ? 108 ASP   A OD1   1 
ATOM   871  O  OD2   . ASP   A 1 111 ? -17.067 7.447  14.545 1.00 36.05 ? 108 ASP   A OD2   1 
ATOM   872  N  N     . VAL   A 1 112 ? -12.042 10.292 16.008 1.00 23.34 ? 109 VAL   A N     1 
ATOM   873  C  CA    . VAL   A 1 112 ? -11.428 11.617 15.680 1.00 20.13 ? 109 VAL   A CA    1 
ATOM   874  C  C     . VAL   A 1 112 ? -10.392 11.523 14.534 1.00 16.77 ? 109 VAL   A C     1 
ATOM   875  O  O     . VAL   A 1 112 ? -9.395  10.867 14.690 1.00 15.57 ? 109 VAL   A O     1 
ATOM   876  C  CB    . VAL   A 1 112 ? -10.835 12.367 16.886 1.00 20.73 ? 109 VAL   A CB    1 
ATOM   877  C  CG1   . VAL   A 1 112 ? -10.540 13.803 16.519 1.00 20.98 ? 109 VAL   A CG1   1 
ATOM   878  C  CG2   . VAL   A 1 112 ? -11.733 12.319 18.120 1.00 22.44 ? 109 VAL   A CG2   1 
ATOM   879  N  N     . PRO   A 1 113 ? -10.595 12.214 13.393 1.00 14.86 ? 110 PRO   A N     1 
ATOM   880  C  CA    . PRO   A 1 113 ? -9.601  12.206 12.317 1.00 13.68 ? 110 PRO   A CA    1 
ATOM   881  C  C     . PRO   A 1 113 ? -8.289  12.837 12.808 1.00 13.84 ? 110 PRO   A C     1 
ATOM   882  O  O     . PRO   A 1 113 ? -8.293  13.950 13.209 1.00 11.44 ? 110 PRO   A O     1 
ATOM   883  C  CB    . PRO   A 1 113 ? -10.241 13.065 11.211 1.00 13.68 ? 110 PRO   A CB    1 
ATOM   884  C  CG    . PRO   A 1 113 ? -11.726 12.974 11.488 1.00 14.28 ? 110 PRO   A CG    1 
ATOM   885  C  CD    . PRO   A 1 113 ? -11.831 12.902 12.987 1.00 15.23 ? 110 PRO   A CD    1 
ATOM   886  N  N     . MET   A 1 114 ? -7.204  12.069 12.653 1.00 13.79 ? 111 MET   A N     1 
ATOM   887  C  CA    . MET   A 1 114 ? -5.852  12.485 13.113 1.00 13.68 ? 111 MET   A CA    1 
ATOM   888  C  C     . MET   A 1 114 ? -4.762  11.801 12.263 1.00 12.65 ? 111 MET   A C     1 
ATOM   889  O  O     . MET   A 1 114 ? -4.994  10.740 11.768 1.00 11.06 ? 111 MET   A O     1 
ATOM   890  C  CB    . MET   A 1 114 ? -5.610  12.077 14.567 1.00 16.33 ? 111 MET   A CB    1 
ATOM   891  C  CG    . MET   A 1 114 ? -6.437  12.801 15.654 1.00 19.28 ? 111 MET   A CG    1 
ATOM   892  S  SD    . MET   A 1 114 ? -5.817  12.553 17.379 1.00 26.49 ? 111 MET   A SD    1 
ATOM   893  C  CE    . MET   A 1 114 ? -4.225  11.850 17.041 1.00 21.36 ? 111 MET   A CE    1 
ATOM   894  N  N     . VAL   A 1 115 ? -3.677  12.522 12.024 1.00 11.00 ? 112 VAL   A N     1 
ATOM   895  C  CA    . VAL   A 1 115 ? -2.483  11.966 11.406 1.00 9.62  ? 112 VAL   A CA    1 
ATOM   896  C  C     . VAL   A 1 115 ? -1.318  12.331 12.359 1.00 9.25  ? 112 VAL   A C     1 
ATOM   897  O  O     . VAL   A 1 115 ? -1.234  13.486 12.852 1.00 8.94  ? 112 VAL   A O     1 
ATOM   898  C  CB    . VAL   A 1 115 ? -2.268  12.504 9.970  1.00 9.53  ? 112 VAL   A CB    1 
ATOM   899  C  CG1   . VAL   A 1 115 ? -0.893  12.097 9.431  1.00 9.74  ? 112 VAL   A CG1   1 
ATOM   900  C  CG2   . VAL   A 1 115 ? -3.361  12.004 9.022  1.00 9.42  ? 112 VAL   A CG2   1 
ATOM   901  N  N     . LEU   A 1 116 ? -0.497  11.336 12.690 1.00 8.88  ? 113 LEU   A N     1 
ATOM   902  C  CA    . LEU   A 1 116 ? 0.746   11.579 13.448 1.00 9.13  ? 113 LEU   A CA    1 
ATOM   903  C  C     . LEU   A 1 116 ? 1.862   11.958 12.481 1.00 9.60  ? 113 LEU   A C     1 
ATOM   904  O  O     . LEU   A 1 116 ? 2.093   11.227 11.472 1.00 8.89  ? 113 LEU   A O     1 
ATOM   905  C  CB    . LEU   A 1 116 ? 1.123   10.353 14.292 1.00 9.87  ? 113 LEU   A CB    1 
ATOM   906  C  CG    . LEU   A 1 116 ? 2.412   10.430 15.119 1.00 9.69  ? 113 LEU   A CG    1 
ATOM   907  C  CD1   . LEU   A 1 116 ? 2.226   11.501 16.192 1.00 9.69  ? 113 LEU   A CD1   1 
ATOM   908  C  CD2   . LEU   A 1 116 ? 2.804   9.102  15.736 1.00 10.03 ? 113 LEU   A CD2   1 
ATOM   909  N  N     . VAL   A 1 117 ? 2.522   13.103 12.752 1.00 8.95  ? 114 VAL   A N     1 
ATOM   910  C  CA    . VAL   A 1 117 ? 3.578   13.631 11.877 1.00 8.72  ? 114 VAL   A CA    1 
ATOM   911  C  C     . VAL   A 1 117 ? 4.883   13.733 12.674 1.00 8.75  ? 114 VAL   A C     1 
ATOM   912  O  O     . VAL   A 1 117 ? 4.956   14.475 13.644 1.00 8.87  ? 114 VAL   A O     1 
ATOM   913  C  CB    . VAL   A 1 117 ? 3.240   15.012 11.269 1.00 8.87  ? 114 VAL   A CB    1 
ATOM   914  C  CG1   . VAL   A 1 117 ? 4.410   15.587 10.465 1.00 9.27  ? 114 VAL   A CG1   1 
ATOM   915  C  CG2   . VAL   A 1 117 ? 1.989   14.939 10.398 1.00 10.04 ? 114 VAL   A CG2   1 
ATOM   916  N  N     . GLY   A 1 118 ? 5.901   13.005 12.226 1.00 8.22  ? 115 GLY   A N     1 
ATOM   917  C  CA    . GLY   A 1 118 ? 7.288   13.177 12.724 1.00 8.83  ? 115 GLY   A CA    1 
ATOM   918  C  C     . GLY   A 1 118 ? 8.026   14.115 11.772 1.00 7.97  ? 115 GLY   A C     1 
ATOM   919  O  O     . GLY   A 1 118 ? 8.453   13.697 10.711 1.00 7.45  ? 115 GLY   A O     1 
ATOM   920  N  N     . ASN   A 1 119 ? 8.160   15.387 12.154 1.00 7.76  ? 116 ASN   A N     1 
ATOM   921  C  CA    . ASN   A 1 119 ? 8.829   16.364 11.315 1.00 7.94  ? 116 ASN   A CA    1 
ATOM   922  C  C     . ASN   A 1 119 ? 10.346  16.485 11.630 1.00 7.99  ? 116 ASN   A C     1 
ATOM   923  O  O     . ASN   A 1 119 ? 10.871  15.889 12.581 1.00 8.16  ? 116 ASN   A O     1 
ATOM   924  C  CB    . ASN   A 1 119 ? 8.138   17.729 11.509 1.00 8.48  ? 116 ASN   A CB    1 
ATOM   925  C  CG    . ASN   A 1 119 ? 8.625   18.800 10.523 1.00 8.35  ? 116 ASN   A CG    1 
ATOM   926  O  OD1   . ASN   A 1 119 ? 8.700   18.556 9.328  1.00 9.41  ? 116 ASN   A OD1   1 
ATOM   927  N  ND2   . ASN   A 1 119 ? 8.942   20.014 11.038 1.00 9.40  ? 116 ASN   A ND2   1 
ATOM   928  N  N     . LYS   A 1 120 ? 11.028  17.245 10.794 1.00 8.58  ? 117 LYS   A N     1 
ATOM   929  C  CA    . LYS   A 1 120 ? 12.483  17.413 10.803 1.00 9.04  ? 117 LYS   A CA    1 
ATOM   930  C  C     . LYS   A 1 120 ? 13.253  16.148 10.412 1.00 8.81  ? 117 LYS   A C     1 
ATOM   931  O  O     . LYS   A 1 120 ? 14.352  15.899 10.926 1.00 8.92  ? 117 LYS   A O     1 
ATOM   932  C  CB    . LYS   A 1 120 ? 12.962  18.003 12.156 1.00 9.55  ? 117 LYS   A CB    1 
ATOM   933  C  CG    . LYS   A 1 120 ? 12.130  19.165 12.686 1.00 9.61  ? 117 LYS   A CG    1 
ATOM   934  C  CD    . LYS   A 1 120 ? 12.849  19.915 13.812 1.00 9.98  ? 117 LYS   A CD    1 
ATOM   935  C  CE    . LYS   A 1 120 ? 12.032  21.058 14.388 1.00 10.16 ? 117 LYS   A CE    1 
ATOM   936  N  NZ    . LYS   A 1 120 ? 12.769  21.939 15.352 1.00 11.24 ? 117 LYS   A NZ    1 
ATOM   937  N  N     . SER   A 1 121 ? 12.671  15.363 9.496  1.00 9.00  ? 118 SER   A N     1 
ATOM   938  C  CA    . SER   A 1 121 ? 13.299  14.127 8.965  1.00 9.60  ? 118 SER   A CA    1 
ATOM   939  C  C     . SER   A 1 121 ? 14.669  14.334 8.258  1.00 10.52 ? 118 SER   A C     1 
ATOM   940  O  O     . SER   A 1 121 ? 15.476  13.386 8.136  1.00 11.60 ? 118 SER   A O     1 
ATOM   941  C  CB    . SER   A 1 121 ? 12.326  13.411 7.993  1.00 9.10  ? 118 SER   A CB    1 
ATOM   942  O  OG    . SER   A 1 121 ? 12.255  14.118 6.745  1.00 9.08  ? 118 SER   A OG    1 
ATOM   943  N  N     . ASP   A 1 122 ? 14.932  15.563 7.802  1.00 10.63 ? 119 ASP   A N     1 
ATOM   944  C  CA    . ASP   A 1 122 ? 16.247  15.984 7.277  1.00 11.54 ? 119 ASP   A CA    1 
ATOM   945  C  C     . ASP   A 1 122 ? 17.396  16.035 8.291  1.00 12.18 ? 119 ASP   A C     1 
ATOM   946  O  O     . ASP   A 1 122 ? 18.563  16.128 7.884  1.00 12.94 ? 119 ASP   A O     1 
ATOM   947  C  CB    . ASP   A 1 122 ? 16.128  17.369 6.616  1.00 11.95 ? 119 ASP   A CB    1 
ATOM   948  C  CG    . ASP   A 1 122 ? 15.706  18.457 7.611  1.00 12.33 ? 119 ASP   A CG    1 
ATOM   949  O  OD1   . ASP   A 1 122 ? 14.482  18.535 7.940  1.00 12.20 ? 119 ASP   A OD1   1 
ATOM   950  O  OD2   . ASP   A 1 122 ? 16.596  19.205 8.097  1.00 13.53 ? 119 ASP   A OD2   1 
ATOM   951  N  N     . LEU   A 1 123 ? 17.090  16.026 9.589  1.00 11.62 ? 120 LEU   A N     1 
ATOM   952  C  CA    . LEU   A 1 123 ? 18.136  16.142 10.611 1.00 12.44 ? 120 LEU   A CA    1 
ATOM   953  C  C     . LEU   A 1 123 ? 18.711  14.760 10.960 1.00 12.84 ? 120 LEU   A C     1 
ATOM   954  O  O     . LEU   A 1 123 ? 17.965  13.817 11.244 1.00 12.79 ? 120 LEU   A O     1 
ATOM   955  C  CB    . LEU   A 1 123 ? 17.580  16.789 11.891 1.00 12.40 ? 120 LEU   A CB    1 
ATOM   956  C  CG    . LEU   A 1 123 ? 17.202  18.280 11.785 1.00 12.45 ? 120 LEU   A CG    1 
ATOM   957  C  CD1   . LEU   A 1 123 ? 16.725  18.779 13.134 1.00 12.42 ? 120 LEU   A CD1   1 
ATOM   958  C  CD2   . LEU   A 1 123 ? 18.314  19.173 11.292 1.00 13.31 ? 120 LEU   A CD2   1 
ATOM   959  N  N     . PRO   A 1 124 ? 20.036  14.635 10.938 1.00 13.44 ? 121 PRO   A N     1 
ATOM   960  C  CA    . PRO   A 1 124 ? 20.647  13.300 11.063 1.00 13.85 ? 121 PRO   A CA    1 
ATOM   961  C  C     . PRO   A 1 124 ? 20.638  12.698 12.481 1.00 14.02 ? 121 PRO   A C     1 
ATOM   962  O  O     . PRO   A 1 124 ? 20.687  11.481 12.591 1.00 14.66 ? 121 PRO   A O     1 
ATOM   963  C  CB    . PRO   A 1 124 ? 22.097  13.518 10.559 1.00 14.53 ? 121 PRO   A CB    1 
ATOM   964  C  CG    . PRO   A 1 124 ? 22.353  14.985 10.774 1.00 14.68 ? 121 PRO   A CG    1 
ATOM   965  C  CD    . PRO   A 1 124 ? 21.014  15.679 10.588 1.00 13.78 ? 121 PRO   A CD    1 
ATOM   966  N  N     . SER   A 1 125 ? 20.612  13.520 13.537 1.00 13.88 ? 122 SER   A N     1 
ATOM   967  C  CA    . SER   A 1 125 ? 20.643  12.994 14.929 1.00 14.62 ? 122 SER   A CA    1 
ATOM   968  C  C     . SER   A 1 125 ? 19.235  12.752 15.512 1.00 14.66 ? 122 SER   A C     1 
ATOM   969  O  O     . SER   A 1 125 ? 18.804  13.459 16.370 1.00 14.93 ? 122 SER   A O     1 
ATOM   970  C  CB    . SER   A 1 125 ? 21.505  13.821 15.832 1.00 15.01 ? 122 SER   A CB    1 
ATOM   971  O  OG    . SER   A 1 125 ? 22.861  13.730 15.449 1.00 16.13 ? 122 SER   A OG    1 
ATOM   972  N  N     . ARG   A 1 126 ? 18.598  11.712 15.026 1.00 14.57 ? 123 ARG   A N     1 
ATOM   973  C  CA    . ARG   A 1 126 ? 17.241  11.273 15.446 1.00 14.19 ? 123 ARG   A CA    1 
ATOM   974  C  C     . ARG   A 1 126 ? 17.249  10.777 16.903 1.00 14.78 ? 123 ARG   A C     1 
ATOM   975  O  O     . ARG   A 1 126 ? 18.211  10.170 17.291 1.00 14.98 ? 123 ARG   A O     1 
ATOM   976  C  CB    . ARG   A 1 126 ? 16.883  10.168 14.447 1.00 14.22 ? 123 ARG   A CB    1 
ATOM   977  C  CG    . ARG   A 1 126 ? 15.714  9.272  14.817 1.00 14.90 ? 123 ARG   A CG    1 
ATOM   978  C  CD    . ARG   A 1 126 ? 15.508  8.099  13.887 1.00 14.77 ? 123 ARG   A CD    1 
ATOM   979  N  NE    . ARG   A 1 126 ? 15.173  8.481  12.548 1.00 14.66 ? 123 ARG   A NE    1 
ATOM   980  C  CZ    . ARG   A 1 126 ? 13.967  8.826  12.150 1.00 13.96 ? 123 ARG   A CZ    1 
ATOM   981  N  NH1   . ARG   A 1 126 ? 12.974  8.857  13.019 1.00 13.25 ? 123 ARG   A NH1   1 
ATOM   982  N  NH2   . ARG   A 1 126 ? 13.762  9.135  10.902 1.00 13.64 ? 123 ARG   A NH2   1 
ATOM   983  N  N     . THR   A 1 127 ? 16.211  11.104 17.686 1.00 14.79 ? 124 THR   A N     1 
ATOM   984  C  CA    . THR   A 1 127 ? 16.049  10.596 19.071 1.00 15.36 ? 124 THR   A CA    1 
ATOM   985  C  C     . THR   A 1 127 ? 14.788  9.724  19.180 1.00 14.98 ? 124 THR   A C     1 
ATOM   986  O  O     . THR   A 1 127 ? 14.665  9.030  20.137 1.00 15.31 ? 124 THR   A O     1 
ATOM   987  C  CB    . THR   A 1 127 ? 16.047  11.684 20.159 1.00 16.04 ? 124 THR   A CB    1 
ATOM   988  O  OG1   . THR   A 1 127 ? 14.921  12.530 20.013 1.00 15.65 ? 124 THR   A OG1   1 
ATOM   989  C  CG2   . THR   A 1 127 ? 17.305  12.529 20.164 1.00 16.91 ? 124 THR   A CG2   1 
ATOM   990  N  N     . VAL   A 1 128 ? 13.853  9.871  18.252 1.00 14.48 ? 125 VAL   A N     1 
ATOM   991  C  CA    . VAL   A 1 128 ? 12.649  9.016  18.245 1.00 14.69 ? 125 VAL   A CA    1 
ATOM   992  C  C     . VAL   A 1 128 ? 12.721  7.991  17.119 1.00 15.42 ? 125 VAL   A C     1 
ATOM   993  O  O     . VAL   A 1 128 ? 12.669  8.343  15.948 1.00 14.55 ? 125 VAL   A O     1 
ATOM   994  C  CB    . VAL   A 1 128 ? 11.372  9.877  18.107 1.00 14.02 ? 125 VAL   A CB    1 
ATOM   995  C  CG1   . VAL   A 1 128 ? 10.112  9.012  18.152 1.00 13.34 ? 125 VAL   A CG1   1 
ATOM   996  C  CG2   . VAL   A 1 128 ? 11.363  10.965 19.177 1.00 13.71 ? 125 VAL   A CG2   1 
ATOM   997  N  N     . ASP   A 1 129 ? 12.810  6.722  17.508 1.00 17.81 ? 126 ASP   A N     1 
ATOM   998  C  CA    . ASP   A 1 129 ? 12.861  5.605  16.590 1.00 20.13 ? 126 ASP   A CA    1 
ATOM   999  C  C     . ASP   A 1 129 ? 11.584  5.560  15.782 1.00 19.93 ? 126 ASP   A C     1 
ATOM   1000 O  O     . ASP   A 1 129 ? 10.501  5.619  16.351 1.00 18.49 ? 126 ASP   A O     1 
ATOM   1001 C  CB    . ASP   A 1 129 ? 12.979  4.290  17.371 1.00 23.25 ? 126 ASP   A CB    1 
ATOM   1002 C  CG    . ASP   A 1 129 ? 13.543  3.148  16.537 1.00 28.31 ? 126 ASP   A CG    1 
ATOM   1003 O  OD1   . ASP   A 1 129 ? 13.426  3.167  15.282 1.00 31.90 ? 126 ASP   A OD1   1 
ATOM   1004 O  OD2   . ASP   A 1 129 ? 14.125  2.213  17.156 1.00 34.12 ? 126 ASP   A OD2   1 
ATOM   1005 N  N     . THR   A 1 130 ? 11.715  5.426  14.464 1.00 19.36 ? 127 THR   A N     1 
ATOM   1006 C  CA    . THR   A 1 130 ? 10.552  5.234  13.567 1.00 19.97 ? 127 THR   A CA    1 
ATOM   1007 C  C     . THR   A 1 130 ? 9.655   4.068  14.044 1.00 19.99 ? 127 THR   A C     1 
ATOM   1008 O  O     . THR   A 1 130 ? 8.425   4.163  13.978 1.00 18.69 ? 127 THR   A O     1 
ATOM   1009 C  CB    . THR   A 1 130 ? 10.988  4.998  12.100 1.00 21.05 ? 127 THR   A CB    1 
ATOM   1010 O  OG1   . THR   A 1 130 ? 11.719  6.130  11.615 1.00 22.49 ? 127 THR   A OG1   1 
ATOM   1011 C  CG2   . THR   A 1 130 ? 9.790   4.813  11.203 1.00 22.00 ? 127 THR   A CG2   1 
ATOM   1012 N  N     . LYS   A 1 131 ? 10.253  2.999  14.567 1.00 20.31 ? 128 LYS   A N     1 
ATOM   1013 C  CA    . LYS   A 1 131 ? 9.493   1.854  15.079 1.00 22.60 ? 128 LYS   A CA    1 
ATOM   1014 C  C     . LYS   A 1 131 ? 8.534   2.257  16.206 1.00 21.95 ? 128 LYS   A C     1 
ATOM   1015 O  O     . LYS   A 1 131 ? 7.379   1.780  16.270 1.00 21.14 ? 128 LYS   A O     1 
ATOM   1016 C  CB    . LYS   A 1 131 ? 10.429  0.724  15.533 1.00 25.58 ? 128 LYS   A CB    1 
ATOM   1017 C  CG    . LYS   A 1 131 ? 9.839   -0.271 16.542 1.00 30.00 ? 128 LYS   A CG    1 
ATOM   1018 C  CD    . LYS   A 1 131 ? 10.904  -1.223 17.098 1.00 33.82 ? 128 LYS   A CD    1 
ATOM   1019 C  CE    . LYS   A 1 131 ? 10.366  -2.612 17.454 1.00 35.24 ? 128 LYS   A CE    1 
ATOM   1020 N  NZ    . LYS   A 1 131 ? 9.122   -2.592 18.277 1.00 36.10 ? 128 LYS   A NZ    1 
ATOM   1021 N  N     . GLN   A 1 132 ? 9.017   3.120  17.090 1.00 20.15 ? 129 GLN   A N     1 
ATOM   1022 C  CA    . GLN   A 1 132 ? 8.225   3.590  18.209 1.00 20.21 ? 129 GLN   A CA    1 
ATOM   1023 C  C     . GLN   A 1 132 ? 7.063   4.449  17.743 1.00 16.88 ? 129 GLN   A C     1 
ATOM   1024 O  O     . GLN   A 1 132 ? 5.961   4.344  18.259 1.00 16.16 ? 129 GLN   A O     1 
ATOM   1025 C  CB    . GLN   A 1 132 ? 9.101   4.365  19.198 1.00 22.56 ? 129 GLN   A CB    1 
ATOM   1026 C  CG    . GLN   A 1 132 ? 10.134  3.477  19.904 1.00 26.49 ? 129 GLN   A CG    1 
ATOM   1027 C  CD    . GLN   A 1 132 ? 10.717  4.088  21.160 1.00 27.80 ? 129 GLN   A CD    1 
ATOM   1028 O  OE1   . GLN   A 1 132 ? 11.461  3.430  21.881 1.00 35.83 ? 129 GLN   A OE1   1 
ATOM   1029 N  NE2   . GLN   A 1 132 ? 10.381  5.350  21.435 1.00 31.22 ? 129 GLN   A NE2   1 
ATOM   1030 N  N     . ALA   A 1 133 ? 7.323   5.302  16.761 1.00 13.81 ? 130 ALA   A N     1 
ATOM   1031 C  CA    . ALA   A 1 133 ? 6.308   6.213  16.271 1.00 12.80 ? 130 ALA   A CA    1 
ATOM   1032 C  C     . ALA   A 1 133 ? 5.229   5.424  15.522 1.00 11.70 ? 130 ALA   A C     1 
ATOM   1033 O  O     . ALA   A 1 133 ? 4.028   5.702  15.676 1.00 10.98 ? 130 ALA   A O     1 
ATOM   1034 C  CB    . ALA   A 1 133 ? 6.943   7.278  15.399 1.00 12.16 ? 130 ALA   A CB    1 
ATOM   1035 N  N     . GLN   A 1 134 ? 5.646   4.398  14.770 1.00 11.85 ? 131 GLN   A N     1 
ATOM   1036 C  CA    . GLN   A 1 134 ? 4.679   3.496  14.095 1.00 11.95 ? 131 GLN   A CA    1 
ATOM   1037 C  C     . GLN   A 1 134 ? 3.832   2.754  15.097 1.00 12.43 ? 131 GLN   A C     1 
ATOM   1038 O  O     . GLN   A 1 134 ? 2.640   2.619  14.917 1.00 12.16 ? 131 GLN   A O     1 
ATOM   1039 C  CB    . GLN   A 1 134 ? 5.395   2.497  13.185 1.00 12.64 ? 131 GLN   A CB    1 
ATOM   1040 C  CG    . GLN   A 1 134 ? 6.092   3.136  11.994 1.00 12.61 ? 131 GLN   A CG    1 
ATOM   1041 C  CD    . GLN   A 1 134 ? 6.677   2.103  11.049 1.00 12.71 ? 131 GLN   A CD    1 
ATOM   1042 O  OE1   . GLN   A 1 134 ? 6.958   0.980  11.451 1.00 13.43 ? 131 GLN   A OE1   1 
ATOM   1043 N  NE2   . GLN   A 1 134 ? 6.835   2.471  9.785  1.00 12.62 ? 131 GLN   A NE2   1 
ATOM   1044 N  N     A ASP   A 1 135 ? 4.446   2.266  16.172 0.50 12.95 ? 132 ASP   A N     1 
ATOM   1045 N  N     B ASP   A 1 135 ? 4.474   2.266  16.157 0.50 13.41 ? 132 ASP   A N     1 
ATOM   1046 C  CA    A ASP   A 1 135 ? 3.682   1.551  17.190 0.50 13.69 ? 132 ASP   A CA    1 
ATOM   1047 C  CA    B ASP   A 1 135 ? 3.775   1.599  17.253 0.50 14.46 ? 132 ASP   A CA    1 
ATOM   1048 C  C     A ASP   A 1 135 ? 2.677   2.473  17.893 0.50 13.52 ? 132 ASP   A C     1 
ATOM   1049 C  C     B ASP   A 1 135 ? 2.692   2.485  17.855 0.50 13.93 ? 132 ASP   A C     1 
ATOM   1050 O  O     A ASP   A 1 135 ? 1.574   2.039  18.205 0.50 13.56 ? 132 ASP   A O     1 
ATOM   1051 O  O     B ASP   A 1 135 ? 1.568   2.042  18.069 0.50 13.92 ? 132 ASP   A O     1 
ATOM   1052 C  CB    A ASP   A 1 135 ? 4.602   0.878  18.210 0.50 14.30 ? 132 ASP   A CB    1 
ATOM   1053 C  CB    B ASP   A 1 135 ? 4.767   1.214  18.345 0.50 15.55 ? 132 ASP   A CB    1 
ATOM   1054 C  CG    A ASP   A 1 135 ? 3.835   0.251  19.369 0.50 15.02 ? 132 ASP   A CG    1 
ATOM   1055 C  CG    B ASP   A 1 135 ? 5.486   -0.059 18.040 0.50 16.67 ? 132 ASP   A CG    1 
ATOM   1056 O  OD1   A ASP   A 1 135 ? 3.054   -0.708 19.147 0.50 15.41 ? 132 ASP   A OD1   1 
ATOM   1057 O  OD1   B ASP   A 1 135 ? 4.875   -0.900 17.364 0.50 17.66 ? 132 ASP   A OD1   1 
ATOM   1058 O  OD2   A ASP   A 1 135 ? 3.989   0.727  20.510 0.50 15.36 ? 132 ASP   A OD2   1 
ATOM   1059 O  OD2   B ASP   A 1 135 ? 6.641   -0.228 18.471 0.50 17.32 ? 132 ASP   A OD2   1 
ATOM   1060 N  N     . LEU   A 1 136 ? 3.034   3.733  18.136 1.00 13.46 ? 133 LEU   A N     1 
ATOM   1061 C  CA    . LEU   A 1 136 ? 2.073   4.650  18.760 1.00 13.86 ? 133 LEU   A CA    1 
ATOM   1062 C  C     . LEU   A 1 136 ? 0.872   4.894  17.809 1.00 13.59 ? 133 LEU   A C     1 
ATOM   1063 O  O     . LEU   A 1 136 ? -0.297  4.774  18.224 1.00 13.75 ? 133 LEU   A O     1 
ATOM   1064 C  CB    . LEU   A 1 136 ? 2.727   5.965  19.163 1.00 13.68 ? 133 LEU   A CB    1 
ATOM   1065 C  CG    . LEU   A 1 136 ? 1.820   6.876  19.992 1.00 14.32 ? 133 LEU   A CG    1 
ATOM   1066 C  CD1   . LEU   A 1 136 ? 1.537   6.328  21.382 1.00 15.42 ? 133 LEU   A CD1   1 
ATOM   1067 C  CD2   . LEU   A 1 136 ? 2.443   8.268  20.075 1.00 13.70 ? 133 LEU   A CD2   1 
ATOM   1068 N  N     . ALA   A 1 137 ? 1.175   5.228  16.554 1.00 13.27 ? 134 ALA   A N     1 
ATOM   1069 C  CA    . ALA   A 1 137 ? 0.145   5.401  15.513 1.00 13.43 ? 134 ALA   A CA    1 
ATOM   1070 C  C     . ALA   A 1 137 ? -0.764  4.166  15.369 1.00 14.35 ? 134 ALA   A C     1 
ATOM   1071 O  O     . ALA   A 1 137 ? -2.001  4.303  15.285 1.00 14.01 ? 134 ALA   A O     1 
ATOM   1072 C  CB    . ALA   A 1 137 ? 0.766   5.787  14.174 1.00 12.33 ? 134 ALA   A CB    1 
ATOM   1073 N  N     . ARG   A 1 138 ? -0.152  2.975  15.386 1.00 15.51 ? 135 ARG   A N     1 
ATOM   1074 C  CA    . ARG   A 1 138 ? -0.908  1.720  15.401 1.00 17.36 ? 135 ARG   A CA    1 
ATOM   1075 C  C     . ARG   A 1 138 ? -1.854  1.649  16.617 1.00 17.49 ? 135 ARG   A C     1 
ATOM   1076 O  O     . ARG   A 1 138 ? -3.036  1.298  16.457 1.00 18.43 ? 135 ARG   A O     1 
ATOM   1077 C  CB    . ARG   A 1 138 ? 0.021   0.501  15.382 1.00 19.75 ? 135 ARG   A CB    1 
ATOM   1078 C  CG    . ARG   A 1 138 ? -0.704  -0.817 15.068 1.00 22.44 ? 135 ARG   A CG    1 
ATOM   1079 C  CD    . ARG   A 1 138 ? 0.230   -1.988 14.748 1.00 24.89 ? 135 ARG   A CD    1 
ATOM   1080 N  NE    . ARG   A 1 138 ? 1.282   -1.606 13.807 1.00 27.27 ? 135 ARG   A NE    1 
ATOM   1081 C  CZ    . ARG   A 1 138 ? 2.563   -1.389 14.127 1.00 29.03 ? 135 ARG   A CZ    1 
ATOM   1082 N  NH1   . ARG   A 1 138 ? 3.012   -1.545 15.383 1.00 31.06 ? 135 ARG   A NH1   1 
ATOM   1083 N  NH2   . ARG   A 1 138 ? 3.407   -1.022 13.180 1.00 29.28 ? 135 ARG   A NH2   1 
ATOM   1084 N  N     . SER   A 1 139 ? -1.363  1.997  17.810 1.00 16.66 ? 136 SER   A N     1 
ATOM   1085 C  CA    . SER   A 1 139 ? -2.213  1.927  19.034 1.00 17.57 ? 136 SER   A CA    1 
ATOM   1086 C  C     . SER   A 1 139 ? -3.411  2.899  18.991 1.00 16.95 ? 136 SER   A C     1 
ATOM   1087 O  O     . SER   A 1 139 ? -4.460  2.615  19.591 1.00 16.37 ? 136 SER   A O     1 
ATOM   1088 C  CB    . SER   A 1 139 ? -1.389  2.137  20.313 1.00 18.60 ? 136 SER   A CB    1 
ATOM   1089 O  OG    . SER   A 1 139 ? -1.216  3.514  20.576 1.00 18.70 ? 136 SER   A OG    1 
ATOM   1090 N  N     . TYR   A 1 140 ? -3.266  4.003  18.251 1.00 15.99 ? 137 TYR   A N     1 
ATOM   1091 C  CA    . TYR   A 1 140 ? -4.360  4.971  18.022 1.00 16.64 ? 137 TYR   A CA    1 
ATOM   1092 C  C     . TYR   A 1 140 ? -5.239  4.653  16.808 1.00 15.68 ? 137 TYR   A C     1 
ATOM   1093 O  O     . TYR   A 1 140 ? -6.343  5.202  16.676 1.00 15.84 ? 137 TYR   A O     1 
ATOM   1094 C  CB    . TYR   A 1 140 ? -3.809  6.390  17.851 1.00 16.77 ? 137 TYR   A CB    1 
ATOM   1095 C  CG    . TYR   A 1 140 ? -3.067  6.965  19.039 1.00 18.40 ? 137 TYR   A CG    1 
ATOM   1096 C  CD1   . TYR   A 1 140 ? -3.249  6.471  20.333 1.00 19.48 ? 137 TYR   A CD1   1 
ATOM   1097 C  CD2   . TYR   A 1 140 ? -2.173  8.016  18.864 1.00 18.49 ? 137 TYR   A CD2   1 
ATOM   1098 C  CE1   . TYR   A 1 140 ? -2.559  7.013  21.425 1.00 21.34 ? 137 TYR   A CE1   1 
ATOM   1099 C  CE2   . TYR   A 1 140 ? -1.475  8.567  19.942 1.00 19.85 ? 137 TYR   A CE2   1 
ATOM   1100 C  CZ    . TYR   A 1 140 ? -1.652  8.051  21.214 1.00 20.97 ? 137 TYR   A CZ    1 
ATOM   1101 O  OH    . TYR   A 1 140 ? -0.968  8.602  22.290 1.00 22.21 ? 137 TYR   A OH    1 
ATOM   1102 N  N     . GLY   A 1 141 ? -4.770  3.770  15.933 1.00 14.42 ? 138 GLY   A N     1 
ATOM   1103 C  CA    . GLY   A 1 141 ? -5.458  3.489  14.677 1.00 13.54 ? 138 GLY   A CA    1 
ATOM   1104 C  C     . GLY   A 1 141 ? -5.460  4.675  13.728 1.00 12.54 ? 138 GLY   A C     1 
ATOM   1105 O  O     . GLY   A 1 141 ? -6.505  4.994  13.131 1.00 12.10 ? 138 GLY   A O     1 
ATOM   1106 N  N     . ILE   A 1 142 ? -4.295  5.334  13.610 1.00 11.07 ? 139 ILE   A N     1 
ATOM   1107 C  CA    . ILE   A 1 142 ? -4.133  6.498  12.736 1.00 10.40 ? 139 ILE   A CA    1 
ATOM   1108 C  C     . ILE   A 1 142 ? -2.895  6.356  11.846 1.00 9.98  ? 139 ILE   A C     1 
ATOM   1109 O  O     . ILE   A 1 142 ? -1.963  5.620  12.187 1.00 10.82 ? 139 ILE   A O     1 
ATOM   1110 C  CB    . ILE   A 1 142 ? -4.067  7.840  13.521 1.00 9.94  ? 139 ILE   A CB    1 
ATOM   1111 C  CG1   . ILE   A 1 142 ? -2.747  7.977  14.301 1.00 10.43 ? 139 ILE   A CG1   1 
ATOM   1112 C  CG2   . ILE   A 1 142 ? -5.314  7.999  14.395 1.00 10.81 ? 139 ILE   A CG2   1 
ATOM   1113 C  CD1   . ILE   A 1 142 ? -2.621  9.207  15.182 1.00 10.02 ? 139 ILE   A CD1   1 
ATOM   1114 N  N     . PRO   A 1 143 ? -2.849  7.109  10.737 1.00 9.32  ? 140 PRO   A N     1 
ATOM   1115 C  CA    . PRO   A 1 143 ? -1.643  7.074  9.898  1.00 9.02  ? 140 PRO   A CA    1 
ATOM   1116 C  C     . PRO   A 1 143 ? -0.443  7.721  10.574 1.00 8.79  ? 140 PRO   A C     1 
ATOM   1117 O  O     . PRO   A 1 143 ? -0.615  8.569  11.489 1.00 8.80  ? 140 PRO   A O     1 
ATOM   1118 C  CB    . PRO   A 1 143 ? -2.066  7.841  8.630  1.00 8.45  ? 140 PRO   A CB    1 
ATOM   1119 C  CG    . PRO   A 1 143 ? -3.534  7.661  8.593  1.00 9.15  ? 140 PRO   A CG    1 
ATOM   1120 C  CD    . PRO   A 1 143 ? -3.985  7.720  10.019 1.00 9.23  ? 140 PRO   A CD    1 
ATOM   1121 N  N     . PHE   A 1 144 ? 0.755   7.364  10.089 1.00 8.89  ? 141 PHE   A N     1 
ATOM   1122 C  CA    . PHE   A 1 144 ? 2.023   7.973  10.566 1.00 8.99  ? 141 PHE   A CA    1 
ATOM   1123 C  C     . PHE   A 1 144 ? 2.902   8.319  9.356  1.00 8.92  ? 141 PHE   A C     1 
ATOM   1124 O  O     . PHE   A 1 144 ? 3.114   7.482  8.504  1.00 9.22  ? 141 PHE   A O     1 
ATOM   1125 C  CB    . PHE   A 1 144 ? 2.822   7.049  11.485 1.00 9.84  ? 141 PHE   A CB    1 
ATOM   1126 C  CG    . PHE   A 1 144 ? 4.199   7.577  11.785 1.00 9.79  ? 141 PHE   A CG    1 
ATOM   1127 C  CD1   . PHE   A 1 144 ? 4.350   8.795  12.402 1.00 9.84  ? 141 PHE   A CD1   1 
ATOM   1128 C  CD2   . PHE   A 1 144 ? 5.334   6.904  11.387 1.00 10.78 ? 141 PHE   A CD2   1 
ATOM   1129 C  CE1   . PHE   A 1 144 ? 5.599   9.293  12.690 1.00 10.84 ? 141 PHE   A CE1   1 
ATOM   1130 C  CE2   . PHE   A 1 144 ? 6.585   7.411  11.680 1.00 11.28 ? 141 PHE   A CE2   1 
ATOM   1131 C  CZ    . PHE   A 1 144 ? 6.716   8.613  12.302 1.00 11.11 ? 141 PHE   A CZ    1 
ATOM   1132 N  N     . ILE   A 1 145 ? 3.283   9.591  9.293  1.00 8.43  ? 142 ILE   A N     1 
ATOM   1133 C  CA    . ILE   A 1 145 ? 4.147   10.157 8.213  1.00 8.18  ? 142 ILE   A CA    1 
ATOM   1134 C  C     . ILE   A 1 145 ? 5.313   10.995 8.786  1.00 7.48  ? 142 ILE   A C     1 
ATOM   1135 O  O     . ILE   A 1 145 ? 5.079   11.821 9.600  1.00 7.45  ? 142 ILE   A O     1 
ATOM   1136 C  CB    . ILE   A 1 145 ? 3.265   11.033 7.301  1.00 8.48  ? 142 ILE   A CB    1 
ATOM   1137 C  CG1   . ILE   A 1 145 ? 2.164   10.193 6.638  1.00 8.69  ? 142 ILE   A CG1   1 
ATOM   1138 C  CG2   . ILE   A 1 145 ? 4.086   11.843 6.302  1.00 7.90  ? 142 ILE   A CG2   1 
ATOM   1139 C  CD1   . ILE   A 1 145 ? 1.127   10.965 5.897  1.00 9.90  ? 142 ILE   A CD1   1 
ATOM   1140 N  N     . GLU   A 1 146 ? 6.521   10.762 8.289  1.00 7.93  ? 143 GLU   A N     1 
ATOM   1141 C  CA    . GLU   A 1 146 ? 7.661   11.641 8.623  1.00 8.24  ? 143 GLU   A CA    1 
ATOM   1142 C  C     . GLU   A 1 146 ? 7.800   12.696 7.506  1.00 8.24  ? 143 GLU   A C     1 
ATOM   1143 O  O     . GLU   A 1 146 ? 7.781   12.355 6.374  1.00 8.05  ? 143 GLU   A O     1 
ATOM   1144 C  CB    . GLU   A 1 146 ? 8.967   10.884 8.832  1.00 9.14  ? 143 GLU   A CB    1 
ATOM   1145 C  CG    . GLU   A 1 146 ? 8.972   10.071 10.102 1.00 9.75  ? 143 GLU   A CG    1 
ATOM   1146 C  CD    . GLU   A 1 146 ? 10.335  9.543  10.548 1.00 11.27 ? 143 GLU   A CD    1 
ATOM   1147 O  OE1   . GLU   A 1 146 ? 11.297  9.817  9.899  1.00 12.57 ? 143 GLU   A OE1   1 
ATOM   1148 O  OE2   . GLU   A 1 146 ? 10.389  8.848  11.509 1.00 11.63 ? 143 GLU   A OE2   1 
ATOM   1149 N  N     . THR   A 1 147 ? 7.966   13.944 7.899  1.00 7.87  ? 144 THR   A N     1 
ATOM   1150 C  CA    . THR   A 1 147 ? 8.056   15.041 6.926  1.00 8.67  ? 144 THR   A CA    1 
ATOM   1151 C  C     . THR   A 1 147 ? 9.300   15.901 7.174  1.00 9.31  ? 144 THR   A C     1 
ATOM   1152 O  O     . THR   A 1 147 ? 9.876   15.797 8.226  1.00 9.33  ? 144 THR   A O     1 
ATOM   1153 C  CB    . THR   A 1 147 ? 6.886   16.015 7.135  1.00 8.77  ? 144 THR   A CB    1 
ATOM   1154 O  OG1   . THR   A 1 147 ? 6.914   16.513 8.462  1.00 9.36  ? 144 THR   A OG1   1 
ATOM   1155 C  CG2   . THR   A 1 147 ? 5.543   15.406 6.818  1.00 8.96  ? 144 THR   A CG2   1 
ATOM   1156 N  N     . SER   A 1 148 ? 9.697   16.628 6.130  1.00 10.04 ? 145 SER   A N     1 
ATOM   1157 C  CA    . SER   A 1 148 ? 10.685  17.716 6.279  1.00 10.81 ? 145 SER   A CA    1 
ATOM   1158 C  C     . SER   A 1 148 ? 10.078  19.045 5.762  1.00 11.12 ? 145 SER   A C     1 
ATOM   1159 O  O     . SER   A 1 148 ? 9.923   19.185 4.615  1.00 11.40 ? 145 SER   A O     1 
ATOM   1160 C  CB    . SER   A 1 148 ? 11.965  17.445 5.569  1.00 11.12 ? 145 SER   A CB    1 
ATOM   1161 O  OG    . SER   A 1 148 ? 12.841  18.526 5.731  1.00 12.00 ? 145 SER   A OG    1 
ATOM   1162 N  N     . ALA   A 1 149 ? 9.817   19.997 6.646  1.00 11.81 ? 146 ALA   A N     1 
ATOM   1163 C  CA    . ALA   A 1 149 ? 9.353   21.320 6.153  1.00 12.17 ? 146 ALA   A CA    1 
ATOM   1164 C  C     . ALA   A 1 149 ? 10.519  22.024 5.437  1.00 13.85 ? 146 ALA   A C     1 
ATOM   1165 O  O     . ALA   A 1 149 ? 10.287  22.876 4.610  1.00 15.16 ? 146 ALA   A O     1 
ATOM   1166 C  CB    . ALA   A 1 149 ? 8.804   22.149 7.289  1.00 12.03 ? 146 ALA   A CB    1 
ATOM   1167 N  N     . LYS   A 1 150 ? 11.747  21.624 5.748  1.00 14.57 ? 147 LYS   A N     1 
ATOM   1168 C  CA    . LYS   A 1 150 ? 12.933  22.259 5.153  1.00 16.16 ? 147 LYS   A CA    1 
ATOM   1169 C  C     . LYS   A 1 150 ? 13.101  21.872 3.702  1.00 17.09 ? 147 LYS   A C     1 
ATOM   1170 O  O     . LYS   A 1 150 ? 13.272  22.744 2.842  1.00 17.37 ? 147 LYS   A O     1 
ATOM   1171 C  CB    . LYS   A 1 150 ? 14.217  21.953 5.961  1.00 17.50 ? 147 LYS   A CB    1 
ATOM   1172 C  CG    . LYS   A 1 150 ? 15.464  22.678 5.423  1.00 19.26 ? 147 LYS   A CG    1 
ATOM   1173 C  CD    . LYS   A 1 150 ? 16.674  22.684 6.351  1.00 20.87 ? 147 LYS   A CD    1 
ATOM   1174 C  CE    . LYS   A 1 150 ? 17.859  23.395 5.696  1.00 23.32 ? 147 LYS   A CE    1 
ATOM   1175 N  NZ    . LYS   A 1 150 ? 19.144  23.026 6.323  1.00 25.01 ? 147 LYS   A NZ    1 
ATOM   1176 N  N     . THR   A 1 151 ? 13.055  20.568 3.430  1.00 16.35 ? 148 THR   A N     1 
ATOM   1177 C  CA    . THR   A 1 151 ? 13.180  20.050 2.064  1.00 17.10 ? 148 THR   A CA    1 
ATOM   1178 C  C     . THR   A 1 151 ? 11.838  19.825 1.334  1.00 16.00 ? 148 THR   A C     1 
ATOM   1179 O  O     . THR   A 1 151 ? 11.851  19.447 0.169  1.00 16.14 ? 148 THR   A O     1 
ATOM   1180 C  CB    . THR   A 1 151 ? 13.928  18.710 2.060  1.00 17.72 ? 148 THR   A CB    1 
ATOM   1181 O  OG1   . THR   A 1 151 ? 13.090  17.696 2.658  1.00 16.74 ? 148 THR   A OG1   1 
ATOM   1182 C  CG2   . THR   A 1 151 ? 15.265  18.842 2.787  1.00 18.71 ? 148 THR   A CG2   1 
ATOM   1183 N  N     . ARG   A 1 152 ? 10.722  19.999 2.032  1.00 15.36 ? 149 ARG   A N     1 
ATOM   1184 C  CA    . ARG   A 1 152 ? 9.326   19.835 1.532  1.00 16.24 ? 149 ARG   A CA    1 
ATOM   1185 C  C     . ARG   A 1 152 ? 8.941   18.353 1.367  1.00 16.51 ? 149 ARG   A C     1 
ATOM   1186 O  O     . ARG   A 1 152 ? 7.897   18.069 0.757  1.00 19.33 ? 149 ARG   A O     1 
ATOM   1187 C  CB    . ARG   A 1 152 ? 8.999   20.716 0.314  1.00 18.85 ? 149 ARG   A CB    1 
ATOM   1188 C  CG    . ARG   A 1 152 ? 7.559   21.164 0.161  1.00 21.30 ? 149 ARG   A CG    1 
ATOM   1189 C  CD    . ARG   A 1 152 ? 7.452   22.238 -0.920 1.00 22.93 ? 149 ARG   A CD    1 
ATOM   1190 N  NE    . ARG   A 1 152 ? 6.226   22.997 -0.761 1.00 22.35 ? 149 ARG   A NE    1 
ATOM   1191 C  CZ    . ARG   A 1 152 ? 5.099   22.587 -1.265 1.00 24.49 ? 149 ARG   A CZ    1 
ATOM   1192 N  NH1   . ARG   A 1 152 ? 3.990   23.276 -1.136 1.00 26.93 ? 149 ARG   A NH1   1 
ATOM   1193 N  NH2   . ARG   A 1 152 ? 5.085   21.474 -1.934 1.00 24.65 ? 149 ARG   A NH2   1 
ATOM   1194 N  N     . GLN   A 1 153 ? 9.663   17.466 2.041  1.00 13.70 ? 150 GLN   A N     1 
ATOM   1195 C  CA    . GLN   A 1 153 ? 9.408   16.014 1.950  1.00 13.91 ? 150 GLN   A CA    1 
ATOM   1196 C  C     . GLN   A 1 153 ? 8.105   15.642 2.664  1.00 10.68 ? 150 GLN   A C     1 
ATOM   1197 O  O     . GLN   A 1 153 ? 7.972   15.898 3.800  1.00 9.51  ? 150 GLN   A O     1 
ATOM   1198 C  CB    . GLN   A 1 153 ? 10.525  15.190 2.576  1.00 14.34 ? 150 GLN   A CB    1 
ATOM   1199 C  CG    . GLN   A 1 153 ? 10.590  13.764 2.002  1.00 16.89 ? 150 GLN   A CG    1 
ATOM   1200 C  CD    . GLN   A 1 153 ? 11.283  13.660 0.664  1.00 18.05 ? 150 GLN   A CD    1 
ATOM   1201 O  OE1   . GLN   A 1 153 ? 10.764  13.117 -0.299 1.00 21.18 ? 150 GLN   A OE1   1 
ATOM   1202 N  NE2   . GLN   A 1 153 ? 12.460  14.226 0.603  1.00 19.61 ? 150 GLN   A NE2   1 
ATOM   1203 N  N     . ARG   A 1 154 ? 7.170   15.128 1.882  1.00 10.02 ? 151 ARG   A N     1 
ATOM   1204 C  CA    . ARG   A 1 154 ? 5.862   14.599 2.352  1.00 9.92  ? 151 ARG   A CA    1 
ATOM   1205 C  C     . ARG   A 1 154 ? 4.967   15.678 2.987  1.00 9.85  ? 151 ARG   A C     1 
ATOM   1206 O  O     . ARG   A 1 154 ? 4.054   15.334 3.641  1.00 9.46  ? 151 ARG   A O     1 
ATOM   1207 C  CB    . ARG   A 1 154 ? 6.081   13.355 3.227  1.00 9.64  ? 151 ARG   A CB    1 
ATOM   1208 C  CG    . ARG   A 1 154 ? 6.682   12.161 2.492  1.00 9.91  ? 151 ARG   A CG    1 
ATOM   1209 C  CD    . ARG   A 1 154 ? 6.414   10.861 3.234  1.00 10.44 ? 151 ARG   A CD    1 
ATOM   1210 N  NE    . ARG   A 1 154 ? 5.103   10.328 2.967  1.00 11.24 ? 151 ARG   A NE    1 
ATOM   1211 C  CZ    . ARG   A 1 154 ? 4.553   9.265  3.544  1.00 12.14 ? 151 ARG   A CZ    1 
ATOM   1212 N  NH1   . ARG   A 1 154 ? 3.330   8.934  3.214  1.00 13.43 ? 151 ARG   A NH1   1 
ATOM   1213 N  NH2   . ARG   A 1 154 ? 5.189   8.572  4.454  1.00 12.28 ? 151 ARG   A NH2   1 
ATOM   1214 N  N     . VAL   A 1 155 ? 5.176   16.945 2.674  1.00 10.64 ? 152 VAL   A N     1 
ATOM   1215 C  CA    . VAL   A 1 155 ? 4.324   17.998 3.299  1.00 11.28 ? 152 VAL   A CA    1 
ATOM   1216 C  C     . VAL   A 1 155 ? 2.908   17.940 2.695  1.00 11.31 ? 152 VAL   A C     1 
ATOM   1217 O  O     . VAL   A 1 155 ? 2.000   17.944 3.416  1.00 10.40 ? 152 VAL   A O     1 
ATOM   1218 C  CB    . VAL   A 1 155 ? 4.959   19.382 3.131  1.00 12.01 ? 152 VAL   A CB    1 
ATOM   1219 C  CG1   . VAL   A 1 155 ? 3.985   20.470 3.544  1.00 11.89 ? 152 VAL   A CG1   1 
ATOM   1220 C  CG2   . VAL   A 1 155 ? 6.254   19.462 3.922  1.00 11.76 ? 152 VAL   A CG2   1 
ATOM   1221 N  N     . GLU   A 1 156 ? 2.805   17.895 1.381  1.00 12.41 ? 153 GLU   A N     1 
ATOM   1222 C  CA    . GLU   A 1 156 ? 1.488   17.750 0.750  1.00 13.66 ? 153 GLU   A CA    1 
ATOM   1223 C  C     . GLU   A 1 156 ? 0.825   16.437 1.195  1.00 12.44 ? 153 GLU   A C     1 
ATOM   1224 O  O     . GLU   A 1 156 ? -0.327  16.404 1.688  1.00 10.49 ? 153 GLU   A O     1 
ATOM   1225 C  CB    . GLU   A 1 156 ? 1.608   17.857 -0.763 1.00 17.04 ? 153 GLU   A CB    1 
ATOM   1226 C  CG    . GLU   A 1 156 ? 2.155   19.222 -1.184 1.00 19.48 ? 153 GLU   A CG    1 
ATOM   1227 C  CD    . GLU   A 1 156 ? 1.987   19.554 -2.648 1.00 24.17 ? 153 GLU   A CD    1 
ATOM   1228 O  OE1   . GLU   A 1 156 ? 2.073   18.663 -3.496 1.00 30.20 ? 153 GLU   A OE1   1 
ATOM   1229 O  OE2   . GLU   A 1 156 ? 1.783   20.743 -2.965 1.00 28.52 ? 153 GLU   A OE2   1 
ATOM   1230 N  N     . ASP   A 1 157 ? 1.593   15.363 1.090  1.00 12.03 ? 154 ASP   A N     1 
ATOM   1231 C  CA    . ASP   A 1 157 ? 1.212   14.063 1.651  1.00 12.74 ? 154 ASP   A CA    1 
ATOM   1232 C  C     . ASP   A 1 157 ? 0.520   14.074 3.029  1.00 11.28 ? 154 ASP   A C     1 
ATOM   1233 O  O     . ASP   A 1 157 ? -0.541  13.453 3.203  1.00 10.86 ? 154 ASP   A O     1 
ATOM   1234 C  CB    . ASP   A 1 157 ? 2.472   13.201 1.762  1.00 15.42 ? 154 ASP   A CB    1 
ATOM   1235 C  CG    . ASP   A 1 157 ? 2.211   11.769 1.506  1.00 18.83 ? 154 ASP   A CG    1 
ATOM   1236 O  OD1   . ASP   A 1 157 ? 1.129   11.269 1.938  1.00 21.09 ? 154 ASP   A OD1   1 
ATOM   1237 O  OD2   . ASP   A 1 157 ? 3.115   11.139 0.908  1.00 19.73 ? 154 ASP   A OD2   1 
ATOM   1238 N  N     . ALA   A 1 158 ? 1.143   14.728 4.024  1.00 10.07 ? 155 ALA   A N     1 
ATOM   1239 C  CA    . ALA   A 1 158 ? 0.619   14.759 5.391  1.00 9.94  ? 155 ALA   A CA    1 
ATOM   1240 C  C     . ALA   A 1 158 ? -0.776  15.412 5.473  1.00 9.22  ? 155 ALA   A C     1 
ATOM   1241 O  O     . ALA   A 1 158 ? -1.709  14.863 6.081  1.00 8.70  ? 155 ALA   A O     1 
ATOM   1242 C  CB    . ALA   A 1 158 ? 1.611   15.462 6.338  1.00 10.14 ? 155 ALA   A CB    1 
ATOM   1243 N  N     . PHE   A 1 159 ? -0.921  16.572 4.828  1.00 9.29  ? 156 PHE   A N     1 
ATOM   1244 C  CA    . PHE   A 1 159 ? -2.212  17.292 4.841  1.00 8.96  ? 156 PHE   A CA    1 
ATOM   1245 C  C     . PHE   A 1 159 ? -3.266  16.537 4.038  1.00 8.71  ? 156 PHE   A C     1 
ATOM   1246 O  O     . PHE   A 1 159 ? -4.440  16.464 4.425  1.00 8.79  ? 156 PHE   A O     1 
ATOM   1247 C  CB    . PHE   A 1 159 ? -2.059  18.708 4.272  1.00 9.53  ? 156 PHE   A CB    1 
ATOM   1248 C  CG    . PHE   A 1 159 ? -1.381  19.671 5.213  1.00 9.81  ? 156 PHE   A CG    1 
ATOM   1249 C  CD1   . PHE   A 1 159 ? -2.099  20.334 6.190  1.00 9.92  ? 156 PHE   A CD1   1 
ATOM   1250 C  CD2   . PHE   A 1 159 ? -0.015  19.895 5.124  1.00 9.53  ? 156 PHE   A CD2   1 
ATOM   1251 C  CE1   . PHE   A 1 159 ? -1.473  21.246 7.036  1.00 10.10 ? 156 PHE   A CE1   1 
ATOM   1252 C  CE2   . PHE   A 1 159 ? 0.631   20.771 5.992  1.00 9.76  ? 156 PHE   A CE2   1 
ATOM   1253 C  CZ    . PHE   A 1 159 ? -0.102  21.456 6.938  1.00 10.42 ? 156 PHE   A CZ    1 
ATOM   1254 N  N     . TYR   A 1 160 ? -2.882  15.988 2.900  1.00 8.57  ? 157 TYR   A N     1 
ATOM   1255 C  CA    . TYR   A 1 160 ? -3.857  15.324 2.039  1.00 9.58  ? 157 TYR   A CA    1 
ATOM   1256 C  C     . TYR   A 1 160 ? -4.300  13.988 2.668  1.00 8.49  ? 157 TYR   A C     1 
ATOM   1257 O  O     . TYR   A 1 160 ? -5.412  13.539 2.461  1.00 9.04  ? 157 TYR   A O     1 
ATOM   1258 C  CB    . TYR   A 1 160 ? -3.250  15.044 0.663  1.00 10.45 ? 157 TYR   A CB    1 
ATOM   1259 C  CG    . TYR   A 1 160 ? -2.942  16.245 -0.233 1.00 11.57 ? 157 TYR   A CG    1 
ATOM   1260 C  CD1   . TYR   A 1 160 ? -3.023  17.571 0.223  1.00 12.60 ? 157 TYR   A CD1   1 
ATOM   1261 C  CD2   . TYR   A 1 160 ? -2.560  16.020 -1.534 1.00 13.49 ? 157 TYR   A CD2   1 
ATOM   1262 C  CE1   . TYR   A 1 160 ? -2.713  18.640 -0.619 1.00 14.24 ? 157 TYR   A CE1   1 
ATOM   1263 C  CE2   . TYR   A 1 160 ? -2.280  17.079 -2.383 1.00 15.48 ? 157 TYR   A CE2   1 
ATOM   1264 C  CZ    . TYR   A 1 160 ? -2.337  18.372 -1.915 1.00 14.56 ? 157 TYR   A CZ    1 
ATOM   1265 O  OH    . TYR   A 1 160 ? -2.056  19.410 -2.798 1.00 17.86 ? 157 TYR   A OH    1 
ATOM   1266 N  N     . THR   A 1 161 ? -3.401  13.331 3.392  1.00 7.78  ? 158 THR   A N     1 
ATOM   1267 C  CA    . THR   A 1 161 ? -3.732  12.129 4.144  1.00 7.62  ? 158 THR   A CA    1 
ATOM   1268 C  C     . THR   A 1 161 ? -4.799  12.441 5.213  1.00 8.24  ? 158 THR   A C     1 
ATOM   1269 O  O     . THR   A 1 161 ? -5.737  11.653 5.432  1.00 7.89  ? 158 THR   A O     1 
ATOM   1270 C  CB    . THR   A 1 161 ? -2.453  11.457 4.718  1.00 7.49  ? 158 THR   A CB    1 
ATOM   1271 O  OG1   . THR   A 1 161 ? -1.602  11.027 3.644  1.00 8.12  ? 158 THR   A OG1   1 
ATOM   1272 C  CG2   . THR   A 1 161 ? -2.790  10.228 5.554  1.00 7.79  ? 158 THR   A CG2   1 
ATOM   1273 N  N     . LEU   A 1 162 ? -4.666  13.582 5.867  1.00 7.35  ? 159 LEU   A N     1 
ATOM   1274 C  CA    . LEU   A 1 162 ? -5.658  13.988 6.845  1.00 8.04  ? 159 LEU   A CA    1 
ATOM   1275 C  C     . LEU   A 1 162 ? -7.026  14.272 6.226  1.00 8.37  ? 159 LEU   A C     1 
ATOM   1276 O  O     . LEU   A 1 162 ? -8.035  13.873 6.808  1.00 9.72  ? 159 LEU   A O     1 
ATOM   1277 C  CB    . LEU   A 1 162 ? -5.149  15.177 7.679  1.00 8.06  ? 159 LEU   A CB    1 
ATOM   1278 C  CG    . LEU   A 1 162 ? -6.093  15.710 8.764  1.00 8.32  ? 159 LEU   A CG    1 
ATOM   1279 C  CD1   . LEU   A 1 162 ? -6.348  14.643 9.837  1.00 8.80  ? 159 LEU   A CD1   1 
ATOM   1280 C  CD2   . LEU   A 1 162 ? -5.438  16.955 9.345  1.00 8.95  ? 159 LEU   A CD2   1 
ATOM   1281 N  N     . VAL   A 1 163 ? -7.070  14.946 5.075  1.00 8.79  ? 160 VAL   A N     1 
ATOM   1282 C  CA    . VAL   A 1 163 ? -8.302  15.065 4.276  1.00 9.78  ? 160 VAL   A CA    1 
ATOM   1283 C  C     . VAL   A 1 163 ? -8.979  13.718 4.009  1.00 10.16 ? 160 VAL   A C     1 
ATOM   1284 O  O     . VAL   A 1 163 ? -10.218 13.561 4.220  1.00 10.57 ? 160 VAL   A O     1 
ATOM   1285 C  CB    . VAL   A 1 163 ? -8.065  15.785 2.908  1.00 9.66  ? 160 VAL   A CB    1 
ATOM   1286 C  CG1   . VAL   A 1 163 ? -9.343  15.776 2.055  1.00 10.30 ? 160 VAL   A CG1   1 
ATOM   1287 C  CG2   . VAL   A 1 163 ? -7.639  17.224 3.130  1.00 10.10 ? 160 VAL   A CG2   1 
ATOM   1288 N  N     . ARG   A 1 164 ? -8.202  12.747 3.539  1.00 10.23 ? 161 ARG   A N     1 
ATOM   1289 C  CA    . ARG   A 1 164 ? -8.750  11.423 3.232  1.00 10.71 ? 161 ARG   A CA    1 
ATOM   1290 C  C     . ARG   A 1 164 ? -9.354  10.784 4.497  1.00 10.67 ? 161 ARG   A C     1 
ATOM   1291 O  O     . ARG   A 1 164 ? -10.395 10.152 4.427  1.00 10.92 ? 161 ARG   A O     1 
ATOM   1292 C  CB    . ARG   A 1 164 ? -7.675  10.500 2.656  1.00 11.24 ? 161 ARG   A CB    1 
ATOM   1293 C  CG    . ARG   A 1 164 ? -7.291  10.824 1.232  1.00 12.00 ? 161 ARG   A CG    1 
ATOM   1294 C  CD    . ARG   A 1 164 ? -5.940  10.244 0.835  1.00 13.12 ? 161 ARG   A CD    1 
ATOM   1295 N  NE    . ARG   A 1 164 ? -5.881  10.079 -0.619 1.00 14.07 ? 161 ARG   A NE    1 
ATOM   1296 C  CZ    . ARG   A 1 164 ? -4.821  9.631  -1.298 1.00 16.96 ? 161 ARG   A CZ    1 
ATOM   1297 N  NH1   . ARG   A 1 164 ? -3.673  9.313  -0.683 1.00 15.72 ? 161 ARG   A NH1   1 
ATOM   1298 N  NH2   . ARG   A 1 164 ? -4.912  9.478  -2.612 1.00 18.13 ? 161 ARG   A NH2   1 
ATOM   1299 N  N     . GLU   A 1 165 ? -8.712  10.981 5.652  1.00 10.08 ? 162 GLU   A N     1 
ATOM   1300 C  CA    . GLU   A 1 165 ? -9.254  10.502 6.947  1.00 10.19 ? 162 GLU   A CA    1 
ATOM   1301 C  C     . GLU   A 1 165 ? -10.608 11.128 7.314  1.00 10.35 ? 162 GLU   A C     1 
ATOM   1302 O  O     . GLU   A 1 165 ? -11.521 10.424 7.729  1.00 11.17 ? 162 GLU   A O     1 
ATOM   1303 C  CB    . GLU   A 1 165 ? -8.277  10.722 8.122  1.00 10.43 ? 162 GLU   A CB    1 
ATOM   1304 C  CG    . GLU   A 1 165 ? -7.005  9.891  8.085  1.00 10.64 ? 162 GLU   A CG    1 
ATOM   1305 C  CD    . GLU   A 1 165 ? -7.247  8.392  8.194  1.00 11.65 ? 162 GLU   A CD    1 
ATOM   1306 O  OE1   . GLU   A 1 165 ? -7.712  7.932  9.269  1.00 13.26 ? 162 GLU   A OE1   1 
ATOM   1307 O  OE2   . GLU   A 1 165 ? -6.988  7.639  7.199  1.00 13.01 ? 162 GLU   A OE2   1 
ATOM   1308 N  N     . ILE   A 1 166 ? -10.711 12.452 7.208  1.00 10.21 ? 163 ILE   A N     1 
ATOM   1309 C  CA    . ILE   A 1 166 ? -11.989 13.152 7.405  1.00 10.60 ? 163 ILE   A CA    1 
ATOM   1310 C  C     . ILE   A 1 166 ? -13.067 12.606 6.453  1.00 11.36 ? 163 ILE   A C     1 
ATOM   1311 O  O     . ILE   A 1 166 ? -14.206 12.295 6.870  1.00 11.85 ? 163 ILE   A O     1 
ATOM   1312 C  CB    . ILE   A 1 166 ? -11.849 14.678 7.177  1.00 10.08 ? 163 ILE   A CB    1 
ATOM   1313 C  CG1   . ILE   A 1 166 ? -10.948 15.299 8.234  1.00 10.04 ? 163 ILE   A CG1   1 
ATOM   1314 C  CG2   . ILE   A 1 166 ? -13.205 15.369 7.257  1.00 10.53 ? 163 ILE   A CG2   1 
ATOM   1315 C  CD1   . ILE   A 1 166 ? -10.360 16.640 7.826  1.00 9.83  ? 163 ILE   A CD1   1 
ATOM   1316 N  N     . ARG   A 1 167 ? -12.728 12.512 5.170  1.00 11.62 ? 164 ARG   A N     1 
ATOM   1317 C  CA    . ARG   A 1 167 ? -13.692 12.040 4.147  1.00 12.39 ? 164 ARG   A CA    1 
ATOM   1318 C  C     . ARG   A 1 167 ? -14.271 10.639 4.485  1.00 13.32 ? 164 ARG   A C     1 
ATOM   1319 O  O     . ARG   A 1 167 ? -15.496 10.402 4.364  1.00 13.99 ? 164 ARG   A O     1 
ATOM   1320 C  CB    . ARG   A 1 167 ? -13.009 12.025 2.794  1.00 12.03 ? 164 ARG   A CB    1 
ATOM   1321 C  CG    . ARG   A 1 167 ? -13.953 11.875 1.610  1.00 13.07 ? 164 ARG   A CG    1 
ATOM   1322 C  CD    . ARG   A 1 167 ? -13.146 11.489 0.399  1.00 12.99 ? 164 ARG   A CD    1 
ATOM   1323 N  NE    . ARG   A 1 167 ? -12.537 12.653 -0.236 1.00 12.16 ? 164 ARG   A NE    1 
ATOM   1324 C  CZ    . ARG   A 1 167 ? -11.308 12.677 -0.789 1.00 11.93 ? 164 ARG   A CZ    1 
ATOM   1325 N  NH1   . ARG   A 1 167 ? -10.891 13.778 -1.399 1.00 11.45 ? 164 ARG   A NH1   1 
ATOM   1326 N  NH2   . ARG   A 1 167 ? -10.492 11.612 -0.764 1.00 11.37 ? 164 ARG   A NH2   1 
ATOM   1327 N  N     . GLN   A 1 168 ? -13.395 9.735  4.918  1.00 13.08 ? 165 GLN   A N     1 
ATOM   1328 C  CA    . GLN   A 1 168 ? -13.786 8.399  5.345  1.00 14.70 ? 165 GLN   A CA    1 
ATOM   1329 C  C     . GLN   A 1 168 ? -14.648 8.392  6.610  1.00 14.68 ? 165 GLN   A C     1 
ATOM   1330 O  O     . GLN   A 1 168 ? -15.655 7.665  6.673  1.00 16.23 ? 165 GLN   A O     1 
ATOM   1331 C  CB    . GLN   A 1 168 ? -12.556 7.528  5.576  1.00 15.47 ? 165 GLN   A CB    1 
ATOM   1332 C  CG    . GLN   A 1 168 ? -11.819 7.083  4.325  1.00 16.53 ? 165 GLN   A CG    1 
ATOM   1333 C  CD    . GLN   A 1 168 ? -10.346 6.708  4.578  1.00 18.25 ? 165 GLN   A CD    1 
ATOM   1334 O  OE1   . GLN   A 1 168 ? -10.010 6.046  5.565  1.00 22.04 ? 165 GLN   A OE1   1 
ATOM   1335 N  NE2   . GLN   A 1 168 ? -9.475  7.100  3.674  1.00 18.71 ? 165 GLN   A NE2   1 
ATOM   1336 N  N     . TYR   A 1 169 ? -14.266 9.176  7.620  1.00 13.41 ? 166 TYR   A N     1 
ATOM   1337 C  CA    . TYR   A 1 169 ? -15.066 9.239  8.853  1.00 14.42 ? 166 TYR   A CA    1 
ATOM   1338 C  C     . TYR   A 1 169 ? -16.491 9.748  8.577  1.00 14.41 ? 166 TYR   A C     1 
ATOM   1339 O  O     . TYR   A 1 169 ? -17.439 9.278  9.214  1.00 14.97 ? 166 TYR   A O     1 
ATOM   1340 C  CB    . TYR   A 1 169 ? -14.391 10.103 9.921  1.00 14.56 ? 166 TYR   A CB    1 
ATOM   1341 C  CG    . TYR   A 1 169 ? -13.497 9.327  10.862 1.00 15.58 ? 166 TYR   A CG    1 
ATOM   1342 C  CD1   . TYR   A 1 169 ? -14.018 8.675  11.959 1.00 18.30 ? 166 TYR   A CD1   1 
ATOM   1343 C  CD2   . TYR   A 1 169 ? -12.133 9.248  10.654 1.00 15.72 ? 166 TYR   A CD2   1 
ATOM   1344 C  CE1   . TYR   A 1 169 ? -13.191 7.961  12.828 1.00 18.87 ? 166 TYR   A CE1   1 
ATOM   1345 C  CE2   . TYR   A 1 169 ? -11.303 8.548  11.521 1.00 16.83 ? 166 TYR   A CE2   1 
ATOM   1346 C  CZ    . TYR   A 1 169 ? -11.840 7.909  12.607 1.00 17.86 ? 166 TYR   A CZ    1 
ATOM   1347 O  OH    . TYR   A 1 169 ? -11.040 7.191  13.488 1.00 20.11 ? 166 TYR   A OH    1 
ATOM   1348 N  N     . ARG   A 1 170 ? -16.653 10.671 7.630  1.00 14.14 ? 167 ARG   A N     1 
ATOM   1349 C  CA    . ARG   A 1 170 ? -17.995 11.139 7.226  1.00 15.36 ? 167 ARG   A CA    1 
ATOM   1350 C  C     . ARG   A 1 170 ? -18.935 10.027 6.711  1.00 16.45 ? 167 ARG   A C     1 
ATOM   1351 O  O     . ARG   A 1 170 ? -20.153 10.140 6.844  1.00 15.44 ? 167 ARG   A O     1 
ATOM   1352 C  CB    . ARG   A 1 170 ? -17.896 12.259 6.176  1.00 15.21 ? 167 ARG   A CB    1 
ATOM   1353 C  CG    . ARG   A 1 170 ? -17.288 13.562 6.686  1.00 15.12 ? 167 ARG   A CG    1 
ATOM   1354 C  CD    . ARG   A 1 170 ? -17.244 14.588 5.567  1.00 15.46 ? 167 ARG   A CD    1 
ATOM   1355 N  NE    . ARG   A 1 170 ? -16.776 15.922 5.985  1.00 16.04 ? 167 ARG   A NE    1 
ATOM   1356 C  CZ    . ARG   A 1 170 ? -16.019 16.719 5.235  1.00 15.85 ? 167 ARG   A CZ    1 
ATOM   1357 N  NH1   . ARG   A 1 170 ? -15.603 16.311 4.046  1.00 16.79 ? 167 ARG   A NH1   1 
ATOM   1358 N  NH2   . ARG   A 1 170 ? -15.646 17.920 5.678  1.00 17.22 ? 167 ARG   A NH2   1 
ATOM   1359 N  N     . LEU   A 1 171 ? -18.382 8.959  6.135  1.00 16.61 ? 168 LEU   A N     1 
ATOM   1360 C  CA    . LEU   A 1 171 ? -19.202 7.805  5.701  1.00 18.96 ? 168 LEU   A CA    1 
ATOM   1361 C  C     . LEU   A 1 171 ? -19.500 6.755  6.807  1.00 20.83 ? 168 LEU   A C     1 
ATOM   1362 O  O     . LEU   A 1 171 ? -20.148 5.734  6.521  1.00 22.03 ? 168 LEU   A O     1 
ATOM   1363 C  CB    . LEU   A 1 171 ? -18.581 7.122  4.462  1.00 18.34 ? 168 LEU   A CB    1 
ATOM   1364 C  CG    . LEU   A 1 171 ? -18.475 8.022  3.208  1.00 19.17 ? 168 LEU   A CG    1 
ATOM   1365 C  CD1   . LEU   A 1 171 ? -17.667 7.321  2.123  1.00 19.74 ? 168 LEU   A CD1   1 
ATOM   1366 C  CD2   . LEU   A 1 171 ? -19.824 8.473  2.652  1.00 19.21 ? 168 LEU   A CD2   1 
ATOM   1367 N  N     . LYS   A 1 172 ? -19.075 7.012  8.038  1.00 23.09 ? 169 LYS   A N     1 
ATOM   1368 C  CA    . LYS   A 1 172 ? -19.235 6.111  9.218  1.00 24.96 ? 169 LYS   A CA    1 
ATOM   1369 C  C     . LYS   A 1 172 ? -20.117 6.736  10.317 1.00 25.35 ? 169 LYS   A C     1 
ATOM   1370 O  O     . LYS   A 1 172 ? -20.652 5.990  11.116 1.00 26.34 ? 169 LYS   A O     1 
ATOM   1371 C  CB    . LYS   A 1 172 ? -17.919 5.903  9.976  1.00 27.34 ? 169 LYS   A CB    1 
ATOM   1372 C  CG    . LYS   A 1 172 ? -16.880 4.983  9.342  1.00 31.23 ? 169 LYS   A CG    1 
ATOM   1373 C  CD    . LYS   A 1 172 ? -15.727 4.600  10.218 1.00 31.88 ? 169 LYS   A CD    1 
ATOM   1374 C  CE    . LYS   A 1 172 ? -14.632 5.644  10.389 1.00 32.92 ? 169 LYS   A CE    1 
ATOM   1375 N  NZ    . LYS   A 1 172 ? -13.483 5.324  9.524  1.00 35.27 ? 169 LYS   A NZ    1 
ATOM   1376 O  OXT   . LYS   A 1 172 ? -20.189 7.950  10.388 1.00 22.34 ? 169 LYS   A OXT   1 
HETATM 1377 P  PB    . GDP   B 2 .   ? 6.284   25.841 15.680 1.00 13.19 ? 201 GDP   A PB    1 
HETATM 1378 O  O1B   . GDP   B 2 .   ? 5.446   26.669 14.748 1.00 12.85 ? 201 GDP   A O1B   1 
HETATM 1379 O  O2B   . GDP   B 2 .   ? 5.874   24.406 15.816 1.00 12.48 ? 201 GDP   A O2B   1 
HETATM 1380 O  O3B   . GDP   B 2 .   ? 6.602   26.551 16.991 1.00 14.00 ? 201 GDP   A O3B   1 
HETATM 1381 O  O3A   . GDP   B 2 .   ? 7.734   25.685 14.931 1.00 12.37 ? 201 GDP   A O3A   1 
HETATM 1382 P  PA    . GDP   B 2 .   ? 8.350   26.513 13.672 1.00 12.89 ? 201 GDP   A PA    1 
HETATM 1383 O  O1A   . GDP   B 2 .   ? 7.626   26.072 12.435 1.00 12.96 ? 201 GDP   A O1A   1 
HETATM 1384 O  O2A   . GDP   B 2 .   ? 8.390   27.982 13.984 1.00 13.85 ? 201 GDP   A O2A   1 
HETATM 1385 O  "O5'" . GDP   B 2 .   ? 9.846   25.902 13.610 1.00 12.88 ? 201 GDP   A "O5'" 1 
HETATM 1386 C  "C5'" . GDP   B 2 .   ? 10.710  25.983 14.748 1.00 13.27 ? 201 GDP   A "C5'" 1 
HETATM 1387 C  "C4'" . GDP   B 2 .   ? 12.170  25.961 14.325 1.00 13.49 ? 201 GDP   A "C4'" 1 
HETATM 1388 O  "O4'" . GDP   B 2 .   ? 12.443  24.669 13.756 1.00 13.13 ? 201 GDP   A "O4'" 1 
HETATM 1389 C  "C3'" . GDP   B 2 .   ? 12.517  26.991 13.271 1.00 13.79 ? 201 GDP   A "C3'" 1 
HETATM 1390 O  "O3'" . GDP   B 2 .   ? 13.857  27.460 13.478 1.00 15.23 ? 201 GDP   A "O3'" 1 
HETATM 1391 C  "C2'" . GDP   B 2 .   ? 12.338  26.230 11.970 1.00 13.23 ? 201 GDP   A "C2'" 1 
HETATM 1392 O  "O2'" . GDP   B 2 .   ? 13.069  26.724 10.819 1.00 14.14 ? 201 GDP   A "O2'" 1 
HETATM 1393 C  "C1'" . GDP   B 2 .   ? 12.800  24.836 12.397 1.00 12.62 ? 201 GDP   A "C1'" 1 
HETATM 1394 N  N9    . GDP   B 2 .   ? 12.184  23.780 11.567 1.00 11.74 ? 201 GDP   A N9    1 
HETATM 1395 C  C8    . GDP   B 2 .   ? 10.861  23.570 11.336 1.00 11.22 ? 201 GDP   A C8    1 
HETATM 1396 N  N7    . GDP   B 2 .   ? 10.680  22.508 10.539 1.00 10.91 ? 201 GDP   A N7    1 
HETATM 1397 C  C5    . GDP   B 2 .   ? 11.890  22.002 10.243 1.00 10.50 ? 201 GDP   A C5    1 
HETATM 1398 C  C6    . GDP   B 2 .   ? 12.404  20.871 9.425  1.00 10.56 ? 201 GDP   A C6    1 
HETATM 1399 O  O6    . GDP   B 2 .   ? 11.636  20.085 8.808  1.00 9.78  ? 201 GDP   A O6    1 
HETATM 1400 N  N1    . GDP   B 2 .   ? 13.726  20.706 9.396  1.00 10.71 ? 201 GDP   A N1    1 
HETATM 1401 C  C2    . GDP   B 2 .   ? 14.579  21.502 10.051 1.00 11.47 ? 201 GDP   A C2    1 
HETATM 1402 N  N2    . GDP   B 2 .   ? 15.911  21.266 9.951  1.00 12.25 ? 201 GDP   A N2    1 
HETATM 1403 N  N3    . GDP   B 2 .   ? 14.191  22.560 10.817 1.00 11.73 ? 201 GDP   A N3    1 
HETATM 1404 C  C4    . GDP   B 2 .   ? 12.873  22.850 10.927 1.00 11.70 ? 201 GDP   A C4    1 
HETATM 1405 MG MG    . MG    C 3 .   ? 4.369   28.583 14.999 1.00 15.07 2 202 MG    A MG    1 
HETATM 1406 N  NAL   . A1IK7 D 4 .   ? -10.466 29.477 11.854 1.00 33.48 ? 203 A1IK7 A NAL   1 
HETATM 1407 C  CAM   . A1IK7 D 4 .   ? -10.190 28.188 11.554 1.00 31.41 ? 203 A1IK7 A CAM   1 
HETATM 1408 C  CAN   . A1IK7 D 4 .   ? -9.643  27.649 10.387 1.00 28.25 ? 203 A1IK7 A CAN   1 
HETATM 1409 C  CAO   . A1IK7 D 4 .   ? -9.424  26.270 10.278 1.00 27.62 ? 203 A1IK7 A CAO   1 
HETATM 1410 C  CAP   . A1IK7 D 4 .   ? -9.738  25.397 11.316 1.00 27.24 ? 203 A1IK7 A CAP   1 
HETATM 1411 C  CAQ   . A1IK7 D 4 .   ? -10.295 25.938 12.491 1.00 29.50 ? 203 A1IK7 A CAQ   1 
HETATM 1412 CL CLAR  . A1IK7 D 4 .   ? -10.683 24.923 13.829 1.00 30.04 ? 203 A1IK7 A CLAR  1 
HETATM 1413 C  CAT   . A1IK7 D 4 .   ? -10.504 27.303 12.613 1.00 31.89 ? 203 A1IK7 A CAT   1 
HETATM 1414 S  SAU   . A1IK7 D 4 .   ? -11.159 28.211 13.928 1.00 31.83 ? 203 A1IK7 A SAU   1 
HETATM 1415 C  CAK   . A1IK7 D 4 .   ? -10.998 29.708 13.066 1.00 35.17 ? 203 A1IK7 A CAK   1 
HETATM 1416 N  NAJ   . A1IK7 D 4 .   ? -11.356 30.885 13.565 1.00 37.99 ? 203 A1IK7 A NAJ   1 
HETATM 1417 S  SAB   . A1IK7 D 4 .   ? -11.871 31.051 15.107 1.00 44.18 ? 203 A1IK7 A SAB   1 
HETATM 1418 O  OAA   . A1IK7 D 4 .   ? -12.442 32.440 15.277 1.00 45.88 ? 203 A1IK7 A OAA   1 
HETATM 1419 O  OAC   . A1IK7 D 4 .   ? -12.914 30.021 15.476 1.00 42.65 ? 203 A1IK7 A OAC   1 
HETATM 1420 C  CAI   . A1IK7 D 4 .   ? -10.477 30.890 16.171 1.00 45.57 ? 203 A1IK7 A CAI   1 
HETATM 1421 C  CAS   . A1IK7 D 4 .   ? -9.216  31.271 15.708 1.00 44.43 ? 203 A1IK7 A CAS   1 
HETATM 1422 C  CAE   . A1IK7 D 4 .   ? -8.100  31.164 16.533 1.00 43.00 ? 203 A1IK7 A CAE   1 
HETATM 1423 O  OAD   . A1IK7 D 4 .   ? -6.880  31.543 16.056 1.00 39.69 ? 203 A1IK7 A OAD   1 
HETATM 1424 C  CAF   . A1IK7 D 4 .   ? -8.252  30.667 17.830 1.00 44.38 ? 203 A1IK7 A CAF   1 
HETATM 1425 C  CAG   . A1IK7 D 4 .   ? -9.518  30.289 18.298 1.00 46.11 ? 203 A1IK7 A CAG   1 
HETATM 1426 C  CAH   . A1IK7 D 4 .   ? -10.634 30.397 17.471 1.00 46.22 ? 203 A1IK7 A CAH   1 
HETATM 1427 C  C1    . EDO   E 5 .   ? -4.457  12.048 -6.315 1.00 24.22 ? 204 EDO   A C1    1 
HETATM 1428 O  O1    . EDO   E 5 .   ? -5.372  12.886 -5.603 1.00 21.47 ? 204 EDO   A O1    1 
HETATM 1429 C  C2    . EDO   E 5 .   ? -5.180  10.784 -6.782 1.00 24.58 ? 204 EDO   A C2    1 
HETATM 1430 O  O2    . EDO   E 5 .   ? -6.215  11.128 -7.604 1.00 27.40 ? 204 EDO   A O2    1 
HETATM 1431 O  O     . HOH   F 6 .   ? 0.862   33.048 10.168 1.00 24.37 ? 301 HOH   A O     1 
HETATM 1432 O  O     . HOH   F 6 .   ? -17.722 8.744  12.502 1.00 27.86 ? 302 HOH   A O     1 
HETATM 1433 O  O     . HOH   F 6 .   ? 5.836   -1.161 12.529 1.00 21.81 ? 303 HOH   A O     1 
HETATM 1434 O  O     . HOH   F 6 .   ? 15.517  10.480 23.937 1.00 22.47 ? 304 HOH   A O     1 
HETATM 1435 O  O     . HOH   F 6 .   ? 6.431   29.443 14.736 1.00 16.59 ? 305 HOH   A O     1 
HETATM 1436 O  O     . HOH   F 6 .   ? -6.316  7.305  22.314 1.00 31.29 ? 306 HOH   A O     1 
HETATM 1437 O  O     . HOH   F 6 .   ? 2.582   27.700 14.964 1.00 13.82 ? 307 HOH   A O     1 
HETATM 1438 O  O     . HOH   F 6 .   ? 14.118  15.218 2.332  1.00 20.88 ? 308 HOH   A O     1 
HETATM 1439 O  O     . HOH   F 6 .   ? 10.034  8.180  25.964 1.00 23.55 ? 309 HOH   A O     1 
HETATM 1440 O  O     . HOH   F 6 .   ? 8.262   11.346 30.689 1.00 28.92 ? 310 HOH   A O     1 
HETATM 1441 O  O     . HOH   F 6 .   ? -16.577 14.088 -0.275 1.00 23.70 ? 311 HOH   A O     1 
HETATM 1442 O  O     . HOH   F 6 .   ? -3.696  27.990 20.397 1.00 20.15 ? 312 HOH   A O     1 
HETATM 1443 O  O     . HOH   F 6 .   ? -7.386  9.151  11.551 1.00 12.89 ? 313 HOH   A O     1 
HETATM 1444 O  O     . HOH   F 6 .   ? -6.948  6.727  3.132  1.00 29.15 ? 314 HOH   A O     1 
HETATM 1445 O  O     . HOH   F 6 .   ? -8.475  6.964  13.023 1.00 18.10 ? 315 HOH   A O     1 
HETATM 1446 O  O     . HOH   F 6 .   ? -7.106  19.963 33.084 1.00 37.45 ? 316 HOH   A O     1 
HETATM 1447 O  O     . HOH   F 6 .   ? 13.513  19.834 17.373 1.00 13.54 ? 317 HOH   A O     1 
HETATM 1448 O  O     . HOH   F 6 .   ? -13.363 26.599 27.971 1.00 30.22 ? 318 HOH   A O     1 
HETATM 1449 O  O     . HOH   F 6 .   ? -15.202 28.701 15.374 1.00 37.87 ? 319 HOH   A O     1 
HETATM 1450 O  O     . HOH   F 6 .   ? 8.769   27.979 17.526 1.00 20.60 ? 320 HOH   A O     1 
HETATM 1451 O  O     . HOH   F 6 .   ? -7.262  5.435  10.038 1.00 27.69 ? 321 HOH   A O     1 
HETATM 1452 O  O     . HOH   F 6 .   ? 0.444   -0.650 18.649 1.00 27.54 ? 322 HOH   A O     1 
HETATM 1453 O  O     . HOH   F 6 .   ? -8.716  5.812  15.624 1.00 28.81 ? 323 HOH   A O     1 
HETATM 1454 O  O     . HOH   F 6 .   ? -17.120 18.176 -4.082 1.00 27.54 ? 324 HOH   A O     1 
HETATM 1455 O  O     . HOH   F 6 .   ? -11.751 30.773 8.133  1.00 34.82 ? 325 HOH   A O     1 
HETATM 1456 O  O     . HOH   F 6 .   ? -13.672 16.000 14.042 1.00 17.91 ? 326 HOH   A O     1 
HETATM 1457 O  O     . HOH   F 6 .   ? -16.713 14.554 2.368  1.00 25.08 ? 327 HOH   A O     1 
HETATM 1458 O  O     . HOH   F 6 .   ? 15.630  10.848 8.966  1.00 11.35 ? 328 HOH   A O     1 
HETATM 1459 O  O     . HOH   F 6 .   ? 19.391  15.273 18.250 1.00 17.04 ? 329 HOH   A O     1 
HETATM 1460 O  O     . HOH   F 6 .   ? -8.699  8.681  16.071 1.00 25.84 ? 330 HOH   A O     1 
HETATM 1461 O  O     . HOH   F 6 .   ? -16.924 22.100 12.422 1.00 26.86 ? 331 HOH   A O     1 
HETATM 1462 O  O     . HOH   F 6 .   ? -16.082 21.856 24.803 1.00 42.21 ? 332 HOH   A O     1 
HETATM 1463 O  O     . HOH   F 6 .   ? 10.090  29.516 15.407 1.00 21.93 ? 333 HOH   A O     1 
HETATM 1464 O  O     . HOH   F 6 .   ? 2.849   -2.830 20.802 1.00 36.61 ? 334 HOH   A O     1 
HETATM 1465 O  O     . HOH   F 6 .   ? -4.263  0.085  14.374 1.00 22.63 ? 335 HOH   A O     1 
HETATM 1466 O  O     . HOH   F 6 .   ? -14.524 27.525 24.875 1.00 32.90 ? 336 HOH   A O     1 
HETATM 1467 O  O     . HOH   F 6 .   ? 3.776   6.755  5.878  1.00 14.69 ? 337 HOH   A O     1 
HETATM 1468 O  O     . HOH   F 6 .   ? -8.306  7.675  -5.376 1.00 9.88  ? 338 HOH   A O     1 
HETATM 1469 O  O     . HOH   F 6 .   ? -2.013  20.979 25.253 1.00 36.89 ? 339 HOH   A O     1 
HETATM 1470 O  O     . HOH   F 6 .   ? -3.801  14.982 -4.833 1.00 19.16 ? 340 HOH   A O     1 
HETATM 1471 O  O     . HOH   F 6 .   ? -1.065  3.053  11.857 1.00 13.33 ? 341 HOH   A O     1 
HETATM 1472 O  O     . HOH   F 6 .   ? -2.615  9.097  1.977  1.00 29.24 ? 342 HOH   A O     1 
HETATM 1473 O  O     . HOH   F 6 .   ? 10.988  20.292 18.745 1.00 28.16 ? 343 HOH   A O     1 
HETATM 1474 O  O     . HOH   F 6 .   ? 0.509   31.189 12.158 1.00 19.37 ? 344 HOH   A O     1 
HETATM 1475 O  O     . HOH   F 6 .   ? -14.606 20.588 -9.160 1.00 19.51 ? 345 HOH   A O     1 
HETATM 1476 O  O     . HOH   F 6 .   ? -18.233 20.166 7.096  1.00 23.48 ? 346 HOH   A O     1 
HETATM 1477 O  O     . HOH   F 6 .   ? -5.698  8.594  4.941  1.00 23.45 ? 347 HOH   A O     1 
HETATM 1478 O  O     . HOH   F 6 .   ? -15.724 4.933  6.210  1.00 35.35 ? 348 HOH   A O     1 
HETATM 1479 O  O     . HOH   F 6 .   ? 6.384   -1.319 15.072 1.00 29.60 ? 349 HOH   A O     1 
HETATM 1480 O  O     . HOH   F 6 .   ? -7.096  13.677 -8.265 1.00 15.55 ? 350 HOH   A O     1 
HETATM 1481 O  O     . HOH   F 6 .   ? 0.745   5.141  8.411  1.00 11.29 ? 351 HOH   A O     1 
HETATM 1482 O  O     . HOH   F 6 .   ? 16.234  8.480  22.377 1.00 31.41 ? 352 HOH   A O     1 
HETATM 1483 O  O     . HOH   F 6 .   ? -22.003 14.590 22.937 1.00 25.54 ? 353 HOH   A O     1 
HETATM 1484 O  O     . HOH   F 6 .   ? 1.556   2.295  12.359 1.00 18.60 ? 354 HOH   A O     1 
HETATM 1485 O  O     . HOH   F 6 .   ? 21.758  22.055 6.576  1.00 22.25 ? 355 HOH   A O     1 
HETATM 1486 O  O     . HOH   F 6 .   ? 8.095   27.191 5.974  1.00 13.75 ? 356 HOH   A O     1 
HETATM 1487 O  O     . HOH   F 6 .   ? 15.867  26.560 10.832 1.00 29.08 ? 357 HOH   A O     1 
HETATM 1488 O  O     . HOH   F 6 .   ? -0.453  7.131  24.632 1.00 29.76 ? 358 HOH   A O     1 
HETATM 1489 O  O     . HOH   F 6 .   ? 14.385  14.128 4.906  1.00 16.99 ? 359 HOH   A O     1 
HETATM 1490 O  O     . HOH   F 6 .   ? 4.535   28.461 16.848 1.00 19.93 ? 360 HOH   A O     1 
HETATM 1491 O  O     . HOH   F 6 .   ? 11.377  32.087 4.221  1.00 26.74 ? 361 HOH   A O     1 
HETATM 1492 O  O     . HOH   F 6 .   ? 1.294   9.007  0.265  1.00 16.47 ? 362 HOH   A O     1 
HETATM 1493 O  O     . HOH   F 6 .   ? 2.837   10.425 23.475 1.00 20.39 ? 363 HOH   A O     1 
HETATM 1494 O  O     . HOH   F 6 .   ? 3.790   30.618 15.236 1.00 13.39 ? 364 HOH   A O     1 
HETATM 1495 O  O     . HOH   F 6 .   ? -16.066 14.250 26.830 1.00 33.75 ? 365 HOH   A O     1 
HETATM 1496 O  O     . HOH   F 6 .   ? 13.298  23.893 17.330 1.00 26.74 ? 366 HOH   A O     1 
HETATM 1497 O  O     . HOH   F 6 .   ? -14.624 24.559 6.137  1.00 32.68 ? 367 HOH   A O     1 
HETATM 1498 O  O     . HOH   F 6 .   ? 12.835  28.387 1.372  1.00 25.63 ? 368 HOH   A O     1 
HETATM 1499 O  O     . HOH   F 6 .   ? 10.036  29.143 11.717 1.00 30.21 ? 369 HOH   A O     1 
HETATM 1500 O  O     . HOH   F 6 .   ? 4.386   17.659 20.109 1.00 13.10 ? 370 HOH   A O     1 
HETATM 1501 O  O     . HOH   F 6 .   ? 11.222  33.163 9.501  1.00 29.52 ? 371 HOH   A O     1 
HETATM 1502 O  O     . HOH   F 6 .   ? 16.711  21.053 15.903 1.00 18.08 ? 372 HOH   A O     1 
HETATM 1503 O  O     . HOH   F 6 .   ? -15.191 16.252 -8.492 1.00 15.52 ? 373 HOH   A O     1 
HETATM 1504 O  O     . HOH   F 6 .   ? 12.860  6.262  20.335 1.00 25.79 ? 374 HOH   A O     1 
HETATM 1505 O  O     . HOH   F 6 .   ? -18.601 5.442  13.194 1.00 36.85 ? 375 HOH   A O     1 
HETATM 1506 O  O     . HOH   F 6 .   ? 3.970   26.620 19.497 1.00 20.21 ? 376 HOH   A O     1 
HETATM 1507 O  O     . HOH   F 6 .   ? -9.944  11.884 26.528 1.00 25.70 ? 377 HOH   A O     1 
HETATM 1508 O  O     . HOH   F 6 .   ? -1.880  31.484 20.705 1.00 25.95 ? 378 HOH   A O     1 
HETATM 1509 O  O     . HOH   F 6 .   ? 5.278   17.793 -0.412 1.00 12.27 ? 379 HOH   A O     1 
HETATM 1510 O  O     . HOH   F 6 .   ? 15.762  25.612 14.610 1.00 20.95 ? 380 HOH   A O     1 
HETATM 1511 O  O     . HOH   F 6 .   ? -4.611  34.062 5.740  1.00 29.30 ? 381 HOH   A O     1 
HETATM 1512 O  O     . HOH   F 6 .   ? -21.610 11.857 5.015  1.00 17.18 ? 382 HOH   A O     1 
HETATM 1513 O  O     . HOH   F 6 .   ? -8.651  31.209 6.532  1.00 31.11 ? 383 HOH   A O     1 
HETATM 1514 O  O     . HOH   F 6 .   ? 3.709   30.078 21.501 1.00 31.75 ? 384 HOH   A O     1 
HETATM 1515 O  O     . HOH   F 6 .   ? 17.589  10.941 11.025 1.00 13.53 ? 385 HOH   A O     1 
HETATM 1516 O  O     . HOH   F 6 .   ? -5.303  27.905 -3.064 1.00 22.71 ? 386 HOH   A O     1 
HETATM 1517 O  O     . HOH   F 6 .   ? -5.193  0.040  20.755 1.00 26.68 ? 387 HOH   A O     1 
HETATM 1518 O  O     . HOH   F 6 .   ? -5.013  15.693 -8.134 1.00 29.36 ? 388 HOH   A O     1 
HETATM 1519 O  O     . HOH   F 6 .   ? 12.673  8.335  22.164 1.00 27.84 ? 389 HOH   A O     1 
HETATM 1520 O  O     . HOH   F 6 .   ? -19.246 24.965 0.143  1.00 34.61 ? 390 HOH   A O     1 
HETATM 1521 O  O     . HOH   F 6 .   ? -15.148 18.324 -6.745 1.00 14.38 ? 391 HOH   A O     1 
HETATM 1522 O  O     . HOH   F 6 .   ? -9.888  25.866 29.000 1.00 41.55 ? 392 HOH   A O     1 
HETATM 1523 O  O     . HOH   F 6 .   ? -1.554  28.850 -1.985 1.00 34.15 ? 393 HOH   A O     1 
HETATM 1524 O  O     . HOH   F 6 .   ? 7.376   14.781 -1.019 1.00 16.11 ? 394 HOH   A O     1 
HETATM 1525 O  O     . HOH   F 6 .   ? 9.382   20.017 23.476 1.00 22.96 ? 395 HOH   A O     1 
HETATM 1526 O  O     . HOH   F 6 .   ? -2.618  25.974 30.882 1.00 33.65 ? 396 HOH   A O     1 
HETATM 1527 O  O     . HOH   F 6 .   ? -17.912 20.968 14.602 1.00 24.67 ? 397 HOH   A O     1 
HETATM 1528 O  O     . HOH   F 6 .   ? 19.242  17.641 17.062 1.00 22.20 ? 398 HOH   A O     1 
HETATM 1529 O  O     . HOH   F 6 .   ? 15.214  24.876 2.261  1.00 31.07 ? 399 HOH   A O     1 
HETATM 1530 O  O     . HOH   F 6 .   ? 10.255  7.551  23.385 1.00 41.40 ? 400 HOH   A O     1 
HETATM 1531 O  O     . HOH   F 6 .   ? -10.398 22.312 -9.446 1.00 21.15 ? 401 HOH   A O     1 
HETATM 1532 O  O     . HOH   F 6 .   ? 5.051   12.238 -1.020 1.00 20.19 ? 402 HOH   A O     1 
HETATM 1533 O  O     . HOH   F 6 .   ? 15.253  22.795 14.020 1.00 18.69 ? 403 HOH   A O     1 
HETATM 1534 O  O     . HOH   F 6 .   ? -17.444 11.826 2.671  1.00 19.29 ? 404 HOH   A O     1 
HETATM 1535 O  O     . HOH   F 6 .   ? -18.396 21.102 2.153  1.00 23.11 ? 405 HOH   A O     1 
HETATM 1536 O  O     . HOH   F 6 .   ? -13.785 27.724 -6.322 1.00 36.64 ? 406 HOH   A O     1 
HETATM 1537 O  O     . HOH   F 6 .   ? -12.977 25.079 4.090  1.00 33.41 ? 407 HOH   A O     1 
HETATM 1538 O  O     . HOH   F 6 .   ? -4.575  29.506 22.899 1.00 33.19 ? 408 HOH   A O     1 
HETATM 1539 O  O     . HOH   F 6 .   ? -3.061  17.959 -6.370 1.00 37.46 ? 409 HOH   A O     1 
HETATM 1540 O  O     . HOH   F 6 .   ? 7.873   35.864 20.205 1.00 38.25 ? 410 HOH   A O     1 
HETATM 1541 O  O     . HOH   F 6 .   ? -5.705  32.368 3.217  1.00 25.65 ? 411 HOH   A O     1 
HETATM 1542 O  O     . HOH   F 6 .   ? 9.633   -0.328 11.720 1.00 22.92 ? 412 HOH   A O     1 
HETATM 1543 O  O     . HOH   F 6 .   ? -17.794 7.960  19.011 1.00 36.66 ? 413 HOH   A O     1 
HETATM 1544 O  O     . HOH   F 6 .   ? 1.720   6.468  3.750  1.00 23.24 ? 414 HOH   A O     1 
HETATM 1545 O  O     . HOH   F 6 .   ? 13.423  16.057 24.564 1.00 22.27 ? 415 HOH   A O     1 
HETATM 1546 O  O     . HOH   F 6 .   ? 7.916   36.033 12.187 1.00 25.07 ? 416 HOH   A O     1 
HETATM 1547 O  O     . HOH   F 6 .   ? -6.804  32.875 13.346 1.00 38.09 ? 417 HOH   A O     1 
HETATM 1548 O  O     . HOH   F 6 .   ? -1.321  35.912 16.207 1.00 26.53 ? 418 HOH   A O     1 
HETATM 1549 O  O     . HOH   F 6 .   ? -5.739  34.514 9.782  1.00 29.87 ? 419 HOH   A O     1 
HETATM 1550 O  O     . HOH   F 6 .   ? -4.180  20.539 -6.722 1.00 31.90 ? 420 HOH   A O     1 
HETATM 1551 O  O     . HOH   F 6 .   ? 8.772   23.256 23.464 1.00 30.54 ? 421 HOH   A O     1 
HETATM 1552 O  O     . HOH   F 6 .   ? 0.511   36.928 17.936 1.00 35.91 ? 422 HOH   A O     1 
HETATM 1553 O  O     . HOH   F 6 .   ? -10.300 6.399  8.696  1.00 26.15 ? 423 HOH   A O     1 
HETATM 1554 O  O     . HOH   F 6 .   ? -19.638 17.277 -8.977 1.00 22.71 ? 424 HOH   A O     1 
HETATM 1555 O  O     . HOH   F 6 .   ? 14.552  5.152  13.221 1.00 23.47 ? 425 HOH   A O     1 
HETATM 1556 O  O     . HOH   F 6 .   ? 2.218   28.446 -3.429 1.00 33.69 ? 426 HOH   A O     1 
HETATM 1557 O  O     . HOH   F 6 .   ? 9.977   9.147  14.582 1.00 17.07 ? 427 HOH   A O     1 
HETATM 1558 O  O     . HOH   F 6 .   ? 4.156   15.200 -0.702 1.00 11.75 ? 428 HOH   A O     1 
HETATM 1559 O  O     . HOH   F 6 .   ? -17.114 19.586 18.585 1.00 44.67 ? 429 HOH   A O     1 
HETATM 1560 O  O     . HOH   F 6 .   ? -7.498  34.259 7.818  1.00 31.12 ? 430 HOH   A O     1 
HETATM 1561 O  O     . HOH   F 6 .   ? 15.451  29.363 15.485 1.00 42.01 ? 431 HOH   A O     1 
HETATM 1562 O  O     . HOH   F 6 .   ? -10.766 8.882  0.901  1.00 8.23  ? 432 HOH   A O     1 
HETATM 1563 O  O     . HOH   F 6 .   ? -18.125 19.255 4.072  1.00 27.45 ? 433 HOH   A O     1 
HETATM 1564 O  O     . HOH   F 6 .   ? 1.301   34.965 5.919  1.00 24.19 ? 434 HOH   A O     1 
HETATM 1565 O  O     . HOH   F 6 .   ? -3.633  35.404 7.846  1.00 31.39 ? 435 HOH   A O     1 
HETATM 1566 O  O     . HOH   F 6 .   ? 16.592  4.532  15.074 1.00 28.80 ? 436 HOH   A O     1 
HETATM 1567 O  O     . HOH   F 6 .   ? -0.448  35.556 3.917  1.00 25.83 ? 437 HOH   A O     1 
HETATM 1568 O  O     . HOH   F 6 .   ? 3.369   2.156  10.351 1.00 17.08 ? 438 HOH   A O     1 
HETATM 1569 O  O     . HOH   F 6 .   ? -16.458 16.927 13.982 1.00 11.85 ? 439 HOH   A O     1 
HETATM 1570 O  O     . HOH   F 6 .   ? 11.978  22.458 20.047 1.00 35.02 ? 440 HOH   A O     1 
HETATM 1571 O  O     . HOH   F 6 .   ? 9.126   16.579 -2.283 1.00 40.90 ? 441 HOH   A O     1 
HETATM 1572 O  O     . HOH   F 6 .   ? -19.108 16.687 3.268  1.00 20.15 ? 442 HOH   A O     1 
HETATM 1573 O  O     . HOH   F 6 .   ? 0.083   32.971 21.731 1.00 42.01 ? 443 HOH   A O     1 
HETATM 1574 O  O     . HOH   F 6 .   ? 11.956  36.792 11.678 1.00 38.10 ? 444 HOH   A O     1 
HETATM 1575 O  O     . HOH   F 6 .   ? 10.026  35.504 10.435 1.00 26.96 ? 445 HOH   A O     1 
HETATM 1576 O  O     . HOH   F 6 .   ? -4.869  4.068  9.923  1.00 24.77 ? 446 HOH   A O     1 
HETATM 1577 O  O     . HOH   F 6 .   ? 12.678  29.082 16.743 1.00 43.62 ? 447 HOH   A O     1 
HETATM 1578 O  O     . HOH   F 6 .   ? 11.992  33.501 6.686  1.00 30.11 ? 448 HOH   A O     1 
HETATM 1579 O  O     . HOH   F 6 .   ? 17.472  24.959 9.419  1.00 43.87 ? 449 HOH   A O     1 
HETATM 1580 O  O     . HOH   F 6 .   ? 2.302   31.886 22.676 1.00 39.67 ? 450 HOH   A O     1 
HETATM 1581 O  O     . HOH   F 6 .   ? 6.450   22.583 25.227 1.00 40.95 ? 451 HOH   A O     1 
HETATM 1582 O  O     . HOH   F 6 .   ? 4.948   27.673 22.032 1.00 36.11 ? 452 HOH   A O     1 
HETATM 1583 O  O     . HOH   F 6 .   ? -15.355 25.762 -7.308 1.00 32.92 ? 453 HOH   A O     1 
HETATM 1584 O  O     . HOH   F 6 .   ? 12.545  26.263 17.990 1.00 36.40 ? 454 HOH   A O     1 
HETATM 1585 O  O     . HOH   F 6 .   ? -3.100  1.054  12.125 1.00 23.37 ? 455 HOH   A O     1 
HETATM 1586 O  O     . HOH   F 6 .   ? -14.427 4.729  3.716  1.00 38.77 ? 456 HOH   A O     1 
HETATM 1587 O  O     . HOH   F 6 .   ? 6.109   37.478 10.578 1.00 22.55 ? 457 HOH   A O     1 
HETATM 1588 O  O     . HOH   F 6 .   ? -7.738  33.526 2.123  1.00 39.01 ? 458 HOH   A O     1 
HETATM 1589 O  O     . HOH   F 6 .   ? -20.109 12.133 2.781  1.00 23.36 ? 459 HOH   A O     1 
HETATM 1590 O  O     . HOH   F 6 .   ? 9.276   38.196 13.531 1.00 34.82 ? 460 HOH   A O     1 
HETATM 1591 O  O     . HOH   F 6 .   ? 2.606   8.192  25.142 1.00 30.11 ? 461 HOH   A O     1 
HETATM 1592 O  O     . HOH   F 6 .   ? -5.773  4.669  23.494 1.00 35.19 ? 462 HOH   A O     1 
HETATM 1593 O  O     . HOH   F 6 .   ? 16.914  26.327 3.713  1.00 42.59 ? 463 HOH   A O     1 
HETATM 1594 O  O     . HOH   F 6 .   ? -0.451  6.706  5.423  1.00 32.02 ? 464 HOH   A O     1 
HETATM 1595 O  O     . HOH   F 6 .   ? -19.561 23.120 11.466 1.00 39.51 ? 465 HOH   A O     1 
HETATM 1596 O  O     . HOH   F 6 .   ? -20.548 14.670 1.473  1.00 27.99 ? 466 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 
7    N  N     . MET   A 4   ? 0.3559 0.3977 0.4017 0.0456  -0.0659 0.0069  1   MET   A N     
8    C  CA    . MET   A 4   ? 0.3218 0.3526 0.3632 0.0423  -0.0579 0.0070  1   MET   A CA    
9    C  C     . MET   A 4   ? 0.2819 0.3186 0.3361 0.0414  -0.0521 0.0009  1   MET   A C     
10   O  O     . MET   A 4   ? 0.2660 0.3111 0.3329 0.0457  -0.0539 -0.0016 1   MET   A O     
11   C  CB    . MET   A 4   ? 0.3457 0.3632 0.3825 0.0467  -0.0590 0.0131  1   MET   A CB    
12   C  CG    . MET   A 4   ? 0.3600 0.3664 0.3948 0.0447  -0.0522 0.0128  1   MET   A CG    
13   S  SD    . MET   A 4   ? 0.3886 0.3985 0.4386 0.0480  -0.0475 0.0061  1   MET   A SD    
14   C  CE    . MET   A 4   ? 0.3853 0.3861 0.4405 0.0569  -0.0524 0.0091  1   MET   A CE    
15   N  N     . THR   A 5   ? 0.2298 0.2616 0.2803 0.0364  -0.0452 -0.0007 2   THR   A N     
16   C  CA    . THR   A 5   ? 0.1991 0.2366 0.2595 0.0348  -0.0392 -0.0055 2   THR   A CA    
17   C  C     . THR   A 5   ? 0.1830 0.2098 0.2388 0.0348  -0.0338 -0.0047 2   THR   A C     
18   O  O     . THR   A 5   ? 0.1799 0.1973 0.2249 0.0323  -0.0330 -0.0017 2   THR   A O     
19   C  CB    . THR   A 5   ? 0.1924 0.2352 0.2528 0.0280  -0.0365 -0.0083 2   THR   A CB    
20   O  OG1   . THR   A 5   ? 0.1833 0.2359 0.2483 0.0277  -0.0421 -0.0099 2   THR   A OG1   
21   C  CG2   . THR   A 5   ? 0.1871 0.2347 0.2554 0.0253  -0.0300 -0.0114 2   THR   A CG2   
22   N  N     . GLU   A 6   ? 0.1725 0.2022 0.2367 0.0377  -0.0306 -0.0078 3   GLU   A N     
23   C  CA    . GLU   A 6   ? 0.1717 0.1919 0.2317 0.0379  -0.0261 -0.0083 3   GLU   A CA    
24   C  C     . GLU   A 6   ? 0.1496 0.1726 0.2082 0.0325  -0.0195 -0.0106 3   GLU   A C     
25   O  O     . GLU   A 6   ? 0.1544 0.1884 0.2201 0.0303  -0.0172 -0.0129 3   GLU   A O     
26   C  CB    . GLU   A 6   ? 0.1884 0.2099 0.2574 0.0447  -0.0262 -0.0114 3   GLU   A CB    
27   C  CG    . GLU   A 6   ? 0.2239 0.2404 0.2951 0.0513  -0.0330 -0.0086 3   GLU   A CG    
28   C  CD    . GLU   A 6   ? 0.2656 0.2866 0.3492 0.0591  -0.0334 -0.0131 3   GLU   A CD    
29   O  OE1   . GLU   A 6   ? 0.2966 0.3227 0.3851 0.0593  -0.0276 -0.0187 3   GLU   A OE1   
30   O  OE2   . GLU   A 6   ? 0.3185 0.3387 0.4073 0.0655  -0.0396 -0.0113 3   GLU   A OE2   
31   N  N     . TYR   A 7   ? 0.1371 0.1505 0.1875 0.0304  -0.0165 -0.0097 4   TYR   A N     
32   C  CA    . TYR   A 7   ? 0.1270 0.1421 0.1751 0.0261  -0.0107 -0.0114 4   TYR   A CA    
33   C  C     . TYR   A 7   ? 0.1290 0.1369 0.1736 0.0275  -0.0082 -0.0130 4   TYR   A C     
34   O  O     . TYR   A 7   ? 0.1351 0.1322 0.1736 0.0277  -0.0103 -0.0108 4   TYR   A O     
35   C  CB    . TYR   A 7   ? 0.1210 0.1321 0.1610 0.0206  -0.0103 -0.0085 4   TYR   A CB    
36   C  CG    . TYR   A 7   ? 0.1188 0.1364 0.1616 0.0184  -0.0126 -0.0082 4   TYR   A CG    
37   C  CD1   . TYR   A 7   ? 0.1241 0.1406 0.1648 0.0198  -0.0179 -0.0064 4   TYR   A CD1   
38   C  CD2   . TYR   A 7   ? 0.1118 0.1362 0.1591 0.0146  -0.0097 -0.0095 4   TYR   A CD2   
39   C  CE1   . TYR   A 7   ? 0.1238 0.1466 0.1667 0.0176  -0.0205 -0.0073 4   TYR   A CE1   
40   C  CE2   . TYR   A 7   ? 0.1149 0.1441 0.1655 0.0120  -0.0122 -0.0100 4   TYR   A CE2   
41   C  CZ    . TYR   A 7   ? 0.1234 0.1523 0.1720 0.0136  -0.0177 -0.0096 4   TYR   A CZ    
42   O  OH    . TYR   A 7   ? 0.1231 0.1576 0.1753 0.0110  -0.0205 -0.0114 4   TYR   A OH    
43   N  N     . LYS   A 8   ? 0.1340 0.1482 0.1820 0.0279  -0.0037 -0.0169 5   LYS   A N     
44   C  CA    . LYS   A 8   ? 0.1415 0.1505 0.1862 0.0293  -0.0014 -0.0200 5   LYS   A CA    
45   C  C     . LYS   A 8   ? 0.1307 0.1390 0.1679 0.0241  0.0021  -0.0191 5   LYS   A C     
46   O  O     . LYS   A 8   ? 0.1173 0.1345 0.1557 0.0217  0.0058  -0.0193 5   LYS   A O     
47   C  CB    . LYS   A 8   ? 0.1568 0.1744 0.2089 0.0339  0.0013  -0.0258 5   LYS   A CB    
48   C  CG    . LYS   A 8   ? 0.1811 0.1986 0.2417 0.0407  -0.0025 -0.0277 5   LYS   A CG    
49   C  CD    . LYS   A 8   ? 0.2005 0.2331 0.2716 0.0442  0.0004  -0.0322 5   LYS   A CD    
50   C  CE    . LYS   A 8   ? 0.2299 0.2614 0.3085 0.0525  -0.0013 -0.0376 5   LYS   A CE    
51   N  NZ    . LYS   A 8   ? 0.2436 0.2690 0.3266 0.0567  -0.0082 -0.0343 5   LYS   A NZ    
52   N  N     . LEU   A 9   ? 0.1304 0.1286 0.1606 0.0222  0.0008  -0.0175 6   LEU   A N     
53   C  CA    . LEU   A 9   ? 0.1344 0.1317 0.1579 0.0176  0.0031  -0.0163 6   LEU   A CA    
54   C  C     . LEU   A 9   ? 0.1346 0.1288 0.1549 0.0182  0.0044  -0.0202 6   LEU   A C     
55   O  O     . LEU   A 9   ? 0.1476 0.1347 0.1691 0.0210  0.0023  -0.0228 6   LEU   A O     
56   C  CB    . LEU   A 9   ? 0.1369 0.1278 0.1556 0.0143  0.0009  -0.0118 6   LEU   A CB    
57   C  CG    . LEU   A 9   ? 0.1461 0.1384 0.1662 0.0139  -0.0014 -0.0086 6   LEU   A CG    
58   C  CD1   . LEU   A 9   ? 0.1463 0.1340 0.1604 0.0105  -0.0024 -0.0053 6   LEU   A CD1   
59   C  CD2   . LEU   A 9   ? 0.1487 0.1503 0.1737 0.0130  0.0002  -0.0090 6   LEU   A CD2   
60   N  N     . VAL   A 10  ? 0.1245 0.1236 0.1408 0.0157  0.0073  -0.0208 7   VAL   A N     
61   C  CA    . VAL   A 10  ? 0.1353 0.1332 0.1476 0.0158  0.0082  -0.0251 7   VAL   A CA    
62   C  C     . VAL   A 10  ? 0.1406 0.1378 0.1467 0.0115  0.0083  -0.0224 7   VAL   A C     
63   O  O     . VAL   A 10  ? 0.1326 0.1353 0.1373 0.0094  0.0100  -0.0188 7   VAL   A O     
64   C  CB    . VAL   A 10  ? 0.1324 0.1404 0.1453 0.0182  0.0119  -0.0298 7   VAL   A CB    
65   C  CG1   . VAL   A 10  ? 0.1430 0.1495 0.1511 0.0188  0.0121  -0.0358 7   VAL   A CG1   
66   C  CG2   . VAL   A 10  ? 0.1329 0.1445 0.1539 0.0230  0.0123  -0.0327 7   VAL   A CG2   
67   N  N     . VAL   A 11  ? 0.1491 0.1394 0.1525 0.0102  0.0062  -0.0241 8   VAL   A N     
68   C  CA    . VAL   A 11  ? 0.1617 0.1520 0.1609 0.0064  0.0057  -0.0220 8   VAL   A CA    
69   C  C     . VAL   A 11  ? 0.1690 0.1636 0.1641 0.0064  0.0063  -0.0268 8   VAL   A C     
70   O  O     . VAL   A 11  ? 0.1796 0.1703 0.1748 0.0076  0.0052  -0.0326 8   VAL   A O     
71   C  CB    . VAL   A 11  ? 0.1668 0.1481 0.1666 0.0041  0.0029  -0.0203 8   VAL   A CB    
72   C  CG1   . VAL   A 11  ? 0.1731 0.1564 0.1702 0.0004  0.0025  -0.0184 8   VAL   A CG1   
73   C  CG2   . VAL   A 11  ? 0.1695 0.1472 0.1718 0.0046  0.0021  -0.0159 8   VAL   A CG2   
74   N  N     . VAL   A 12  ? 0.1658 0.1683 0.1571 0.0053  0.0080  -0.0244 9   VAL   A N     
75   C  CA    . VAL   A 12  ? 0.1826 0.1914 0.1681 0.0053  0.0086  -0.0282 9   VAL   A CA    
76   C  C     . VAL   A 12  ? 0.1760 0.1870 0.1580 0.0024  0.0067  -0.0249 9   VAL   A C     
77   O  O     . VAL   A 12  ? 0.1723 0.1813 0.1564 0.0010  0.0062  -0.0196 9   VAL   A O     
78   C  CB    . VAL   A 12  ? 0.1877 0.2062 0.1710 0.0071  0.0124  -0.0280 9   VAL   A CB    
79   C  CG1   . VAL   A 12  ? 0.1859 0.2042 0.1749 0.0103  0.0142  -0.0311 9   VAL   A CG1   
80   C  CG2   . VAL   A 12  ? 0.1768 0.1994 0.1596 0.0052  0.0138  -0.0200 9   VAL   A CG2   
81   N  N     . GLY   A 13  ? 0.1833 0.1988 0.1601 0.0021  0.0056  -0.0288 10  GLY   A N     
82   C  CA    . GLY   A 13  ? 0.1865 0.2059 0.1600 0.0000  0.0033  -0.0261 10  GLY   A CA    
83   C  C     . GLY   A 13  ? 0.2042 0.2254 0.1745 -0.0009 0.0004  -0.0331 10  GLY   A C     
84   O  O     . GLY   A 13  ? 0.1959 0.2121 0.1679 -0.0005 -0.0001 -0.0396 10  GLY   A O     
85   N  N     . ALA   A 14  ? 0.2020 0.2294 0.1686 -0.0021 -0.0021 -0.0315 11  ALA   A N     
86   C  CA    . ALA   A 14  ? 0.2060 0.2364 0.1695 -0.0034 -0.0055 -0.0388 11  ALA   A CA    
87   C  C     . ALA   A 14  ? 0.2001 0.2219 0.1707 -0.0063 -0.0082 -0.0434 11  ALA   A C     
88   O  O     . ALA   A 14  ? 0.2017 0.2174 0.1788 -0.0079 -0.0079 -0.0394 11  ALA   A O     
89   C  CB    . ALA   A 14  ? 0.2171 0.2570 0.1759 -0.0039 -0.0084 -0.0355 11  ALA   A CB    
90   N  N     . GLY   A 15  ? 0.2023 0.2243 0.1713 -0.0073 -0.0108 -0.0521 12  GLY   A N     
91   C  CA    . GLY   A 15  ? 0.2043 0.2185 0.1803 -0.0112 -0.0139 -0.0563 12  GLY   A CA    
92   C  C     . GLY   A 15  ? 0.1982 0.2149 0.1794 -0.0149 -0.0159 -0.0506 12  GLY   A C     
93   O  O     . GLY   A 15  ? 0.1992 0.2258 0.1775 -0.0146 -0.0175 -0.0478 12  GLY   A O     
94   N  N     . GLY   A 16  ? 0.1896 0.1978 0.1784 -0.0178 -0.0156 -0.0484 13  GLY   A N     
95   C  CA    . GLY   A 16  ? 0.1874 0.1984 0.1826 -0.0217 -0.0168 -0.0441 13  GLY   A CA    
96   C  C     . GLY   A 16  ? 0.1783 0.1924 0.1745 -0.0200 -0.0141 -0.0355 13  GLY   A C     
97   O  O     . GLY   A 16  ? 0.1700 0.1880 0.1718 -0.0226 -0.0147 -0.0324 13  GLY   A O     
98   N  N     . VAL   A 17  ? 0.1748 0.1881 0.1666 -0.0158 -0.0112 -0.0321 14  VAL   A N     
99   C  CA    . VAL   A 17  ? 0.1645 0.1795 0.1576 -0.0141 -0.0090 -0.0248 14  VAL   A CA    
100  C  C     . VAL   A 17  ? 0.1588 0.1669 0.1569 -0.0157 -0.0069 -0.0216 14  VAL   A C     
101  O  O     . VAL   A 17  ? 0.1546 0.1655 0.1551 -0.0153 -0.0057 -0.0170 14  VAL   A O     
102  C  CB    . VAL   A 17  ? 0.1644 0.1812 0.1520 -0.0098 -0.0067 -0.0217 14  VAL   A CB    
103  C  CG1   . VAL   A 17  ? 0.1689 0.1943 0.1505 -0.0083 -0.0085 -0.0226 14  VAL   A CG1   
104  C  CG2   . VAL   A 17  ? 0.1714 0.1815 0.1576 -0.0082 -0.0043 -0.0235 14  VAL   A CG2   
105  N  N     . GLY   A 18  ? 0.1583 0.1574 0.1576 -0.0172 -0.0067 -0.0239 15  GLY   A N     
106  C  CA    . GLY   A 18  ? 0.1565 0.1487 0.1590 -0.0187 -0.0051 -0.0202 15  GLY   A CA    
107  C  C     . GLY   A 18  ? 0.1579 0.1428 0.1584 -0.0155 -0.0035 -0.0189 15  GLY   A C     
108  O  O     . GLY   A 18  ? 0.1587 0.1405 0.1602 -0.0158 -0.0022 -0.0147 15  GLY   A O     
109  N  N     . LYS   A 19  ? 0.1584 0.1417 0.1563 -0.0125 -0.0036 -0.0230 16  LYS   A N     
110  C  CA    . LYS   A 19  ? 0.1568 0.1344 0.1545 -0.0091 -0.0024 -0.0226 16  LYS   A CA    
111  C  C     . LYS   A 19  ? 0.1554 0.1226 0.1563 -0.0105 -0.0034 -0.0211 16  LYS   A C     
112  O  O     . LYS   A 19  ? 0.1603 0.1246 0.1615 -0.0093 -0.0026 -0.0166 16  LYS   A O     
113  C  CB    . LYS   A 19  ? 0.1675 0.1460 0.1630 -0.0057 -0.0023 -0.0287 16  LYS   A CB    
114  C  CG    . LYS   A 19  ? 0.1716 0.1605 0.1627 -0.0040 -0.0009 -0.0291 16  LYS   A CG    
115  C  CD    . LYS   A 19  ? 0.1764 0.1679 0.1646 -0.0010 -0.0002 -0.0358 16  LYS   A CD    
116  C  CE    . LYS   A 19  ? 0.1871 0.1757 0.1748 -0.0024 -0.0029 -0.0433 16  LYS   A CE    
117  N  NZ    . LYS   A 19  ? 0.1891 0.1840 0.1740 -0.0056 -0.0051 -0.0439 16  LYS   A NZ    
118  N  N     . SER   A 20  ? 0.1619 0.1232 0.1650 -0.0134 -0.0055 -0.0246 17  SER   A N     
119  C  CA    . SER   A 20  ? 0.1681 0.1181 0.1745 -0.0156 -0.0068 -0.0225 17  SER   A CA    
120  C  C     . SER   A 20  ? 0.1666 0.1174 0.1737 -0.0196 -0.0058 -0.0151 17  SER   A C     
121  O  O     . SER   A 20  ? 0.1647 0.1092 0.1717 -0.0191 -0.0057 -0.0102 17  SER   A O     
122  C  CB    . SER   A 20  ? 0.1869 0.1303 0.1965 -0.0188 -0.0094 -0.0282 17  SER   A CB    
123  O  OG    . SER   A 20  ? 0.2111 0.1528 0.2198 -0.0145 -0.0103 -0.0359 17  SER   A OG    
124  N  N     . ALA   A 21  ? 0.1572 0.1166 0.1649 -0.0231 -0.0051 -0.0145 18  ALA   A N     
125  C  CA    . ALA   A 21  ? 0.1570 0.1196 0.1657 -0.0267 -0.0034 -0.0085 18  ALA   A CA    
126  C  C     . ALA   A 21  ? 0.1494 0.1143 0.1545 -0.0233 -0.0014 -0.0040 18  ALA   A C     
127  O  O     . ALA   A 21  ? 0.1503 0.1126 0.1546 -0.0251 -0.0004 0.0011  18  ALA   A O     
128  C  CB    . ALA   A 21  ? 0.1517 0.1253 0.1630 -0.0299 -0.0029 -0.0095 18  ALA   A CB    
129  N  N     . LEU   A 22  ? 0.1413 0.1113 0.1442 -0.0188 -0.0008 -0.0058 19  LEU   A N     
130  C  CA    . LEU   A 22  ? 0.1463 0.1183 0.1467 -0.0156 0.0006  -0.0027 19  LEU   A CA    
131  C  C     . LEU   A 22  ? 0.1509 0.1144 0.1502 -0.0137 -0.0005 -0.0006 19  LEU   A C     
132  O  O     . LEU   A 22  ? 0.1630 0.1257 0.1603 -0.0138 -0.0002 0.0037  19  LEU   A O     
133  C  CB    . LEU   A 22  ? 0.1362 0.1140 0.1356 -0.0119 0.0011  -0.0050 19  LEU   A CB    
134  C  CG    . LEU   A 22  ? 0.1340 0.1203 0.1340 -0.0125 0.0019  -0.0051 19  LEU   A CG    
135  C  CD1   . LEU   A 22  ? 0.1332 0.1233 0.1319 -0.0093 0.0020  -0.0066 19  LEU   A CD1   
136  C  CD2   . LEU   A 22  ? 0.1369 0.1267 0.1371 -0.0128 0.0034  -0.0020 19  LEU   A CD2   
137  N  N     . THR   A 23  ? 0.1616 0.1198 0.1623 -0.0114 -0.0020 -0.0041 20  THR   A N     
138  C  CA    . THR   A 23  ? 0.1706 0.1211 0.1716 -0.0082 -0.0036 -0.0027 20  THR   A CA    
139  C  C     . THR   A 23  ? 0.1740 0.1161 0.1748 -0.0114 -0.0049 0.0025  20  THR   A C     
140  O  O     . THR   A 23  ? 0.1791 0.1186 0.1781 -0.0099 -0.0058 0.0069  20  THR   A O     
141  C  CB    . THR   A 23  ? 0.1768 0.1234 0.1804 -0.0048 -0.0049 -0.0085 20  THR   A CB    
142  O  OG1   . THR   A 23  ? 0.1748 0.1302 0.1777 -0.0025 -0.0032 -0.0125 20  THR   A OG1   
143  C  CG2   . THR   A 23  ? 0.1821 0.1219 0.1876 -0.0005 -0.0068 -0.0074 20  THR   A CG2   
144  N  N     . ILE   A 24  ? 0.1870 0.1252 0.1899 -0.0160 -0.0052 0.0019  21  ILE   A N     
145  C  CA    . ILE   A 24  ? 0.1967 0.1260 0.2000 -0.0203 -0.0062 0.0077  21  ILE   A CA    
146  C  C     . ILE   A 24  ? 0.1955 0.1314 0.1947 -0.0232 -0.0039 0.0143  21  ILE   A C     
147  O  O     . ILE   A 24  ? 0.2014 0.1319 0.1982 -0.0244 -0.0045 0.0207  21  ILE   A O     
148  C  CB    . ILE   A 24  ? 0.2154 0.1386 0.2233 -0.0251 -0.0073 0.0047  21  ILE   A CB    
149  C  CG1   . ILE   A 24  ? 0.2221 0.1381 0.2330 -0.0209 -0.0098 -0.0025 21  ILE   A CG1   
150  C  CG2   . ILE   A 24  ? 0.2277 0.1426 0.2367 -0.0310 -0.0077 0.0119  21  ILE   A CG2   
151  C  CD1   . ILE   A 24  ? 0.2459 0.1542 0.2615 -0.0249 -0.0118 -0.0070 21  ILE   A CD1   
152  N  N     . GLN   A 25  ? 0.1851 0.1327 0.1837 -0.0241 -0.0013 0.0125  22  GLN   A N     
153  C  CA    . GLN   A 25  ? 0.1889 0.1438 0.1837 -0.0258 0.0012  0.0172  22  GLN   A CA    
154  C  C     . GLN   A 25  ? 0.1950 0.1494 0.1850 -0.0212 0.0003  0.0196  22  GLN   A C     
155  O  O     . GLN   A 25  ? 0.1957 0.1498 0.1814 -0.0227 0.0007  0.0250  22  GLN   A O     
156  C  CB    . GLN   A 25  ? 0.1882 0.1553 0.1842 -0.0258 0.0036  0.0137  22  GLN   A CB    
157  C  CG    . GLN   A 25  ? 0.2006 0.1730 0.2003 -0.0316 0.0055  0.0144  22  GLN   A CG    
158  C  CD    . GLN   A 25  ? 0.2116 0.1883 0.2090 -0.0356 0.0084  0.0201  22  GLN   A CD    
159  O  OE1   . GLN   A 25  ? 0.2359 0.2093 0.2277 -0.0349 0.0085  0.0248  22  GLN   A OE1   
160  N  NE2   . GLN   A 25  ? 0.2068 0.1922 0.2084 -0.0399 0.0108  0.0198  22  GLN   A NE2   
161  N  N     . LEU   A 26  ? 0.1920 0.1475 0.1828 -0.0161 -0.0009 0.0155  23  LEU   A N     
162  C  CA    . LEU   A 26  ? 0.1872 0.1435 0.1748 -0.0121 -0.0023 0.0171  23  LEU   A CA    
163  C  C     . LEU   A 26  ? 0.2104 0.1573 0.1961 -0.0115 -0.0052 0.0225  23  LEU   A C     
164  O  O     . LEU   A 26  ? 0.2159 0.1644 0.1967 -0.0108 -0.0061 0.0267  23  LEU   A O     
165  C  CB    . LEU   A 26  ? 0.1858 0.1443 0.1765 -0.0075 -0.0031 0.0119  23  LEU   A CB    
166  C  CG    . LEU   A 26  ? 0.1992 0.1597 0.1886 -0.0037 -0.0049 0.0127  23  LEU   A CG    
167  C  CD1   . LEU   A 26  ? 0.2051 0.1738 0.1914 -0.0043 -0.0034 0.0125  23  LEU   A CD1   
168  C  CD2   . LEU   A 26  ? 0.1893 0.1503 0.1835 0.0005  -0.0059 0.0086  23  LEU   A CD2   
169  N  N     . ILE   A 27  ? 0.2176 0.1550 0.2073 -0.0111 -0.0071 0.0216  24  ILE   A N     
170  C  CA    . ILE   A 27  ? 0.2414 0.1677 0.2311 -0.0093 -0.0107 0.0263  24  ILE   A CA    
171  C  C     . ILE   A 27  ? 0.2529 0.1726 0.2397 -0.0148 -0.0106 0.0341  24  ILE   A C     
172  O  O     . ILE   A 27  ? 0.2703 0.1857 0.2531 -0.0138 -0.0128 0.0407  24  ILE   A O     
173  C  CB    . ILE   A 27  ? 0.2439 0.1620 0.2402 -0.0061 -0.0128 0.0211  24  ILE   A CB    
174  C  CG1   . ILE   A 27  ? 0.2379 0.1637 0.2371 -0.0011 -0.0122 0.0139  24  ILE   A CG1   
175  C  CG2   . ILE   A 27  ? 0.2666 0.1724 0.2642 -0.0032 -0.0169 0.0256  24  ILE   A CG2   
176  C  CD1   . ILE   A 27  ? 0.2362 0.1656 0.2348 0.0038  -0.0141 0.0155  24  ILE   A CD1   
177  N  N     . GLN   A 28  ? 0.2614 0.1804 0.2508 -0.0206 -0.0084 0.0332  25  GLN   A N     
178  C  CA    . GLN   A 28  ? 0.2777 0.1893 0.2662 -0.0269 -0.0081 0.0409  25  GLN   A CA    
179  C  C     . GLN   A 28  ? 0.2889 0.2110 0.2741 -0.0332 -0.0037 0.0443  25  GLN   A C     
180  O  O     . GLN   A 28  ? 0.2867 0.2041 0.2710 -0.0390 -0.0029 0.0515  25  GLN   A O     
181  C  CB    . GLN   A 28  ? 0.2944 0.1938 0.2903 -0.0292 -0.0100 0.0381  25  GLN   A CB    
182  C  CG    . GLN   A 28  ? 0.3002 0.1894 0.2996 -0.0223 -0.0142 0.0342  25  GLN   A CG    
183  C  CD    . GLN   A 28  ? 0.3243 0.2025 0.3312 -0.0238 -0.0160 0.0287  25  GLN   A CD    
184  O  OE1   . GLN   A 28  ? 0.3392 0.2159 0.3487 -0.0307 -0.0148 0.0288  25  GLN   A OE1   
185  N  NE2   . GLN   A 28  ? 0.3440 0.2151 0.3547 -0.0172 -0.0190 0.0232  25  GLN   A NE2   
186  N  N     . ASN   A 29  ? 0.2784 0.2141 0.2624 -0.0320 -0.0008 0.0395  26  ASN   A N     
187  C  CA    . ASN   A 29  ? 0.2883 0.2357 0.2696 -0.0368 0.0037  0.0420  26  ASN   A CA    
188  C  C     . ASN   A 29  ? 0.2939 0.2413 0.2810 -0.0444 0.0058  0.0432  26  ASN   A C     
189  O  O     . ASN   A 29  ? 0.3132 0.2627 0.2980 -0.0499 0.0083  0.0499  26  ASN   A O     
190  C  CB    . ASN   A 29  ? 0.3196 0.2701 0.2918 -0.0368 0.0045  0.0493  26  ASN   A CB    
191  C  CG    . ASN   A 29  ? 0.3365 0.3013 0.3054 -0.0403 0.0096  0.0502  26  ASN   A CG    
192  O  OD1   . ASN   A 29  ? 0.3591 0.3337 0.3315 -0.0394 0.0119  0.0437  26  ASN   A OD1   
193  N  ND2   . ASN   A 29  ? 0.3810 0.3476 0.3428 -0.0439 0.0114  0.0583  26  ASN   A ND2   
194  N  N     . HIS   A 30  ? 0.2599 0.2051 0.2542 -0.0447 0.0045  0.0367  27  HIS   A N     
195  C  CA    . HIS   A 30  ? 0.2454 0.1933 0.2470 -0.0518 0.0060  0.0355  27  HIS   A CA    
196  C  C     . HIS   A 30  ? 0.2235 0.1761 0.2302 -0.0492 0.0047  0.0260  27  HIS   A C     
197  O  O     . HIS   A 30  ? 0.2103 0.1596 0.2154 -0.0431 0.0026  0.0219  27  HIS   A O     
198  C  CB    . HIS   A 30  ? 0.2464 0.1807 0.2512 -0.0578 0.0043  0.0408  27  HIS   A CB    
199  C  CG    . HIS   A 30  ? 0.2446 0.1637 0.2522 -0.0544 -0.0005 0.0371  27  HIS   A CG    
200  N  ND1   . HIS   A 30  ? 0.2570 0.1712 0.2721 -0.0570 -0.0026 0.0309  27  HIS   A ND1   
201  C  CD2   . HIS   A 30  ? 0.2544 0.1631 0.2589 -0.0482 -0.0037 0.0379  27  HIS   A CD2   
202  C  CE1   . HIS   A 30  ? 0.2694 0.1708 0.2855 -0.0522 -0.0064 0.0273  27  HIS   A CE1   
203  N  NE2   . HIS   A 30  ? 0.2628 0.1608 0.2730 -0.0467 -0.0071 0.0318  27  HIS   A NE2   
204  N  N     . PHE   A 31  ? 0.2181 0.1781 0.2312 -0.0542 0.0059  0.0234  28  PHE   A N     
205  C  CA    . PHE   A 31  ? 0.2183 0.1844 0.2356 -0.0521 0.0044  0.0152  28  PHE   A CA    
206  C  C     . PHE   A 31  ? 0.2419 0.1992 0.2653 -0.0562 0.0011  0.0116  28  PHE   A C     
207  O  O     . PHE   A 31  ? 0.2505 0.2071 0.2793 -0.0639 0.0016  0.0142  28  PHE   A O     
208  C  CB    . PHE   A 31  ? 0.2072 0.1901 0.2283 -0.0542 0.0073  0.0141  28  PHE   A CB    
209  C  CG    . PHE   A 31  ? 0.2031 0.1933 0.2287 -0.0524 0.0052  0.0069  28  PHE   A CG    
210  C  CD1   . PHE   A 31  ? 0.1820 0.1706 0.2039 -0.0456 0.0031  0.0024  28  PHE   A CD1   
211  C  CD2   . PHE   A 31  ? 0.1914 0.1911 0.2249 -0.0578 0.0053  0.0050  28  PHE   A CD2   
212  C  CE1   . PHE   A 31  ? 0.1812 0.1769 0.2058 -0.0441 0.0010  -0.0032 28  PHE   A CE1   
213  C  CE2   . PHE   A 31  ? 0.1900 0.1972 0.2270 -0.0559 0.0026  -0.0013 28  PHE   A CE2   
214  C  CZ    . PHE   A 31  ? 0.1748 0.1797 0.2066 -0.0489 0.0004  -0.0050 28  PHE   A CZ    
215  N  N     . VAL   A 32  ? 0.2556 0.2068 0.2783 -0.0516 -0.0021 0.0052  29  VAL   A N     
216  C  CA    . VAL   A 32  ? 0.2799 0.2229 0.3082 -0.0550 -0.0056 -0.0002 29  VAL   A CA    
217  C  C     . VAL   A 32  ? 0.2963 0.2516 0.3282 -0.0561 -0.0066 -0.0070 29  VAL   A C     
218  O  O     . VAL   A 32  ? 0.2900 0.2538 0.3184 -0.0508 -0.0064 -0.0100 29  VAL   A O     
219  C  CB    . VAL   A 32  ? 0.2886 0.2180 0.3148 -0.0497 -0.0086 -0.0042 29  VAL   A CB    
220  C  CG1   . VAL   A 32  ? 0.2978 0.2138 0.3225 -0.0497 -0.0088 0.0030  29  VAL   A CG1   
221  C  CG2   . VAL   A 32  ? 0.2852 0.2209 0.3060 -0.0415 -0.0083 -0.0082 29  VAL   A CG2   
222  N  N     . ASP   A 33  ? 0.3402 0.2957 0.3796 -0.0635 -0.0081 -0.0090 30  ASP   A N     
223  C  CA    . ASP   A 33  ? 0.3528 0.3214 0.3967 -0.0654 -0.0099 -0.0153 30  ASP   A CA    
224  C  C     . ASP   A 33  ? 0.3586 0.3221 0.4028 -0.0641 -0.0146 -0.0249 30  ASP   A C     
225  O  O     . ASP   A 33  ? 0.3658 0.3407 0.4102 -0.0628 -0.0164 -0.0302 30  ASP   A O     
226  C  CB    . ASP   A 33  ? 0.4188 0.3919 0.4722 -0.0751 -0.0095 -0.0133 30  ASP   A CB    
227  C  CG    . ASP   A 33  ? 0.4325 0.4154 0.4866 -0.0772 -0.0045 -0.0052 30  ASP   A CG    
228  O  OD1   . ASP   A 33  ? 0.4216 0.4173 0.4736 -0.0725 -0.0028 -0.0055 30  ASP   A OD1   
229  O  OD2   . ASP   A 33  ? 0.4828 0.4592 0.5388 -0.0829 -0.0022 0.0016  30  ASP   A OD2   
230  N  N     . GLU   A 34  ? 0.3655 0.3128 0.4106 -0.0652 -0.0167 -0.0272 31  GLU   A N     
231  C  CA    . GLU   A 34  ? 0.3871 0.3311 0.4330 -0.0644 -0.0212 -0.0380 31  GLU   A CA    
232  C  C     . GLU   A 34  ? 0.3530 0.2828 0.3942 -0.0580 -0.0221 -0.0414 31  GLU   A C     
233  O  O     . GLU   A 34  ? 0.3410 0.2600 0.3853 -0.0593 -0.0255 -0.0486 31  GLU   A O     
234  C  CB    . GLU   A 34  ? 0.4617 0.4009 0.5175 -0.0741 -0.0242 -0.0409 31  GLU   A CB    
235  C  CG    . GLU   A 34  ? 0.5128 0.4690 0.5750 -0.0802 -0.0239 -0.0398 31  GLU   A CG    
236  C  CD    . GLU   A 34  ? 0.5557 0.5106 0.6295 -0.0910 -0.0265 -0.0420 31  GLU   A CD    
237  O  OE1   . GLU   A 34  ? 0.5827 0.5244 0.6612 -0.0969 -0.0255 -0.0366 31  GLU   A OE1   
238  O  OE2   . GLU   A 34  ? 0.5928 0.5604 0.6710 -0.0936 -0.0297 -0.0488 31  GLU   A OE2   
239  N  N     . TYR   A 35  ? 0.3094 0.2408 0.3437 -0.0507 -0.0195 -0.0379 32  TYR   A N     
240  C  CA    . TYR   A 35  ? 0.3140 0.2327 0.3455 -0.0446 -0.0199 -0.0397 32  TYR   A CA    
241  C  C     . TYR   A 35  ? 0.3136 0.2329 0.3428 -0.0402 -0.0223 -0.0513 32  TYR   A C     
242  O  O     . TYR   A 35  ? 0.3010 0.2335 0.3251 -0.0370 -0.0216 -0.0546 32  TYR   A O     
243  C  CB    . TYR   A 35  ? 0.2970 0.2191 0.3227 -0.0385 -0.0166 -0.0329 32  TYR   A CB    
244  C  CG    . TYR   A 35  ? 0.2960 0.2040 0.3216 -0.0341 -0.0171 -0.0308 32  TYR   A CG    
245  C  CD1   . TYR   A 35  ? 0.3127 0.2077 0.3420 -0.0380 -0.0179 -0.0241 32  TYR   A CD1   
246  C  CD2   . TYR   A 35  ? 0.2920 0.2003 0.3142 -0.0261 -0.0168 -0.0351 32  TYR   A CD2   
247  C  CE1   . TYR   A 35  ? 0.3281 0.2102 0.3577 -0.0333 -0.0191 -0.0216 32  TYR   A CE1   
248  C  CE2   . TYR   A 35  ? 0.3071 0.2040 0.3305 -0.0214 -0.0176 -0.0335 32  TYR   A CE2   
249  C  CZ    . TYR   A 35  ? 0.3296 0.2130 0.3566 -0.0247 -0.0192 -0.0267 32  TYR   A CZ    
250  O  OH    . TYR   A 35  ? 0.3460 0.2180 0.3744 -0.0192 -0.0208 -0.0247 32  TYR   A OH    
251  N  N     . ASP   A 36  ? 0.3220 0.2268 0.3550 -0.0401 -0.0252 -0.0574 33  ASP   A N     
252  C  CA    . ASP   A 36  ? 0.3366 0.2412 0.3675 -0.0357 -0.0274 -0.0699 33  ASP   A CA    
253  C  C     . ASP   A 36  ? 0.3222 0.2393 0.3447 -0.0279 -0.0243 -0.0705 33  ASP   A C     
254  O  O     . ASP   A 36  ? 0.3203 0.2354 0.3411 -0.0230 -0.0217 -0.0647 33  ASP   A O     
255  C  CB    . ASP   A 36  ? 0.3574 0.2425 0.3932 -0.0334 -0.0298 -0.0747 33  ASP   A CB    
256  C  CG    . ASP   A 36  ? 0.3722 0.2569 0.4064 -0.0288 -0.0320 -0.0895 33  ASP   A CG    
257  O  OD1   . ASP   A 36  ? 0.3616 0.2616 0.3885 -0.0251 -0.0306 -0.0949 33  ASP   A OD1   
258  O  OD2   . ASP   A 36  ? 0.3885 0.2569 0.4288 -0.0288 -0.0352 -0.0958 33  ASP   A OD2   
259  N  N     . PRO   A 37  ? 0.3163 0.2469 0.3336 -0.0271 -0.0248 -0.0770 34  PRO   A N     
260  C  CA    . PRO   A 37  ? 0.3056 0.2492 0.3149 -0.0210 -0.0215 -0.0757 34  PRO   A CA    
261  C  C     . PRO   A 37  ? 0.3204 0.2618 0.3265 -0.0136 -0.0201 -0.0824 34  PRO   A C     
262  O  O     . PRO   A 37  ? 0.3172 0.2689 0.3175 -0.0089 -0.0169 -0.0806 34  PRO   A O     
263  C  CB    . PRO   A 37  ? 0.3057 0.2638 0.3105 -0.0233 -0.0232 -0.0796 34  PRO   A CB    
264  C  CG    . PRO   A 37  ? 0.3334 0.2855 0.3431 -0.0284 -0.0278 -0.0882 34  PRO   A CG    
265  C  CD    . PRO   A 37  ? 0.3298 0.2662 0.3486 -0.0329 -0.0283 -0.0833 34  PRO   A CD    
266  N  N     . THR   A 38  ? 0.3178 0.2461 0.3287 -0.0124 -0.0224 -0.0901 35  THR   A N     
267  C  CA    . THR   A 38  ? 0.3253 0.2518 0.3348 -0.0046 -0.0210 -0.0976 35  THR   A CA    
268  C  C     . THR   A 38  ? 0.3210 0.2366 0.3358 -0.0003 -0.0197 -0.0916 35  THR   A C     
269  O  O     . THR   A 38  ? 0.3291 0.2442 0.3445 0.0069  -0.0183 -0.0969 35  THR   A O     
270  C  CB    . THR   A 38  ? 0.3454 0.2653 0.3568 -0.0044 -0.0246 -0.1120 35  THR   A CB    
271  O  OG1   . THR   A 38  ? 0.3618 0.2621 0.3825 -0.0078 -0.0282 -0.1122 35  THR   A OG1   
272  C  CG2   . THR   A 38  ? 0.3544 0.2857 0.3605 -0.0092 -0.0268 -0.1174 35  THR   A CG2   
273  N  N     . ILE   A 39  ? 0.3047 0.2126 0.3235 -0.0044 -0.0203 -0.0808 36  ILE   A N     
274  C  CA    . ILE   A 39  ? 0.3025 0.1993 0.3259 -0.0006 -0.0203 -0.0748 36  ILE   A CA    
275  C  C     . ILE   A 39  ? 0.2824 0.1913 0.3018 0.0040  -0.0163 -0.0688 36  ILE   A C     
276  O  O     . ILE   A 39  ? 0.2680 0.1874 0.2831 0.0010  -0.0143 -0.0621 36  ILE   A O     
277  C  CB    . ILE   A 39  ? 0.3097 0.1941 0.3376 -0.0068 -0.0223 -0.0650 36  ILE   A CB    
278  C  CG1   . ILE   A 39  ? 0.3248 0.1957 0.3584 -0.0121 -0.0263 -0.0707 36  ILE   A CG1   
279  C  CG2   . ILE   A 39  ? 0.3171 0.1920 0.3480 -0.0024 -0.0225 -0.0575 36  ILE   A CG2   
280  C  CD1   . ILE   A 39  ? 0.3334 0.1910 0.3722 -0.0186 -0.0280 -0.0606 36  ILE   A CD1   
281  N  N     . GLU   A 40  ? 0.2782 0.1858 0.2999 0.0115  -0.0155 -0.0718 37  GLU   A N     
282  C  CA    . GLU   A 40  ? 0.2703 0.1898 0.2898 0.0159  -0.0119 -0.0673 37  GLU   A CA    
283  C  C     . GLU   A 40  ? 0.2728 0.1829 0.2983 0.0203  -0.0135 -0.0624 37  GLU   A C     
284  O  O     . GLU   A 40  ? 0.2934 0.1964 0.3241 0.0258  -0.0150 -0.0689 37  GLU   A O     
285  C  CB    . GLU   A 40  ? 0.2741 0.2058 0.2910 0.0211  -0.0090 -0.0765 37  GLU   A CB    
286  C  CG    . GLU   A 40  ? 0.2717 0.2168 0.2871 0.0243  -0.0050 -0.0721 37  GLU   A CG    
287  C  CD    . GLU   A 40  ? 0.2814 0.2409 0.2924 0.0274  -0.0012 -0.0797 37  GLU   A CD    
288  O  OE1   . GLU   A 40  ? 0.2708 0.2391 0.2747 0.0237  0.0000  -0.0795 37  GLU   A OE1   
289  O  OE2   . GLU   A 40  ? 0.3122 0.2742 0.3273 0.0338  0.0003  -0.0858 37  GLU   A OE2   
290  N  N     . ASP   A 41  ? 0.2625 0.1730 0.2871 0.0179  -0.0134 -0.0517 38  ASP   A N     
291  C  CA    . ASP   A 41  ? 0.2750 0.1768 0.3042 0.0216  -0.0157 -0.0457 38  ASP   A CA    
292  C  C     . ASP   A 41  ? 0.2495 0.1627 0.2765 0.0228  -0.0135 -0.0387 38  ASP   A C     
293  O  O     . ASP   A 41  ? 0.2416 0.1657 0.2637 0.0193  -0.0107 -0.0369 38  ASP   A O     
294  C  CB    . ASP   A 41  ? 0.3046 0.1924 0.3343 0.0163  -0.0188 -0.0376 38  ASP   A CB    
295  C  CG    . ASP   A 41  ? 0.3500 0.2197 0.3852 0.0160  -0.0227 -0.0410 38  ASP   A CG    
296  O  OD1   . ASP   A 41  ? 0.3654 0.2289 0.4062 0.0231  -0.0245 -0.0470 38  ASP   A OD1   
297  O  OD2   . ASP   A 41  ? 0.3832 0.2453 0.4180 0.0087  -0.0239 -0.0379 38  ASP   A OD2   
298  N  N     . SER   A 42  ? 0.2465 0.1568 0.2778 0.0280  -0.0154 -0.0356 39  SER   A N     
299  C  CA    . SER   A 42  ? 0.2314 0.1513 0.2615 0.0289  -0.0145 -0.0290 39  SER   A CA    
300  C  C     . SER   A 42  ? 0.2447 0.1548 0.2735 0.0267  -0.0180 -0.0192 39  SER   A C     
301  O  O     . SER   A 42  ? 0.2542 0.1504 0.2855 0.0274  -0.0214 -0.0176 39  SER   A O     
302  C  CB    . SER   A 42  ? 0.2366 0.1645 0.2726 0.0362  -0.0140 -0.0329 39  SER   A CB    
303  O  OG    . SER   A 42  ? 0.2646 0.1819 0.3073 0.0421  -0.0181 -0.0336 39  SER   A OG    
304  N  N     . TYR   A 43  ? 0.2310 0.1487 0.2555 0.0241  -0.0171 -0.0129 40  TYR   A N     
305  C  CA    . TYR   A 43  ? 0.2471 0.1591 0.2681 0.0217  -0.0197 -0.0034 40  TYR   A CA    
306  C  C     . TYR   A 43  ? 0.2382 0.1598 0.2592 0.0249  -0.0204 -0.0004 40  TYR   A C     
307  O  O     . TYR   A 43  ? 0.2228 0.1567 0.2440 0.0250  -0.0176 -0.0036 40  TYR   A O     
308  C  CB    . TYR   A 43  ? 0.2477 0.1616 0.2622 0.0139  -0.0173 0.0004  40  TYR   A CB    
309  C  CG    . TYR   A 43  ? 0.2695 0.1752 0.2846 0.0096  -0.0169 -0.0022 40  TYR   A CG    
310  C  CD1   . TYR   A 43  ? 0.2669 0.1783 0.2824 0.0084  -0.0144 -0.0098 40  TYR   A CD1   
311  C  CD2   . TYR   A 43  ? 0.3093 0.2020 0.3244 0.0062  -0.0193 0.0033  40  TYR   A CD2   
312  C  CE1   . TYR   A 43  ? 0.3008 0.2056 0.3173 0.0041  -0.0148 -0.0129 40  TYR   A CE1   
313  C  CE2   . TYR   A 43  ? 0.3351 0.2203 0.3521 0.0014  -0.0193 0.0005  40  TYR   A CE2   
314  C  CZ    . TYR   A 43  ? 0.3354 0.2271 0.3532 0.0004  -0.0172 -0.0080 40  TYR   A CZ    
315  O  OH    . TYR   A 43  ? 0.3845 0.2696 0.4045 -0.0047 -0.0178 -0.0114 40  TYR   A OH    
316  N  N     . ARG   A 44  ? 0.2618 0.1779 0.2828 0.0274  -0.0246 0.0059  41  ARG   A N     
317  C  CA    . ARG   A 44  ? 0.2844 0.2101 0.3046 0.0296  -0.0261 0.0091  41  ARG   A CA    
318  C  C     . ARG   A 44  ? 0.2871 0.2125 0.2982 0.0244  -0.0266 0.0170  41  ARG   A C     
319  O  O     . ARG   A 44  ? 0.3091 0.2244 0.3162 0.0211  -0.0275 0.0225  41  ARG   A O     
320  C  CB    . ARG   A 44  ? 0.3353 0.2586 0.3623 0.0373  -0.0311 0.0097  41  ARG   A CB    
321  C  CG    . ARG   A 44  ? 0.3798 0.3068 0.4165 0.0432  -0.0299 0.0007  41  ARG   A CG    
322  C  CD    . ARG   A 44  ? 0.4531 0.3846 0.4984 0.0514  -0.0341 0.0002  41  ARG   A CD    
323  N  NE    . ARG   A 44  ? 0.4938 0.4426 0.5441 0.0527  -0.0311 -0.0052 41  ARG   A NE    
324  C  CZ    . ARG   A 44  ? 0.4829 0.4411 0.5427 0.0591  -0.0334 -0.0075 41  ARG   A CZ    
325  N  NH1   . ARG   A 44  ? 0.4709 0.4451 0.5351 0.0584  -0.0298 -0.0119 41  ARG   A NH1   
326  N  NH2   . ARG   A 44  ? 0.4454 0.3974 0.5108 0.0660  -0.0393 -0.0051 41  ARG   A NH2   
327  N  N     . LYS   A 45  ? 0.2639 0.2009 0.2721 0.0232  -0.0256 0.0171  42  LYS   A N     
328  C  CA    . LYS   A 45  ? 0.2781 0.2169 0.2774 0.0192  -0.0259 0.0234  42  LYS   A CA    
329  C  C     . LYS   A 45  ? 0.2591 0.2089 0.2578 0.0213  -0.0279 0.0230  42  LYS   A C     
330  O  O     . LYS   A 45  ? 0.2086 0.1673 0.2119 0.0220  -0.0260 0.0173  42  LYS   A O     
331  C  CB    . LYS   A 45  ? 0.3137 0.2552 0.3086 0.0129  -0.0210 0.0222  42  LYS   A CB    
332  C  CG    . LYS   A 45  ? 0.3492 0.2948 0.3353 0.0092  -0.0205 0.0272  42  LYS   A CG    
333  C  CD    . LYS   A 45  ? 0.3740 0.3190 0.3561 0.0032  -0.0163 0.0282  42  LYS   A CD    
334  C  CE    . LYS   A 45  ? 0.4009 0.3469 0.3741 0.0000  -0.0164 0.0352  42  LYS   A CE    
335  N  NZ    . LYS   A 45  ? 0.4249 0.3798 0.3946 -0.0039 -0.0120 0.0330  42  LYS   A NZ    
336  N  N     . GLN   A 46  ? 0.2545 0.2039 0.2469 0.0216  -0.0316 0.0293  43  GLN   A N     
337  C  CA    . GLN   A 46  ? 0.2414 0.2018 0.2324 0.0232  -0.0343 0.0285  43  GLN   A CA    
338  C  C     . GLN   A 46  ? 0.2278 0.1935 0.2094 0.0180  -0.0316 0.0292  43  GLN   A C     
339  O  O     . GLN   A 46  ? 0.2339 0.1951 0.2075 0.0149  -0.0308 0.0348  43  GLN   A O     
340  C  CB    . GLN   A 46  ? 0.2658 0.2238 0.2556 0.0279  -0.0410 0.0344  43  GLN   A CB    
341  C  CG    . GLN   A 46  ? 0.2835 0.2530 0.2707 0.0291  -0.0448 0.0339  43  GLN   A CG    
342  C  CD    . GLN   A 46  ? 0.3187 0.2861 0.3064 0.0349  -0.0522 0.0396  43  GLN   A CD    
343  O  OE1   . GLN   A 46  ? 0.3823 0.3507 0.3806 0.0404  -0.0553 0.0372  43  GLN   A OE1   
344  N  NE2   . GLN   A 46  ? 0.3418 0.3072 0.3182 0.0337  -0.0552 0.0472  43  GLN   A NE2   
345  N  N     . VAL   A 47  ? 0.2040 0.1794 0.1876 0.0169  -0.0300 0.0234  44  VAL   A N     
346  C  CA    . VAL   A 47  ? 0.2023 0.1833 0.1790 0.0128  -0.0272 0.0218  44  VAL   A CA    
347  C  C     . VAL   A 47  ? 0.1926 0.1834 0.1707 0.0139  -0.0300 0.0173  44  VAL   A C     
348  O  O     . VAL   A 47  ? 0.1937 0.1881 0.1801 0.0170  -0.0329 0.0148  44  VAL   A O     
349  C  CB    . VAL   A 47  ? 0.2047 0.1850 0.1841 0.0096  -0.0214 0.0178  44  VAL   A CB    
350  C  CG1   . VAL   A 47  ? 0.2343 0.2059 0.2130 0.0079  -0.0191 0.0212  44  VAL   A CG1   
351  C  CG2   . VAL   A 47  ? 0.2111 0.1949 0.2004 0.0110  -0.0204 0.0121  44  VAL   A CG2   
352  N  N     . VAL   A 48  ? 0.1920 0.1878 0.1627 0.0114  -0.0292 0.0158  45  VAL   A N     
353  C  CA    . VAL   A 48  ? 0.1905 0.1951 0.1629 0.0116  -0.0319 0.0102  45  VAL   A CA    
354  C  C     . VAL   A 48  ? 0.1783 0.1845 0.1540 0.0087  -0.0272 0.0042  45  VAL   A C     
355  O  O     . VAL   A 48  ? 0.1681 0.1730 0.1378 0.0064  -0.0234 0.0043  45  VAL   A O     
356  C  CB    . VAL   A 48  ? 0.2147 0.2245 0.1760 0.0117  -0.0356 0.0118  45  VAL   A CB    
357  C  CG1   . VAL   A 48  ? 0.2169 0.2354 0.1806 0.0114  -0.0384 0.0043  45  VAL   A CG1   
358  C  CG2   . VAL   A 48  ? 0.2296 0.2379 0.1876 0.0152  -0.0412 0.0187  45  VAL   A CG2   
359  N  N     . ILE   A 49  ? 0.1634 0.1723 0.1493 0.0088  -0.0274 -0.0005 46  ILE   A N     
360  C  CA    . ILE   A 49  ? 0.1522 0.1617 0.1429 0.0062  -0.0238 -0.0055 46  ILE   A CA    
361  C  C     . ILE   A 49  ? 0.1476 0.1634 0.1438 0.0056  -0.0273 -0.0110 46  ILE   A C     
362  O  O     . ILE   A 49  ? 0.1351 0.1546 0.1391 0.0067  -0.0301 -0.0113 46  ILE   A O     
363  C  CB    . ILE   A 49  ? 0.1566 0.1625 0.1550 0.0060  -0.0201 -0.0048 46  ILE   A CB    
364  C  CG1   . ILE   A 49  ? 0.1591 0.1587 0.1531 0.0064  -0.0176 -0.0003 46  ILE   A CG1   
365  C  CG2   . ILE   A 49  ? 0.1567 0.1623 0.1593 0.0034  -0.0166 -0.0084 46  ILE   A CG2   
366  C  CD1   . ILE   A 49  ? 0.1505 0.1476 0.1514 0.0074  -0.0156 0.0002  46  ILE   A CD1   
367  N  N     . ASP   A 50  ? 0.1438 0.1613 0.1367 0.0038  -0.0272 -0.0157 47  ASP   A N     
368  C  CA    . ASP   A 50  ? 0.1436 0.1662 0.1420 0.0024  -0.0309 -0.0221 47  ASP   A CA    
369  C  C     . ASP   A 50  ? 0.1460 0.1756 0.1440 0.0041  -0.0374 -0.0222 47  ASP   A C     
370  O  O     . ASP   A 50  ? 0.1378 0.1726 0.1455 0.0033  -0.0407 -0.0255 47  ASP   A O     
371  C  CB    . ASP   A 50  ? 0.1427 0.1640 0.1541 0.0000  -0.0288 -0.0243 47  ASP   A CB    
372  C  CG    . ASP   A 50  ? 0.1392 0.1536 0.1509 -0.0013 -0.0232 -0.0238 47  ASP   A CG    
373  O  OD1   . ASP   A 50  ? 0.1555 0.1678 0.1629 -0.0018 -0.0221 -0.0273 47  ASP   A OD1   
374  O  OD2   . ASP   A 50  ? 0.1311 0.1431 0.1473 -0.0015 -0.0200 -0.0203 47  ASP   A OD2   
375  N  N     . GLY   A 51  ? 0.1505 0.1808 0.1377 0.0065  -0.0394 -0.0178 48  GLY   A N     
376  C  CA    . GLY   A 51  ? 0.1617 0.1987 0.1464 0.0088  -0.0463 -0.0167 48  GLY   A CA    
377  C  C     . GLY   A 51  ? 0.1614 0.1989 0.1541 0.0118  -0.0486 -0.0120 48  GLY   A C     
378  O  O     . GLY   A 51  ? 0.1701 0.2131 0.1615 0.0145  -0.0547 -0.0104 48  GLY   A O     
379  N  N     . GLU   A 52  ? 0.1567 0.1887 0.1564 0.0119  -0.0438 -0.0099 49  GLU   A N     
380  C  CA    . GLU   A 52  ? 0.1594 0.1920 0.1678 0.0153  -0.0452 -0.0067 49  GLU   A CA    
381  C  C     . GLU   A 52  ? 0.1557 0.1796 0.1577 0.0179  -0.0435 0.0002  49  GLU   A C     
382  O  O     . GLU   A 52  ? 0.1485 0.1659 0.1467 0.0158  -0.0384 0.0012  49  GLU   A O     
383  C  CB    . GLU   A 52  ? 0.1530 0.1864 0.1740 0.0136  -0.0408 -0.0097 49  GLU   A CB    
384  C  CG    . GLU   A 52  ? 0.1572 0.1946 0.1892 0.0172  -0.0419 -0.0086 49  GLU   A CG    
385  C  CD    . GLU   A 52  ? 0.1508 0.1910 0.1941 0.0148  -0.0369 -0.0115 49  GLU   A CD    
386  O  OE1   . GLU   A 52  ? 0.1500 0.1843 0.1902 0.0119  -0.0316 -0.0115 49  GLU   A OE1   
387  O  OE2   . GLU   A 52  ? 0.1562 0.2051 0.2109 0.0156  -0.0383 -0.0136 49  GLU   A OE2   
388  N  N     . THR   A 53  ? 0.1653 0.1894 0.1669 0.0223  -0.0485 0.0047  50  THR   A N     
389  C  CA    . THR   A 53  ? 0.1755 0.1896 0.1737 0.0247  -0.0473 0.0111  50  THR   A CA    
390  C  C     . THR   A 53  ? 0.1601 0.1719 0.1698 0.0260  -0.0435 0.0087  50  THR   A C     
391  O  O     . THR   A 53  ? 0.1612 0.1795 0.1813 0.0288  -0.0458 0.0062  50  THR   A O     
392  C  CB    . THR   A 53  ? 0.1897 0.2035 0.1848 0.0295  -0.0544 0.0169  50  THR   A CB    
393  O  OG1   . THR   A 53  ? 0.1974 0.2153 0.1806 0.0278  -0.0573 0.0184  50  THR   A OG1   
394  C  CG2   . THR   A 53  ? 0.2002 0.2021 0.1932 0.0319  -0.0537 0.0236  50  THR   A CG2   
395  N  N     . CYS   A 54  ? 0.1634 0.1676 0.1710 0.0236  -0.0378 0.0092  51  CYS   A N     
396  C  CA    . CYS   A 54  ? 0.1629 0.1659 0.1796 0.0243  -0.0336 0.0062  51  CYS   A CA    
397  C  C     . CYS   A 54  ? 0.1648 0.1572 0.1801 0.0269  -0.0332 0.0098  51  CYS   A C     
398  O  O     . CYS   A 54  ? 0.1728 0.1577 0.1792 0.0250  -0.0328 0.0140  51  CYS   A O     
399  C  CB    . CYS   A 54  ? 0.1570 0.1599 0.1725 0.0194  -0.0277 0.0031  51  CYS   A CB    
400  S  SG    . CYS   A 54  ? 0.1669 0.1784 0.1840 0.0155  -0.0277 -0.0013 51  CYS   A SG    
401  N  N     . LEU   A 55  ? 0.1613 0.1538 0.1859 0.0311  -0.0332 0.0076  52  LEU   A N     
402  C  CA    . LEU   A 55  ? 0.1778 0.1596 0.2027 0.0334  -0.0322 0.0088  52  LEU   A CA    
403  C  C     . LEU   A 55  ? 0.1765 0.1587 0.2039 0.0309  -0.0260 0.0038  52  LEU   A C     
404  O  O     . LEU   A 55  ? 0.1701 0.1603 0.2053 0.0324  -0.0241 -0.0007 52  LEU   A O     
405  C  CB    . LEU   A 55  ? 0.1919 0.1729 0.2251 0.0406  -0.0367 0.0089  52  LEU   A CB    
406  C  CG    . LEU   A 55  ? 0.2129 0.1811 0.2473 0.0434  -0.0365 0.0094  52  LEU   A CG    
407  C  CD1   . LEU   A 55  ? 0.2205 0.1762 0.2442 0.0396  -0.0371 0.0161  52  LEU   A CD1   
408  C  CD2   . LEU   A 55  ? 0.2247 0.1920 0.2682 0.0516  -0.0416 0.0093  52  LEU   A CD2   
409  N  N     . LEU   A 56  ? 0.1785 0.1531 0.1989 0.0269  -0.0231 0.0053  53  LEU   A N     
410  C  CA    . LEU   A 56  ? 0.1786 0.1533 0.1998 0.0245  -0.0180 0.0013  53  LEU   A CA    
411  C  C     . LEU   A 56  ? 0.1850 0.1516 0.2092 0.0276  -0.0181 -0.0007 53  LEU   A C     
412  O  O     . LEU   A 56  ? 0.1974 0.1536 0.2189 0.0281  -0.0207 0.0029  53  LEU   A O     
413  C  CB    . LEU   A 56  ? 0.1809 0.1527 0.1940 0.0188  -0.0153 0.0032  53  LEU   A CB    
414  C  CG    . LEU   A 56  ? 0.1843 0.1615 0.1930 0.0157  -0.0154 0.0049  53  LEU   A CG    
415  C  CD1   . LEU   A 56  ? 0.1824 0.1572 0.1852 0.0111  -0.0122 0.0058  53  LEU   A CD1   
416  C  CD2   . LEU   A 56  ? 0.1889 0.1758 0.2034 0.0160  -0.0146 0.0013  53  LEU   A CD2   
417  N  N     . ASP   A 57  ? 0.1757 0.1475 0.2057 0.0297  -0.0153 -0.0065 54  ASP   A N     
418  C  CA    . ASP   A 57  ? 0.1838 0.1485 0.2163 0.0324  -0.0147 -0.0105 54  ASP   A CA    
419  C  C     . ASP   A 57  ? 0.1684 0.1354 0.1970 0.0282  -0.0101 -0.0137 54  ASP   A C     
420  O  O     . ASP   A 57  ? 0.1628 0.1403 0.1930 0.0276  -0.0067 -0.0165 54  ASP   A O     
421  C  CB    . ASP   A 57  ? 0.2118 0.1821 0.2540 0.0393  -0.0153 -0.0154 54  ASP   A CB    
422  C  CG    . ASP   A 57  ? 0.2403 0.2002 0.2861 0.0440  -0.0169 -0.0192 54  ASP   A CG    
423  O  OD1   . ASP   A 57  ? 0.2696 0.2176 0.3106 0.0413  -0.0174 -0.0185 54  ASP   A OD1   
424  O  OD2   . ASP   A 57  ? 0.2755 0.2391 0.3300 0.0507  -0.0179 -0.0234 54  ASP   A OD2   
425  N  N     . ILE   A 58  ? 0.1594 0.1173 0.1831 0.0249  -0.0102 -0.0127 55  ILE   A N     
426  C  CA    . ILE   A 58  ? 0.1567 0.1175 0.1759 0.0204  -0.0067 -0.0148 55  ILE   A CA    
427  C  C     . ILE   A 58  ? 0.1613 0.1170 0.1813 0.0214  -0.0062 -0.0207 55  ILE   A C     
428  O  O     . ILE   A 58  ? 0.1677 0.1121 0.1884 0.0217  -0.0089 -0.0204 55  ILE   A O     
429  C  CB    . ILE   A 58  ? 0.1601 0.1174 0.1733 0.0149  -0.0069 -0.0095 55  ILE   A CB    
430  C  CG1   . ILE   A 58  ? 0.1618 0.1240 0.1734 0.0141  -0.0075 -0.0049 55  ILE   A CG1   
431  C  CG2   . ILE   A 58  ? 0.1536 0.1146 0.1635 0.0111  -0.0040 -0.0118 55  ILE   A CG2   
432  C  CD1   . ILE   A 58  ? 0.1668 0.1252 0.1728 0.0100  -0.0082 0.0003  55  ILE   A CD1   
433  N  N     . LEU   A 59  ? 0.1522 0.1161 0.1717 0.0216  -0.0029 -0.0259 56  LEU   A N     
434  C  CA    . LEU   A 59  ? 0.1700 0.1309 0.1889 0.0223  -0.0024 -0.0328 56  LEU   A CA    
435  C  C     . LEU   A 59  ? 0.1652 0.1274 0.1780 0.0168  -0.0013 -0.0327 56  LEU   A C     
436  O  O     . LEU   A 59  ? 0.1551 0.1270 0.1645 0.0150  0.0014  -0.0318 56  LEU   A O     
437  C  CB    . LEU   A 59  ? 0.1725 0.1431 0.1942 0.0269  0.0005  -0.0394 56  LEU   A CB    
438  C  CG    . LEU   A 59  ? 0.1857 0.1540 0.2065 0.0285  0.0009  -0.0482 56  LEU   A CG    
439  C  CD1   . LEU   A 59  ? 0.2023 0.1564 0.2284 0.0319  -0.0031 -0.0511 56  LEU   A CD1   
440  C  CD2   . LEU   A 59  ? 0.1874 0.1690 0.2089 0.0322  0.0051  -0.0544 56  LEU   A CD2   
441  N  N     . ASP   A 60  ? 0.1811 0.1333 0.1934 0.0142  -0.0037 -0.0335 57  ASP   A N     
442  C  CA    . ASP   A 60  ? 0.1873 0.1404 0.1954 0.0091  -0.0036 -0.0343 57  ASP   A CA    
443  C  C     . ASP   A 60  ? 0.2035 0.1587 0.2107 0.0106  -0.0033 -0.0433 57  ASP   A C     
444  O  O     . ASP   A 60  ? 0.2056 0.1515 0.2157 0.0117  -0.0055 -0.0486 57  ASP   A O     
445  C  CB    . ASP   A 60  ? 0.1910 0.1334 0.2001 0.0046  -0.0062 -0.0303 57  ASP   A CB    
446  C  CG    . ASP   A 60  ? 0.1930 0.1370 0.2000 -0.0007 -0.0066 -0.0323 57  ASP   A CG    
447  O  OD1   . ASP   A 60  ? 0.1857 0.1403 0.1891 -0.0011 -0.0049 -0.0339 57  ASP   A OD1   
448  O  OD2   . ASP   A 60  ? 0.2143 0.1492 0.2237 -0.0045 -0.0088 -0.0319 57  ASP   A OD2   
449  N  N     . THR   A 61  ? 0.2049 0.1723 0.2078 0.0109  -0.0005 -0.0451 58  THR   A N     
450  C  CA    . THR   A 61  ? 0.2233 0.1955 0.2237 0.0131  0.0004  -0.0539 58  THR   A CA    
451  C  C     . THR   A 61  ? 0.2349 0.2049 0.2322 0.0089  -0.0021 -0.0579 58  THR   A C     
452  O  O     . THR   A 61  ? 0.2304 0.2015 0.2260 0.0043  -0.0031 -0.0529 58  THR   A O     
453  C  CB    . THR   A 61  ? 0.2289 0.2158 0.2250 0.0149  0.0045  -0.0538 58  THR   A CB    
454  O  OG1   . THR   A 61  ? 0.2251 0.2186 0.2162 0.0109  0.0051  -0.0480 58  THR   A OG1   
455  C  CG2   . THR   A 61  ? 0.2214 0.2114 0.2226 0.0186  0.0068  -0.0506 58  THR   A CG2   
456  N  N     . ALA   A 62  ? 0.2663 0.2331 0.2638 0.0109  -0.0033 -0.0677 59  ALA   A N     
457  C  CA    . ALA   A 62  ? 0.2935 0.2588 0.2887 0.0070  -0.0063 -0.0735 59  ALA   A CA    
458  C  C     . ALA   A 62  ? 0.3013 0.2806 0.2884 0.0081  -0.0047 -0.0789 59  ALA   A C     
459  O  O     . ALA   A 62  ? 0.2890 0.2772 0.2712 0.0052  -0.0043 -0.0740 59  ALA   A O     
460  C  CB    . ALA   A 62  ? 0.3158 0.2671 0.3167 0.0078  -0.0095 -0.0815 59  ALA   A CB    
461  N  N     . GLY   A 63  ? 0.3342 0.3159 0.3197 0.0126  -0.0036 -0.0888 60  GLY   A N     
462  C  CA    . GLY   A 63  ? 0.3598 0.3560 0.3359 0.0134  -0.0019 -0.0940 60  GLY   A CA    
463  C  C     . GLY   A 63  ? 0.3702 0.3797 0.3412 0.0143  0.0026  -0.0858 60  GLY   A C     
464  O  O     . GLY   A 63  ? 0.3590 0.3684 0.3343 0.0171  0.0057  -0.0819 60  GLY   A O     
465  N  N     . GLN   A 64  ? 0.3642 0.3847 0.3265 0.0119  0.0026  -0.0834 61  GLN   A N     
466  C  CA    . GLN   A 64  ? 0.3667 0.3987 0.3245 0.0124  0.0068  -0.0746 61  GLN   A CA    
467  C  C     . GLN   A 64  ? 0.4068 0.4529 0.3548 0.0149  0.0100  -0.0801 61  GLN   A C     
468  O  O     . GLN   A 64  ? 0.4363 0.4929 0.3773 0.0136  0.0121  -0.0730 61  GLN   A O     
469  C  CB    . GLN   A 64  ? 0.3344 0.3684 0.2900 0.0083  0.0050  -0.0645 61  GLN   A CB    
470  C  CG    . GLN   A 64  ? 0.2977 0.3205 0.2614 0.0054  0.0023  -0.0587 61  GLN   A CG    
471  C  CD    . GLN   A 64  ? 0.2892 0.3060 0.2600 0.0069  0.0048  -0.0538 61  GLN   A CD    
472  O  OE1   . GLN   A 64  ? 0.2671 0.2888 0.2377 0.0074  0.0077  -0.0470 61  GLN   A OE1   
473  N  NE2   . GLN   A 64  ? 0.2665 0.2722 0.2439 0.0075  0.0031  -0.0572 61  GLN   A NE2   
474  N  N     . GLU   A 65  ? 0.4374 0.4838 0.3849 0.0183  0.0105  -0.0922 62  GLU   A N     
475  C  CA    . GLU   A 65  ? 0.4455 0.5068 0.3820 0.0206  0.0134  -0.0994 62  GLU   A CA    
476  C  C     . GLU   A 65  ? 0.4383 0.5131 0.3717 0.0226  0.0204  -0.0936 62  GLU   A C     
477  O  O     . GLU   A 65  ? 0.4015 0.4736 0.3438 0.0245  0.0235  -0.0905 62  GLU   A O     
478  C  CB    . GLU   A 65  ? 0.4737 0.5316 0.4105 0.0238  0.0115  -0.1154 62  GLU   A CB    
479  C  CG    . GLU   A 65  ? 0.5021 0.5431 0.4465 0.0212  0.0049  -0.1193 62  GLU   A CG    
480  C  CD    . GLU   A 65  ? 0.5118 0.5365 0.4691 0.0238  0.0039  -0.1229 62  GLU   A CD    
481  O  OE1   . GLU   A 65  ? 0.4846 0.5082 0.4480 0.0266  0.0074  -0.1175 62  GLU   A OE1   
482  O  OE2   . GLU   A 65  ? 0.5093 0.5221 0.4708 0.0228  -0.0008 -0.1309 62  GLU   A OE2   
483  N  N     . GLU   A 66  ? 0.4759 0.5656 0.3969 0.0218  0.0226  -0.0920 63  GLU   A N     
484  C  CA    . GLU   A 66  ? 0.4582 0.5622 0.3752 0.0225  0.0298  -0.0859 63  GLU   A CA    
485  C  C     . GLU   A 66  ? 0.4131 0.5222 0.3350 0.0278  0.0350  -0.0960 63  GLU   A C     
486  O  O     . GLU   A 66  ? 0.4210 0.5318 0.3510 0.0287  0.0391  -0.0909 63  GLU   A O     
487  C  CB    . GLU   A 66  ? 0.4965 0.6153 0.3976 0.0207  0.0309  -0.0824 63  GLU   A CB    
488  C  CG    . GLU   A 66  ? 0.5323 0.6672 0.4285 0.0213  0.0389  -0.0779 63  GLU   A CG    
489  C  CD    . GLU   A 66  ? 0.5510 0.6863 0.4492 0.0173  0.0409  -0.0614 63  GLU   A CD    
490  O  OE1   . GLU   A 66  ? 0.6037 0.7274 0.5057 0.0147  0.0357  -0.0544 63  GLU   A OE1   
491  O  OE2   . GLU   A 66  ? 0.5968 0.7438 0.4935 0.0167  0.0477  -0.0560 63  GLU   A OE2   
492  N  N     . TYR   A 67  ? 0.3783 0.4895 0.2962 0.0314  0.0341  -0.1105 64  TYR   A N     
493  C  CA    . TYR   A 67  ? 0.3569 0.4731 0.2806 0.0376  0.0389  -0.1215 64  TYR   A CA    
494  C  C     . TYR   A 67  ? 0.3293 0.4271 0.2671 0.0408  0.0346  -0.1287 64  TYR   A C     
495  O  O     . TYR   A 67  ? 0.3380 0.4261 0.2754 0.0417  0.0295  -0.1391 64  TYR   A O     
496  C  CB    . TYR   A 67  ? 0.3798 0.5107 0.2909 0.0406  0.0415  -0.1344 64  TYR   A CB    
497  C  CG    . TYR   A 67  ? 0.3853 0.5342 0.2811 0.0371  0.0453  -0.1257 64  TYR   A CG    
498  C  CD1   . TYR   A 67  ? 0.3888 0.5514 0.2850 0.0365  0.0532  -0.1166 64  TYR   A CD1   
499  C  CD2   . TYR   A 67  ? 0.3882 0.5403 0.2700 0.0339  0.0408  -0.1256 64  TYR   A CD2   
500  C  CE1   . TYR   A 67  ? 0.3961 0.5738 0.2784 0.0327  0.0567  -0.1068 64  TYR   A CE1   
501  C  CE2   . TYR   A 67  ? 0.4055 0.5734 0.2728 0.0309  0.0438  -0.1161 64  TYR   A CE2   
502  C  CZ    . TYR   A 67  ? 0.4174 0.5974 0.2849 0.0302  0.0519  -0.1063 64  TYR   A CZ    
503  O  OH    . TYR   A 67  ? 0.4469 0.6415 0.3003 0.0268  0.0550  -0.0954 64  TYR   A OH    
504  N  N     . SER   A 68  ? 0.2949 0.3882 0.2452 0.0423  0.0364  -0.1228 65  SER   A N     
505  C  CA    . SER   A 68  ? 0.2898 0.3665 0.2536 0.0459  0.0327  -0.1275 65  SER   A CA    
506  C  C     . SER   A 68  ? 0.2830 0.3639 0.2587 0.0500  0.0370  -0.1243 65  SER   A C     
507  O  O     . SER   A 68  ? 0.2612 0.3430 0.2405 0.0467  0.0380  -0.1121 65  SER   A O     
508  C  CB    . SER   A 68  ? 0.2812 0.3403 0.2479 0.0408  0.0260  -0.1195 65  SER   A CB    
509  O  OG    . SER   A 68  ? 0.2850 0.3285 0.2645 0.0433  0.0229  -0.1194 65  SER   A OG    
510  N  N     . ALA   A 69  ? 0.2978 0.3817 0.2802 0.0573  0.0392  -0.1361 66  ALA   A N     
511  C  CA    . ALA   A 69  ? 0.3094 0.3973 0.3053 0.0621  0.0422  -0.1344 66  ALA   A CA    
512  C  C     . ALA   A 69  ? 0.2966 0.3679 0.3028 0.0604  0.0368  -0.1247 66  ALA   A C     
513  O  O     . ALA   A 69  ? 0.2790 0.3558 0.2927 0.0604  0.0389  -0.1169 66  ALA   A O     
514  C  CB    . ALA   A 69  ? 0.3216 0.4120 0.3249 0.0713  0.0438  -0.1498 66  ALA   A CB    
515  N  N     . MET   A 70  ? 0.3128 0.3646 0.3193 0.0590  0.0300  -0.1255 67  MET   A N     
516  C  CA    . MET   A 70  ? 0.3356 0.3715 0.3506 0.0575  0.0249  -0.1164 67  MET   A CA    
517  C  C     . MET   A 70  ? 0.2968 0.3359 0.3071 0.0502  0.0255  -0.1023 67  MET   A C     
518  O  O     . MET   A 70  ? 0.2586 0.2956 0.2761 0.0498  0.0247  -0.0945 67  MET   A O     
519  C  CB    . MET   A 70  ? 0.3859 0.4006 0.4024 0.0570  0.0180  -0.1199 67  MET   A CB    
520  C  CG    . MET   A 70  ? 0.4591 0.4658 0.4848 0.0653  0.0163  -0.1319 67  MET   A CG    
521  S  SD    . MET   A 70  ? 0.5909 0.5808 0.6311 0.0696  0.0111  -0.1261 67  MET   A SD    
522  C  CE    . MET   A 70  ? 0.5360 0.5452 0.5849 0.0757  0.0165  -0.1245 67  MET   A CE    
523  N  N     . ARG   A 71  ? 0.2821 0.3267 0.2810 0.0449  0.0265  -0.1000 68  ARG   A N     
524  C  CA    . ARG   A 71  ? 0.2846 0.3326 0.2792 0.0385  0.0271  -0.0872 68  ARG   A CA    
525  C  C     . ARG   A 71  ? 0.2655 0.3284 0.2637 0.0390  0.0328  -0.0823 68  ARG   A C     
526  O  O     . ARG   A 71  ? 0.2366 0.2982 0.2385 0.0360  0.0324  -0.0728 68  ARG   A O     
527  C  CB    . ARG   A 71  ? 0.3148 0.3674 0.2967 0.0339  0.0270  -0.0864 68  ARG   A CB    
528  C  CG    . ARG   A 71  ? 0.3477 0.3999 0.3260 0.0279  0.0261  -0.0739 68  ARG   A CG    
529  C  CD    . ARG   A 71  ? 0.4013 0.4482 0.3717 0.0240  0.0219  -0.0737 68  ARG   A CD    
530  N  NE    . ARG   A 71  ? 0.4448 0.4925 0.4131 0.0194  0.0214  -0.0621 68  ARG   A NE    
531  C  CZ    . ARG   A 71  ? 0.4682 0.5055 0.4392 0.0162  0.0174  -0.0566 68  ARG   A CZ    
532  N  NH1   . ARG   A 71  ? 0.4752 0.5002 0.4508 0.0160  0.0133  -0.0595 68  ARG   A NH1   
533  N  NH2   . ARG   A 71  ? 0.4809 0.5204 0.4500 0.0131  0.0176  -0.0475 68  ARG   A NH2   
534  N  N     . ASP   A 72  ? 0.2685 0.3462 0.2657 0.0426  0.0383  -0.0892 69  ASP   A N     
535  C  CA    . ASP   A 72  ? 0.2692 0.3626 0.2716 0.0425  0.0442  -0.0844 69  ASP   A CA    
536  C  C     . ASP   A 72  ? 0.2511 0.3397 0.2681 0.0459  0.0423  -0.0831 69  ASP   A C     
537  O  O     . ASP   A 72  ? 0.2327 0.3265 0.2547 0.0429  0.0438  -0.0747 69  ASP   A O     
538  C  CB    . ASP   A 72  ? 0.2972 0.4093 0.2957 0.0458  0.0511  -0.0925 69  ASP   A CB    
539  C  CG    . ASP   A 72  ? 0.3190 0.4390 0.3015 0.0418  0.0534  -0.0915 69  ASP   A CG    
540  O  OD1   . ASP   A 72  ? 0.3255 0.4422 0.3015 0.0356  0.0517  -0.0810 69  ASP   A OD1   
541  O  OD2   . ASP   A 72  ? 0.3692 0.4991 0.3460 0.0453  0.0565  -0.1015 69  ASP   A OD2   
542  N  N     . GLN   A 73  ? 0.2514 0.3297 0.2751 0.0519  0.0386  -0.0910 70  GLN   A N     
543  C  CA    . GLN   A 73  ? 0.2580 0.3313 0.2952 0.0559  0.0358  -0.0895 70  GLN   A CA    
544  C  C     . GLN   A 73  ? 0.2376 0.2988 0.2755 0.0508  0.0308  -0.0783 70  GLN   A C     
545  O  O     . GLN   A 73  ? 0.2241 0.2892 0.2699 0.0506  0.0306  -0.0727 70  GLN   A O     
546  C  CB    . GLN   A 73  ? 0.2898 0.3522 0.3336 0.0637  0.0320  -0.0996 70  GLN   A CB    
547  C  CG    . GLN   A 73  ? 0.3180 0.3796 0.3767 0.0699  0.0297  -0.0996 70  GLN   A CG    
548  C  CD    . GLN   A 73  ? 0.3387 0.4218 0.4055 0.0713  0.0356  -0.0985 70  GLN   A CD    
549  O  OE1   . GLN   A 73  ? 0.4108 0.5106 0.4766 0.0731  0.0422  -0.1050 70  GLN   A OE1   
550  N  NE2   . GLN   A 73  ? 0.3550 0.4387 0.4299 0.0701  0.0332  -0.0905 70  GLN   A NE2   
551  N  N     . TYR   A 74  ? 0.2303 0.2777 0.2602 0.0468  0.0268  -0.0755 71  TYR   A N     
552  C  CA    . TYR   A 74  ? 0.2218 0.2595 0.2523 0.0423  0.0227  -0.0656 71  TYR   A CA    
553  C  C     . TYR   A 74  ? 0.1998 0.2460 0.2265 0.0362  0.0255  -0.0568 71  TYR   A C     
554  O  O     . TYR   A 74  ? 0.1827 0.2254 0.2129 0.0337  0.0233  -0.0497 71  TYR   A O     
555  C  CB    . TYR   A 74  ? 0.2345 0.2545 0.2607 0.0403  0.0173  -0.0649 71  TYR   A CB    
556  C  CG    . TYR   A 74  ? 0.2494 0.2675 0.2649 0.0356  0.0173  -0.0654 71  TYR   A CG    
557  C  CD1   . TYR   A 74  ? 0.2463 0.2705 0.2553 0.0300  0.0190  -0.0584 71  TYR   A CD1   
558  C  CD2   . TYR   A 74  ? 0.2694 0.2786 0.2825 0.0367  0.0146  -0.0729 71  TYR   A CD2   
559  C  CE1   . TYR   A 74  ? 0.2632 0.2860 0.2632 0.0263  0.0182  -0.0586 71  TYR   A CE1   
560  C  CE2   . TYR   A 74  ? 0.2744 0.2827 0.2787 0.0323  0.0138  -0.0736 71  TYR   A CE2   
561  C  CZ    . TYR   A 74  ? 0.2753 0.2909 0.2730 0.0274  0.0155  -0.0664 71  TYR   A CZ    
562  O  OH    . TYR   A 74  ? 0.2991 0.3147 0.2888 0.0235  0.0140  -0.0671 71  TYR   A OH    
563  N  N     . MET   A 75  ? 0.1927 0.2504 0.2128 0.0338  0.0303  -0.0571 72  MET   A N     
564  C  CA    . MET   A 75  ? 0.2017 0.2674 0.2205 0.0285  0.0331  -0.0484 72  MET   A CA    
565  C  C     . MET   A 75  ? 0.1969 0.2739 0.2265 0.0298  0.0361  -0.0472 72  MET   A C     
566  O  O     . MET   A 75  ? 0.2000 0.2775 0.2333 0.0259  0.0356  -0.0401 72  MET   A O     
567  C  CB    . MET   A 75  ? 0.2004 0.2744 0.2085 0.0252  0.0369  -0.0471 72  MET   A CB    
568  C  CG    . MET   A 75  ? 0.2169 0.2804 0.2154 0.0229  0.0329  -0.0465 72  MET   A CG    
569  S  SD    . MET   A 75  ? 0.2390 0.3127 0.2244 0.0191  0.0362  -0.0432 72  MET   A SD    
570  C  CE    . MET   A 75  ? 0.2529 0.3134 0.2316 0.0169  0.0298  -0.0428 72  MET   A CE    
571  N  N     . ARG   A 76  ? 0.2011 0.2873 0.2368 0.0354  0.0390  -0.0549 73  ARG   A N     
572  C  CA    . ARG   A 76  ? 0.2017 0.2993 0.2503 0.0375  0.0411  -0.0550 73  ARG   A CA    
573  C  C     . ARG   A 76  ? 0.1900 0.2777 0.2474 0.0392  0.0349  -0.0523 73  ARG   A C     
574  O  O     . ARG   A 76  ? 0.1768 0.2702 0.2417 0.0366  0.0347  -0.0473 73  ARG   A O     
575  C  CB    . ARG   A 76  ? 0.2241 0.3341 0.2780 0.0444  0.0453  -0.0651 73  ARG   A CB    
576  C  CG    . ARG   A 76  ? 0.2492 0.3761 0.2965 0.0420  0.0532  -0.0663 73  ARG   A CG    
577  C  CD    . ARG   A 76  ? 0.2771 0.4200 0.3318 0.0488  0.0584  -0.0763 73  ARG   A CD    
578  N  NE    . ARG   A 76  ? 0.3146 0.4486 0.3686 0.0565  0.0554  -0.0875 73  ARG   A NE    
579  C  CZ    . ARG   A 76  ? 0.3387 0.4741 0.3824 0.0584  0.0576  -0.0954 73  ARG   A CZ    
580  N  NH1   . ARG   A 76  ? 0.3424 0.4887 0.3740 0.0534  0.0628  -0.0928 73  ARG   A NH1   
581  N  NH2   . ARG   A 76  ? 0.3520 0.4774 0.3974 0.0654  0.0541  -0.1061 73  ARG   A NH2   
582  N  N     . THR   A 77  ? 0.1862 0.2590 0.2424 0.0430  0.0295  -0.0553 74  THR   A N     
583  C  CA    . THR   A 77  ? 0.1740 0.2372 0.2371 0.0451  0.0233  -0.0525 74  THR   A CA    
584  C  C     . THR   A 77  ? 0.1644 0.2188 0.2225 0.0388  0.0199  -0.0437 74  THR   A C     
585  O  O     . THR   A 77  ? 0.1605 0.2142 0.2246 0.0387  0.0165  -0.0399 74  THR   A O     
586  C  CB    . THR   A 77  ? 0.1868 0.2362 0.2503 0.0510  0.0189  -0.0579 74  THR   A CB    
587  O  OG1   . THR   A 77  ? 0.2024 0.2603 0.2716 0.0577  0.0220  -0.0673 74  THR   A OG1   
588  C  CG2   . THR   A 77  ? 0.1921 0.2324 0.2621 0.0538  0.0125  -0.0542 74  THR   A CG2   
589  N  N     . GLY   A 78  ? 0.1449 0.1935 0.1924 0.0339  0.0206  -0.0409 75  GLY   A N     
590  C  CA    . GLY   A 78  ? 0.1375 0.1770 0.1805 0.0288  0.0173  -0.0338 75  GLY   A CA    
591  C  C     . GLY   A 78  ? 0.1270 0.1748 0.1733 0.0244  0.0190  -0.0285 75  GLY   A C     
592  O  O     . GLY   A 78  ? 0.1388 0.1983 0.1867 0.0226  0.0239  -0.0285 75  GLY   A O     
593  N  N     . GLU   A 79  ? 0.1201 0.1616 0.1671 0.0223  0.0151  -0.0241 76  GLU   A N     
594  C  CA    . GLU   A 79  ? 0.1207 0.1681 0.1718 0.0179  0.0157  -0.0199 76  GLU   A CA    
595  C  C     . GLU   A 79  ? 0.1139 0.1562 0.1575 0.0124  0.0163  -0.0152 76  GLU   A C     
596  O  O     . GLU   A 79  ? 0.1119 0.1603 0.1576 0.0084  0.0191  -0.0122 76  GLU   A O     
597  C  CB    . GLU   A 79  ? 0.1237 0.1695 0.1809 0.0193  0.0107  -0.0191 76  GLU   A CB    
598  C  CG    . GLU   A 79  ? 0.1411 0.1946 0.2082 0.0249  0.0099  -0.0230 76  GLU   A CG    
599  C  CD    . GLU   A 79  ? 0.1542 0.2063 0.2264 0.0268  0.0039  -0.0218 76  GLU   A CD    
600  O  OE1   . GLU   A 79  ? 0.1570 0.1977 0.2229 0.0273  -0.0004 -0.0195 76  GLU   A OE1   
601  O  OE2   . GLU   A 79  ? 0.2067 0.2704 0.2895 0.0274  0.0035  -0.0228 76  GLU   A OE2   
602  N  N     . GLY   A 80  ? 0.1109 0.1422 0.1468 0.0122  0.0138  -0.0143 77  GLY   A N     
603  C  CA    . GLY   A 80  ? 0.1080 0.1350 0.1375 0.0081  0.0142  -0.0106 77  GLY   A CA    
604  C  C     . GLY   A 80  ? 0.1096 0.1305 0.1310 0.0088  0.0140  -0.0119 77  GLY   A C     
605  O  O     . GLY   A 80  ? 0.1153 0.1312 0.1358 0.0116  0.0121  -0.0151 77  GLY   A O     
606  N  N     . PHE   A 81  ? 0.1118 0.1329 0.1283 0.0059  0.0154  -0.0091 78  PHE   A N     
607  C  CA    . PHE   A 81  ? 0.1183 0.1368 0.1275 0.0059  0.0154  -0.0104 78  PHE   A CA    
608  C  C     . PHE   A 81  ? 0.1227 0.1353 0.1283 0.0035  0.0133  -0.0070 78  PHE   A C     
609  O  O     . PHE   A 81  ? 0.1270 0.1406 0.1330 0.0014  0.0138  -0.0029 78  PHE   A O     
610  C  CB    . PHE   A 81  ? 0.1204 0.1476 0.1265 0.0056  0.0191  -0.0107 78  PHE   A CB    
611  C  CG    . PHE   A 81  ? 0.1171 0.1516 0.1272 0.0085  0.0217  -0.0151 78  PHE   A CG    
612  C  CD1   . PHE   A 81  ? 0.1155 0.1571 0.1328 0.0080  0.0239  -0.0135 78  PHE   A CD1   
613  C  CD2   . PHE   A 81  ? 0.1238 0.1581 0.1318 0.0119  0.0217  -0.0217 78  PHE   A CD2   
614  C  CE1   . PHE   A 81  ? 0.1187 0.1686 0.1412 0.0111  0.0264  -0.0180 78  PHE   A CE1   
615  C  CE2   . PHE   A 81  ? 0.1302 0.1716 0.1430 0.0156  0.0241  -0.0267 78  PHE   A CE2   
616  C  CZ    . PHE   A 81  ? 0.1247 0.1745 0.1450 0.0153  0.0265  -0.0247 78  PHE   A CZ    
617  N  N     . LEU   A 82  ? 0.1226 0.1293 0.1258 0.0040  0.0110  -0.0089 79  LEU   A N     
618  C  CA    . LEU   A 82  ? 0.1288 0.1315 0.1291 0.0021  0.0093  -0.0067 79  LEU   A CA    
619  C  C     . LEU   A 82  ? 0.1339 0.1400 0.1295 0.0016  0.0098  -0.0076 79  LEU   A C     
620  O  O     . LEU   A 82  ? 0.1285 0.1343 0.1222 0.0025  0.0094  -0.0117 79  LEU   A O     
621  C  CB    . LEU   A 82  ? 0.1379 0.1339 0.1386 0.0021  0.0069  -0.0078 79  LEU   A CB    
622  C  CG    . LEU   A 82  ? 0.1447 0.1385 0.1449 0.0002  0.0059  -0.0050 79  LEU   A CG    
623  C  CD1   . LEU   A 82  ? 0.1518 0.1461 0.1547 0.0003  0.0059  -0.0031 79  LEU   A CD1   
624  C  CD2   . LEU   A 82  ? 0.1488 0.1375 0.1482 -0.0008 0.0043  -0.0054 79  LEU   A CD2   
625  N  N     . CYS   A 83  ? 0.1354 0.1447 0.1293 0.0005  0.0103  -0.0038 80  CYS   A N     
626  C  CA    . CYS   A 83  ? 0.1468 0.1606 0.1352 0.0002  0.0102  -0.0038 80  CYS   A CA    
627  C  C     . CYS   A 83  ? 0.1474 0.1590 0.1353 -0.0006 0.0074  -0.0030 80  CYS   A C     
628  O  O     . CYS   A 83  ? 0.1396 0.1503 0.1294 -0.0009 0.0069  0.0009  80  CYS   A O     
629  C  CB    . CYS   A 83  ? 0.1564 0.1756 0.1432 -0.0002 0.0124  0.0009  80  CYS   A CB    
630  S  SG    . CYS   A 83  ? 0.2149 0.2401 0.2026 0.0006  0.0163  -0.0016 80  CYS   A SG    
631  N  N     . VAL   A 84  ? 0.1423 0.1537 0.1282 -0.0010 0.0058  -0.0072 81  VAL   A N     
632  C  CA    . VAL   A 84  ? 0.1394 0.1499 0.1267 -0.0024 0.0032  -0.0071 81  VAL   A CA    
633  C  C     . VAL   A 84  ? 0.1393 0.1559 0.1228 -0.0026 0.0011  -0.0077 81  VAL   A C     
634  O  O     . VAL   A 84  ? 0.1370 0.1563 0.1164 -0.0025 0.0008  -0.0115 81  VAL   A O     
635  C  CB    . VAL   A 84  ? 0.1357 0.1406 0.1256 -0.0037 0.0023  -0.0106 81  VAL   A CB    
636  C  CG1   . VAL   A 84  ? 0.1401 0.1450 0.1329 -0.0059 0.0007  -0.0099 81  VAL   A CG1   
637  C  CG2   . VAL   A 84  ? 0.1354 0.1350 0.1279 -0.0029 0.0037  -0.0101 81  VAL   A CG2   
638  N  N     . PHE   A 85  ? 0.1343 0.1531 0.1197 -0.0026 -0.0005 -0.0043 82  PHE   A N     
639  C  CA    . PHE   A 85  ? 0.1364 0.1616 0.1202 -0.0028 -0.0037 -0.0045 82  PHE   A CA    
640  C  C     . PHE   A 85  ? 0.1338 0.1591 0.1241 -0.0041 -0.0052 -0.0051 82  PHE   A C     
641  O  O     . PHE   A 85  ? 0.1363 0.1573 0.1306 -0.0044 -0.0035 -0.0041 82  PHE   A O     
642  C  CB    . PHE   A 85  ? 0.1311 0.1609 0.1113 -0.0007 -0.0044 0.0009  82  PHE   A CB    
643  C  CG    . PHE   A 85  ? 0.1300 0.1574 0.1154 0.0007  -0.0045 0.0061  82  PHE   A CG    
644  C  CD1   . PHE   A 85  ? 0.1287 0.1506 0.1158 0.0012  -0.0019 0.0092  82  PHE   A CD1   
645  C  CD2   . PHE   A 85  ? 0.1286 0.1594 0.1181 0.0018  -0.0075 0.0072  82  PHE   A CD2   
646  C  CE1   . PHE   A 85  ? 0.1245 0.1433 0.1168 0.0026  -0.0022 0.0126  82  PHE   A CE1   
647  C  CE2   . PHE   A 85  ? 0.1229 0.1511 0.1178 0.0039  -0.0075 0.0108  82  PHE   A CE2   
648  C  CZ    . PHE   A 85  ? 0.1265 0.1481 0.1227 0.0043  -0.0049 0.0132  82  PHE   A CZ    
649  N  N     . ALA   A 86  ? 0.1291 0.1605 0.1201 -0.0050 -0.0084 -0.0070 83  ALA   A N     
650  C  CA    . ALA   A 86  ? 0.1330 0.1676 0.1311 -0.0065 -0.0098 -0.0075 83  ALA   A CA    
651  C  C     . ALA   A 86  ? 0.1362 0.1773 0.1369 -0.0035 -0.0119 -0.0037 83  ALA   A C     
652  O  O     . ALA   A 86  ? 0.1365 0.1823 0.1326 -0.0017 -0.0146 -0.0020 83  ALA   A O     
653  C  CB    . ALA   A 86  ? 0.1335 0.1713 0.1328 -0.0100 -0.0122 -0.0128 83  ALA   A CB    
654  N  N     . ILE   A 87  ? 0.1338 0.1755 0.1413 -0.0026 -0.0110 -0.0022 84  ILE   A N     
655  C  CA    . ILE   A 87  ? 0.1394 0.1858 0.1502 0.0015  -0.0131 0.0015  84  ILE   A CA    
656  C  C     . ILE   A 87  ? 0.1467 0.2038 0.1604 0.0020  -0.0178 0.0007  84  ILE   A C     
657  O  O     . ILE   A 87  ? 0.1487 0.2100 0.1647 0.0061  -0.0206 0.0042  84  ILE   A O     
658  C  CB    . ILE   A 87  ? 0.1376 0.1826 0.1556 0.0033  -0.0109 0.0022  84  ILE   A CB    
659  C  CG1   . ILE   A 87  ? 0.1417 0.1926 0.1663 0.0004  -0.0100 -0.0015 84  ILE   A CG1   
660  C  CG2   . ILE   A 87  ? 0.1417 0.1769 0.1566 0.0033  -0.0073 0.0032  84  ILE   A CG2   
661  C  CD1   . ILE   A 87  ? 0.1465 0.2015 0.1789 0.0033  -0.0087 -0.0015 84  ILE   A CD1   
662  N  N     . ASN   A 88  ? 0.1545 0.2157 0.1684 -0.0021 -0.0191 -0.0040 85  ASN   A N     
663  C  CA    . ASN   A 88  ? 0.1648 0.2373 0.1812 -0.0025 -0.0242 -0.0060 85  ASN   A CA    
664  C  C     . ASN   A 88  ? 0.1767 0.2508 0.1835 -0.0035 -0.0272 -0.0080 85  ASN   A C     
665  O  O     . ASN   A 88  ? 0.2005 0.2835 0.2085 -0.0052 -0.0317 -0.0117 85  ASN   A O     
666  C  CB    . ASN   A 88  ? 0.1652 0.2432 0.1907 -0.0072 -0.0241 -0.0105 85  ASN   A CB    
667  C  CG    . ASN   A 88  ? 0.1689 0.2399 0.1916 -0.0129 -0.0222 -0.0149 85  ASN   A CG    
668  O  OD1   . ASN   A 88  ? 0.1731 0.2340 0.1892 -0.0127 -0.0193 -0.0144 85  ASN   A OD1   
669  N  ND2   . ASN   A 88  ? 0.1581 0.2346 0.1870 -0.0180 -0.0240 -0.0192 85  ASN   A ND2   
670  N  N     . ASN   A 89  ? 0.1772 0.2441 0.1749 -0.0023 -0.0249 -0.0062 86  ASN   A N     
671  C  CA    . ASN   A 89  ? 0.1912 0.2602 0.1791 -0.0032 -0.0266 -0.0091 86  ASN   A CA    
672  C  C     . ASN   A 89  ? 0.1897 0.2566 0.1692 0.0004  -0.0253 -0.0027 86  ASN   A C     
673  O  O     . ASN   A 89  ? 0.1761 0.2353 0.1526 0.0003  -0.0208 -0.0016 86  ASN   A O     
674  C  CB    . ASN   A 89  ? 0.2066 0.2687 0.1930 -0.0069 -0.0239 -0.0155 86  ASN   A CB    
675  C  CG    . ASN   A 89  ? 0.2284 0.2921 0.2046 -0.0071 -0.0248 -0.0199 86  ASN   A CG    
676  O  OD1   . ASN   A 89  ? 0.2398 0.3096 0.2079 -0.0046 -0.0265 -0.0174 86  ASN   A OD1   
677  N  ND2   . ASN   A 89  ? 0.2619 0.3197 0.2383 -0.0099 -0.0234 -0.0267 86  ASN   A ND2   
678  N  N     . THR   A 90  ? 0.1920 0.2662 0.1687 0.0034  -0.0293 0.0020  87  THR   A N     
679  C  CA    . THR   A 90  ? 0.2021 0.2747 0.1708 0.0063  -0.0284 0.0096  87  THR   A CA    
680  C  C     . THR   A 90  ? 0.2213 0.2937 0.1786 0.0048  -0.0256 0.0076  87  THR   A C     
681  O  O     . THR   A 90  ? 0.2416 0.3088 0.1954 0.0053  -0.0215 0.0123  87  THR   A O     
682  C  CB    . THR   A 90  ? 0.2127 0.2935 0.1798 0.0098  -0.0343 0.0154  87  THR   A CB    
683  O  OG1   . THR   A 90  ? 0.2165 0.2967 0.1954 0.0123  -0.0360 0.0178  87  THR   A OG1   
684  C  CG2   . THR   A 90  ? 0.2244 0.3031 0.1821 0.0120  -0.0333 0.0244  87  THR   A CG2   
685  N  N     . LYS   A 91  ? 0.2212 0.2993 0.1738 0.0028  -0.0275 -0.0001 88  LYS   A N     
686  C  CA    . LYS   A 91  ? 0.2403 0.3192 0.1827 0.0019  -0.0245 -0.0040 88  LYS   A CA    
687  C  C     . LYS   A 91  ? 0.2249 0.2939 0.1704 0.0009  -0.0182 -0.0054 88  LYS   A C     
688  O  O     . LYS   A 91  ? 0.2298 0.2986 0.1689 0.0015  -0.0142 -0.0034 88  LYS   A O     
689  C  CB    . LYS   A 91  ? 0.2629 0.3479 0.2020 -0.0001 -0.0280 -0.0144 88  LYS   A CB    
690  C  CG    . LYS   A 91  ? 0.3107 0.3968 0.2402 -0.0005 -0.0250 -0.0209 88  LYS   A CG    
691  C  CD    . LYS   A 91  ? 0.3414 0.4364 0.2573 0.0017  -0.0244 -0.0156 88  LYS   A CD    
692  C  CE    . LYS   A 91  ? 0.3838 0.4841 0.2893 0.0015  -0.0224 -0.0245 88  LYS   A CE    
693  N  NZ    . LYS   A 91  ? 0.4080 0.4997 0.3180 0.0011  -0.0166 -0.0304 88  LYS   A NZ    
694  N  N     . SER   A 92  ? 0.1999 0.2618 0.1554 -0.0007 -0.0174 -0.0087 89  SER   A N     
695  C  CA    . SER   A 92  ? 0.1894 0.2420 0.1486 -0.0013 -0.0124 -0.0097 89  SER   A CA    
696  C  C     . SER   A 92  ? 0.1860 0.2347 0.1462 0.0002  -0.0091 -0.0015 89  SER   A C     
697  O  O     . SER   A 92  ? 0.1898 0.2346 0.1496 0.0002  -0.0049 -0.0016 89  SER   A O     
698  C  CB    . SER   A 92  ? 0.1814 0.2280 0.1502 -0.0036 -0.0129 -0.0136 89  SER   A CB    
699  O  OG    . SER   A 92  ? 0.1546 0.1999 0.1305 -0.0030 -0.0133 -0.0084 89  SER   A OG    
700  N  N     . PHE   A 93  ? 0.1792 0.2291 0.1417 0.0017  -0.0112 0.0052  90  PHE   A N     
701  C  CA    . PHE   A 93  ? 0.1915 0.2367 0.1556 0.0030  -0.0088 0.0130  90  PHE   A CA    
702  C  C     . PHE   A 93  ? 0.2082 0.2577 0.1629 0.0033  -0.0071 0.0179  90  PHE   A C     
703  O  O     . PHE   A 93  ? 0.1961 0.2421 0.1510 0.0026  -0.0031 0.0217  90  PHE   A O     
704  C  CB    . PHE   A 93  ? 0.1833 0.2275 0.1538 0.0051  -0.0120 0.0179  90  PHE   A CB    
705  C  CG    . PHE   A 93  ? 0.1815 0.2198 0.1542 0.0065  -0.0106 0.0258  90  PHE   A CG    
706  C  CD1   . PHE   A 93  ? 0.1770 0.2074 0.1550 0.0055  -0.0069 0.0255  90  PHE   A CD1   
707  C  CD2   . PHE   A 93  ? 0.1979 0.2383 0.1675 0.0087  -0.0134 0.0337  90  PHE   A CD2   
708  C  CE1   . PHE   A 93  ? 0.1813 0.2057 0.1623 0.0062  -0.0061 0.0319  90  PHE   A CE1   
709  C  CE2   . PHE   A 93  ? 0.2009 0.2342 0.1735 0.0096  -0.0124 0.0411  90  PHE   A CE2   
710  C  CZ    . PHE   A 93  ? 0.1921 0.2172 0.1707 0.0081  -0.0087 0.0398  90  PHE   A CZ    
711  N  N     . GLU   A 94  ? 0.2297 0.2879 0.1761 0.0039  -0.0101 0.0176  91  GLU   A N     
712  C  CA    . GLU   A 94  ? 0.2610 0.3257 0.1962 0.0039  -0.0082 0.0217  91  GLU   A CA    
713  C  C     . GLU   A 94  ? 0.2690 0.3357 0.2002 0.0025  -0.0033 0.0152  91  GLU   A C     
714  O  O     . GLU   A 94  ? 0.2960 0.3664 0.2212 0.0020  0.0007  0.0194  91  GLU   A O     
715  C  CB    . GLU   A 94  ? 0.2794 0.3541 0.2058 0.0051  -0.0134 0.0222  91  GLU   A CB    
716  C  CG    . GLU   A 94  ? 0.2972 0.3714 0.2271 0.0074  -0.0184 0.0305  91  GLU   A CG    
717  C  CD    . GLU   A 94  ? 0.3262 0.4114 0.2461 0.0090  -0.0239 0.0328  91  GLU   A CD    
718  O  OE1   . GLU   A 94  ? 0.3842 0.4776 0.2927 0.0080  -0.0230 0.0290  91  GLU   A OE1   
719  O  OE2   . GLU   A 94  ? 0.3279 0.4145 0.2512 0.0116  -0.0293 0.0380  91  GLU   A OE2   
720  N  N     . ASP   A 95  ? 0.2697 0.3340 0.2048 0.0020  -0.0034 0.0054  92  ASP   A N     
721  C  CA    . ASP   A 95  ? 0.2688 0.3333 0.2026 0.0016  0.0011  -0.0015 92  ASP   A CA    
722  C  C     . ASP   A 95  ? 0.2486 0.3077 0.1884 0.0012  0.0061  0.0023  92  ASP   A C     
723  O  O     . ASP   A 95  ? 0.2357 0.2983 0.1733 0.0014  0.0104  -0.0008 92  ASP   A O     
724  C  CB    . ASP   A 95  ? 0.2904 0.3508 0.2287 0.0012  -0.0008 -0.0120 92  ASP   A CB    
725  C  CG    . ASP   A 95  ? 0.3205 0.3880 0.2521 0.0011  -0.0050 -0.0191 92  ASP   A CG    
726  O  OD1   . ASP   A 95  ? 0.3307 0.4078 0.2522 0.0018  -0.0063 -0.0168 92  ASP   A OD1   
727  O  OD2   . ASP   A 95  ? 0.3465 0.4096 0.2829 -0.0001 -0.0074 -0.0269 92  ASP   A OD2   
728  N  N     . ILE   A 96  ? 0.2126 0.2642 0.1604 0.0008  0.0055  0.0080  93  ILE   A N     
729  C  CA    . ILE   A 96  ? 0.2031 0.2486 0.1583 0.0001  0.0092  0.0097  93  ILE   A CA    
730  C  C     . ILE   A 96  ? 0.2099 0.2610 0.1616 -0.0008 0.0139  0.0141  93  ILE   A C     
731  O  O     . ILE   A 96  ? 0.2052 0.2565 0.1609 -0.0011 0.0176  0.0114  93  ILE   A O     
732  C  CB    . ILE   A 96  ? 0.1875 0.2252 0.1504 -0.0001 0.0073  0.0152  93  ILE   A CB    
733  C  CG1   . ILE   A 96  ? 0.1698 0.2028 0.1379 0.0003  0.0041  0.0103  93  ILE   A CG1   
734  C  CG2   . ILE   A 96  ? 0.1933 0.2263 0.1625 -0.0013 0.0106  0.0182  93  ILE   A CG2   
735  C  CD1   . ILE   A 96  ? 0.1655 0.1942 0.1378 -0.0002 0.0054  0.0037  93  ILE   A CD1   
736  N  N     . HIS   A 97  ? 0.2269 0.2831 0.1718 -0.0012 0.0136  0.0214  94  HIS   A N     
737  C  CA    . HIS   A 97  ? 0.2581 0.3204 0.1991 -0.0029 0.0183  0.0275  94  HIS   A CA    
738  C  C     . HIS   A 97  ? 0.2507 0.3220 0.1877 -0.0025 0.0228  0.0200  94  HIS   A C     
739  O  O     . HIS   A 97  ? 0.2522 0.3268 0.1928 -0.0038 0.0279  0.0212  94  HIS   A O     
740  C  CB    . HIS   A 97  ? 0.3042 0.3709 0.2361 -0.0031 0.0163  0.0365  94  HIS   A CB    
741  C  CG    . HIS   A 97  ? 0.3380 0.4146 0.2617 -0.0050 0.0213  0.0421  94  HIS   A CG    
742  N  ND1   . HIS   A 97  ? 0.3836 0.4584 0.3110 -0.0081 0.0249  0.0516  94  HIS   A ND1   
743  C  CD2   . HIS   A 97  ? 0.3580 0.4471 0.2700 -0.0046 0.0236  0.0392  94  HIS   A CD2   
744  C  CE1   . HIS   A 97  ? 0.3773 0.4637 0.2957 -0.0099 0.0296  0.0552  94  HIS   A CE1   
745  N  NE2   . HIS   A 97  ? 0.3916 0.4872 0.3000 -0.0074 0.0290  0.0475  94  HIS   A NE2   
746  N  N     . HIS   A 98  ? 0.2369 0.3124 0.1677 -0.0005 0.0208  0.0117  95  HIS   A N     
747  C  CA    . HIS   A 98  ? 0.2541 0.3382 0.1810 0.0008  0.0247  0.0031  95  HIS   A CA    
748  C  C     . HIS   A 98  ? 0.2489 0.3281 0.1863 0.0020  0.0269  -0.0038 95  HIS   A C     
749  O  O     . HIS   A 98  ? 0.2370 0.3237 0.1750 0.0028  0.0321  -0.0072 95  HIS   A O     
750  C  CB    . HIS   A 98  ? 0.2782 0.3662 0.1967 0.0026  0.0210  -0.0053 95  HIS   A CB    
751  C  CG    . HIS   A 98  ? 0.3193 0.4148 0.2261 0.0021  0.0184  0.0006  95  HIS   A CG    
752  N  ND1   . HIS   A 98  ? 0.3651 0.4702 0.2632 0.0009  0.0222  0.0088  95  HIS   A ND1   
753  C  CD2   . HIS   A 98  ? 0.3428 0.4380 0.2453 0.0025  0.0121  0.0001  95  HIS   A CD2   
754  C  CE1   . HIS   A 98  ? 0.3802 0.4902 0.2682 0.0011  0.0180  0.0133  95  HIS   A CE1   
755  N  NE2   . HIS   A 98  ? 0.3611 0.4656 0.2519 0.0022  0.0117  0.0078  95  HIS   A NE2   
756  N  N     . TYR   A 99  ? 0.2423 0.3100 0.1877 0.0023  0.0231  -0.0060 96  TYR   A N     
757  C  CA    . TYR   A 99  ? 0.2401 0.3021 0.1958 0.0034  0.0244  -0.0104 96  TYR   A CA    
758  C  C     . TYR   A 99  ? 0.2298 0.2937 0.1919 0.0018  0.0284  -0.0042 96  TYR   A C     
759  O  O     . TYR   A 99  ? 0.2162 0.2839 0.1834 0.0031  0.0317  -0.0081 96  TYR   A O     
760  C  CB    . TYR   A 99  ? 0.2504 0.3003 0.2124 0.0033  0.0197  -0.0116 96  TYR   A CB    
761  C  CG    . TYR   A 99  ? 0.2764 0.3239 0.2350 0.0041  0.0160  -0.0185 96  TYR   A CG    
762  C  CD1   . TYR   A 99  ? 0.3059 0.3553 0.2629 0.0062  0.0167  -0.0279 96  TYR   A CD1   
763  C  CD2   . TYR   A 99  ? 0.2909 0.3347 0.2486 0.0027  0.0116  -0.0163 96  TYR   A CD2   
764  C  CE1   . TYR   A 99  ? 0.3289 0.3755 0.2835 0.0063  0.0129  -0.0349 96  TYR   A CE1   
765  C  CE2   . TYR   A 99  ? 0.3033 0.3460 0.2589 0.0025  0.0080  -0.0229 96  TYR   A CE2   
766  C  CZ    . TYR   A 99  ? 0.3304 0.3738 0.2844 0.0040  0.0085  -0.0323 96  TYR   A CZ    
767  O  OH    . TYR   A 99  ? 0.3642 0.4058 0.3169 0.0034  0.0047  -0.0396 96  TYR   A OH    
768  N  N     . ARG   A 100 ? 0.2331 0.2942 0.1960 -0.0009 0.0277  0.0050  97  ARG   A N     
769  C  CA    . ARG   A 100 ? 0.2412 0.3034 0.2110 -0.0032 0.0310  0.0108  97  ARG   A CA    
770  C  C     . ARG   A 100 ? 0.2513 0.3268 0.2179 -0.0043 0.0371  0.0122  97  ARG   A C     
771  O  O     . ARG   A 100 ? 0.2432 0.3229 0.2176 -0.0050 0.0407  0.0115  97  ARG   A O     
772  C  CB    . ARG   A 100 ? 0.2493 0.3044 0.2209 -0.0058 0.0288  0.0200  97  ARG   A CB    
773  C  CG    . ARG   A 100 ? 0.2695 0.3248 0.2492 -0.0091 0.0317  0.0255  97  ARG   A CG    
774  C  CD    . ARG   A 100 ? 0.2961 0.3421 0.2790 -0.0112 0.0290  0.0332  97  ARG   A CD    
775  N  NE    . ARG   A 100 ? 0.3096 0.3565 0.2998 -0.0153 0.0320  0.0387  97  ARG   A NE    
776  C  CZ    . ARG   A 100 ? 0.3089 0.3531 0.3095 -0.0165 0.0321  0.0361  97  ARG   A CZ    
777  N  NH1   . ARG   A 100 ? 0.3142 0.3543 0.3183 -0.0136 0.0295  0.0285  97  ARG   A NH1   
778  N  NH2   . ARG   A 100 ? 0.3295 0.3753 0.3370 -0.0210 0.0348  0.0413  97  ARG   A NH2   
779  N  N     . GLU   A 101 ? 0.2653 0.3486 0.2206 -0.0044 0.0383  0.0141  98  GLU   A N     
780  C  CA    . GLU   A 101 ? 0.2903 0.3883 0.2405 -0.0054 0.0447  0.0151  98  GLU   A CA    
781  C  C     . GLU   A 101 ? 0.2826 0.3884 0.2350 -0.0018 0.0479  0.0036  98  GLU   A C     
782  O  O     . GLU   A 101 ? 0.2762 0.3933 0.2317 -0.0025 0.0540  0.0037  98  GLU   A O     
783  C  CB    . GLU   A 101 ? 0.3257 0.4307 0.2611 -0.0058 0.0445  0.0194  98  GLU   A CB    
784  C  CG    . GLU   A 101 ? 0.3654 0.4648 0.2983 -0.0090 0.0421  0.0323  98  GLU   A CG    
785  C  CD    . GLU   A 101 ? 0.4085 0.5104 0.3470 -0.0137 0.0470  0.0420  98  GLU   A CD    
786  O  OE1   . GLU   A 101 ? 0.4546 0.5701 0.3875 -0.0154 0.0530  0.0444  98  GLU   A OE1   
787  O  OE2   . GLU   A 101 ? 0.4542 0.5452 0.4031 -0.0158 0.0450  0.0468  98  GLU   A OE2   
788  N  N     . GLN   A 102 ? 0.2845 0.3844 0.2360 0.0020  0.0439  -0.0059 99  GLN   A N     
789  C  CA    . GLN   A 102 ? 0.2883 0.3920 0.2435 0.0063  0.0457  -0.0176 99  GLN   A CA    
790  C  C     . GLN   A 102 ? 0.2564 0.3577 0.2260 0.0069  0.0471  -0.0181 99  GLN   A C     
791  O  O     . GLN   A 102 ? 0.2312 0.3426 0.2055 0.0090  0.0517  -0.0227 99  GLN   A O     
792  C  CB    . GLN   A 102 ? 0.3154 0.4096 0.2688 0.0094  0.0402  -0.0266 99  GLN   A CB    
793  C  CG    . GLN   A 102 ? 0.3654 0.4651 0.3057 0.0103  0.0390  -0.0313 99  GLN   A CG    
794  C  CD    . GLN   A 102 ? 0.3909 0.4803 0.3314 0.0122  0.0330  -0.0399 99  GLN   A CD    
795  O  OE1   . GLN   A 102 ? 0.4271 0.5040 0.3765 0.0125  0.0297  -0.0407 99  GLN   A OE1   
796  N  NE2   . GLN   A 102 ? 0.4453 0.5402 0.3755 0.0132  0.0316  -0.0464 99  GLN   A NE2   
797  N  N     . ILE   A 103 ? 0.2278 0.3169 0.2042 0.0053  0.0429  -0.0138 100 ILE   A N     
798  C  CA    . ILE   A 103 ? 0.2270 0.3131 0.2162 0.0060  0.0428  -0.0146 100 ILE   A CA    
799  C  C     . ILE   A 103 ? 0.2218 0.3191 0.2167 0.0028  0.0482  -0.0090 100 ILE   A C     
800  O  O     . ILE   A 103 ? 0.2118 0.3162 0.2161 0.0046  0.0508  -0.0128 100 ILE   A O     
801  C  CB    . ILE   A 103 ? 0.2223 0.2938 0.2157 0.0046  0.0372  -0.0110 100 ILE   A CB    
802  C  CG1   . ILE   A 103 ? 0.2247 0.2860 0.2146 0.0073  0.0323  -0.0166 100 ILE   A CG1   
803  C  CG2   . ILE   A 103 ? 0.2302 0.3004 0.2358 0.0049  0.0368  -0.0110 100 ILE   A CG2   
804  C  CD1   . ILE   A 103 ? 0.2350 0.2846 0.2252 0.0052  0.0276  -0.0121 100 ILE   A CD1   
805  N  N     . LYS   A 104 ? 0.2193 0.3183 0.2095 -0.0020 0.0497  0.0003  101 LYS   A N     
806  C  CA    . LYS   A 104 ? 0.2318 0.3409 0.2271 -0.0065 0.0550  0.0072  101 LYS   A CA    
807  C  C     . LYS   A 104 ? 0.2355 0.3626 0.2299 -0.0053 0.0621  0.0033  101 LYS   A C     
808  O  O     . LYS   A 104 ? 0.2162 0.3531 0.2210 -0.0069 0.0663  0.0037  101 LYS   A O     
809  C  CB    . LYS   A 104 ? 0.2488 0.3548 0.2376 -0.0117 0.0550  0.0186  101 LYS   A CB    
810  C  CG    . LYS   A 104 ? 0.2594 0.3513 0.2552 -0.0144 0.0503  0.0240  101 LYS   A CG    
811  C  CD    . LYS   A 104 ? 0.2749 0.3594 0.2632 -0.0170 0.0478  0.0331  101 LYS   A CD    
812  C  CE    . LYS   A 104 ? 0.3155 0.4073 0.3018 -0.0223 0.0526  0.0434  101 LYS   A CE    
813  N  NZ    . LYS   A 104 ? 0.3416 0.4320 0.3146 -0.0223 0.0511  0.0500  101 LYS   A NZ    
814  N  N     . ARG   A 105 ? 0.2394 0.3717 0.2214 -0.0027 0.0633  -0.0008 102 ARG   A N     
815  C  CA    . ARG   A 105 ? 0.2622 0.4119 0.2415 0.0000  0.0698  -0.0074 102 ARG   A CA    
816  C  C     . ARG   A 105 ? 0.2429 0.3964 0.2346 0.0053  0.0707  -0.0180 102 ARG   A C     
817  O  O     . ARG   A 105 ? 0.2312 0.3998 0.2304 0.0053  0.0768  -0.0194 102 ARG   A O     
818  C  CB    . ARG   A 105 ? 0.2912 0.4424 0.2547 0.0028  0.0688  -0.0125 102 ARG   A CB    
819  C  CG    . ARG   A 105 ? 0.3237 0.4898 0.2839 0.0077  0.0738  -0.0238 102 ARG   A CG    
820  C  CD    . ARG   A 105 ? 0.3756 0.5472 0.3181 0.0086  0.0739  -0.0265 102 ARG   A CD    
821  N  NE    . ARG   A 105 ? 0.4070 0.5627 0.3437 0.0096  0.0656  -0.0282 102 ARG   A NE    
822  C  CZ    . ARG   A 105 ? 0.4500 0.6008 0.3767 0.0063  0.0619  -0.0197 102 ARG   A CZ    
823  N  NH1   . ARG   A 105 ? 0.4524 0.6112 0.3724 0.0017  0.0653  -0.0078 102 ARG   A NH1   
824  N  NH2   . ARG   A 105 ? 0.4485 0.5865 0.3726 0.0075  0.0545  -0.0227 102 ARG   A NH2   
825  N  N     . VAL   A 106 ? 0.2300 0.3703 0.2240 0.0099  0.0646  -0.0251 103 VAL   A N     
826  C  CA    . VAL   A 106 ? 0.2333 0.3741 0.2389 0.0157  0.0640  -0.0345 103 VAL   A CA    
827  C  C     . VAL   A 106 ? 0.2240 0.3679 0.2448 0.0136  0.0647  -0.0301 103 VAL   A C     
828  O  O     . VAL   A 106 ? 0.2316 0.3879 0.2624 0.0167  0.0683  -0.0353 103 VAL   A O     
829  C  CB    . VAL   A 106 ? 0.2409 0.3640 0.2455 0.0197  0.0565  -0.0403 103 VAL   A CB    
830  C  CG1   . VAL   A 106 ? 0.2472 0.3669 0.2652 0.0250  0.0541  -0.0466 103 VAL   A CG1   
831  C  CG2   . VAL   A 106 ? 0.2531 0.3760 0.2459 0.0227  0.0561  -0.0480 103 VAL   A CG2   
832  N  N     . LYS   A 107 ? 0.2116 0.3456 0.2345 0.0084  0.0612  -0.0212 104 LYS   A N     
833  C  CA    . LYS   A 107 ? 0.2077 0.3439 0.2448 0.0059  0.0608  -0.0177 104 LYS   A CA    
834  C  C     . LYS   A 107 ? 0.2228 0.3754 0.2643 0.0002  0.0680  -0.0116 104 LYS   A C     
835  O  O     . LYS   A 107 ? 0.2337 0.3910 0.2885 -0.0022 0.0682  -0.0097 104 LYS   A O     
836  C  CB    . LYS   A 107 ? 0.1936 0.3136 0.2314 0.0021  0.0547  -0.0112 104 LYS   A CB    
837  C  CG    . LYS   A 107 ? 0.1797 0.2838 0.2151 0.0063  0.0477  -0.0153 104 LYS   A CG    
838  C  CD    . LYS   A 107 ? 0.1720 0.2761 0.2179 0.0113  0.0450  -0.0215 104 LYS   A CD    
839  C  CE    . LYS   A 107 ? 0.1665 0.2551 0.2092 0.0151  0.0387  -0.0248 104 LYS   A CE    
840  N  NZ    . LYS   A 107 ? 0.1663 0.2548 0.2188 0.0206  0.0358  -0.0300 104 LYS   A NZ    
841  N  N     . ASP   A 108 ? 0.2237 0.3834 0.2539 -0.0027 0.0729  -0.0074 105 ASP   A N     
842  C  CA    . ASP   A 108 ? 0.2394 0.4135 0.2719 -0.0095 0.0799  0.0008  105 ASP   A CA    
843  C  C     . ASP   A 108 ? 0.2488 0.4134 0.2900 -0.0160 0.0766  0.0096  105 ASP   A C     
844  O  O     . ASP   A 108 ? 0.2563 0.4309 0.3092 -0.0203 0.0801  0.0126  105 ASP   A O     
845  C  CB    . ASP   A 108 ? 0.2457 0.4413 0.2882 -0.0073 0.0869  -0.0052 105 ASP   A CB    
846  C  CG    . ASP   A 108 ? 0.2669 0.4790 0.3147 -0.0151 0.0947  0.0033  105 ASP   A CG    
847  O  OD1   . ASP   A 108 ? 0.2695 0.4818 0.3061 -0.0204 0.0975  0.0124  105 ASP   A OD1   
848  O  OD2   . ASP   A 108 ? 0.2532 0.4775 0.3172 -0.0160 0.0974  0.0014  105 ASP   A OD2   
849  N  N     . SER   A 109 ? 0.2787 0.4244 0.3149 -0.0166 0.0698  0.0128  106 SER   A N     
850  C  CA    . SER   A 109 ? 0.3052 0.4412 0.3508 -0.0218 0.0661  0.0188  106 SER   A CA    
851  C  C     . SER   A 109 ? 0.3393 0.4580 0.3761 -0.0240 0.0612  0.0253  106 SER   A C     
852  O  O     . SER   A 109 ? 0.3409 0.4536 0.3665 -0.0200 0.0589  0.0230  106 SER   A O     
853  C  CB    . SER   A 109 ? 0.3091 0.4404 0.3656 -0.0179 0.0609  0.0115  106 SER   A CB    
854  O  OG    . SER   A 109 ? 0.3297 0.4526 0.3946 -0.0227 0.0571  0.0159  106 SER   A OG    
855  N  N     . GLU   A 110 ? 0.3592 0.4711 0.4023 -0.0300 0.0597  0.0328  107 GLU   A N     
856  C  CA    . GLU   A 110 ? 0.3903 0.4848 0.4284 -0.0314 0.0544  0.0381  107 GLU   A CA    
857  C  C     . GLU   A 110 ? 0.3658 0.4491 0.4102 -0.0286 0.0479  0.0320  107 GLU   A C     
858  O  O     . GLU   A 110 ? 0.3831 0.4530 0.4230 -0.0272 0.0430  0.0325  107 GLU   A O     
859  C  CB    . GLU   A 110 ? 0.4230 0.5146 0.4672 -0.0393 0.0557  0.0480  107 GLU   A CB    
860  C  CG    . GLU   A 110 ? 0.4516 0.5547 0.4904 -0.0436 0.0626  0.0563  107 GLU   A CG    
861  C  CD    . GLU   A 110 ? 0.4791 0.5757 0.5027 -0.0424 0.0614  0.0628  107 GLU   A CD    
862  O  OE1   . GLU   A 110 ? 0.5242 0.6293 0.5411 -0.0457 0.0664  0.0705  107 GLU   A OE1   
863  O  OE2   . GLU   A 110 ? 0.4875 0.5718 0.5062 -0.0383 0.0556  0.0602  107 GLU   A OE2   
864  N  N     . ASP   A 111 ? 0.3682 0.4585 0.4240 -0.0284 0.0481  0.0269  108 ASP   A N     
865  C  CA    . ASP   A 111 ? 0.3474 0.4293 0.4090 -0.0259 0.0421  0.0213  108 ASP   A CA    
866  C  C     . ASP   A 111 ? 0.3031 0.3818 0.3570 -0.0187 0.0397  0.0147  108 ASP   A C     
867  O  O     . ASP   A 111 ? 0.3105 0.3969 0.3692 -0.0151 0.0402  0.0089  108 ASP   A O     
868  C  CB    . ASP   A 111 ? 0.3618 0.4539 0.4381 -0.0275 0.0425  0.0180  108 ASP   A CB    
869  C  CG    . ASP   A 111 ? 0.3958 0.4862 0.4823 -0.0351 0.0420  0.0230  108 ASP   A CG    
870  O  OD1   . ASP   A 111 ? 0.3888 0.4702 0.4711 -0.0392 0.0422  0.0299  108 ASP   A OD1   
871  O  OD2   . ASP   A 111 ? 0.3907 0.4892 0.4900 -0.0369 0.0413  0.0200  108 ASP   A OD2   
872  N  N     . VAL   A 112 ? 0.2586 0.3259 0.3023 -0.0167 0.0366  0.0155  109 VAL   A N     
873  C  CA    . VAL   A 112 ? 0.2212 0.2844 0.2594 -0.0107 0.0338  0.0090  109 VAL   A CA    
874  C  C     . VAL   A 112 ? 0.1839 0.2334 0.2198 -0.0097 0.0280  0.0084  109 VAL   A C     
875  O  O     . VAL   A 112 ? 0.1729 0.2153 0.2035 -0.0111 0.0269  0.0122  109 VAL   A O     
876  C  CB    . VAL   A 112 ? 0.2312 0.2976 0.2589 -0.0080 0.0362  0.0075  109 VAL   A CB    
877  C  CG1   . VAL   A 112 ? 0.2361 0.2992 0.2618 -0.0024 0.0336  0.0000  109 VAL   A CG1   
878  C  CG2   . VAL   A 112 ? 0.2479 0.3291 0.2758 -0.0093 0.0426  0.0086  109 VAL   A CG2   
879  N  N     . PRO   A 113 ? 0.1595 0.2058 0.1991 -0.0068 0.0245  0.0037  110 PRO   A N     
880  C  CA    . PRO   A 113 ? 0.1494 0.1846 0.1858 -0.0059 0.0198  0.0031  110 PRO   A CA    
881  C  C     . PRO   A 113 ? 0.1564 0.1863 0.1830 -0.0038 0.0193  0.0026  110 PRO   A C     
882  O  O     . PRO   A 113 ? 0.1263 0.1581 0.1503 -0.0008 0.0199  -0.0008 110 PRO   A O     
883  C  CB    . PRO   A 113 ? 0.1477 0.1832 0.1888 -0.0029 0.0167  -0.0013 110 PRO   A CB    
884  C  CG    . PRO   A 113 ? 0.1484 0.1953 0.1989 -0.0036 0.0191  -0.0022 110 PRO   A CG    
885  C  CD    . PRO   A 113 ? 0.1588 0.2129 0.2068 -0.0046 0.0245  -0.0005 110 PRO   A CD    
886  N  N     . MET   A 114 ? 0.1594 0.1824 0.1823 -0.0053 0.0178  0.0057  111 MET   A N     
887  C  CA    . MET   A 114 ? 0.1620 0.1811 0.1769 -0.0039 0.0169  0.0057  111 MET   A CA    
888  C  C     . MET   A 114 ? 0.1517 0.1630 0.1659 -0.0044 0.0139  0.0071  111 MET   A C     
889  O  O     . MET   A 114 ? 0.1310 0.1400 0.1494 -0.0063 0.0134  0.0091  111 MET   A O     
890  C  CB    . MET   A 114 ? 0.1956 0.2192 0.2056 -0.0050 0.0195  0.0092  111 MET   A CB    
891  C  CG    . MET   A 114 ? 0.2304 0.2635 0.2387 -0.0041 0.0232  0.0071  111 MET   A CG    
892  S  SD    . MET   A 114 ? 0.3231 0.3620 0.3215 -0.0048 0.0256  0.0106  111 MET   A SD    
893  C  CE    . MET   A 114 ? 0.2623 0.2920 0.2574 -0.0051 0.0213  0.0144  111 MET   A CE    
894  N  N     . VAL   A 115 ? 0.1334 0.1412 0.1432 -0.0028 0.0122  0.0052  112 VAL   A N     
895  C  CA    . VAL   A 115 ? 0.1180 0.1207 0.1268 -0.0029 0.0101  0.0061  112 VAL   A CA    
896  C  C     . VAL   A 115 ? 0.1147 0.1186 0.1181 -0.0022 0.0099  0.0067  112 VAL   A C     
897  O  O     . VAL   A 115 ? 0.1112 0.1171 0.1114 -0.0014 0.0101  0.0039  112 VAL   A O     
898  C  CB    . VAL   A 115 ? 0.1178 0.1170 0.1273 -0.0021 0.0081  0.0031  112 VAL   A CB    
899  C  CG1   . VAL   A 115 ? 0.1219 0.1181 0.1300 -0.0018 0.0068  0.0033  112 VAL   A CG1   
900  C  CG2   . VAL   A 115 ? 0.1148 0.1139 0.1293 -0.0027 0.0075  0.0024  112 VAL   A CG2   
901  N  N     . LEU   A 116 ? 0.1104 0.1133 0.1135 -0.0023 0.0091  0.0100  113 LEU   A N     
902  C  CA    . LEU   A 116 ? 0.1144 0.1192 0.1133 -0.0014 0.0078  0.0105  113 LEU   A CA    
903  C  C     . LEU   A 116 ? 0.1207 0.1232 0.1208 -0.0008 0.0060  0.0078  113 LEU   A C     
904  O  O     . LEU   A 116 ? 0.1115 0.1109 0.1153 -0.0004 0.0054  0.0079  113 LEU   A O     
905  C  CB    . LEU   A 116 ? 0.1239 0.1291 0.1221 -0.0013 0.0073  0.0160  113 LEU   A CB    
906  C  CG    . LEU   A 116 ? 0.1217 0.1302 0.1162 0.0001  0.0051  0.0171  113 LEU   A CG    
907  C  CD1   . LEU   A 116 ? 0.1219 0.1362 0.1099 -0.0003 0.0058  0.0150  113 LEU   A CD1   
908  C  CD2   . LEU   A 116 ? 0.1263 0.1337 0.1211 0.0009  0.0037  0.0235  113 LEU   A CD2   
909  N  N     . VAL   A 117 ? 0.1127 0.1173 0.1101 -0.0009 0.0053  0.0050  114 VAL   A N     
910  C  CA    . VAL   A 117 ? 0.1095 0.1133 0.1084 -0.0013 0.0041  0.0029  114 VAL   A CA    
911  C  C     . VAL   A 117 ? 0.1087 0.1169 0.1067 -0.0012 0.0023  0.0029  114 VAL   A C     
912  O  O     . VAL   A 117 ? 0.1105 0.1214 0.1052 -0.0017 0.0017  0.0013  114 VAL   A O     
913  C  CB    . VAL   A 117 ? 0.1125 0.1138 0.1108 -0.0024 0.0044  -0.0002 114 VAL   A CB    
914  C  CG1   . VAL   A 117 ? 0.1171 0.1184 0.1167 -0.0038 0.0037  -0.0013 114 VAL   A CG1   
915  C  CG2   . VAL   A 117 ? 0.1279 0.1259 0.1275 -0.0020 0.0054  -0.0001 114 VAL   A CG2   
916  N  N     . GLY   A 118 ? 0.1004 0.1101 0.1019 -0.0002 0.0014  0.0039  115 GLY   A N     
917  C  CA    . GLY   A 118 ? 0.1057 0.1212 0.1084 -0.0001 -0.0008 0.0033  115 GLY   A CA    
918  C  C     . GLY   A 118 ? 0.0937 0.1102 0.0991 -0.0023 -0.0003 0.0003  115 GLY   A C     
919  O  O     . GLY   A 118 ? 0.0856 0.1026 0.0947 -0.0018 0.0007  0.0002  115 GLY   A O     
920  N  N     . ASN   A 119 ? 0.0913 0.1084 0.0951 -0.0049 -0.0009 -0.0022 116 ASN   A N     
921  C  CA    . ASN   A 119 ? 0.0926 0.1099 0.0991 -0.0080 -0.0004 -0.0040 116 ASN   A CA    
922  C  C     . ASN   A 119 ? 0.0890 0.1145 0.1001 -0.0094 -0.0022 -0.0052 116 ASN   A C     
923  O  O     . ASN   A 119 ? 0.0892 0.1202 0.1007 -0.0075 -0.0045 -0.0048 116 ASN   A O     
924  C  CB    . ASN   A 119 ? 0.1023 0.1139 0.1059 -0.0103 -0.0004 -0.0063 116 ASN   A CB    
925  C  CG    . ASN   A 119 ? 0.1006 0.1097 0.1067 -0.0141 0.0003  -0.0067 116 ASN   A CG    
926  O  OD1   . ASN   A 119 ? 0.1139 0.1225 0.1212 -0.0144 0.0022  -0.0047 116 ASN   A OD1   
927  N  ND2   . ASN   A 119 ? 0.1144 0.1217 0.1212 -0.0172 -0.0012 -0.0095 116 ASN   A ND2   
928  N  N     . LYS   A 120 ? 0.0949 0.1216 0.1095 -0.0129 -0.0011 -0.0060 117 LYS   A N     
929  C  CA    . LYS   A 120 ? 0.0955 0.1315 0.1166 -0.0151 -0.0021 -0.0071 117 LYS   A CA    
930  C  C     . LYS   A 120 ? 0.0884 0.1321 0.1145 -0.0115 -0.0015 -0.0061 117 LYS   A C     
931  O  O     . LYS   A 120 ? 0.0847 0.1378 0.1164 -0.0110 -0.0037 -0.0069 117 LYS   A O     
932  C  CB    . LYS   A 120 ? 0.1006 0.1404 0.1218 -0.0167 -0.0059 -0.0098 117 LYS   A CB    
933  C  CG    . LYS   A 120 ? 0.1057 0.1375 0.1220 -0.0190 -0.0066 -0.0123 117 LYS   A CG    
934  C  CD    . LYS   A 120 ? 0.1084 0.1450 0.1259 -0.0217 -0.0105 -0.0166 117 LYS   A CD    
935  C  CE    . LYS   A 120 ? 0.1150 0.1433 0.1279 -0.0233 -0.0113 -0.0205 117 LYS   A CE    
936  N  NZ    . LYS   A 120 ? 0.1267 0.1588 0.1414 -0.0268 -0.0153 -0.0261 117 LYS   A NZ    
937  N  N     . SER   A 121 ? 0.0925 0.1324 0.1172 -0.0088 0.0010  -0.0047 118 SER   A N     
938  C  CA    . SER   A 121 ? 0.0965 0.1420 0.1263 -0.0048 0.0018  -0.0048 118 SER   A CA    
939  C  C     . SER   A 121 ? 0.1018 0.1586 0.1393 -0.0065 0.0035  -0.0064 118 SER   A C     
940  O  O     . SER   A 121 ? 0.1109 0.1753 0.1547 -0.0025 0.0033  -0.0074 118 SER   A O     
941  C  CB    . SER   A 121 ? 0.0935 0.1321 0.1200 -0.0024 0.0041  -0.0044 118 SER   A CB    
942  O  OG    . SER   A 121 ? 0.0940 0.1323 0.1188 -0.0056 0.0073  -0.0048 118 SER   A OG    
943  N  N     . ASP   A 122 ? 0.1029 0.1608 0.1404 -0.0123 0.0052  -0.0065 119 ASP   A N     
944  C  CA    . ASP   A 122 ? 0.1078 0.1776 0.1531 -0.0157 0.0071  -0.0075 119 ASP   A CA    
945  C  C     . ASP   A 122 ? 0.1097 0.1901 0.1631 -0.0161 0.0037  -0.0091 119 ASP   A C     
946  O  O     . ASP   A 122 ? 0.1123 0.2052 0.1743 -0.0180 0.0052  -0.0103 119 ASP   A O     
947  C  CB    . ASP   A 122 ? 0.1149 0.1810 0.1579 -0.0228 0.0095  -0.0059 119 ASP   A CB    
948  C  CG    . ASP   A 122 ? 0.1233 0.1816 0.1636 -0.0265 0.0061  -0.0061 119 ASP   A CG    
949  O  OD1   . ASP   A 122 ? 0.1279 0.1749 0.1608 -0.0246 0.0049  -0.0056 119 ASP   A OD1   
950  O  OD2   . ASP   A 122 ? 0.1346 0.1987 0.1808 -0.0311 0.0046  -0.0074 119 ASP   A OD2   
951  N  N     . LEU   A 123 ? 0.1046 0.1816 0.1552 -0.0147 -0.0009 -0.0093 120 LEU   A N     
952  C  CA    . LEU   A 123 ? 0.1094 0.1969 0.1665 -0.0152 -0.0051 -0.0110 120 LEU   A CA    
953  C  C     . LEU   A 123 ? 0.1102 0.2055 0.1724 -0.0079 -0.0074 -0.0107 120 LEU   A C     
954  O  O     . LEU   A 123 ? 0.1136 0.2016 0.1707 -0.0026 -0.0084 -0.0087 120 LEU   A O     
955  C  CB    . LEU   A 123 ? 0.1130 0.1945 0.1636 -0.0168 -0.0093 -0.0118 120 LEU   A CB    
956  C  CG    . LEU   A 123 ? 0.1170 0.1913 0.1648 -0.0238 -0.0085 -0.0133 120 LEU   A CG    
957  C  CD1   . LEU   A 123 ? 0.1199 0.1900 0.1618 -0.0241 -0.0128 -0.0157 120 LEU   A CD1   
958  C  CD2   . LEU   A 123 ? 0.1221 0.2044 0.1790 -0.0305 -0.0075 -0.0147 120 LEU   A CD2   
959  N  N     . PRO   A 124 ? 0.1092 0.2192 0.1824 -0.0077 -0.0084 -0.0124 121 PRO   A N     
960  C  CA    . PRO   A 124 ? 0.1096 0.2272 0.1896 0.0001  -0.0103 -0.0122 121 PRO   A CA    
961  C  C     . PRO   A 124 ? 0.1126 0.2300 0.1903 0.0048  -0.0170 -0.0102 121 PRO   A C     
962  O  O     . PRO   A 124 ? 0.1201 0.2370 0.2000 0.0120  -0.0186 -0.0084 121 PRO   A O     
963  C  CB    . PRO   A 124 ? 0.1077 0.2432 0.2013 -0.0017 -0.0090 -0.0151 121 PRO   A CB    
964  C  CG    . PRO   A 124 ? 0.1085 0.2466 0.2026 -0.0109 -0.0092 -0.0162 121 PRO   A CG    
965  C  CD    . PRO   A 124 ? 0.1073 0.2279 0.1886 -0.0147 -0.0071 -0.0145 121 PRO   A CD    
966  N  N     . SER   A 125 ? 0.1119 0.2300 0.1855 0.0009  -0.0210 -0.0107 122 SER   A N     
967  C  CA    . SER   A 125 ? 0.1218 0.2417 0.1918 0.0051  -0.0275 -0.0084 122 SER   A CA    
968  C  C     . SER   A 125 ? 0.1318 0.2370 0.1880 0.0064  -0.0275 -0.0050 122 SER   A C     
969  O  O     . SER   A 125 ? 0.1387 0.2416 0.1871 0.0034  -0.0295 -0.0058 122 SER   A O     
970  C  CB    . SER   A 125 ? 0.1218 0.2533 0.1952 0.0014  -0.0326 -0.0114 122 SER   A CB    
971  O  OG    . SER   A 125 ? 0.1259 0.2733 0.2138 0.0017  -0.0335 -0.0137 122 SER   A OG    
972  N  N     . ARG   A 126 ? 0.1341 0.2309 0.1886 0.0111  -0.0251 -0.0018 123 ARG   A N     
973  C  CA    . ARG   A 126 ? 0.1373 0.2209 0.1808 0.0124  -0.0244 0.0021  123 ARG   A CA    
974  C  C     . ARG   A 126 ? 0.1459 0.2317 0.1838 0.0156  -0.0300 0.0063  123 ARG   A C     
975  O  O     . ARG   A 126 ? 0.1435 0.2378 0.1876 0.0198  -0.0344 0.0078  123 ARG   A O     
976  C  CB    . ARG   A 126 ? 0.1390 0.2155 0.1858 0.0166  -0.0212 0.0037  123 ARG   A CB    
977  C  CG    . ARG   A 126 ? 0.1541 0.2185 0.1936 0.0192  -0.0211 0.0086  123 ARG   A CG    
978  C  CD    . ARG   A 126 ? 0.1530 0.2106 0.1975 0.0235  -0.0191 0.0093  123 ARG   A CD    
979  N  NE    . ARG   A 126 ? 0.1521 0.2070 0.1978 0.0209  -0.0140 0.0050  123 ARG   A NE    
980  C  CZ    . ARG   A 126 ? 0.1485 0.1943 0.1874 0.0175  -0.0108 0.0050  123 ARG   A CZ    
981  N  NH1   . ARG   A 126 ? 0.1443 0.1837 0.1754 0.0162  -0.0117 0.0086  123 ARG   A NH1   
982  N  NH2   . ARG   A 126 ? 0.1447 0.1891 0.1845 0.0157  -0.0069 0.0014  123 ARG   A NH2   
983  N  N     . THR   A 127 ? 0.1521 0.2314 0.1784 0.0136  -0.0299 0.0079  124 THR   A N     
984  C  CA    . THR   A 127 ? 0.1613 0.2425 0.1798 0.0163  -0.0344 0.0129  124 THR   A CA    
985  C  C     . THR   A 127 ? 0.1627 0.2322 0.1742 0.0181  -0.0318 0.0189  124 THR   A C     
986  O  O     . THR   A 127 ? 0.1686 0.2384 0.1747 0.0208  -0.0348 0.0249  124 THR   A O     
987  C  CB    . THR   A 127 ? 0.1705 0.2579 0.1809 0.0126  -0.0371 0.0096  124 THR   A CB    
988  O  OG1   . THR   A 127 ? 0.1705 0.2500 0.1739 0.0083  -0.0326 0.0065  124 THR   A OG1   
989  C  CG2   . THR   A 127 ? 0.1750 0.2743 0.1932 0.0100  -0.0405 0.0036  124 THR   A CG2   
990  N  N     . VAL   A 128 ? 0.1596 0.2198 0.1709 0.0158  -0.0263 0.0173  125 VAL   A N     
991  C  CA    . VAL   A 128 ? 0.1672 0.2168 0.1740 0.0168  -0.0237 0.0226  125 VAL   A CA    
992  C  C     . VAL   A 128 ? 0.1759 0.2189 0.1913 0.0198  -0.0222 0.0235  125 VAL   A C     
993  O  O     . VAL   A 128 ? 0.1640 0.2050 0.1840 0.0183  -0.0188 0.0187  125 VAL   A O     
994  C  CB    . VAL   A 128 ? 0.1627 0.2070 0.1628 0.0123  -0.0192 0.0199  125 VAL   A CB    
995  C  CG1   . VAL   A 128 ? 0.1582 0.1937 0.1548 0.0126  -0.0165 0.0252  125 VAL   A CG1   
996  C  CG2   . VAL   A 128 ? 0.1593 0.2101 0.1514 0.0097  -0.0207 0.0170  125 VAL   A CG2   
997  N  N     . ASP   A 129 ? 0.2067 0.2462 0.2239 0.0242  -0.0248 0.0298  126 ASP   A N     
998  C  CA    . ASP   A 129 ? 0.2358 0.2677 0.2613 0.0278  -0.0240 0.0305  126 ASP   A CA    
999  C  C     . ASP   A 129 ? 0.2371 0.2591 0.2608 0.0246  -0.0192 0.0290  126 ASP   A C     
1000 O  O     . ASP   A 129 ? 0.2228 0.2405 0.2392 0.0216  -0.0176 0.0326  126 ASP   A O     
1001 C  CB    . ASP   A 129 ? 0.2766 0.3039 0.3029 0.0324  -0.0281 0.0389  126 ASP   A CB    
1002 C  CG    . ASP   A 129 ? 0.3386 0.3606 0.3764 0.0380  -0.0293 0.0382  126 ASP   A CG    
1003 O  OD1   . ASP   A 129 ? 0.3832 0.4022 0.4265 0.0376  -0.0257 0.0318  126 ASP   A OD1   
1004 O  OD2   . ASP   A 129 ? 0.4113 0.4323 0.4527 0.0433  -0.0342 0.0441  126 ASP   A OD2   
1005 N  N     . THR   A 130 ? 0.2286 0.2481 0.2590 0.0252  -0.0168 0.0237  127 THR   A N     
1006 C  CA    . THR   A 130 ? 0.2396 0.2499 0.2693 0.0228  -0.0130 0.0219  127 THR   A CA    
1007 C  C     . THR   A 130 ? 0.2435 0.2435 0.2725 0.0234  -0.0137 0.0283  127 THR   A C     
1008 O  O     . THR   A 130 ? 0.2301 0.2249 0.2553 0.0196  -0.0111 0.0292  127 THR   A O     
1009 C  CB    . THR   A 130 ? 0.2510 0.2610 0.2880 0.0247  -0.0111 0.0155  127 THR   A CB    
1010 O  OG1   . THR   A 130 ? 0.2659 0.2855 0.3033 0.0229  -0.0096 0.0105  127 THR   A OG1   
1011 C  CG2   . THR   A 130 ? 0.2663 0.2679 0.3019 0.0222  -0.0081 0.0133  127 THR   A CG2   
1012 N  N     . LYS   A 131 ? 0.2470 0.2443 0.2802 0.0279  -0.0174 0.0333  128 LYS   A N     
1013 C  CA    . LYS   A 131 ? 0.2797 0.2663 0.3128 0.0280  -0.0185 0.0407  128 LYS   A CA    
1014 C  C     . LYS   A 131 ? 0.2745 0.2621 0.2975 0.0234  -0.0172 0.0470  128 LYS   A C     
1015 O  O     . LYS   A 131 ? 0.2671 0.2472 0.2889 0.0200  -0.0150 0.0507  128 LYS   A O     
1016 C  CB    . LYS   A 131 ? 0.3164 0.2999 0.3557 0.0342  -0.0234 0.0458  128 LYS   A CB    
1017 C  CG    . LYS   A 131 ? 0.3763 0.3506 0.4130 0.0339  -0.0256 0.0569  128 LYS   A CG    
1018 C  CD    . LYS   A 131 ? 0.4235 0.3959 0.4657 0.0409  -0.0315 0.0628  128 LYS   A CD    
1019 C  CE    . LYS   A 131 ? 0.4455 0.4026 0.4908 0.0417  -0.0336 0.0721  128 LYS   A CE    
1020 N  NZ    . LYS   A 131 ? 0.4607 0.4144 0.4964 0.0349  -0.0310 0.0805  128 LYS   A NZ    
1021 N  N     . GLN   A 132 ? 0.2504 0.2483 0.2667 0.0231  -0.0184 0.0478  129 GLN   A N     
1022 C  CA    . GLN   A 132 ? 0.2536 0.2550 0.2595 0.0193  -0.0171 0.0525  129 GLN   A CA    
1023 C  C     . GLN   A 132 ? 0.2124 0.2137 0.2152 0.0144  -0.0120 0.0475  129 GLN   A C     
1024 O  O     . GLN   A 132 ? 0.2054 0.2050 0.2035 0.0111  -0.0094 0.0516  129 GLN   A O     
1025 C  CB    . GLN   A 132 ? 0.2814 0.2945 0.2810 0.0205  -0.0202 0.0525  129 GLN   A CB    
1026 C  CG    . GLN   A 132 ? 0.3301 0.3446 0.3315 0.0256  -0.0260 0.0592  129 GLN   A CG    
1027 C  CD    . GLN   A 132 ? 0.3458 0.3720 0.3384 0.0260  -0.0295 0.0612  129 GLN   A CD    
1028 O  OE1   . GLN   A 132 ? 0.4468 0.4754 0.4392 0.0300  -0.0348 0.0677  129 GLN   A OE1   
1029 N  NE2   . GLN   A 132 ? 0.3891 0.4226 0.3745 0.0221  -0.0271 0.0555  129 GLN   A NE2   
1030 N  N     . ALA   A 133 ? 0.1717 0.1755 0.1775 0.0140  -0.0107 0.0392  130 ALA   A N     
1031 C  CA    . ALA   A 133 ? 0.1597 0.1636 0.1631 0.0101  -0.0067 0.0344  130 ALA   A CA    
1032 C  C     . ALA   A 133 ? 0.1472 0.1423 0.1550 0.0085  -0.0044 0.0353  130 ALA   A C     
1033 O  O     . ALA   A 133 ? 0.1391 0.1339 0.1441 0.0052  -0.0015 0.0358  130 ALA   A O     
1034 C  CB    . ALA   A 133 ? 0.1495 0.1574 0.1549 0.0100  -0.0063 0.0267  130 ALA   A CB    
1035 N  N     . GLN   A 134 ? 0.1488 0.1373 0.1640 0.0110  -0.0060 0.0352  131 GLN   A N     
1036 C  CA    . GLN   A 134 ? 0.1514 0.1307 0.1718 0.0094  -0.0047 0.0356  131 GLN   A CA    
1037 C  C     . GLN   A 134 ? 0.1594 0.1350 0.1780 0.0068  -0.0042 0.0441  131 GLN   A C     
1038 O  O     . GLN   A 134 ? 0.1565 0.1295 0.1761 0.0030  -0.0017 0.0446  131 GLN   A O     
1039 C  CB    . GLN   A 134 ? 0.1596 0.1323 0.1884 0.0132  -0.0069 0.0330  131 GLN   A CB    
1040 C  CG    . GLN   A 134 ? 0.1571 0.1342 0.1881 0.0150  -0.0063 0.0243  131 GLN   A CG    
1041 C  CD    . GLN   A 134 ? 0.1575 0.1289 0.1967 0.0190  -0.0078 0.0204  131 GLN   A CD    
1042 O  OE1   . GLN   A 134 ? 0.1672 0.1319 0.2113 0.0218  -0.0104 0.0245  131 GLN   A OE1   
1043 N  NE2   . GLN   A 134 ? 0.1549 0.1288 0.1957 0.0193  -0.0062 0.0126  131 GLN   A NE2   
1044 N  N     A ASP   A 135 ? 0.1667 0.1428 0.1825 0.0089  -0.0067 0.0514  132 ASP   A N     
1045 N  N     B ASP   A 135 ? 0.1724 0.1486 0.1884 0.0090  -0.0068 0.0513  132 ASP   A N     
1046 C  CA    A ASP   A 135 ? 0.1780 0.1512 0.1910 0.0060  -0.0060 0.0611  132 ASP   A CA    
1047 C  CA    B ASP   A 135 ? 0.1878 0.1616 0.2002 0.0063  -0.0062 0.0612  132 ASP   A CA    
1048 C  C     A ASP   A 135 ? 0.1757 0.1575 0.1805 0.0017  -0.0019 0.0617  132 ASP   A C     
1049 C  C     B ASP   A 135 ? 0.1808 0.1625 0.1859 0.0017  -0.0019 0.0614  132 ASP   A C     
1050 O  O     A ASP   A 135 ? 0.1768 0.1567 0.1819 -0.0025 0.0009  0.0665  132 ASP   A O     
1051 O  O     B ASP   A 135 ? 0.1813 0.1606 0.1872 -0.0024 0.0009  0.0657  132 ASP   A O     
1052 C  CB    A ASP   A 135 ? 0.1868 0.1594 0.1973 0.0095  -0.0101 0.0696  132 ASP   A CB    
1053 C  CB    B ASP   A 135 ? 0.2022 0.1782 0.2105 0.0099  -0.0101 0.0686  132 ASP   A CB    
1054 C  CG    A ASP   A 135 ? 0.1982 0.1691 0.2034 0.0061  -0.0089 0.0810  132 ASP   A CG    
1055 C  CG    B ASP   A 135 ? 0.2170 0.1827 0.2337 0.0141  -0.0142 0.0720  132 ASP   A CG    
1056 O  OD1   A ASP   A 135 ? 0.2045 0.1656 0.2154 0.0031  -0.0078 0.0855  132 ASP   A OD1   
1057 O  OD1   B ASP   A 135 ? 0.2306 0.1855 0.2548 0.0126  -0.0135 0.0720  132 ASP   A OD1   
1058 O  OD2   A ASP   A 135 ? 0.2029 0.1829 0.1980 0.0059  -0.0090 0.0855  132 ASP   A OD2   
1059 O  OD2   B ASP   A 135 ? 0.2244 0.1927 0.2410 0.0191  -0.0185 0.0743  132 ASP   A OD2   
1060 N  N     . LEU   A 136 ? 0.1738 0.1652 0.1724 0.0025  -0.0014 0.0565  133 LEU   A N     
1061 C  CA    . LEU   A 136 ? 0.1784 0.1779 0.1701 -0.0008 0.0025  0.0555  133 LEU   A CA    
1062 C  C     . LEU   A 136 ? 0.1739 0.1712 0.1712 -0.0038 0.0060  0.0506  133 LEU   A C     
1063 O  O     . LEU   A 136 ? 0.1754 0.1750 0.1721 -0.0074 0.0095  0.0536  133 LEU   A O     
1064 C  CB    . LEU   A 136 ? 0.1755 0.1840 0.1604 0.0009  0.0018  0.0498  133 LEU   A CB    
1065 C  CG    . LEU   A 136 ? 0.1833 0.2004 0.1606 -0.0015 0.0055  0.0483  133 LEU   A CG    
1066 C  CD1   . LEU   A 136 ? 0.1981 0.2202 0.1674 -0.0027 0.0064  0.0570  133 LEU   A CD1   
1067 C  CD2   . LEU   A 136 ? 0.1747 0.1981 0.1479 0.0000  0.0043  0.0401  133 LEU   A CD2   
1068 N  N     . ALA   A 137 ? 0.1692 0.1631 0.1718 -0.0024 0.0050  0.0433  134 ALA   A N     
1069 C  CA    . ALA   A 137 ? 0.1701 0.1618 0.1782 -0.0046 0.0071  0.0385  134 ALA   A CA    
1070 C  C     . ALA   A 137 ? 0.1818 0.1672 0.1963 -0.0078 0.0079  0.0432  134 ALA   A C     
1071 O  O     . ALA   A 137 ? 0.1758 0.1638 0.1926 -0.0112 0.0107  0.0427  134 ALA   A O     
1072 C  CB    . ALA   A 137 ? 0.1560 0.1450 0.1676 -0.0024 0.0053  0.0312  134 ALA   A CB    
1073 N  N     . ARG   A 138 ? 0.1980 0.1753 0.2162 -0.0066 0.0053  0.0477  135 ARG   A N     
1074 C  CA    . ARG   A 138 ? 0.2218 0.1913 0.2465 -0.0100 0.0056  0.0532  135 ARG   A CA    
1075 C  C     . ARG   A 138 ? 0.2229 0.1979 0.2437 -0.0145 0.0091  0.0612  135 ARG   A C     
1076 O  O     . ARG   A 138 ? 0.2331 0.2078 0.2593 -0.0193 0.0116  0.0624  135 ARG   A O     
1077 C  CB    . ARG   A 138 ? 0.2542 0.2131 0.2831 -0.0072 0.0017  0.0573  135 ARG   A CB    
1078 C  CG    . ARG   A 138 ? 0.2890 0.2366 0.3271 -0.0107 0.0012  0.0609  135 ARG   A CG    
1079 C  CD    . ARG   A 138 ? 0.3220 0.2571 0.3666 -0.0068 -0.0032 0.0622  135 ARG   A CD    
1080 N  NE    . ARG   A 138 ? 0.3514 0.2875 0.3970 -0.0010 -0.0054 0.0530  135 ARG   A NE    
1081 C  CZ    . ARG   A 138 ? 0.3738 0.3130 0.4162 0.0046  -0.0077 0.0534  135 ARG   A CZ    
1082 N  NH1   . ARG   A 138 ? 0.4006 0.3416 0.4380 0.0058  -0.0090 0.0626  135 ARG   A NH1   
1083 N  NH2   . ARG   A 138 ? 0.3756 0.3171 0.4200 0.0089  -0.0088 0.0446  135 ARG   A NH2   
1084 N  N     . SER   A 139 ? 0.2134 0.1948 0.2249 -0.0131 0.0094  0.0663  136 SER   A N     
1085 C  CA    . SER   A 139 ? 0.2243 0.2128 0.2304 -0.0172 0.0134  0.0742  136 SER   A CA    
1086 C  C     . SER   A 139 ? 0.2130 0.2120 0.2188 -0.0200 0.0182  0.0688  136 SER   A C     
1087 O  O     . SER   A 139 ? 0.2039 0.2079 0.2103 -0.0247 0.0224  0.0740  136 SER   A O     
1088 C  CB    . SER   A 139 ? 0.2392 0.2336 0.2338 -0.0147 0.0122  0.0799  136 SER   A CB    
1089 O  OG    . SER   A 139 ? 0.2393 0.2445 0.2266 -0.0127 0.0134  0.0727  136 SER   A OG    
1090 N  N     . TYR   A 140 ? 0.1999 0.2020 0.2057 -0.0172 0.0177  0.0588  137 TYR   A N     
1091 C  CA    . TYR   A 140 ? 0.2049 0.2154 0.2121 -0.0186 0.0213  0.0527  137 TYR   A CA    
1092 C  C     . TYR   A 140 ? 0.1904 0.1969 0.2086 -0.0210 0.0213  0.0488  137 TYR   A C     
1093 O  O     . TYR   A 140 ? 0.1888 0.2028 0.2104 -0.0227 0.0242  0.0455  137 TYR   A O     
1094 C  CB    . TYR   A 140 ? 0.2068 0.2219 0.2086 -0.0145 0.0203  0.0444  137 TYR   A CB    
1095 C  CG    . TYR   A 140 ? 0.2289 0.2503 0.2199 -0.0124 0.0203  0.0457  137 TYR   A CG    
1096 C  CD1   . TYR   A 140 ? 0.2428 0.2698 0.2275 -0.0142 0.0224  0.0535  137 TYR   A CD1   
1097 C  CD2   . TYR   A 140 ? 0.2311 0.2534 0.2182 -0.0089 0.0178  0.0391  137 TYR   A CD2   
1098 C  CE1   . TYR   A 140 ? 0.2678 0.3016 0.2414 -0.0121 0.0218  0.0540  137 TYR   A CE1   
1099 C  CE2   . TYR   A 140 ? 0.2494 0.2779 0.2270 -0.0072 0.0171  0.0391  137 TYR   A CE2   
1100 C  CZ    . TYR   A 140 ? 0.2640 0.2984 0.2345 -0.0085 0.0188  0.0462  137 TYR   A CZ    
1101 O  OH    . TYR   A 140 ? 0.2807 0.3224 0.2409 -0.0068 0.0176  0.0456  137 TYR   A OH    
1102 N  N     . GLY   A 141 ? 0.1760 0.1716 0.2002 -0.0208 0.0177  0.0487  138 GLY   A N     
1103 C  CA    . GLY   A 141 ? 0.1631 0.1547 0.1967 -0.0225 0.0167  0.0436  138 GLY   A CA    
1104 C  C     . GLY   A 141 ? 0.1494 0.1447 0.1822 -0.0194 0.0157  0.0344  138 GLY   A C     
1105 O  O     . GLY   A 141 ? 0.1408 0.1402 0.1789 -0.0211 0.0165  0.0306  138 GLY   A O     
1106 N  N     . ILE   A 142 ? 0.1334 0.1275 0.1598 -0.0151 0.0138  0.0316  139 ILE   A N     
1107 C  CA    . ILE   A 142 ? 0.1247 0.1211 0.1495 -0.0123 0.0128  0.0242  139 ILE   A CA    
1108 C  C     . ILE   A 142 ? 0.1218 0.1117 0.1458 -0.0094 0.0095  0.0211  139 ILE   A C     
1109 O  O     . ILE   A 142 ? 0.1340 0.1197 0.1574 -0.0082 0.0082  0.0243  139 ILE   A O     
1110 C  CB    . ILE   A 142 ? 0.1187 0.1226 0.1364 -0.0105 0.0146  0.0227  139 ILE   A CB    
1111 C  CG1   . ILE   A 142 ? 0.1274 0.1309 0.1381 -0.0083 0.0135  0.0248  139 ILE   A CG1   
1112 C  CG2   . ILE   A 142 ? 0.1267 0.1388 0.1453 -0.0129 0.0184  0.0248  139 ILE   A CG2   
1113 C  CD1   . ILE   A 142 ? 0.1222 0.1326 0.1259 -0.0069 0.0148  0.0226  139 ILE   A CD1   
1114 N  N     . PRO   A 143 ? 0.1133 0.1037 0.1372 -0.0079 0.0084  0.0152  140 PRO   A N     
1115 C  CA    . PRO   A 143 ? 0.1111 0.0978 0.1338 -0.0053 0.0063  0.0122  140 PRO   A CA    
1116 C  C     . PRO   A 143 ? 0.1093 0.0983 0.1264 -0.0031 0.0062  0.0131  140 PRO   A C     
1117 O  O     . PRO   A 143 ? 0.1093 0.1030 0.1222 -0.0034 0.0075  0.0142  140 PRO   A O     
1118 C  CB    . PRO   A 143 ? 0.1035 0.0915 0.1262 -0.0050 0.0055  0.0068  140 PRO   A CB    
1119 C  CG    . PRO   A 143 ? 0.1102 0.1001 0.1374 -0.0075 0.0061  0.0069  140 PRO   A CG    
1120 C  CD    . PRO   A 143 ? 0.1101 0.1038 0.1367 -0.0089 0.0087  0.0115  140 PRO   A CD    
1121 N  N     . PHE   A 144 ? 0.1112 0.0978 0.1289 -0.0009 0.0046  0.0118  141 PHE   A N     
1122 C  CA    . PHE   A 144 ? 0.1125 0.1026 0.1266 0.0010  0.0040  0.0119  141 PHE   A CA    
1123 C  C     . PHE   A 144 ? 0.1111 0.1018 0.1260 0.0024  0.0034  0.0073  141 PHE   A C     
1124 O  O     . PHE   A 144 ? 0.1147 0.1024 0.1332 0.0036  0.0028  0.0053  141 PHE   A O     
1125 C  CB    . PHE   A 144 ? 0.1233 0.1125 0.1382 0.0027  0.0025  0.0164  141 PHE   A CB    
1126 C  CG    . PHE   A 144 ? 0.1217 0.1156 0.1348 0.0047  0.0012  0.0156  141 PHE   A CG    
1127 C  CD1   . PHE   A 144 ? 0.1222 0.1214 0.1302 0.0037  0.0016  0.0146  141 PHE   A CD1   
1128 C  CD2   . PHE   A 144 ? 0.1330 0.1264 0.1503 0.0077  -0.0006 0.0148  141 PHE   A CD2   
1129 C  CE1   . PHE   A 144 ? 0.1335 0.1377 0.1408 0.0048  0.0000  0.0135  141 PHE   A CE1   
1130 C  CE2   . PHE   A 144 ? 0.1374 0.1369 0.1543 0.0093  -0.0019 0.0139  141 PHE   A CE2   
1131 C  CZ    . PHE   A 144 ? 0.1351 0.1400 0.1472 0.0075  -0.0017 0.0132  141 PHE   A CZ    
1132 N  N     . ILE   A 145 ? 0.1049 0.0994 0.1162 0.0019  0.0039  0.0056  142 ILE   A N     
1133 C  CA    . ILE   A 145 ? 0.1010 0.0976 0.1122 0.0022  0.0041  0.0022  142 ILE   A CA    
1134 C  C     . ILE   A 145 ? 0.0910 0.0924 0.1008 0.0020  0.0037  0.0023  142 ILE   A C     
1135 O  O     . ILE   A 145 ? 0.0912 0.0936 0.0982 0.0007  0.0036  0.0030  142 ILE   A O     
1136 C  CB    . ILE   A 145 ? 0.1060 0.1015 0.1148 0.0006  0.0048  0.0003  142 ILE   A CB    
1137 C  CG1   . ILE   A 145 ? 0.1090 0.1013 0.1199 0.0006  0.0045  -0.0006 142 ILE   A CG1   
1138 C  CG2   . ILE   A 145 ? 0.0984 0.0963 0.1054 0.0001  0.0054  -0.0016 142 ILE   A CG2   
1139 C  CD1   . ILE   A 145 ? 0.1251 0.1171 0.1341 -0.0004 0.0043  -0.0018 142 ILE   A CD1   
1140 N  N     . GLU   A 146 ? 0.0945 0.0994 0.1072 0.0032  0.0036  0.0009  143 GLU   A N     
1141 C  CA    . GLU   A 146 ? 0.0965 0.1072 0.1094 0.0021  0.0033  0.0003  143 GLU   A CA    
1142 C  C     . GLU   A 146 ? 0.0966 0.1083 0.1081 -0.0005 0.0050  -0.0015 143 GLU   A C     
1143 O  O     . GLU   A 146 ? 0.0941 0.1058 0.1059 0.0000  0.0064  -0.0029 143 GLU   A O     
1144 C  CB    . GLU   A 146 ? 0.1044 0.1206 0.1224 0.0047  0.0022  0.0002  143 GLU   A CB    
1145 C  CG    . GLU   A 146 ? 0.1121 0.1276 0.1307 0.0070  -0.0003 0.0035  143 GLU   A CG    
1146 C  CD    . GLU   A 146 ? 0.1274 0.1494 0.1512 0.0100  -0.0025 0.0039  143 GLU   A CD    
1147 O  OE1   . GLU   A 146 ? 0.1405 0.1686 0.1684 0.0101  -0.0018 0.0011  143 GLU   A OE1   
1148 O  OE2   . GLU   A 146 ? 0.1322 0.1535 0.1561 0.0122  -0.0050 0.0073  143 GLU   A OE2   
1149 N  N     . THR   A 147 ? 0.0923 0.1047 0.1019 -0.0033 0.0048  -0.0014 144 THR   A N     
1150 C  CA    . THR   A 147 ? 0.1031 0.1149 0.1112 -0.0064 0.0062  -0.0018 144 THR   A CA    
1151 C  C     . THR   A 147 ? 0.1086 0.1256 0.1194 -0.0094 0.0061  -0.0022 144 THR   A C     
1152 O  O     . THR   A 147 ? 0.1069 0.1275 0.1200 -0.0090 0.0043  -0.0028 144 THR   A O     
1153 C  CB    . THR   A 147 ? 0.1079 0.1129 0.1121 -0.0076 0.0056  -0.0012 144 THR   A CB    
1154 O  OG1   . THR   A 147 ? 0.1156 0.1205 0.1195 -0.0080 0.0042  -0.0020 144 THR   A OG1   
1155 C  CG2   . THR   A 147 ? 0.1124 0.1133 0.1148 -0.0055 0.0057  -0.0009 144 THR   A CG2   
1156 N  N     . SER   A 148 ? 0.1176 0.1356 0.1283 -0.0125 0.0079  -0.0016 145 SER   A N     
1157 C  CA    . SER   A 148 ? 0.1253 0.1466 0.1390 -0.0170 0.0080  -0.0014 145 SER   A CA    
1158 C  C     . SER   A 148 ? 0.1330 0.1463 0.1431 -0.0206 0.0082  0.0005  145 SER   A C     
1159 O  O     . SER   A 148 ? 0.1377 0.1502 0.1453 -0.0216 0.0102  0.0027  145 SER   A O     
1160 C  CB    . SER   A 148 ? 0.1242 0.1555 0.1427 -0.0184 0.0103  -0.0016 145 SER   A CB    
1161 O  OG    . SER   A 148 ? 0.1330 0.1676 0.1553 -0.0237 0.0103  -0.0012 145 SER   A OG    
1162 N  N     . ALA   A 149 ? 0.1436 0.1514 0.1537 -0.0223 0.0061  -0.0004 146 ALA   A N     
1163 C  CA    . ALA   A 149 ? 0.1518 0.1508 0.1599 -0.0255 0.0059  0.0016  146 ALA   A CA    
1164 C  C     . ALA   A 149 ? 0.1708 0.1733 0.1823 -0.0313 0.0076  0.0040  146 ALA   A C     
1165 O  O     . ALA   A 149 ? 0.1900 0.1864 0.1995 -0.0342 0.0083  0.0077  146 ALA   A O     
1166 C  CB    . ALA   A 149 ? 0.1523 0.1444 0.1603 -0.0254 0.0031  -0.0013 146 ALA   A CB    
1167 N  N     . LYS   A 150 ? 0.1746 0.1875 0.1916 -0.0330 0.0082  0.0024  147 LYS   A N     
1168 C  CA    . LYS   A 150 ? 0.1911 0.2099 0.2131 -0.0392 0.0102  0.0044  147 LYS   A CA    
1169 C  C     . LYS   A 150 ? 0.2020 0.2258 0.2215 -0.0396 0.0144  0.0081  147 LYS   A C     
1170 O  O     . LYS   A 150 ? 0.2067 0.2282 0.2251 -0.0446 0.0163  0.0126  147 LYS   A O     
1171 C  CB    . LYS   A 150 ? 0.2013 0.2320 0.2315 -0.0406 0.0093  0.0010  147 LYS   A CB    
1172 C  CG    . LYS   A 150 ? 0.2187 0.2570 0.2560 -0.0480 0.0115  0.0029  147 LYS   A CG    
1173 C  CD    . LYS   A 150 ? 0.2324 0.2816 0.2791 -0.0505 0.0094  -0.0009 147 LYS   A CD    
1174 C  CE    . LYS   A 150 ? 0.2578 0.3157 0.3127 -0.0586 0.0123  0.0014  147 LYS   A CE    
1175 N  NZ    . LYS   A 150 ? 0.2703 0.3442 0.3358 -0.0596 0.0110  -0.0023 147 LYS   A NZ    
1176 N  N     . THR   A 151 ? 0.1908 0.2214 0.2092 -0.0343 0.0157  0.0062  148 THR   A N     
1177 C  CA    . THR   A 151 ? 0.1993 0.2358 0.2145 -0.0337 0.0196  0.0080  148 THR   A CA    
1178 C  C     . THR   A 151 ? 0.1911 0.2193 0.1974 -0.0303 0.0192  0.0096  148 THR   A C     
1179 O  O     . THR   A 151 ? 0.1928 0.2256 0.1948 -0.0298 0.0220  0.0106  148 THR   A O     
1180 C  CB    . THR   A 151 ? 0.2015 0.2502 0.2214 -0.0294 0.0212  0.0040  148 THR   A CB    
1181 O  OG1   . THR   A 151 ? 0.1915 0.2351 0.2094 -0.0231 0.0185  0.0012  148 THR   A OG1   
1182 C  CG2   . THR   A 151 ? 0.2074 0.2663 0.2371 -0.0319 0.0210  0.0022  148 THR   A CG2   
1183 N  N     . ARG   A 152 ? 0.1874 0.2051 0.1912 -0.0279 0.0158  0.0090  149 ARG   A N     
1184 C  CA    . ARG   A 152 ? 0.2033 0.2133 0.2003 -0.0245 0.0144  0.0100  149 ARG   A CA    
1185 C  C     . ARG   A 152 ? 0.2056 0.2197 0.2019 -0.0193 0.0146  0.0064  149 ARG   A C     
1186 O  O     . ARG   A 152 ? 0.2443 0.2546 0.2356 -0.0170 0.0137  0.0067  149 ARG   A O     
1187 C  CB    . ARG   A 152 ? 0.2396 0.2459 0.2306 -0.0274 0.0153  0.0153  149 ARG   A CB    
1188 C  CG    . ARG   A 152 ? 0.2758 0.2716 0.2620 -0.0250 0.0122  0.0172  149 ARG   A CG    
1189 C  CD    . ARG   A 152 ? 0.2996 0.2910 0.2805 -0.0284 0.0125  0.0239  149 ARG   A CD    
1190 N  NE    . ARG   A 152 ? 0.2966 0.2767 0.2758 -0.0263 0.0086  0.0259  149 ARG   A NE    
1191 C  CZ    . ARG   A 152 ? 0.3256 0.3044 0.3005 -0.0221 0.0066  0.0258  149 ARG   A CZ    
1192 N  NH1   . ARG   A 152 ? 0.3596 0.3295 0.3341 -0.0197 0.0031  0.0274  149 ARG   A NH1   
1193 N  NH2   . ARG   A 152 ? 0.3260 0.3131 0.2975 -0.0202 0.0081  0.0236  149 ARG   A NH2   
1194 N  N     . GLN   A 153 ? 0.1662 0.1864 0.1678 -0.0173 0.0149  0.0031  150 GLN   A N     
1195 C  CA    . GLN   A 153 ? 0.1678 0.1904 0.1702 -0.0124 0.0148  -0.0003 150 GLN   A CA    
1196 C  C     . GLN   A 153 ? 0.1301 0.1446 0.1311 -0.0097 0.0119  -0.0008 150 GLN   A C     
1197 O  O     . GLN   A 153 ? 0.1156 0.1273 0.1184 -0.0098 0.0103  -0.0006 150 GLN   A O     
1198 C  CB    . GLN   A 153 ? 0.1684 0.1987 0.1778 -0.0105 0.0152  -0.0030 150 GLN   A CB    
1199 C  CG    . GLN   A 153 ? 0.1990 0.2328 0.2098 -0.0059 0.0161  -0.0066 150 GLN   A CG    
1200 C  CD    . GLN   A 153 ? 0.2113 0.2537 0.2210 -0.0064 0.0198  -0.0083 150 GLN   A CD    
1201 O  OE1   . GLN   A 153 ? 0.2524 0.2944 0.2578 -0.0045 0.0206  -0.0105 150 GLN   A OE1   
1202 N  NE2   . GLN   A 153 ? 0.2268 0.2781 0.2404 -0.0093 0.0221  -0.0074 150 GLN   A NE2   
1203 N  N     . ARG   A 154 ? 0.1239 0.1358 0.1212 -0.0078 0.0116  -0.0016 151 ARG   A N     
1204 C  CA    . ARG   A 154 ? 0.1246 0.1305 0.1217 -0.0055 0.0094  -0.0023 151 ARG   A CA    
1205 C  C     . ARG   A 154 ? 0.1262 0.1262 0.1219 -0.0066 0.0077  0.0000  151 ARG   A C     
1206 O  O     . ARG   A 154 ? 0.1219 0.1189 0.1186 -0.0051 0.0065  -0.0005 151 ARG   A O     
1207 C  CB    . ARG   A 154 ? 0.1192 0.1259 0.1212 -0.0028 0.0088  -0.0042 151 ARG   A CB    
1208 C  CG    . ARG   A 154 ? 0.1204 0.1312 0.1247 -0.0004 0.0098  -0.0075 151 ARG   A CG    
1209 C  CD    . ARG   A 154 ? 0.1268 0.1344 0.1356 0.0025  0.0083  -0.0087 151 ARG   A CD    
1210 N  NE    . ARG   A 154 ? 0.1390 0.1413 0.1469 0.0028  0.0070  -0.0095 151 ARG   A NE    
1211 C  CZ    . ARG   A 154 ? 0.1506 0.1484 0.1623 0.0042  0.0056  -0.0096 151 ARG   A CZ    
1212 N  NH1   . ARG   A 154 ? 0.1683 0.1624 0.1797 0.0035  0.0045  -0.0104 151 ARG   A NH1   
1213 N  NH2   . ARG   A 154 ? 0.1511 0.1484 0.1670 0.0059  0.0051  -0.0084 151 ARG   A NH2   
1214 N  N     . VAL   A 155 ? 0.1376 0.1357 0.1309 -0.0093 0.0079  0.0024  152 VAL   A N     
1215 C  CA    . VAL   A 155 ? 0.1481 0.1396 0.1411 -0.0095 0.0061  0.0037  152 VAL   A CA    
1216 C  C     . VAL   A 155 ? 0.1502 0.1385 0.1409 -0.0074 0.0044  0.0041  152 VAL   A C     
1217 O  O     . VAL   A 155 ? 0.1389 0.1249 0.1315 -0.0056 0.0033  0.0031  152 VAL   A O     
1218 C  CB    . VAL   A 155 ? 0.1584 0.1471 0.1507 -0.0131 0.0062  0.0062  152 VAL   A CB    
1219 C  CG1   . VAL   A 155 ? 0.1598 0.1403 0.1518 -0.0124 0.0040  0.0069  152 VAL   A CG1   
1220 C  CG2   . VAL   A 155 ? 0.1527 0.1454 0.1488 -0.0154 0.0071  0.0050  152 VAL   A CG2   
1221 N  N     . GLU   A 156 ? 0.1651 0.1547 0.1518 -0.0076 0.0044  0.0055  153 GLU   A N     
1222 C  CA    . GLU   A 156 ? 0.1820 0.1702 0.1670 -0.0054 0.0021  0.0056  153 GLU   A CA    
1223 C  C     . GLU   A 156 ? 0.1645 0.1549 0.1531 -0.0033 0.0017  0.0019  153 GLU   A C     
1224 O  O     . GLU   A 156 ? 0.1394 0.1283 0.1310 -0.0018 0.0001  0.0012  153 GLU   A O     
1225 C  CB    . GLU   A 156 ? 0.2261 0.2167 0.2048 -0.0061 0.0019  0.0076  153 GLU   A CB    
1226 C  CG    . GLU   A 156 ? 0.2593 0.2465 0.2343 -0.0088 0.0022  0.0129  153 GLU   A CG    
1227 C  CD    . GLU   A 156 ? 0.3208 0.3095 0.2881 -0.0093 0.0014  0.0167  153 GLU   A CD    
1228 O  OE1   . GLU   A 156 ? 0.3962 0.3915 0.3597 -0.0087 0.0022  0.0144  153 GLU   A OE1   
1229 O  OE2   . GLU   A 156 ? 0.3786 0.3616 0.3433 -0.0103 -0.0002 0.0221  153 GLU   A OE2   
1230 N  N     . ASP   A 157 ? 0.1578 0.1519 0.1474 -0.0034 0.0033  -0.0004 154 ASP   A N     
1231 C  CA    . ASP   A 157 ? 0.1651 0.1598 0.1592 -0.0020 0.0031  -0.0032 154 ASP   A CA    
1232 C  C     . ASP   A 157 ? 0.1460 0.1385 0.1442 -0.0017 0.0028  -0.0026 154 ASP   A C     
1233 O  O     . ASP   A 157 ? 0.1397 0.1319 0.1409 -0.0011 0.0018  -0.0035 154 ASP   A O     
1234 C  CB    . ASP   A 157 ? 0.1975 0.1950 0.1934 -0.0018 0.0049  -0.0050 154 ASP   A CB    
1235 C  CG    . ASP   A 157 ? 0.2397 0.2373 0.2385 -0.0002 0.0044  -0.0084 154 ASP   A CG    
1236 O  OD1   . ASP   A 157 ? 0.2682 0.2630 0.2701 -0.0001 0.0029  -0.0086 154 ASP   A OD1   
1237 O  OD2   . ASP   A 157 ? 0.2501 0.2506 0.2490 0.0008  0.0055  -0.0111 154 ASP   A OD2   
1238 N  N     . ALA   A 158 ? 0.1307 0.1226 0.1292 -0.0023 0.0037  -0.0013 155 ALA   A N     
1239 C  CA    . ALA   A 158 ? 0.1285 0.1198 0.1294 -0.0019 0.0039  -0.0010 155 ALA   A CA    
1240 C  C     . ALA   A 158 ? 0.1194 0.1096 0.1212 -0.0010 0.0029  -0.0011 155 ALA   A C     
1241 O  O     . ALA   A 158 ? 0.1112 0.1030 0.1162 -0.0005 0.0032  -0.0015 155 ALA   A O     
1242 C  CB    . ALA   A 158 ? 0.1312 0.1229 0.1313 -0.0027 0.0045  -0.0007 155 ALA   A CB    
1243 N  N     . PHE   A 159 ? 0.1219 0.1096 0.1216 -0.0008 0.0018  -0.0004 156 PHE   A N     
1244 C  CA    . PHE   A 159 ? 0.1175 0.1041 0.1190 0.0011  0.0003  -0.0007 156 PHE   A CA    
1245 C  C     . PHE   A 159 ? 0.1126 0.1020 0.1162 0.0019  -0.0012 -0.0012 156 PHE   A C     
1246 O  O     . PHE   A 159 ? 0.1113 0.1033 0.1194 0.0032  -0.0016 -0.0022 156 PHE   A O     
1247 C  CB    . PHE   A 159 ? 0.1272 0.1089 0.1262 0.0014  -0.0012 0.0010  156 PHE   A CB    
1248 C  CG    . PHE   A 159 ? 0.1319 0.1100 0.1307 0.0006  -0.0005 0.0004  156 PHE   A CG    
1249 C  CD1   . PHE   A 159 ? 0.1328 0.1097 0.1344 0.0027  -0.0006 -0.0020 156 PHE   A CD1   
1250 C  CD2   . PHE   A 159 ? 0.1295 0.1065 0.1260 -0.0023 0.0004  0.0014  156 PHE   A CD2   
1251 C  CE1   . PHE   A 159 ? 0.1364 0.1098 0.1377 0.0020  -0.0004 -0.0038 156 PHE   A CE1   
1252 C  CE2   . PHE   A 159 ? 0.1333 0.1073 0.1304 -0.0036 0.0006  0.0002  156 PHE   A CE2   
1253 C  CZ    . PHE   A 159 ? 0.1417 0.1134 0.1408 -0.0014 0.0000  -0.0027 156 PHE   A CZ    
1254 N  N     . TYR   A 160 ? 0.1116 0.1016 0.1124 0.0011  -0.0020 -0.0011 157 TYR   A N     
1255 C  CA    . TYR   A 160 ? 0.1229 0.1158 0.1253 0.0016  -0.0042 -0.0024 157 TYR   A CA    
1256 C  C     . TYR   A 160 ? 0.1063 0.1016 0.1144 0.0007  -0.0033 -0.0045 157 TYR   A C     
1257 O  O     . TYR   A 160 ? 0.1109 0.1091 0.1235 0.0007  -0.0049 -0.0058 157 TYR   A O     
1258 C  CB    . TYR   A 160 ? 0.1356 0.1292 0.1324 0.0010  -0.0052 -0.0027 157 TYR   A CB    
1259 C  CG    . TYR   A 160 ? 0.1525 0.1443 0.1429 0.0013  -0.0064 0.0005  157 TYR   A CG    
1260 C  CD1   . TYR   A 160 ? 0.1670 0.1545 0.1574 0.0020  -0.0068 0.0036  157 TYR   A CD1   
1261 C  CD2   . TYR   A 160 ? 0.1780 0.1722 0.1621 0.0008  -0.0072 0.0006  157 TYR   A CD2   
1262 C  CE1   . TYR   A 160 ? 0.1906 0.1749 0.1754 0.0018  -0.0081 0.0077  157 TYR   A CE1   
1263 C  CE2   . TYR   A 160 ? 0.2059 0.1988 0.1834 0.0006  -0.0081 0.0048  157 TYR   A CE2   
1264 C  CZ    . TYR   A 160 ? 0.1959 0.1832 0.1740 0.0008  -0.0086 0.0089  157 TYR   A CZ    
1265 O  OH    . TYR   A 160 ? 0.2408 0.2255 0.2124 0.0001  -0.0097 0.0143  157 TYR   A OH    
1266 N  N     . THR   A 161 ? 0.0978 0.0919 0.1061 -0.0004 -0.0009 -0.0043 158 THR   A N     
1267 C  CA    . THR   A 161 ? 0.0938 0.0886 0.1072 -0.0015 0.0001  -0.0047 158 THR   A CA    
1268 C  C     . THR   A 161 ? 0.0993 0.0969 0.1170 -0.0016 0.0011  -0.0036 158 THR   A C     
1269 O  O     . THR   A 161 ? 0.0920 0.0921 0.1155 -0.0030 0.0012  -0.0038 158 THR   A O     
1270 C  CB    . THR   A 161 ? 0.0932 0.0859 0.1056 -0.0018 0.0018  -0.0039 158 THR   A CB    
1271 O  OG1   . THR   A 161 ? 0.1022 0.0940 0.1123 -0.0014 0.0012  -0.0060 158 THR   A OG1   
1272 C  CG2   . THR   A 161 ? 0.0955 0.0875 0.1130 -0.0030 0.0026  -0.0028 158 THR   A CG2   
1273 N  N     . LEU   A 162 ? 0.0888 0.0865 0.1042 -0.0003 0.0021  -0.0028 159 LEU   A N     
1274 C  CA    . LEU   A 162 ? 0.0950 0.0966 0.1140 0.0004  0.0035  -0.0028 159 LEU   A CA    
1275 C  C     . LEU   A 162 ? 0.0962 0.1016 0.1203 0.0015  0.0016  -0.0042 159 LEU   A C     
1276 O  O     . LEU   A 162 ? 0.1094 0.1204 0.1395 0.0008  0.0030  -0.0044 159 LEU   A O     
1277 C  CB    . LEU   A 162 ? 0.0969 0.0972 0.1123 0.0019  0.0046  -0.0031 159 LEU   A CB    
1278 C  CG    . LEU   A 162 ? 0.0976 0.1027 0.1158 0.0033  0.0066  -0.0045 159 LEU   A CG    
1279 C  CD1   . LEU   A 162 ? 0.1014 0.1116 0.1214 0.0012  0.0096  -0.0028 159 LEU   A CD1   
1280 C  CD2   . LEU   A 162 ? 0.1080 0.1100 0.1221 0.0049  0.0067  -0.0061 159 LEU   A CD2   
1281 N  N     . VAL   A 163 ? 0.1029 0.1062 0.1249 0.0031  -0.0014 -0.0047 160 VAL   A N     
1282 C  CA    . VAL   A 163 ? 0.1125 0.1200 0.1392 0.0044  -0.0045 -0.0058 160 VAL   A CA    
1283 C  C     . VAL   A 163 ? 0.1138 0.1257 0.1463 0.0017  -0.0050 -0.0071 160 VAL   A C     
1284 O  O     . VAL   A 163 ? 0.1141 0.1328 0.1547 0.0016  -0.0054 -0.0082 160 VAL   A O     
1285 C  CB    . VAL   A 163 ? 0.1138 0.1181 0.1353 0.0061  -0.0083 -0.0051 160 VAL   A CB    
1286 C  CG1   . VAL   A 163 ? 0.1185 0.1282 0.1447 0.0076  -0.0123 -0.0062 160 VAL   A CG1   
1287 C  CG2   . VAL   A 163 ? 0.1222 0.1214 0.1400 0.0085  -0.0083 -0.0034 160 VAL   A CG2   
1288 N  N     . ARG   A 164 ? 0.1169 0.1253 0.1466 -0.0005 -0.0052 -0.0075 161 ARG   A N     
1289 C  CA    . ARG   A 164 ? 0.1204 0.1308 0.1558 -0.0034 -0.0062 -0.0093 161 ARG   A CA    
1290 C  C     . ARG   A 164 ? 0.1164 0.1299 0.1591 -0.0059 -0.0030 -0.0078 161 ARG   A C     
1291 O  O     . ARG   A 164 ? 0.1152 0.1336 0.1661 -0.0083 -0.0038 -0.0088 161 ARG   A O     
1292 C  CB    . ARG   A 164 ? 0.1302 0.1352 0.1615 -0.0046 -0.0065 -0.0106 161 ARG   A CB    
1293 C  CG    . ARG   A 164 ? 0.1422 0.1466 0.1670 -0.0031 -0.0095 -0.0128 161 ARG   A CG    
1294 C  CD    . ARG   A 164 ? 0.1597 0.1596 0.1791 -0.0031 -0.0085 -0.0141 161 ARG   A CD    
1295 N  NE    . ARG   A 164 ? 0.1727 0.1742 0.1875 -0.0026 -0.0114 -0.0177 161 ARG   A NE    
1296 C  CZ    . ARG   A 164 ? 0.2116 0.2116 0.2212 -0.0020 -0.0108 -0.0202 161 ARG   A CZ    
1297 N  NH1   . ARG   A 164 ? 0.1972 0.1938 0.2065 -0.0017 -0.0076 -0.0193 161 ARG   A NH1   
1298 N  NH2   . ARG   A 164 ? 0.2270 0.2299 0.2318 -0.0015 -0.0134 -0.0241 161 ARG   A NH2   
1299 N  N     . GLU   A 165 ? 0.1106 0.1223 0.1502 -0.0057 0.0006  -0.0051 162 GLU   A N     
1300 C  CA    . GLU   A 165 ? 0.1089 0.1247 0.1535 -0.0080 0.0042  -0.0026 162 GLU   A CA    
1301 C  C     . GLU   A 165 ? 0.1057 0.1309 0.1569 -0.0073 0.0053  -0.0035 162 GLU   A C     
1302 O  O     . GLU   A 165 ? 0.1114 0.1425 0.1705 -0.0104 0.0069  -0.0026 162 GLU   A O     
1303 C  CB    . GLU   A 165 ? 0.1149 0.1282 0.1532 -0.0074 0.0074  0.0003  162 GLU   A CB    
1304 C  CG    . GLU   A 165 ? 0.1213 0.1273 0.1555 -0.0082 0.0070  0.0019  162 GLU   A CG    
1305 C  CD    . GLU   A 165 ? 0.1330 0.1367 0.1729 -0.0117 0.0071  0.0039  162 GLU   A CD    
1306 O  OE1   . GLU   A 165 ? 0.1516 0.1582 0.1941 -0.0141 0.0099  0.0078  162 GLU   A OE1   
1307 O  OE2   . GLU   A 165 ? 0.1513 0.1501 0.1929 -0.0123 0.0045  0.0016  162 GLU   A OE2   
1308 N  N     . ILE   A 166 ? 0.1042 0.1308 0.1529 -0.0031 0.0045  -0.0051 163 ILE   A N     
1309 C  CA    . ILE   A 166 ? 0.1037 0.1394 0.1596 -0.0009 0.0047  -0.0070 163 ILE   A CA    
1310 C  C     . ILE   A 166 ? 0.1085 0.1499 0.1733 -0.0024 0.0014  -0.0086 163 ILE   A C     
1311 O  O     . ILE   A 166 ? 0.1081 0.1594 0.1828 -0.0041 0.0030  -0.0091 163 ILE   A O     
1312 C  CB    . ILE   A 166 ? 0.0992 0.1326 0.1514 0.0045  0.0030  -0.0087 163 ILE   A CB    
1313 C  CG1   . ILE   A 166 ? 0.1023 0.1316 0.1475 0.0057  0.0061  -0.0083 163 ILE   A CG1   
1314 C  CG2   . ILE   A 166 ? 0.0988 0.1415 0.1599 0.0078  0.0025  -0.0112 163 ILE   A CG2   
1315 C  CD1   . ILE   A 166 ? 0.1038 0.1260 0.1436 0.0096  0.0037  -0.0094 163 ILE   A CD1   
1316 N  N     . ARG   A 167 ? 0.1145 0.1509 0.1760 -0.0020 -0.0033 -0.0098 164 ARG   A N     
1317 C  CA    . ARG   A 167 ? 0.1200 0.1620 0.1887 -0.0032 -0.0076 -0.0122 164 ARG   A CA    
1318 C  C     . ARG   A 167 ? 0.1274 0.1733 0.2052 -0.0092 -0.0061 -0.0123 164 ARG   A C     
1319 O  O     . ARG   A 167 ? 0.1290 0.1848 0.2178 -0.0109 -0.0073 -0.0140 164 ARG   A O     
1320 C  CB    . ARG   A 167 ? 0.1203 0.1558 0.1812 -0.0023 -0.0123 -0.0134 164 ARG   A CB    
1321 C  CG    . ARG   A 167 ? 0.1297 0.1715 0.1955 -0.0021 -0.0180 -0.0164 164 ARG   A CG    
1322 C  CD    . ARG   A 167 ? 0.1337 0.1694 0.1905 -0.0025 -0.0214 -0.0181 164 ARG   A CD    
1323 N  NE    . ARG   A 167 ? 0.1278 0.1596 0.1744 0.0018  -0.0232 -0.0161 164 ARG   A NE    
1324 C  CZ    . ARG   A 167 ? 0.1310 0.1557 0.1667 0.0020  -0.0228 -0.0153 164 ARG   A CZ    
1325 N  NH1   . ARG   A 167 ? 0.1285 0.1506 0.1559 0.0052  -0.0245 -0.0127 164 ARG   A NH1   
1326 N  NH2   . ARG   A 167 ? 0.1261 0.1464 0.1596 -0.0010 -0.0207 -0.0171 164 ARG   A NH2   
1327 N  N     . GLN   A 168 ? 0.1283 0.1666 0.2023 -0.0124 -0.0036 -0.0103 165 GLN   A N     
1328 C  CA    . GLN   A 168 ? 0.1459 0.1850 0.2278 -0.0184 -0.0020 -0.0091 165 GLN   A CA    
1329 C  C     . GLN   A 168 ? 0.1400 0.1884 0.2295 -0.0207 0.0031  -0.0060 165 GLN   A C     
1330 O  O     . GLN   A 168 ? 0.1535 0.2089 0.2543 -0.0255 0.0034  -0.0061 165 GLN   A O     
1331 C  CB    . GLN   A 168 ? 0.1615 0.1892 0.2372 -0.0201 -0.0007 -0.0069 165 GLN   A CB    
1332 C  CG    . GLN   A 168 ? 0.1790 0.1988 0.2501 -0.0194 -0.0051 -0.0107 165 GLN   A CG    
1333 C  CD    . GLN   A 168 ? 0.2070 0.2166 0.2700 -0.0182 -0.0036 -0.0089 165 GLN   A CD    
1334 O  OE1   . GLN   A 168 ? 0.2557 0.2617 0.3199 -0.0204 -0.0006 -0.0048 165 GLN   A OE1   
1335 N  NE2   . GLN   A 168 ? 0.2167 0.2225 0.2717 -0.0150 -0.0057 -0.0116 165 GLN   A NE2   
1336 N  N     . TYR   A 169 ? 0.1255 0.1750 0.2091 -0.0178 0.0072  -0.0037 166 TYR   A N     
1337 C  CA    . TYR   A 169 ? 0.1328 0.1928 0.2221 -0.0195 0.0126  -0.0013 166 TYR   A CA    
1338 C  C     . TYR   A 169 ? 0.1242 0.1980 0.2251 -0.0184 0.0119  -0.0047 166 TYR   A C     
1339 O  O     . TYR   A 169 ? 0.1245 0.2090 0.2352 -0.0225 0.0155  -0.0032 166 TYR   A O     
1340 C  CB    . TYR   A 169 ? 0.1380 0.1974 0.2179 -0.0158 0.0166  0.0001  166 TYR   A CB    
1341 C  CG    . TYR   A 169 ? 0.1551 0.2084 0.2283 -0.0189 0.0198  0.0054  166 TYR   A CG    
1342 C  CD1   . TYR   A 169 ? 0.1861 0.2464 0.2629 -0.0233 0.0249  0.0100  166 TYR   A CD1   
1343 C  CD2   . TYR   A 169 ? 0.1641 0.2056 0.2276 -0.0173 0.0177  0.0063  166 TYR   A CD2   
1344 C  CE1   . TYR   A 169 ? 0.1975 0.2520 0.2674 -0.0258 0.0272  0.0159  166 TYR   A CE1   
1345 C  CE2   . TYR   A 169 ? 0.1817 0.2182 0.2397 -0.0194 0.0199  0.0113  166 TYR   A CE2   
1346 C  CZ    . TYR   A 169 ? 0.1918 0.2343 0.2526 -0.0234 0.0244  0.0164  166 TYR   A CZ    
1347 O  OH    . TYR   A 169 ? 0.2240 0.2615 0.2787 -0.0253 0.0261  0.0225  166 TYR   A OH    
1348 N  N     . ARG   A 170 ? 0.1210 0.1951 0.2213 -0.0132 0.0071  -0.0087 167 ARG   A N     
1349 C  CA    . ARG   A 170 ? 0.1281 0.2153 0.2402 -0.0113 0.0050  -0.0120 167 ARG   A CA    
1350 C  C     . ARG   A 170 ? 0.1352 0.2297 0.2602 -0.0175 0.0029  -0.0129 167 ARG   A C     
1351 O  O     . ARG   A 170 ? 0.1132 0.2222 0.2510 -0.0180 0.0035  -0.0146 167 ARG   A O     
1352 C  CB    . ARG   A 170 ? 0.1285 0.2127 0.2366 -0.0045 -0.0009 -0.0150 167 ARG   A CB    
1353 C  CG    . ARG   A 170 ? 0.1320 0.2112 0.2314 0.0018  0.0008  -0.0150 167 ARG   A CG    
1354 C  CD    . ARG   A 170 ? 0.1387 0.2138 0.2350 0.0077  -0.0055 -0.0166 167 ARG   A CD    
1355 N  NE    . ARG   A 170 ? 0.1499 0.2195 0.2399 0.0137  -0.0046 -0.0169 167 ARG   A NE    
1356 C  CZ    . ARG   A 170 ? 0.1541 0.2129 0.2352 0.0171  -0.0085 -0.0159 167 ARG   A CZ    
1357 N  NH1   . ARG   A 170 ? 0.1694 0.2229 0.2454 0.0154  -0.0130 -0.0146 167 ARG   A NH1   
1358 N  NH2   . ARG   A 170 ? 0.1746 0.2279 0.2517 0.0219  -0.0078 -0.0163 167 ARG   A NH2   
1359 N  N     . LEU   A 171 ? 0.1413 0.2261 0.2638 -0.0222 0.0004  -0.0124 168 LEU   A N     
1360 C  CA    . LEU   A 171 ? 0.1653 0.2550 0.3002 -0.0291 -0.0017 -0.0137 168 LEU   A CA    
1361 C  C     . LEU   A 171 ? 0.1856 0.2778 0.3279 -0.0368 0.0043  -0.0090 168 LEU   A C     
1362 O  O     . LEU   A 171 ? 0.1962 0.2912 0.3498 -0.0437 0.0028  -0.0095 168 LEU   A O     
1363 C  CB    . LEU   A 171 ? 0.1628 0.2411 0.2929 -0.0304 -0.0079 -0.0168 168 LEU   A CB    
1364 C  CG    . LEU   A 171 ? 0.1755 0.2536 0.2993 -0.0241 -0.0145 -0.0210 168 LEU   A CG    
1365 C  CD1   . LEU   A 171 ? 0.1889 0.2558 0.3052 -0.0253 -0.0191 -0.0240 168 LEU   A CD1   
1366 C  CD2   . LEU   A 171 ? 0.1672 0.2602 0.3026 -0.0227 -0.0188 -0.0245 168 LEU   A CD2   
1367 N  N     . LYS   A 172 ? 0.2164 0.3082 0.3525 -0.0361 0.0108  -0.0042 169 LYS   A N     
1368 C  CA    . LYS   A 172 ? 0.2382 0.3321 0.3782 -0.0429 0.0172  0.0021  169 LYS   A CA    
1369 C  C     . LYS   A 172 ? 0.2355 0.3467 0.3810 -0.0424 0.0239  0.0036  169 LYS   A C     
1370 O  O     . LYS   A 172 ? 0.2434 0.3614 0.3960 -0.0491 0.0290  0.0084  169 LYS   A O     
1371 C  CB    . LYS   A 172 ? 0.2773 0.3582 0.4032 -0.0422 0.0201  0.0073  169 LYS   A CB    
1372 C  CG    . LYS   A 172 ? 0.3342 0.3978 0.4547 -0.0438 0.0160  0.0079  169 LYS   A CG    
1373 C  CD    . LYS   A 172 ? 0.3495 0.4025 0.4594 -0.0438 0.0189  0.0139  169 LYS   A CD    
1374 C  CE    . LYS   A 172 ? 0.3689 0.4174 0.4646 -0.0365 0.0188  0.0128  169 LYS   A CE    
1375 N  NZ    . LYS   A 172 ? 0.4056 0.4400 0.4947 -0.0343 0.0142  0.0108  169 LYS   A NZ    
1376 O  OXT   . LYS   A 172 ? 0.1967 0.3134 0.3386 -0.0351 0.0241  0.0001  169 LYS   A OXT   
1377 P  PB    . GDP   B .   ? 0.1741 0.1544 0.1725 -0.0169 -0.0101 -0.0404 201 GDP   A PB    
1378 O  O1B   . GDP   B .   ? 0.1728 0.1411 0.1744 -0.0159 -0.0094 -0.0392 201 GDP   A O1B   
1379 O  O2B   . GDP   B .   ? 0.1636 0.1529 0.1578 -0.0135 -0.0077 -0.0358 201 GDP   A O2B   
1380 O  O3B   . GDP   B .   ? 0.1843 0.1668 0.1809 -0.0175 -0.0129 -0.0494 201 GDP   A O3B   
1381 O  O3A   . GDP   B .   ? 0.1612 0.1441 0.1645 -0.0224 -0.0110 -0.0360 201 GDP   A O3A   
1382 P  PA    . GDP   B .   ? 0.1683 0.1431 0.1782 -0.0277 -0.0111 -0.0324 201 GDP   A PA    
1383 O  O1A   . GDP   B .   ? 0.1708 0.1418 0.1797 -0.0255 -0.0082 -0.0255 201 GDP   A O1A   
1384 O  O2A   . GDP   B .   ? 0.1828 0.1473 0.1960 -0.0306 -0.0138 -0.0381 201 GDP   A O2A   
1385 O  "O5'" . GDP   B .   ? 0.1634 0.1494 0.1768 -0.0318 -0.0116 -0.0303 201 GDP   A "O5'" 
1386 C  "C5'" . GDP   B .   ? 0.1653 0.1592 0.1797 -0.0337 -0.0149 -0.0358 201 GDP   A "C5'" 
1387 C  "C4'" . GDP   B .   ? 0.1631 0.1644 0.1849 -0.0394 -0.0156 -0.0339 201 GDP   A "C4'" 
1388 O  "O4'" . GDP   B .   ? 0.1557 0.1658 0.1773 -0.0368 -0.0132 -0.0280 201 GDP   A "O4'" 
1389 C  "C3'" . GDP   B .   ? 0.1677 0.1604 0.1958 -0.0455 -0.0147 -0.0313 201 GDP   A "C3'" 
1390 O  "O3'" . GDP   B .   ? 0.1812 0.1803 0.2171 -0.0521 -0.0170 -0.0337 201 GDP   A "O3'" 
1391 C  "C2'" . GDP   B .   ? 0.1605 0.1544 0.1877 -0.0439 -0.0104 -0.0233 201 GDP   A "C2'" 
1392 O  "O2'" . GDP   B .   ? 0.1704 0.1634 0.2033 -0.0500 -0.0084 -0.0184 201 GDP   A "O2'" 
1393 C  "C1'" . GDP   B .   ? 0.1484 0.1563 0.1746 -0.0402 -0.0103 -0.0228 201 GDP   A "C1'" 
1394 N  N9    . GDP   B .   ? 0.1383 0.1469 0.1607 -0.0356 -0.0069 -0.0175 201 GDP   A N9    
1395 C  C8    . GDP   B .   ? 0.1363 0.1372 0.1528 -0.0313 -0.0055 -0.0161 201 GDP   A C8    
1396 N  N7    . GDP   B .   ? 0.1317 0.1360 0.1468 -0.0284 -0.0029 -0.0119 201 GDP   A N7    
1397 C  C5    . GDP   B .   ? 0.1216 0.1358 0.1416 -0.0302 -0.0022 -0.0107 201 GDP   A C5    
1398 C  C6    . GDP   B .   ? 0.1190 0.1413 0.1410 -0.0284 0.0002  -0.0078 201 GDP   A C6    
1399 O  O6    . GDP   B .   ? 0.1112 0.1310 0.1295 -0.0245 0.0021  -0.0057 201 GDP   A O6    
1400 N  N1    . GDP   B .   ? 0.1151 0.1480 0.1439 -0.0307 0.0002  -0.0083 201 GDP   A N1    
1401 C  C2    . GDP   B .   ? 0.1217 0.1584 0.1555 -0.0352 -0.0022 -0.0110 201 GDP   A C2    
1402 N  N2    . GDP   B .   ? 0.1247 0.1741 0.1667 -0.0374 -0.0022 -0.0114 201 GDP   A N2    
1403 N  N3    . GDP   B .   ? 0.1282 0.1573 0.1603 -0.0377 -0.0049 -0.0141 201 GDP   A N3    
1404 C  C4    . GDP   B .   ? 0.1340 0.1515 0.1591 -0.0351 -0.0049 -0.0142 201 GDP   A C4    
1405 MG MG    . MG    C .   ? 0.2053 0.1571 0.2102 -0.0132 -0.0114 -0.0477 202 MG    A MG    
1406 N  NAL   . A1IK7 D .   ? 0.4185 0.3837 0.4700 0.0519  -0.0057 -0.0509 203 A1IK7 A NAL   
1407 C  CAM   . A1IK7 D .   ? 0.3912 0.3647 0.4377 0.0462  -0.0036 -0.0448 203 A1IK7 A CAM   
1408 C  CAN   . A1IK7 D .   ? 0.3539 0.3231 0.3965 0.0416  -0.0060 -0.0360 203 A1IK7 A CAN   
1409 C  CAO   . A1IK7 D .   ? 0.3443 0.3226 0.3826 0.0366  -0.0033 -0.0319 203 A1IK7 A CAO   
1410 C  CAP   . A1IK7 D .   ? 0.3352 0.3265 0.3732 0.0355  0.0015  -0.0349 203 A1IK7 A CAP   
1411 C  CAQ   . A1IK7 D .   ? 0.3610 0.3579 0.4021 0.0396  0.0043  -0.0428 203 A1IK7 A CAQ   
1412 CL CLAR  . A1IK7 D .   ? 0.3627 0.3766 0.4020 0.0379  0.0109  -0.0456 203 A1IK7 A CLAR  
1413 C  CAT   . A1IK7 D .   ? 0.3926 0.3812 0.4378 0.0451  0.0019  -0.0483 203 A1IK7 A CAT   
1414 S  SAU   . A1IK7 D .   ? 0.3888 0.3821 0.4384 0.0516  0.0045  -0.0600 203 A1IK7 A SAU   
1415 C  CAK   . A1IK7 D .   ? 0.4361 0.4097 0.4904 0.0559  -0.0021 -0.0602 203 A1IK7 A CAK   
1416 N  NAJ   . A1IK7 D .   ? 0.4720 0.4397 0.5317 0.0623  -0.0033 -0.0686 203 A1IK7 A NAJ   
1417 S  SAB   . A1IK7 D .   ? 0.5458 0.5259 0.6068 0.0665  0.0020  -0.0808 203 A1IK7 A SAB   
1418 O  OAA   . A1IK7 D .   ? 0.5673 0.5387 0.6372 0.0752  -0.0008 -0.0897 203 A1IK7 A OAA   
1419 O  OAC   . A1IK7 D .   ? 0.5185 0.5197 0.5824 0.0675  0.0073  -0.0807 203 A1IK7 A OAC   
1420 C  CAI   . A1IK7 D .   ? 0.5682 0.5467 0.6167 0.0596  0.0041  -0.0844 203 A1IK7 A CAI   
1421 C  CAS   . A1IK7 D .   ? 0.5605 0.5234 0.6042 0.0543  0.0001  -0.0806 203 A1IK7 A CAS   
1422 C  CAE   . A1IK7 D .   ? 0.5453 0.5081 0.5804 0.0490  0.0010  -0.0837 203 A1IK7 A CAE   
1423 O  OAD   . A1IK7 D .   ? 0.5090 0.4579 0.5410 0.0434  -0.0028 -0.0801 203 A1IK7 A OAD   
1424 C  CAF   . A1IK7 D .   ? 0.5595 0.5374 0.5893 0.0493  0.0059  -0.0902 203 A1IK7 A CAF   
1425 C  CAG   . A1IK7 D .   ? 0.5750 0.5683 0.6085 0.0544  0.0105  -0.0935 203 A1IK7 A CAG   
1426 C  CAH   . A1IK7 D .   ? 0.5728 0.5667 0.6164 0.0595  0.0098  -0.0908 203 A1IK7 A CAH   
1427 C  C1    . EDO   E .   ? 0.3107 0.3259 0.2839 0.0019  -0.0185 -0.0199 204 EDO   A C1    
1428 O  O1    . EDO   E .   ? 0.2748 0.2879 0.2532 0.0025  -0.0203 -0.0152 204 EDO   A O1    
1429 C  C2    . EDO   E .   ? 0.3129 0.3309 0.2900 0.0015  -0.0218 -0.0277 204 EDO   A C2    
1430 O  O2    . EDO   E .   ? 0.3478 0.3709 0.3222 0.0021  -0.0271 -0.0279 204 EDO   A O2    
1431 O  O     . HOH   F .   ? 0.3392 0.2226 0.3640 -0.0034 -0.0188 -0.0297 301 HOH   A O     
1432 O  O     . HOH   F .   ? 0.2833 0.3831 0.3919 -0.0289 0.0322  0.0073  302 HOH   A O     
1433 O  O     . HOH   F .   ? 0.2781 0.2227 0.3278 0.0202  -0.0133 0.0375  303 HOH   A O     
1434 O  O     . HOH   F .   ? 0.2583 0.3560 0.2394 0.0188  -0.0482 0.0240  304 HOH   A O     
1435 O  O     . HOH   F .   ? 0.2237 0.1715 0.2350 -0.0237 -0.0151 -0.0478 305 HOH   A O     
1436 O  O     . HOH   F .   ? 0.3840 0.4414 0.3634 -0.0206 0.0375  0.0549  306 HOH   A O     
1437 O  O     . HOH   F .   ? 0.1890 0.1459 0.1904 -0.0053 -0.0077 -0.0456 307 HOH   A O     
1438 O  O     . HOH   F .   ? 0.2361 0.2954 0.2618 -0.0138 0.0205  -0.0056 308 HOH   A O     
1439 O  O     . HOH   F .   ? 0.2946 0.3659 0.2342 0.0160  -0.0310 0.0528  309 HOH   A O     
1440 O  O     . HOH   F .   ? 0.3678 0.4817 0.2493 0.0096  -0.0272 0.0370  310 HOH   A O     
1441 O  O     . HOH   F .   ? 0.2542 0.3158 0.3307 0.0090  -0.0320 -0.0186 311 HOH   A O     
1442 O  O     . HOH   F .   ? 0.2590 0.2570 0.2498 0.0249  0.0075  -0.0831 312 HOH   A O     
1443 O  O     . HOH   F .   ? 0.1473 0.1620 0.1805 -0.0121 0.0155  0.0120  313 HOH   A O     
1444 O  O     . HOH   F .   ? 0.3572 0.3508 0.3994 -0.0112 -0.0054 -0.0129 314 HOH   A O     
1445 O  O     . HOH   F .   ? 0.2094 0.2276 0.2508 -0.0206 0.0204  0.0229  315 HOH   A O     
1446 O  O     . HOH   F .   ? 0.4550 0.6379 0.3301 0.0184  0.0597  -0.0607 316 HOH   A O     
1447 O  O     . HOH   F .   ? 0.1511 0.2035 0.1600 -0.0190 -0.0208 -0.0240 317 HOH   A O     
1448 O  O     . HOH   F .   ? 0.3381 0.4873 0.3228 0.0590  0.0643  -0.1262 318 HOH   A O     
1449 O  O     . HOH   F .   ? 0.4423 0.4760 0.5207 0.0717  0.0133  -0.0787 319 HOH   A O     
1450 O  O     . HOH   F .   ? 0.2656 0.2471 0.2699 -0.0276 -0.0196 -0.0577 320 HOH   A O     
1451 O  O     . HOH   F .   ? 0.3359 0.3323 0.3840 -0.0196 0.0105  0.0156  321 HOH   A O     
1452 O  O     . HOH   F .   ? 0.3568 0.3172 0.3722 -0.0084 0.0008  0.0842  322 HOH   A O     
1453 O  O     . HOH   F .   ? 0.3443 0.3696 0.3808 -0.0264 0.0276  0.0376  323 HOH   A O     
1454 O  O     . HOH   F .   ? 0.3116 0.3688 0.3662 0.0300  -0.0557 -0.0074 324 HOH   A O     
1455 O  O     . HOH   F .   ? 0.4388 0.3825 0.5019 0.0606  -0.0213 -0.0325 325 HOH   A O     
1456 O  O     . HOH   F .   ? 0.1839 0.2574 0.2390 0.0081  0.0287  -0.0144 326 HOH   A O     
1457 O  O     . HOH   F .   ? 0.2678 0.3319 0.3532 0.0094  -0.0202 -0.0169 327 HOH   A O     
1458 O  O     . HOH   F .   ? 0.1060 0.1698 0.1554 0.0096  -0.0010 -0.0065 328 HOH   A O     
1459 O  O     . HOH   F .   ? 0.1635 0.2773 0.2068 -0.0041 -0.0375 -0.0126 329 HOH   A O     
1460 O  O     . HOH   F .   ? 0.3055 0.3447 0.3314 -0.0179 0.0295  0.0258  330 HOH   A O     
1461 O  O     . HOH   F .   ? 0.2853 0.3626 0.3728 0.0432  0.0166  -0.0413 331 HOH   A O     
1462 O  O     . HOH   F .   ? 0.4713 0.6398 0.4927 0.0392  0.0723  -0.0735 332 HOH   A O     
1463 O  O     . HOH   F .   ? 0.2827 0.2473 0.3032 -0.0396 -0.0205 -0.0508 333 HOH   A O     
1464 O  O     . HOH   F .   ? 0.4781 0.4254 0.4876 0.0012  -0.0110 0.1103  334 HOH   A O     
1465 O  O     . HOH   F .   ? 0.2841 0.2456 0.3300 -0.0242 0.0098  0.0547  335 HOH   A O     
1466 O  O     . HOH   F .   ? 0.3691 0.4898 0.3913 0.0666  0.0545  -0.1217 336 HOH   A O     
1467 O  O     . HOH   F .   ? 0.1831 0.1697 0.2054 0.0062  0.0026  -0.0042 337 HOH   A O     
1468 O  O     . HOH   F .   ? 0.1152 0.1317 0.1285 -0.0049 -0.0290 -0.0409 338 HOH   A O     
1469 O  O     . HOH   F .   ? 0.4645 0.5352 0.4019 0.0111  0.0196  -0.0493 339 HOH   A O     
1470 O  O     . HOH   F .   ? 0.2502 0.2557 0.2222 0.0023  -0.0147 -0.0039 340 HOH   A O     
1471 O  O     . HOH   F .   ? 0.1681 0.1375 0.2008 -0.0073 0.0042  0.0290  341 HOH   A O     
1472 O  O     . HOH   F .   ? 0.3683 0.3594 0.3834 -0.0021 -0.0023 -0.0126 342 HOH   A O     
1473 O  O     . HOH   F .   ? 0.3458 0.3873 0.3369 -0.0149 -0.0185 -0.0277 343 HOH   A O     
1474 O  O     . HOH   F .   ? 0.2688 0.1804 0.2865 0.0009  -0.0136 -0.0409 344 HOH   A O     
1475 O  O     . HOH   F .   ? 0.2381 0.2741 0.2292 0.0351  -0.0726 0.0172  345 HOH   A O     
1476 O  O     . HOH   F .   ? 0.2383 0.3135 0.3403 0.0372  -0.0057 -0.0257 346 HOH   A O     
1477 O  O     . HOH   F .   ? 0.2881 0.2830 0.3200 -0.0074 0.0000  -0.0053 347 HOH   A O     
1478 O  O     . HOH   F .   ? 0.3955 0.4398 0.5079 -0.0376 0.0010  -0.0052 348 HOH   A O     
1479 O  O     . HOH   F .   ? 0.3784 0.3271 0.4191 0.0213  -0.0168 0.0555  349 HOH   A O     
1480 O  O     . HOH   F .   ? 0.2002 0.2256 0.1649 0.0054  -0.0323 -0.0145 350 HOH   A O     
1481 O  O     . HOH   F .   ? 0.1418 0.1174 0.1700 0.0000  0.0020  0.0080  351 HOH   A O     
1482 O  O     . HOH   F .   ? 0.3678 0.4566 0.3690 0.0267  -0.0479 0.0319  352 HOH   A O     
1483 O  O     . HOH   F .   ? 0.2123 0.4532 0.3051 -0.0032 0.0959  -0.0184 353 HOH   A O     
1484 O  O     . HOH   F .   ? 0.2370 0.2014 0.2683 0.0008  -0.0005 0.0322  354 HOH   A O     
1485 O  O     . HOH   F .   ? 0.2154 0.3266 0.3034 -0.0608 0.0120  -0.0068 355 HOH   A O     
1486 O  O     . HOH   F .   ? 0.1864 0.1389 0.1971 -0.0372 -0.0011 0.0060  356 HOH   A O     
1487 O  O     . HOH   F .   ? 0.3462 0.3634 0.3952 -0.0602 -0.0090 -0.0190 357 HOH   A O     
1488 O  O     . HOH   F .   ? 0.3791 0.4292 0.3224 -0.0079 0.0167  0.0641  358 HOH   A O     
1489 O  O     . HOH   F .   ? 0.1846 0.2423 0.2188 -0.0075 0.0131  -0.0076 359 HOH   A O     
1490 O  O     . HOH   F .   ? 0.2651 0.2274 0.2645 -0.0117 -0.0124 -0.0578 360 HOH   A O     
1491 O  O     . HOH   F .   ? 0.3542 0.2771 0.3849 -0.0709 -0.0020 0.0236  361 HOH   A O     
1492 O  O     . HOH   F .   ? 0.2087 0.2041 0.2130 0.0021  0.0017  -0.0177 362 HOH   A O     
1493 O  O     . HOH   F .   ? 0.2598 0.3103 0.2045 0.0007  0.0039  0.0345  363 HOH   A O     
1494 O  O     . HOH   F .   ? 0.1882 0.1215 0.1988 -0.0118 -0.0148 -0.0569 364 HOH   A O     
1495 O  O     . HOH   F .   ? 0.3613 0.5620 0.3591 -0.0059 0.0920  -0.0037 365 HOH   A O     
1496 O  O     . HOH   F .   ? 0.3231 0.3559 0.3369 -0.0324 -0.0228 -0.0400 366 HOH   A O     
1497 O  O     . HOH   F .   ? 0.3865 0.3991 0.4562 0.0483  -0.0161 -0.0206 367 HOH   A O     
1498 O  O     . HOH   F .   ? 0.3268 0.3026 0.3445 -0.0684 0.0135  0.0342  368 HOH   A O     
1499 O  O     . HOH   F .   ? 0.3893 0.3442 0.4144 -0.0436 -0.0129 -0.0271 369 HOH   A O     
1500 O  O     . HOH   F .   ? 0.1660 0.2006 0.1312 -0.0014 -0.0013 -0.0147 370 HOH   A O     
1501 O  O     . HOH   F .   ? 0.3878 0.3023 0.4316 -0.0652 -0.0159 -0.0162 371 HOH   A O     
1502 O  O     . HOH   F .   ? 0.1945 0.2627 0.2299 -0.0313 -0.0229 -0.0273 372 HOH   A O     
1503 O  O     . HOH   F .   ? 0.1740 0.2317 0.1839 0.0213  -0.0668 -0.0093 373 HOH   A O     
1504 O  O     . HOH   F .   ? 0.3105 0.3574 0.3120 0.0262  -0.0324 0.0426  374 HOH   A O     
1505 O  O     . HOH   F .   ? 0.3912 0.4913 0.5176 -0.0502 0.0374  0.0218  375 HOH   A O     
1506 O  O     . HOH   F .   ? 0.2647 0.2559 0.2474 -0.0054 -0.0093 -0.0633 376 HOH   A O     
1507 O  O     . HOH   F .   ? 0.2962 0.4289 0.2515 -0.0129 0.0639  0.0254  377 HOH   A O     
1508 O  O     . HOH   F .   ? 0.3415 0.3052 0.3394 0.0228  -0.0046 -0.1049 378 HOH   A O     
1509 O  O     . HOH   F .   ? 0.1611 0.1623 0.1429 -0.0123 0.0098  0.0075  379 HOH   A O     
1510 O  O     . HOH   F .   ? 0.2414 0.2728 0.2820 -0.0502 -0.0203 -0.0353 380 HOH   A O     
1511 O  O     . HOH   F .   ? 0.4054 0.2691 0.4387 0.0253  -0.0299 -0.0034 381 HOH   A O     
1512 O  O     . HOH   F .   ? 0.1269 0.2504 0.2755 -0.0065 -0.0085 -0.0225 382 HOH   A O     
1513 O  O     . HOH   F .   ? 0.4081 0.3227 0.4512 0.0443  -0.0250 -0.0159 383 HOH   A O     
1514 O  O     . HOH   F .   ? 0.4151 0.3920 0.3992 -0.0033 -0.0157 -0.0955 384 HOH   A O     
1515 O  O     . HOH   F .   ? 0.1241 0.2062 0.1836 0.0117  -0.0093 -0.0055 385 HOH   A O     
1516 O  O     . HOH   F .   ? 0.3182 0.2456 0.2992 0.0154  -0.0321 0.0441  386 HOH   A O     
1517 O  O     . HOH   F .   ? 0.3363 0.3295 0.3480 -0.0342 0.0243  0.0976  387 HOH   A O     
1518 O  O     . HOH   F .   ? 0.3824 0.3993 0.3337 0.0047  -0.0249 -0.0009 388 HOH   A O     
1519 O  O     . HOH   F .   ? 0.3374 0.4005 0.3200 0.0201  -0.0340 0.0372  389 HOH   A O     
1520 O  O     . HOH   F .   ? 0.3935 0.4329 0.4887 0.0674  -0.0523 -0.0062 390 HOH   A O     
1521 O  O     . HOH   F .   ? 0.1610 0.2060 0.1796 0.0278  -0.0614 0.0000  391 HOH   A O     
1522 O  O     . HOH   F .   ? 0.4989 0.6318 0.4481 0.0454  0.0536  -0.1174 392 HOH   A O     
1523 O  O     . HOH   F .   ? 0.4685 0.3823 0.4469 -0.0021 -0.0210 0.0464  393 HOH   A O     
1524 O  O     . HOH   F .   ? 0.2012 0.2218 0.1893 -0.0080 0.0153  -0.0030 394 HOH   A O     
1525 O  O     . HOH   F .   ? 0.2848 0.3465 0.2409 -0.0074 -0.0223 -0.0358 395 HOH   A O     
1526 O  O     . HOH   F .   ? 0.4237 0.5308 0.3240 0.0259  0.0214  -0.1179 396 HOH   A O     
1527 O  O     . HOH   F .   ? 0.2464 0.3531 0.3378 0.0389  0.0304  -0.0443 397 HOH   A O     
1528 O  O     . HOH   F .   ? 0.2300 0.3360 0.2776 -0.0174 -0.0317 -0.0206 398 HOH   A O     
1529 O  O     . HOH   F .   ? 0.3752 0.4008 0.4045 -0.0615 0.0195  0.0194  399 HOH   A O     
1530 O  O     . HOH   F .   ? 0.5183 0.5722 0.4826 0.0172  -0.0278 0.0490  400 HOH   A O     
1531 O  O     . HOH   F .   ? 0.2813 0.2849 0.2374 0.0264  -0.0576 0.0355  401 HOH   A O     
1532 O  O     . HOH   F .   ? 0.2550 0.2670 0.2452 -0.0009 0.0100  -0.0113 402 HOH   A O     
1533 O  O     . HOH   F .   ? 0.2114 0.2540 0.2449 -0.0377 -0.0155 -0.0256 403 HOH   A O     
1534 O  O     . HOH   F .   ? 0.1869 0.2595 0.2866 -0.0036 -0.0176 -0.0194 404 HOH   A O     
1535 O  O     . HOH   F .   ? 0.2419 0.3007 0.3354 0.0441  -0.0325 -0.0152 405 HOH   A O     
1536 O  O     . HOH   F .   ? 0.4723 0.4409 0.4790 0.0551  -0.0714 0.0456  406 HOH   A O     
1537 O  O     . HOH   F .   ? 0.4087 0.3990 0.4616 0.0443  -0.0235 -0.0091 407 HOH   A O     
1538 O  O     . HOH   F .   ? 0.4220 0.4320 0.4070 0.0338  0.0105  -0.1094 408 HOH   A O     
1539 O  O     . HOH   F .   ? 0.4896 0.4907 0.4430 0.0019  -0.0161 0.0122  409 HOH   A O     
1540 O  O     . HOH   F .   ? 0.5051 0.4183 0.5301 -0.0329 -0.0381 -0.1168 410 HOH   A O     
1541 O  O     . HOH   F .   ? 0.3563 0.2382 0.3800 0.0273  -0.0315 0.0135  411 HOH   A O     
1542 O  O     . HOH   F .   ? 0.2824 0.2489 0.3395 0.0351  -0.0171 0.0249  412 HOH   A O     
1543 O  O     . HOH   F .   ? 0.3910 0.5279 0.4739 -0.0398 0.0650  0.0313  413 HOH   A O     
1544 O  O     . HOH   F .   ? 0.2927 0.2760 0.3144 0.0035  0.0015  -0.0114 414 HOH   A O     
1545 O  O     . HOH   F .   ? 0.2634 0.3578 0.2251 -0.0003 -0.0390 -0.0118 415 HOH   A O     
1546 O  O     . HOH   F .   ? 0.3462 0.2151 0.3913 -0.0475 -0.0275 -0.0449 416 HOH   A O     
1547 O  O     . HOH   F .   ? 0.4959 0.4133 0.5381 0.0438  -0.0125 -0.0654 417 HOH   A O     
1548 O  O     . HOH   F .   ? 0.3646 0.2447 0.3986 0.0190  -0.0217 -0.0919 418 HOH   A O     
1549 O  O     . HOH   F .   ? 0.4046 0.2802 0.4502 0.0373  -0.0247 -0.0393 419 HOH   A O     
1550 O  O     . HOH   F .   ? 0.4237 0.4141 0.3743 0.0051  -0.0231 0.0258  420 HOH   A O     
1551 O  O     . HOH   F .   ? 0.3843 0.4315 0.3444 -0.0119 -0.0228 -0.0581 421 HOH   A O     
1552 O  O     . HOH   F .   ? 0.4854 0.3612 0.5177 0.0103  -0.0262 -0.1098 422 HOH   A O     
1553 O  O     . HOH   F .   ? 0.3054 0.3194 0.3688 -0.0226 0.0094  0.0072  423 HOH   A O     
1554 O  O     . HOH   F .   ? 0.2413 0.3337 0.2880 0.0338  -0.0886 -0.0114 424 HOH   A O     
1555 O  O     . HOH   F .   ? 0.2683 0.3048 0.3186 0.0334  -0.0193 0.0149  425 HOH   A O     
1556 O  O     . HOH   F .   ? 0.4630 0.3888 0.4281 -0.0220 -0.0092 0.0572  426 HOH   A O     
1557 O  O     . HOH   F .   ? 0.2038 0.2287 0.2161 0.0114  -0.0097 0.0153  427 HOH   A O     
1558 O  O     . HOH   F .   ? 0.1528 0.1574 0.1363 -0.0059 0.0082  -0.0008 428 HOH   A O     
1559 O  O     . HOH   F .   ? 0.4995 0.6308 0.5668 0.0286  0.0506  -0.0435 429 HOH   A O     
1560 O  O     . HOH   F .   ? 0.4181 0.2960 0.4682 0.0459  -0.0292 -0.0260 430 HOH   A O     
1561 O  O     . HOH   F .   ? 0.5158 0.5176 0.5628 -0.0633 -0.0273 -0.0506 431 HOH   A O     
1562 O  O     . HOH   F .   ? 0.0815 0.0992 0.1318 -0.0097 -0.0155 -0.0193 432 HOH   A O     
1563 O  O     . HOH   F .   ? 0.2926 0.3612 0.3894 0.0333  -0.0194 -0.0191 433 HOH   A O     
1564 O  O     . HOH   F .   ? 0.3484 0.1964 0.3744 -0.0122 -0.0246 0.0043  434 HOH   A O     
1565 O  O     . HOH   F .   ? 0.4341 0.2845 0.4742 0.0229  -0.0294 -0.0202 435 HOH   A O     
1566 O  O     . HOH   F .   ? 0.3280 0.3803 0.3860 0.0418  -0.0300 0.0213  436 HOH   A O     
1567 O  O     . HOH   F .   ? 0.3741 0.2096 0.3979 -0.0033 -0.0298 0.0196  437 HOH   A O     
1568 O  O     . HOH   F .   ? 0.2164 0.1791 0.2536 0.0081  -0.0033 0.0197  438 HOH   A O     
1569 O  O     . HOH   F .   ? 0.0909 0.1897 0.1696 0.0147  0.0314  -0.0224 439 HOH   A O     
1570 O  O     . HOH   F .   ? 0.4314 0.4759 0.4232 -0.0214 -0.0253 -0.0424 440 HOH   A O     
1571 O  O     . HOH   F .   ? 0.5131 0.5442 0.4967 -0.0159 0.0211  0.0038  441 HOH   A O     
1572 O  O     . HOH   F .   ? 0.1907 0.2762 0.2985 0.0218  -0.0210 -0.0202 442 HOH   A O     
1573 O  O     . HOH   F .   ? 0.5492 0.5015 0.5455 0.0156  -0.0125 -0.1197 443 HOH   A O     
1574 O  O     . HOH   F .   ? 0.5016 0.3802 0.5658 -0.0777 -0.0290 -0.0388 444 HOH   A O     
1575 O  O     . HOH   F .   ? 0.3648 0.2453 0.4143 -0.0632 -0.0233 -0.0268 445 HOH   A O     
1576 O  O     . HOH   F .   ? 0.3058 0.2857 0.3495 -0.0161 0.0070  0.0179  446 HOH   A O     
1577 O  O     . HOH   F .   ? 0.5472 0.5362 0.5738 -0.0480 -0.0265 -0.0571 447 HOH   A O     
1578 O  O     . HOH   F .   ? 0.3959 0.3074 0.4407 -0.0756 -0.0097 0.0064  448 HOH   A O     
1579 O  O     . HOH   F .   ? 0.5222 0.5650 0.5796 -0.0605 -0.0028 -0.0122 449 HOH   A O     
1580 O  O     . HOH   F .   ? 0.5179 0.4867 0.5026 0.0049  -0.0158 -0.1169 450 HOH   A O     
1581 O  O     . HOH   F .   ? 0.5196 0.5771 0.4593 -0.0041 -0.0157 -0.0590 451 HOH   A O     
1582 O  O     . HOH   F .   ? 0.4657 0.4673 0.4392 -0.0067 -0.0149 -0.0823 452 HOH   A O     
1583 O  O     . HOH   F .   ? 0.4136 0.4129 0.4242 0.0555  -0.0774 0.0376  453 HOH   A O     
1584 O  O     . HOH   F .   ? 0.4514 0.4673 0.4642 -0.0368 -0.0255 -0.0525 454 HOH   A O     
1585 O  O     . HOH   F .   ? 0.2941 0.2539 0.3401 -0.0163 0.0053  0.0366  455 HOH   A O     
1586 O  O     . HOH   F .   ? 0.4477 0.4769 0.5485 -0.0325 -0.0096 -0.0156 456 HOH   A O     
1587 O  O     . HOH   F .   ? 0.3240 0.1607 0.3722 -0.0406 -0.0295 -0.0341 457 HOH   A O     
1588 O  O     . HOH   F .   ? 0.5257 0.3986 0.5576 0.0407  -0.0411 0.0195  458 HOH   A O     
1589 O  O     . HOH   F .   ? 0.2198 0.3208 0.3468 -0.0024 -0.0202 -0.0233 459 HOH   A O     
1590 O  O     . HOH   F .   ? 0.4708 0.3213 0.5307 -0.0593 -0.0358 -0.0617 460 HOH   A O     
1591 O  O     . HOH   F .   ? 0.3853 0.4394 0.3194 -0.0002 0.0039  0.0561  461 HOH   A O     
1592 O  O     . HOH   F .   ? 0.4380 0.4866 0.4126 -0.0270 0.0365  0.0798  462 HOH   A O     
1593 O  O     . HOH   F .   ? 0.5140 0.5430 0.5611 -0.0735 0.0161  0.0155  463 HOH   A O     
1594 O  O     . HOH   F .   ? 0.4036 0.3849 0.4280 -0.0012 0.0016  -0.0042 464 HOH   A O     
1595 O  O     . HOH   F .   ? 0.4294 0.5257 0.5459 0.0562  0.0116  -0.0476 465 HOH   A O     
1596 O  O     . HOH   F .   ? 0.2796 0.3821 0.4018 0.0133  -0.0304 -0.0238 466 HOH   A O     
# 
