data_9G4B
# 
_entry.id   9G4B 
# 
_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   9G4B         pdb_00009g4b 10.2210/pdb9g4b/pdb 
WWPDB D_1292140114 ?            ?                   
# 
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                        9G4B 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-15 
_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 9GGT PDB . 
unspecified 9GGV 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 1,2-ETHANEDIOL 62.068    3   ?       ?     ? ? 
5 non-polymer syn 
;(3Z)-7-chloro-10,21-dihydroxy-2,2-dioxo-18-(4-piperidyl)-2-lambda-6,5-dithia-3,12,18-triazatetracyclo[18.3.1.04,12.06,11]tetracosa-1(23),3,6,8,10,20(24),21-heptaen-19-one
;
551.078   1   ?       ?     ? ? 
6 water       nat water 18.015    130 ?       ?     ? ? 
# 
_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 1,2-ETHANEDIOL EDO   
5 
;(3Z)-7-chloro-10,21-dihydroxy-2,2-dioxo-18-(4-piperidyl)-2-lambda-6,5-dithia-3,12,18-triazatetracyclo[18.3.1.04,12.06,11]tetracosa-1(23),3,6,8,10,20(24),21-heptaen-19-one
;
A1IIU 
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 
A1IIU non-polymer         . 
;(3Z)-7-chloro-10,21-dihydroxy-2,2-dioxo-18-(4-piperidyl)-2-lambda-6,5-dithia-3,12,18-triazatetracyclo[18.3.1.04,12.06,11]tetracosa-1(23),3,6,8,10,20(24),21-heptaen-19-one
;
;19-chloro-6,16-dihydroxy-2,2,8-trioxo-9-(piperidin-4-yl)-1,8,9,10,11,12,13,14-octahydro-2H-3,7-(metheno)-2-lambda-6-[1,2,4,10]thiatriazacyclohexadecino[3,4-b][1,3]benzothiazol-15-ium
;
'C24 H27 Cl N4 O5 S2' 551.078 
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   ?   ?   ?   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 EDO   1   203 1    EDO   EDO A . 
E 4 EDO   1   204 2    EDO   EDO A . 
F 4 EDO   1   205 3    EDO   EDO A . 
G 5 A1IIU 1   206 1    A1IIU DRG A . 
H 6 HOH   1   301 16   HOH   HOH A . 
H 6 HOH   2   302 251  HOH   HOH A . 
H 6 HOH   3   303 264  HOH   HOH A . 
H 6 HOH   4   304 64   HOH   HOH A . 
H 6 HOH   5   305 49   HOH   HOH A . 
H 6 HOH   6   306 166  HOH   HOH A . 
H 6 HOH   7   307 170  HOH   HOH A . 
H 6 HOH   8   308 48   HOH   HOH A . 
H 6 HOH   9   309 91   HOH   HOH A . 
H 6 HOH   10  310 250  HOH   HOH A . 
H 6 HOH   11  311 161  HOH   HOH A . 
H 6 HOH   12  312 209  HOH   HOH A . 
H 6 HOH   13  313 98   HOH   HOH A . 
H 6 HOH   14  314 80   HOH   HOH A . 
H 6 HOH   15  315 180  HOH   HOH A . 
H 6 HOH   16  316 106  HOH   HOH A . 
H 6 HOH   17  317 158  HOH   HOH A . 
H 6 HOH   18  318 147  HOH   HOH A . 
H 6 HOH   19  319 123  HOH   HOH A . 
H 6 HOH   20  320 54   HOH   HOH A . 
H 6 HOH   21  321 7    HOH   HOH A . 
H 6 HOH   22  322 3    HOH   HOH A . 
H 6 HOH   23  323 27   HOH   HOH A . 
H 6 HOH   24  324 62   HOH   HOH A . 
H 6 HOH   25  325 37   HOH   HOH A . 
H 6 HOH   26  326 12   HOH   HOH A . 
H 6 HOH   27  327 157  HOH   HOH A . 
H 6 HOH   28  328 89   HOH   HOH A . 
H 6 HOH   29  329 160  HOH   HOH A . 
H 6 HOH   30  330 5    HOH   HOH A . 
H 6 HOH   31  331 4    HOH   HOH A . 
H 6 HOH   32  332 26   HOH   HOH A . 
H 6 HOH   33  333 132  HOH   HOH A . 
H 6 HOH   34  334 213  HOH   HOH A . 
H 6 HOH   35  335 87   HOH   HOH A . 
H 6 HOH   36  336 184  HOH   HOH A . 
H 6 HOH   37  337 176  HOH   HOH A . 
H 6 HOH   38  338 44   HOH   HOH A . 
H 6 HOH   39  339 9    HOH   HOH A . 
H 6 HOH   40  340 254  HOH   HOH A . 
H 6 HOH   41  341 10   HOH   HOH A . 
H 6 HOH   42  342 178  HOH   HOH A . 
H 6 HOH   43  343 223  HOH   HOH A . 
H 6 HOH   44  344 167  HOH   HOH A . 
H 6 HOH   45  345 171  HOH   HOH A . 
H 6 HOH   46  346 21   HOH   HOH A . 
H 6 HOH   47  347 129  HOH   HOH A . 
H 6 HOH   48  348 248  HOH   HOH A . 
H 6 HOH   49  349 179  HOH   HOH A . 
H 6 HOH   50  350 63   HOH   HOH A . 
H 6 HOH   51  351 1    HOH   HOH A . 
H 6 HOH   52  352 23   HOH   HOH A . 
H 6 HOH   53  353 40   HOH   HOH A . 
H 6 HOH   54  354 31   HOH   HOH A . 
H 6 HOH   55  355 188  HOH   HOH A . 
H 6 HOH   56  356 97   HOH   HOH A . 
H 6 HOH   57  357 17   HOH   HOH A . 
H 6 HOH   58  358 174  HOH   HOH A . 
H 6 HOH   59  359 99   HOH   HOH A . 
H 6 HOH   60  360 57   HOH   HOH A . 
H 6 HOH   61  361 163  HOH   HOH A . 
H 6 HOH   62  362 41   HOH   HOH A . 
H 6 HOH   63  363 71   HOH   HOH A . 
H 6 HOH   64  364 215  HOH   HOH A . 
H 6 HOH   65  365 137  HOH   HOH A . 
H 6 HOH   66  366 69   HOH   HOH A . 
H 6 HOH   67  367 94   HOH   HOH A . 
H 6 HOH   68  368 245  HOH   HOH A . 
H 6 HOH   69  369 100  HOH   HOH A . 
H 6 HOH   70  370 19   HOH   HOH A . 
H 6 HOH   71  371 198  HOH   HOH A . 
H 6 HOH   72  372 29   HOH   HOH A . 
H 6 HOH   73  373 121  HOH   HOH A . 
H 6 HOH   74  374 128  HOH   HOH A . 
H 6 HOH   75  375 122  HOH   HOH A . 
H 6 HOH   76  376 108  HOH   HOH A . 
H 6 HOH   77  377 263  HOH   HOH A . 
H 6 HOH   78  378 154  HOH   HOH A . 
H 6 HOH   79  379 39   HOH   HOH A . 
H 6 HOH   80  380 65   HOH   HOH A . 
H 6 HOH   81  381 134  HOH   HOH A . 
H 6 HOH   82  382 155  HOH   HOH A . 
H 6 HOH   83  383 13   HOH   HOH A . 
H 6 HOH   84  384 14   HOH   HOH A . 
H 6 HOH   85  385 58   HOH   HOH A . 
H 6 HOH   86  386 197  HOH   HOH A . 
H 6 HOH   87  387 153  HOH   HOH A . 
H 6 HOH   88  388 50   HOH   HOH A . 
H 6 HOH   89  389 66   HOH   HOH A . 
H 6 HOH   90  390 33   HOH   HOH A . 
H 6 HOH   91  391 76   HOH   HOH A . 
H 6 HOH   92  392 150  HOH   HOH A . 
H 6 HOH   93  393 169  HOH   HOH A . 
H 6 HOH   94  394 92   HOH   HOH A . 
H 6 HOH   95  395 120  HOH   HOH A . 
H 6 HOH   96  396 35   HOH   HOH A . 
H 6 HOH   97  397 162  HOH   HOH A . 
H 6 HOH   98  398 38   HOH   HOH A . 
H 6 HOH   99  399 183  HOH   HOH A . 
H 6 HOH   100 400 145  HOH   HOH A . 
H 6 HOH   101 401 138  HOH   HOH A . 
H 6 HOH   102 402 261  HOH   HOH A . 
H 6 HOH   103 403 185  HOH   HOH A . 
H 6 HOH   104 404 165  HOH   HOH A . 
H 6 HOH   105 405 152  HOH   HOH A . 
H 6 HOH   106 406 244  HOH   HOH A . 
H 6 HOH   107 407 216  HOH   HOH A . 
H 6 HOH   108 408 51   HOH   HOH A . 
H 6 HOH   109 409 168  HOH   HOH A . 
H 6 HOH   110 410 181  HOH   HOH A . 
H 6 HOH   111 411 59   HOH   HOH A . 
H 6 HOH   112 412 238  HOH   HOH A . 
H 6 HOH   113 413 85   HOH   HOH A . 
H 6 HOH   114 414 2    HOH   HOH A . 
H 6 HOH   115 415 262  HOH   HOH A . 
H 6 HOH   116 416 256  HOH   HOH A . 
H 6 HOH   117 417 42   HOH   HOH A . 
H 6 HOH   118 418 75   HOH   HOH A . 
H 6 HOH   119 419 252  HOH   HOH A . 
H 6 HOH   120 420 259  HOH   HOH A . 
H 6 HOH   121 421 243  HOH   HOH A . 
H 6 HOH   122 422 177  HOH   HOH A . 
H 6 HOH   123 423 102  HOH   HOH A . 
H 6 HOH   124 424 104  HOH   HOH A . 
H 6 HOH   125 425 260  HOH   HOH A . 
H 6 HOH   126 426 258  HOH   HOH A . 
H 6 HOH   127 427 72   HOH   HOH A . 
H 6 HOH   128 428 257  HOH   HOH A . 
H 6 HOH   129 429 130  HOH   HOH A . 
H 6 HOH   130 430 235  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        ? ? ? .        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                     9G4B 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.010 
_cell.length_a_esd                 ? 
_cell.length_b                     40.140 
_cell.length_b_esd                 ? 
_cell.length_c                     110.660 
_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                         9G4B 
_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                   9G4B 
_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             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.32 
_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               0.167 
_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              8.7 
_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, 500 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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-10-01 
_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   0.97632 
_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 I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97632 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          10.387 
_reflns.entry_id                                       9G4B 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.140 
_reflns.d_resolution_low                               37.010 
_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                                     61058 
_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                           100.000 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.900 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.200 
_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                                0.052 
_reflns.pdbx_Rpim_I_all                                0.021 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_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                              0.047 
_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 
1.140 1.160  ? 1.600  ? ? ? ? 2950 ? ? ? ? ? ? ? ? ? ? ? 3.300 ? ? ? 0.900 0.479 ? 1 1 ? ? ? 97.800  ? ? ? ? ? ? ? ? ? ? ? 
3.090 37.030 ? 65.200 ? ? ? ? 3302 ? ? ? ? ? ? ? ? ? ? ? 6.000 ? ? ? 0.026 0.011 ? 2 1 ? ? ? 100.000 ? ? ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.3300 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            -0.3200 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -0.0100 
_refine.B_iso_max                                74.160 
_refine.B_iso_mean                               15.8990 
_refine.B_iso_min                                6.990 
_refine.correlation_coeff_Fo_to_Fc               0.9720 
_refine.correlation_coeff_Fo_to_Fc_free          0.9640 
_refine.details                                  
'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES      : REFINED INDIVIDUALLY' 
_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                                 9G4B 
_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                            1.1400 
_refine.ls_d_res_low                             35.1200 
_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                     57986 
_refine.ls_number_reflns_R_free                  2993 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.8300 
_refine.ls_percent_reflns_R_free                 4.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1648 
_refine.ls_R_factor_R_free                       0.1926 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1634 
_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                       0.0360 
_refine.pdbx_overall_ESU_R_Free                  0.0370 
_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                             1.4800 
_refine.overall_SU_ML                            0.0300 
_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                       1.1400 
_refine_hist.d_res_low                        35.1200 
_refine_hist.number_atoms_solvent             130 
_refine_hist.number_atoms_total               1569 
_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       169 
_refine_hist.pdbx_B_iso_mean_ligand           17.28 
_refine_hist.pdbx_B_iso_mean_solvent          31.21 
_refine_hist.pdbx_number_atoms_protein        1362 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         77 
_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  1479 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.035  0.018  1351 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 2.094  1.730  2004 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 2.354  1.649  3134 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 5.066  5.000  172  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 33.972 22.048 83   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.770 15.000 258  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 16.363 15.000 12   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.132  0.200  191  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  1626 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.016  0.020  311  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 1.540  1.357  685  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 1.540  1.355  684  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 1.903  2.046  858  ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 2.227  3.000  2830 ? r_rigid_bond_restr     ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.1400 
_refine_ls_shell.d_res_low                        1.1700 
_refine_ls_shell.number_reflns_all                4361 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             226 
_refine_ls_shell.number_reflns_R_work             4135 
_refine_ls_shell.percent_reflns_obs               98.2900 
_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                  0.2850 
_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                  0.3150 
# 
_struct.entry_id                     9G4B 
_struct.title                        'Human KRas4A (GDP) in complex with compound 15' 
_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        9G4B 
_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 4 ? 
F N N 4 ? 
G N N 5 ? 
H 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              9G4B 
_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 9G4B GLY A 1   ? UNP P01116 ?   ?   'expression tag'      -2  1 
1 9G4B GLY A 2   ? UNP P01116 ?   ?   'expression tag'      -1  2 
1 9G4B SER A 3   ? UNP P01116 ?   ?   'expression tag'      0   3 
1 9G4B SER A 121 ? UNP P01116 CYS 118 'engineered mutation' 118 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 1350 ? 
1 MORE         -12  ? 
1 'SSA (A^2)'  8300 ? 
# 
_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,G,H 
# 
_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 ? ? ? ? ? ? ? 2.099 ? ? 
metalc2 metalc ? ? B GDP .  O1B ? ? ? 1_555 C MG  . MG ? ? A GDP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc3 metalc ? ? C MG  .  MG  ? ? ? 1_555 H HOH . O  ? ? A MG  202 A HOH 310 1_555 ? ? ? ? ? ? ? 2.093 ? ? 
metalc4 metalc ? ? C MG  .  MG  ? ? ? 1_555 H HOH . O  ? ? A MG  202 A HOH 321 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc5 metalc ? ? C MG  .  MG  ? ? ? 1_555 H HOH . O  ? ? A MG  202 A HOH 330 1_555 ? ? ? ? ? ? ? 2.145 ? ? 
metalc6 metalc ? ? C MG  .  MG  ? ? ? 1_555 H HOH . O  ? ? A MG  202 A HOH 368 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
# 
_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 92.3  ? 
2  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 310 ? 1_555 82.5  ? 
3  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 310 ? 1_555 95.6  ? 
4  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 321 ? 1_555 93.1  ? 
5  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 321 ? 1_555 86.5  ? 
6  O   ? H HOH .  ? A HOH 310 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 321 ? 1_555 175.2 ? 
7  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 330 ? 1_555 172.7 ? 
8  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 330 ? 1_555 89.0  ? 
9  O   ? H HOH .  ? A HOH 310 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 330 ? 1_555 90.2  ? 
10 O   ? H HOH .  ? A HOH 321 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 330 ? 1_555 94.2  ? 
11 OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 368 ? 1_555 90.2  ? 
12 O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 368 ? 1_555 170.8 ? 
13 O   ? H HOH .  ? A HOH 310 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 368 ? 1_555 93.5  ? 
14 O   ? H HOH .  ? A HOH 321 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 368 ? 1_555 84.5  ? 
15 O   ? H HOH .  ? A HOH 330 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? H HOH . ? A HOH 368 ? 1_555 89.6  ? 
# 
_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 LEU A 55  ? O LEU A 52  N THR A 5   ? N THR A 2   
AA1 3 4 N VAL A 12  ? N VAL A 9   O VAL A 84  ? O VAL A 81  
AA1 4 5 N PHE A 85  ? N PHE A 82  O ASN A 119 ? O ASN A 116 
AA1 5 6 N LEU A 116 ? N LEU A 113 O ILE A 145 ? O ILE A 142 
# 
_pdbx_entry_details.entry_id                   9G4B 
_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 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD A GLU 153 ? ? OE1 A GLU 153 ? ? 1.168 1.252 -0.084 0.011 N 
2 1 CD A GLU 153 ? ? OE2 A GLU 153 ? ? 1.166 1.252 -0.086 0.011 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_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             CD 
_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             NE 
_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                92.74 
_pdbx_validate_rmsd_angle.angle_target_value         111.80 
_pdbx_validate_rmsd_angle.angle_deviation            -19.06 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 31  ? ? -148.06 59.18  
2 1 ALA A 59  ? ? -105.52 -83.85 
3 1 LYS A 117 ? ? 71.46   39.43  
4 1 ARG A 149 ? ? 80.26   7.17   
# 
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 
3 1 Y 1 A SER 0  ? A SER 3 
# 
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 
A1IIU OAR    O  N N 1   
A1IIU CAQ    C  N N 2   
A1IIU CAG    C  Y N 3   
A1IIU CAH    C  Y N 4   
A1IIU CAF    C  Y N 5   
A1IIU OAP    O  N N 6   
A1IIU CAE    C  Y N 7   
A1IIU CAD    C  Y N 8   
A1IIU CAC    C  Y N 9   
A1IIU SAB    S  N N 10  
A1IIU OAA    O  N N 11  
A1IIU OAI    O  N N 12  
A1IIU NAJ    N  N N 13  
A1IIU CAK    C  N N 14  
A1IIU SAL    S  N N 15  
A1IIU CAM    C  Y N 16  
A1IIU CAN    C  Y N 17  
A1IIU CLAO   CL N N 18  
A1IIU CAV    C  Y N 19  
A1IIU CAU    C  Y N 20  
A1IIU CAT    C  Y N 21  
A1IIU OAS    O  N N 22  
A1IIU CAW    C  Y N 23  
A1IIU NBJ    N  N N 24  
A1IIU CBI    C  N N 25  
A1IIU CBH    C  N N 26  
A1IIU CBG    C  N N 27  
A1IIU CBF    C  N N 28  
A1IIU CBE    C  N N 29  
A1IIU NAX    N  N N 30  
A1IIU CAY    C  N N 31  
A1IIU CAZ    C  N N 32  
A1IIU CBA    C  N N 33  
A1IIU NBB    N  N N 34  
A1IIU CBC    C  N N 35  
A1IIU CBD    C  N N 36  
A1IIU H1     H  N N 37  
A1IIU H2     H  N N 38  
A1IIU H3     H  N N 39  
A1IIU H4     H  N N 40  
A1IIU H6     H  N N 41  
A1IIU H7     H  N N 42  
A1IIU H8     H  N N 43  
A1IIU H9     H  N N 44  
A1IIU H10    H  N N 45  
A1IIU H11    H  N N 46  
A1IIU H12    H  N N 47  
A1IIU H13    H  N N 48  
A1IIU H14    H  N N 49  
A1IIU H15    H  N N 50  
A1IIU H16    H  N N 51  
A1IIU H17    H  N N 52  
A1IIU H18    H  N N 53  
A1IIU H19    H  N N 54  
A1IIU H20    H  N N 55  
A1IIU H21    H  N N 56  
A1IIU H22    H  N N 57  
A1IIU H23    H  N N 58  
A1IIU H24    H  N N 59  
A1IIU H26    H  N N 60  
A1IIU H27    H  N N 61  
A1IIU H28    H  N N 62  
A1IIU H29    H  N N 63  
ALA   N      N  N N 64  
ALA   CA     C  N S 65  
ALA   C      C  N N 66  
ALA   O      O  N N 67  
ALA   CB     C  N N 68  
ALA   OXT    O  N N 69  
ALA   H      H  N N 70  
ALA   H2     H  N N 71  
ALA   HA     H  N N 72  
ALA   HB1    H  N N 73  
ALA   HB2    H  N N 74  
ALA   HB3    H  N N 75  
ALA   HXT    H  N N 76  
ARG   N      N  N N 77  
ARG   CA     C  N S 78  
ARG   C      C  N N 79  
ARG   O      O  N N 80  
ARG   CB     C  N N 81  
ARG   CG     C  N N 82  
ARG   CD     C  N N 83  
ARG   NE     N  N N 84  
ARG   CZ     C  N N 85  
ARG   NH1    N  N N 86  
ARG   NH2    N  N N 87  
ARG   OXT    O  N N 88  
ARG   H      H  N N 89  
ARG   H2     H  N N 90  
ARG   HA     H  N N 91  
ARG   HB2    H  N N 92  
ARG   HB3    H  N N 93  
ARG   HG2    H  N N 94  
ARG   HG3    H  N N 95  
ARG   HD2    H  N N 96  
ARG   HD3    H  N N 97  
ARG   HE     H  N N 98  
ARG   HH11   H  N N 99  
ARG   HH12   H  N N 100 
ARG   HH21   H  N N 101 
ARG   HH22   H  N N 102 
ARG   HXT    H  N N 103 
ASN   N      N  N N 104 
ASN   CA     C  N S 105 
ASN   C      C  N N 106 
ASN   O      O  N N 107 
ASN   CB     C  N N 108 
ASN   CG     C  N N 109 
ASN   OD1    O  N N 110 
ASN   ND2    N  N N 111 
ASN   OXT    O  N N 112 
ASN   H      H  N N 113 
ASN   H2     H  N N 114 
ASN   HA     H  N N 115 
ASN   HB2    H  N N 116 
ASN   HB3    H  N N 117 
ASN   HD21   H  N N 118 
ASN   HD22   H  N N 119 
ASN   HXT    H  N N 120 
ASP   N      N  N N 121 
ASP   CA     C  N S 122 
ASP   C      C  N N 123 
ASP   O      O  N N 124 
ASP   CB     C  N N 125 
ASP   CG     C  N N 126 
ASP   OD1    O  N N 127 
ASP   OD2    O  N N 128 
ASP   OXT    O  N N 129 
ASP   H      H  N N 130 
ASP   H2     H  N N 131 
ASP   HA     H  N N 132 
ASP   HB2    H  N N 133 
ASP   HB3    H  N N 134 
ASP   HD2    H  N N 135 
ASP   HXT    H  N N 136 
CYS   N      N  N N 137 
CYS   CA     C  N R 138 
CYS   C      C  N N 139 
CYS   O      O  N N 140 
CYS   CB     C  N N 141 
CYS   SG     S  N N 142 
CYS   OXT    O  N N 143 
CYS   H      H  N N 144 
CYS   H2     H  N N 145 
CYS   HA     H  N N 146 
CYS   HB2    H  N N 147 
CYS   HB3    H  N N 148 
CYS   HG     H  N N 149 
CYS   HXT    H  N N 150 
EDO   C1     C  N N 151 
EDO   O1     O  N N 152 
EDO   C2     C  N N 153 
EDO   O2     O  N N 154 
EDO   H11    H  N N 155 
EDO   H12    H  N N 156 
EDO   HO1    H  N N 157 
EDO   H21    H  N N 158 
EDO   H22    H  N N 159 
EDO   HO2    H  N N 160 
GDP   PB     P  N N 161 
GDP   O1B    O  N N 162 
GDP   O2B    O  N N 163 
GDP   O3B    O  N N 164 
GDP   O3A    O  N N 165 
GDP   PA     P  N N 166 
GDP   O1A    O  N N 167 
GDP   O2A    O  N N 168 
GDP   "O5'"  O  N N 169 
GDP   "C5'"  C  N N 170 
GDP   "C4'"  C  N R 171 
GDP   "O4'"  O  N N 172 
GDP   "C3'"  C  N S 173 
GDP   "O3'"  O  N N 174 
GDP   "C2'"  C  N R 175 
GDP   "O2'"  O  N N 176 
GDP   "C1'"  C  N R 177 
GDP   N9     N  Y N 178 
GDP   C8     C  Y N 179 
GDP   N7     N  Y N 180 
GDP   C5     C  Y N 181 
GDP   C6     C  N N 182 
GDP   O6     O  N N 183 
GDP   N1     N  N N 184 
GDP   C2     C  N N 185 
GDP   N2     N  N N 186 
GDP   N3     N  N N 187 
GDP   C4     C  Y N 188 
GDP   HOB2   H  N N 189 
GDP   HOB3   H  N N 190 
GDP   HOA2   H  N N 191 
GDP   "H5'"  H  N N 192 
GDP   "H5''" H  N N 193 
GDP   "H4'"  H  N N 194 
GDP   "H3'"  H  N N 195 
GDP   "HO3'" H  N N 196 
GDP   "H2'"  H  N N 197 
GDP   "HO2'" H  N N 198 
GDP   "H1'"  H  N N 199 
GDP   H8     H  N N 200 
GDP   HN1    H  N N 201 
GDP   HN21   H  N N 202 
GDP   HN22   H  N N 203 
GLN   N      N  N N 204 
GLN   CA     C  N S 205 
GLN   C      C  N N 206 
GLN   O      O  N N 207 
GLN   CB     C  N N 208 
GLN   CG     C  N N 209 
GLN   CD     C  N N 210 
GLN   OE1    O  N N 211 
GLN   NE2    N  N N 212 
GLN   OXT    O  N N 213 
GLN   H      H  N N 214 
GLN   H2     H  N N 215 
GLN   HA     H  N N 216 
GLN   HB2    H  N N 217 
GLN   HB3    H  N N 218 
GLN   HG2    H  N N 219 
GLN   HG3    H  N N 220 
GLN   HE21   H  N N 221 
GLN   HE22   H  N N 222 
GLN   HXT    H  N N 223 
GLU   N      N  N N 224 
GLU   CA     C  N S 225 
GLU   C      C  N N 226 
GLU   O      O  N N 227 
GLU   CB     C  N N 228 
GLU   CG     C  N N 229 
GLU   CD     C  N N 230 
GLU   OE1    O  N N 231 
GLU   OE2    O  N N 232 
GLU   OXT    O  N N 233 
GLU   H      H  N N 234 
GLU   H2     H  N N 235 
GLU   HA     H  N N 236 
GLU   HB2    H  N N 237 
GLU   HB3    H  N N 238 
GLU   HG2    H  N N 239 
GLU   HG3    H  N N 240 
GLU   HE2    H  N N 241 
GLU   HXT    H  N N 242 
GLY   N      N  N N 243 
GLY   CA     C  N N 244 
GLY   C      C  N N 245 
GLY   O      O  N N 246 
GLY   OXT    O  N N 247 
GLY   H      H  N N 248 
GLY   H2     H  N N 249 
GLY   HA2    H  N N 250 
GLY   HA3    H  N N 251 
GLY   HXT    H  N N 252 
HIS   N      N  N N 253 
HIS   CA     C  N S 254 
HIS   C      C  N N 255 
HIS   O      O  N N 256 
HIS   CB     C  N N 257 
HIS   CG     C  Y N 258 
HIS   ND1    N  Y N 259 
HIS   CD2    C  Y N 260 
HIS   CE1    C  Y N 261 
HIS   NE2    N  Y N 262 
HIS   OXT    O  N N 263 
HIS   H      H  N N 264 
HIS   H2     H  N N 265 
HIS   HA     H  N N 266 
HIS   HB2    H  N N 267 
HIS   HB3    H  N N 268 
HIS   HD1    H  N N 269 
HIS   HD2    H  N N 270 
HIS   HE1    H  N N 271 
HIS   HE2    H  N N 272 
HIS   HXT    H  N N 273 
HOH   O      O  N N 274 
HOH   H1     H  N N 275 
HOH   H2     H  N N 276 
ILE   N      N  N N 277 
ILE   CA     C  N S 278 
ILE   C      C  N N 279 
ILE   O      O  N N 280 
ILE   CB     C  N S 281 
ILE   CG1    C  N N 282 
ILE   CG2    C  N N 283 
ILE   CD1    C  N N 284 
ILE   OXT    O  N N 285 
ILE   H      H  N N 286 
ILE   H2     H  N N 287 
ILE   HA     H  N N 288 
ILE   HB     H  N N 289 
ILE   HG12   H  N N 290 
ILE   HG13   H  N N 291 
ILE   HG21   H  N N 292 
ILE   HG22   H  N N 293 
ILE   HG23   H  N N 294 
ILE   HD11   H  N N 295 
ILE   HD12   H  N N 296 
ILE   HD13   H  N N 297 
ILE   HXT    H  N N 298 
LEU   N      N  N N 299 
LEU   CA     C  N S 300 
LEU   C      C  N N 301 
LEU   O      O  N N 302 
LEU   CB     C  N N 303 
LEU   CG     C  N N 304 
LEU   CD1    C  N N 305 
LEU   CD2    C  N N 306 
LEU   OXT    O  N N 307 
LEU   H      H  N N 308 
LEU   H2     H  N N 309 
LEU   HA     H  N N 310 
LEU   HB2    H  N N 311 
LEU   HB3    H  N N 312 
LEU   HG     H  N N 313 
LEU   HD11   H  N N 314 
LEU   HD12   H  N N 315 
LEU   HD13   H  N N 316 
LEU   HD21   H  N N 317 
LEU   HD22   H  N N 318 
LEU   HD23   H  N N 319 
LEU   HXT    H  N N 320 
LYS   N      N  N N 321 
LYS   CA     C  N S 322 
LYS   C      C  N N 323 
LYS   O      O  N N 324 
LYS   CB     C  N N 325 
LYS   CG     C  N N 326 
LYS   CD     C  N N 327 
LYS   CE     C  N N 328 
LYS   NZ     N  N N 329 
LYS   OXT    O  N N 330 
LYS   H      H  N N 331 
LYS   H2     H  N N 332 
LYS   HA     H  N N 333 
LYS   HB2    H  N N 334 
LYS   HB3    H  N N 335 
LYS   HG2    H  N N 336 
LYS   HG3    H  N N 337 
LYS   HD2    H  N N 338 
LYS   HD3    H  N N 339 
LYS   HE2    H  N N 340 
LYS   HE3    H  N N 341 
LYS   HZ1    H  N N 342 
LYS   HZ2    H  N N 343 
LYS   HZ3    H  N N 344 
LYS   HXT    H  N N 345 
MET   N      N  N N 346 
MET   CA     C  N S 347 
MET   C      C  N N 348 
MET   O      O  N N 349 
MET   CB     C  N N 350 
MET   CG     C  N N 351 
MET   SD     S  N N 352 
MET   CE     C  N N 353 
MET   OXT    O  N N 354 
MET   H      H  N N 355 
MET   H2     H  N N 356 
MET   HA     H  N N 357 
MET   HB2    H  N N 358 
MET   HB3    H  N N 359 
MET   HG2    H  N N 360 
MET   HG3    H  N N 361 
MET   HE1    H  N N 362 
MET   HE2    H  N N 363 
MET   HE3    H  N N 364 
MET   HXT    H  N N 365 
MG    MG     MG N N 366 
PHE   N      N  N N 367 
PHE   CA     C  N S 368 
PHE   C      C  N N 369 
PHE   O      O  N N 370 
PHE   CB     C  N N 371 
PHE   CG     C  Y N 372 
PHE   CD1    C  Y N 373 
PHE   CD2    C  Y N 374 
PHE   CE1    C  Y N 375 
PHE   CE2    C  Y N 376 
PHE   CZ     C  Y N 377 
PHE   OXT    O  N N 378 
PHE   H      H  N N 379 
PHE   H2     H  N N 380 
PHE   HA     H  N N 381 
PHE   HB2    H  N N 382 
PHE   HB3    H  N N 383 
PHE   HD1    H  N N 384 
PHE   HD2    H  N N 385 
PHE   HE1    H  N N 386 
PHE   HE2    H  N N 387 
PHE   HZ     H  N N 388 
PHE   HXT    H  N N 389 
PRO   N      N  N N 390 
PRO   CA     C  N S 391 
PRO   C      C  N N 392 
PRO   O      O  N N 393 
PRO   CB     C  N N 394 
PRO   CG     C  N N 395 
PRO   CD     C  N N 396 
PRO   OXT    O  N N 397 
PRO   H      H  N N 398 
PRO   HA     H  N N 399 
PRO   HB2    H  N N 400 
PRO   HB3    H  N N 401 
PRO   HG2    H  N N 402 
PRO   HG3    H  N N 403 
PRO   HD2    H  N N 404 
PRO   HD3    H  N N 405 
PRO   HXT    H  N N 406 
SER   N      N  N N 407 
SER   CA     C  N S 408 
SER   C      C  N N 409 
SER   O      O  N N 410 
SER   CB     C  N N 411 
SER   OG     O  N N 412 
SER   OXT    O  N N 413 
SER   H      H  N N 414 
SER   H2     H  N N 415 
SER   HA     H  N N 416 
SER   HB2    H  N N 417 
SER   HB3    H  N N 418 
SER   HG     H  N N 419 
SER   HXT    H  N N 420 
THR   N      N  N N 421 
THR   CA     C  N S 422 
THR   C      C  N N 423 
THR   O      O  N N 424 
THR   CB     C  N R 425 
THR   OG1    O  N N 426 
THR   CG2    C  N N 427 
THR   OXT    O  N N 428 
THR   H      H  N N 429 
THR   H2     H  N N 430 
THR   HA     H  N N 431 
THR   HB     H  N N 432 
THR   HG1    H  N N 433 
THR   HG21   H  N N 434 
THR   HG22   H  N N 435 
THR   HG23   H  N N 436 
THR   HXT    H  N N 437 
TYR   N      N  N N 438 
TYR   CA     C  N S 439 
TYR   C      C  N N 440 
TYR   O      O  N N 441 
TYR   CB     C  N N 442 
TYR   CG     C  Y N 443 
TYR   CD1    C  Y N 444 
TYR   CD2    C  Y N 445 
TYR   CE1    C  Y N 446 
TYR   CE2    C  Y N 447 
TYR   CZ     C  Y N 448 
TYR   OH     O  N N 449 
TYR   OXT    O  N N 450 
TYR   H      H  N N 451 
TYR   H2     H  N N 452 
TYR   HA     H  N N 453 
TYR   HB2    H  N N 454 
TYR   HB3    H  N N 455 
TYR   HD1    H  N N 456 
TYR   HD2    H  N N 457 
TYR   HE1    H  N N 458 
TYR   HE2    H  N N 459 
TYR   HH     H  N N 460 
TYR   HXT    H  N N 461 
VAL   N      N  N N 462 
VAL   CA     C  N S 463 
VAL   C      C  N N 464 
VAL   O      O  N N 465 
VAL   CB     C  N N 466 
VAL   CG1    C  N N 467 
VAL   CG2    C  N N 468 
VAL   OXT    O  N N 469 
VAL   H      H  N N 470 
VAL   H2     H  N N 471 
VAL   HA     H  N N 472 
VAL   HB     H  N N 473 
VAL   HG11   H  N N 474 
VAL   HG12   H  N N 475 
VAL   HG13   H  N N 476 
VAL   HG21   H  N N 477 
VAL   HG22   H  N N 478 
VAL   HG23   H  N N 479 
VAL   HXT    H  N N 480 
# 
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 
A1IIU OAS   CAT    sing N N 1   
A1IIU CAU   CAT    doub Y N 2   
A1IIU CAU   CAV    sing Y N 3   
A1IIU CAT   CAW    sing Y N 4   
A1IIU CAV   CAN    doub Y N 5   
A1IIU CBH   CBI    sing N N 6   
A1IIU CBH   CBG    sing N N 7   
A1IIU CBI   NBJ    sing N N 8   
A1IIU CAW   NBJ    sing N N 9   
A1IIU CAW   CAM    doub Y N 10  
A1IIU NBB   CBA    sing N N 11  
A1IIU NBB   CBC    sing N N 12  
A1IIU CAN   CAM    sing Y N 13  
A1IIU CAN   CLAO   sing N N 14  
A1IIU NBJ   CAK    sing N N 15  
A1IIU CBF   CBG    sing N N 16  
A1IIU CBF   CBE    sing N N 17  
A1IIU CAM   SAL    sing N N 18  
A1IIU CBA   CAZ    sing N N 19  
A1IIU CBC   CBD    sing N N 20  
A1IIU CAZ   CAY    sing N N 21  
A1IIU CBD   CAY    sing N N 22  
A1IIU CAK   SAL    sing N N 23  
A1IIU CAK   NAJ    doub N N 24  
A1IIU CBE   NAX    sing N N 25  
A1IIU CAY   NAX    sing N N 26  
A1IIU NAJ   SAB    sing N N 27  
A1IIU NAX   CAQ    sing N N 28  
A1IIU CAQ   CAG    sing N N 29  
A1IIU CAQ   OAR    doub N N 30  
A1IIU CAH   CAG    doub Y N 31  
A1IIU CAH   CAC    sing Y N 32  
A1IIU SAB   CAC    sing N N 33  
A1IIU SAB   OAI    doub N N 34  
A1IIU SAB   OAA    doub N N 35  
A1IIU CAG   CAF    sing Y N 36  
A1IIU CAC   CAD    doub Y N 37  
A1IIU CAF   OAP    sing N N 38  
A1IIU CAF   CAE    doub Y N 39  
A1IIU CAD   CAE    sing Y N 40  
A1IIU CAH   H1     sing N N 41  
A1IIU OAP   H2     sing N N 42  
A1IIU CAE   H3     sing N N 43  
A1IIU CAD   H4     sing N N 44  
A1IIU CAV   H6     sing N N 45  
A1IIU CAU   H7     sing N N 46  
A1IIU OAS   H8     sing N N 47  
A1IIU CBI   H9     sing N N 48  
A1IIU CBI   H10    sing N N 49  
A1IIU CBH   H11    sing N N 50  
A1IIU CBH   H12    sing N N 51  
A1IIU CBG   H13    sing N N 52  
A1IIU CBG   H14    sing N N 53  
A1IIU CBF   H15    sing N N 54  
A1IIU CBF   H16    sing N N 55  
A1IIU CBE   H17    sing N N 56  
A1IIU CBE   H18    sing N N 57  
A1IIU CAY   H19    sing N N 58  
A1IIU CAZ   H20    sing N N 59  
A1IIU CAZ   H21    sing N N 60  
A1IIU CBA   H22    sing N N 61  
A1IIU CBA   H23    sing N N 62  
A1IIU NBB   H24    sing N N 63  
A1IIU CBC   H26    sing N N 64  
A1IIU CBC   H27    sing N N 65  
A1IIU CBD   H28    sing N N 66  
A1IIU CBD   H29    sing N N 67  
ALA   N     CA     sing N N 68  
ALA   N     H      sing N N 69  
ALA   N     H2     sing N N 70  
ALA   CA    C      sing N N 71  
ALA   CA    CB     sing N N 72  
ALA   CA    HA     sing N N 73  
ALA   C     O      doub N N 74  
ALA   C     OXT    sing N N 75  
ALA   CB    HB1    sing N N 76  
ALA   CB    HB2    sing N N 77  
ALA   CB    HB3    sing N N 78  
ALA   OXT   HXT    sing N N 79  
ARG   N     CA     sing N N 80  
ARG   N     H      sing N N 81  
ARG   N     H2     sing N N 82  
ARG   CA    C      sing N N 83  
ARG   CA    CB     sing N N 84  
ARG   CA    HA     sing N N 85  
ARG   C     O      doub N N 86  
ARG   C     OXT    sing N N 87  
ARG   CB    CG     sing N N 88  
ARG   CB    HB2    sing N N 89  
ARG   CB    HB3    sing N N 90  
ARG   CG    CD     sing N N 91  
ARG   CG    HG2    sing N N 92  
ARG   CG    HG3    sing N N 93  
ARG   CD    NE     sing N N 94  
ARG   CD    HD2    sing N N 95  
ARG   CD    HD3    sing N N 96  
ARG   NE    CZ     sing N N 97  
ARG   NE    HE     sing N N 98  
ARG   CZ    NH1    sing N N 99  
ARG   CZ    NH2    doub N N 100 
ARG   NH1   HH11   sing N N 101 
ARG   NH1   HH12   sing N N 102 
ARG   NH2   HH21   sing N N 103 
ARG   NH2   HH22   sing N N 104 
ARG   OXT   HXT    sing N N 105 
ASN   N     CA     sing N N 106 
ASN   N     H      sing N N 107 
ASN   N     H2     sing N N 108 
ASN   CA    C      sing N N 109 
ASN   CA    CB     sing N N 110 
ASN   CA    HA     sing N N 111 
ASN   C     O      doub N N 112 
ASN   C     OXT    sing N N 113 
ASN   CB    CG     sing N N 114 
ASN   CB    HB2    sing N N 115 
ASN   CB    HB3    sing N N 116 
ASN   CG    OD1    doub N N 117 
ASN   CG    ND2    sing N N 118 
ASN   ND2   HD21   sing N N 119 
ASN   ND2   HD22   sing N N 120 
ASN   OXT   HXT    sing N N 121 
ASP   N     CA     sing N N 122 
ASP   N     H      sing N N 123 
ASP   N     H2     sing N N 124 
ASP   CA    C      sing N N 125 
ASP   CA    CB     sing N N 126 
ASP   CA    HA     sing N N 127 
ASP   C     O      doub N N 128 
ASP   C     OXT    sing N N 129 
ASP   CB    CG     sing N N 130 
ASP   CB    HB2    sing N N 131 
ASP   CB    HB3    sing N N 132 
ASP   CG    OD1    doub N N 133 
ASP   CG    OD2    sing N N 134 
ASP   OD2   HD2    sing N N 135 
ASP   OXT   HXT    sing N N 136 
CYS   N     CA     sing N N 137 
CYS   N     H      sing N N 138 
CYS   N     H2     sing N N 139 
CYS   CA    C      sing N N 140 
CYS   CA    CB     sing N N 141 
CYS   CA    HA     sing N N 142 
CYS   C     O      doub N N 143 
CYS   C     OXT    sing N N 144 
CYS   CB    SG     sing N N 145 
CYS   CB    HB2    sing N N 146 
CYS   CB    HB3    sing N N 147 
CYS   SG    HG     sing N N 148 
CYS   OXT   HXT    sing N N 149 
EDO   C1    O1     sing N N 150 
EDO   C1    C2     sing N N 151 
EDO   C1    H11    sing N N 152 
EDO   C1    H12    sing N N 153 
EDO   O1    HO1    sing N N 154 
EDO   C2    O2     sing N N 155 
EDO   C2    H21    sing N N 156 
EDO   C2    H22    sing N N 157 
EDO   O2    HO2    sing N N 158 
GDP   PB    O1B    doub N N 159 
GDP   PB    O2B    sing N N 160 
GDP   PB    O3B    sing N N 161 
GDP   PB    O3A    sing N N 162 
GDP   O2B   HOB2   sing N N 163 
GDP   O3B   HOB3   sing N N 164 
GDP   O3A   PA     sing N N 165 
GDP   PA    O1A    doub N N 166 
GDP   PA    O2A    sing N N 167 
GDP   PA    "O5'"  sing N N 168 
GDP   O2A   HOA2   sing N N 169 
GDP   "O5'" "C5'"  sing N N 170 
GDP   "C5'" "C4'"  sing N N 171 
GDP   "C5'" "H5'"  sing N N 172 
GDP   "C5'" "H5''" sing N N 173 
GDP   "C4'" "O4'"  sing N N 174 
GDP   "C4'" "C3'"  sing N N 175 
GDP   "C4'" "H4'"  sing N N 176 
GDP   "O4'" "C1'"  sing N N 177 
GDP   "C3'" "O3'"  sing N N 178 
GDP   "C3'" "C2'"  sing N N 179 
GDP   "C3'" "H3'"  sing N N 180 
GDP   "O3'" "HO3'" sing N N 181 
GDP   "C2'" "O2'"  sing N N 182 
GDP   "C2'" "C1'"  sing N N 183 
GDP   "C2'" "H2'"  sing N N 184 
GDP   "O2'" "HO2'" sing N N 185 
GDP   "C1'" N9     sing N N 186 
GDP   "C1'" "H1'"  sing N N 187 
GDP   N9    C8     sing Y N 188 
GDP   N9    C4     sing Y N 189 
GDP   C8    N7     doub Y N 190 
GDP   C8    H8     sing N N 191 
GDP   N7    C5     sing Y N 192 
GDP   C5    C6     sing N N 193 
GDP   C5    C4     doub Y N 194 
GDP   C6    O6     doub N N 195 
GDP   C6    N1     sing N N 196 
GDP   N1    C2     sing N N 197 
GDP   N1    HN1    sing N N 198 
GDP   C2    N2     sing N N 199 
GDP   C2    N3     doub N N 200 
GDP   N2    HN21   sing N N 201 
GDP   N2    HN22   sing N N 202 
GDP   N3    C4     sing N N 203 
GLN   N     CA     sing N N 204 
GLN   N     H      sing N N 205 
GLN   N     H2     sing N N 206 
GLN   CA    C      sing N N 207 
GLN   CA    CB     sing N N 208 
GLN   CA    HA     sing N N 209 
GLN   C     O      doub N N 210 
GLN   C     OXT    sing N N 211 
GLN   CB    CG     sing N N 212 
GLN   CB    HB2    sing N N 213 
GLN   CB    HB3    sing N N 214 
GLN   CG    CD     sing N N 215 
GLN   CG    HG2    sing N N 216 
GLN   CG    HG3    sing N N 217 
GLN   CD    OE1    doub N N 218 
GLN   CD    NE2    sing N N 219 
GLN   NE2   HE21   sing N N 220 
GLN   NE2   HE22   sing N N 221 
GLN   OXT   HXT    sing N N 222 
GLU   N     CA     sing N N 223 
GLU   N     H      sing N N 224 
GLU   N     H2     sing N N 225 
GLU   CA    C      sing N N 226 
GLU   CA    CB     sing N N 227 
GLU   CA    HA     sing N N 228 
GLU   C     O      doub N N 229 
GLU   C     OXT    sing N N 230 
GLU   CB    CG     sing N N 231 
GLU   CB    HB2    sing N N 232 
GLU   CB    HB3    sing N N 233 
GLU   CG    CD     sing N N 234 
GLU   CG    HG2    sing N N 235 
GLU   CG    HG3    sing N N 236 
GLU   CD    OE1    doub N N 237 
GLU   CD    OE2    sing N N 238 
GLU   OE2   HE2    sing N N 239 
GLU   OXT   HXT    sing N N 240 
GLY   N     CA     sing N N 241 
GLY   N     H      sing N N 242 
GLY   N     H2     sing N N 243 
GLY   CA    C      sing N N 244 
GLY   CA    HA2    sing N N 245 
GLY   CA    HA3    sing N N 246 
GLY   C     O      doub N N 247 
GLY   C     OXT    sing N N 248 
GLY   OXT   HXT    sing N N 249 
HIS   N     CA     sing N N 250 
HIS   N     H      sing N N 251 
HIS   N     H2     sing N N 252 
HIS   CA    C      sing N N 253 
HIS   CA    CB     sing N N 254 
HIS   CA    HA     sing N N 255 
HIS   C     O      doub N N 256 
HIS   C     OXT    sing N N 257 
HIS   CB    CG     sing N N 258 
HIS   CB    HB2    sing N N 259 
HIS   CB    HB3    sing N N 260 
HIS   CG    ND1    sing Y N 261 
HIS   CG    CD2    doub Y N 262 
HIS   ND1   CE1    doub Y N 263 
HIS   ND1   HD1    sing N N 264 
HIS   CD2   NE2    sing Y N 265 
HIS   CD2   HD2    sing N N 266 
HIS   CE1   NE2    sing Y N 267 
HIS   CE1   HE1    sing N N 268 
HIS   NE2   HE2    sing N N 269 
HIS   OXT   HXT    sing N N 270 
HOH   O     H1     sing N N 271 
HOH   O     H2     sing N N 272 
ILE   N     CA     sing N N 273 
ILE   N     H      sing N N 274 
ILE   N     H2     sing N N 275 
ILE   CA    C      sing N N 276 
ILE   CA    CB     sing N N 277 
ILE   CA    HA     sing N N 278 
ILE   C     O      doub N N 279 
ILE   C     OXT    sing N N 280 
ILE   CB    CG1    sing N N 281 
ILE   CB    CG2    sing N N 282 
ILE   CB    HB     sing N N 283 
ILE   CG1   CD1    sing N N 284 
ILE   CG1   HG12   sing N N 285 
ILE   CG1   HG13   sing N N 286 
ILE   CG2   HG21   sing N N 287 
ILE   CG2   HG22   sing N N 288 
ILE   CG2   HG23   sing N N 289 
ILE   CD1   HD11   sing N N 290 
ILE   CD1   HD12   sing N N 291 
ILE   CD1   HD13   sing N N 292 
ILE   OXT   HXT    sing N N 293 
LEU   N     CA     sing N N 294 
LEU   N     H      sing N N 295 
LEU   N     H2     sing N N 296 
LEU   CA    C      sing N N 297 
LEU   CA    CB     sing N N 298 
LEU   CA    HA     sing N N 299 
LEU   C     O      doub N N 300 
LEU   C     OXT    sing N N 301 
LEU   CB    CG     sing N N 302 
LEU   CB    HB2    sing N N 303 
LEU   CB    HB3    sing N N 304 
LEU   CG    CD1    sing N N 305 
LEU   CG    CD2    sing N N 306 
LEU   CG    HG     sing N N 307 
LEU   CD1   HD11   sing N N 308 
LEU   CD1   HD12   sing N N 309 
LEU   CD1   HD13   sing N N 310 
LEU   CD2   HD21   sing N N 311 
LEU   CD2   HD22   sing N N 312 
LEU   CD2   HD23   sing N N 313 
LEU   OXT   HXT    sing N N 314 
LYS   N     CA     sing N N 315 
LYS   N     H      sing N N 316 
LYS   N     H2     sing N N 317 
LYS   CA    C      sing N N 318 
LYS   CA    CB     sing N N 319 
LYS   CA    HA     sing N N 320 
LYS   C     O      doub N N 321 
LYS   C     OXT    sing N N 322 
LYS   CB    CG     sing N N 323 
LYS   CB    HB2    sing N N 324 
LYS   CB    HB3    sing N N 325 
LYS   CG    CD     sing N N 326 
LYS   CG    HG2    sing N N 327 
LYS   CG    HG3    sing N N 328 
LYS   CD    CE     sing N N 329 
LYS   CD    HD2    sing N N 330 
LYS   CD    HD3    sing N N 331 
LYS   CE    NZ     sing N N 332 
LYS   CE    HE2    sing N N 333 
LYS   CE    HE3    sing N N 334 
LYS   NZ    HZ1    sing N N 335 
LYS   NZ    HZ2    sing N N 336 
LYS   NZ    HZ3    sing N N 337 
LYS   OXT   HXT    sing N N 338 
MET   N     CA     sing N N 339 
MET   N     H      sing N N 340 
MET   N     H2     sing N N 341 
MET   CA    C      sing N N 342 
MET   CA    CB     sing N N 343 
MET   CA    HA     sing N N 344 
MET   C     O      doub N N 345 
MET   C     OXT    sing N N 346 
MET   CB    CG     sing N N 347 
MET   CB    HB2    sing N N 348 
MET   CB    HB3    sing N N 349 
MET   CG    SD     sing N N 350 
MET   CG    HG2    sing N N 351 
MET   CG    HG3    sing N N 352 
MET   SD    CE     sing N N 353 
MET   CE    HE1    sing N N 354 
MET   CE    HE2    sing N N 355 
MET   CE    HE3    sing N N 356 
MET   OXT   HXT    sing N N 357 
PHE   N     CA     sing N N 358 
PHE   N     H      sing N N 359 
PHE   N     H2     sing N N 360 
PHE   CA    C      sing N N 361 
PHE   CA    CB     sing N N 362 
PHE   CA    HA     sing N N 363 
PHE   C     O      doub N N 364 
PHE   C     OXT    sing N N 365 
PHE   CB    CG     sing N N 366 
PHE   CB    HB2    sing N N 367 
PHE   CB    HB3    sing N N 368 
PHE   CG    CD1    doub Y N 369 
PHE   CG    CD2    sing Y N 370 
PHE   CD1   CE1    sing Y N 371 
PHE   CD1   HD1    sing N N 372 
PHE   CD2   CE2    doub Y N 373 
PHE   CD2   HD2    sing N N 374 
PHE   CE1   CZ     doub Y N 375 
PHE   CE1   HE1    sing N N 376 
PHE   CE2   CZ     sing Y N 377 
PHE   CE2   HE2    sing N N 378 
PHE   CZ    HZ     sing N N 379 
PHE   OXT   HXT    sing N N 380 
PRO   N     CA     sing N N 381 
PRO   N     CD     sing N N 382 
PRO   N     H      sing N N 383 
PRO   CA    C      sing N N 384 
PRO   CA    CB     sing N N 385 
PRO   CA    HA     sing N N 386 
PRO   C     O      doub N N 387 
PRO   C     OXT    sing N N 388 
PRO   CB    CG     sing N N 389 
PRO   CB    HB2    sing N N 390 
PRO   CB    HB3    sing N N 391 
PRO   CG    CD     sing N N 392 
PRO   CG    HG2    sing N N 393 
PRO   CG    HG3    sing N N 394 
PRO   CD    HD2    sing N N 395 
PRO   CD    HD3    sing N N 396 
PRO   OXT   HXT    sing N N 397 
SER   N     CA     sing N N 398 
SER   N     H      sing N N 399 
SER   N     H2     sing N N 400 
SER   CA    C      sing N N 401 
SER   CA    CB     sing N N 402 
SER   CA    HA     sing N N 403 
SER   C     O      doub N N 404 
SER   C     OXT    sing N N 405 
SER   CB    OG     sing N N 406 
SER   CB    HB2    sing N N 407 
SER   CB    HB3    sing N N 408 
SER   OG    HG     sing N N 409 
SER   OXT   HXT    sing N N 410 
THR   N     CA     sing N N 411 
THR   N     H      sing N N 412 
THR   N     H2     sing N N 413 
THR   CA    C      sing N N 414 
THR   CA    CB     sing N N 415 
THR   CA    HA     sing N N 416 
THR   C     O      doub N N 417 
THR   C     OXT    sing N N 418 
THR   CB    OG1    sing N N 419 
THR   CB    CG2    sing N N 420 
THR   CB    HB     sing N N 421 
THR   OG1   HG1    sing N N 422 
THR   CG2   HG21   sing N N 423 
THR   CG2   HG22   sing N N 424 
THR   CG2   HG23   sing N N 425 
THR   OXT   HXT    sing N N 426 
TYR   N     CA     sing N N 427 
TYR   N     H      sing N N 428 
TYR   N     H2     sing N N 429 
TYR   CA    C      sing N N 430 
TYR   CA    CB     sing N N 431 
TYR   CA    HA     sing N N 432 
TYR   C     O      doub N N 433 
TYR   C     OXT    sing N N 434 
TYR   CB    CG     sing N N 435 
TYR   CB    HB2    sing N N 436 
TYR   CB    HB3    sing N N 437 
TYR   CG    CD1    doub Y N 438 
TYR   CG    CD2    sing Y N 439 
TYR   CD1   CE1    sing Y N 440 
TYR   CD1   HD1    sing N N 441 
TYR   CD2   CE2    doub Y N 442 
TYR   CD2   HD2    sing N N 443 
TYR   CE1   CZ     doub Y N 444 
TYR   CE1   HE1    sing N N 445 
TYR   CE2   CZ     sing Y N 446 
TYR   CE2   HE2    sing N N 447 
TYR   CZ    OH     sing N N 448 
TYR   OH    HH     sing N N 449 
TYR   OXT   HXT    sing N N 450 
VAL   N     CA     sing N N 451 
VAL   N     H      sing N N 452 
VAL   N     H2     sing N N 453 
VAL   CA    C      sing N N 454 
VAL   CA    CB     sing N N 455 
VAL   CA    HA     sing N N 456 
VAL   C     O      doub N N 457 
VAL   C     OXT    sing N N 458 
VAL   CB    CG1    sing N N 459 
VAL   CB    CG2    sing N N 460 
VAL   CB    HB     sing N N 461 
VAL   CG1   HG11   sing N N 462 
VAL   CG1   HG12   sing N N 463 
VAL   CG1   HG13   sing N N 464 
VAL   CG2   HG21   sing N N 465 
VAL   CG2   HG22   sing N N 466 
VAL   CG2   HG23   sing N N 467 
VAL   OXT   HXT    sing N N 468 
# 
_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                    9G4B 
_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]   0.027020 
_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]   0.024913 
_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]   0.009037 
_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     . MET   A 1 4   ? -17.084 21.449 -4.897 1.00 40.70 ? 1   MET   A N     1 
ATOM   2    C  CA    . MET   A 1 4   ? -16.353 21.956 -3.686 1.00 39.06 ? 1   MET   A CA    1 
ATOM   3    C  C     . MET   A 1 4   ? -16.779 21.240 -2.405 1.00 34.29 ? 1   MET   A C     1 
ATOM   4    O  O     . MET   A 1 4   ? -17.965 21.175 -2.101 1.00 36.29 ? 1   MET   A O     1 
ATOM   5    C  CB    . MET   A 1 4   ? -16.587 23.459 -3.476 1.00 44.53 ? 1   MET   A CB    1 
ATOM   6    C  CG    . MET   A 1 4   ? -15.450 24.168 -2.756 1.00 43.64 ? 1   MET   A CG    1 
ATOM   7    S  SD    . MET   A 1 4   ? -13.896 24.262 -3.670 1.00 33.78 ? 1   MET   A SD    1 
ATOM   8    C  CE    . MET   A 1 4   ? -14.437 24.507 -5.367 1.00 40.16 ? 1   MET   A CE    1 
ATOM   9    N  N     . THR   A 1 5   ? -15.806 20.726 -1.663 1.00 28.22 ? 2   THR   A N     1 
ATOM   10   C  CA    . THR   A 1 5   ? -16.040 20.172 -0.333 1.00 21.93 ? 2   THR   A CA    1 
ATOM   11   C  C     . THR   A 1 5   ? -15.023 20.843 0.593  1.00 22.81 ? 2   THR   A C     1 
ATOM   12   O  O     . THR   A 1 5   ? -13.852 20.906 0.249  1.00 26.10 ? 2   THR   A O     1 
ATOM   13   C  CB    . THR   A 1 5   ? -15.871 18.654 -0.376 1.00 23.16 ? 2   THR   A CB    1 
ATOM   14   O  OG1   . THR   A 1 5   ? -16.796 18.116 -1.333 1.00 24.63 ? 2   THR   A OG1   1 
ATOM   15   C  CG2   . THR   A 1 5   ? -16.117 18.023 0.987  1.00 27.89 ? 2   THR   A CG2   1 
ATOM   16   N  N     . GLU   A 1 6   ? -15.490 21.360 1.731  1.00 18.99 ? 3   GLU   A N     1 
ATOM   17   C  CA    . GLU   A 1 6   ? -14.642 22.022 2.727  1.00 18.15 ? 3   GLU   A CA    1 
ATOM   18   C  C     . GLU   A 1 6   ? -14.107 21.032 3.763  1.00 14.88 ? 3   GLU   A C     1 
ATOM   19   O  O     . GLU   A 1 6   ? -14.823 20.112 4.188  1.00 18.49 ? 3   GLU   A O     1 
ATOM   20   C  CB    . GLU   A 1 6   ? -15.430 23.131 3.436  1.00 22.12 ? 3   GLU   A CB    1 
ATOM   21   C  CG    . GLU   A 1 6   ? -14.617 24.047 4.362  1.00 27.28 ? 3   GLU   A CG    1 
ATOM   22   C  CD    . GLU   A 1 6   ? -15.425 25.140 5.097  1.00 32.64 ? 3   GLU   A CD    1 
ATOM   23   O  OE1   . GLU   A 1 6   ? -14.834 25.902 5.818  1.00 40.05 ? 3   GLU   A OE1   1 
ATOM   24   O  OE2   . GLU   A 1 6   ? -16.681 25.178 4.926  1.00 42.83 ? 3   GLU   A OE2   1 
ATOM   25   N  N     . TYR   A 1 7   ? -12.839 21.231 4.163  1.00 12.16 ? 4   TYR   A N     1 
ATOM   26   C  CA    . TYR   A 1 7   ? -12.211 20.415 5.200  1.00 12.31 ? 4   TYR   A CA    1 
ATOM   27   C  C     . TYR   A 1 7   ? -11.506 21.345 6.163  1.00 12.47 ? 4   TYR   A C     1 
ATOM   28   O  O     . TYR   A 1 7   ? -10.581 22.058 5.761  1.00 13.17 ? 4   TYR   A O     1 
ATOM   29   C  CB    . TYR   A 1 7   ? -11.194 19.431 4.612  1.00 12.47 ? 4   TYR   A CB    1 
ATOM   30   C  CG    . TYR   A 1 7   ? -11.800 18.385 3.716  1.00 12.91 ? 4   TYR   A CG    1 
ATOM   31   C  CD1   . TYR   A 1 7   ? -12.034 18.630 2.380  1.00 13.15 ? 4   TYR   A CD1   1 
ATOM   32   C  CD2   . TYR   A 1 7   ? -12.181 17.168 4.233  1.00 14.66 ? 4   TYR   A CD2   1 
ATOM   33   C  CE1   . TYR   A 1 7   ? -12.592 17.653 1.564  1.00 12.56 ? 4   TYR   A CE1   1 
ATOM   34   C  CE2   . TYR   A 1 7   ? -12.737 16.183 3.433  1.00 15.53 ? 4   TYR   A CE2   1 
ATOM   35   C  CZ    . TYR   A 1 7   ? -12.969 16.433 2.110  1.00 13.25 ? 4   TYR   A CZ    1 
ATOM   36   O  OH    . TYR   A 1 7   ? -13.543 15.425 1.380  1.00 14.84 ? 4   TYR   A OH    1 
ATOM   37   N  N     . LYS   A 1 8   ? -11.946 21.327 7.417  1.00 11.20 ? 5   LYS   A N     1 
ATOM   38   C  CA    . LYS   A 1 8   ? -11.341 22.147 8.485  1.00 11.98 ? 5   LYS   A CA    1 
ATOM   39   C  C     . LYS   A 1 8   ? -10.283 21.349 9.216  1.00 10.30 ? 5   LYS   A C     1 
ATOM   40   O  O     . LYS   A 1 8   ? -10.608 20.376 9.885  1.00 11.12 ? 5   LYS   A O     1 
ATOM   41   C  CB    . LYS   A 1 8   ? -12.417 22.624 9.462  1.00 13.56 ? 5   LYS   A CB    1 
ATOM   42   C  CG    . LYS   A 1 8   ? -13.458 23.540 8.822  1.00 16.19 ? 5   LYS   A CG    1 
ATOM   43   C  CD    . LYS   A 1 8   ? -14.506 24.063 9.782  1.00 20.51 ? 5   LYS   A CD    1 
ATOM   44   C  CE    . LYS   A 1 8   ? -15.356 25.126 9.110  1.00 26.54 ? 5   LYS   A CE    1 
ATOM   45   N  NZ    . LYS   A 1 8   ? -16.357 24.530 8.192  1.00 33.35 ? 5   LYS   A NZ    1 
ATOM   46   N  N     . LEU   A 1 9   ? -9.027  21.718 9.000  1.00 9.83  ? 6   LEU   A N     1 
ATOM   47   C  CA    . LEU   A 1 9   ? -7.875  20.994 9.550  1.00 9.88  ? 6   LEU   A CA    1 
ATOM   48   C  C     . LEU   A 1 9   ? -7.206  21.830 10.599 1.00 9.66  ? 6   LEU   A C     1 
ATOM   49   O  O     . LEU   A 1 9   ? -7.161  23.065 10.487 1.00 11.67 ? 6   LEU   A O     1 
ATOM   50   C  CB    . LEU   A 1 9   ? -6.897  20.633 8.451  1.00 10.15 ? 6   LEU   A CB    1 
ATOM   51   C  CG    . LEU   A 1 9   ? -7.502  20.017 7.175  1.00 11.06 ? 6   LEU   A CG    1 
ATOM   52   C  CD1   . LEU   A 1 9   ? -6.400  19.677 6.185  1.00 12.56 ? 6   LEU   A CD1   1 
ATOM   53   C  CD2   . LEU   A 1 9   ? -8.376  18.811 7.487  1.00 13.10 ? 6   LEU   A CD2   1 
ATOM   54   N  N     . VAL   A 1 10  ? -6.685  21.165 11.605 1.00 9.05  ? 7   VAL   A N     1 
ATOM   55   C  CA    . VAL   A 1 10  ? -5.950  21.841 12.684 1.00 9.54  ? 7   VAL   A CA    1 
ATOM   56   C  C     . VAL   A 1 10  ? -4.594  21.176 12.868 1.00 9.92  ? 7   VAL   A C     1 
ATOM   57   O  O     . VAL   A 1 10  ? -4.512  19.949 12.991 1.00 10.49 ? 7   VAL   A O     1 
ATOM   58   C  CB    . VAL   A 1 10  ? -6.752  21.756 13.997 1.00 10.31 ? 7   VAL   A CB    1 
ATOM   59   C  CG1   . VAL   A 1 10  ? -6.067  22.539 15.130 1.00 10.43 ? 7   VAL   A CG1   1 
ATOM   60   C  CG2   . VAL   A 1 10  ? -8.188  22.292 13.830 1.00 12.39 ? 7   VAL   A CG2   1 
ATOM   61   N  N     . VAL   A 1 11  ? -3.539  21.975 12.918 1.00 8.93  ? 8   VAL   A N     1 
ATOM   62   C  CA    . VAL   A 1 11  ? -2.181  21.479 13.125 1.00 8.76  ? 8   VAL   A CA    1 
ATOM   63   C  C     . VAL   A 1 11  ? -1.781  21.768 14.557 1.00 8.69  ? 8   VAL   A C     1 
ATOM   64   O  O     . VAL   A 1 11  ? -1.736  22.945 14.961 1.00 9.77  ? 8   VAL   A O     1 
ATOM   65   C  CB    . VAL   A 1 11  ? -1.195  22.100 12.126 1.00 9.71  ? 8   VAL   A CB    1 
ATOM   66   C  CG1   . VAL   A 1 11  ? 0.162   21.448 12.224 1.00 11.14 ? 8   VAL   A CG1   1 
ATOM   67   C  CG2   . VAL   A 1 11  ? -1.756  22.003 10.720 1.00 11.16 ? 8   VAL   A CG2   1 
ATOM   68   N  N     . VAL   A 1 12  ? -1.514  20.712 15.322 1.00 8.89  ? 9   VAL   A N     1 
ATOM   69   C  CA    . VAL   A 1 12  ? -1.122  20.815 16.727 1.00 9.20  ? 9   VAL   A CA    1 
ATOM   70   C  C     . VAL   A 1 12  ? 0.203   20.110 16.951 1.00 8.84  ? 9   VAL   A C     1 
ATOM   71   O  O     . VAL   A 1 12  ? 0.648   19.305 16.124 1.00 9.42  ? 9   VAL   A O     1 
ATOM   72   C  CB    . VAL   A 1 12  ? -2.206  20.241 17.648 1.00 10.07 ? 9   VAL   A CB    1 
ATOM   73   C  CG1   . VAL   A 1 12  ? -3.548  20.911 17.422 1.00 11.38 ? 9   VAL   A CG1   1 
ATOM   74   C  CG2   . VAL   A 1 12  ? -2.358  18.721 17.504 1.00 10.65 ? 9   VAL   A CG2   1 
ATOM   75   N  N     . GLY   A 1 13  ? 0.812   20.380 18.101 1.00 8.96  ? 10  GLY   A N     1 
ATOM   76   C  CA    . GLY   A 1 13  ? 2.129   19.828 18.428 1.00 10.19 ? 10  GLY   A CA    1 
ATOM   77   C  C     . GLY   A 1 13  ? 2.942   20.844 19.202 1.00 9.73  ? 10  GLY   A C     1 
ATOM   78   O  O     . GLY   A 1 13  ? 2.657   22.046 19.203 1.00 9.85  ? 10  GLY   A O     1 
ATOM   79   N  N     . ALA   A 1 14  ? 3.983   20.355 19.872 1.00 9.49  ? 11  ALA   A N     1 
ATOM   80   C  CA    . ALA   A 1 14  ? 4.780   21.199 20.758 1.00 10.19 ? 11  ALA   A CA    1 
ATOM   81   C  C     . ALA   A 1 14  ? 5.432   22.351 19.998 1.00 9.77  ? 11  ALA   A C     1 
ATOM   82   O  O     . ALA   A 1 14  ? 5.673   22.264 18.814 1.00 10.51 ? 11  ALA   A O     1 
ATOM   83   C  CB    . ALA   A 1 14  ? 5.819   20.341 21.451 1.00 10.76 ? 11  ALA   A CB    1 
ATOM   84   N  N     . GLY   A 1 15  ? 5.722   23.424 20.724 1.00 12.18 ? 12  GLY   A N     1 
ATOM   85   C  CA    . GLY   A 1 15  ? 6.465   24.503 20.135 1.00 13.03 ? 12  GLY   A CA    1 
ATOM   86   C  C     . GLY   A 1 15  ? 7.729   24.007 19.481 1.00 11.91 ? 12  GLY   A C     1 
ATOM   87   O  O     . GLY   A 1 15  ? 8.474   23.200 20.034 1.00 13.26 ? 12  GLY   A O     1 
ATOM   88   N  N     . GLY   A 1 16  ? 7.953   24.502 18.274 1.00 12.09 ? 13  GLY   A N     1 
ATOM   89   C  CA    . GLY   A 1 16  ? 9.182   24.219 17.563 1.00 11.77 ? 13  GLY   A CA    1 
ATOM   90   C  C     . GLY   A 1 16  ? 9.181   22.954 16.720 1.00 11.81 ? 13  GLY   A C     1 
ATOM   91   O  O     . GLY   A 1 16  ? 10.214  22.658 16.111 1.00 12.73 ? 13  GLY   A O     1 
ATOM   92   N  N     . VAL   A 1 17  ? 8.089   22.179 16.679 1.00 10.43 ? 14  VAL   A N     1 
ATOM   93   C  CA    . VAL   A 1 17  ? 8.127   20.925 15.908 1.00 9.84  ? 14  VAL   A CA    1 
ATOM   94   C  C     . VAL   A 1 17  ? 8.026   21.118 14.399 1.00 9.14  ? 14  VAL   A C     1 
ATOM   95   O  O     . VAL   A 1 17  ? 8.399   20.197 13.668 1.00 9.67  ? 14  VAL   A O     1 
ATOM   96   C  CB    . VAL   A 1 17  ? 7.050   19.903 16.357 1.00 9.40  ? 14  VAL   A CB    1 
ATOM   97   C  CG1   . VAL   A 1 17  ? 7.249   19.489 17.813 1.00 9.55  ? 14  VAL   A CG1   1 
ATOM   98   C  CG2   . VAL   A 1 17  ? 5.624   20.421 16.109 1.00 9.35  ? 14  VAL   A CG2   1 
ATOM   99   N  N     . GLY   A 1 18  ? 7.533   22.283 13.959 1.00 9.13  ? 15  GLY   A N     1 
ATOM   100  C  CA    . GLY   A 1 18  ? 7.343   22.587 12.543 1.00 10.25 ? 15  GLY   A CA    1 
ATOM   101  C  C     . GLY   A 1 18  ? 5.918   22.728 12.065 1.00 10.25 ? 15  GLY   A C     1 
ATOM   102  O  O     . GLY   A 1 18  ? 5.681   22.566 10.879 1.00 11.16 ? 15  GLY   A O     1 
ATOM   103  N  N     . LYS   A 1 19  ? 4.975   23.057 12.940 1.00 9.86  ? 16  LYS   A N     1 
ATOM   104  C  CA    . LYS   A 1 19  ? 3.585   23.280 12.533 1.00 10.21 ? 16  LYS   A CA    1 
ATOM   105  C  C     . LYS   A 1 19  ? 3.468   24.362 11.491 1.00 10.31 ? 16  LYS   A C     1 
ATOM   106  O  O     . LYS   A 1 19  ? 2.850   24.159 10.440 1.00 11.33 ? 16  LYS   A O     1 
ATOM   107  C  CB    . LYS   A 1 19  ? 2.749   23.673 13.727 1.00 10.06 ? 16  LYS   A CB    1 
ATOM   108  C  CG    . LYS   A 1 19  ? 2.680   22.663 14.860 1.00 11.16 ? 16  LYS   A CG    1 
ATOM   109  C  CD    . LYS   A 1 19  ? 1.824   23.200 16.026 1.00 13.69 ? 16  LYS   A CD    1 
ATOM   110  C  CE    . LYS   A 1 19  ? 2.400   24.397 16.761 1.00 12.76 ? 16  LYS   A CE    1 
ATOM   111  N  NZ    . LYS   A 1 19  ? 3.722   24.048 17.396 1.00 11.63 ? 16  LYS   A NZ    1 
ATOM   112  N  N     . SER   A 1 20  ? 4.064   25.518 11.769 1.00 10.40 ? 17  SER   A N     1 
ATOM   113  C  CA    . SER   A 1 20  ? 4.026   26.622 10.809 1.00 11.04 ? 17  SER   A CA    1 
ATOM   114  C  C     . SER   A 1 20  ? 4.747   26.301 9.537  1.00 12.03 ? 17  SER   A C     1 
ATOM   115  O  O     . SER   A 1 20  ? 4.255   26.561 8.439  1.00 12.68 ? 17  SER   A O     1 
ATOM   116  C  CB    . SER   A 1 20  ? 4.568   27.902 11.395 1.00 11.81 ? 17  SER   A CB    1 
ATOM   117  O  OG    . SER   A 1 20  ? 3.815   28.285 12.494 1.00 13.27 ? 17  SER   A OG    1 
ATOM   118  N  N     . ALA   A 1 21  ? 5.945   25.752 9.668  1.00 11.60 ? 18  ALA   A N     1 
ATOM   119  C  CA    . ALA   A 1 21  ? 6.742   25.406 8.483  1.00 11.92 ? 18  ALA   A CA    1 
ATOM   120  C  C     . ALA   A 1 21  ? 6.007   24.427 7.563  1.00 11.66 ? 18  ALA   A C     1 
ATOM   121  O  O     . ALA   A 1 21  ? 6.020   24.557 6.349  1.00 12.87 ? 18  ALA   A O     1 
ATOM   122  C  CB    . ALA   A 1 21  ? 8.070   24.837 8.891  1.00 11.67 ? 18  ALA   A CB    1 
ATOM   123  N  N     . LEU   A 1 22  ? 5.377   23.418 8.146  1.00 11.06 ? 19  LEU   A N     1 
ATOM   124  C  CA    . LEU   A 1 22  ? 4.586   22.489 7.332  1.00 11.39 ? 19  LEU   A CA    1 
ATOM   125  C  C     . LEU   A 1 22  ? 3.416   23.177 6.643  1.00 11.36 ? 19  LEU   A C     1 
ATOM   126  O  O     . LEU   A 1 22  ? 3.164   22.918 5.448  1.00 11.99 ? 19  LEU   A O     1 
ATOM   127  C  CB    . LEU   A 1 22  ? 4.057   21.333 8.208  1.00 11.47 ? 19  LEU   A CB    1 
ATOM   128  C  CG    . LEU   A 1 22  ? 5.109   20.282 8.590  1.00 12.30 ? 19  LEU   A CG    1 
ATOM   129  C  CD1   . LEU   A 1 22  ? 4.584   19.423 9.731  1.00 13.22 ? 19  LEU   A CD1   1 
ATOM   130  C  CD2   . LEU   A 1 22  ? 5.520   19.416 7.398  1.00 13.62 ? 19  LEU   A CD2   1 
ATOM   131  N  N     . THR   A 1 23  ? 2.675   23.992 7.381  1.00 11.91 ? 20  THR   A N     1 
ATOM   132  C  CA    . THR   A 1 23  ? 1.468   24.636 6.814  1.00 12.87 ? 20  THR   A CA    1 
ATOM   133  C  C     . THR   A 1 23  ? 1.815   25.622 5.702  1.00 12.23 ? 20  THR   A C     1 
ATOM   134  O  O     . THR   A 1 23  ? 1.191   25.657 4.638  1.00 14.50 ? 20  THR   A O     1 
ATOM   135  C  CB    . THR   A 1 23  ? 0.702   25.387 7.909  1.00 13.11 ? 20  THR   A CB    1 
ATOM   136  O  OG1   . THR   A 1 23  ? 0.335   24.471 8.963  1.00 13.45 ? 20  THR   A OG1   1 
ATOM   137  C  CG2   . THR   A 1 23  ? -0.559  26.036 7.360  1.00 14.35 ? 20  THR   A CG2   1 
ATOM   138  N  N     . ILE   A 1 24  ? 2.868   26.387 5.936  1.00 13.86 ? 21  ILE   A N     1 
ATOM   139  C  CA    . ILE   A 1 24  ? 3.320   27.375 4.970  1.00 14.96 ? 21  ILE   A CA    1 
ATOM   140  C  C     . ILE   A 1 24  ? 3.935   26.683 3.735  1.00 14.80 ? 21  ILE   A C     1 
ATOM   141  O  O     . ILE   A 1 24  ? 3.732   27.126 2.590  1.00 16.84 ? 21  ILE   A O     1 
ATOM   142  C  CB    . ILE   A 1 24  ? 4.286   28.376 5.644  1.00 15.73 ? 21  ILE   A CB    1 
ATOM   143  C  CG1   . ILE   A 1 24  ? 3.543   29.231 6.662  1.00 17.98 ? 21  ILE   A CG1   1 
ATOM   144  C  CG2   . ILE   A 1 24  ? 4.968   29.248 4.592  1.00 16.24 ? 21  ILE   A CG2   1 
ATOM   145  C  CD1   . ILE   A 1 24  ? 4.469   29.907 7.654  1.00 20.64 ? 21  ILE   A CD1   1 
ATOM   146  N  N     . GLN   A 1 25  ? 4.666   25.585 3.930  1.00 14.41 ? 22  GLN   A N     1 
ATOM   147  C  CA    . GLN   A 1 25  ? 5.123   24.807 2.764  1.00 14.78 ? 22  GLN   A CA    1 
ATOM   148  C  C     . GLN   A 1 25  ? 3.968   24.341 1.924  1.00 15.87 ? 22  GLN   A C     1 
ATOM   149  O  O     . GLN   A 1 25  ? 4.012   24.469 0.688  1.00 16.26 ? 22  GLN   A O     1 
ATOM   150  C  CB    . GLN   A 1 25  ? 5.914   23.567 3.165  1.00 16.33 ? 22  GLN   A CB    1 
ATOM   151  C  CG    . GLN   A 1 25  ? 7.369   23.813 3.232  1.00 17.56 ? 22  GLN   A CG    1 
ATOM   152  C  CD    . GLN   A 1 25  ? 8.027   23.947 1.857  1.00 18.91 ? 22  GLN   A CD    1 
ATOM   153  O  OE1   . GLN   A 1 25  ? 7.406   24.292 0.805  1.00 17.78 ? 22  GLN   A OE1   1 
ATOM   154  N  NE2   . GLN   A 1 25  ? 9.304   23.707 1.866  1.00 18.27 ? 22  GLN   A NE2   1 
ATOM   155  N  N     . LEU   A 1 26  ? 2.962   23.787 2.575  1.00 15.56 ? 23  LEU   A N     1 
ATOM   156  C  CA    . LEU   A 1 26  ? 1.796   23.319 1.803  1.00 15.78 ? 23  LEU   A CA    1 
ATOM   157  C  C     . LEU   A 1 26  ? 1.151   24.476 1.010  1.00 17.48 ? 23  LEU   A C     1 
ATOM   158  O  O     . LEU   A 1 26  ? 0.948   24.342 -0.212 1.00 19.57 ? 23  LEU   A O     1 
ATOM   159  C  CB    . LEU   A 1 26  ? 0.783   22.683 2.756  1.00 15.08 ? 23  LEU   A CB    1 
ATOM   160  C  CG    . LEU   A 1 26  ? -0.436  22.134 2.035  1.00 15.64 ? 23  LEU   A CG    1 
ATOM   161  C  CD1   . LEU   A 1 26  ? -0.077  20.808 1.375  1.00 14.47 ? 23  LEU   A CD1   1 
ATOM   162  C  CD2   . LEU   A 1 26  ? -1.622  21.997 2.975  1.00 18.23 ? 23  LEU   A CD2   1 
ATOM   163  N  N     . ILE   A 1 27  ? 0.776   25.536 1.726  1.00 17.25 ? 24  ILE   A N     1 
ATOM   164  C  CA    . ILE   A 1 27  ? 0.015   26.664 1.120  1.00 19.58 ? 24  ILE   A CA    1 
ATOM   165  C  C     . ILE   A 1 27  ? 0.829   27.568 0.206  1.00 18.68 ? 24  ILE   A C     1 
ATOM   166  O  O     . ILE   A 1 27  ? 0.313   27.939 -0.858 1.00 23.35 ? 24  ILE   A O     1 
ATOM   167  C  CB    . ILE   A 1 27  ? -0.614  27.522 2.217  1.00 23.55 ? 24  ILE   A CB    1 
ATOM   168  C  CG1   . ILE   A 1 27  ? -1.495  26.676 3.113  1.00 24.52 ? 24  ILE   A CG1   1 
ATOM   169  C  CG2   . ILE   A 1 27  ? -1.402  28.645 1.569  1.00 24.69 ? 24  ILE   A CG2   1 
ATOM   170  C  CD1   . ILE   A 1 27  ? -2.641  26.069 2.415  1.00 26.19 ? 24  ILE   A CD1   1 
ATOM   171  N  N     . GLN   A 1 28  ? 2.036   27.905 0.616  1.00 22.00 ? 25  GLN   A N     1 
ATOM   172  C  CA    . GLN   A 1 28  ? 2.804   28.979 -0.056 1.00 22.72 ? 25  GLN   A CA    1 
ATOM   173  C  C     . GLN   A 1 28  ? 4.072   28.475 -0.693 1.00 22.29 ? 25  GLN   A C     1 
ATOM   174  O  O     . GLN   A 1 28  ? 4.740   29.264 -1.295 1.00 26.52 ? 25  GLN   A O     1 
ATOM   175  C  CB    . GLN   A 1 28  ? 3.088   30.113 0.924  1.00 23.07 ? 25  GLN   A CB    1 
ATOM   176  C  CG    . GLN   A 1 28  ? 1.827   30.644 1.566  1.00 26.71 ? 25  GLN   A CG    1 
ATOM   177  C  CD    . GLN   A 1 28  ? 2.013   31.773 2.552  1.00 28.30 ? 25  GLN   A CD    1 
ATOM   178  O  OE1   . GLN   A 1 28  ? 3.110   32.091 2.928  1.00 31.05 ? 25  GLN   A OE1   1 
ATOM   179  N  NE2   . GLN   A 1 28  ? 0.912   32.366 2.983  1.00 32.99 ? 25  GLN   A NE2   1 
ATOM   180  N  N     . ASN   A 1 29  ? 4.375   27.188 -0.538 1.00 21.86 ? 26  ASN   A N     1 
ATOM   181  C  CA    . ASN   A 1 29  ? 5.546   26.590 -1.228 1.00 21.52 ? 26  ASN   A CA    1 
ATOM   182  C  C     . ASN   A 1 29  ? 6.884   27.270 -0.922 1.00 24.09 ? 26  ASN   A C     1 
ATOM   183  O  O     . ASN   A 1 29  ? 7.667   27.584 -1.843 1.00 27.54 ? 26  ASN   A O     1 
ATOM   184  C  CB    . ASN   A 1 29  ? 5.234   26.435 -2.720 1.00 23.19 ? 26  ASN   A CB    1 
ATOM   185  C  CG    . ASN   A 1 29  ? 6.310   25.732 -3.497 1.00 27.42 ? 26  ASN   A CG    1 
ATOM   186  O  OD1   . ASN   A 1 29  ? 7.008   24.861 -3.019 1.00 31.70 ? 26  ASN   A OD1   1 
ATOM   187  N  ND2   . ASN   A 1 29  ? 6.407   26.093 -4.770 1.00 31.59 ? 26  ASN   A ND2   1 
ATOM   188  N  N     . HIS   A 1 30  ? 7.116   27.558 0.344  1.00 20.22 ? 27  HIS   A N     1 
ATOM   189  C  CA    . HIS   A 1 30  ? 8.445   28.043 0.781  1.00 19.21 ? 27  HIS   A CA    1 
ATOM   190  C  C     . HIS   A 1 30  ? 8.671   27.536 2.206  1.00 18.01 ? 27  HIS   A C     1 
ATOM   191  O  O     . HIS   A 1 30  ? 7.697   27.266 2.900  1.00 18.22 ? 27  HIS   A O     1 
ATOM   192  C  CB    . HIS   A 1 30  ? 8.647   29.571 0.644  1.00 20.94 ? 27  HIS   A CB    1 
ATOM   193  C  CG    . HIS   A 1 30  ? 7.704   30.377 1.445  1.00 21.93 ? 27  HIS   A CG    1 
ATOM   194  N  ND1   . HIS   A 1 30  ? 8.074   30.978 2.590  1.00 23.25 ? 27  HIS   A ND1   1 
ATOM   195  C  CD2   . HIS   A 1 30  ? 6.409   30.662 1.257  1.00 24.91 ? 27  HIS   A CD2   1 
ATOM   196  C  CE1   . HIS   A 1 30  ? 7.038   31.624 3.078  1.00 24.75 ? 27  HIS   A CE1   1 
ATOM   197  N  NE2   . HIS   A 1 30  ? 6.012   31.473 2.275  1.00 23.25 ? 27  HIS   A NE2   1 
ATOM   198  N  N     . PHE   A 1 31  ? 9.930   27.356 2.555  1.00 20.09 ? 28  PHE   A N     1 
ATOM   199  C  CA    . PHE   A 1 31  ? 10.326  27.007 3.929  1.00 16.85 ? 28  PHE   A CA    1 
ATOM   200  C  C     . PHE   A 1 31  ? 10.667  28.215 4.791  1.00 19.50 ? 28  PHE   A C     1 
ATOM   201  O  O     . PHE   A 1 31  ? 11.554  29.014 4.436  1.00 21.50 ? 28  PHE   A O     1 
ATOM   202  C  CB    . PHE   A 1 31  ? 11.551  26.107 3.886  1.00 15.50 ? 28  PHE   A CB    1 
ATOM   203  C  CG    . PHE   A 1 31  ? 12.053  25.672 5.224  1.00 17.54 ? 28  PHE   A CG    1 
ATOM   204  C  CD1   . PHE   A 1 31  ? 11.242  24.949 6.102  1.00 16.79 ? 28  PHE   A CD1   1 
ATOM   205  C  CD2   . PHE   A 1 31  ? 13.350  25.952 5.604  1.00 18.76 ? 28  PHE   A CD2   1 
ATOM   206  C  CE1   . PHE   A 1 31  ? 11.731  24.533 7.338  1.00 17.32 ? 28  PHE   A CE1   1 
ATOM   207  C  CE2   . PHE   A 1 31  ? 13.844  25.535 6.829  1.00 16.97 ? 28  PHE   A CE2   1 
ATOM   208  C  CZ    . PHE   A 1 31  ? 13.041  24.817 7.699  1.00 18.21 ? 28  PHE   A CZ    1 
ATOM   209  N  N     . VAL   A 1 32  ? 10.022  28.295 5.942  1.00 17.71 ? 29  VAL   A N     1 
ATOM   210  C  CA    . VAL   A 1 32  ? 10.313  29.406 6.891  1.00 21.25 ? 29  VAL   A CA    1 
ATOM   211  C  C     . VAL   A 1 32  ? 11.283  28.934 7.971  1.00 24.18 ? 29  VAL   A C     1 
ATOM   212  O  O     . VAL   A 1 32  ? 11.051  27.903 8.574  1.00 27.33 ? 29  VAL   A O     1 
ATOM   213  C  CB    . VAL   A 1 32  ? 9.038   30.030 7.472  1.00 23.86 ? 29  VAL   A CB    1 
ATOM   214  C  CG1   . VAL   A 1 32  ? 8.252   30.801 6.420  1.00 25.46 ? 29  VAL   A CG1   1 
ATOM   215  C  CG2   . VAL   A 1 32  ? 8.188   28.997 8.187  1.00 25.07 ? 29  VAL   A CG2   1 
ATOM   216  N  N     . ASP   A 1 33  ? 12.383  29.667 8.126  1.00 28.90 ? 30  ASP   A N     1 
ATOM   217  C  CA    . ASP   A 1 33  ? 13.423  29.437 9.158  1.00 30.45 ? 30  ASP   A CA    1 
ATOM   218  C  C     . ASP   A 1 33  ? 12.994  30.137 10.459 1.00 27.04 ? 30  ASP   A C     1 
ATOM   219  O  O     . ASP   A 1 33  ? 13.351  29.691 11.485 1.00 29.49 ? 30  ASP   A O     1 
ATOM   220  C  CB    . ASP   A 1 33  ? 14.734  30.123 8.721  1.00 34.96 ? 30  ASP   A CB    1 
ATOM   221  C  CG    . ASP   A 1 33  ? 16.003  29.448 9.193  1.00 44.50 ? 30  ASP   A CG    1 
ATOM   222  O  OD1   . ASP   A 1 33  ? 16.295  29.500 10.401 1.00 55.34 ? 30  ASP   A OD1   1 
ATOM   223  O  OD2   . ASP   A 1 33  ? 16.669  28.848 8.354  1.00 54.74 ? 30  ASP   A OD2   1 
ATOM   224  N  N     . GLU   A 1 34  ? 12.196  31.192 10.391 1.00 28.60 ? 31  GLU   A N     1 
ATOM   225  C  CA    . GLU   A 1 34  ? 12.046  32.048 11.603 1.00 29.44 ? 31  GLU   A CA    1 
ATOM   226  C  C     . GLU   A 1 34  ? 10.661  32.678 11.712 1.00 30.11 ? 31  GLU   A C     1 
ATOM   227  O  O     . GLU   A 1 34  ? 10.529  33.913 11.884 1.00 38.88 ? 31  GLU   A O     1 
ATOM   228  C  CB    . GLU   A 1 34  ? 13.016  33.213 11.457 1.00 34.59 ? 31  GLU   A CB    1 
ATOM   229  C  CG    . GLU   A 1 34  ? 14.438  32.877 11.816 1.00 38.06 ? 31  GLU   A CG    1 
ATOM   230  C  CD    . GLU   A 1 34  ? 15.463  33.759 11.139 1.00 45.36 ? 31  GLU   A CD    1 
ATOM   231  O  OE1   . GLU   A 1 34  ? 15.263  34.124 9.953  1.00 53.63 ? 31  GLU   A OE1   1 
ATOM   232  O  OE2   . GLU   A 1 34  ? 16.399  34.106 11.823 1.00 53.11 ? 31  GLU   A OE2   1 
ATOM   233  N  N     . TYR   A 1 35  ? 9.650   31.817 11.765 1.00 26.40 ? 32  TYR   A N     1 
ATOM   234  C  CA    . TYR   A 1 35  ? 8.270   32.236 11.817 1.00 24.32 ? 32  TYR   A CA    1 
ATOM   235  C  C     . TYR   A 1 35  ? 7.864   32.383 13.261 1.00 23.20 ? 32  TYR   A C     1 
ATOM   236  O  O     . TYR   A 1 35  ? 7.937   31.426 14.020 1.00 21.03 ? 32  TYR   A O     1 
ATOM   237  C  CB    . TYR   A 1 35  ? 7.382   31.201 11.133 1.00 20.58 ? 32  TYR   A CB    1 
ATOM   238  C  CG    . TYR   A 1 35  ? 6.091   31.786 10.697 1.00 22.46 ? 32  TYR   A CG    1 
ATOM   239  C  CD1   . TYR   A 1 35  ? 6.080   32.704 9.646  1.00 24.73 ? 32  TYR   A CD1   1 
ATOM   240  C  CD2   . TYR   A 1 35  ? 4.885   31.472 11.329 1.00 20.59 ? 32  TYR   A CD2   1 
ATOM   241  C  CE1   . TYR   A 1 35  ? 4.910   33.272 9.207  1.00 30.11 ? 32  TYR   A CE1   1 
ATOM   242  C  CE2   . TYR   A 1 35  ? 3.693   32.047 10.888 1.00 26.48 ? 32  TYR   A CE2   1 
ATOM   243  C  CZ    . TYR   A 1 35  ? 3.729   32.951 9.824  1.00 26.32 ? 32  TYR   A CZ    1 
ATOM   244  O  OH    . TYR   A 1 35  ? 2.595   33.531 9.352  1.00 34.82 ? 32  TYR   A OH    1 
ATOM   245  N  N     . ASP   A 1 36  ? 7.434   33.581 13.643 1.00 20.83 ? 33  ASP   A N     1 
ATOM   246  C  CA    . ASP   A 1 36  ? 7.153   33.876 15.046 1.00 19.04 ? 33  ASP   A CA    1 
ATOM   247  C  C     . ASP   A 1 36  ? 6.240   32.785 15.650 1.00 16.63 ? 33  ASP   A C     1 
ATOM   248  O  O     . ASP   A 1 36  ? 5.141   32.506 15.120 1.00 16.38 ? 33  ASP   A O     1 
ATOM   249  C  CB    . ASP   A 1 36  ? 6.540   35.278 15.178 1.00 22.16 ? 33  ASP   A CB    1 
ATOM   250  C  CG    . ASP   A 1 36  ? 6.304   35.694 16.618 1.00 21.82 ? 33  ASP   A CG    1 
ATOM   251  O  OD1   . ASP   A 1 36  ? 5.962   34.863 17.490 1.00 23.76 ? 33  ASP   A OD1   1 
ATOM   252  O  OD2   . ASP   A 1 36  ? 6.470   36.903 16.878 1.00 29.81 ? 33  ASP   A OD2   1 
ATOM   253  N  N     . PRO   A 1 37  ? 6.697   32.152 16.753 1.00 18.02 ? 34  PRO   A N     1 
ATOM   254  C  CA    . PRO   A 1 37  ? 5.968   31.006 17.312 1.00 16.89 ? 34  PRO   A CA    1 
ATOM   255  C  C     . PRO   A 1 37  ? 4.624   31.323 17.927 1.00 16.91 ? 34  PRO   A C     1 
ATOM   256  O  O     . PRO   A 1 37  ? 3.876   30.393 18.243 1.00 17.71 ? 34  PRO   A O     1 
ATOM   257  C  CB    . PRO   A 1 37  ? 6.908   30.473 18.388 1.00 20.85 ? 34  PRO   A CB    1 
ATOM   258  C  CG    . PRO   A 1 37  ? 7.724   31.648 18.784 1.00 22.31 ? 34  PRO   A CG    1 
ATOM   259  C  CD    . PRO   A 1 37  ? 7.940   32.403 17.507 1.00 19.99 ? 34  PRO   A CD    1 
ATOM   260  N  N     . THR   A 1 38  ? 4.338   32.610 18.149 1.00 16.54 ? 35  THR   A N     1 
ATOM   261  C  CA    . THR   A 1 38  ? 3.072   33.042 18.701 1.00 17.07 ? 35  THR   A CA    1 
ATOM   262  C  C     . THR   A 1 38  ? 1.996   33.327 17.640 1.00 16.56 ? 35  THR   A C     1 
ATOM   263  O  O     . THR   A 1 38  ? 0.869   33.616 17.995 1.00 18.22 ? 35  THR   A O     1 
ATOM   264  C  CB    . THR   A 1 38  ? 3.297   34.311 19.570 1.00 20.51 ? 35  THR   A CB    1 
ATOM   265  O  OG1   . THR   A 1 38  ? 3.626   35.412 18.720 1.00 23.28 ? 35  THR   A OG1   1 
ATOM   266  C  CG2   . THR   A 1 38  ? 4.419   34.078 20.590 1.00 20.74 ? 35  THR   A CG2   1 
ATOM   267  N  N     . ILE   A 1 39  ? 2.327   33.255 16.351 1.00 16.52 ? 36  ILE   A N     1 
ATOM   268  C  CA    . ILE   A 1 39  ? 1.344   33.529 15.298 1.00 16.24 ? 36  ILE   A CA    1 
ATOM   269  C  C     . ILE   A 1 39  ? 0.418   32.320 15.115 1.00 14.50 ? 36  ILE   A C     1 
ATOM   270  O  O     . ILE   A 1 39  ? 0.871   31.209 14.766 1.00 15.44 ? 36  ILE   A O     1 
ATOM   271  C  CB    . ILE   A 1 39  ? 2.030   33.884 13.968 1.00 15.71 ? 36  ILE   A CB    1 
ATOM   272  C  CG1   . ILE   A 1 39  ? 2.916   35.132 14.146 1.00 16.96 ? 36  ILE   A CG1   1 
ATOM   273  C  CG2   . ILE   A 1 39  ? 0.995   34.083 12.863 1.00 17.51 ? 36  ILE   A CG2   1 
ATOM   274  C  CD1   . ILE   A 1 39  ? 3.729   35.489 12.931 1.00 18.74 ? 36  ILE   A CD1   1 
ATOM   275  N  N     . GLU   A 1 40  ? -0.871  32.556 15.325 1.00 14.10 ? 37  GLU   A N     1 
ATOM   276  C  CA    . GLU   A 1 40  ? -1.901  31.558 15.101 1.00 15.62 ? 37  GLU   A CA    1 
ATOM   277  C  C     . GLU   A 1 40  ? -2.831  32.108 14.043 1.00 15.22 ? 37  GLU   A C     1 
ATOM   278  O  O     . GLU   A 1 40  ? -3.426  33.170 14.225 1.00 17.49 ? 37  GLU   A O     1 
ATOM   279  C  CB    . GLU   A 1 40  ? -2.648  31.293 16.390 1.00 15.41 ? 37  GLU   A CB    1 
ATOM   280  C  CG    . GLU   A 1 40  ? -3.823  30.335 16.290 1.00 14.19 ? 37  GLU   A CG    1 
ATOM   281  C  CD    . GLU   A 1 40  ? -4.203  29.795 17.651 1.00 13.90 ? 37  GLU   A CD    1 
ATOM   282  O  OE1   . GLU   A 1 40  ? -3.417  29.006 18.218 1.00 15.75 ? 37  GLU   A OE1   1 
ATOM   283  O  OE2   . GLU   A 1 40  ? -5.240  30.200 18.208 1.00 17.96 ? 37  GLU   A OE2   1 
ATOM   284  N  N     . ASP   A 1 41  ? -2.964  31.411 12.926 1.00 14.33 ? 38  ASP   A N     1 
ATOM   285  C  CA    . ASP   A 1 41  ? -3.789  31.892 11.843 1.00 15.57 ? 38  ASP   A CA    1 
ATOM   286  C  C     . ASP   A 1 41  ? -4.193  30.753 10.949 1.00 14.02 ? 38  ASP   A C     1 
ATOM   287  O  O     . ASP   A 1 41  ? -3.684  29.629 11.069 1.00 14.67 ? 38  ASP   A O     1 
ATOM   288  C  CB    . ASP   A 1 41  ? -3.060  32.973 11.043 1.00 18.39 ? 38  ASP   A CB    1 
ATOM   289  C  CG    . ASP   A 1 41  ? -4.015  34.069 10.521 1.00 20.15 ? 38  ASP   A CG    1 
ATOM   290  O  OD1   . ASP   A 1 41  ? -5.234  33.825 10.336 1.00 19.72 ? 38  ASP   A OD1   1 
ATOM   291  O  OD2   . ASP   A 1 41  ? -3.557  35.218 10.342 1.00 31.31 ? 38  ASP   A OD2   1 
ATOM   292  N  N     . SER   A 1 42  ? -5.161  31.037 10.097 1.00 14.36 ? 39  SER   A N     1 
ATOM   293  C  CA    . SER   A 1 42  ? -5.664  30.055 9.156  1.00 14.26 ? 39  SER   A CA    1 
ATOM   294  C  C     . SER   A 1 42  ? -5.250  30.360 7.757  1.00 15.24 ? 39  SER   A C     1 
ATOM   295  O  O     . SER   A 1 42  ? -4.991  31.511 7.398  1.00 17.41 ? 39  SER   A O     1 
ATOM   296  C  CB    . SER   A 1 42  ? -7.169  29.948 9.284  1.00 17.69 ? 39  SER   A CB    1 
ATOM   297  O  OG    . SER   A 1 42  ? -7.804  31.160 8.949  1.00 22.56 ? 39  SER   A OG    1 
ATOM   298  N  N     . TYR   A 1 43  ? -5.173  29.288 6.968  1.00 15.72 ? 40  TYR   A N     1 
ATOM   299  C  CA    . TYR   A 1 43  ? -4.752  29.346 5.567  1.00 18.43 ? 40  TYR   A CA    1 
ATOM   300  C  C     . TYR   A 1 43  ? -5.749  28.534 4.772  1.00 18.21 ? 40  TYR   A C     1 
ATOM   301  O  O     . TYR   A 1 43  ? -6.030  27.407 5.138  1.00 17.27 ? 40  TYR   A O     1 
ATOM   302  C  CB    . TYR   A 1 43  ? -3.399  28.698 5.390  1.00 22.04 ? 40  TYR   A CB    1 
ATOM   303  C  CG    . TYR   A 1 43  ? -2.237  29.363 6.052  1.00 24.95 ? 40  TYR   A CG    1 
ATOM   304  C  CD1   . TYR   A 1 43  ? -2.085  29.329 7.434  1.00 23.44 ? 40  TYR   A CD1   1 
ATOM   305  C  CD2   . TYR   A 1 43  ? -1.243  29.993 5.284  1.00 29.23 ? 40  TYR   A CD2   1 
ATOM   306  C  CE1   . TYR   A 1 43  ? -0.985  29.922 8.044  1.00 27.60 ? 40  TYR   A CE1   1 
ATOM   307  C  CE2   . TYR   A 1 43  ? -0.150  30.591 5.878  1.00 28.77 ? 40  TYR   A CE2   1 
ATOM   308  C  CZ    . TYR   A 1 43  ? -0.029  30.561 7.256  1.00 30.32 ? 40  TYR   A CZ    1 
ATOM   309  O  OH    . TYR   A 1 43  ? 1.072   31.142 7.818  1.00 31.68 ? 40  TYR   A OH    1 
ATOM   310  N  N     . ARG   A 1 44  ? -6.287  29.110 3.709  1.00 20.90 ? 41  ARG   A N     1 
ATOM   311  C  CA    . ARG   A 1 44  ? -7.316  28.476 2.891  1.00 23.57 ? 41  ARG   A CA    1 
ATOM   312  C  C     . ARG   A 1 44  ? -6.720  28.263 1.493  1.00 23.52 ? 41  ARG   A C     1 
ATOM   313  O  O     . ARG   A 1 44  ? -5.984  29.116 0.972  1.00 27.02 ? 41  ARG   A O     1 
ATOM   314  C  CB    . ARG   A 1 44  ? -8.652  29.282 2.874  1.00 29.59 ? 41  ARG   A CB    1 
ATOM   315  C  CG    . ARG   A 1 44  ? -9.676  28.991 4.000  1.00 30.86 ? 41  ARG   A CG    1 
ATOM   316  C  CD    . ARG   A 1 44  ? -10.797 30.041 4.256  1.00 33.41 ? 41  ARG   A CD    1 
ATOM   317  N  NE    . ARG   A 1 44  ? -12.093 29.890 3.537  1.00 35.56 ? 41  ARG   A NE    1 
ATOM   318  C  CZ    . ARG   A 1 44  ? -13.150 29.135 3.900  1.00 36.03 ? 41  ARG   A CZ    1 
ATOM   319  N  NH1   . ARG   A 1 44  ? -13.134 28.346 4.981  1.00 35.07 ? 41  ARG   A NH1   1 
ATOM   320  N  NH2   . ARG   A 1 44  ? -14.252 29.129 3.145  1.00 35.91 ? 41  ARG   A NH2   1 
ATOM   321  N  N     . LYS   A 1 45  ? -7.039  27.123 0.881  1.00 18.16 ? 42  LYS   A N     1 
ATOM   322  C  CA    . LYS   A 1 45  ? -6.578  26.818 -0.471 1.00 18.78 ? 42  LYS   A CA    1 
ATOM   323  C  C     . LYS   A 1 45  ? -7.380  25.666 -1.018 1.00 16.38 ? 42  LYS   A C     1 
ATOM   324  O  O     . LYS   A 1 45  ? -7.654  24.693 -0.309 1.00 18.30 ? 42  LYS   A O     1 
ATOM   325  C  CB    . LYS   A 1 45  ? -5.095  26.433 -0.466 1.00 24.64 ? 42  LYS   A CB    1 
ATOM   326  C  CG    . LYS   A 1 45  ? -4.462  25.983 -1.776 1.00 31.54 ? 42  LYS   A CG    1 
ATOM   327  C  CD    . LYS   A 1 45  ? -3.280  25.080 -1.445 1.00 35.82 ? 42  LYS   A CD    1 
ATOM   328  C  CE    . LYS   A 1 45  ? -2.377  24.791 -2.624 1.00 36.81 ? 42  LYS   A CE    1 
ATOM   329  N  NZ    . LYS   A 1 45  ? -1.328  23.826 -2.202 1.00 36.06 ? 42  LYS   A NZ    1 
ATOM   330  N  N     . GLN   A 1 46  ? -7.756  25.808 -2.281 1.00 18.00 ? 43  GLN   A N     1 
ATOM   331  C  CA    . GLN   A 1 46  ? -8.400  24.777 -3.058 1.00 17.88 ? 43  GLN   A CA    1 
ATOM   332  C  C     . GLN   A 1 46  ? -7.383  23.842 -3.717 1.00 19.28 ? 43  GLN   A C     1 
ATOM   333  O  O     . GLN   A 1 46  ? -6.420  24.289 -4.342 1.00 21.77 ? 43  GLN   A O     1 
ATOM   334  C  CB    . GLN   A 1 46  ? -9.219  25.483 -4.123 1.00 24.93 ? 43  GLN   A CB    1 
ATOM   335  C  CG    . GLN   A 1 46  ? -10.225 24.625 -4.823 1.00 28.19 ? 43  GLN   A CG    1 
ATOM   336  C  CD    . GLN   A 1 46  ? -11.063 25.466 -5.767 1.00 37.45 ? 43  GLN   A CD    1 
ATOM   337  O  OE1   . GLN   A 1 46  ? -11.865 26.278 -5.324 1.00 39.70 ? 43  GLN   A OE1   1 
ATOM   338  N  NE2   . GLN   A 1 46  ? -10.855 25.305 -7.058 1.00 37.12 ? 43  GLN   A NE2   1 
ATOM   339  N  N     . VAL   A 1 47  ? -7.600  22.531 -3.551 1.00 16.73 ? 44  VAL   A N     1 
ATOM   340  C  CA    . VAL   A 1 47  ? -6.729  21.489 -4.117 1.00 17.66 ? 44  VAL   A CA    1 
ATOM   341  C  C     . VAL   A 1 47  ? -7.608  20.333 -4.634 1.00 16.24 ? 44  VAL   A C     1 
ATOM   342  O  O     . VAL   A 1 47  ? -8.746  20.229 -4.235 1.00 22.03 ? 44  VAL   A O     1 
ATOM   343  C  CB    . VAL   A 1 47  ? -5.739  20.938 -3.065 1.00 19.52 ? 44  VAL   A CB    1 
ATOM   344  C  CG1   . VAL   A 1 47  ? -4.856  22.049 -2.504 1.00 22.49 ? 44  VAL   A CG1   1 
ATOM   345  C  CG2   . VAL   A 1 47  ? -6.476  20.261 -1.925 1.00 21.18 ? 44  VAL   A CG2   1 
ATOM   346  N  N     . VAL   A 1 48  ? -7.083  19.508 -5.537 1.00 17.06 ? 45  VAL   A N     1 
ATOM   347  C  CA    . VAL   A 1 48  ? -7.810  18.313 -6.016 1.00 14.98 ? 45  VAL   A CA    1 
ATOM   348  C  C     . VAL   A 1 48  ? -7.158  17.065 -5.392 1.00 13.16 ? 45  VAL   A C     1 
ATOM   349  O  O     . VAL   A 1 48  ? -5.950  16.834 -5.519 1.00 15.01 ? 45  VAL   A O     1 
ATOM   350  C  CB    . VAL   A 1 48  ? -7.860  18.223 -7.550 1.00 17.89 ? 45  VAL   A CB    1 
ATOM   351  C  CG1   . VAL   A 1 48  ? -8.639  16.983 -7.956 1.00 18.75 ? 45  VAL   A CG1   1 
ATOM   352  C  CG2   . VAL   A 1 48  ? -8.530  19.461 -8.136 1.00 19.20 ? 45  VAL   A CG2   1 
ATOM   353  N  N     . ILE   A 1 49  ? -7.990  16.267 -4.725 1.00 12.82 ? 46  ILE   A N     1 
ATOM   354  C  CA    . ILE   A 1 49  ? -7.554  15.075 -4.027 1.00 12.10 ? 46  ILE   A CA    1 
ATOM   355  C  C     . ILE   A 1 49  ? -8.547  13.980 -4.410 1.00 10.32 ? 46  ILE   A C     1 
ATOM   356  O  O     . ILE   A 1 49  ? -9.749  14.092 -4.124 1.00 10.41 ? 46  ILE   A O     1 
ATOM   357  C  CB    . ILE   A 1 49  ? -7.565  15.271 -2.493 1.00 11.52 ? 46  ILE   A CB    1 
ATOM   358  C  CG1   . ILE   A 1 49  ? -6.719  16.489 -2.090 1.00 13.26 ? 46  ILE   A CG1   1 
ATOM   359  C  CG2   . ILE   A 1 49  ? -7.106  13.995 -1.789 1.00 13.39 ? 46  ILE   A CG2   1 
ATOM   360  C  CD1   . ILE   A 1 49  ? -6.854  16.859 -0.626 1.00 12.79 ? 46  ILE   A CD1   1 
ATOM   361  N  N     . ASP   A 1 50  ? -8.065  12.932 -5.066 1.00 10.57 ? 47  ASP   A N     1 
ATOM   362  C  CA    . ASP   A 1 50  ? -8.944  11.818 -5.452 1.00 9.87  ? 47  ASP   A CA    1 
ATOM   363  C  C     . ASP   A 1 50  ? -10.132 12.240 -6.308 1.00 9.12  ? 47  ASP   A C     1 
ATOM   364  O  O     . ASP   A 1 50  ? -11.255 11.757 -6.147 1.00 10.55 ? 47  ASP   A O     1 
ATOM   365  C  CB    . ASP   A 1 50  ? -9.415  11.013 -4.237 1.00 10.72 ? 47  ASP   A CB    1 
ATOM   366  C  CG    . ASP   A 1 50  ? -8.267  10.498 -3.395 1.00 11.76 ? 47  ASP   A CG    1 
ATOM   367  O  OD1   . ASP   A 1 50  ? -7.396  9.790  -3.956 1.00 12.42 ? 47  ASP   A OD1   1 
ATOM   368  O  OD2   . ASP   A 1 50  ? -8.235  10.816 -2.194 1.00 12.06 ? 47  ASP   A OD2   1 
ATOM   369  N  N     . GLY   A 1 51  ? -9.891  13.229 -7.154 1.00 10.76 ? 48  GLY   A N     1 
ATOM   370  C  CA    . GLY   A 1 51  ? -10.898 13.739 -8.107 1.00 10.63 ? 48  GLY   A CA    1 
ATOM   371  C  C     . GLY   A 1 51  ? -11.844 14.763 -7.491 1.00 11.26 ? 48  GLY   A C     1 
ATOM   372  O  O     . GLY   A 1 51  ? -12.632 15.331 -8.219 1.00 13.44 ? 48  GLY   A O     1 
ATOM   373  N  N     . GLU   A 1 52  ? -11.725 15.016 -6.200 1.00 11.16 ? 49  GLU   A N     1 
ATOM   374  C  CA    . GLU   A 1 52  ? -12.588 16.007 -5.514 1.00 11.90 ? 49  GLU   A CA    1 
ATOM   375  C  C     . GLU   A 1 52  ? -11.868 17.360 -5.407 1.00 12.40 ? 49  GLU   A C     1 
ATOM   376  O  O     . GLU   A 1 52  ? -10.733 17.419 -4.903 1.00 12.59 ? 49  GLU   A O     1 
ATOM   377  C  CB    . GLU   A 1 52  ? -12.931 15.527 -4.101 1.00 12.63 ? 49  GLU   A CB    1 
ATOM   378  C  CG    . GLU   A 1 52  ? -13.917 16.390 -3.344 1.00 13.94 ? 49  GLU   A CG    1 
ATOM   379  C  CD    . GLU   A 1 52  ? -14.274 15.798 -1.990 1.00 16.35 ? 49  GLU   A CD    1 
ATOM   380  O  OE1   . GLU   A 1 52  ? -13.379 15.427 -1.256 1.00 15.39 ? 49  GLU   A OE1   1 
ATOM   381  O  OE2   . GLU   A 1 52  ? -15.483 15.654 -1.721 1.00 22.89 ? 49  GLU   A OE2   1 
ATOM   382  N  N     . THR   A 1 53  ? -12.555 18.418 -5.831 1.00 13.66 ? 50  THR   A N     1 
ATOM   383  C  CA    . THR   A 1 53  ? -12.058 19.794 -5.559 1.00 14.82 ? 50  THR   A CA    1 
ATOM   384  C  C     . THR   A 1 53  ? -12.375 20.086 -4.090 1.00 14.88 ? 50  THR   A C     1 
ATOM   385  O  O     . THR   A 1 53  ? -13.491 20.086 -3.706 1.00 17.37 ? 50  THR   A O     1 
ATOM   386  C  CB    . THR   A 1 53  ? -12.639 20.807 -6.550 1.00 17.00 ? 50  THR   A CB    1 
ATOM   387  O  OG1   . THR   A 1 53  ? -12.254 20.361 -7.852 1.00 20.39 ? 50  THR   A OG1   1 
ATOM   388  C  CG2   . THR   A 1 53  ? -12.067 22.187 -6.301 1.00 19.91 ? 50  THR   A CG2   1 
ATOM   389  N  N     . CYS   A 1 54  ? -11.310 20.231 -3.300 1.00 16.28 ? 51  CYS   A N     1 
ATOM   390  C  CA    . CYS   A 1 54  ? -11.373 20.343 -1.814 1.00 17.13 ? 51  CYS   A CA    1 
ATOM   391  C  C     . CYS   A 1 54  ? -10.965 21.781 -1.405 1.00 17.65 ? 51  CYS   A C     1 
ATOM   392  O  O     . CYS   A 1 54  ? -9.995  22.263 -1.925 1.00 17.77 ? 51  CYS   A O     1 
ATOM   393  C  CB    . CYS   A 1 54  ? -10.422 19.314 -1.140 1.00 11.45 ? 51  CYS   A CB    1 
ATOM   394  S  SG    . CYS   A 1 54  ? -10.736 17.571 -1.513 1.00 16.80 ? 51  CYS   A SG    1 
ATOM   395  N  N     . LEU   A 1 55  ? -11.722 22.408 -0.523 1.00 14.61 ? 52  LEU   A N     1 
ATOM   396  C  CA    . LEU   A 1 55  ? -11.257 23.672 0.071  1.00 14.93 ? 52  LEU   A CA    1 
ATOM   397  C  C     . LEU   A 1 55  ? -10.666 23.310 1.441  1.00 12.04 ? 52  LEU   A C     1 
ATOM   398  O  O     . LEU   A 1 55  ? -11.404 22.836 2.276  1.00 13.85 ? 52  LEU   A O     1 
ATOM   399  C  CB    . LEU   A 1 55  ? -12.444 24.625 0.218  1.00 17.35 ? 52  LEU   A CB    1 
ATOM   400  C  CG    . LEU   A 1 55  ? -12.128 25.942 0.918  1.00 20.29 ? 52  LEU   A CG    1 
ATOM   401  C  CD1   . LEU   A 1 55  ? -10.981 26.646 0.198  1.00 22.13 ? 52  LEU   A CD1   1 
ATOM   402  C  CD2   . LEU   A 1 55  ? -13.393 26.805 0.973  1.00 24.44 ? 52  LEU   A CD2   1 
ATOM   403  N  N     . LEU   A 1 56  ? -9.345  23.433 1.556  1.00 13.43 ? 53  LEU   A N     1 
ATOM   404  C  CA    . LEU   A 1 56  ? -8.660  23.177 2.867  1.00 13.42 ? 53  LEU   A CA    1 
ATOM   405  C  C     . LEU   A 1 56  ? -8.638  24.484 3.681  1.00 13.90 ? 53  LEU   A C     1 
ATOM   406  O  O     . LEU   A 1 56  ? -8.208  25.482 3.148  1.00 16.59 ? 53  LEU   A O     1 
ATOM   407  C  CB    . LEU   A 1 56  ? -7.223  22.708 2.647  1.00 13.84 ? 53  LEU   A CB    1 
ATOM   408  C  CG    . LEU   A 1 56  ? -7.037  21.489 1.750  1.00 15.27 ? 53  LEU   A CG    1 
ATOM   409  C  CD1   . LEU   A 1 56  ? -5.617  20.966 1.855  1.00 17.50 ? 53  LEU   A CD1   1 
ATOM   410  C  CD2   . LEU   A 1 56  ? -8.059  20.404 2.094  1.00 15.05 ? 53  LEU   A CD2   1 
ATOM   411  N  N     . ASP   A 1 57  ? -9.167  24.440 4.887  1.00 11.87 ? 54  ASP   A N     1 
ATOM   412  C  CA    . ASP   A 1 57  ? -9.164  25.606 5.808  1.00 11.64 ? 54  ASP   A CA    1 
ATOM   413  C  C     . ASP   A 1 57  ? -8.335  25.104 6.993  1.00 11.51 ? 54  ASP   A C     1 
ATOM   414  O  O     . ASP   A 1 57  ? -8.839  24.355 7.772  1.00 11.38 ? 54  ASP   A O     1 
ATOM   415  C  CB    . ASP   A 1 57  ? -10.587 26.019 6.152  1.00 13.72 ? 54  ASP   A CB    1 
ATOM   416  C  CG    . ASP   A 1 57  ? -10.655 27.326 6.912  1.00 14.88 ? 54  ASP   A CG    1 
ATOM   417  O  OD1   . ASP   A 1 57  ? -9.624  27.829 7.291  1.00 18.08 ? 54  ASP   A OD1   1 
ATOM   418  O  OD2   . ASP   A 1 57  ? -11.744 27.794 7.093  1.00 22.69 ? 54  ASP   A OD2   1 
ATOM   419  N  N     . ILE   A 1 58  ? -7.076  25.520 7.010  1.00 11.79 ? 55  ILE   A N     1 
ATOM   420  C  CA    . ILE   A 1 58  ? -6.076  24.974 7.969  1.00 11.46 ? 55  ILE   A CA    1 
ATOM   421  C  C     . ILE   A 1 58  ? -5.728  26.007 9.040  1.00 10.73 ? 55  ILE   A C     1 
ATOM   422  O  O     . ILE   A 1 58  ? -5.266  27.086 8.720  1.00 12.83 ? 55  ILE   A O     1 
ATOM   423  C  CB    . ILE   A 1 58  ? -4.793  24.558 7.230  1.00 12.17 ? 55  ILE   A CB    1 
ATOM   424  C  CG1   . ILE   A 1 58  ? -5.086  23.577 6.088  1.00 13.47 ? 55  ILE   A CG1   1 
ATOM   425  C  CG2   . ILE   A 1 58  ? -3.750  24.012 8.192  1.00 13.62 ? 55  ILE   A CG2   1 
ATOM   426  C  CD1   . ILE   A 1 58  ? -3.928  23.366 5.176  1.00 14.43 ? 55  ILE   A CD1   1 
ATOM   427  N  N     . LEU   A 1 59  ? -5.968  25.604 10.273 1.00 10.28 ? 56  LEU   A N     1 
ATOM   428  C  CA    . LEU   A 1 59  ? -5.544  26.431 11.423 1.00 10.82 ? 56  LEU   A CA    1 
ATOM   429  C  C     . LEU   A 1 59  ? -4.187  25.942 11.925 1.00 11.21 ? 56  LEU   A C     1 
ATOM   430  O  O     . LEU   A 1 59  ? -4.053  24.808 12.399 1.00 11.01 ? 56  LEU   A O     1 
ATOM   431  C  CB    . LEU   A 1 59  ? -6.566  26.381 12.535 1.00 10.91 ? 56  LEU   A CB    1 
ATOM   432  C  CG    . LEU   A 1 59  ? -6.295  27.269 13.743 1.00 12.68 ? 56  LEU   A CG    1 
ATOM   433  C  CD1   . LEU   A 1 59  ? -6.351  28.749 13.364 1.00 14.60 ? 56  LEU   A CD1   1 
ATOM   434  C  CD2   . LEU   A 1 59  ? -7.284  26.942 14.845 1.00 14.27 ? 56  LEU   A CD2   1 
ATOM   435  N  N     . ASP   A 1 60  ? -3.198  26.821 11.848 1.00 10.48 ? 57  ASP   A N     1 
ATOM   436  C  CA    . ASP   A 1 60  ? -1.850  26.598 12.342 1.00 11.52 ? 57  ASP   A CA    1 
ATOM   437  C  C     . ASP   A 1 60  ? -1.870  27.162 13.758 1.00 10.77 ? 57  ASP   A C     1 
ATOM   438  O  O     . ASP   A 1 60  ? -1.962  28.375 13.958 1.00 13.84 ? 57  ASP   A O     1 
ATOM   439  C  CB    . ASP   A 1 60  ? -0.868  27.343 11.461 1.00 12.61 ? 57  ASP   A CB    1 
ATOM   440  C  CG    . ASP   A 1 60  ? 0.547   27.312 11.975 1.00 12.44 ? 57  ASP   A CG    1 
ATOM   441  O  OD1   . ASP   A 1 60  ? 0.924   26.352 12.667 1.00 13.17 ? 57  ASP   A OD1   1 
ATOM   442  O  OD2   . ASP   A 1 60  ? 1.308   28.263 11.664 1.00 14.79 ? 57  ASP   A OD2   1 
ATOM   443  N  N     . THR   A 1 61  ? -1.818  26.278 14.750 1.00 11.18 ? 58  THR   A N     1 
ATOM   444  C  CA    . THR   A 1 61  ? -1.946  26.718 16.168 1.00 11.88 ? 58  THR   A CA    1 
ATOM   445  C  C     . THR   A 1 61  ? -0.626  27.190 16.772 1.00 12.89 ? 58  THR   A C     1 
ATOM   446  O  O     . THR   A 1 61  ? 0.397   26.706 16.413 1.00 12.48 ? 58  THR   A O     1 
ATOM   447  C  CB    . THR   A 1 61  ? -2.621  25.631 17.001 1.00 10.89 ? 58  THR   A CB    1 
ATOM   448  O  OG1   . THR   A 1 61  ? -1.746  24.515 17.171 1.00 11.69 ? 58  THR   A OG1   1 
ATOM   449  C  CG2   . THR   A 1 61  ? -3.967  25.237 16.431 1.00 11.80 ? 58  THR   A CG2   1 
ATOM   450  N  N     . ALA   A 1 62  ? -0.725  28.141 17.710 1.00 13.32 ? 59  ALA   A N     1 
ATOM   451  C  CA    . ALA   A 1 62  ? 0.495   28.656 18.363 1.00 13.79 ? 59  ALA   A CA    1 
ATOM   452  C  C     . ALA   A 1 62  ? 0.576   28.088 19.776 1.00 13.73 ? 59  ALA   A C     1 
ATOM   453  O  O     . ALA   A 1 62  ? 1.191   27.108 19.953 1.00 15.50 ? 59  ALA   A O     1 
ATOM   454  C  CB    . ALA   A 1 62  ? 0.491   30.170 18.354 1.00 16.56 ? 59  ALA   A CB    1 
ATOM   455  N  N     . GLY   A 1 63  ? -0.094  28.702 20.732 1.00 15.27 ? 60  GLY   A N     1 
ATOM   456  C  CA    . GLY   A 1 63  ? -0.007  28.210 22.116 1.00 16.52 ? 60  GLY   A CA    1 
ATOM   457  C  C     . GLY   A 1 63  ? -0.637  26.839 22.247 1.00 14.44 ? 60  GLY   A C     1 
ATOM   458  O  O     . GLY   A 1 63  ? -1.666  26.633 21.691 1.00 18.95 ? 60  GLY   A O     1 
ATOM   459  N  N     . GLN   A 1 64  ? -0.053  25.971 23.055 1.00 15.78 ? 61  GLN   A N     1 
ATOM   460  C  CA    . GLN   A 1 64  ? -0.568  24.618 23.209 1.00 16.24 ? 61  GLN   A CA    1 
ATOM   461  C  C     . GLN   A 1 64  ? -1.126  24.390 24.616 1.00 17.67 ? 61  GLN   A C     1 
ATOM   462  O  O     . GLN   A 1 64  ? -1.232  23.259 25.055 1.00 22.87 ? 61  GLN   A O     1 
ATOM   463  C  CB    . GLN   A 1 64  ? 0.521   23.593 22.854 1.00 16.92 ? 61  GLN   A CB    1 
ATOM   464  C  CG    . GLN   A 1 64  ? 1.140   23.748 21.457 1.00 15.44 ? 61  GLN   A CG    1 
ATOM   465  C  CD    . GLN   A 1 64  ? 0.146   23.539 20.326 1.00 14.55 ? 61  GLN   A CD    1 
ATOM   466  O  OE1   . GLN   A 1 64  ? -0.459  22.473 20.196 1.00 15.47 ? 61  GLN   A OE1   1 
ATOM   467  N  NE2   . GLN   A 1 64  ? 0.000   24.543 19.479 1.00 13.69 ? 61  GLN   A NE2   1 
ATOM   468  N  N     . GLU   A 1 65  ? -1.525  25.462 25.305 1.00 16.65 ? 62  GLU   A N     1 
ATOM   469  C  CA    . GLU   A 1 65  ? -1.991  25.387 26.692 1.00 19.56 ? 62  GLU   A CA    1 
ATOM   470  C  C     . GLU   A 1 65  ? -3.297  24.561 26.809 1.00 18.68 ? 62  GLU   A C     1 
ATOM   471  O  O     . GLU   A 1 65  ? -4.228  24.756 26.045 1.00 23.34 ? 62  GLU   A O     1 
ATOM   472  C  CB    . GLU   A 1 65  ? -2.245  26.800 27.281 1.00 21.65 ? 62  GLU   A CB    1 
ATOM   473  C  CG    . GLU   A 1 65  ? -1.155  27.870 27.091 1.00 27.79 ? 62  GLU   A CG    1 
ATOM   474  C  CD    . GLU   A 1 65  ? -1.343  28.744 25.829 1.00 36.95 ? 62  GLU   A CD    1 
ATOM   475  O  OE1   . GLU   A 1 65  ? -2.183  28.414 24.951 1.00 40.03 ? 62  GLU   A OE1   1 
ATOM   476  O  OE2   . GLU   A 1 65  ? -0.654  29.778 25.692 1.00 44.33 ? 62  GLU   A OE2   1 
ATOM   477  N  N     . GLU   A 1 66  ? -3.340  23.663 27.798 1.00 21.53 ? 63  GLU   A N     1 
ATOM   478  C  CA    . GLU   A 1 66  ? -4.530  22.898 28.206 1.00 26.03 ? 63  GLU   A CA    1 
ATOM   479  C  C     . GLU   A 1 66  ? -5.757  23.792 28.438 1.00 22.25 ? 63  GLU   A C     1 
ATOM   480  O  O     . GLU   A 1 66  ? -6.861  23.497 27.944 1.00 26.37 ? 63  GLU   A O     1 
ATOM   481  C  CB    . GLU   A 1 66  ? -4.155  22.135 29.501 1.00 29.82 ? 63  GLU   A CB    1 
ATOM   482  C  CG    . GLU   A 1 66  ? -5.257  21.507 30.338 1.00 34.48 ? 63  GLU   A CG    1 
ATOM   483  C  CD    . GLU   A 1 66  ? -5.572  20.068 29.964 1.00 42.60 ? 63  GLU   A CD    1 
ATOM   484  O  OE1   . GLU   A 1 66  ? -5.399  19.683 28.796 1.00 53.57 ? 63  GLU   A OE1   1 
ATOM   485  O  OE2   . GLU   A 1 66  ? -6.012  19.314 30.855 1.00 47.37 ? 63  GLU   A OE2   1 
ATOM   486  N  N     . TYR   A 1 67  ? -5.555  24.878 29.198 1.00 19.02 ? 64  TYR   A N     1 
ATOM   487  C  CA    . TYR   A 1 67  ? -6.634  25.762 29.634 1.00 15.29 ? 64  TYR   A CA    1 
ATOM   488  C  C     . TYR   A 1 67  ? -6.744  26.963 28.706 1.00 15.35 ? 64  TYR   A C     1 
ATOM   489  O  O     . TYR   A 1 67  ? -6.113  28.015 28.913 1.00 19.89 ? 64  TYR   A O     1 
ATOM   490  C  CB    . TYR   A 1 67  ? -6.453  26.206 31.090 1.00 14.99 ? 64  TYR   A CB    1 
ATOM   491  C  CG    . TYR   A 1 67  ? -6.448  25.017 32.013 1.00 15.39 ? 64  TYR   A CG    1 
ATOM   492  C  CD1   . TYR   A 1 67  ? -7.535  24.163 32.069 1.00 19.54 ? 64  TYR   A CD1   1 
ATOM   493  C  CD2   . TYR   A 1 67  ? -5.327  24.693 32.772 1.00 16.76 ? 64  TYR   A CD2   1 
ATOM   494  C  CE1   . TYR   A 1 67  ? -7.523  23.041 32.872 1.00 20.48 ? 64  TYR   A CE1   1 
ATOM   495  C  CE2   . TYR   A 1 67  ? -5.317  23.586 33.598 1.00 18.80 ? 64  TYR   A CE2   1 
ATOM   496  C  CZ    . TYR   A 1 67  ? -6.408  22.755 33.628 1.00 17.87 ? 64  TYR   A CZ    1 
ATOM   497  O  OH    . TYR   A 1 67  ? -6.435  21.625 34.421 1.00 21.27 ? 64  TYR   A OH    1 
ATOM   498  N  N     . SER   A 1 68  ? -7.543  26.794 27.666 1.00 14.09 ? 65  SER   A N     1 
ATOM   499  C  CA    . SER   A 1 68  ? -7.713  27.825 26.691 1.00 13.67 ? 65  SER   A CA    1 
ATOM   500  C  C     . SER   A 1 68  ? -9.077  27.661 26.039 1.00 13.25 ? 65  SER   A C     1 
ATOM   501  O  O     . SER   A 1 68  ? -9.360  26.645 25.387 1.00 14.30 ? 65  SER   A O     1 
ATOM   502  C  CB    . SER   A 1 68  ? -6.641  27.705 25.616 1.00 14.22 ? 65  SER   A CB    1 
ATOM   503  O  OG    . SER   A 1 68  ? -6.968  28.524 24.496 1.00 15.58 ? 65  SER   A OG    1 
ATOM   504  N  N     . ALA   A 1 69  ? -9.912  28.667 26.220 1.00 13.55 ? 66  ALA   A N     1 
ATOM   505  C  CA    . ALA   A 1 69  ? -11.215 28.670 25.594 1.00 15.04 ? 66  ALA   A CA    1 
ATOM   506  C  C     . ALA   A 1 69  ? -11.092 28.584 24.063 1.00 16.02 ? 66  ALA   A C     1 
ATOM   507  O  O     . ALA   A 1 69  ? -11.898 27.929 23.402 1.00 16.68 ? 66  ALA   A O     1 
ATOM   508  C  CB    . ALA   A 1 69  ? -11.973 29.921 26.007 1.00 17.43 ? 66  ALA   A CB    1 
ATOM   509  N  N     . MET   A 1 70  ? -10.100 29.243 23.479 1.00 14.89 ? 67  MET   A N     1 
ATOM   510  C  CA    . MET   A 1 70  ? -10.001 29.236 22.023 1.00 16.14 ? 67  MET   A CA    1 
ATOM   511  C  C     . MET   A 1 70  ? -9.522  27.875 21.507 1.00 15.04 ? 67  MET   A C     1 
ATOM   512  O  O     . MET   A 1 70  ? -9.987  27.416 20.468 1.00 14.27 ? 67  MET   A O     1 
ATOM   513  C  CB    . MET   A 1 70  ? -9.180  30.418 21.519 1.00 22.08 ? 67  MET   A CB    1 
ATOM   514  C  CG    . MET   A 1 70  ? -9.880  31.768 21.752 1.00 27.01 ? 67  MET   A CG    1 
ATOM   515  S  SD    . MET   A 1 70  ? -11.662 31.875 21.374 1.00 36.12 ? 67  MET   A SD    1 
ATOM   516  C  CE    . MET   A 1 70  ? -11.588 31.427 19.645 1.00 32.90 ? 67  MET   A CE    1 
ATOM   517  N  N     . ARG   A 1 71  ? -8.722  27.165 22.307 1.00 13.72 ? 68  ARG   A N     1 
ATOM   518  C  CA    . ARG   A 1 71  ? -8.295  25.797 21.921 1.00 13.57 ? 68  ARG   A CA    1 
ATOM   519  C  C     . ARG   A 1 71  ? -9.528  24.890 22.005 1.00 12.02 ? 68  ARG   A C     1 
ATOM   520  O  O     . ARG   A 1 71  ? -9.687  24.060 21.115 1.00 12.93 ? 68  ARG   A O     1 
ATOM   521  C  CB    . ARG   A 1 71  ? -7.170  25.333 22.853 1.00 15.13 ? 68  ARG   A CB    1 
ATOM   522  C  CG    . ARG   A 1 71  ? -6.637  23.936 22.576 1.00 20.46 ? 68  ARG   A CG    1 
ATOM   523  C  CD    . ARG   A 1 71  ? -5.374  23.813 23.433 1.00 27.13 ? 68  ARG   A CD    1 
ATOM   524  N  NE    . ARG   A 1 71  ? -4.530  23.780 22.305 1.00 31.22 ? 68  ARG   A NE    1 
ATOM   525  C  CZ    . ARG   A 1 71  ? -3.848  22.739 21.817 1.00 29.53 ? 68  ARG   A CZ    1 
ATOM   526  N  NH1   . ARG   A 1 71  ? -3.253  22.863 20.647 1.00 24.96 ? 68  ARG   A NH1   1 
ATOM   527  N  NH2   . ARG   A 1 71  ? -3.712  21.654 22.534 1.00 34.81 ? 68  ARG   A NH2   1 
ATOM   528  N  N     . ASP   A 1 72  ? -10.352 25.021 23.048 1.00 12.36 ? 69  ASP   A N     1 
ATOM   529  C  CA    . ASP   A 1 72  ? -11.568 24.199 23.126 1.00 14.09 ? 69  ASP   A CA    1 
ATOM   530  C  C     . ASP   A 1 72  ? -12.423 24.454 21.886 1.00 13.84 ? 69  ASP   A C     1 
ATOM   531  O  O     . ASP   A 1 72  ? -12.936 23.526 21.277 1.00 14.55 ? 69  ASP   A O     1 
ATOM   532  C  CB    . ASP   A 1 72  ? -12.396 24.495 24.384 1.00 17.24 ? 69  ASP   A CB    1 
ATOM   533  C  CG    . ASP   A 1 72  ? -11.719 24.042 25.662 1.00 25.05 ? 69  ASP   A CG    1 
ATOM   534  O  OD1   . ASP   A 1 72  ? -10.771 23.222 25.603 1.00 29.56 ? 69  ASP   A OD1   1 
ATOM   535  O  OD2   . ASP   A 1 72  ? -12.148 24.514 26.737 1.00 31.63 ? 69  ASP   A OD2   1 
ATOM   536  N  N     . GLN   A 1 73  ? -12.504 25.721 21.473 1.00 14.69 ? 70  GLN   A N     1 
ATOM   537  C  CA    . GLN   A 1 73  ? -13.325 26.068 20.325 1.00 14.04 ? 70  GLN   A CA    1 
ATOM   538  C  C     . GLN   A 1 73  ? -12.774 25.459 19.049 1.00 13.53 ? 70  GLN   A C     1 
ATOM   539  O  O     . GLN   A 1 73  ? -13.543 24.919 18.262 1.00 14.62 ? 70  GLN   A O     1 
ATOM   540  C  CB    . GLN   A 1 73  ? -13.452 27.591 20.163 1.00 16.70 ? 70  GLN   A CB    1 
ATOM   541  C  CG    . GLN   A 1 73  ? -14.419 27.964 19.048 1.00 17.95 ? 70  GLN   A CG    1 
ATOM   542  C  CD    . GLN   A 1 73  ? -15.794 27.338 19.255 1.00 23.31 ? 70  GLN   A CD    1 
ATOM   543  O  OE1   . GLN   A 1 73  ? -16.440 27.561 20.280 1.00 28.84 ? 70  GLN   A OE1   1 
ATOM   544  N  NE2   . GLN   A 1 73  ? -16.225 26.517 18.313 1.00 25.00 ? 70  GLN   A NE2   1 
ATOM   545  N  N     . TYR   A 1 74  ? -11.476 25.595 18.801 1.00 13.54 ? 71  TYR   A N     1 
ATOM   546  C  CA    . TYR   A 1 74  ? -10.968 25.004 17.572 1.00 13.06 ? 71  TYR   A CA    1 
ATOM   547  C  C     . TYR   A 1 74  ? -10.945 23.476 17.585 1.00 13.06 ? 71  TYR   A C     1 
ATOM   548  O  O     . TYR   A 1 74  ? -11.049 22.840 16.502 1.00 12.92 ? 71  TYR   A O     1 
ATOM   549  C  CB    . TYR   A 1 74  ? -9.682  25.648 17.079 1.00 13.94 ? 71  TYR   A CB    1 
ATOM   550  C  CG    . TYR   A 1 74  ? -8.395  25.478 17.857 1.00 12.79 ? 71  TYR   A CG    1 
ATOM   551  C  CD1   . TYR   A 1 74  ? -7.819  24.223 18.079 1.00 13.22 ? 71  TYR   A CD1   1 
ATOM   552  C  CD2   . TYR   A 1 74  ? -7.705  26.606 18.305 1.00 13.96 ? 71  TYR   A CD2   1 
ATOM   553  C  CE1   . TYR   A 1 74  ? -6.607  24.119 18.750 1.00 12.63 ? 71  TYR   A CE1   1 
ATOM   554  C  CE2   . TYR   A 1 74  ? -6.478  26.509 18.916 1.00 14.87 ? 71  TYR   A CE2   1 
ATOM   555  C  CZ    . TYR   A 1 74  ? -5.945  25.276 19.184 1.00 14.61 ? 71  TYR   A CZ    1 
ATOM   556  O  OH    . TYR   A 1 74  ? -4.715  25.185 19.794 1.00 15.42 ? 71  TYR   A OH    1 
ATOM   557  N  N     . MET   A 1 75  ? -10.902 22.852 18.757 1.00 12.11 ? 72  MET   A N     1 
ATOM   558  C  CA    . MET   A 1 75  ? -11.088 21.400 18.818 1.00 13.40 ? 72  MET   A CA    1 
ATOM   559  C  C     . MET   A 1 75  ? -12.545 20.986 18.557 1.00 12.93 ? 72  MET   A C     1 
ATOM   560  O  O     . MET   A 1 75  ? -12.768 19.952 17.966 1.00 15.71 ? 72  MET   A O     1 
ATOM   561  C  CB    . MET   A 1 75  ? -10.558 20.807 20.106 1.00 13.70 ? 72  MET   A CB    1 
ATOM   562  C  CG    . MET   A 1 75  ? -9.044  20.919 20.189 1.00 13.41 ? 72  MET   A CG    1 
ATOM   563  S  SD    . MET   A 1 75  ? -8.408  20.135 21.657 1.00 15.15 ? 72  MET   A SD    1 
ATOM   564  C  CE    . MET   A 1 75  ? -6.648  20.314 21.325 1.00 16.65 ? 72  MET   A CE    1 
ATOM   565  N  N     . ARG   A 1 76  ? -13.513 21.816 18.936 1.00 14.00 ? 73  ARG   A N     1 
ATOM   566  C  CA    . ARG   A 1 76  ? -14.913 21.596 18.551 1.00 14.32 ? 73  ARG   A CA    1 
ATOM   567  C  C     . ARG   A 1 76  ? -15.126 21.748 17.038 1.00 15.20 ? 73  ARG   A C     1 
ATOM   568  O  O     . ARG   A 1 76  ? -15.791 20.905 16.399 1.00 16.54 ? 73  ARG   A O     1 
ATOM   569  C  CB    . ARG   A 1 76  ? -15.858 22.513 19.343 1.00 15.26 ? 73  ARG   A CB    1 
ATOM   570  C  CG    . ARG   A 1 76  ? -16.027 22.062 20.775 1.00 18.33 ? 73  ARG   A CG    1 
ATOM   571  C  CD    . ARG   A 1 76  ? -17.159 22.788 21.447 1.00 22.23 ? 73  ARG   A CD    1 
ATOM   572  N  NE    . ARG   A 1 76  ? -16.823 24.196 21.610 1.00 31.03 ? 73  ARG   A NE    1 
ATOM   573  C  CZ    . ARG   A 1 76  ? -16.278 24.746 22.700 1.00 30.39 ? 73  ARG   A CZ    1 
ATOM   574  N  NH1   . ARG   A 1 76  ? -15.980 24.022 23.781 1.00 36.41 ? 73  ARG   A NH1   1 
ATOM   575  N  NH2   . ARG   A 1 76  ? -16.024 26.044 22.698 1.00 29.85 ? 73  ARG   A NH2   1 
ATOM   576  N  N     . THR   A 1 77  ? -14.553 22.796 16.456 1.00 13.66 ? 74  THR   A N     1 
ATOM   577  C  CA    . THR   A 1 77  ? -14.764 23.149 15.051 1.00 13.45 ? 74  THR   A CA    1 
ATOM   578  C  C     . THR   A 1 77  ? -13.955 22.270 14.092 1.00 13.55 ? 74  THR   A C     1 
ATOM   579  O  O     . THR   A 1 77  ? -14.401 21.932 12.989 1.00 14.32 ? 74  THR   A O     1 
ATOM   580  C  CB    . THR   A 1 77  ? -14.460 24.642 14.844 1.00 15.15 ? 74  THR   A CB    1 
ATOM   581  O  OG1   . THR   A 1 77  ? -15.346 25.384 15.695 1.00 18.17 ? 74  THR   A OG1   1 
ATOM   582  C  CG2   . THR   A 1 77  ? -14.673 25.082 13.428 1.00 16.54 ? 74  THR   A CG2   1 
ATOM   583  N  N     . GLY   A 1 78  ? -12.749 21.902 14.499 1.00 12.61 ? 75  GLY   A N     1 
ATOM   584  C  CA    . GLY   A 1 78  ? -11.837 21.144 13.620 1.00 12.02 ? 75  GLY   A CA    1 
ATOM   585  C  C     . GLY   A 1 78  ? -12.386 19.766 13.273 1.00 11.37 ? 75  GLY   A C     1 
ATOM   586  O  O     . GLY   A 1 78  ? -12.906 19.055 14.140 1.00 13.68 ? 75  GLY   A O     1 
ATOM   587  N  N     . GLU   A 1 79  ? -12.228 19.375 12.010 1.00 10.67 ? 76  GLU   A N     1 
ATOM   588  C  CA    . GLU   A 1 79  ? -12.687 18.084 11.533 1.00 10.44 ? 76  GLU   A CA    1 
ATOM   589  C  C     . GLU   A 1 79  ? -11.578 17.052 11.518 1.00 9.97  ? 76  GLU   A C     1 
ATOM   590  O  O     . GLU   A 1 79  ? -11.842 15.881 11.724 1.00 11.88 ? 76  GLU   A O     1 
ATOM   591  C  CB    . GLU   A 1 79  ? -13.274 18.190 10.146 1.00 11.60 ? 76  GLU   A CB    1 
ATOM   592  C  CG    . GLU   A 1 79  ? -14.544 19.019 10.105 1.00 13.42 ? 76  GLU   A CG    1 
ATOM   593  C  CD    . GLU   A 1 79  ? -15.025 19.122 8.683  1.00 19.10 ? 76  GLU   A CD    1 
ATOM   594  O  OE1   . GLU   A 1 79  ? -14.369 19.788 7.875  1.00 16.61 ? 76  GLU   A OE1   1 
ATOM   595  O  OE2   . GLU   A 1 79  ? -16.043 18.475 8.344  1.00 35.71 ? 76  GLU   A OE2   1 
ATOM   596  N  N     . GLY   A 1 80  ? -10.334 17.468 11.273 1.00 9.44  ? 77  GLY   A N     1 
ATOM   597  C  CA    . GLY   A 1 80  ? -9.184  16.579 11.346 1.00 8.69  ? 77  GLY   A CA    1 
ATOM   598  C  C     . GLY   A 1 80  ? -8.007  17.265 11.963 1.00 8.31  ? 77  GLY   A C     1 
ATOM   599  O  O     . GLY   A 1 80  ? -7.864  18.473 11.851 1.00 9.12  ? 77  GLY   A O     1 
ATOM   600  N  N     . PHE   A 1 81  ? -7.150  16.464 12.600 1.00 8.33  ? 78  PHE   A N     1 
ATOM   601  C  CA    . PHE   A 1 81  ? -6.015  16.976 13.398 1.00 8.78  ? 78  PHE   A CA    1 
ATOM   602  C  C     . PHE   A 1 81  ? -4.716  16.360 12.935 1.00 8.59  ? 78  PHE   A C     1 
ATOM   603  O  O     . PHE   A 1 81  ? -4.579  15.139 12.891 1.00 9.51  ? 78  PHE   A O     1 
ATOM   604  C  CB    . PHE   A 1 81  ? -6.275  16.720 14.873 1.00 9.16  ? 78  PHE   A CB    1 
ATOM   605  C  CG    . PHE   A 1 81  ? -7.527  17.405 15.344 1.00 9.84  ? 78  PHE   A CG    1 
ATOM   606  C  CD1   . PHE   A 1 81  ? -8.779  16.826 15.152 1.00 10.34 ? 78  PHE   A CD1   1 
ATOM   607  C  CD2   . PHE   A 1 81  ? -7.459  18.671 15.907 1.00 9.34  ? 78  PHE   A CD2   1 
ATOM   608  C  CE1   . PHE   A 1 81  ? -9.943  17.490 15.518 1.00 11.99 ? 78  PHE   A CE1   1 
ATOM   609  C  CE2   . PHE   A 1 81  ? -8.624  19.335 16.259 1.00 10.55 ? 78  PHE   A CE2   1 
ATOM   610  C  CZ    . PHE   A 1 81  ? -9.865  18.759 16.070 1.00 11.92 ? 78  PHE   A CZ    1 
ATOM   611  N  N     . LEU   A 1 82  ? -3.769  17.212 12.552 1.00 8.32  ? 79  LEU   A N     1 
ATOM   612  C  CA    . LEU   A 1 82  ? -2.386  16.800 12.214 1.00 8.57  ? 79  LEU   A CA    1 
ATOM   613  C  C     . LEU   A 1 82  ? -1.612  16.949 13.538 1.00 8.35  ? 79  LEU   A C     1 
ATOM   614  O  O     . LEU   A 1 82  ? -1.491  18.070 14.033 1.00 10.49 ? 79  LEU   A O     1 
ATOM   615  C  CB    . LEU   A 1 82  ? -1.845  17.748 11.141 1.00 11.28 ? 79  LEU   A CB    1 
ATOM   616  C  CG    . LEU   A 1 82  ? -0.849  17.110 10.186 1.00 13.54 ? 79  LEU   A CG    1 
ATOM   617  C  CD1   . LEU   A 1 82  ? -1.532  16.039 9.304  1.00 12.44 ? 79  LEU   A CD1   1 
ATOM   618  C  CD2   . LEU   A 1 82  ? -0.223  18.192 9.325  1.00 14.53 ? 79  LEU   A CD2   1 
ATOM   619  N  N     . CYS   A 1 83  ? -1.204  15.826 14.117 1.00 8.46  ? 80  CYS   A N     1 
ATOM   620  C  CA    . CYS   A 1 83  ? -0.515  15.797 15.441 1.00 8.75  ? 80  CYS   A CA    1 
ATOM   621  C  C     . CYS   A 1 83  ? 0.971   15.607 15.138 1.00 7.91  ? 80  CYS   A C     1 
ATOM   622  O  O     . CYS   A 1 83  ? 1.408   14.517 14.769 1.00 8.14  ? 80  CYS   A O     1 
ATOM   623  C  CB    . CYS   A 1 83  ? -1.097  14.688 16.307 1.00 10.14 ? 80  CYS   A CB    1 
ATOM   624  S  SG    . CYS   A 1 83  ? -2.828  14.990 16.765 1.00 14.72 ? 80  CYS   A SG    1 
ATOM   625  N  N     . VAL   A 1 84  ? 1.677   16.710 15.284 1.00 7.49  ? 81  VAL   A N     1 
ATOM   626  C  CA    . VAL   A 1 84  ? 3.089   16.780 14.811 1.00 7.26  ? 81  VAL   A CA    1 
ATOM   627  C  C     . VAL   A 1 84  ? 4.065   16.715 15.992 1.00 7.46  ? 81  VAL   A C     1 
ATOM   628  O  O     . VAL   A 1 84  ? 3.868   17.422 16.977 1.00 7.83  ? 81  VAL   A O     1 
ATOM   629  C  CB    . VAL   A 1 84  ? 3.330   18.101 14.039 1.00 7.83  ? 81  VAL   A CB    1 
ATOM   630  C  CG1   . VAL   A 1 84  ? 4.750   18.173 13.464 1.00 8.28  ? 81  VAL   A CG1   1 
ATOM   631  C  CG2   . VAL   A 1 84  ? 2.269   18.301 12.953 1.00 8.71  ? 81  VAL   A CG2   1 
ATOM   632  N  N     . PHE   A 1 85  ? 5.052   15.836 15.851 1.00 7.40  ? 82  PHE   A N     1 
ATOM   633  C  CA    . PHE   A 1 85  ? 6.230   15.833 16.754 1.00 7.75  ? 82  PHE   A CA    1 
ATOM   634  C  C     . PHE   A 1 85  ? 7.464   15.974 15.843 1.00 7.90  ? 82  PHE   A C     1 
ATOM   635  O  O     . PHE   A 1 85  ? 7.378   15.906 14.642 1.00 8.44  ? 82  PHE   A O     1 
ATOM   636  C  CB    . PHE   A 1 85  ? 6.284   14.577 17.643 1.00 8.12  ? 82  PHE   A CB    1 
ATOM   637  C  CG    . PHE   A 1 85  ? 6.598   13.300 16.901 1.00 8.28  ? 82  PHE   A CG    1 
ATOM   638  C  CD1   . PHE   A 1 85  ? 5.582   12.583 16.272 1.00 8.28  ? 82  PHE   A CD1   1 
ATOM   639  C  CD2   . PHE   A 1 85  ? 7.894   12.800 16.838 1.00 8.70  ? 82  PHE   A CD2   1 
ATOM   640  C  CE1   . PHE   A 1 85  ? 5.858   11.402 15.600 1.00 8.24  ? 82  PHE   A CE1   1 
ATOM   641  C  CE2   . PHE   A 1 85  ? 8.158   11.619 16.154 1.00 8.34  ? 82  PHE   A CE2   1 
ATOM   642  C  CZ    . PHE   A 1 85  ? 7.145   10.920 15.522 1.00 9.02  ? 82  PHE   A CZ    1 
ATOM   643  N  N     . ALA   A 1 86  ? 8.614   16.225 16.458 1.00 8.34  ? 83  ALA   A N     1 
ATOM   644  C  CA    . ALA   A 1 86  ? 9.864   16.261 15.711 1.00 8.94  ? 83  ALA   A CA    1 
ATOM   645  C  C     . ALA   A 1 86  ? 10.653  15.019 16.037 1.00 9.05  ? 83  ALA   A C     1 
ATOM   646  O  O     . ALA   A 1 86  ? 10.765  14.622 17.205 1.00 9.02  ? 83  ALA   A O     1 
ATOM   647  C  CB    . ALA   A 1 86  ? 10.642  17.510 16.041 1.00 9.77  ? 83  ALA   A CB    1 
ATOM   648  N  N     . ILE   A 1 87  ? 11.271  14.407 15.005 1.00 9.14  ? 84  ILE   A N     1 
ATOM   649  C  CA    . ILE   A 1 87  ? 11.943  13.136 15.210 1.00 9.95  ? 84  ILE   A CA    1 
ATOM   650  C  C     . ILE   A 1 87  ? 13.227  13.226 16.062 1.00 10.36 ? 84  ILE   A C     1 
ATOM   651  O  O     . ILE   A 1 87  ? 13.769  12.211 16.472 1.00 10.61 ? 84  ILE   A O     1 
ATOM   652  C  CB    . ILE   A 1 87  ? 12.263  12.423 13.876 1.00 10.11 ? 84  ILE   A CB    1 
ATOM   653  C  CG1   . ILE   A 1 87  ? 13.289  13.200 13.014 1.00 11.00 ? 84  ILE   A CG1   1 
ATOM   654  C  CG2   . ILE   A 1 87  ? 10.993  12.128 13.096 1.00 10.80 ? 84  ILE   A CG2   1 
ATOM   655  C  CD1   . ILE   A 1 87  ? 14.129  12.330 12.110 1.00 13.76 ? 84  ILE   A CD1   1 
ATOM   656  N  N     . ASN   A 1 88  ? 13.653  14.457 16.319 1.00 10.33 ? 85  ASN   A N     1 
ATOM   657  C  CA    . ASN   A 1 88  ? 14.839  14.715 17.177 1.00 11.64 ? 85  ASN   A CA    1 
ATOM   658  C  C     . ASN   A 1 88  ? 14.402  15.291 18.527 1.00 11.76 ? 85  ASN   A C     1 
ATOM   659  O  O     . ASN   A 1 88  ? 15.271  15.792 19.224 1.00 13.73 ? 85  ASN   A O     1 
ATOM   660  C  CB    . ASN   A 1 88  ? 15.817  15.679 16.496 1.00 11.58 ? 85  ASN   A CB    1 
ATOM   661  C  CG    . ASN   A 1 88  ? 15.273  17.080 16.352 1.00 12.04 ? 85  ASN   A CG    1 
ATOM   662  O  OD1   . ASN   A 1 88  ? 14.081  17.278 16.180 1.00 12.18 ? 85  ASN   A OD1   1 
ATOM   663  N  ND2   . ASN   A 1 88  ? 16.155  18.074 16.432 1.00 14.14 ? 85  ASN   A ND2   1 
ATOM   664  N  N     . ASN   A 1 89  ? 13.114  15.198 18.895 1.00 11.33 ? 86  ASN   A N     1 
ATOM   665  C  CA    . ASN   A 1 89  ? 12.608  15.776 20.185 1.00 12.19 ? 86  ASN   A CA    1 
ATOM   666  C  C     . ASN   A 1 89  ? 11.713  14.740 20.864 1.00 10.85 ? 86  ASN   A C     1 
ATOM   667  O  O     . ASN   A 1 89  ? 10.555  14.676 20.573 1.00 10.47 ? 86  ASN   A O     1 
ATOM   668  C  CB    . ASN   A 1 89  ? 11.944  17.140 19.945 1.00 13.40 ? 86  ASN   A CB    1 
ATOM   669  C  CG    . ASN   A 1 89  ? 11.296  17.799 21.160 1.00 17.33 ? 86  ASN   A CG    1 
ATOM   670  O  OD1   . ASN   A 1 89  ? 11.132  17.187 22.169 1.00 14.30 ? 86  ASN   A OD1   1 
ATOM   671  N  ND2   . ASN   A 1 89  ? 10.807  19.015 20.987 1.00 18.82 ? 86  ASN   A ND2   1 
ATOM   672  N  N     . THR   A 1 90  ? 12.266  13.938 21.762 1.00 12.11 ? 87  THR   A N     1 
ATOM   673  C  CA    . THR   A 1 90  ? 11.471  12.881 22.421 1.00 12.99 ? 87  THR   A CA    1 
ATOM   674  C  C     . THR   A 1 90  ? 10.300  13.486 23.210 1.00 11.58 ? 87  THR   A C     1 
ATOM   675  O  O     . THR   A 1 90  ? 9.225   12.922 23.218 1.00 12.32 ? 87  THR   A O     1 
ATOM   676  C  CB    . THR   A 1 90  ? 12.424  12.010 23.244 1.00 16.36 ? 87  THR   A CB    1 
ATOM   677  O  OG1   . THR   A 1 90  ? 13.306  11.365 22.324 1.00 19.82 ? 87  THR   A OG1   1 
ATOM   678  C  CG2   . THR   A 1 90  ? 11.699  10.985 24.073 1.00 19.44 ? 87  THR   A CG2   1 
ATOM   679  N  N     . LYS   A 1 91  ? 10.520  14.593 23.881 1.00 12.23 ? 88  LYS   A N     1 
ATOM   680  C  CA    . LYS   A 1 91  ? 9.447   15.235 24.645 1.00 12.75 ? 88  LYS   A CA    1 
ATOM   681  C  C     . LYS   A 1 91  ? 8.267   15.553 23.729 1.00 11.58 ? 88  LYS   A C     1 
ATOM   682  O  O     . LYS   A 1 91  ? 7.103   15.340 24.108 1.00 12.72 ? 88  LYS   A O     1 
ATOM   683  C  CB    . LYS   A 1 91  ? 9.959   16.497 25.359 1.00 13.75 ? 88  LYS   A CB    1 
ATOM   684  C  CG    . LYS   A 1 91  ? 8.935   17.301 26.163 1.00 19.60 ? 88  LYS   A CG    1 
ATOM   685  C  CD    . LYS   A 1 91  ? 8.210   16.537 27.261 1.00 27.61 ? 88  LYS   A CD    1 
ATOM   686  C  CE    . LYS   A 1 91  ? 7.447   17.476 28.194 1.00 29.12 ? 88  LYS   A CE    1 
ATOM   687  N  NZ    . LYS   A 1 91  ? 6.570   18.454 27.478 1.00 33.33 ? 88  LYS   A NZ    1 
ATOM   688  N  N     . SER   A 1 92  ? 8.524   16.032 22.510 1.00 10.33 ? 89  SER   A N     1 
ATOM   689  C  CA    . SER   A 1 92  ? 7.412   16.346 21.603 1.00 9.86  ? 89  SER   A CA    1 
ATOM   690  C  C     . SER   A 1 92  ? 6.627   15.097 21.217 1.00 9.54  ? 89  SER   A C     1 
ATOM   691  O  O     . SER   A 1 92  ? 5.419   15.165 21.002 1.00 10.31 ? 89  SER   A O     1 
ATOM   692  C  CB    . SER   A 1 92  ? 7.895   17.107 20.360 1.00 10.39 ? 89  SER   A CB    1 
ATOM   693  O  OG    . SER   A 1 92  ? 8.613   16.278 19.442 1.00 9.72  ? 89  SER   A OG    1 
ATOM   694  N  N     . PHE   A 1 93  ? 7.322   13.966 21.130 1.00 9.59  ? 90  PHE   A N     1 
ATOM   695  C  CA    . PHE   A 1 93  ? 6.642   12.669 20.878 1.00 10.49 ? 90  PHE   A CA    1 
ATOM   696  C  C     . PHE   A 1 93  ? 5.795   12.256 22.096 1.00 11.03 ? 90  PHE   A C     1 
ATOM   697  O  O     . PHE   A 1 93  ? 4.692   11.814 21.925 1.00 10.50 ? 90  PHE   A O     1 
ATOM   698  C  CB    . PHE   A 1 93  ? 7.690   11.614 20.534 1.00 9.74  ? 90  PHE   A CB    1 
ATOM   699  C  CG    . PHE   A 1 93  ? 7.129   10.249 20.249 1.00 10.22 ? 90  PHE   A CG    1 
ATOM   700  C  CD1   . PHE   A 1 93  ? 6.369   10.000 19.117 1.00 9.12  ? 90  PHE   A CD1   1 
ATOM   701  C  CD2   . PHE   A 1 93  ? 7.419   9.193  21.099 1.00 12.50 ? 90  PHE   A CD2   1 
ATOM   702  C  CE1   . PHE   A 1 93  ? 5.923   8.727  18.823 1.00 10.91 ? 90  PHE   A CE1   1 
ATOM   703  C  CE2   . PHE   A 1 93  ? 6.969   7.911  20.818 1.00 14.77 ? 90  PHE   A CE2   1 
ATOM   704  C  CZ    . PHE   A 1 93  ? 6.225   7.692  19.675 1.00 11.63 ? 90  PHE   A CZ    1 
ATOM   705  N  N     . GLU   A 1 94  ? 6.327   12.432 23.300 1.00 12.62 ? 91  GLU   A N     1 
ATOM   706  C  CA    . GLU   A 1 94  ? 5.546   12.195 24.563 1.00 14.84 ? 91  GLU   A CA    1 
ATOM   707  C  C     . GLU   A 1 94  ? 4.351   13.139 24.649 1.00 14.61 ? 91  GLU   A C     1 
ATOM   708  O  O     . GLU   A 1 94  ? 3.388   12.750 25.298 1.00 19.88 ? 91  GLU   A O     1 
ATOM   709  C  CB    . GLU   A 1 94  ? 6.447   12.345 25.782 1.00 17.00 ? 91  GLU   A CB    1 
ATOM   710  C  CG    . GLU   A 1 94  ? 7.443   11.248 25.793 1.00 17.94 ? 91  GLU   A CG    1 
ATOM   711  C  CD    . GLU   A 1 94  ? 8.294   11.174 27.053 1.00 20.42 ? 91  GLU   A CD    1 
ATOM   712  O  OE1   . GLU   A 1 94  ? 7.931   11.780 28.063 1.00 28.21 ? 91  GLU   A OE1   1 
ATOM   713  O  OE2   . GLU   A 1 94  ? 9.317   10.565 26.966 1.00 19.48 ? 91  GLU   A OE2   1 
ATOM   714  N  N     . ASP   A 1 95  ? 4.407   14.352 24.119 1.00 13.76 ? 92  ASP   A N     1 
ATOM   715  C  CA    . ASP   A 1 95  ? 3.233   15.247 24.209 1.00 15.92 ? 92  ASP   A CA    1 
ATOM   716  C  C     . ASP   A 1 95  ? 2.047   14.720 23.383 1.00 14.32 ? 92  ASP   A C     1 
ATOM   717  O  O     . ASP   A 1 95  ? 0.937   15.126 23.644 1.00 15.45 ? 92  ASP   A O     1 
ATOM   718  C  CB    . ASP   A 1 95  ? 3.568   16.631 23.665 1.00 18.46 ? 92  ASP   A CB    1 
ATOM   719  C  CG    . ASP   A 1 95  ? 4.471   17.473 24.551 1.00 20.28 ? 92  ASP   A CG    1 
ATOM   720  O  OD1   . ASP   A 1 95  ? 4.687   17.096 25.755 1.00 21.32 ? 92  ASP   A OD1   1 
ATOM   721  O  OD2   . ASP   A 1 95  ? 4.980   18.477 24.016 1.00 29.37 ? 92  ASP   A OD2   1 
ATOM   722  N  N     . ILE   A 1 96  ? 2.284   13.857 22.391 1.00 12.61 ? 93  ILE   A N     1 
ATOM   723  C  CA    . ILE   A 1 96  ? 1.231   13.453 21.465 1.00 11.70 ? 93  ILE   A CA    1 
ATOM   724  C  C     . ILE   A 1 96  ? 0.014   12.889 22.181 1.00 11.30 ? 93  ILE   A C     1 
ATOM   725  O  O     . ILE   A 1 96  ? -1.114  13.249 21.871 1.00 11.82 ? 93  ILE   A O     1 
ATOM   726  C  CB    . ILE   A 1 96  ? 1.751   12.470 20.384 1.00 11.19 ? 93  ILE   A CB    1 
ATOM   727  C  CG1   . ILE   A 1 96  ? 2.811   13.158 19.477 1.00 10.29 ? 93  ILE   A CG1   1 
ATOM   728  C  CG2   . ILE   A 1 96  ? 0.590   11.852 19.593 1.00 11.42 ? 93  ILE   A CG2   1 
ATOM   729  C  CD1   . ILE   A 1 96  ? 2.283   14.271 18.609 1.00 12.13 ? 93  ILE   A CD1   1 
ATOM   730  N  N     . HIS   A 1 97  ? 0.216   11.988 23.128 1.00 11.44 ? 94  HIS   A N     1 
ATOM   731  C  CA    . HIS   A 1 97  ? -0.951  11.371 23.764 1.00 12.68 ? 94  HIS   A CA    1 
ATOM   732  C  C     . HIS   A 1 97  ? -1.837  12.404 24.472 1.00 12.08 ? 94  HIS   A C     1 
ATOM   733  O  O     . HIS   A 1 97  ? -3.054  12.242 24.532 1.00 13.64 ? 94  HIS   A O     1 
ATOM   734  C  CB    . HIS   A 1 97  ? -0.543  10.238 24.709 1.00 14.30 ? 94  HIS   A CB    1 
ATOM   735  C  CG    . HIS   A 1 97  ? -0.027  10.697 26.021 1.00 17.46 ? 94  HIS   A CG    1 
ATOM   736  N  ND1   . HIS   A 1 97  ? 1.268   11.134 26.207 1.00 19.74 ? 94  HIS   A ND1   1 
ATOM   737  C  CD2   . HIS   A 1 97  ? -0.638  10.806 27.222 1.00 20.26 ? 94  HIS   A CD2   1 
ATOM   738  C  CE1   . HIS   A 1 97  ? 1.434   11.484 27.470 1.00 20.65 ? 94  HIS   A CE1   1 
ATOM   739  N  NE2   . HIS   A 1 97  ? 0.291   11.298 28.105 1.00 23.37 ? 94  HIS   A NE2   1 
ATOM   740  N  N     . HIS   A 1 98  ? -1.229  13.463 24.996 1.00 11.65 ? 95  HIS   A N     1 
ATOM   741  C  CA    . HIS   A 1 98  ? -2.041  14.508 25.676 1.00 12.61 ? 95  HIS   A CA    1 
ATOM   742  C  C     . HIS   A 1 98  ? -2.943  15.209 24.661 1.00 12.31 ? 95  HIS   A C     1 
ATOM   743  O  O     . HIS   A 1 98  ? -4.072  15.518 24.995 1.00 13.06 ? 95  HIS   A O     1 
ATOM   744  C  CB    . HIS   A 1 98  ? -1.139  15.548 26.342 1.00 15.56 ? 95  HIS   A CB    1 
ATOM   745  C  CG    . HIS   A 1 98  ? -0.379  15.031 27.511 1.00 19.06 ? 95  HIS   A CG    1 
ATOM   746  N  ND1   . HIS   A 1 98  ? -0.984  14.598 28.677 1.00 23.05 ? 95  HIS   A ND1   1 
ATOM   747  C  CD2   . HIS   A 1 98  ? 0.941   14.871 27.702 1.00 23.23 ? 95  HIS   A CD2   1 
ATOM   748  C  CE1   . HIS   A 1 98  ? -0.053  14.203 29.520 1.00 24.11 ? 95  HIS   A CE1   1 
ATOM   749  N  NE2   . HIS   A 1 98  ? 1.113   14.390 28.956 1.00 24.19 ? 95  HIS   A NE2   1 
ATOM   750  N  N     . TYR   A 1 99  ? -2.410  15.519 23.477 1.00 12.49 ? 96  TYR   A N     1 
ATOM   751  C  CA    . TYR   A 1 99  ? -3.258  16.145 22.434 1.00 13.59 ? 96  TYR   A CA    1 
ATOM   752  C  C     . TYR   A 1 99  ? -4.396  15.216 22.045 1.00 13.32 ? 96  TYR   A C     1 
ATOM   753  O  O     . TYR   A 1 99  ? -5.512  15.669 21.898 1.00 14.17 ? 96  TYR   A O     1 
ATOM   754  C  CB    . TYR   A 1 99  ? -2.453  16.259 21.139 1.00 15.05 ? 96  TYR   A CB    1 
ATOM   755  C  CG    . TYR   A 1 99  ? -1.487  17.384 21.256 1.00 15.51 ? 96  TYR   A CG    1 
ATOM   756  C  CD1   . TYR   A 1 99  ? -1.979  18.665 21.254 1.00 18.74 ? 96  TYR   A CD1   1 
ATOM   757  C  CD2   . TYR   A 1 99  ? -0.119  17.194 21.237 1.00 16.29 ? 96  TYR   A CD2   1 
ATOM   758  C  CE1   . TYR   A 1 99  ? -1.136  19.742 21.322 1.00 19.07 ? 96  TYR   A CE1   1 
ATOM   759  C  CE2   . TYR   A 1 99  ? 0.746   18.259 21.323 1.00 17.50 ? 96  TYR   A CE2   1 
ATOM   760  C  CZ    . TYR   A 1 99  ? 0.220   19.539 21.357 1.00 19.01 ? 96  TYR   A CZ    1 
ATOM   761  O  OH    . TYR   A 1 99  ? 1.039   20.610 21.400 1.00 18.88 ? 96  TYR   A OH    1 
ATOM   762  N  N     . ARG   A 1 100 ? -4.087  13.953 21.810 1.00 14.66 ? 97  ARG   A N     1 
ATOM   763  C  CA    . ARG   A 1 100 ? -5.158  13.023 21.423 1.00 15.82 ? 97  ARG   A CA    1 
ATOM   764  C  C     . ARG   A 1 100 ? -6.228  12.978 22.528 1.00 14.12 ? 97  ARG   A C     1 
ATOM   765  O  O     . ARG   A 1 100 ? -7.392  12.974 22.207 1.00 15.87 ? 97  ARG   A O     1 
ATOM   766  C  CB    . ARG   A 1 100 ? -4.582  11.646 21.114 1.00 16.81 ? 97  ARG   A CB    1 
ATOM   767  C  CG    . ARG   A 1 100 ? -5.687  10.706 20.681 1.00 17.16 ? 97  ARG   A CG    1 
ATOM   768  C  CD    . ARG   A 1 100 ? -5.119  9.530  19.944 1.00 20.36 ? 97  ARG   A CD    1 
ATOM   769  N  NE    . ARG   A 1 100 ? -6.133  8.518  19.827 1.00 21.82 ? 97  ARG   A NE    1 
ATOM   770  C  CZ    . ARG   A 1 100 ? -6.951  8.378  18.807 1.00 23.77 ? 97  ARG   A CZ    1 
ATOM   771  N  NH1   . ARG   A 1 100 ? -6.864  9.156  17.748 1.00 24.44 ? 97  ARG   A NH1   1 
ATOM   772  N  NH2   . ARG   A 1 100 ? -7.830  7.402  18.819 1.00 29.53 ? 97  ARG   A NH2   1 
ATOM   773  N  N     . GLU   A 1 101 ? -5.811  12.893 23.782 1.00 14.42 ? 98  GLU   A N     1 
ATOM   774  C  CA    . GLU   A 1 101 ? -6.750  12.896 24.897 1.00 15.93 ? 98  GLU   A CA    1 
ATOM   775  C  C     . GLU   A 1 101 ? -7.586  14.157 24.952 1.00 14.33 ? 98  GLU   A C     1 
ATOM   776  O  O     . GLU   A 1 101 ? -8.810  14.078 25.182 1.00 16.03 ? 98  GLU   A O     1 
ATOM   777  C  CB    . GLU   A 1 101 ? -6.015  12.710 26.224 1.00 17.10 ? 98  GLU   A CB    1 
ATOM   778  C  CG    . GLU   A 1 101 ? -5.502  11.301 26.448 1.00 22.85 ? 98  GLU   A CG    1 
ATOM   779  C  CD    . GLU   A 1 101 ? -6.613  10.272 26.468 1.00 32.23 ? 98  GLU   A CD    1 
ATOM   780  O  OE1   . GLU   A 1 101 ? -7.595  10.476 27.213 1.00 37.31 ? 98  GLU   A OE1   1 
ATOM   781  O  OE2   . GLU   A 1 101 ? -6.515  9.265  25.729 1.00 45.20 ? 98  GLU   A OE2   1 
ATOM   782  N  N     . GLN   A 1 102 ? -6.984  15.325 24.740 1.00 13.97 ? 99  GLN   A N     1 
ATOM   783  C  CA    . GLN   A 1 102 ? -7.733  16.598 24.768 1.00 15.13 ? 99  GLN   A CA    1 
ATOM   784  C  C     . GLN   A 1 102 ? -8.765  16.600 23.681 1.00 13.98 ? 99  GLN   A C     1 
ATOM   785  O  O     . GLN   A 1 102 ? -9.904  16.946 23.913 1.00 13.85 ? 99  GLN   A O     1 
ATOM   786  C  CB    . GLN   A 1 102 ? -6.818  17.800 24.554 1.00 16.18 ? 99  GLN   A CB    1 
ATOM   787  C  CG    . GLN   A 1 102 ? -5.876  18.111 25.697 1.00 17.69 ? 99  GLN   A CG    1 
ATOM   788  C  CD    . GLN   A 1 102 ? -4.786  19.128 25.359 1.00 19.71 ? 99  GLN   A CD    1 
ATOM   789  O  OE1   . GLN   A 1 102 ? -4.558  19.493 24.199 1.00 24.52 ? 99  GLN   A OE1   1 
ATOM   790  N  NE2   . GLN   A 1 102 ? -4.073  19.568 26.395 1.00 29.24 ? 99  GLN   A NE2   1 
ATOM   791  N  N     . ILE   A 1 103 ? -8.368  16.204 22.470 1.00 12.24 ? 100 ILE   A N     1 
ATOM   792  C  CA    . ILE   A 1 103 ? -9.282  16.246 21.334 1.00 12.37 ? 100 ILE   A CA    1 
ATOM   793  C  C     . ILE   A 1 103 ? -10.446 15.261 21.522 1.00 12.98 ? 100 ILE   A C     1 
ATOM   794  O  O     . ILE   A 1 103 ? -11.604 15.622 21.284 1.00 13.94 ? 100 ILE   A O     1 
ATOM   795  C  CB    . ILE   A 1 103 ? -8.540  15.965 20.017 1.00 11.55 ? 100 ILE   A CB    1 
ATOM   796  C  CG1   . ILE   A 1 103 ? -7.461  17.020 19.731 1.00 11.88 ? 100 ILE   A CG1   1 
ATOM   797  C  CG2   . ILE   A 1 103 ? -9.528  15.957 18.869 1.00 12.97 ? 100 ILE   A CG2   1 
ATOM   798  C  CD1   . ILE   A 1 103 ? -6.363  16.596 18.774 1.00 12.60 ? 100 ILE   A CD1   1 
ATOM   799  N  N     . LYS   A 1 104 ? -10.175 14.038 21.962 1.00 13.40 ? 101 LYS   A N     1 
ATOM   800  C  CA    . LYS   A 1 104 ? -11.224 13.065 22.209 1.00 15.21 ? 101 LYS   A CA    1 
ATOM   801  C  C     . LYS   A 1 104 ? -12.203 13.547 23.264 1.00 14.41 ? 101 LYS   A C     1 
ATOM   802  O  O     . LYS   A 1 104 ? -13.406 13.332 23.139 1.00 15.34 ? 101 LYS   A O     1 
ATOM   803  C  CB    . LYS   A 1 104 ? -10.669 11.720 22.648 1.00 16.91 ? 101 LYS   A CB    1 
ATOM   804  C  CG    . LYS   A 1 104 ? -9.978  10.929 21.553 1.00 20.00 ? 101 LYS   A CG    1 
ATOM   805  C  CD    . LYS   A 1 104 ? -9.736  9.478  21.938 1.00 28.54 ? 101 LYS   A CD    1 
ATOM   806  C  CE    . LYS   A 1 104 ? -8.748  9.319  23.086 1.00 32.38 ? 101 LYS   A CE    1 
ATOM   807  N  NZ    . LYS   A 1 104 ? -8.882  7.993  23.750 1.00 37.99 ? 101 LYS   A NZ    1 
ATOM   808  N  N     . ARG   A 1 105 ? -11.705 14.206 24.307 1.00 13.79 ? 102 ARG   A N     1 
ATOM   809  C  CA    . ARG   A 1 105 ? -12.574 14.752 25.351 1.00 16.06 ? 102 ARG   A CA    1 
ATOM   810  C  C     . ARG   A 1 105 ? -13.485 15.840 24.794 1.00 15.23 ? 102 ARG   A C     1 
ATOM   811  O  O     . ARG   A 1 105 ? -14.684 15.829 25.060 1.00 16.58 ? 102 ARG   A O     1 
ATOM   812  C  CB    . ARG   A 1 105 ? -11.765 15.291 26.534 1.00 19.46 ? 102 ARG   A CB    1 
ATOM   813  C  CG    . ARG   A 1 105 ? -12.650 15.799 27.665 1.00 23.96 ? 102 ARG   A CG    1 
ATOM   814  C  CD    . ARG   A 1 105 ? -11.884 16.309 28.874 1.00 27.81 ? 102 ARG   A CD    1 
ATOM   815  N  NE    . ARG   A 1 105 ? -10.711 17.146 28.559 1.00 35.01 ? 102 ARG   A NE    1 
ATOM   816  C  CZ    . ARG   A 1 105 ? -9.428  16.820 28.765 1.00 39.61 ? 102 ARG   A CZ    1 
ATOM   817  N  NH1   . ARG   A 1 105 ? -9.071  15.640 29.284 1.00 45.72 ? 102 ARG   A NH1   1 
ATOM   818  N  NH2   . ARG   A 1 105 ? -8.466  17.688 28.437 1.00 38.54 ? 102 ARG   A NH2   1 
ATOM   819  N  N     . VAL   A 1 106 ? -12.948 16.756 24.010 1.00 14.74 ? 103 VAL   A N     1 
ATOM   820  C  CA    . VAL   A 1 106 ? -13.749 17.830 23.408 1.00 15.85 ? 103 VAL   A CA    1 
ATOM   821  C  C     . VAL   A 1 106 ? -14.798 17.259 22.446 1.00 16.21 ? 103 VAL   A C     1 
ATOM   822  O  O     . VAL   A 1 106 ? -15.947 17.741 22.409 1.00 17.30 ? 103 VAL   A O     1 
ATOM   823  C  CB    . VAL   A 1 106 ? -12.862 18.863 22.704 1.00 17.11 ? 103 VAL   A CB    1 
ATOM   824  C  CG1   . VAL   A 1 106 ? -13.691 19.871 21.935 1.00 19.54 ? 103 VAL   A CG1   1 
ATOM   825  C  CG2   . VAL   A 1 106 ? -11.998 19.571 23.730 1.00 16.19 ? 103 VAL   A CG2   1 
ATOM   826  N  N     . LYS   A 1 107 ? -14.417 16.249 21.668 1.00 14.82 ? 104 LYS   A N     1 
ATOM   827  C  CA    . LYS   A 1 107 ? -15.335 15.636 20.703 1.00 15.95 ? 104 LYS   A CA    1 
ATOM   828  C  C     . LYS   A 1 107 ? -16.318 14.695 21.354 1.00 17.10 ? 104 LYS   A C     1 
ATOM   829  O  O     . LYS   A 1 107 ? -17.356 14.371 20.756 1.00 20.01 ? 104 LYS   A O     1 
ATOM   830  C  CB    . LYS   A 1 107 ? -14.559 14.825 19.663 1.00 16.07 ? 104 LYS   A CB    1 
ATOM   831  C  CG    . LYS   A 1 107 ? -13.713 15.643 18.731 1.00 16.53 ? 104 LYS   A CG    1 
ATOM   832  C  CD    . LYS   A 1 107 ? -14.490 16.686 17.988 1.00 14.65 ? 104 LYS   A CD    1 
ATOM   833  C  CE    . LYS   A 1 107 ? -13.679 17.198 16.819 1.00 14.53 ? 104 LYS   A CE    1 
ATOM   834  N  NZ    . LYS   A 1 107 ? -14.377 18.346 16.179 1.00 15.95 ? 104 LYS   A NZ    1 
ATOM   835  N  N     . ASP   A 1 108 ? -15.980 14.217 22.550 1.00 17.89 ? 105 ASP   A N     1 
ATOM   836  C  CA    . ASP   A 1 108 ? -16.815 13.203 23.249 1.00 18.86 ? 105 ASP   A CA    1 
ATOM   837  C  C     . ASP   A 1 108 ? -16.945 12.017 22.292 1.00 16.71 ? 105 ASP   A C     1 
ATOM   838  O  O     . ASP   A 1 108 ? -18.033 11.458 22.195 1.00 21.16 ? 105 ASP   A O     1 
ATOM   839  C  CB    . ASP   A 1 108 ? -18.184 13.754 23.710 1.00 20.97 ? 105 ASP   A CB    1 
ATOM   840  C  CG    . ASP   A 1 108 ? -19.041 12.726 24.424 1.00 22.40 ? 105 ASP   A CG    1 
ATOM   841  O  OD1   . ASP   A 1 108 ? -18.459 12.058 25.255 1.00 27.35 ? 105 ASP   A OD1   1 
ATOM   842  O  OD2   . ASP   A 1 108 ? -20.276 12.640 24.146 1.00 28.97 ? 105 ASP   A OD2   1 
ATOM   843  N  N     . SER   A 1 109 ? -15.843 11.678 21.606 1.00 19.09 ? 106 SER   A N     1 
ATOM   844  C  CA    . SER   A 1 109 ? -15.864 10.628 20.557 1.00 17.92 ? 106 SER   A CA    1 
ATOM   845  C  C     . SER   A 1 109 ? -14.511 9.927  20.432 1.00 18.35 ? 106 SER   A C     1 
ATOM   846  O  O     . SER   A 1 109 ? -13.491 10.570 20.615 1.00 22.25 ? 106 SER   A O     1 
ATOM   847  C  CB    . SER   A 1 109 ? -16.191 11.270 19.228 1.00 20.41 ? 106 SER   A CB    1 
ATOM   848  O  OG    . SER   A 1 109 ? -16.315 10.316 18.186 1.00 22.63 ? 106 SER   A OG    1 
ATOM   849  N  N     . GLU   A 1 110 ? -14.570 8.665  20.034 1.00 22.88 ? 107 GLU   A N     1 
ATOM   850  C  CA    . GLU   A 1 110 ? -13.391 7.865  19.632 1.00 26.78 ? 107 GLU   A CA    1 
ATOM   851  C  C     . GLU   A 1 110 ? -13.125 8.110  18.135 1.00 22.75 ? 107 GLU   A C     1 
ATOM   852  O  O     . GLU   A 1 110 ? -12.031 7.784  17.686 1.00 26.49 ? 107 GLU   A O     1 
ATOM   853  C  CB    . GLU   A 1 110 ? -13.711 6.385  19.869 1.00 30.58 ? 107 GLU   A CB    1 
ATOM   854  C  CG    . GLU   A 1 110 ? -13.690 6.014  21.335 1.00 34.10 ? 107 GLU   A CG    1 
ATOM   855  C  CD    . GLU   A 1 110 ? -12.284 6.099  21.894 1.00 40.57 ? 107 GLU   A CD    1 
ATOM   856  O  OE1   . GLU   A 1 110 ? -11.367 6.107  21.120 1.00 52.59 ? 107 GLU   A OE1   1 
ATOM   857  O  OE2   . GLU   A 1 110 ? -12.141 6.167  23.089 1.00 52.51 ? 107 GLU   A OE2   1 
ATOM   858  N  N     . ASP   A 1 111 ? -14.106 8.615  17.387 1.00 21.90 ? 108 ASP   A N     1 
ATOM   859  C  CA    . ASP   A 1 111 ? -13.973 8.780  15.940 1.00 21.10 ? 108 ASP   A CA    1 
ATOM   860  C  C     . ASP   A 1 111 ? -13.361 10.128 15.694 1.00 19.56 ? 108 ASP   A C     1 
ATOM   861  O  O     . ASP   A 1 111 ? -14.088 11.087 15.458 1.00 28.84 ? 108 ASP   A O     1 
ATOM   862  C  CB    . ASP   A 1 111 ? -15.338 8.713  15.218 1.00 19.45 ? 108 ASP   A CB    1 
ATOM   863  C  CG    . ASP   A 1 111 ? -15.951 7.330  15.221 1.00 21.17 ? 108 ASP   A CG    1 
ATOM   864  O  OD1   . ASP   A 1 111 ? -15.323 6.400  15.753 1.00 25.29 ? 108 ASP   A OD1   1 
ATOM   865  O  OD2   . ASP   A 1 111 ? -17.078 7.190  14.686 1.00 23.54 ? 108 ASP   A OD2   1 
ATOM   866  N  N     . VAL   A 1 112 ? -12.031 10.239 15.773 1.00 16.14 ? 109 VAL   A N     1 
ATOM   867  C  CA    . VAL   A 1 112 ? -11.416 11.522 15.480 1.00 14.47 ? 109 VAL   A CA    1 
ATOM   868  C  C     . VAL   A 1 112 ? -10.404 11.398 14.348 1.00 12.41 ? 109 VAL   A C     1 
ATOM   869  O  O     . VAL   A 1 112 ? -9.356  10.751 14.517 1.00 13.56 ? 109 VAL   A O     1 
ATOM   870  C  CB    . VAL   A 1 112 ? -10.714 12.149 16.696 1.00 18.99 ? 109 VAL   A CB    1 
ATOM   871  C  CG1   . VAL   A 1 112 ? -10.414 13.613 16.378 1.00 24.77 ? 109 VAL   A CG1   1 
ATOM   872  C  CG2   . VAL   A 1 112 ? -11.577 12.064 17.942 1.00 20.75 ? 109 VAL   A CG2   1 
ATOM   873  N  N     . PRO   A 1 113 ? -10.689 12.011 13.193 1.00 10.89 ? 110 PRO   A N     1 
ATOM   874  C  CA    . PRO   A 1 113 ? -9.689  11.959 12.122 1.00 10.02 ? 110 PRO   A CA    1 
ATOM   875  C  C     . PRO   A 1 113 ? -8.385  12.618 12.539 1.00 9.36  ? 110 PRO   A C     1 
ATOM   876  O  O     . PRO   A 1 113 ? -8.375  13.779 12.957 1.00 9.69  ? 110 PRO   A O     1 
ATOM   877  C  CB    . PRO   A 1 113 ? -10.359 12.742 10.992 1.00 10.45 ? 110 PRO   A CB    1 
ATOM   878  C  CG    . PRO   A 1 113 ? -11.839 12.667 11.280 1.00 11.96 ? 110 PRO   A CG    1 
ATOM   879  C  CD    . PRO   A 1 113 ? -11.902 12.737 12.771 1.00 12.16 ? 110 PRO   A CD    1 
ATOM   880  N  N     A MET   A 1 114 ? -7.306  11.835 12.510 0.50 9.52  ? 111 MET   A N     1 
ATOM   881  N  N     B MET   A 1 114 ? -7.291  11.888 12.366 0.50 9.24  ? 111 MET   A N     1 
ATOM   882  C  CA    A MET   A 1 114 ? -6.005  12.273 12.985 0.50 9.88  ? 111 MET   A CA    1 
ATOM   883  C  CA    B MET   A 1 114 ? -6.028  12.313 12.897 0.50 9.06  ? 111 MET   A CA    1 
ATOM   884  C  C     A MET   A 1 114 ? -4.926  11.603 12.143 0.50 8.64  ? 111 MET   A C     1 
ATOM   885  C  C     B MET   A 1 114 ? -4.916  11.596 12.163 0.50 8.41  ? 111 MET   A C     1 
ATOM   886  O  O     A MET   A 1 114 ? -5.079  10.456 11.715 0.50 9.91  ? 111 MET   A O     1 
ATOM   887  O  O     B MET   A 1 114 ? -5.037  10.417 11.830 0.50 9.36  ? 111 MET   A O     1 
ATOM   888  C  CB    A MET   A 1 114 ? -5.797  11.868 14.451 0.50 11.94 ? 111 MET   A CB    1 
ATOM   889  C  CB    B MET   A 1 114 ? -5.990  11.972 14.377 0.50 9.72  ? 111 MET   A CB    1 
ATOM   890  C  CG    A MET   A 1 114 ? -6.547  12.682 15.488 0.50 13.87 ? 111 MET   A CG    1 
ATOM   891  C  CG    B MET   A 1 114 ? -4.681  12.257 15.065 0.50 10.90 ? 111 MET   A CG    1 
ATOM   892  S  SD    A MET   A 1 114 ? -6.067  12.291 17.191 0.50 16.94 ? 111 MET   A SD    1 
ATOM   893  S  SD    B MET   A 1 114 ? -4.811  11.874 16.824 0.50 13.05 ? 111 MET   A SD    1 
ATOM   894  C  CE    A MET   A 1 114 ? -4.340  11.898 16.930 0.50 16.14 ? 111 MET   A CE    1 
ATOM   895  C  CE    B MET   A 1 114 ? -6.004  13.116 17.325 0.50 12.50 ? 111 MET   A CE    1 
ATOM   896  N  N     . VAL   A 1 115 ? -3.821  12.311 11.922 1.00 8.34  ? 112 VAL   A N     1 
ATOM   897  C  CA    . VAL   A 1 115 ? -2.602  11.731 11.337 1.00 7.94  ? 112 VAL   A CA    1 
ATOM   898  C  C     . VAL   A 1 115 ? -1.433  12.100 12.236 1.00 7.26  ? 112 VAL   A C     1 
ATOM   899  O  O     . VAL   A 1 115 ? -1.336  13.245 12.659 1.00 8.35  ? 112 VAL   A O     1 
ATOM   900  C  CB    . VAL   A 1 115 ? -2.365  12.232 9.908  1.00 8.61  ? 112 VAL   A CB    1 
ATOM   901  C  CG1   . VAL   A 1 115 ? -1.006  11.748 9.389  1.00 9.20  ? 112 VAL   A CG1   1 
ATOM   902  C  CG2   . VAL   A 1 115 ? -3.488  11.792 8.998  1.00 9.64  ? 112 VAL   A CG2   1 
ATOM   903  N  N     . LEU   A 1 116 ? -0.625  11.110 12.581 1.00 7.11  ? 113 LEU   A N     1 
ATOM   904  C  CA    . LEU   A 1 116 ? 0.591   11.333 13.353 1.00 7.84  ? 113 LEU   A CA    1 
ATOM   905  C  C     . LEU   A 1 116 ? 1.710   11.720 12.381 1.00 7.10  ? 113 LEU   A C     1 
ATOM   906  O  O     . LEU   A 1 116 ? 1.981   10.964 11.440 1.00 7.61  ? 113 LEU   A O     1 
ATOM   907  C  CB    . LEU   A 1 116 ? 0.947   10.048 14.111 1.00 8.05  ? 113 LEU   A CB    1 
ATOM   908  C  CG    . LEU   A 1 116 ? 2.179   10.175 15.028 1.00 8.66  ? 113 LEU   A CG    1 
ATOM   909  C  CD1   . LEU   A 1 116 ? 1.971   11.200 16.117 1.00 9.48  ? 113 LEU   A CD1   1 
ATOM   910  C  CD2   . LEU   A 1 116 ? 2.523   8.827  15.630 1.00 9.72  ? 113 LEU   A CD2   1 
ATOM   911  N  N     . VAL   A 1 117 ? 2.338   12.866 12.619 1.00 7.39  ? 114 VAL   A N     1 
ATOM   912  C  CA    . VAL   A 1 117 ? 3.417   13.342 11.740 1.00 7.40  ? 114 VAL   A CA    1 
ATOM   913  C  C     . VAL   A 1 117 ? 4.704   13.466 12.524 1.00 7.01  ? 114 VAL   A C     1 
ATOM   914  O  O     . VAL   A 1 117 ? 4.764   14.210 13.518 1.00 7.54  ? 114 VAL   A O     1 
ATOM   915  C  CB    . VAL   A 1 117 ? 3.056   14.692 11.119 1.00 7.95  ? 114 VAL   A CB    1 
ATOM   916  C  CG1   . VAL   A 1 117 ? 4.229   15.238 10.306 1.00 8.56  ? 114 VAL   A CG1   1 
ATOM   917  C  CG2   . VAL   A 1 117 ? 1.794   14.532 10.284 1.00 10.10 ? 114 VAL   A CG2   1 
ATOM   918  N  N     . GLY   A 1 118 ? 5.731   12.744 12.076 1.00 6.99  ? 115 GLY   A N     1 
ATOM   919  C  CA    . GLY   A 1 118 ? 7.091   12.920 12.596 1.00 7.26  ? 115 GLY   A CA    1 
ATOM   920  C  C     . GLY   A 1 118 ? 7.836   13.830 11.649 1.00 7.67  ? 115 GLY   A C     1 
ATOM   921  O  O     . GLY   A 1 118 ? 8.249   13.395 10.570 1.00 8.36  ? 115 GLY   A O     1 
ATOM   922  N  N     . ASN   A 1 119 ? 7.988   15.099 12.027 1.00 7.70  ? 116 ASN   A N     1 
ATOM   923  C  CA    . ASN   A 1 119 ? 8.597   16.092 11.150 1.00 8.00  ? 116 ASN   A CA    1 
ATOM   924  C  C     . ASN   A 1 119 ? 10.090  16.181 11.425 1.00 8.34  ? 116 ASN   A C     1 
ATOM   925  O  O     . ASN   A 1 119 ? 10.613  15.607 12.393 1.00 9.31  ? 116 ASN   A O     1 
ATOM   926  C  CB    . ASN   A 1 119 ? 7.922   17.443 11.358 1.00 8.49  ? 116 ASN   A CB    1 
ATOM   927  C  CG    . ASN   A 1 119 ? 8.321   18.496 10.346 1.00 8.59  ? 116 ASN   A CG    1 
ATOM   928  O  OD1   . ASN   A 1 119 ? 8.417   18.210 9.141  1.00 9.36  ? 116 ASN   A OD1   1 
ATOM   929  N  ND2   . ASN   A 1 119 ? 8.620   19.690 10.827 1.00 9.41  ? 116 ASN   A ND2   1 
ATOM   930  N  N     . LYS   A 1 120 ? 10.782  16.871 10.524 1.00 8.77  ? 117 LYS   A N     1 
ATOM   931  C  CA    . LYS   A 1 120 ? 12.236  17.065 10.560 1.00 9.63  ? 117 LYS   A CA    1 
ATOM   932  C  C     . LYS   A 1 120 ? 12.971  15.778 10.225 1.00 9.76  ? 117 LYS   A C     1 
ATOM   933  O  O     . LYS   A 1 120 ? 14.098  15.522 10.721 1.00 10.35 ? 117 LYS   A O     1 
ATOM   934  C  CB    . LYS   A 1 120 ? 12.745  17.703 11.859 1.00 10.67 ? 117 LYS   A CB    1 
ATOM   935  C  CG    . LYS   A 1 120 ? 11.918  18.860 12.381 1.00 9.61  ? 117 LYS   A CG    1 
ATOM   936  C  CD    . LYS   A 1 120 ? 12.698  19.687 13.383 1.00 10.62 ? 117 LYS   A CD    1 
ATOM   937  C  CE    . LYS   A 1 120 ? 11.839  20.832 13.934 1.00 11.36 ? 117 LYS   A CE    1 
ATOM   938  N  NZ    . LYS   A 1 120 ? 12.591  21.639 14.951 1.00 11.74 ? 117 LYS   A NZ    1 
ATOM   939  N  N     . SER   A 1 121 ? 12.416  15.049 9.248  1.00 9.64  ? 118 SER   A N     1 
ATOM   940  C  CA    . SER   A 1 121 ? 13.016  13.792 8.835  1.00 11.28 ? 118 SER   A CA    1 
ATOM   941  C  C     . SER   A 1 121 ? 14.388  13.956 8.163  1.00 11.87 ? 118 SER   A C     1 
ATOM   942  O  O     . SER   A 1 121 ? 15.125  12.990 8.045  1.00 13.40 ? 118 SER   A O     1 
ATOM   943  C  CB    . SER   A 1 121 ? 12.095  13.013 7.900  1.00 11.77 ? 118 SER   A CB    1 
ATOM   944  O  OG    . SER   A 1 121 ? 12.021  13.699 6.653  1.00 11.55 ? 118 SER   A OG    1 
ATOM   945  N  N     . ASP   A 1 122 ? 14.675  15.169 7.699  1.00 11.40 ? 119 ASP   A N     1 
ATOM   946  C  CA    . ASP   A 1 122 ? 16.006  15.531 7.149  1.00 12.36 ? 119 ASP   A CA    1 
ATOM   947  C  C     . ASP   A 1 122 ? 17.098  15.609 8.212  1.00 12.72 ? 119 ASP   A C     1 
ATOM   948  O  O     . ASP   A 1 122 ? 18.262  15.666 7.845  1.00 16.41 ? 119 ASP   A O     1 
ATOM   949  C  CB    . ASP   A 1 122 ? 15.912  16.877 6.426  1.00 13.25 ? 119 ASP   A CB    1 
ATOM   950  C  CG    . ASP   A 1 122 ? 15.482  18.009 7.360  1.00 13.42 ? 119 ASP   A CG    1 
ATOM   951  O  OD1   . ASP   A 1 122 ? 14.260  18.064 7.702  1.00 12.96 ? 119 ASP   A OD1   1 
ATOM   952  O  OD2   . ASP   A 1 122 ? 16.345  18.822 7.785  1.00 15.26 ? 119 ASP   A OD2   1 
ATOM   953  N  N     . LEU   A 1 123 ? 16.769  15.615 9.502  1.00 12.85 ? 120 LEU   A N     1 
ATOM   954  C  CA    . LEU   A 1 123 ? 17.805  15.758 10.527 1.00 12.76 ? 120 LEU   A CA    1 
ATOM   955  C  C     . LEU   A 1 123 ? 18.368  14.404 10.835 1.00 12.01 ? 120 LEU   A C     1 
ATOM   956  O  O     . LEU   A 1 123 ? 17.644  13.451 11.089 1.00 14.20 ? 120 LEU   A O     1 
ATOM   957  C  CB    . LEU   A 1 123 ? 17.238  16.380 11.810 1.00 12.56 ? 120 LEU   A CB    1 
ATOM   958  C  CG    . LEU   A 1 123 ? 16.867  17.842 11.701 1.00 14.76 ? 120 LEU   A CG    1 
ATOM   959  C  CD1   . LEU   A 1 123 ? 16.359  18.324 13.041 1.00 14.98 ? 120 LEU   A CD1   1 
ATOM   960  C  CD2   . LEU   A 1 123 ? 18.019  18.722 11.245 1.00 16.22 ? 120 LEU   A CD2   1 
ATOM   961  N  N     . PRO   A 1 124 ? 19.713  14.281 10.816 1.00 12.76 ? 121 PRO   A N     1 
ATOM   962  C  CA    . PRO   A 1 124 ? 20.319  12.948 11.023 1.00 12.24 ? 121 PRO   A CA    1 
ATOM   963  C  C     . PRO   A 1 124 ? 20.310  12.396 12.458 1.00 12.48 ? 121 PRO   A C     1 
ATOM   964  O  O     . PRO   A 1 124 ? 20.357  11.186 12.644 1.00 15.07 ? 121 PRO   A O     1 
ATOM   965  C  CB    . PRO   A 1 124 ? 21.770  13.117 10.503 1.00 14.03 ? 121 PRO   A CB    1 
ATOM   966  C  CG    . PRO   A 1 124 ? 22.045  14.563 10.705 1.00 13.46 ? 121 PRO   A CG    1 
ATOM   967  C  CD    . PRO   A 1 124 ? 20.733  15.258 10.401 1.00 13.69 ? 121 PRO   A CD    1 
ATOM   968  N  N     . SER   A 1 125 ? 20.256  13.266 13.472 1.00 12.51 ? 122 SER   A N     1 
ATOM   969  C  CA    . SER   A 1 125 ? 20.354  12.807 14.854 1.00 13.35 ? 122 SER   A CA    1 
ATOM   970  C  C     . SER   A 1 125 ? 18.954  12.568 15.434 1.00 12.87 ? 122 SER   A C     1 
ATOM   971  O  O     . SER   A 1 125 ? 18.457  13.269 16.321 1.00 14.27 ? 122 SER   A O     1 
ATOM   972  C  CB    . SER   A 1 125 ? 21.160  13.780 15.704 1.00 13.93 ? 122 SER   A CB    1 
ATOM   973  O  OG    . SER   A 1 125 ? 22.541  13.756 15.354 1.00 15.29 ? 122 SER   A OG    1 
ATOM   974  N  N     . ARG   A 1 126 ? 18.392  11.478 14.954 1.00 12.79 ? 123 ARG   A N     1 
ATOM   975  C  CA    . ARG   A 1 126 ? 17.071  11.005 15.389 1.00 12.23 ? 123 ARG   A CA    1 
ATOM   976  C  C     . ARG   A 1 126 ? 17.070  10.593 16.839 1.00 12.65 ? 123 ARG   A C     1 
ATOM   977  O  O     . ARG   A 1 126 ? 18.044  10.026 17.314 1.00 14.72 ? 123 ARG   A O     1 
ATOM   978  C  CB    . ARG   A 1 126 ? 16.721  9.788  14.535 1.00 12.90 ? 123 ARG   A CB    1 
ATOM   979  C  CG    . ARG   A 1 126 ? 15.387  9.104  14.857 1.00 12.10 ? 123 ARG   A CG    1 
ATOM   980  C  CD    . ARG   A 1 126 ? 15.189  7.923  13.933 1.00 12.32 ? 123 ARG   A CD    1 
ATOM   981  N  NE    . ARG   A 1 126 ? 14.895  8.321  12.565 1.00 12.28 ? 123 ARG   A NE    1 
ATOM   982  C  CZ    . ARG   A 1 126 ? 13.682  8.594  12.086 1.00 12.58 ? 123 ARG   A CZ    1 
ATOM   983  N  NH1   . ARG   A 1 126 ? 12.627  8.623  12.895 1.00 12.41 ? 123 ARG   A NH1   1 
ATOM   984  N  NH2   . ARG   A 1 126 ? 13.535  8.914  10.817 1.00 13.31 ? 123 ARG   A NH2   1 
ATOM   985  N  N     . THR   A 1 127 ? 15.981  10.911 17.550 1.00 11.47 ? 124 THR   A N     1 
ATOM   986  C  CA    . THR   A 1 127 ? 15.768  10.403 18.911 1.00 12.32 ? 124 THR   A CA    1 
ATOM   987  C  C     . THR   A 1 127 ? 14.520  9.556  19.058 1.00 12.51 ? 124 THR   A C     1 
ATOM   988  O  O     . THR   A 1 127 ? 14.402  8.843  20.043 1.00 16.09 ? 124 THR   A O     1 
ATOM   989  C  CB    . THR   A 1 127 ? 15.731  11.549 19.946 1.00 14.45 ? 124 THR   A CB    1 
ATOM   990  O  OG1   . THR   A 1 127 ? 14.560  12.329 19.747 1.00 13.75 ? 124 THR   A OG1   1 
ATOM   991  C  CG2   . THR   A 1 127 ? 16.947  12.474 19.839 1.00 17.22 ? 124 THR   A CG2   1 
ATOM   992  N  N     . VAL   A 1 128 ? 13.615  9.593  18.070 1.00 11.61 ? 125 VAL   A N     1 
ATOM   993  C  CA    . VAL   A 1 128 ? 12.371  8.837  18.123 1.00 11.03 ? 125 VAL   A CA    1 
ATOM   994  C  C     . VAL   A 1 128 ? 12.457  7.815  16.992 1.00 11.45 ? 125 VAL   A C     1 
ATOM   995  O  O     . VAL   A 1 128 ? 12.440  8.171  15.806 1.00 10.90 ? 125 VAL   A O     1 
ATOM   996  C  CB    . VAL   A 1 128 ? 11.131  9.744  17.940 1.00 10.91 ? 125 VAL   A CB    1 
ATOM   997  C  CG1   . VAL   A 1 128 ? 9.850   8.909  17.999 1.00 11.10 ? 125 VAL   A CG1   1 
ATOM   998  C  CG2   . VAL   A 1 128 ? 11.054  10.839 18.993 1.00 12.33 ? 125 VAL   A CG2   1 
ATOM   999  N  N     . ASP   A 1 129 ? 12.535  6.549  17.364 1.00 13.29 ? 126 ASP   A N     1 
ATOM   1000 C  CA    . ASP   A 1 129 ? 12.633  5.456  16.417 1.00 14.37 ? 126 ASP   A CA    1 
ATOM   1001 C  C     . ASP   A 1 129 ? 11.363  5.412  15.613 1.00 13.20 ? 126 ASP   A C     1 
ATOM   1002 O  O     . ASP   A 1 129 ? 10.276  5.474  16.165 1.00 12.54 ? 126 ASP   A O     1 
ATOM   1003 C  CB    . ASP   A 1 129 ? 12.846  4.146  17.196 1.00 17.37 ? 126 ASP   A CB    1 
ATOM   1004 C  CG    . ASP   A 1 129 ? 13.260  2.955  16.324 1.00 24.55 ? 126 ASP   A CG    1 
ATOM   1005 O  OD1   . ASP   A 1 129 ? 12.714  2.703  15.228 1.00 27.30 ? 126 ASP   A OD1   1 
ATOM   1006 O  OD2   . ASP   A 1 129 ? 14.132  2.192  16.786 1.00 35.56 ? 126 ASP   A OD2   1 
ATOM   1007 N  N     A THR   A 1 130 ? 11.504  5.312  14.302 0.50 13.92 ? 127 THR   A N     1 
ATOM   1008 N  N     B THR   A 1 130 ? 11.508  5.294  14.307 0.50 13.42 ? 127 THR   A N     1 
ATOM   1009 C  CA    A THR   A 1 130 ? 10.356  5.206  13.415 0.50 14.47 ? 127 THR   A CA    1 
ATOM   1010 C  CA    B THR   A 1 130 ? 10.362  5.271  13.421 0.50 13.89 ? 127 THR   A CA    1 
ATOM   1011 C  C     A THR   A 1 130 ? 9.406   4.116  13.848 0.50 14.80 ? 127 THR   A C     1 
ATOM   1012 C  C     B THR   A 1 130 ? 9.421   4.101  13.762 0.50 14.99 ? 127 THR   A C     1 
ATOM   1013 O  O     A THR   A 1 130 ? 8.194   4.310  13.842 0.50 15.01 ? 127 THR   A O     1 
ATOM   1014 O  O     B THR   A 1 130 ? 8.211   4.242  13.628 0.50 15.57 ? 127 THR   A O     1 
ATOM   1015 C  CB    A THR   A 1 130 ? 10.805  4.897  11.986 0.50 17.00 ? 127 THR   A CB    1 
ATOM   1016 C  CB    B THR   A 1 130 ? 10.836  5.274  11.946 0.50 15.12 ? 127 THR   A CB    1 
ATOM   1017 O  OG1   A THR   A 1 130 ? 11.543  6.014  11.477 0.50 17.38 ? 127 THR   A OG1   1 
ATOM   1018 O  OG1   B THR   A 1 130 ? 9.772   5.673  11.068 0.50 16.53 ? 127 THR   A OG1   1 
ATOM   1019 C  CG2   A THR   A 1 130 ? 9.621   4.632  11.104 0.50 17.43 ? 127 THR   A CG2   1 
ATOM   1020 C  CG2   B THR   A 1 130 ? 11.402  3.921  11.542 0.50 13.96 ? 127 THR   A CG2   1 
ATOM   1021 N  N     . LYS   A 1 131 ? 9.949   2.976  14.258 1.00 15.07 ? 128 LYS   A N     1 
ATOM   1022 C  CA    . LYS   A 1 131 ? 9.122   1.833  14.653 1.00 18.01 ? 128 LYS   A CA    1 
ATOM   1023 C  C     . LYS   A 1 131 ? 8.321   2.075  15.944 1.00 14.57 ? 128 LYS   A C     1 
ATOM   1024 O  O     . LYS   A 1 131 ? 7.214   1.532  16.078 1.00 15.22 ? 128 LYS   A O     1 
ATOM   1025 C  CB    . LYS   A 1 131 ? 9.958   0.554  14.687 1.00 23.10 ? 128 LYS   A CB    1 
ATOM   1026 C  CG    . LYS   A 1 131 ? 10.422  0.167  13.274 1.00 29.58 ? 128 LYS   A CG    1 
ATOM   1027 C  CD    . LYS   A 1 131 ? 10.344  -1.336 13.026 1.00 36.98 ? 128 LYS   A CD    1 
ATOM   1028 C  CE    . LYS   A 1 131 ? 10.603  -1.696 11.569 1.00 40.95 ? 128 LYS   A CE    1 
ATOM   1029 N  NZ    . LYS   A 1 131 ? 12.048  -1.914 11.279 1.00 47.74 ? 128 LYS   A NZ    1 
ATOM   1030 N  N     . GLN   A 1 132 ? 8.839   2.906  16.853 1.00 14.29 ? 129 GLN   A N     1 
ATOM   1031 C  CA    . GLN   A 1 132 ? 8.058   3.300  18.030 1.00 12.96 ? 129 GLN   A CA    1 
ATOM   1032 C  C     . GLN   A 1 132 ? 6.892   4.190  17.632 1.00 11.31 ? 129 GLN   A C     1 
ATOM   1033 O  O     . GLN   A 1 132 ? 5.788   4.038  18.145 1.00 12.08 ? 129 GLN   A O     1 
ATOM   1034 C  CB    . GLN   A 1 132 ? 8.941   3.998  19.060 1.00 17.08 ? 129 GLN   A CB    1 
ATOM   1035 C  CG    . GLN   A 1 132 ? 9.947   3.056  19.709 1.00 20.91 ? 129 GLN   A CG    1 
ATOM   1036 C  CD    . GLN   A 1 132 ? 10.693  3.628  20.903 1.00 28.76 ? 129 GLN   A CD    1 
ATOM   1037 O  OE1   . GLN   A 1 132 ? 10.502  4.770  21.297 1.00 36.07 ? 129 GLN   A OE1   1 
ATOM   1038 N  NE2   . GLN   A 1 132 ? 11.525  2.794  21.516 1.00 35.96 ? 129 GLN   A NE2   1 
ATOM   1039 N  N     . ALA   A 1 133 ? 7.120   5.118  16.708 1.00 10.81 ? 130 ALA   A N     1 
ATOM   1040 C  CA    . ALA   A 1 133 ? 6.044   5.979  16.216 1.00 10.08 ? 130 ALA   A CA    1 
ATOM   1041 C  C     . ALA   A 1 133 ? 5.011   5.170  15.435 1.00 9.70  ? 130 ALA   A C     1 
ATOM   1042 O  O     . ALA   A 1 133 ? 3.806   5.397  15.594 1.00 9.79  ? 130 ALA   A O     1 
ATOM   1043 C  CB    . ALA   A 1 133 ? 6.607   7.118  15.364 1.00 11.36 ? 130 ALA   A CB    1 
ATOM   1044 N  N     . GLN   A 1 134 ? 5.447   4.182  14.643 1.00 9.99  ? 131 GLN   A N     1 
ATOM   1045 C  CA    . GLN   A 1 134 ? 4.501   3.313  13.957 1.00 11.14 ? 131 GLN   A CA    1 
ATOM   1046 C  C     . GLN   A 1 134 ? 3.672   2.518  14.957 1.00 10.94 ? 131 GLN   A C     1 
ATOM   1047 O  O     . GLN   A 1 134 ? 2.450   2.357  14.779 1.00 11.16 ? 131 GLN   A O     1 
ATOM   1048 C  CB    . GLN   A 1 134 ? 5.220   2.334  13.045 1.00 10.61 ? 131 GLN   A CB    1 
ATOM   1049 C  CG    . GLN   A 1 134 ? 5.802   2.955  11.798 1.00 11.60 ? 131 GLN   A CG    1 
ATOM   1050 C  CD    . GLN   A 1 134 ? 6.445   1.924  10.889 1.00 13.76 ? 131 GLN   A CD    1 
ATOM   1051 O  OE1   . GLN   A 1 134 ? 6.908   0.891  11.349 1.00 17.33 ? 131 GLN   A OE1   1 
ATOM   1052 N  NE2   . GLN   A 1 134 ? 6.462   2.205  9.597  1.00 14.45 ? 131 GLN   A NE2   1 
ATOM   1053 N  N     . ASP   A 1 135 ? 4.282   2.042  16.033 1.00 11.01 ? 132 ASP   A N     1 
ATOM   1054 C  CA    . ASP   A 1 135 ? 3.531   1.324  17.062 1.00 11.61 ? 132 ASP   A CA    1 
ATOM   1055 C  C     . ASP   A 1 135 ? 2.493   2.224  17.721 1.00 10.85 ? 132 ASP   A C     1 
ATOM   1056 O  O     . ASP   A 1 135 ? 1.360   1.824  17.930 1.00 12.05 ? 132 ASP   A O     1 
ATOM   1057 C  CB    . ASP   A 1 135 ? 4.474   0.742  18.102 1.00 13.41 ? 132 ASP   A CB    1 
ATOM   1058 C  CG    . ASP   A 1 135 ? 3.756   0.109  19.266 1.00 16.67 ? 132 ASP   A CG    1 
ATOM   1059 O  OD1   . ASP   A 1 135 ? 2.953   -0.812 19.054 1.00 22.00 ? 132 ASP   A OD1   1 
ATOM   1060 O  OD2   . ASP   A 1 135 ? 3.995   0.542  20.404 1.00 23.55 ? 132 ASP   A OD2   1 
ATOM   1061 N  N     . LEU   A 1 136 ? 2.873   3.462  18.025 1.00 11.57 ? 133 LEU   A N     1 
ATOM   1062 C  CA    . LEU   A 1 136 ? 1.939   4.392  18.653 1.00 11.05 ? 133 LEU   A CA    1 
ATOM   1063 C  C     . LEU   A 1 136 ? 0.765   4.663  17.738 1.00 11.07 ? 133 LEU   A C     1 
ATOM   1064 O  O     . LEU   A 1 136 ? -0.396  4.600  18.149 1.00 11.28 ? 133 LEU   A O     1 
ATOM   1065 C  CB    . LEU   A 1 136 ? 2.631   5.706  19.032 1.00 11.56 ? 133 LEU   A CB    1 
ATOM   1066 C  CG    . LEU   A 1 136 ? 1.758   6.732  19.757 1.00 13.02 ? 133 LEU   A CG    1 
ATOM   1067 C  CD1   . LEU   A 1 136 ? 1.507   6.245  21.183 1.00 13.68 ? 133 LEU   A CD1   1 
ATOM   1068 C  CD2   . LEU   A 1 136 ? 2.392   8.114  19.718 1.00 14.15 ? 133 LEU   A CD2   1 
ATOM   1069 N  N     . ALA   A 1 137 ? 1.048   4.948  16.475 1.00 10.07 ? 134 ALA   A N     1 
ATOM   1070 C  CA    . ALA   A 1 137 ? -0.021  5.191  15.512 1.00 9.91  ? 134 ALA   A CA    1 
ATOM   1071 C  C     . ALA   A 1 137 ? -0.954  3.979  15.362 1.00 9.62  ? 134 ALA   A C     1 
ATOM   1072 O  O     . ALA   A 1 137 ? -2.175  4.097  15.316 1.00 11.04 ? 134 ALA   A O     1 
ATOM   1073 C  CB    . ALA   A 1 137 ? 0.575   5.597  14.167 1.00 10.10 ? 134 ALA   A CB    1 
ATOM   1074 N  N     . ARG   A 1 138 ? -0.375  2.788  15.317 1.00 11.67 ? 135 ARG   A N     1 
ATOM   1075 C  CA    . ARG   A 1 138 ? -1.167  1.571  15.271 1.00 12.45 ? 135 ARG   A CA    1 
ATOM   1076 C  C     . ARG   A 1 138 ? -2.078  1.443  16.488 1.00 12.02 ? 135 ARG   A C     1 
ATOM   1077 O  O     . ARG   A 1 138 ? -3.247  1.103  16.352 1.00 14.16 ? 135 ARG   A O     1 
ATOM   1078 C  CB    . ARG   A 1 138 ? -0.244  0.357  15.212 1.00 14.35 ? 135 ARG   A CB    1 
ATOM   1079 C  CG    . ARG   A 1 138 ? -0.916  -0.940 14.884 1.00 19.03 ? 135 ARG   A CG    1 
ATOM   1080 C  CD    . ARG   A 1 138 ? 0.110   -2.013 14.616 1.00 21.60 ? 135 ARG   A CD    1 
ATOM   1081 N  NE    . ARG   A 1 138 ? 1.041   -1.653 13.549 1.00 22.82 ? 135 ARG   A NE    1 
ATOM   1082 C  CZ    . ARG   A 1 138 ? 2.364   -1.427 13.674 1.00 28.16 ? 135 ARG   A CZ    1 
ATOM   1083 N  NH1   . ARG   A 1 138 ? 2.997   -1.493 14.840 1.00 27.41 ? 135 ARG   A NH1   1 
ATOM   1084 N  NH2   . ARG   A 1 138 ? 3.077   -1.112 12.601 1.00 30.97 ? 135 ARG   A NH2   1 
ATOM   1085 N  N     . SER   A 1 139 ? -1.552  1.775  17.660 1.00 11.87 ? 136 SER   A N     1 
ATOM   1086 C  CA    . SER   A 1 139 ? -2.346  1.712  18.888 1.00 13.35 ? 136 SER   A CA    1 
ATOM   1087 C  C     . SER   A 1 139 ? -3.545  2.655  18.864 1.00 13.13 ? 136 SER   A C     1 
ATOM   1088 O  O     . SER   A 1 139 ? -4.579  2.387  19.486 1.00 16.39 ? 136 SER   A O     1 
ATOM   1089 C  CB    . SER   A 1 139 ? -1.475  1.957  20.130 1.00 14.16 ? 136 SER   A CB    1 
ATOM   1090 O  OG    . SER   A 1 139 ? -1.262  3.321  20.394 1.00 17.45 ? 136 SER   A OG    1 
ATOM   1091 N  N     . TYR   A 1 140 ? -3.420  3.756  18.129 1.00 12.79 ? 137 TYR   A N     1 
ATOM   1092 C  CA    . TYR   A 1 140 ? -4.492  4.744  18.000 1.00 13.05 ? 137 TYR   A CA    1 
ATOM   1093 C  C     . TYR   A 1 140 ? -5.378  4.516  16.796 1.00 12.88 ? 137 TYR   A C     1 
ATOM   1094 O  O     . TYR   A 1 140 ? -6.387  5.177  16.646 1.00 15.96 ? 137 TYR   A O     1 
ATOM   1095 C  CB    . TYR   A 1 140 ? -3.900  6.155  17.877 1.00 13.65 ? 137 TYR   A CB    1 
ATOM   1096 C  CG    . TYR   A 1 140 ? -3.169  6.697  19.071 1.00 13.96 ? 137 TYR   A CG    1 
ATOM   1097 C  CD1   . TYR   A 1 140 ? -3.380  6.206  20.355 1.00 15.65 ? 137 TYR   A CD1   1 
ATOM   1098 C  CD2   . TYR   A 1 140 ? -2.283  7.749  18.912 1.00 15.57 ? 137 TYR   A CD2   1 
ATOM   1099 C  CE1   . TYR   A 1 140 ? -2.702  6.739  21.443 1.00 16.90 ? 137 TYR   A CE1   1 
ATOM   1100 C  CE2   . TYR   A 1 140 ? -1.599  8.276  19.989 1.00 17.46 ? 137 TYR   A CE2   1 
ATOM   1101 C  CZ    . TYR   A 1 140 ? -1.820  7.781  21.252 1.00 17.09 ? 137 TYR   A CZ    1 
ATOM   1102 O  OH    . TYR   A 1 140 ? -1.142  8.349  22.302 1.00 21.22 ? 137 TYR   A OH    1 
ATOM   1103 N  N     . GLY   A 1 141 ? -4.976  3.606  15.916 1.00 11.60 ? 138 GLY   A N     1 
ATOM   1104 C  CA    . GLY   A 1 141 ? -5.645  3.375  14.651 1.00 12.51 ? 138 GLY   A CA    1 
ATOM   1105 C  C     . GLY   A 1 141 ? -5.571  4.529  13.679 1.00 11.29 ? 138 GLY   A C     1 
ATOM   1106 O  O     . GLY   A 1 141 ? -6.546  4.767  12.960 1.00 14.00 ? 138 GLY   A O     1 
ATOM   1107 N  N     . ILE   A 1 142 ? -4.413  5.205  13.611 1.00 10.76 ? 139 ILE   A N     1 
ATOM   1108 C  CA    . ILE   A 1 142 ? -4.237  6.369  12.746 1.00 9.77  ? 139 ILE   A CA    1 
ATOM   1109 C  C     . ILE   A 1 142 ? -3.020  6.186  11.853 1.00 9.18  ? 139 ILE   A C     1 
ATOM   1110 O  O     . ILE   A 1 142 ? -2.097  5.449  12.204 1.00 10.21 ? 139 ILE   A O     1 
ATOM   1111 C  CB    . ILE   A 1 142 ? -4.105  7.683  13.556 1.00 10.81 ? 139 ILE   A CB    1 
ATOM   1112 C  CG1   . ILE   A 1 142 ? -2.816  7.719  14.395 1.00 10.87 ? 139 ILE   A CG1   1 
ATOM   1113 C  CG2   . ILE   A 1 142 ? -5.368  7.930  14.396 1.00 12.25 ? 139 ILE   A CG2   1 
ATOM   1114 C  CD1   . ILE   A 1 142 ? -2.647  8.993  15.186 1.00 12.79 ? 139 ILE   A CD1   1 
ATOM   1115 N  N     . PRO   A 1 143 ? -2.995  6.870  10.703 1.00 9.37  ? 140 PRO   A N     1 
ATOM   1116 C  CA    . PRO   A 1 143 ? -1.784  6.839  9.871  1.00 9.18  ? 140 PRO   A CA    1 
ATOM   1117 C  C     . PRO   A 1 143 ? -0.612  7.551  10.534 1.00 8.20  ? 140 PRO   A C     1 
ATOM   1118 O  O     . PRO   A 1 143 ? -0.794  8.479  11.332 1.00 8.95  ? 140 PRO   A O     1 
ATOM   1119 C  CB    . PRO   A 1 143 ? -2.205  7.593  8.599  1.00 10.07 ? 140 PRO   A CB    1 
ATOM   1120 C  CG    . PRO   A 1 143 ? -3.681  7.551  8.595  1.00 10.41 ? 140 PRO   A CG    1 
ATOM   1121 C  CD    . PRO   A 1 143 ? -4.108  7.561  10.038 1.00 9.49  ? 140 PRO   A CD    1 
ATOM   1122 N  N     . PHE   A 1 144 ? 0.584   7.117  10.132 1.00 8.31  ? 141 PHE   A N     1 
ATOM   1123 C  CA    . PHE   A 1 144 ? 1.846   7.769  10.572 1.00 7.82  ? 141 PHE   A CA    1 
ATOM   1124 C  C     . PHE   A 1 144 ? 2.654   8.086  9.307  1.00 7.31  ? 141 PHE   A C     1 
ATOM   1125 O  O     . PHE   A 1 144 ? 2.904   7.200  8.480  1.00 8.39  ? 141 PHE   A O     1 
ATOM   1126 C  CB    . PHE   A 1 144 ? 2.677   6.820  11.442 1.00 8.60  ? 141 PHE   A CB    1 
ATOM   1127 C  CG    . PHE   A 1 144 ? 4.068   7.347  11.728 1.00 8.76  ? 141 PHE   A CG    1 
ATOM   1128 C  CD1   . PHE   A 1 144 ? 4.245   8.615  12.261 1.00 9.54  ? 141 PHE   A CD1   1 
ATOM   1129 C  CD2   . PHE   A 1 144 ? 5.194   6.597  11.419 1.00 10.96 ? 141 PHE   A CD2   1 
ATOM   1130 C  CE1   . PHE   A 1 144 ? 5.520   9.104  12.516 1.00 10.42 ? 141 PHE   A CE1   1 
ATOM   1131 C  CE2   . PHE   A 1 144 ? 6.467   7.092  11.674 1.00 11.40 ? 141 PHE   A CE2   1 
ATOM   1132 C  CZ    . PHE   A 1 144 ? 6.620   8.336  12.206 1.00 10.49 ? 141 PHE   A CZ    1 
ATOM   1133 N  N     . ILE   A 1 145 ? 3.079   9.335  9.218  1.00 7.73  ? 142 ILE   A N     1 
ATOM   1134 C  CA    . ILE   A 1 145 ? 3.906   9.838  8.087  1.00 7.95  ? 142 ILE   A CA    1 
ATOM   1135 C  C     . ILE   A 1 145 ? 5.081   10.643 8.658  1.00 7.46  ? 142 ILE   A C     1 
ATOM   1136 O  O     . ILE   A 1 145 ? 4.856   11.478 9.536  1.00 8.39  ? 142 ILE   A O     1 
ATOM   1137 C  CB    . ILE   A 1 145 ? 3.017   10.719 7.169  1.00 7.96  ? 142 ILE   A CB    1 
ATOM   1138 C  CG1   . ILE   A 1 145 ? 1.909   9.868  6.523  1.00 8.76  ? 142 ILE   A CG1   1 
ATOM   1139 C  CG2   . ILE   A 1 145 ? 3.850   11.492 6.138  1.00 8.71  ? 142 ILE   A CG2   1 
ATOM   1140 C  CD1   . ILE   A 1 145 ? 0.845   10.657 5.767  1.00 9.95  ? 142 ILE   A CD1   1 
ATOM   1141 N  N     . GLU   A 1 146 ? 6.278   10.408 8.125  1.00 7.65  ? 143 GLU   A N     1 
ATOM   1142 C  CA    . GLU   A 1 146 ? 7.428   11.296 8.463  1.00 7.64  ? 143 GLU   A CA    1 
ATOM   1143 C  C     . GLU   A 1 146 ? 7.569   12.305 7.321  1.00 8.05  ? 143 GLU   A C     1 
ATOM   1144 O  O     . GLU   A 1 146 ? 7.525   11.919 6.133  1.00 8.68  ? 143 GLU   A O     1 
ATOM   1145 C  CB    . GLU   A 1 146 ? 8.741   10.538 8.656  1.00 8.74  ? 143 GLU   A CB    1 
ATOM   1146 C  CG    . GLU   A 1 146 ? 8.695   9.731  9.939  1.00 10.12 ? 143 GLU   A CG    1 
ATOM   1147 C  CD    . GLU   A 1 146 ? 10.042  9.266  10.454 1.00 11.81 ? 143 GLU   A CD    1 
ATOM   1148 O  OE1   . GLU   A 1 146 ? 11.053  9.502  9.778  1.00 17.86 ? 143 GLU   A OE1   1 
ATOM   1149 O  OE2   . GLU   A 1 146 ? 10.083  8.654  11.496 1.00 12.87 ? 143 GLU   A OE2   1 
ATOM   1150 N  N     . THR   A 1 147 ? 7.749   13.552 7.725  1.00 8.31  ? 144 THR   A N     1 
ATOM   1151 C  CA    . THR   A 1 147 ? 7.812   14.685 6.772  1.00 7.97  ? 144 THR   A CA    1 
ATOM   1152 C  C     . THR   A 1 147 ? 9.091   15.498 7.015  1.00 8.85  ? 144 THR   A C     1 
ATOM   1153 O  O     . THR   A 1 147 ? 9.712   15.380 8.087  1.00 8.99  ? 144 THR   A O     1 
ATOM   1154 C  CB    . THR   A 1 147 ? 6.663   15.674 7.034  1.00 8.36  ? 144 THR   A CB    1 
ATOM   1155 O  OG1   . THR   A 1 147 ? 6.686   16.137 8.400  1.00 8.46  ? 144 THR   A OG1   1 
ATOM   1156 C  CG2   . THR   A 1 147 ? 5.284   15.130 6.703  1.00 8.73  ? 144 THR   A CG2   1 
ATOM   1157 N  N     . SER   A 1 148 ? 9.445   16.266 5.987  1.00 9.03  ? 145 SER   A N     1 
ATOM   1158 C  CA    . SER   A 1 148 ? 10.444  17.337 6.176  1.00 9.50  ? 145 SER   A CA    1 
ATOM   1159 C  C     . SER   A 1 148 ? 9.856   18.603 5.564  1.00 10.12 ? 145 SER   A C     1 
ATOM   1160 O  O     . SER   A 1 148 ? 9.671   18.649 4.369  1.00 11.37 ? 145 SER   A O     1 
ATOM   1161 C  CB    . SER   A 1 148 ? 11.772  17.034 5.513  1.00 10.67 ? 145 SER   A CB    1 
ATOM   1162 O  OG    . SER   A 1 148 ? 12.590  18.199 5.583  1.00 13.24 ? 145 SER   A OG    1 
ATOM   1163 N  N     . ALA   A 1 149 ? 9.490   19.556 6.420  1.00 11.09 ? 146 ALA   A N     1 
ATOM   1164 C  CA    . ALA   A 1 149 ? 9.065   20.838 5.897  1.00 12.05 ? 146 ALA   A CA    1 
ATOM   1165 C  C     . ALA   A 1 149 ? 10.208  21.557 5.157  1.00 13.96 ? 146 ALA   A C     1 
ATOM   1166 O  O     . ALA   A 1 149 ? 9.974   22.391 4.286  1.00 18.07 ? 146 ALA   A O     1 
ATOM   1167 C  CB    . ALA   A 1 149 ? 8.546   21.717 7.021  1.00 13.42 ? 146 ALA   A CB    1 
ATOM   1168 N  N     . LYS   A 1 150 ? 11.446  21.233 5.493  1.00 13.12 ? 147 LYS   A N     1 
ATOM   1169 C  CA    . LYS   A 1 150 ? 12.598  21.879 4.863  1.00 15.83 ? 147 LYS   A CA    1 
ATOM   1170 C  C     . LYS   A 1 150 ? 12.718  21.459 3.409  1.00 16.55 ? 147 LYS   A C     1 
ATOM   1171 O  O     . LYS   A 1 150 ? 12.885  22.312 2.536  1.00 20.71 ? 147 LYS   A O     1 
ATOM   1172 C  CB    . LYS   A 1 150 ? 13.854  21.569 5.646  1.00 16.98 ? 147 LYS   A CB    1 
ATOM   1173 C  CG    . LYS   A 1 150 ? 15.092  22.251 5.106  1.00 19.47 ? 147 LYS   A CG    1 
ATOM   1174 C  CD    . LYS   A 1 150 ? 16.226  22.247 6.109  1.00 22.50 ? 147 LYS   A CD    1 
ATOM   1175 C  CE    . LYS   A 1 150 ? 17.385  23.070 5.583  1.00 26.58 ? 147 LYS   A CE    1 
ATOM   1176 N  NZ    . LYS   A 1 150 ? 18.565  22.923 6.461  1.00 31.54 ? 147 LYS   A NZ    1 
ATOM   1177 N  N     . THR   A 1 151 ? 12.590  20.161 3.151  1.00 15.99 ? 148 THR   A N     1 
ATOM   1178 C  CA    . THR   A 1 151 ? 12.746  19.650 1.763  1.00 17.65 ? 148 THR   A CA    1 
ATOM   1179 C  C     . THR   A 1 151 ? 11.427  19.384 1.059  1.00 17.95 ? 148 THR   A C     1 
ATOM   1180 O  O     . THR   A 1 151 ? 11.505  18.967 -0.095 1.00 24.02 ? 148 THR   A O     1 
ATOM   1181 C  CB    . THR   A 1 151 ? 13.459  18.309 1.755  1.00 17.63 ? 148 THR   A CB    1 
ATOM   1182 O  OG1   . THR   A 1 151 ? 12.597  17.304 2.294  1.00 19.06 ? 148 THR   A OG1   1 
ATOM   1183 C  CG2   . THR   A 1 151 ? 14.790  18.354 2.474  1.00 17.52 ? 148 THR   A CG2   1 
ATOM   1184 N  N     . ARG   A 1 152 ? 10.307  19.530 1.774  1.00 16.67 ? 149 ARG   A N     1 
ATOM   1185 C  CA    . ARG   A 1 152 ? 8.914   19.327 1.287  1.00 17.49 ? 149 ARG   A CA    1 
ATOM   1186 C  C     . ARG   A 1 152 ? 8.548   17.828 1.267  1.00 15.83 ? 149 ARG   A C     1 
ATOM   1187 O  O     . ARG   A 1 152 ? 7.415   17.485 0.923  1.00 16.59 ? 149 ARG   A O     1 
ATOM   1188 C  CB    . ARG   A 1 152 ? 8.588   20.118 0.008  1.00 18.72 ? 149 ARG   A CB    1 
ATOM   1189 C  CG    . ARG   A 1 152 ? 7.216   20.753 -0.008 1.00 23.08 ? 149 ARG   A CG    1 
ATOM   1190 C  CD    . ARG   A 1 152 ? 7.143   21.829 -1.077 1.00 24.62 ? 149 ARG   A CD    1 
ATOM   1191 N  NE    . ARG   A 1 152 ? 5.796   22.323 -1.011 1.00 25.41 ? 149 ARG   A NE    1 
ATOM   1192 C  CZ    . ARG   A 1 152 ? 4.806   21.680 -1.538 1.00 25.80 ? 149 ARG   A CZ    1 
ATOM   1193 N  NH1   . ARG   A 1 152 ? 5.045   20.568 -2.198 1.00 28.72 ? 149 ARG   A NH1   1 
ATOM   1194 N  NH2   . ARG   A 1 152 ? 3.596   22.148 -1.438 1.00 30.95 ? 149 ARG   A NH2   1 
ATOM   1195 N  N     . GLN   A 1 153 ? 9.413   16.972 1.799  1.00 12.68 ? 150 GLN   A N     1 
ATOM   1196 C  CA    . GLN   A 1 153 ? 9.148   15.510 1.756  1.00 11.38 ? 150 GLN   A CA    1 
ATOM   1197 C  C     . GLN   A 1 153 ? 7.842   15.173 2.487  1.00 9.49  ? 150 GLN   A C     1 
ATOM   1198 O  O     . GLN   A 1 153 ? 7.744   15.448 3.668  1.00 9.74  ? 150 GLN   A O     1 
ATOM   1199 C  CB    . GLN   A 1 153 ? 10.310  14.710 2.328  1.00 12.20 ? 150 GLN   A CB    1 
ATOM   1200 C  CG    . GLN   A 1 153 ? 10.331  13.284 1.806  1.00 14.89 ? 150 GLN   A CG    1 
ATOM   1201 C  CD    . GLN   A 1 153 ? 10.872  13.245 0.391  1.00 17.89 ? 150 GLN   A CD    1 
ATOM   1202 O  OE1   . GLN   A 1 153 ? 11.997  13.638 0.159  1.00 21.33 ? 150 GLN   A OE1   1 
ATOM   1203 N  NE2   . GLN   A 1 153 ? 10.069  12.792 -0.545 1.00 16.30 ? 150 GLN   A NE2   1 
ATOM   1204 N  N     . ARG   A 1 154 ? 6.911   14.573 1.740  1.00 8.94  ? 151 ARG   A N     1 
ATOM   1205 C  CA    . ARG   A 1 154 ? 5.634   14.102 2.234  1.00 8.96  ? 151 ARG   A CA    1 
ATOM   1206 C  C     . ARG   A 1 154 ? 4.747   15.172 2.855  1.00 9.07  ? 151 ARG   A C     1 
ATOM   1207 O  O     . ARG   A 1 154 ? 3.795   14.841 3.578  1.00 8.80  ? 151 ARG   A O     1 
ATOM   1208 C  CB    . ARG   A 1 154 ? 5.801   12.924 3.165  1.00 9.04  ? 151 ARG   A CB    1 
ATOM   1209 C  CG    . ARG   A 1 154 ? 6.512   11.765 2.490  1.00 10.56 ? 151 ARG   A CG    1 
ATOM   1210 C  CD    . ARG   A 1 154 ? 6.186   10.431 3.135  1.00 10.37 ? 151 ARG   A CD    1 
ATOM   1211 N  NE    . ARG   A 1 154 ? 4.848   9.957  2.828  1.00 11.70 ? 151 ARG   A NE    1 
ATOM   1212 C  CZ    . ARG   A 1 154 ? 4.255   8.932  3.427  1.00 11.40 ? 151 ARG   A CZ    1 
ATOM   1213 N  NH1   . ARG   A 1 154 ? 3.025   8.581  3.048  1.00 12.27 ? 151 ARG   A NH1   1 
ATOM   1214 N  NH2   . ARG   A 1 154 ? 4.870   8.256  4.393  1.00 11.35 ? 151 ARG   A NH2   1 
ATOM   1215 N  N     . VAL   A 1 155 ? 4.946   16.444 2.510  1.00 9.04  ? 152 VAL   A N     1 
ATOM   1216 C  CA    . VAL   A 1 155 ? 4.094   17.496 3.079  1.00 10.44 ? 152 VAL   A CA    1 
ATOM   1217 C  C     . VAL   A 1 155 ? 2.668   17.376 2.571  1.00 9.48  ? 152 VAL   A C     1 
ATOM   1218 O  O     . VAL   A 1 155 ? 1.712   17.326 3.343  1.00 9.16  ? 152 VAL   A O     1 
ATOM   1219 C  CB    . VAL   A 1 155 ? 4.679   18.910 2.862  1.00 12.74 ? 152 VAL   A CB    1 
ATOM   1220 C  CG1   . VAL   A 1 155 ? 3.723   19.994 3.344  1.00 14.37 ? 152 VAL   A CG1   1 
ATOM   1221 C  CG2   . VAL   A 1 155 ? 6.009   19.032 3.627  1.00 13.52 ? 152 VAL   A CG2   1 
ATOM   1222 N  N     . GLU   A 1 156 ? 2.521   17.322 1.241  1.00 10.33 ? 153 GLU   A N     1 
ATOM   1223 C  CA    . GLU   A 1 156 ? 1.151   17.097 0.701  1.00 11.17 ? 153 GLU   A CA    1 
ATOM   1224 C  C     . GLU   A 1 156 ? 0.590   15.757 1.200  1.00 9.75  ? 153 GLU   A C     1 
ATOM   1225 O  O     . GLU   A 1 156 ? -0.593  15.717 1.539  1.00 10.78 ? 153 GLU   A O     1 
ATOM   1226 C  CB    . GLU   A 1 156 ? 1.145   17.162 -0.827 1.00 13.47 ? 153 GLU   A CB    1 
ATOM   1227 C  CG    . GLU   A 1 156 ? 1.554   18.553 -1.319 1.00 17.45 ? 153 GLU   A CG    1 
ATOM   1228 C  CD    . GLU   A 1 156 ? 1.717   18.813 -2.805 1.00 25.34 ? 153 GLU   A CD    1 
ATOM   1229 O  OE1   . GLU   A 1 156 ? 2.722   18.514 -3.319 1.00 33.85 ? 153 GLU   A OE1   1 
ATOM   1230 O  OE2   . GLU   A 1 156 ? 0.857   19.364 -3.368 1.00 37.13 ? 153 GLU   A OE2   1 
ATOM   1231 N  N     . ASP   A 1 157 ? 1.404   14.710 1.238  1.00 10.20 ? 154 ASP   A N     1 
ATOM   1232 C  CA    . ASP   A 1 157 ? 0.915   13.426 1.730  1.00 9.19  ? 154 ASP   A CA    1 
ATOM   1233 C  C     . ASP   A 1 157 ? 0.301   13.557 3.113  1.00 8.29  ? 154 ASP   A C     1 
ATOM   1234 O  O     . ASP   A 1 157 ? -0.751  12.982 3.376  1.00 9.03  ? 154 ASP   A O     1 
ATOM   1235 C  CB    . ASP   A 1 157 ? 2.022   12.361 1.822  1.00 10.73 ? 154 ASP   A CB    1 
ATOM   1236 C  CG    . ASP   A 1 157 ? 2.371   11.704 0.520  1.00 13.56 ? 154 ASP   A CG    1 
ATOM   1237 O  OD1   . ASP   A 1 157 ? 1.632   11.819 -0.466 1.00 16.65 ? 154 ASP   A OD1   1 
ATOM   1238 O  OD2   . ASP   A 1 157 ? 3.423   11.023 0.514  1.00 14.92 ? 154 ASP   A OD2   1 
ATOM   1239 N  N     . ALA   A 1 158 ? 0.938   14.310 4.011  1.00 8.04  ? 155 ALA   A N     1 
ATOM   1240 C  CA    . ALA   A 1 158 ? 0.425   14.393 5.378  1.00 8.73  ? 155 ALA   A CA    1 
ATOM   1241 C  C     . ALA   A 1 158 ? -0.952  15.043 5.400  1.00 8.68  ? 155 ALA   A C     1 
ATOM   1242 O  O     . ALA   A 1 158 ? -1.865  14.529 5.996  1.00 9.21  ? 155 ALA   A O     1 
ATOM   1243 C  CB    . ALA   A 1 158 ? 1.407   15.152 6.249  1.00 9.80  ? 155 ALA   A CB    1 
ATOM   1244 N  N     . PHE   A 1 159 ? -1.082  16.186 4.737  1.00 8.24  ? 156 PHE   A N     1 
ATOM   1245 C  CA    . PHE   A 1 159 ? -2.365  16.888 4.775  1.00 8.99  ? 156 PHE   A CA    1 
ATOM   1246 C  C     . PHE   A 1 159 ? -3.445  16.157 3.965  1.00 8.61  ? 156 PHE   A C     1 
ATOM   1247 O  O     . PHE   A 1 159 ? -4.609  16.097 4.378  1.00 9.14  ? 156 PHE   A O     1 
ATOM   1248 C  CB    . PHE   A 1 159 ? -2.182  18.293 4.231  1.00 9.80  ? 156 PHE   A CB    1 
ATOM   1249 C  CG    . PHE   A 1 159 ? -1.508  19.242 5.192  1.00 10.07 ? 156 PHE   A CG    1 
ATOM   1250 C  CD1   . PHE   A 1 159 ? -2.246  19.907 6.161  1.00 11.56 ? 156 PHE   A CD1   1 
ATOM   1251 C  CD2   . PHE   A 1 159 ? -0.157  19.437 5.152  1.00 9.98  ? 156 PHE   A CD2   1 
ATOM   1252 C  CE1   . PHE   A 1 159 ? -1.648  20.791 7.035  1.00 12.78 ? 156 PHE   A CE1   1 
ATOM   1253 C  CE2   . PHE   A 1 159 ? 0.445   20.340 6.020  1.00 11.19 ? 156 PHE   A CE2   1 
ATOM   1254 C  CZ    . PHE   A 1 159 ? -0.302  21.011 6.957  1.00 11.87 ? 156 PHE   A CZ    1 
ATOM   1255 N  N     . TYR   A 1 160 ? -3.080  15.566 2.829  1.00 8.87  ? 157 TYR   A N     1 
ATOM   1256 C  CA    . TYR   A 1 160 ? -4.071  14.888 1.985  1.00 9.39  ? 157 TYR   A CA    1 
ATOM   1257 C  C     . TYR   A 1 160 ? -4.529  13.605 2.637  1.00 8.49  ? 157 TYR   A C     1 
ATOM   1258 O  O     . TYR   A 1 160 ? -5.695  13.205 2.482  1.00 9.44  ? 157 TYR   A O     1 
ATOM   1259 C  CB    . TYR   A 1 160 ? -3.517  14.628 0.598  1.00 9.75  ? 157 TYR   A CB    1 
ATOM   1260 C  CG    . TYR   A 1 160 ? -3.256  15.849 -0.234 1.00 10.86 ? 157 TYR   A CG    1 
ATOM   1261 C  CD1   . TYR   A 1 160 ? -3.349  17.153 0.258  1.00 12.94 ? 157 TYR   A CD1   1 
ATOM   1262 C  CD2   . TYR   A 1 160 ? -2.886  15.687 -1.549 1.00 13.98 ? 157 TYR   A CD2   1 
ATOM   1263 C  CE1   . TYR   A 1 160 ? -3.099  18.237 -0.550 1.00 15.12 ? 157 TYR   A CE1   1 
ATOM   1264 C  CE2   . TYR   A 1 160 ? -2.634  16.770 -2.376 1.00 18.27 ? 157 TYR   A CE2   1 
ATOM   1265 C  CZ    . TYR   A 1 160 ? -2.726  18.034 -1.863 1.00 18.40 ? 157 TYR   A CZ    1 
ATOM   1266 O  OH    . TYR   A 1 160 ? -2.485  19.103 -2.702 1.00 25.48 ? 157 TYR   A OH    1 
ATOM   1267 N  N     . THR   A 1 161 ? -3.613  12.929 3.348  1.00 8.62  ? 158 THR   A N     1 
ATOM   1268 C  CA    . THR   A 1 161 ? -4.000  11.740 4.112  1.00 8.19  ? 158 THR   A CA    1 
ATOM   1269 C  C     . THR   A 1 161 ? -5.026  12.096 5.176  1.00 8.67  ? 158 THR   A C     1 
ATOM   1270 O  O     . THR   A 1 161 ? -5.983  11.366 5.398  1.00 9.08  ? 158 THR   A O     1 
ATOM   1271 C  CB    . THR   A 1 161 ? -2.771  11.067 4.734  1.00 8.12  ? 158 THR   A CB    1 
ATOM   1272 O  OG1   . THR   A 1 161 ? -1.926  10.569 3.690  1.00 8.74  ? 158 THR   A OG1   1 
ATOM   1273 C  CG2   . THR   A 1 161 ? -3.165  9.921  5.594  1.00 9.36  ? 158 THR   A CG2   1 
ATOM   1274 N  N     . LEU   A 1 162 ? -4.864  13.256 5.816  1.00 8.20  ? 159 LEU   A N     1 
ATOM   1275 C  CA    . LEU   A 1 162 ? -5.841  13.689 6.800  1.00 8.72  ? 159 LEU   A CA    1 
ATOM   1276 C  C     . LEU   A 1 162 ? -7.233  13.946 6.168  1.00 8.80  ? 159 LEU   A C     1 
ATOM   1277 O  O     . LEU   A 1 162 ? -8.253  13.545 6.726  1.00 10.28 ? 159 LEU   A O     1 
ATOM   1278 C  CB    . LEU   A 1 162 ? -5.343  14.917 7.528  1.00 8.26  ? 159 LEU   A CB    1 
ATOM   1279 C  CG    . LEU   A 1 162 ? -6.207  15.453 8.655  1.00 8.69  ? 159 LEU   A CG    1 
ATOM   1280 C  CD1   . LEU   A 1 162 ? -6.501  14.383 9.681  1.00 8.97  ? 159 LEU   A CD1   1 
ATOM   1281 C  CD2   . LEU   A 1 162 ? -5.556  16.671 9.308  1.00 8.76  ? 159 LEU   A CD2   1 
ATOM   1282 N  N     . VAL   A 1 163 ? -7.248  14.572 4.994  1.00 8.94  ? 160 VAL   A N     1 
ATOM   1283 C  CA    . VAL   A 1 163 ? -8.510  14.726 4.233  1.00 10.59 ? 160 VAL   A CA    1 
ATOM   1284 C  C     . VAL   A 1 163 ? -9.150  13.355 3.984  1.00 9.46  ? 160 VAL   A C     1 
ATOM   1285 O  O     . VAL   A 1 163 ? -10.374 13.163 4.179  1.00 10.44 ? 160 VAL   A O     1 
ATOM   1286 C  CB    . VAL   A 1 163 ? -8.255  15.480 2.912  1.00 10.76 ? 160 VAL   A CB    1 
ATOM   1287 C  CG1   . VAL   A 1 163 ? -9.426  15.384 1.956  1.00 12.95 ? 160 VAL   A CG1   1 
ATOM   1288 C  CG2   . VAL   A 1 163 ? -7.895  16.928 3.183  1.00 12.83 ? 160 VAL   A CG2   1 
ATOM   1289 N  N     . ARG   A 1 164 ? -8.360  12.376 3.561  1.00 9.78  ? 161 ARG   A N     1 
ATOM   1290 C  CA    . ARG   A 1 164 ? -8.877  11.036 3.279  1.00 10.18 ? 161 ARG   A CA    1 
ATOM   1291 C  C     . ARG   A 1 164 ? -9.429  10.393 4.534  1.00 10.35 ? 161 ARG   A C     1 
ATOM   1292 O  O     . ARG   A 1 164 ? -10.465 9.763  4.468  1.00 12.52 ? 161 ARG   A O     1 
ATOM   1293 C  CB    . ARG   A 1 164 ? -7.796  10.162 2.651  1.00 9.58  ? 161 ARG   A CB    1 
ATOM   1294 C  CG    . ARG   A 1 164 ? -7.433  10.587 1.241  1.00 10.37 ? 161 ARG   A CG    1 
ATOM   1295 C  CD    . ARG   A 1 164 ? -6.144  9.939  0.763  1.00 12.77 ? 161 ARG   A CD    1 
ATOM   1296 N  NE    . ARG   A 1 164 ? -5.989  10.053 -0.681 1.00 13.62 ? 161 ARG   A NE    1 
ATOM   1297 C  CZ    . ARG   A 1 164 ? -4.910  9.704  -1.390 1.00 18.47 ? 161 ARG   A CZ    1 
ATOM   1298 N  NH1   . ARG   A 1 164 ? -3.793  9.298  -0.791 1.00 19.61 ? 161 ARG   A NH1   1 
ATOM   1299 N  NH2   . ARG   A 1 164 ? -4.908  9.815  -2.727 1.00 22.06 ? 161 ARG   A NH2   1 
ATOM   1300 N  N     . GLU   A 1 165 ? -8.802  10.638 5.688  1.00 10.24 ? 162 GLU   A N     1 
ATOM   1301 C  CA    . GLU   A 1 165 ? -9.343  10.133 6.967  1.00 9.99  ? 162 GLU   A CA    1 
ATOM   1302 C  C     . GLU   A 1 165 ? -10.700 10.739 7.294  1.00 10.68 ? 162 GLU   A C     1 
ATOM   1303 O  O     . GLU   A 1 165 ? -11.629 10.041 7.733  1.00 11.95 ? 162 GLU   A O     1 
ATOM   1304 C  CB    . GLU   A 1 165 ? -8.373  10.360 8.118  1.00 10.50 ? 162 GLU   A CB    1 
ATOM   1305 C  CG    . GLU   A 1 165 ? -7.085  9.575  7.994  1.00 12.03 ? 162 GLU   A CG    1 
ATOM   1306 C  CD    . GLU   A 1 165 ? -7.317  8.091  8.169  1.00 12.41 ? 162 GLU   A CD    1 
ATOM   1307 O  OE1   . GLU   A 1 165 ? -7.745  7.658  9.252  1.00 15.23 ? 162 GLU   A OE1   1 
ATOM   1308 O  OE2   . GLU   A 1 165 ? -7.067  7.315  7.227  1.00 17.26 ? 162 GLU   A OE2   1 
ATOM   1309 N  N     . ILE   A 1 166 ? -10.809 12.033 7.070  1.00 10.48 ? 163 ILE   A N     1 
ATOM   1310 C  CA    . ILE   A 1 166 ? -12.136 12.690 7.335  1.00 11.18 ? 163 ILE   A CA    1 
ATOM   1311 C  C     . ILE   A 1 166 ? -13.233 12.037 6.461  1.00 13.49 ? 163 ILE   A C     1 
ATOM   1312 O  O     . ILE   A 1 166 ? -14.329 11.709 6.967  1.00 14.76 ? 163 ILE   A O     1 
ATOM   1313 C  CB    . ILE   A 1 166 ? -12.017 14.197 7.065  1.00 11.62 ? 163 ILE   A CB    1 
ATOM   1314 C  CG1   . ILE   A 1 166 ? -11.129 14.885 8.118  1.00 11.71 ? 163 ILE   A CG1   1 
ATOM   1315 C  CG2   . ILE   A 1 166 ? -13.393 14.850 7.016  1.00 13.10 ? 163 ILE   A CG2   1 
ATOM   1316 C  CD1   . ILE   A 1 166 ? -10.740 16.294 7.767  1.00 12.28 ? 163 ILE   A CD1   1 
ATOM   1317 N  N     . ARG   A 1 167 ? -12.940 11.803 5.178  1.00 14.04 ? 164 ARG   A N     1 
ATOM   1318 C  CA    . ARG   A 1 167 ? -13.954 11.107 4.321  1.00 14.64 ? 164 ARG   A CA    1 
ATOM   1319 C  C     . ARG   A 1 167 ? -14.284 9.724  4.841  1.00 18.33 ? 164 ARG   A C     1 
ATOM   1320 O  O     . ARG   A 1 167 ? -15.469 9.354  4.767  1.00 21.52 ? 164 ARG   A O     1 
ATOM   1321 C  CB    . ARG   A 1 167 ? -13.338 10.813 2.959  1.00 15.48 ? 164 ARG   A CB    1 
ATOM   1322 C  CG    . ARG   A 1 167 ? -13.032 12.068 2.187  1.00 13.58 ? 164 ARG   A CG    1 
ATOM   1323 C  CD    . ARG   A 1 167 ? -13.024 11.618 0.711  1.00 17.19 ? 164 ARG   A CD    1 
ATOM   1324 N  NE    . ARG   A 1 167 ? -12.556 12.670 -0.159 1.00 14.28 ? 164 ARG   A NE    1 
ATOM   1325 C  CZ    . ARG   A 1 167 ? -11.377 12.662 -0.770 1.00 12.97 ? 164 ARG   A CZ    1 
ATOM   1326 N  NH1   . ARG   A 1 167 ? -11.053 13.708 -1.491 1.00 13.48 ? 164 ARG   A NH1   1 
ATOM   1327 N  NH2   . ARG   A 1 167 ? -10.577 11.606 -0.708 1.00 12.42 ? 164 ARG   A NH2   1 
ATOM   1328 N  N     . GLN   A 1 168 ? -13.326 8.937  5.258  1.00 18.16 ? 165 GLN   A N     1 
ATOM   1329 C  CA    . GLN   A 1 168 ? -13.596 7.578  5.765  1.00 21.25 ? 165 GLN   A CA    1 
ATOM   1330 C  C     . GLN   A 1 168 ? -14.533 7.703  6.965  1.00 18.60 ? 165 GLN   A C     1 
ATOM   1331 O  O     . GLN   A 1 168 ? -15.533 6.977  7.022  1.00 23.43 ? 165 GLN   A O     1 
ATOM   1332 C  CB    . GLN   A 1 168 ? -12.276 6.866  6.068  1.00 24.82 ? 165 GLN   A CB    1 
ATOM   1333 C  CG    . GLN   A 1 168 ? -11.536 6.422  4.796  1.00 32.79 ? 165 GLN   A CG    1 
ATOM   1334 C  CD    . GLN   A 1 168 ? -10.058 6.151  4.951  1.00 37.99 ? 165 GLN   A CD    1 
ATOM   1335 O  OE1   . GLN   A 1 168 ? -9.232  6.645  4.170  1.00 43.92 ? 165 GLN   A OE1   1 
ATOM   1336 N  NE2   . GLN   A 1 168 ? -9.714  5.354  5.940  1.00 45.33 ? 165 GLN   A NE2   1 
ATOM   1337 N  N     . TYR   A 1 169 ? -14.252 8.648  7.846  1.00 16.66 ? 166 TYR   A N     1 
ATOM   1338 C  CA    . TYR   A 1 169 ? -15.124 8.860  8.983  1.00 16.81 ? 166 TYR   A CA    1 
ATOM   1339 C  C     . TYR   A 1 169 ? -16.517 9.409  8.642  1.00 16.31 ? 166 TYR   A C     1 
ATOM   1340 O  O     . TYR   A 1 169 ? -17.473 9.074  9.385  1.00 18.80 ? 166 TYR   A O     1 
ATOM   1341 C  CB    . TYR   A 1 169 ? -14.430 9.714  10.039 1.00 16.05 ? 166 TYR   A CB    1 
ATOM   1342 C  CG    . TYR   A 1 169 ? -13.509 8.915  10.928 1.00 16.51 ? 166 TYR   A CG    1 
ATOM   1343 C  CD1   . TYR   A 1 169 ? -14.026 8.005  11.864 1.00 19.35 ? 166 TYR   A CD1   1 
ATOM   1344 C  CD2   . TYR   A 1 169 ? -12.124 9.055  10.845 1.00 17.01 ? 166 TYR   A CD2   1 
ATOM   1345 C  CE1   . TYR   A 1 169 ? -13.204 7.280  12.697 1.00 20.21 ? 166 TYR   A CE1   1 
ATOM   1346 C  CE2   . TYR   A 1 169 ? -11.287 8.324  11.675 1.00 18.62 ? 166 TYR   A CE2   1 
ATOM   1347 C  CZ    . TYR   A 1 169 ? -11.827 7.437  12.597 1.00 22.54 ? 166 TYR   A CZ    1 
ATOM   1348 O  OH    . TYR   A 1 169 ? -11.024 6.702  13.439 1.00 24.24 ? 166 TYR   A OH    1 
ATOM   1349 N  N     . ARG   A 1 170 ? -16.652 10.268 7.618  1.00 16.40 ? 167 ARG   A N     1 
ATOM   1350 C  CA    . ARG   A 1 170 ? -17.990 10.760 7.193  1.00 18.30 ? 167 ARG   A CA    1 
ATOM   1351 C  C     . ARG   A 1 170 ? -18.930 9.599  6.797  1.00 19.35 ? 167 ARG   A C     1 
ATOM   1352 O  O     . ARG   A 1 170 ? -20.139 9.792  6.845  1.00 20.12 ? 167 ARG   A O     1 
ATOM   1353 C  CB    . ARG   A 1 170 ? -17.889 11.857 6.086  1.00 21.43 ? 167 ARG   A CB    1 
ATOM   1354 C  CG    . ARG   A 1 170 ? -17.370 13.246 6.512  1.00 24.00 ? 167 ARG   A CG    1 
ATOM   1355 C  CD    . ARG   A 1 170 ? -17.297 14.278 5.374  1.00 22.48 ? 167 ARG   A CD    1 
ATOM   1356 N  NE    . ARG   A 1 170 ? -16.843 15.610 5.822  1.00 24.11 ? 167 ARG   A NE    1 
ATOM   1357 C  CZ    . ARG   A 1 170 ? -16.111 16.476 5.119  1.00 21.46 ? 167 ARG   A CZ    1 
ATOM   1358 N  NH1   . ARG   A 1 170 ? -15.728 16.205 3.879  1.00 26.13 ? 167 ARG   A NH1   1 
ATOM   1359 N  NH2   . ARG   A 1 170 ? -15.752 17.636 5.670  1.00 25.81 ? 167 ARG   A NH2   1 
ATOM   1360 N  N     . LEU   A 1 171 ? -18.411 8.408  6.444  1.00 19.84 ? 168 LEU   A N     1 
ATOM   1361 C  CA    . LEU   A 1 171 ? -19.278 7.206  6.173  1.00 20.23 ? 168 LEU   A CA    1 
ATOM   1362 C  C     . LEU   A 1 171 ? -19.569 6.274  7.365  1.00 24.88 ? 168 LEU   A C     1 
ATOM   1363 O  O     . LEU   A 1 171 ? -20.395 5.339  7.248  1.00 27.47 ? 168 LEU   A O     1 
ATOM   1364 C  CB    . LEU   A 1 171 ? -18.677 6.357  5.064  1.00 23.24 ? 168 LEU   A CB    1 
ATOM   1365 C  CG    . LEU   A 1 171 ? -18.504 7.076  3.742  1.00 24.24 ? 168 LEU   A CG    1 
ATOM   1366 C  CD1   . LEU   A 1 171 ? -17.951 6.081  2.736  1.00 28.03 ? 168 LEU   A CD1   1 
ATOM   1367 C  CD2   . LEU   A 1 171 ? -19.785 7.702  3.204  1.00 25.49 ? 168 LEU   A CD2   1 
ATOM   1368 N  N     . LYS   A 1 172 ? -18.905 6.501  8.491  1.00 21.28 ? 169 LYS   A N     1 
ATOM   1369 C  CA    . LYS   A 1 172 ? -19.064 5.661  9.676  1.00 23.50 ? 169 LYS   A CA    1 
ATOM   1370 C  C     . LYS   A 1 172 ? -20.127 6.332  10.533 1.00 23.88 ? 169 LYS   A C     1 
ATOM   1371 O  O     . LYS   A 1 172 ? -21.097 5.696  10.958 1.00 28.39 ? 169 LYS   A O     1 
ATOM   1372 C  CB    . LYS   A 1 172 ? -17.742 5.516  10.452 1.00 26.38 ? 169 LYS   A CB    1 
ATOM   1373 C  CG    . LYS   A 1 172 ? -17.857 4.700  11.738 1.00 28.64 ? 169 LYS   A CG    1 
ATOM   1374 C  CD    . LYS   A 1 172 ? -16.529 4.541  12.470 1.00 31.87 ? 169 LYS   A CD    1 
ATOM   1375 C  CE    . LYS   A 1 172 ? -16.698 3.695  13.724 1.00 37.52 ? 169 LYS   A CE    1 
ATOM   1376 N  NZ    . LYS   A 1 172 ? -15.491 3.634  14.599 1.00 42.61 ? 169 LYS   A NZ    1 
ATOM   1377 O  OXT   . LYS   A 1 172 ? -20.046 7.533  10.786 1.00 20.66 ? 169 LYS   A OXT   1 
HETATM 1378 P  PB    . GDP   B 2 .   ? 6.142   25.593 15.294 1.00 11.13 ? 201 GDP   A PB    1 
HETATM 1379 O  O1B   . GDP   B 2 .   ? 5.257   26.402 14.373 1.00 11.32 ? 201 GDP   A O1B   1 
HETATM 1380 O  O2B   . GDP   B 2 .   ? 5.698   24.156 15.479 1.00 10.93 ? 201 GDP   A O2B   1 
HETATM 1381 O  O3B   . GDP   B 2 .   ? 6.454   26.282 16.602 1.00 11.00 ? 201 GDP   A O3B   1 
HETATM 1382 O  O3A   . GDP   B 2 .   ? 7.572   25.436 14.549 1.00 10.49 ? 201 GDP   A O3A   1 
HETATM 1383 P  PA    . GDP   B 2 .   ? 8.118   26.223 13.253 1.00 12.20 ? 201 GDP   A PA    1 
HETATM 1384 O  O1A   . GDP   B 2 .   ? 7.421   25.813 12.013 1.00 13.64 ? 201 GDP   A O1A   1 
HETATM 1385 O  O2A   . GDP   B 2 .   ? 8.234   27.644 13.596 1.00 15.48 ? 201 GDP   A O2A   1 
HETATM 1386 O  "O5'" . GDP   B 2 .   ? 9.551   25.589 13.198 1.00 11.99 ? 201 GDP   A "O5'" 1 
HETATM 1387 C  "C5'" . GDP   B 2 .   ? 10.481  25.694 14.284 1.00 12.17 ? 201 GDP   A "C5'" 1 
HETATM 1388 C  "C4'" . GDP   B 2 .   ? 11.923  25.627 13.799 1.00 12.83 ? 201 GDP   A "C4'" 1 
HETATM 1389 O  "O4'" . GDP   B 2 .   ? 12.195  24.336 13.221 1.00 13.03 ? 201 GDP   A "O4'" 1 
HETATM 1390 C  "C3'" . GDP   B 2 .   ? 12.219  26.650 12.721 1.00 14.35 ? 201 GDP   A "C3'" 1 
HETATM 1391 O  "O3'" . GDP   B 2 .   ? 13.565  27.115 12.887 1.00 16.71 ? 201 GDP   A "O3'" 1 
HETATM 1392 C  "C2'" . GDP   B 2 .   ? 12.108  25.878 11.422 1.00 13.49 ? 201 GDP   A "C2'" 1 
HETATM 1393 O  "O2'" . GDP   B 2 .   ? 12.924  26.359 10.362 1.00 19.84 ? 201 GDP   A "O2'" 1 
HETATM 1394 C  "C1'" . GDP   B 2 .   ? 12.581  24.509 11.872 1.00 13.46 ? 201 GDP   A "C1'" 1 
HETATM 1395 N  N9    . GDP   B 2 .   ? 11.958  23.424 11.091 1.00 12.10 ? 201 GDP   A N9    1 
HETATM 1396 C  C8    . GDP   B 2 .   ? 10.636  23.226 10.871 1.00 11.27 ? 201 GDP   A C8    1 
HETATM 1397 N  N7    . GDP   B 2 .   ? 10.423  22.123 10.138 1.00 11.18 ? 201 GDP   A N7    1 
HETATM 1398 C  C5    . GDP   B 2 .   ? 11.640  21.625 9.907  1.00 11.24 ? 201 GDP   A C5    1 
HETATM 1399 C  C6    . GDP   B 2 .   ? 12.126  20.463 9.152  1.00 11.47 ? 201 GDP   A C6    1 
HETATM 1400 O  O6    . GDP   B 2 .   ? 11.348  19.668 8.547  1.00 11.15 ? 201 GDP   A O6    1 
HETATM 1401 N  N1    . GDP   B 2 .   ? 13.464  20.286 9.147  1.00 12.27 ? 201 GDP   A N1    1 
HETATM 1402 C  C2    . GDP   B 2 .   ? 14.356  21.104 9.778  1.00 13.24 ? 201 GDP   A C2    1 
HETATM 1403 N  N2    . GDP   B 2 .   ? 15.666  20.835 9.712  1.00 15.40 ? 201 GDP   A N2    1 
HETATM 1404 N  N3    . GDP   B 2 .   ? 13.969  22.183 10.463 1.00 11.83 ? 201 GDP   A N3    1 
HETATM 1405 C  C4    . GDP   B 2 .   ? 12.649  22.463 10.529 1.00 11.63 ? 201 GDP   A C4    1 
HETATM 1406 MG MG    . MG    C 3 .   ? 4.238   28.225 14.549 1.00 10.54 2 202 MG    A MG    1 
HETATM 1407 C  C1    . EDO   D 4 .   ? -4.612  11.608 -6.151 1.00 25.04 ? 203 EDO   A C1    1 
HETATM 1408 O  O1    . EDO   D 4 .   ? -5.336  12.686 -5.566 1.00 20.36 ? 203 EDO   A O1    1 
HETATM 1409 C  C2    . EDO   D 4 .   ? -5.597  10.615 -6.693 1.00 22.66 ? 203 EDO   A C2    1 
HETATM 1410 O  O2    . EDO   D 4 .   ? -6.539  11.238 -7.582 1.00 23.86 ? 203 EDO   A O2    1 
HETATM 1411 C  C1    . EDO   E 4 .   ? -0.488  7.036  5.185  1.00 29.36 ? 204 EDO   A C1    1 
HETATM 1412 O  O1    . EDO   E 4 .   ? -0.641  5.711  5.721  1.00 33.17 ? 204 EDO   A O1    1 
HETATM 1413 C  C2    . EDO   E 4 .   ? 0.105   6.864  3.813  1.00 28.19 ? 204 EDO   A C2    1 
HETATM 1414 O  O2    . EDO   E 4 .   ? 1.432   6.353  3.944  1.00 24.90 ? 204 EDO   A O2    1 
HETATM 1415 C  C1    . EDO   F 4 .   ? 2.717   9.309  22.709 1.00 20.42 ? 205 EDO   A C1    1 
HETATM 1416 O  O1    . EDO   F 4 .   ? 2.678   10.546 23.355 1.00 14.76 ? 205 EDO   A O1    1 
HETATM 1417 C  C2    . EDO   F 4 .   ? 3.564   8.408  23.553 1.00 22.30 ? 205 EDO   A C2    1 
HETATM 1418 O  O2    . EDO   F 4 .   ? 2.881   8.173  24.773 1.00 26.24 ? 205 EDO   A O2    1 
HETATM 1419 O  OAR   . A1IIU G 5 .   ? -8.981  34.664 16.408 1.00 22.37 ? 206 A1IIU A OAR   1 
HETATM 1420 C  CAQ   . A1IIU G 5 .   ? -8.517  33.661 15.823 1.00 18.00 ? 206 A1IIU A CAQ   1 
HETATM 1421 C  CAG   . A1IIU G 5 .   ? -8.884  32.392 16.277 1.00 16.94 ? 206 A1IIU A CAG   1 
HETATM 1422 C  CAH   . A1IIU G 5 .   ? -10.188 31.957 16.015 1.00 17.86 ? 206 A1IIU A CAH   1 
HETATM 1423 C  CAF   . A1IIU G 5 .   ? -8.025  31.531 16.974 1.00 17.55 ? 206 A1IIU A CAF   1 
HETATM 1424 O  OAP   . A1IIU G 5 .   ? -6.757  31.936 17.227 1.00 19.18 ? 206 A1IIU A OAP   1 
HETATM 1425 C  CAE   . A1IIU G 5 .   ? -8.465  30.282 17.381 1.00 16.94 ? 206 A1IIU A CAE   1 
HETATM 1426 C  CAD   . A1IIU G 5 .   ? -9.749  29.856 17.109 1.00 18.57 ? 206 A1IIU A CAD   1 
HETATM 1427 C  CAC   . A1IIU G 5 .   ? -10.621 30.699 16.438 1.00 17.35 ? 206 A1IIU A CAC   1 
HETATM 1428 S  SAB   . A1IIU G 5 .   ? -12.222 30.160 16.023 1.00 19.25 ? 206 A1IIU A SAB   1 
HETATM 1429 O  OAA   . A1IIU G 5 .   ? -12.479 28.826 16.655 1.00 19.36 ? 206 A1IIU A OAA   1 
HETATM 1430 O  OAI   . A1IIU G 5 .   ? -13.248 31.170 16.476 1.00 20.87 ? 206 A1IIU A OAI   1 
HETATM 1431 N  NAJ   . A1IIU G 5 .   ? -12.131 30.167 14.434 1.00 18.19 ? 206 A1IIU A NAJ   1 
HETATM 1432 C  CAK   . A1IIU G 5 .   ? -11.673 29.103 13.770 1.00 17.77 ? 206 A1IIU A CAK   1 
HETATM 1433 S  SAL   . A1IIU G 5 .   ? -11.572 27.511 14.310 1.00 16.59 ? 206 A1IIU A SAL   1 
HETATM 1434 C  CAM   . A1IIU G 5 .   ? -10.917 26.973 12.814 1.00 14.77 ? 206 A1IIU A CAM   1 
HETATM 1435 C  CAN   . A1IIU G 5 .   ? -10.557 25.703 12.475 1.00 13.73 ? 206 A1IIU A CAN   1 
HETATM 1436 CL CLAO  . A1IIU G 5 .   ? -10.807 24.448 13.608 1.00 15.57 ? 206 A1IIU A CLAO  1 
HETATM 1437 C  CAV   . A1IIU G 5 .   ? -10.007 25.433 11.222 1.00 14.41 ? 206 A1IIU A CAV   1 
HETATM 1438 C  CAU   . A1IIU G 5 .   ? -9.825  26.474 10.333 1.00 16.66 ? 206 A1IIU A CAU   1 
HETATM 1439 C  CAT   . A1IIU G 5 .   ? -10.216 27.768 10.715 1.00 15.42 ? 206 A1IIU A CAT   1 
HETATM 1440 O  OAS   . A1IIU G 5 .   ? -10.027 28.766 9.817  1.00 17.70 ? 206 A1IIU A OAS   1 
HETATM 1441 C  CAW   . A1IIU G 5 .   ? -10.758 28.036 11.954 1.00 14.75 ? 206 A1IIU A CAW   1 
HETATM 1442 N  NBJ   . A1IIU G 5 .   ? -11.172 29.245 12.537 1.00 16.54 ? 206 A1IIU A NBJ   1 
HETATM 1443 C  CBI   . A1IIU G 5 .   ? -11.153 30.592 11.892 1.00 17.82 ? 206 A1IIU A CBI   1 
HETATM 1444 C  CBH   . A1IIU G 5 .   ? -9.724  31.099 11.744 1.00 20.69 ? 206 A1IIU A CBH   1 
HETATM 1445 C  CBG   . A1IIU G 5 .   ? -9.189  31.658 13.031 1.00 21.15 ? 206 A1IIU A CBG   1 
HETATM 1446 C  CBF   . A1IIU G 5 .   ? -7.866  32.338 12.724 1.00 19.79 ? 206 A1IIU A CBF   1 
HETATM 1447 C  CBE   . A1IIU G 5 .   ? -7.135  32.628 13.983 1.00 18.92 ? 206 A1IIU A CBE   1 
HETATM 1448 N  NAX   . A1IIU G 5 .   ? -7.737  33.829 14.741 1.00 19.34 ? 206 A1IIU A NAX   1 
HETATM 1449 C  CAY   . A1IIU G 5 .   ? -7.454  35.245 14.289 1.00 22.07 ? 206 A1IIU A CAY   1 
HETATM 1450 C  CAZ   . A1IIU G 5 .   ? -8.643  35.731 13.454 1.00 23.48 ? 206 A1IIU A CAZ   1 
HETATM 1451 C  CBA   . A1IIU G 5 .   ? -8.338  37.203 13.071 1.00 24.64 ? 206 A1IIU A CBA   1 
HETATM 1452 N  NBB   . A1IIU G 5 .   ? -7.060  37.324 12.350 1.00 23.62 ? 206 A1IIU A NBB   1 
HETATM 1453 C  CBC   . A1IIU G 5 .   ? -5.935  36.867 13.164 1.00 22.60 ? 206 A1IIU A CBC   1 
HETATM 1454 C  CBD   . A1IIU G 5 .   ? -6.134  35.403 13.516 1.00 21.21 ? 206 A1IIU A CBD   1 
HETATM 1455 O  O     . HOH   H 6 .   ? -7.191  13.536 -8.120 1.00 18.92 ? 301 HOH   A O     1 
HETATM 1456 O  O     . HOH   H 6 .   ? 2.594   20.381 23.317 1.00 26.52 ? 302 HOH   A O     1 
HETATM 1457 O  O     . HOH   H 6 .   ? 10.061  8.592  25.642 1.00 31.27 ? 303 HOH   A O     1 
HETATM 1458 O  O     . HOH   H 6 .   ? -3.696  27.593 20.323 1.00 17.77 ? 304 HOH   A O     1 
HETATM 1459 O  O     . HOH   H 6 .   ? -8.478  6.995  13.332 1.00 24.42 ? 305 HOH   A O     1 
HETATM 1460 O  O     . HOH   H 6 .   ? -16.216 13.746 -0.132 1.00 39.94 ? 306 HOH   A O     1 
HETATM 1461 O  O     . HOH   H 6 .   ? 23.310  15.770 13.909 1.00 14.88 ? 307 HOH   A O     1 
HETATM 1462 O  O     . HOH   H 6 .   ? -7.493  8.967  11.515 1.00 12.82 ? 308 HOH   A O     1 
HETATM 1463 O  O     . HOH   H 6 .   ? -14.540 27.434 24.363 1.00 30.67 ? 309 HOH   A O     1 
HETATM 1464 O  O     . HOH   H 6 .   ? 2.324   27.382 14.640 1.00 12.94 ? 310 HOH   A O     1 
HETATM 1465 O  O     . HOH   H 6 .   ? 8.348   11.149 30.583 1.00 25.03 ? 311 HOH   A O     1 
HETATM 1466 O  O     . HOH   H 6 .   ? -7.040  35.706 9.983  1.00 28.48 ? 312 HOH   A O     1 
HETATM 1467 O  O     . HOH   H 6 .   ? 7.017   19.930 24.834 1.00 35.15 ? 313 HOH   A O     1 
HETATM 1468 O  O     . HOH   H 6 .   ? -0.950  3.138  11.645 1.00 33.35 ? 314 HOH   A O     1 
HETATM 1469 O  O     . HOH   H 6 .   ? -1.570  20.714 25.725 1.00 43.81 ? 315 HOH   A O     1 
HETATM 1470 O  O     . HOH   H 6 .   ? 6.132   -1.347 12.560 1.00 24.63 ? 316 HOH   A O     1 
HETATM 1471 O  O     . HOH   H 6 .   ? 19.390  8.702  12.473 1.00 19.27 ? 317 HOH   A O     1 
HETATM 1472 O  O     . HOH   H 6 .   ? -1.024  3.899  23.007 1.00 37.08 ? 318 HOH   A O     1 
HETATM 1473 O  O     . HOH   H 6 .   ? 4.382   15.054 27.475 1.00 32.78 ? 319 HOH   A O     1 
HETATM 1474 O  O     . HOH   H 6 .   ? -16.828 21.386 11.970 1.00 30.89 ? 320 HOH   A O     1 
HETATM 1475 O  O     . HOH   H 6 .   ? 6.116   29.151 14.306 1.00 14.23 ? 321 HOH   A O     1 
HETATM 1476 O  O     . HOH   H 6 .   ? 13.244  19.724 16.940 1.00 14.40 ? 322 HOH   A O     1 
HETATM 1477 O  O     . HOH   H 6 .   ? -8.764  8.476  15.852 1.00 26.30 ? 323 HOH   A O     1 
HETATM 1478 O  O     . HOH   H 6 .   ? 10.665  31.492 3.171  1.00 34.36 ? 324 HOH   A O     1 
HETATM 1479 O  O     . HOH   H 6 .   ? 1.592   10.273 -2.687 1.00 21.55 ? 325 HOH   A O     1 
HETATM 1480 O  O     . HOH   H 6 .   ? 0.255   30.741 11.949 1.00 18.67 ? 326 HOH   A O     1 
HETATM 1481 O  O     . HOH   H 6 .   ? -8.369  7.586  -5.193 1.00 12.51 ? 327 HOH   A O     1 
HETATM 1482 O  O     . HOH   H 6 .   ? -4.079  23.445 -5.425 1.00 41.67 ? 328 HOH   A O     1 
HETATM 1483 O  O     . HOH   H 6 .   ? -21.590 10.464 9.041  1.00 14.50 ? 329 HOH   A O     1 
HETATM 1484 O  O     . HOH   H 6 .   ? 4.413   28.075 16.682 1.00 13.56 ? 330 HOH   A O     1 
HETATM 1485 O  O     . HOH   H 6 .   ? 3.693   26.341 19.212 1.00 20.07 ? 331 HOH   A O     1 
HETATM 1486 O  O     . HOH   H 6 .   ? -17.938 15.133 18.210 1.00 17.79 ? 332 HOH   A O     1 
HETATM 1487 O  O     . HOH   H 6 .   ? -6.032  8.092  4.829  1.00 36.58 ? 333 HOH   A O     1 
HETATM 1488 O  O     . HOH   H 6 .   ? -4.693  37.474 9.319  1.00 47.63 ? 334 HOH   A O     1 
HETATM 1489 O  O     . HOH   H 6 .   ? 13.719  14.815 2.186  1.00 21.52 ? 335 HOH   A O     1 
HETATM 1490 O  O     . HOH   H 6 .   ? -1.058  22.720 28.968 1.00 33.22 ? 336 HOH   A O     1 
HETATM 1491 O  O     . HOH   H 6 .   ? 18.867  19.555 7.020  1.00 32.51 ? 337 HOH   A O     1 
HETATM 1492 O  O     . HOH   H 6 .   ? 3.371   6.391  5.875  1.00 12.41 ? 338 HOH   A O     1 
HETATM 1493 O  O     . HOH   H 6 .   ? 8.789   27.656 17.001 1.00 18.85 ? 339 HOH   A O     1 
HETATM 1494 O  O     . HOH   H 6 .   ? -10.656 21.923 -9.435 1.00 32.73 ? 340 HOH   A O     1 
HETATM 1495 O  O     . HOH   H 6 .   ? 7.629   26.713 5.585  1.00 16.68 ? 341 HOH   A O     1 
HETATM 1496 O  O     . HOH   H 6 .   ? 10.794  20.372 18.599 1.00 32.04 ? 342 HOH   A O     1 
HETATM 1497 O  O     . HOH   H 6 .   ? -10.409 31.921 8.464  1.00 43.86 ? 343 HOH   A O     1 
HETATM 1498 O  O     . HOH   H 6 .   ? -15.981 14.283 26.940 1.00 39.28 ? 344 HOH   A O     1 
HETATM 1499 O  O     . HOH   H 6 .   ? 17.037  16.065 21.331 1.00 29.12 ? 345 HOH   A O     1 
HETATM 1500 O  O     . HOH   H 6 .   ? -17.662 20.331 14.442 1.00 26.47 ? 346 HOH   A O     1 
HETATM 1501 O  O     . HOH   H 6 .   ? -4.223  -0.132 14.067 1.00 30.62 ? 347 HOH   A O     1 
HETATM 1502 O  O     . HOH   H 6 .   ? 11.483  13.729 -2.748 1.00 39.16 ? 348 HOH   A O     1 
HETATM 1503 O  O     . HOH   H 6 .   ? -14.651 20.512 -9.254 1.00 32.37 ? 349 HOH   A O     1 
HETATM 1504 O  O     . HOH   H 6 .   ? 6.377   39.089 15.157 1.00 26.03 ? 350 HOH   A O     1 
HETATM 1505 O  O     . HOH   H 6 .   ? 4.281   17.469 19.732 1.00 10.30 ? 351 HOH   A O     1 
HETATM 1506 O  O     . HOH   H 6 .   ? -17.005 17.913 15.356 1.00 21.90 ? 352 HOH   A O     1 
HETATM 1507 O  O     . HOH   H 6 .   ? 5.010   17.233 -0.467 1.00 17.64 ? 353 HOH   A O     1 
HETATM 1508 O  O     . HOH   H 6 .   ? 14.093  13.659 4.785  1.00 22.44 ? 354 HOH   A O     1 
HETATM 1509 O  O     . HOH   H 6 .   ? -3.146  25.389 30.525 1.00 22.95 ? 355 HOH   A O     1 
HETATM 1510 O  O     . HOH   H 6 .   ? -6.199  7.345  22.368 1.00 39.01 ? 356 HOH   A O     1 
HETATM 1511 O  O     . HOH   H 6 .   ? -15.308 16.044 -8.636 1.00 16.70 ? 357 HOH   A O     1 
HETATM 1512 O  O     . HOH   H 6 .   ? -1.666  18.652 -5.353 1.00 56.31 ? 358 HOH   A O     1 
HETATM 1513 O  O     . HOH   H 6 .   ? 9.261   19.923 23.156 1.00 25.12 ? 359 HOH   A O     1 
HETATM 1514 O  O     . HOH   H 6 .   ? 9.758   29.043 11.303 1.00 27.41 ? 360 HOH   A O     1 
HETATM 1515 O  O     . HOH   H 6 .   ? 5.404   12.237 -1.077 1.00 51.22 ? 361 HOH   A O     1 
HETATM 1516 O  O     . HOH   H 6 .   ? -3.166  8.764  1.915  1.00 17.96 ? 362 HOH   A O     1 
HETATM 1517 O  O     . HOH   H 6 .   ? 15.922  8.227  22.337 1.00 28.88 ? 363 HOH   A O     1 
HETATM 1518 O  O     . HOH   H 6 .   ? -15.877 21.808 6.601  1.00 30.53 ? 364 HOH   A O     1 
HETATM 1519 O  O     . HOH   H 6 .   ? -21.839 10.285 24.059 1.00 39.27 ? 365 HOH   A O     1 
HETATM 1520 O  O     . HOH   H 6 .   ? -10.008 11.688 26.355 1.00 35.83 ? 366 HOH   A O     1 
HETATM 1521 O  O     . HOH   H 6 .   ? -4.699  30.821 20.921 1.00 32.02 ? 367 HOH   A O     1 
HETATM 1522 O  O     . HOH   H 6 .   ? 3.521   30.197 14.763 1.00 14.24 ? 368 HOH   A O     1 
HETATM 1523 O  O     . HOH   H 6 .   ? 8.521   23.028 22.870 1.00 31.25 ? 369 HOH   A O     1 
HETATM 1524 O  O     . HOH   H 6 .   ? -15.239 18.090 -6.710 1.00 24.22 ? 370 HOH   A O     1 
HETATM 1525 O  O     . HOH   H 6 .   ? 3.429   29.873 21.010 1.00 27.83 ? 371 HOH   A O     1 
HETATM 1526 O  O     . HOH   H 6 .   ? 17.351  10.607 11.057 1.00 13.45 ? 372 HOH   A O     1 
HETATM 1527 O  O     . HOH   H 6 .   ? 15.774  26.121 10.232 1.00 38.70 ? 373 HOH   A O     1 
HETATM 1528 O  O     . HOH   H 6 .   ? -18.832 8.920  21.130 1.00 30.58 ? 374 HOH   A O     1 
HETATM 1529 O  O     . HOH   H 6 .   ? 18.737  17.758 17.636 1.00 26.12 ? 375 HOH   A O     1 
HETATM 1530 O  O     . HOH   H 6 .   ? 7.649   35.790 11.828 1.00 29.16 ? 376 HOH   A O     1 
HETATM 1531 O  O     . HOH   H 6 .   ? -8.864  5.527  15.243 1.00 35.29 ? 377 HOH   A O     1 
HETATM 1532 O  O     . HOH   H 6 .   ? -22.880 4.945  13.083 1.00 20.90 ? 378 HOH   A O     1 
HETATM 1533 O  O     . HOH   H 6 .   ? 6.997   14.270 -1.128 1.00 22.68 ? 379 HOH   A O     1 
HETATM 1534 O  O     . HOH   H 6 .   ? -4.692  29.010 22.786 1.00 34.75 ? 380 HOH   A O     1 
HETATM 1535 O  O     . HOH   H 6 .   ? -0.947  10.649 0.108  1.00 43.50 ? 381 HOH   A O     1 
HETATM 1536 O  O     . HOH   H 6 .   ? -22.295 5.295  5.061  1.00 26.41 ? 382 HOH   A O     1 
HETATM 1537 O  O     . HOH   H 6 .   ? -1.501  35.269 16.131 1.00 32.62 ? 383 HOH   A O     1 
HETATM 1538 O  O     . HOH   H 6 .   ? -4.470  20.262 -6.544 1.00 38.36 ? 384 HOH   A O     1 
HETATM 1539 O  O     . HOH   H 6 .   ? 15.547  25.192 13.802 1.00 29.18 ? 385 HOH   A O     1 
HETATM 1540 O  O     . HOH   H 6 .   ? -4.520  30.081 27.611 1.00 50.62 ? 386 HOH   A O     1 
HETATM 1541 O  O     . HOH   H 6 .   ? -7.141  4.912  10.036 1.00 40.51 ? 387 HOH   A O     1 
HETATM 1542 O  O     . HOH   H 6 .   ? -18.301 21.037 2.453  1.00 37.72 ? 388 HOH   A O     1 
HETATM 1543 O  O     . HOH   H 6 .   ? 13.158  15.715 24.438 1.00 21.39 ? 389 HOH   A O     1 
HETATM 1544 O  O     . HOH   H 6 .   ? 9.694   8.868  14.391 1.00 16.51 ? 390 HOH   A O     1 
HETATM 1545 O  O     . HOH   H 6 .   ? 12.107  8.183  21.742 1.00 49.26 ? 391 HOH   A O     1 
HETATM 1546 O  O     . HOH   H 6 .   ? 0.486   4.810  8.320  1.00 19.82 ? 392 HOH   A O     1 
HETATM 1547 O  O     . HOH   H 6 .   ? -21.947 14.437 22.534 1.00 22.02 ? 393 HOH   A O     1 
HETATM 1548 O  O     . HOH   H 6 .   ? -1.816  31.090 20.913 1.00 27.42 ? 394 HOH   A O     1 
HETATM 1549 O  O     . HOH   H 6 .   ? 14.862  24.503 2.313  1.00 74.16 ? 395 HOH   A O     1 
HETATM 1550 O  O     . HOH   H 6 .   ? 3.839   14.703 -0.456 1.00 13.33 ? 396 HOH   A O     1 
HETATM 1551 O  O     . HOH   H 6 .   ? -21.486 11.440 4.776  1.00 24.73 ? 397 HOH   A O     1 
HETATM 1552 O  O     . HOH   H 6 .   ? 7.756   10.958 -0.885 1.00 17.21 ? 398 HOH   A O     1 
HETATM 1553 O  O     . HOH   H 6 .   ? 17.793  22.665 10.692 1.00 42.88 ? 399 HOH   A O     1 
HETATM 1554 O  O     . HOH   H 6 .   ? 13.490  -0.633 16.092 1.00 48.61 ? 400 HOH   A O     1 
HETATM 1555 O  O     . HOH   H 6 .   ? 11.104  12.929 27.313 1.00 38.78 ? 401 HOH   A O     1 
HETATM 1556 O  O     . HOH   H 6 .   ? -9.023  37.654 16.455 1.00 41.03 ? 402 HOH   A O     1 
HETATM 1557 O  O     . HOH   H 6 .   ? 13.172  23.616 17.120 1.00 34.08 ? 403 HOH   A O     1 
HETATM 1558 O  O     . HOH   H 6 .   ? 3.760   13.003 29.158 1.00 40.06 ? 404 HOH   A O     1 
HETATM 1559 O  O     . HOH   H 6 .   ? -12.725 5.078  16.577 1.00 52.98 ? 405 HOH   A O     1 
HETATM 1560 O  O     . HOH   H 6 .   ? 1.847   2.593  11.836 1.00 34.57 ? 406 HOH   A O     1 
HETATM 1561 O  O     . HOH   H 6 .   ? -14.387 0.855  15.077 1.00 50.11 ? 407 HOH   A O     1 
HETATM 1562 O  O     . HOH   H 6 .   ? -17.947 19.184 4.259  1.00 42.10 ? 408 HOH   A O     1 
HETATM 1563 O  O     . HOH   H 6 .   ? -3.993  14.345 29.025 1.00 43.62 ? 409 HOH   A O     1 
HETATM 1564 O  O     . HOH   H 6 .   ? 16.570  20.959 15.537 1.00 21.77 ? 410 HOH   A O     1 
HETATM 1565 O  O     . HOH   H 6 .   ? 15.071  22.435 13.364 1.00 22.60 ? 411 HOH   A O     1 
HETATM 1566 O  O     . HOH   H 6 .   ? -3.899  17.052 28.396 1.00 53.64 ? 412 HOH   A O     1 
HETATM 1567 O  O     . HOH   H 6 .   ? -1.357  8.510  -2.482 1.00 31.31 ? 413 HOH   A O     1 
HETATM 1568 O  O     . HOH   H 6 .   ? 4.617   23.464 23.598 1.00 28.03 ? 414 HOH   A O     1 
HETATM 1569 O  O     . HOH   H 6 .   ? -5.297  34.548 6.795  1.00 45.78 ? 415 HOH   A O     1 
HETATM 1570 O  O     . HOH   H 6 .   ? 10.671  29.428 14.632 1.00 42.60 ? 416 HOH   A O     1 
HETATM 1571 O  O     . HOH   H 6 .   ? 1.070   8.638  0.465  1.00 30.05 ? 417 HOH   A O     1 
HETATM 1572 O  O     . HOH   H 6 .   ? 10.133  7.338  23.294 1.00 39.61 ? 418 HOH   A O     1 
HETATM 1573 O  O     . HOH   H 6 .   ? 20.641  16.518 13.481 1.00 19.05 ? 419 HOH   A O     1 
HETATM 1574 O  O     . HOH   H 6 .   ? -4.589  3.852  9.762  1.00 52.41 ? 420 HOH   A O     1 
HETATM 1575 O  O     . HOH   H 6 .   ? 1.711   31.578 22.345 1.00 43.89 ? 421 HOH   A O     1 
HETATM 1576 O  O     . HOH   H 6 .   ? 14.875  19.790 19.544 1.00 40.36 ? 422 HOH   A O     1 
HETATM 1577 O  O     . HOH   H 6 .   ? 9.506   27.753 19.557 1.00 61.59 ? 423 HOH   A O     1 
HETATM 1578 O  O     . HOH   H 6 .   ? 5.036   27.627 21.284 1.00 37.11 ? 424 HOH   A O     1 
HETATM 1579 O  O     . HOH   H 6 .   ? -20.681 4.421  15.052 1.00 37.00 ? 425 HOH   A O     1 
HETATM 1580 O  O     . HOH   H 6 .   ? 17.508  21.908 18.134 1.00 40.65 ? 426 HOH   A O     1 
HETATM 1581 O  O     . HOH   H 6 .   ? 14.173  6.724  23.919 1.00 53.29 ? 427 HOH   A O     1 
HETATM 1582 O  O     . HOH   H 6 .   ? 1.536   7.775  -2.297 1.00 34.06 ? 428 HOH   A O     1 
HETATM 1583 O  O     . HOH   H 6 .   ? -2.830  0.801  11.762 1.00 45.58 ? 429 HOH   A O     1 
HETATM 1584 O  O     . HOH   H 6 .   ? -6.845  0.093  13.082 1.00 37.64 ? 430 HOH   A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . MET   A 4   ? 0.3689 0.7781 0.3994 -0.0061 0.0438  0.0009  1   MET   A N     
2    C  CA    . MET   A 4   ? 0.4275 0.6843 0.3721 0.0220  -0.0431 0.1224  1   MET   A CA    
3    C  C     . MET   A 4   ? 0.3016 0.6324 0.3689 0.0634  -0.0407 0.1150  1   MET   A C     
4    O  O     . MET   A 4   ? 0.3144 0.6136 0.4508 0.1934  0.0582  0.0106  1   MET   A O     
5    C  CB    . MET   A 4   ? 0.5141 0.6756 0.5021 0.0442  -0.0540 0.0916  1   MET   A CB    
6    C  CG    . MET   A 4   ? 0.5438 0.6811 0.4331 -0.0005 0.0376  0.0510  1   MET   A CG    
7    S  SD    . MET   A 4   ? 0.4722 0.4531 0.3579 0.0800  -0.0294 -0.0446 1   MET   A SD    
8    C  CE    . MET   A 4   ? 0.6040 0.5590 0.3627 0.1187  -0.0491 -0.0418 1   MET   A CE    
9    N  N     . THR   A 5   ? 0.3060 0.4631 0.3031 0.0313  -0.0369 0.0587  2   THR   A N     
10   C  CA    . THR   A 5   ? 0.1772 0.3528 0.3030 -0.0019 -0.0838 0.0461  2   THR   A CA    
11   C  C     . THR   A 5   ? 0.2593 0.3637 0.2436 -0.0149 -0.0765 0.0215  2   THR   A C     
12   O  O     . THR   A 5   ? 0.2845 0.4238 0.2831 -0.1021 -0.0637 -0.0337 2   THR   A O     
13   C  CB    . THR   A 5   ? 0.1994 0.3624 0.3182 -0.0089 -0.0388 0.0295  2   THR   A CB    
14   O  OG1   . THR   A 5   ? 0.2650 0.3563 0.3143 -0.0076 -0.0557 0.0092  2   THR   A OG1   
15   C  CG2   . THR   A 5   ? 0.2913 0.4575 0.3109 0.0140  -0.0277 0.0354  2   THR   A CG2   
16   N  N     . GLU   A 6   ? 0.1277 0.3117 0.2821 0.0330  -0.0606 0.0332  3   GLU   A N     
17   C  CA    . GLU   A 6   ? 0.1926 0.2799 0.2168 0.0420  -0.0494 0.0350  3   GLU   A CA    
18   C  C     . GLU   A 6   ? 0.1380 0.2458 0.1816 0.0092  -0.0532 0.0177  3   GLU   A C     
19   O  O     . GLU   A 6   ? 0.1042 0.3325 0.2659 -0.0051 -0.0638 0.0459  3   GLU   A O     
20   C  CB    . GLU   A 6   ? 0.2784 0.2822 0.2799 0.0732  -0.0422 0.0212  3   GLU   A CB    
21   C  CG    . GLU   A 6   ? 0.2427 0.3530 0.4407 0.0133  -0.0279 -0.0265 3   GLU   A CG    
22   C  CD    . GLU   A 6   ? 0.3562 0.3953 0.4886 0.0173  -0.0634 -0.1461 3   GLU   A CD    
23   O  OE1   . GLU   A 6   ? 0.5118 0.4046 0.6051 -0.1274 -0.0023 -0.1704 3   GLU   A OE1   
24   O  OE2   . GLU   A 6   ? 0.3337 0.4711 0.8224 0.0077  0.0378  -0.1026 3   GLU   A OE2   
25   N  N     . TYR   A 7   ? 0.1273 0.1836 0.1510 0.0471  -0.0447 -0.0241 4   TYR   A N     
26   C  CA    . TYR   A 7   ? 0.1381 0.1767 0.1527 0.0247  -0.0527 -0.0234 4   TYR   A CA    
27   C  C     . TYR   A 7   ? 0.1446 0.1850 0.1442 0.0128  -0.0497 -0.0238 4   TYR   A C     
28   O  O     . TYR   A 7   ? 0.1659 0.1724 0.1618 -0.0020 -0.0284 -0.0388 4   TYR   A O     
29   C  CB    . TYR   A 7   ? 0.1366 0.1766 0.1606 0.0328  -0.0574 -0.0258 4   TYR   A CB    
30   C  CG    . TYR   A 7   ? 0.1544 0.1822 0.1537 0.0296  -0.0524 -0.0327 4   TYR   A CG    
31   C  CD1   . TYR   A 7   ? 0.1743 0.1644 0.1607 0.0158  -0.0497 -0.0212 4   TYR   A CD1   
32   C  CD2   . TYR   A 7   ? 0.2365 0.1756 0.1448 0.0447  -0.0767 -0.0212 4   TYR   A CD2   
33   C  CE1   . TYR   A 7   ? 0.1530 0.1865 0.1374 0.0278  -0.0459 -0.0252 4   TYR   A CE1   
34   C  CE2   . TYR   A 7   ? 0.2438 0.1972 0.1489 0.0241  -0.0519 -0.0371 4   TYR   A CE2   
35   C  CZ    . TYR   A 7   ? 0.1414 0.1970 0.1647 0.0095  -0.0672 -0.0229 4   TYR   A CZ    
36   O  OH    . TYR   A 7   ? 0.2015 0.2011 0.1613 0.0014  -0.0405 -0.0463 4   TYR   A OH    
37   N  N     . LYS   A 8   ? 0.1031 0.1692 0.1532 0.0066  -0.0418 -0.0301 5   LYS   A N     
38   C  CA    . LYS   A 8   ? 0.1305 0.1821 0.1425 0.0109  -0.0574 -0.0266 5   LYS   A CA    
39   C  C     . LYS   A 8   ? 0.1051 0.1591 0.1269 0.0065  -0.0362 -0.0302 5   LYS   A C     
40   O  O     . LYS   A 8   ? 0.0999 0.1693 0.1531 0.0081  -0.0306 -0.0230 5   LYS   A O     
41   C  CB    . LYS   A 8   ? 0.1371 0.1967 0.1812 0.0189  -0.0504 -0.0524 5   LYS   A CB    
42   C  CG    . LYS   A 8   ? 0.1723 0.2256 0.2171 0.0560  -0.0499 -0.0547 5   LYS   A CG    
43   C  CD    . LYS   A 8   ? 0.2149 0.3480 0.2164 0.0622  -0.0213 -0.0317 5   LYS   A CD    
44   C  CE    . LYS   A 8   ? 0.3073 0.4093 0.2916 0.1586  -0.0096 -0.0539 5   LYS   A CE    
45   N  NZ    . LYS   A 8   ? 0.2972 0.4939 0.4757 0.0495  0.0108  -0.0813 5   LYS   A NZ    
46   N  N     . LEU   A 9   ? 0.1075 0.1359 0.1298 0.0113  -0.0336 -0.0185 6   LEU   A N     
47   C  CA    . LEU   A 9   ? 0.1084 0.1347 0.1321 0.0083  -0.0377 -0.0183 6   LEU   A CA    
48   C  C     . LEU   A 9   ? 0.1167 0.1429 0.1072 0.0181  -0.0269 -0.0211 6   LEU   A C     
49   O  O     . LEU   A 9   ? 0.1555 0.1402 0.1474 0.0057  -0.0602 -0.0245 6   LEU   A O     
50   C  CB    . LEU   A 9   ? 0.1003 0.1549 0.1303 0.0163  -0.0448 -0.0209 6   LEU   A CB    
51   C  CG    . LEU   A 9   ? 0.1355 0.1485 0.1361 0.0164  -0.0349 -0.0423 6   LEU   A CG    
52   C  CD1   . LEU   A 9   ? 0.1559 0.1767 0.1443 0.0139  -0.0250 -0.0416 6   LEU   A CD1   
53   C  CD2   . LEU   A 9   ? 0.1814 0.1658 0.1505 -0.0040 -0.0395 -0.0419 6   LEU   A CD2   
54   N  N     . VAL   A 10  ? 0.0998 0.1362 0.1076 0.0205  -0.0382 -0.0295 7   VAL   A N     
55   C  CA    . VAL   A 10  ? 0.1034 0.1439 0.1150 0.0045  -0.0417 -0.0321 7   VAL   A CA    
56   C  C     . VAL   A 10  ? 0.1134 0.1395 0.1241 0.0073  -0.0342 -0.0354 7   VAL   A C     
57   O  O     . VAL   A 10  ? 0.1127 0.1384 0.1473 0.0053  -0.0343 -0.0241 7   VAL   A O     
58   C  CB    . VAL   A 10  ? 0.1072 0.1616 0.1229 0.0154  -0.0326 -0.0306 7   VAL   A CB    
59   C  CG1   . VAL   A 10  ? 0.0813 0.1830 0.1318 0.0230  -0.0312 -0.0434 7   VAL   A CG1   
60   C  CG2   . VAL   A 10  ? 0.1171 0.2017 0.1517 0.0212  -0.0212 -0.0157 7   VAL   A CG2   
61   N  N     . VAL   A 11  ? 0.0957 0.1227 0.1210 0.0161  -0.0409 -0.0266 8   VAL   A N     
62   C  CA    . VAL   A 11  ? 0.0947 0.1270 0.1110 0.0156  -0.0314 -0.0308 8   VAL   A CA    
63   C  C     . VAL   A 11  ? 0.0818 0.1408 0.1076 0.0177  -0.0161 -0.0337 8   VAL   A C     
64   O  O     . VAL   A 11  ? 0.1153 0.1411 0.1148 0.0214  -0.0431 -0.0381 8   VAL   A O     
65   C  CB    . VAL   A 11  ? 0.1216 0.1337 0.1135 -0.0030 -0.0291 -0.0166 8   VAL   A CB    
66   C  CG1   . VAL   A 11  ? 0.1156 0.1755 0.1319 -0.0070 -0.0179 -0.0360 8   VAL   A CG1   
67   C  CG2   . VAL   A 11  ? 0.1140 0.1747 0.1351 -0.0122 -0.0395 -0.0240 8   VAL   A CG2   
68   N  N     . VAL   A 12  ? 0.1017 0.1304 0.1054 0.0006  -0.0199 -0.0367 9   VAL   A N     
69   C  CA    . VAL   A 12  ? 0.1115 0.1415 0.0963 0.0200  -0.0099 -0.0299 9   VAL   A CA    
70   C  C     . VAL   A 12  ? 0.0850 0.1569 0.0940 0.0008  -0.0105 -0.0257 9   VAL   A C     
71   O  O     . VAL   A 12  ? 0.0857 0.1647 0.1074 0.0093  -0.0163 -0.0316 9   VAL   A O     
72   C  CB    . VAL   A 12  ? 0.0963 0.1657 0.1205 0.0182  -0.0084 -0.0188 9   VAL   A CB    
73   C  CG1   . VAL   A 12  ? 0.1047 0.1886 0.1388 0.0265  -0.0157 -0.0162 9   VAL   A CG1   
74   C  CG2   . VAL   A 12  ? 0.0951 0.1755 0.1338 0.0029  -0.0098 -0.0113 9   VAL   A CG2   
75   N  N     . GLY   A 13  ? 0.1029 0.1440 0.0932 0.0224  -0.0177 -0.0324 10  GLY   A N     
76   C  CA    . GLY   A 13  ? 0.1030 0.1697 0.1142 0.0244  -0.0242 -0.0378 10  GLY   A CA    
77   C  C     . GLY   A 13  ? 0.0960 0.1764 0.0970 0.0153  -0.0191 -0.0309 10  GLY   A C     
78   O  O     . GLY   A 13  ? 0.0966 0.1711 0.1066 0.0106  -0.0047 -0.0367 10  GLY   A O     
79   N  N     . ALA   A 14  ? 0.0714 0.1801 0.1090 0.0066  -0.0098 -0.0252 11  ALA   A N     
80   C  CA    . ALA   A 14  ? 0.0933 0.1888 0.1050 0.0032  -0.0180 -0.0304 11  ALA   A CA    
81   C  C     . ALA   A 14  ? 0.0851 0.1895 0.0965 0.0175  -0.0401 -0.0255 11  ALA   A C     
82   O  O     . ALA   A 14  ? 0.0996 0.1991 0.1006 0.0022  -0.0281 -0.0418 11  ALA   A O     
83   C  CB    . ALA   A 14  ? 0.1062 0.1953 0.1071 0.0115  -0.0110 -0.0229 11  ALA   A CB    
84   N  N     . GLY   A 15  ? 0.1304 0.2176 0.1146 -0.0312 0.0033  -0.0502 12  GLY   A N     
85   C  CA    . GLY   A 15  ? 0.1651 0.2063 0.1237 -0.0225 0.0079  -0.0276 12  GLY   A CA    
86   C  C     . GLY   A 15  ? 0.1414 0.1913 0.1198 -0.0197 -0.0199 -0.0364 12  GLY   A C     
87   O  O     . GLY   A 15  ? 0.1389 0.2332 0.1317 -0.0226 -0.0403 -0.0128 12  GLY   A O     
88   N  N     . GLY   A 16  ? 0.1335 0.2001 0.1257 -0.0252 0.0006  -0.0425 13  GLY   A N     
89   C  CA    . GLY   A 16  ? 0.1033 0.2024 0.1415 -0.0190 -0.0135 -0.0455 13  GLY   A CA    
90   C  C     . GLY   A 16  ? 0.1204 0.1934 0.1349 -0.0376 -0.0056 -0.0371 13  GLY   A C     
91   O  O     . GLY   A 16  ? 0.1237 0.2062 0.1536 -0.0361 0.0056  -0.0542 13  GLY   A O     
92   N  N     . VAL   A 17  ? 0.1272 0.1704 0.0986 -0.0297 -0.0029 -0.0224 14  VAL   A N     
93   C  CA    . VAL   A 17  ? 0.0967 0.1742 0.1028 -0.0139 -0.0029 -0.0238 14  VAL   A CA    
94   C  C     . VAL   A 17  ? 0.1090 0.1361 0.1022 -0.0352 -0.0171 -0.0190 14  VAL   A C     
95   O  O     . VAL   A 17  ? 0.1139 0.1496 0.1036 -0.0204 -0.0019 -0.0187 14  VAL   A O     
96   C  CB    . VAL   A 17  ? 0.0896 0.1660 0.1015 -0.0078 0.0049  -0.0124 14  VAL   A CB    
97   C  CG1   . VAL   A 17  ? 0.0734 0.1797 0.1097 -0.0104 0.0144  -0.0126 14  VAL   A CG1   
98   C  CG2   . VAL   A 17  ? 0.0847 0.1663 0.1043 -0.0141 -0.0091 -0.0247 14  VAL   A CG2   
99   N  N     . GLY   A 18  ? 0.0968 0.1400 0.1098 -0.0249 0.0082  -0.0118 15  GLY   A N     
100  C  CA    . GLY   A 18  ? 0.1314 0.1531 0.1050 -0.0099 0.0019  -0.0114 15  GLY   A CA    
101  C  C     . GLY   A 18  ? 0.1344 0.1338 0.1212 -0.0172 -0.0091 -0.0243 15  GLY   A C     
102  O  O     . GLY   A 18  ? 0.1725 0.1449 0.1066 -0.0004 -0.0157 -0.0060 15  GLY   A O     
103  N  N     . LYS   A 19  ? 0.1239 0.1408 0.1098 -0.0304 -0.0152 -0.0152 16  LYS   A N     
104  C  CA    . LYS   A 19  ? 0.1256 0.1506 0.1115 -0.0267 -0.0313 -0.0105 16  LYS   A CA    
105  C  C     . LYS   A 19  ? 0.1448 0.1323 0.1145 -0.0071 -0.0350 -0.0228 16  LYS   A C     
106  O  O     . LYS   A 19  ? 0.1503 0.1408 0.1394 -0.0165 -0.0587 -0.0123 16  LYS   A O     
107  C  CB    . LYS   A 19  ? 0.1264 0.1505 0.1049 -0.0250 -0.0324 -0.0055 16  LYS   A CB    
108  C  CG    . LYS   A 19  ? 0.1412 0.1660 0.1169 -0.0352 -0.0440 0.0027  16  LYS   A CG    
109  C  CD    . LYS   A 19  ? 0.1602 0.2236 0.1363 -0.0079 -0.0217 0.0296  16  LYS   A CD    
110  C  CE    . LYS   A 19  ? 0.1289 0.2253 0.1306 0.0296  -0.0168 0.0171  16  LYS   A CE    
111  N  NZ    . LYS   A 19  ? 0.1065 0.2043 0.1311 0.0189  -0.0105 -0.0156 16  LYS   A NZ    
112  N  N     . SER   A 20  ? 0.1336 0.1412 0.1201 -0.0189 -0.0335 -0.0065 17  SER   A N     
113  C  CA    . SER   A 20  ? 0.1449 0.1417 0.1328 -0.0153 -0.0309 -0.0058 17  SER   A CA    
114  C  C     . SER   A 20  ? 0.1921 0.1273 0.1373 -0.0186 -0.0131 -0.0059 17  SER   A C     
115  O  O     . SER   A 20  ? 0.1980 0.1473 0.1364 -0.0028 -0.0138 -0.0177 17  SER   A O     
116  C  CB    . SER   A 20  ? 0.1653 0.1350 0.1483 -0.0236 -0.0286 -0.0091 17  SER   A CB    
117  O  OG    . SER   A 20  ? 0.1976 0.1540 0.1523 -0.0377 -0.0249 -0.0332 17  SER   A OG    
118  N  N     . ALA   A 21  ? 0.1917 0.1338 0.1151 -0.0162 -0.0095 0.0001  18  ALA   A N     
119  C  CA    . ALA   A 21  ? 0.1703 0.1323 0.1500 -0.0122 0.0063  -0.0050 18  ALA   A CA    
120  C  C     . ALA   A 21  ? 0.1792 0.1391 0.1244 -0.0106 -0.0046 0.0117  18  ALA   A C     
121  O  O     . ALA   A 21  ? 0.2045 0.1560 0.1284 -0.0291 -0.0080 0.0045  18  ALA   A O     
122  C  CB    . ALA   A 21  ? 0.1529 0.1563 0.1341 -0.0249 0.0189  -0.0369 18  ALA   A CB    
123  N  N     . LEU   A 22  ? 0.1620 0.1437 0.1145 -0.0244 -0.0148 -0.0025 19  LEU   A N     
124  C  CA    . LEU   A 22  ? 0.1762 0.1354 0.1210 -0.0076 -0.0254 -0.0130 19  LEU   A CA    
125  C  C     . LEU   A 22  ? 0.1778 0.1504 0.1032 0.0141  0.0050  0.0175  19  LEU   A C     
126  O  O     . LEU   A 22  ? 0.1800 0.1599 0.1156 -0.0173 -0.0224 0.0090  19  LEU   A O     
127  C  CB    . LEU   A 22  ? 0.1823 0.1315 0.1217 -0.0096 -0.0288 -0.0061 19  LEU   A CB    
128  C  CG    . LEU   A 22  ? 0.1939 0.1260 0.1474 -0.0137 -0.0409 -0.0004 19  LEU   A CG    
129  C  CD1   . LEU   A 22  ? 0.2162 0.1324 0.1535 0.0017  -0.0313 0.0124  19  LEU   A CD1   
130  C  CD2   . LEU   A 22  ? 0.2221 0.1431 0.1521 -0.0048 -0.0365 0.0047  19  LEU   A CD2   
131  N  N     . THR   A 23  ? 0.1676 0.1293 0.1556 0.0002  -0.0315 -0.0234 20  THR   A N     
132  C  CA    . THR   A 23  ? 0.2117 0.1447 0.1326 0.0199  -0.0392 0.0077  20  THR   A CA    
133  C  C     . THR   A 23  ? 0.1996 0.1464 0.1187 0.0128  -0.0056 -0.0154 20  THR   A C     
134  O  O     . THR   A 23  ? 0.2616 0.1584 0.1308 -0.0010 -0.0384 -0.0007 20  THR   A O     
135  C  CB    . THR   A 23  ? 0.1876 0.1515 0.1588 -0.0001 -0.0224 -0.0064 20  THR   A CB    
136  O  OG1   . THR   A 23  ? 0.1698 0.1979 0.1432 -0.0086 -0.0117 -0.0026 20  THR   A OG1   
137  C  CG2   . THR   A 23  ? 0.1837 0.1903 0.1711 0.0067  -0.0303 0.0122  20  THR   A CG2   
138  N  N     . ILE   A 24  ? 0.2442 0.1501 0.1324 -0.0141 -0.0560 0.0223  21  ILE   A N     
139  C  CA    . ILE   A 24  ? 0.2917 0.1290 0.1477 -0.0112 -0.0300 0.0164  21  ILE   A CA    
140  C  C     . ILE   A 24  ? 0.2325 0.1732 0.1565 -0.0231 -0.0137 0.0144  21  ILE   A C     
141  O  O     . ILE   A 24  ? 0.3100 0.1542 0.1754 -0.0112 -0.0154 0.0270  21  ILE   A O     
142  C  CB    . ILE   A 24  ? 0.2552 0.1533 0.1892 -0.0199 -0.0141 0.0192  21  ILE   A CB    
143  C  CG1   . ILE   A 24  ? 0.3579 0.1610 0.1640 -0.0297 -0.0083 0.0014  21  ILE   A CG1   
144  C  CG2   . ILE   A 24  ? 0.2612 0.1732 0.1824 -0.0500 -0.0220 0.0075  21  ILE   A CG2   
145  C  CD1   . ILE   A 24  ? 0.3428 0.2184 0.2227 -0.0588 0.0052  -0.0267 21  ILE   A CD1   
146  N  N     . GLN   A 25  ? 0.2668 0.1683 0.1123 -0.0138 -0.0389 0.0000  22  GLN   A N     
147  C  CA    . GLN   A 25  ? 0.2818 0.1331 0.1466 -0.0406 -0.0033 0.0160  22  GLN   A CA    
148  C  C     . GLN   A 25  ? 0.3222 0.1665 0.1141 -0.0500 -0.0083 -0.0162 22  GLN   A C     
149  O  O     . GLN   A 25  ? 0.3362 0.1634 0.1181 -0.0297 -0.0055 0.0119  22  GLN   A O     
150  C  CB    . GLN   A 25  ? 0.2631 0.1829 0.1744 -0.0174 -0.0271 -0.0003 22  GLN   A CB    
151  C  CG    . GLN   A 25  ? 0.2660 0.2468 0.1542 -0.0201 -0.0162 0.0359  22  GLN   A CG    
152  C  CD    . GLN   A 25  ? 0.2886 0.2531 0.1765 -0.0565 0.0038  0.0727  22  GLN   A CD    
153  O  OE1   . GLN   A 25  ? 0.2203 0.2727 0.1825 -0.0630 0.0132  0.0515  22  GLN   A OE1   
154  N  NE2   . GLN   A 25  ? 0.2891 0.2562 0.1486 -0.0708 0.0280  0.0381  22  GLN   A NE2   
155  N  N     . LEU   A 26  ? 0.2942 0.1645 0.1323 -0.0451 -0.0278 0.0036  23  LEU   A N     
156  C  CA    . LEU   A 26  ? 0.2873 0.1728 0.1394 -0.0232 -0.0370 -0.0184 23  LEU   A CA    
157  C  C     . LEU   A 26  ? 0.3527 0.1895 0.1219 0.0064  -0.0123 -0.0110 23  LEU   A C     
158  O  O     . LEU   A 26  ? 0.4035 0.2059 0.1341 -0.0112 -0.0560 0.0173  23  LEU   A O     
159  C  CB    . LEU   A 26  ? 0.2655 0.1667 0.1405 0.0094  -0.0320 -0.0153 23  LEU   A CB    
160  C  CG    . LEU   A 26  ? 0.2374 0.1803 0.1766 0.0061  -0.0319 -0.0048 23  LEU   A CG    
161  C  CD1   . LEU   A 26  ? 0.2086 0.1778 0.1632 -0.0027 -0.0250 -0.0082 23  LEU   A CD1   
162  C  CD2   . LEU   A 26  ? 0.2423 0.2178 0.2325 -0.0048 -0.0205 -0.0193 23  LEU   A CD2   
163  N  N     . ILE   A 27  ? 0.3337 0.1711 0.1506 0.0386  -0.0317 -0.0045 24  ILE   A N     
164  C  CA    . ILE   A 27  ? 0.3323 0.2492 0.1625 0.0660  -0.0679 0.0150  24  ILE   A CA    
165  C  C     . ILE   A 27  ? 0.3286 0.2093 0.1716 0.0795  -0.0315 0.0047  24  ILE   A C     
166  O  O     . ILE   A 27  ? 0.4227 0.2702 0.1943 0.0600  -0.0501 0.0511  24  ILE   A O     
167  C  CB    . ILE   A 27  ? 0.3867 0.3021 0.2059 0.1294  -0.0698 -0.0078 24  ILE   A CB    
168  C  CG1   . ILE   A 27  ? 0.3314 0.3610 0.2391 0.1548  -0.0528 0.0255  24  ILE   A CG1   
169  C  CG2   . ILE   A 27  ? 0.3616 0.3188 0.2575 0.1364  -0.0561 0.0233  24  ILE   A CG2   
170  C  CD1   . ILE   A 27  ? 0.3992 0.3862 0.2094 0.1079  -0.0559 0.0441  24  ILE   A CD1   
171  N  N     . GLN   A 28  ? 0.3802 0.2283 0.2274 0.0204  -0.0831 0.0531  25  GLN   A N     
172  C  CA    . GLN   A 28  ? 0.4611 0.1900 0.2122 0.0303  -0.0496 0.0563  25  GLN   A CA    
173  C  C     . GLN   A 28  ? 0.4234 0.2119 0.2114 0.0065  -0.0254 0.0655  25  GLN   A C     
174  O  O     . GLN   A 28  ? 0.4876 0.2253 0.2945 -0.0431 -0.0256 0.0647  25  GLN   A O     
175  C  CB    . GLN   A 28  ? 0.4866 0.2575 0.1321 0.0516  -0.0517 0.0395  25  GLN   A CB    
176  C  CG    . GLN   A 28  ? 0.4190 0.2645 0.3314 0.0633  -0.0787 -0.0136 25  GLN   A CG    
177  C  CD    . GLN   A 28  ? 0.4346 0.2754 0.3651 0.0602  -0.0982 -0.0294 25  GLN   A CD    
178  O  OE1   . GLN   A 28  ? 0.4851 0.2965 0.3978 0.0900  -0.1974 -0.0378 25  GLN   A OE1   
179  N  NE2   . GLN   A 28  ? 0.4469 0.2915 0.5151 0.1040  -0.1059 -0.0470 25  GLN   A NE2   
180  N  N     . ASN   A 29  ? 0.4229 0.1924 0.2150 -0.0360 -0.0042 0.0269  26  ASN   A N     
181  C  CA    . ASN   A 29  ? 0.4414 0.2068 0.1692 -0.0536 0.0229  0.0487  26  ASN   A CA    
182  C  C     . ASN   A 29  ? 0.4749 0.2801 0.1602 -0.0931 0.0223  0.0602  26  ASN   A C     
183  O  O     . ASN   A 29  ? 0.4888 0.3478 0.2095 -0.1518 0.0486  0.0329  26  ASN   A O     
184  C  CB    . ASN   A 29  ? 0.4525 0.2617 0.1668 -0.0881 0.0091  0.0411  26  ASN   A CB    
185  C  CG    . ASN   A 29  ? 0.4964 0.3582 0.1872 -0.0513 0.0267  0.0487  26  ASN   A CG    
186  O  OD1   . ASN   A 29  ? 0.5117 0.5091 0.1834 -0.0325 -0.0166 0.0662  26  ASN   A OD1   
187  N  ND2   . ASN   A 29  ? 0.5484 0.4472 0.2044 -0.0980 -0.0281 0.0861  26  ASN   A ND2   
188  N  N     . HIS   A 30  ? 0.3230 0.2739 0.1712 -0.0778 0.0113  0.0527  27  HIS   A N     
189  C  CA    . HIS   A 30  ? 0.3161 0.2248 0.1890 -0.0695 0.0239  0.0263  27  HIS   A CA    
190  C  C     . HIS   A 30  ? 0.2610 0.2612 0.1619 -0.0612 0.0320  -0.0127 27  HIS   A C     
191  O  O     . HIS   A 30  ? 0.3009 0.2225 0.1688 -0.0420 0.0550  0.0322  27  HIS   A O     
192  C  CB    . HIS   A 30  ? 0.3824 0.2191 0.1941 -0.0593 0.0674  0.0503  27  HIS   A CB    
193  C  CG    . HIS   A 30  ? 0.4041 0.2140 0.2148 -0.0272 0.0695  0.0774  27  HIS   A CG    
194  N  ND1   . HIS   A 30  ? 0.4155 0.2148 0.2531 -0.0537 0.0710  0.0561  27  HIS   A ND1   
195  C  CD2   . HIS   A 30  ? 0.3846 0.2639 0.2978 -0.0590 0.0245  0.0028  27  HIS   A CD2   
196  C  CE1   . HIS   A 30  ? 0.4527 0.2154 0.2722 -0.0313 0.0286  -0.0574 27  HIS   A CE1   
197  N  NE2   . HIS   A 30  ? 0.4218 0.2231 0.2383 -0.0798 0.0379  0.0503  27  HIS   A NE2   
198  N  N     . PHE   A 31  ? 0.2767 0.3171 0.1693 -0.0531 0.0195  0.0474  28  PHE   A N     
199  C  CA    . PHE   A 31  ? 0.2333 0.2453 0.1616 -0.0392 0.0162  -0.0032 28  PHE   A CA    
200  C  C     . PHE   A 31  ? 0.2996 0.2369 0.2042 -0.1079 0.0355  0.0099  28  PHE   A C     
201  O  O     . PHE   A 31  ? 0.3097 0.2372 0.2699 -0.0944 0.0864  -0.0023 28  PHE   A O     
202  C  CB    . PHE   A 31  ? 0.1898 0.2200 0.1791 -0.0589 0.0554  -0.0283 28  PHE   A CB    
203  C  CG    . PHE   A 31  ? 0.2428 0.2273 0.1963 -0.0657 0.0327  -0.0240 28  PHE   A CG    
204  C  CD1   . PHE   A 31  ? 0.1981 0.2469 0.1928 -0.0706 0.0302  -0.0327 28  PHE   A CD1   
205  C  CD2   . PHE   A 31  ? 0.2360 0.3073 0.1693 -0.0874 0.0574  -0.0069 28  PHE   A CD2   
206  C  CE1   . PHE   A 31  ? 0.2209 0.2208 0.2161 -0.0631 0.0403  -0.0116 28  PHE   A CE1   
207  C  CE2   . PHE   A 31  ? 0.1932 0.2427 0.2088 -0.0721 0.0286  -0.0233 28  PHE   A CE2   
208  C  CZ    . PHE   A 31  ? 0.2202 0.2880 0.1836 -0.0557 0.0545  -0.0221 28  PHE   A CZ    
209  N  N     . VAL   A 32  ? 0.2959 0.1999 0.1770 -0.0853 0.0096  0.0134  29  VAL   A N     
210  C  CA    . VAL   A 32  ? 0.3609 0.2177 0.2286 -0.0929 0.0172  -0.0205 29  VAL   A CA    
211  C  C     . VAL   A 32  ? 0.4667 0.2401 0.2118 -0.1230 -0.0209 0.0056  29  VAL   A C     
212  O  O     . VAL   A 32  ? 0.5684 0.2636 0.2062 -0.1888 -0.0496 0.0169  29  VAL   A O     
213  C  CB    . VAL   A 32  ? 0.3354 0.2589 0.3120 -0.0677 -0.0417 -0.0413 29  VAL   A CB    
214  C  CG1   . VAL   A 32  ? 0.3838 0.2228 0.3607 -0.0334 -0.0174 0.0049  29  VAL   A CG1   
215  C  CG2   . VAL   A 32  ? 0.4130 0.2359 0.3034 -0.0661 -0.0449 -0.0332 29  VAL   A CG2   
216  N  N     . ASP   A 33  ? 0.5230 0.2899 0.2849 -0.1750 -0.0707 -0.0003 30  ASP   A N     
217  C  CA    . ASP   A 33  ? 0.4584 0.3672 0.3312 -0.2093 -0.0603 -0.0245 30  ASP   A CA    
218  C  C     . ASP   A 33  ? 0.4521 0.3226 0.2527 -0.2114 -0.0299 0.0502  30  ASP   A C     
219  O  O     . ASP   A 33  ? 0.4835 0.3482 0.2886 -0.2632 -0.0841 0.0717  30  ASP   A O     
220  C  CB    . ASP   A 33  ? 0.4939 0.4907 0.3434 -0.1811 0.0878  -0.0229 30  ASP   A CB    
221  C  CG    . ASP   A 33  ? 0.5459 0.6235 0.5213 -0.0988 0.1135  -0.0432 30  ASP   A CG    
222  O  OD1   . ASP   A 33  ? 0.7869 0.7485 0.5672 -0.0783 0.0469  -0.1118 30  ASP   A OD1   
223  O  OD2   . ASP   A 33  ? 0.6224 0.8196 0.6380 -0.0605 0.2377  -0.0727 30  ASP   A OD2   
224  N  N     . GLU   A 34  ? 0.3909 0.3499 0.3456 -0.1834 -0.0221 -0.0544 31  GLU   A N     
225  C  CA    . GLU   A 34  ? 0.3368 0.4427 0.3390 -0.1048 0.0603  -0.0656 31  GLU   A CA    
226  C  C     . GLU   A 34  ? 0.3156 0.3317 0.4965 -0.1460 0.0610  -0.0298 31  GLU   A C     
227  O  O     . GLU   A 34  ? 0.4942 0.3570 0.6259 -0.2067 0.0608  -0.1102 31  GLU   A O     
228  C  CB    . GLU   A 34  ? 0.4290 0.4391 0.4459 -0.1554 0.0469  -0.1616 31  GLU   A CB    
229  C  CG    . GLU   A 34  ? 0.3829 0.4762 0.5867 -0.2117 0.0894  -0.1273 31  GLU   A CG    
230  C  CD    . GLU   A 34  ? 0.3744 0.6375 0.7115 -0.2496 0.1210  -0.0671 31  GLU   A CD    
231  O  OE1   . GLU   A 34  ? 0.5211 0.7994 0.7170 -0.2106 0.0113  -0.0944 31  GLU   A OE1   
232  O  OE2   . GLU   A 34  ? 0.6106 0.6889 0.7181 -0.1974 -0.0477 -0.0949 31  GLU   A OE2   
233  N  N     . TYR   A 35  ? 0.3137 0.2996 0.3894 -0.1392 -0.0528 -0.0774 32  TYR   A N     
234  C  CA    . TYR   A 35  ? 0.3714 0.2428 0.3097 -0.1050 0.0196  -0.0521 32  TYR   A CA    
235  C  C     . TYR   A 35  ? 0.3292 0.2345 0.3177 -0.0690 0.0416  -0.0412 32  TYR   A C     
236  O  O     . TYR   A 35  ? 0.3209 0.2023 0.2757 -0.0779 0.0098  -0.0708 32  TYR   A O     
237  C  CB    . TYR   A 35  ? 0.2781 0.2579 0.2459 -0.0791 0.0408  -0.0509 32  TYR   A CB    
238  C  CG    . TYR   A 35  ? 0.3776 0.2368 0.2387 -0.0576 -0.0193 -0.0389 32  TYR   A CG    
239  C  CD1   . TYR   A 35  ? 0.4217 0.2402 0.2775 -0.0862 0.0192  -0.0082 32  TYR   A CD1   
240  C  CD2   . TYR   A 35  ? 0.4204 0.1467 0.2152 -0.0423 0.0272  -0.0402 32  TYR   A CD2   
241  C  CE1   . TYR   A 35  ? 0.4833 0.3138 0.3468 0.0040  0.0287  -0.0153 32  TYR   A CE1   
242  C  CE2   . TYR   A 35  ? 0.4548 0.2364 0.3149 0.0260  0.0438  -0.0231 32  TYR   A CE2   
243  C  CZ    . TYR   A 35  ? 0.4444 0.2426 0.3128 0.0181  0.0107  -0.0196 32  TYR   A CZ    
244  O  OH    . TYR   A 35  ? 0.4951 0.3508 0.4771 0.0976  0.0507  0.0879  32  TYR   A OH    
245  N  N     . ASP   A 36  ? 0.2873 0.2352 0.2688 -0.0729 -0.0006 -0.0447 33  ASP   A N     
246  C  CA    . ASP   A 36  ? 0.2541 0.2112 0.2580 -0.0563 0.0197  -0.0184 33  ASP   A CA    
247  C  C     . ASP   A 36  ? 0.1673 0.2056 0.2587 -0.0523 -0.0108 -0.0500 33  ASP   A C     
248  O  O     . ASP   A 36  ? 0.1794 0.1932 0.2495 -0.0473 -0.0194 -0.0463 33  ASP   A O     
249  C  CB    . ASP   A 36  ? 0.3060 0.2081 0.3278 -0.0503 -0.0138 -0.0440 33  ASP   A CB    
250  C  CG    . ASP   A 36  ? 0.2851 0.2280 0.3158 -0.0181 -0.0113 -0.0464 33  ASP   A CG    
251  O  OD1   . ASP   A 36  ? 0.3614 0.2451 0.2961 -0.0655 0.0159  -0.0779 33  ASP   A OD1   
252  O  OD2   . ASP   A 36  ? 0.5243 0.2484 0.3598 -0.1026 -0.0260 -0.0232 33  ASP   A OD2   
253  N  N     . PRO   A 37  ? 0.2543 0.1857 0.2445 -0.0318 -0.0423 -0.0699 34  PRO   A N     
254  C  CA    . PRO   A 37  ? 0.2157 0.1994 0.2264 -0.0080 -0.0177 -0.0651 34  PRO   A CA    
255  C  C     . PRO   A 37  ? 0.2330 0.2059 0.2035 -0.0051 -0.0266 -0.0667 34  PRO   A C     
256  O  O     . PRO   A 37  ? 0.2520 0.2159 0.2050 -0.0265 -0.0165 -0.0595 34  PRO   A O     
257  C  CB    . PRO   A 37  ? 0.2579 0.2541 0.2799 0.0142  -0.0381 -0.0482 34  PRO   A CB    
258  C  CG    . PRO   A 37  ? 0.2605 0.3024 0.2846 -0.0223 -0.0830 -0.0141 34  PRO   A CG    
259  C  CD    . PRO   A 37  ? 0.2318 0.2296 0.2979 -0.0168 -0.0500 -0.0252 34  PRO   A CD    
260  N  N     . THR   A 38  ? 0.2309 0.2010 0.1962 -0.0184 -0.0321 -0.0746 35  THR   A N     
261  C  CA    . THR   A 38  ? 0.2240 0.2320 0.1923 -0.0499 -0.0043 -0.0757 35  THR   A CA    
262  C  C     . THR   A 38  ? 0.2170 0.2043 0.2079 -0.0473 -0.0123 -0.0690 35  THR   A C     
263  O  O     . THR   A 38  ? 0.2240 0.2612 0.2069 -0.0232 -0.0038 -0.0748 35  THR   A O     
264  C  CB    . THR   A 38  ? 0.2809 0.2846 0.2135 -0.0773 -0.0180 -0.1119 35  THR   A CB    
265  O  OG1   . THR   A 38  ? 0.3323 0.2266 0.3256 -0.0517 -0.0106 -0.1107 35  THR   A OG1   
266  C  CG2   . THR   A 38  ? 0.2590 0.2965 0.2324 -0.0731 -0.0029 -0.0993 35  THR   A CG2   
267  N  N     . ILE   A 39  ? 0.2442 0.1712 0.2119 -0.0054 -0.0337 -0.0719 36  ILE   A N     
268  C  CA    . ILE   A 39  ? 0.2442 0.1607 0.2119 -0.0222 -0.0228 -0.0405 36  ILE   A CA    
269  C  C     . ILE   A 39  ? 0.2075 0.1530 0.1903 -0.0097 -0.0050 -0.0461 36  ILE   A C     
270  O  O     . ILE   A 39  ? 0.2115 0.1557 0.2194 -0.0147 -0.0287 -0.0512 36  ILE   A O     
271  C  CB    . ILE   A 39  ? 0.2287 0.1385 0.2297 0.0189  -0.0003 -0.0219 36  ILE   A CB    
272  C  CG1   . ILE   A 39  ? 0.2266 0.1767 0.2411 -0.0043 -0.0097 -0.0478 36  ILE   A CG1   
273  C  CG2   . ILE   A 39  ? 0.2644 0.1768 0.2240 0.0076  -0.0019 0.0084  36  ILE   A CG2   
274  C  CD1   . ILE   A 39  ? 0.2465 0.1956 0.2697 -0.0141 -0.0075 -0.0048 36  ILE   A CD1   
275  N  N     . GLU   A 40  ? 0.2062 0.1477 0.1815 0.0076  -0.0266 -0.0470 37  GLU   A N     
276  C  CA    . GLU   A 40  ? 0.2484 0.1483 0.1966 0.0051  -0.0454 -0.0431 37  GLU   A CA    
277  C  C     . GLU   A 40  ? 0.2390 0.1668 0.1724 0.0030  -0.0367 -0.0509 37  GLU   A C     
278  O  O     . GLU   A 40  ? 0.2629 0.1682 0.2332 0.0271  -0.0837 -0.0512 37  GLU   A O     
279  C  CB    . GLU   A 40  ? 0.1867 0.1932 0.2054 0.0142  -0.0493 -0.0445 37  GLU   A CB    
280  C  CG    . GLU   A 40  ? 0.1885 0.1717 0.1788 0.0188  -0.0443 -0.0616 37  GLU   A CG    
281  C  CD    . GLU   A 40  ? 0.1448 0.1932 0.1902 0.0224  -0.0410 -0.0436 37  GLU   A CD    
282  O  OE1   . GLU   A 40  ? 0.1998 0.2129 0.1857 0.0564  -0.0535 -0.0585 37  GLU   A OE1   
283  O  OE2   . GLU   A 40  ? 0.1844 0.2589 0.2389 0.0650  -0.0216 -0.0666 37  GLU   A OE2   
284  N  N     . ASP   A 41  ? 0.2139 0.1563 0.1739 0.0051  -0.0406 -0.0449 38  ASP   A N     
285  C  CA    . ASP   A 41  ? 0.2540 0.1438 0.1936 0.0309  -0.0520 -0.0363 38  ASP   A CA    
286  C  C     . ASP   A 41  ? 0.1840 0.1466 0.2019 0.0093  -0.0462 -0.0298 38  ASP   A C     
287  O  O     . ASP   A 41  ? 0.2321 0.1404 0.1845 0.0145  -0.0324 -0.0282 38  ASP   A O     
288  C  CB    . ASP   A 41  ? 0.2939 0.1964 0.2083 -0.0041 -0.0391 -0.0267 38  ASP   A CB    
289  C  CG    . ASP   A 41  ? 0.2711 0.1955 0.2990 0.0003  -0.0892 -0.0606 38  ASP   A CG    
290  O  OD1   . ASP   A 41  ? 0.2820 0.1801 0.2872 0.0157  -0.1117 -0.0381 38  ASP   A OD1   
291  O  OD2   . ASP   A 41  ? 0.4210 0.2894 0.4792 -0.0777 -0.0465 0.0101  38  ASP   A OD2   
292  N  N     . SER   A 42  ? 0.2406 0.1407 0.1643 0.0338  -0.0546 -0.0294 39  SER   A N     
293  C  CA    . SER   A 42  ? 0.2122 0.1393 0.1902 0.0234  -0.0196 -0.0442 39  SER   A CA    
294  C  C     . SER   A 42  ? 0.2531 0.1386 0.1872 0.0296  -0.0259 -0.0186 39  SER   A C     
295  O  O     . SER   A 42  ? 0.3004 0.1614 0.1996 -0.0155 -0.0515 -0.0171 39  SER   A O     
296  C  CB    . SER   A 42  ? 0.2077 0.2370 0.2274 0.0076  -0.0298 -0.0364 39  SER   A CB    
297  O  OG    . SER   A 42  ? 0.3395 0.2480 0.2695 0.0563  -0.0338 -0.0409 39  SER   A OG    
298  N  N     . TYR   A 43  ? 0.2822 0.1498 0.1652 -0.0152 -0.0565 -0.0323 40  TYR   A N     
299  C  CA    . TYR   A 43  ? 0.3387 0.1599 0.2015 -0.0207 -0.0095 -0.0079 40  TYR   A CA    
300  C  C     . TYR   A 43  ? 0.3575 0.1640 0.1704 -0.0439 0.0159  -0.0206 40  TYR   A C     
301  O  O     . TYR   A 43  ? 0.3338 0.1637 0.1587 -0.0285 -0.0359 -0.0001 40  TYR   A O     
302  C  CB    . TYR   A 43  ? 0.3296 0.2371 0.2705 -0.0359 0.0033  -0.0380 40  TYR   A CB    
303  C  CG    . TYR   A 43  ? 0.3108 0.2583 0.3787 -0.0626 -0.0034 -0.0172 40  TYR   A CG    
304  C  CD1   . TYR   A 43  ? 0.2492 0.2508 0.3903 -0.0366 -0.0247 -0.0171 40  TYR   A CD1   
305  C  CD2   . TYR   A 43  ? 0.3020 0.4100 0.3986 -0.0830 -0.0140 -0.0030 40  TYR   A CD2   
306  C  CE1   . TYR   A 43  ? 0.2584 0.3481 0.4418 -0.0523 -0.0856 0.0203  40  TYR   A CE1   
307  C  CE2   . TYR   A 43  ? 0.3434 0.3758 0.3739 -0.0922 -0.0154 -0.0060 40  TYR   A CE2   
308  C  CZ    . TYR   A 43  ? 0.3922 0.3977 0.3619 -0.1053 -0.0315 -0.0341 40  TYR   A CZ    
309  O  OH    . TYR   A 43  ? 0.4201 0.3961 0.3874 -0.0988 -0.0253 -0.1195 40  TYR   A OH    
310  N  N     . ARG   A 44  ? 0.4429 0.1639 0.1870 -0.0952 -0.0293 0.0011  41  ARG   A N     
311  C  CA    . ARG   A 44  ? 0.4628 0.1996 0.2332 -0.1173 -0.0533 0.0253  41  ARG   A CA    
312  C  C     . ARG   A 44  ? 0.4695 0.2018 0.2222 -0.1122 -0.0400 0.0472  41  ARG   A C     
313  O  O     . ARG   A 44  ? 0.5244 0.2745 0.2278 -0.1951 -0.0609 0.0315  41  ARG   A O     
314  C  CB    . ARG   A 44  ? 0.5146 0.2621 0.3476 -0.0406 -0.0485 0.1032  41  ARG   A CB    
315  C  CG    . ARG   A 44  ? 0.4822 0.3364 0.3536 -0.0276 -0.0659 0.1555  41  ARG   A CG    
316  C  CD    . ARG   A 44  ? 0.5285 0.3544 0.3862 -0.0063 -0.0922 0.0965  41  ARG   A CD    
317  N  NE    . ARG   A 44  ? 0.4874 0.4128 0.4508 0.0603  -0.0686 0.1322  41  ARG   A NE    
318  C  CZ    . ARG   A 44  ? 0.4716 0.4788 0.4186 0.0771  -0.0416 0.1946  41  ARG   A CZ    
319  N  NH1   . ARG   A 44  ? 0.3857 0.5171 0.4294 0.1315  0.0091  0.2096  41  ARG   A NH1   
320  N  NH2   . ARG   A 44  ? 0.4672 0.5243 0.3727 -0.0334 0.0070  0.2421  41  ARG   A NH2   
321  N  N     . LYS   A 45  ? 0.2900 0.2166 0.1833 -0.0966 -0.0344 0.0434  42  LYS   A N     
322  C  CA    . LYS   A 45  ? 0.2829 0.2499 0.1806 -0.0675 -0.0660 0.0359  42  LYS   A CA    
323  C  C     . LYS   A 45  ? 0.2473 0.2140 0.1611 -0.0477 -0.0091 0.0247  42  LYS   A C     
324  O  O     . LYS   A 45  ? 0.3109 0.2152 0.1689 -0.0920 -0.0375 0.0303  42  LYS   A O     
325  C  CB    . LYS   A 45  ? 0.2307 0.4168 0.2884 -0.1257 -0.0854 0.0308  42  LYS   A CB    
326  C  CG    . LYS   A 45  ? 0.3466 0.4607 0.3910 -0.0684 -0.0594 -0.0392 42  LYS   A CG    
327  C  CD    . LYS   A 45  ? 0.4001 0.4639 0.4967 -0.0298 -0.0790 -0.0665 42  LYS   A CD    
328  C  CE    . LYS   A 45  ? 0.3793 0.4865 0.5325 0.0123  -0.0744 -0.0531 42  LYS   A CE    
329  N  NZ    . LYS   A 45  ? 0.3810 0.5288 0.4603 0.0306  -0.1404 -0.0774 42  LYS   A NZ    
330  N  N     . GLN   A 46  ? 0.3130 0.1834 0.1874 -0.0522 -0.0538 0.0272  43  GLN   A N     
331  C  CA    . GLN   A 46  ? 0.3003 0.1845 0.1942 -0.0766 -0.0432 0.0344  43  GLN   A CA    
332  C  C     . GLN   A 46  ? 0.3112 0.2280 0.1930 -0.0670 -0.0334 0.0568  43  GLN   A C     
333  O  O     . GLN   A 46  ? 0.3503 0.2786 0.1983 -0.1035 -0.0082 0.0260  43  GLN   A O     
334  C  CB    . GLN   A 46  ? 0.4543 0.2638 0.2289 -0.0240 -0.0910 0.0595  43  GLN   A CB    
335  C  CG    . GLN   A 46  ? 0.5055 0.2758 0.2896 -0.0537 -0.0996 0.0342  43  GLN   A CG    
336  C  CD    . GLN   A 46  ? 0.5970 0.3938 0.4318 -0.0094 -0.1715 0.0895  43  GLN   A CD    
337  O  OE1   . GLN   A 46  ? 0.5009 0.5833 0.4239 0.0105  -0.1992 0.0774  43  GLN   A OE1   
338  N  NE2   . GLN   A 46  ? 0.5911 0.4152 0.4039 -0.0316 -0.1905 0.1800  43  GLN   A NE2   
339  N  N     . VAL   A 47  ? 0.2694 0.2145 0.1515 -0.0690 -0.0573 0.0240  44  VAL   A N     
340  C  CA    . VAL   A 47  ? 0.2629 0.2345 0.1735 -0.0933 -0.0571 -0.0042 44  VAL   A CA    
341  C  C     . VAL   A 47  ? 0.2179 0.2535 0.1454 -0.0790 -0.0671 -0.0165 44  VAL   A C     
342  O  O     . VAL   A 47  ? 0.2815 0.3132 0.2420 -0.1223 0.0167  -0.0940 44  VAL   A O     
343  C  CB    . VAL   A 47  ? 0.2614 0.2384 0.2416 -0.0601 -0.0829 -0.0383 44  VAL   A CB    
344  C  CG1   . VAL   A 47  ? 0.2802 0.2823 0.2921 -0.0710 -0.0928 -0.0761 44  VAL   A CG1   
345  C  CG2   . VAL   A 47  ? 0.3085 0.2678 0.2284 -0.0127 -0.0701 -0.0176 44  VAL   A CG2   
346  N  N     . VAL   A 48  ? 0.2169 0.2107 0.2203 -0.0642 -0.0493 -0.0077 45  VAL   A N     
347  C  CA    . VAL   A 48  ? 0.1895 0.1940 0.1856 -0.0364 -0.0443 -0.0038 45  VAL   A CA    
348  C  C     . VAL   A 48  ? 0.1347 0.1892 0.1759 -0.0313 -0.0353 -0.0108 45  VAL   A C     
349  O  O     . VAL   A 48  ? 0.1339 0.2365 0.1997 -0.0375 -0.0368 0.0087  45  VAL   A O     
350  C  CB    . VAL   A 48  ? 0.2470 0.2484 0.1841 -0.0103 -0.0260 0.0061  45  VAL   A CB    
351  C  CG1   . VAL   A 48  ? 0.2235 0.2968 0.1918 -0.0075 -0.0455 -0.0390 45  VAL   A CG1   
352  C  CG2   . VAL   A 48  ? 0.2510 0.2707 0.2076 0.0005  0.0010  0.0338  45  VAL   A CG2   
353  N  N     . ILE   A 49  ? 0.1434 0.1967 0.1469 -0.0392 -0.0526 -0.0019 46  ILE   A N     
354  C  CA    . ILE   A 49  ? 0.1196 0.1995 0.1407 -0.0218 -0.0377 -0.0066 46  ILE   A CA    
355  C  C     . ILE   A 49  ? 0.0877 0.1746 0.1294 -0.0020 -0.0345 -0.0031 46  ILE   A C     
356  O  O     . ILE   A 49  ? 0.0901 0.1703 0.1350 0.0038  -0.0333 -0.0096 46  ILE   A O     
357  C  CB    . ILE   A 49  ? 0.1017 0.1942 0.1417 -0.0159 -0.0409 -0.0103 46  ILE   A CB    
358  C  CG1   . ILE   A 49  ? 0.1379 0.2030 0.1629 -0.0296 -0.0712 -0.0067 46  ILE   A CG1   
359  C  CG2   . ILE   A 49  ? 0.1393 0.2086 0.1606 -0.0409 -0.0592 0.0076  46  ILE   A CG2   
360  C  CD1   . ILE   A 49  ? 0.1074 0.2050 0.1735 0.0029  -0.0687 -0.0124 46  ILE   A CD1   
361  N  N     . ASP   A 50  ? 0.0809 0.1962 0.1243 -0.0192 -0.0062 -0.0162 47  ASP   A N     
362  C  CA    . ASP   A 50  ? 0.0785 0.1796 0.1169 -0.0011 -0.0198 -0.0256 47  ASP   A CA    
363  C  C     . ASP   A 50  ? 0.0975 0.1424 0.1065 0.0109  -0.0186 -0.0344 47  ASP   A C     
364  O  O     . ASP   A 50  ? 0.1052 0.1620 0.1334 0.0106  -0.0231 -0.0192 47  ASP   A O     
365  C  CB    . ASP   A 50  ? 0.1228 0.1572 0.1270 0.0014  -0.0177 -0.0196 47  ASP   A CB    
366  C  CG    . ASP   A 50  ? 0.1143 0.1948 0.1375 0.0109  -0.0184 -0.0313 47  ASP   A CG    
367  O  OD1   . ASP   A 50  ? 0.1222 0.2129 0.1367 0.0324  -0.0245 -0.0145 47  ASP   A OD1   
368  O  OD2   . ASP   A 50  ? 0.1368 0.1958 0.1254 0.0229  -0.0068 -0.0156 47  ASP   A OD2   
369  N  N     . GLY   A 51  ? 0.1068 0.1785 0.1233 -0.0099 -0.0236 -0.0125 48  GLY   A N     
370  C  CA    . GLY   A 51  ? 0.1159 0.1641 0.1236 -0.0121 -0.0294 -0.0101 48  GLY   A CA    
371  C  C     . GLY   A 51  ? 0.1412 0.1491 0.1371 -0.0070 -0.0495 -0.0085 48  GLY   A C     
372  O  O     . GLY   A 51  ? 0.1577 0.1782 0.1748 -0.0065 -0.0715 -0.0004 48  GLY   A O     
373  N  N     . GLU   A 52  ? 0.1199 0.1644 0.1397 0.0063  -0.0547 -0.0138 49  GLU   A N     
374  C  CA    . GLU   A 52  ? 0.1391 0.1603 0.1525 0.0074  -0.0643 -0.0285 49  GLU   A CA    
375  C  C     . GLU   A 52  ? 0.1489 0.1656 0.1567 -0.0002 -0.0745 -0.0286 49  GLU   A C     
376  O  O     . GLU   A 52  ? 0.1410 0.1536 0.1835 -0.0152 -0.0786 0.0011  49  GLU   A O     
377  C  CB    . GLU   A 52  ? 0.1487 0.1709 0.1600 0.0160  -0.0584 -0.0275 49  GLU   A CB    
378  C  CG    . GLU   A 52  ? 0.1226 0.1989 0.2080 0.0035  -0.0394 -0.0424 49  GLU   A CG    
379  C  CD    . GLU   A 52  ? 0.1247 0.2550 0.2415 0.0240  -0.0079 -0.0071 49  GLU   A CD    
380  O  OE1   . GLU   A 52  ? 0.1803 0.2342 0.1700 0.0333  0.0040  -0.0243 49  GLU   A OE1   
381  O  OE2   . GLU   A 52  ? 0.1153 0.3583 0.3960 0.0163  -0.0088 -0.0058 49  GLU   A OE2   
382  N  N     . THR   A 53  ? 0.1745 0.1628 0.1817 -0.0029 -0.0945 -0.0169 50  THR   A N     
383  C  CA    . THR   A 53  ? 0.2332 0.1662 0.1635 -0.0089 -0.1006 -0.0108 50  THR   A CA    
384  C  C     . THR   A 53  ? 0.2015 0.1843 0.1794 0.0094  -0.0682 -0.0224 50  THR   A C     
385  O  O     . THR   A 53  ? 0.2248 0.2103 0.2247 0.0402  -0.0565 -0.0377 50  THR   A O     
386  C  CB    . THR   A 53  ? 0.3056 0.1665 0.1738 0.0018  -0.1099 0.0008  50  THR   A CB    
387  O  OG1   . THR   A 53  ? 0.4035 0.2118 0.1592 0.0044  -0.1334 0.0041  50  THR   A OG1   
388  C  CG2   . THR   A 53  ? 0.3969 0.1562 0.2032 -0.0018 -0.1145 -0.0127 50  THR   A CG2   
389  N  N     . CYS   A 54  ? 0.2306 0.2122 0.1756 -0.0390 -0.0696 -0.0384 51  CYS   A N     
390  C  CA    . CYS   A 54  ? 0.2637 0.2093 0.1776 0.0301  -0.0857 -0.0377 51  CYS   A CA    
391  C  C     . CYS   A 54  ? 0.2491 0.2212 0.2000 -0.0231 -0.0322 -0.0211 51  CYS   A C     
392  O  O     . CYS   A 54  ? 0.2538 0.1801 0.2410 -0.0530 -0.0272 -0.0551 51  CYS   A O     
393  C  CB    . CYS   A 54  ? 0.1174 0.2122 0.1054 -0.0080 -0.0429 -0.0278 51  CYS   A CB    
394  S  SG    . CYS   A 54  ? 0.2262 0.2151 0.1969 0.0055  -0.0627 -0.0231 51  CYS   A SG    
395  N  N     . LEU   A 55  ? 0.2001 0.1930 0.1621 0.0048  -0.0516 0.0092  52  LEU   A N     
396  C  CA    . LEU   A 55  ? 0.2186 0.1806 0.1678 0.0266  -0.0562 0.0191  52  LEU   A CA    
397  C  C     . LEU   A 55  ? 0.1959 0.1312 0.1302 0.0116  -0.0230 0.0031  52  LEU   A C     
398  O  O     . LEU   A 55  ? 0.1920 0.1947 0.1394 -0.0055 -0.0376 0.0208  52  LEU   A O     
399  C  CB    . LEU   A 55  ? 0.2182 0.2249 0.2159 0.0444  -0.0115 0.0461  52  LEU   A CB    
400  C  CG    . LEU   A 55  ? 0.2771 0.2332 0.2605 0.0321  0.0148  0.0452  52  LEU   A CG    
401  C  CD1   . LEU   A 55  ? 0.3286 0.1861 0.3258 -0.0104 0.0376  0.0216  52  LEU   A CD1   
402  C  CD2   . LEU   A 55  ? 0.3153 0.2768 0.3364 0.0737  0.0433  0.0659  52  LEU   A CD2   
403  N  N     . LEU   A 56  ? 0.2206 0.1515 0.1380 0.0057  -0.0328 -0.0109 53  LEU   A N     
404  C  CA    . LEU   A 56  ? 0.2184 0.1487 0.1426 -0.0116 -0.0471 -0.0076 53  LEU   A CA    
405  C  C     . LEU   A 56  ? 0.2391 0.1398 0.1492 -0.0096 -0.0228 0.0009  53  LEU   A C     
406  O  O     . LEU   A 56  ? 0.3291 0.1579 0.1434 -0.0487 -0.0246 -0.0047 53  LEU   A O     
407  C  CB    . LEU   A 56  ? 0.2301 0.1629 0.1326 -0.0215 -0.0168 -0.0155 53  LEU   A CB    
408  C  CG    . LEU   A 56  ? 0.2388 0.1635 0.1778 0.0003  -0.0528 -0.0296 53  LEU   A CG    
409  C  CD1   . LEU   A 56  ? 0.2380 0.2137 0.2132 0.0143  -0.0148 -0.0576 53  LEU   A CD1   
410  C  CD2   . LEU   A 56  ? 0.2302 0.1292 0.2124 0.0184  -0.0542 -0.0213 53  LEU   A CD2   
411  N  N     . ASP   A 57  ? 0.1739 0.1391 0.1377 -0.0155 -0.0393 -0.0093 54  ASP   A N     
412  C  CA    . ASP   A 57  ? 0.1583 0.1453 0.1384 0.0045  -0.0298 -0.0157 54  ASP   A CA    
413  C  C     . ASP   A 57  ? 0.1715 0.1226 0.1430 0.0106  -0.0407 -0.0310 54  ASP   A C     
414  O  O     . ASP   A 57  ? 0.1410 0.1433 0.1478 0.0298  -0.0583 -0.0115 54  ASP   A O     
415  C  CB    . ASP   A 57  ? 0.1632 0.1888 0.1693 0.0450  -0.0596 -0.0038 54  ASP   A CB    
416  C  CG    . ASP   A 57  ? 0.1906 0.2104 0.1642 0.0410  -0.0560 -0.0141 54  ASP   A CG    
417  O  OD1   . ASP   A 57  ? 0.2548 0.1864 0.2454 0.0157  -0.0643 -0.0710 54  ASP   A OD1   
418  O  OD2   . ASP   A 57  ? 0.2368 0.3404 0.2850 0.1340  -0.0824 -0.0534 54  ASP   A OD2   
419  N  N     . ILE   A 58  ? 0.1869 0.1304 0.1304 0.0082  -0.0420 -0.0261 55  ILE   A N     
420  C  CA    . ILE   A 58  ? 0.1849 0.1311 0.1193 0.0013  -0.0330 -0.0075 55  ILE   A CA    
421  C  C     . ILE   A 58  ? 0.1466 0.1372 0.1237 0.0241  -0.0455 -0.0132 55  ILE   A C     
422  O  O     . ILE   A 58  ? 0.2069 0.1384 0.1420 0.0037  -0.0418 -0.0203 55  ILE   A O     
423  C  CB    . ILE   A 58  ? 0.1869 0.1399 0.1356 0.0141  -0.0432 -0.0048 55  ILE   A CB    
424  C  CG1   . ILE   A 58  ? 0.2009 0.1670 0.1436 0.0075  -0.0245 -0.0252 55  ILE   A CG1   
425  C  CG2   . ILE   A 58  ? 0.1863 0.1708 0.1604 0.0365  -0.0534 -0.0095 55  ILE   A CG2   
426  C  CD1   . ILE   A 58  ? 0.1656 0.1849 0.1978 0.0240  -0.0317 -0.0234 55  ILE   A CD1   
427  N  N     . LEU   A 59  ? 0.1379 0.1301 0.1223 0.0228  -0.0364 -0.0248 56  LEU   A N     
428  C  CA    . LEU   A 59  ? 0.1504 0.1465 0.1140 0.0246  -0.0387 -0.0303 56  LEU   A CA    
429  C  C     . LEU   A 59  ? 0.1660 0.1258 0.1340 0.0173  -0.0635 -0.0480 56  LEU   A C     
430  O  O     . LEU   A 59  ? 0.1392 0.1372 0.1416 0.0212  -0.0464 -0.0278 56  LEU   A O     
431  C  CB    . LEU   A 59  ? 0.1285 0.1511 0.1350 0.0095  -0.0447 -0.0194 56  LEU   A CB    
432  C  CG    . LEU   A 59  ? 0.1506 0.1696 0.1615 0.0239  -0.0282 -0.0471 56  LEU   A CG    
433  C  CD1   . LEU   A 59  ? 0.2190 0.1744 0.1610 0.0307  -0.0218 -0.0457 56  LEU   A CD1   
434  C  CD2   . LEU   A 59  ? 0.1655 0.2151 0.1616 0.0355  -0.0266 -0.0553 56  LEU   A CD2   
435  N  N     . ASP   A 60  ? 0.1548 0.1178 0.1256 0.0208  -0.0417 -0.0286 57  ASP   A N     
436  C  CA    . ASP   A 60  ? 0.1493 0.1298 0.1586 0.0063  -0.0402 -0.0458 57  ASP   A CA    
437  C  C     . ASP   A 60  ? 0.1230 0.1419 0.1443 0.0113  -0.0189 -0.0242 57  ASP   A C     
438  O  O     . ASP   A 60  ? 0.2320 0.1473 0.1463 0.0031  -0.0420 -0.0337 57  ASP   A O     
439  C  CB    . ASP   A 60  ? 0.1664 0.1583 0.1542 0.0035  -0.0453 -0.0288 57  ASP   A CB    
440  C  CG    . ASP   A 60  ? 0.1429 0.1540 0.1755 0.0016  -0.0124 -0.0079 57  ASP   A CG    
441  O  OD1   . ASP   A 60  ? 0.1825 0.1492 0.1685 -0.0117 -0.0625 -0.0206 57  ASP   A OD1   
442  O  OD2   . ASP   A 60  ? 0.2078 0.1754 0.1788 -0.0347 -0.0130 -0.0149 57  ASP   A OD2   
443  N  N     . THR   A 61  ? 0.1619 0.1328 0.1301 0.0130  -0.0309 -0.0396 58  THR   A N     
444  C  CA    . THR   A 61  ? 0.1572 0.1667 0.1274 0.0168  -0.0197 -0.0391 58  THR   A CA    
445  C  C     . THR   A 61  ? 0.1622 0.1538 0.1738 0.0127  -0.0236 -0.0352 58  THR   A C     
446  O  O     . THR   A 61  ? 0.1606 0.1746 0.1386 0.0163  -0.0324 -0.0169 58  THR   A O     
447  C  CB    . THR   A 61  ? 0.1234 0.1621 0.1283 0.0160  -0.0186 -0.0439 58  THR   A CB    
448  O  OG1   . THR   A 61  ? 0.1640 0.1581 0.1218 0.0151  -0.0527 -0.0351 58  THR   A OG1   
449  C  CG2   . THR   A 61  ? 0.1129 0.1841 0.1510 0.0217  -0.0202 -0.0566 58  THR   A CG2   
450  N  N     . ALA   A 62  ? 0.1581 0.1934 0.1544 0.0110  -0.0303 -0.0505 59  ALA   A N     
451  C  CA    . ALA   A 62  ? 0.1617 0.1996 0.1627 -0.0108 -0.0241 -0.0345 59  ALA   A CA    
452  C  C     . ALA   A 62  ? 0.1933 0.1728 0.1555 -0.0028 0.0016  -0.0419 59  ALA   A C     
453  O  O     . ALA   A 62  ? 0.2135 0.1940 0.1811 0.0142  -0.0143 -0.0370 59  ALA   A O     
454  C  CB    . ALA   A 62  ? 0.2519 0.2042 0.1729 -0.0331 -0.0507 -0.0512 59  ALA   A CB    
455  N  N     . GLY   A 63  ? 0.2074 0.1891 0.1835 0.0352  -0.0045 -0.0439 60  GLY   A N     
456  C  CA    . GLY   A 63  ? 0.2396 0.2151 0.1727 0.0025  -0.0011 -0.0480 60  GLY   A CA    
457  C  C     . GLY   A 63  ? 0.1628 0.2059 0.1799 0.0221  0.0020  -0.0458 60  GLY   A C     
458  O  O     . GLY   A 63  ? 0.1857 0.2618 0.2723 0.0241  -0.0531 -0.0097 60  GLY   A O     
459  N  N     . GLN   A 64  ? 0.1937 0.2504 0.1555 0.0283  -0.0079 -0.0345 61  GLN   A N     
460  C  CA    . GLN   A 64  ? 0.2140 0.2470 0.1558 0.0477  0.0157  -0.0429 61  GLN   A CA    
461  C  C     . GLN   A 64  ? 0.2608 0.2590 0.1514 0.0551  0.0189  -0.0328 61  GLN   A C     
462  O  O     . GLN   A 64  ? 0.3948 0.2568 0.2171 0.0856  0.0908  -0.0138 61  GLN   A O     
463  C  CB    . GLN   A 64  ? 0.2350 0.2890 0.1188 0.0816  -0.0234 -0.0365 61  GLN   A CB    
464  C  CG    . GLN   A 64  ? 0.1561 0.2867 0.1435 0.0628  -0.0007 -0.0645 61  GLN   A CG    
465  C  CD    . GLN   A 64  ? 0.1835 0.2425 0.1264 0.0527  -0.0125 -0.0270 61  GLN   A CD    
466  O  OE1   . GLN   A 64  ? 0.1815 0.2256 0.1804 0.0774  0.0261  -0.0184 61  GLN   A OE1   
467  N  NE2   . GLN   A 64  ? 0.1713 0.2178 0.1309 0.0508  -0.0175 -0.0359 61  GLN   A NE2   
468  N  N     . GLU   A 65  ? 0.2314 0.2441 0.1570 0.0289  0.0323  -0.0328 62  GLU   A N     
469  C  CA    . GLU   A 65  ? 0.2486 0.3117 0.1827 0.0406  0.0812  -0.0457 62  GLU   A CA    
470  C  C     . GLU   A 65  ? 0.2689 0.2366 0.2040 0.0574  0.0527  -0.0302 62  GLU   A C     
471  O  O     . GLU   A 65  ? 0.2963 0.3984 0.1922 0.0262  0.0376  -0.0479 62  GLU   A O     
472  C  CB    . GLU   A 65  ? 0.2956 0.3073 0.2195 0.0178  0.0815  -0.0509 62  GLU   A CB    
473  C  CG    . GLU   A 65  ? 0.2962 0.4136 0.3459 -0.0404 0.0217  -0.0891 62  GLU   A CG    
474  C  CD    . GLU   A 65  ? 0.4463 0.5311 0.4262 -0.0827 -0.0125 0.0051  62  GLU   A CD    
475  O  OE1   . GLU   A 65  ? 0.4999 0.6486 0.3723 -0.1511 -0.0011 0.0344  62  GLU   A OE1   
476  O  OE2   . GLU   A 65  ? 0.4198 0.6012 0.6632 -0.1106 -0.0356 -0.0374 62  GLU   A OE2   
477  N  N     . GLU   A 66  ? 0.3118 0.2847 0.2215 0.0779  0.0571  0.0014  63  GLU   A N     
478  C  CA    . GLU   A 66  ? 0.3414 0.3434 0.3039 0.0667  0.0793  -0.0267 63  GLU   A CA    
479  C  C     . GLU   A 66  ? 0.2693 0.3265 0.2493 0.0163  0.0770  -0.0470 63  GLU   A C     
480  O  O     . GLU   A 66  ? 0.3514 0.3530 0.2973 -0.0362 0.0132  -0.0860 63  GLU   A O     
481  C  CB    . GLU   A 66  ? 0.4109 0.3227 0.3993 0.0953  0.0972  0.0511  63  GLU   A CB    
482  C  CG    . GLU   A 66  ? 0.5043 0.3900 0.4155 0.0721  0.1402  0.0555  63  GLU   A CG    
483  C  CD    . GLU   A 66  ? 0.6150 0.4221 0.5813 0.0654  0.0947  -0.0237 63  GLU   A CD    
484  O  OE1   . GLU   A 66  ? 0.8303 0.6421 0.5627 0.0939  0.0816  0.0260  63  GLU   A OE1   
485  O  OE2   . GLU   A 66  ? 0.8004 0.4913 0.5081 0.1739  0.0783  0.0272  63  GLU   A OE2   
486  N  N     . TYR   A 67  ? 0.2610 0.2857 0.1759 0.0530  0.0510  -0.0040 64  TYR   A N     
487  C  CA    . TYR   A 67  ? 0.1719 0.2520 0.1568 0.0162  -0.0169 -0.0239 64  TYR   A CA    
488  C  C     . TYR   A 67  ? 0.1744 0.2288 0.1798 0.0490  -0.0554 -0.0292 64  TYR   A C     
489  O  O     . TYR   A 67  ? 0.3118 0.2370 0.2070 0.0073  -0.1115 -0.0308 64  TYR   A O     
490  C  CB    . TYR   A 67  ? 0.1432 0.2797 0.1466 0.0170  -0.0148 -0.0166 64  TYR   A CB    
491  C  CG    . TYR   A 67  ? 0.1453 0.3040 0.1352 0.0110  -0.0090 -0.0064 64  TYR   A CG    
492  C  CD1   . TYR   A 67  ? 0.2184 0.3590 0.1647 -0.0388 0.0147  0.0516  64  TYR   A CD1   
493  C  CD2   . TYR   A 67  ? 0.1541 0.3113 0.1712 0.0154  -0.0255 -0.0049 64  TYR   A CD2   
494  C  CE1   . TYR   A 67  ? 0.1873 0.3914 0.1993 -0.0035 0.0117  0.0747  64  TYR   A CE1   
495  C  CE2   . TYR   A 67  ? 0.2086 0.3124 0.1931 0.0068  0.0122  0.0027  64  TYR   A CE2   
496  C  CZ    . TYR   A 67  ? 0.1822 0.3534 0.1434 0.0135  0.0202  0.0156  64  TYR   A CZ    
497  O  OH    . TYR   A 67  ? 0.2595 0.3543 0.1939 0.0277  0.0059  0.0292  64  TYR   A OH    
498  N  N     . SER   A 68  ? 0.1791 0.2219 0.1342 0.0201  -0.0154 -0.0314 65  SER   A N     
499  C  CA    . SER   A 68  ? 0.1760 0.2276 0.1155 0.0224  -0.0450 -0.0308 65  SER   A CA    
500  C  C     . SER   A 68  ? 0.1592 0.2059 0.1382 0.0295  -0.0284 -0.0499 65  SER   A C     
501  O  O     . SER   A 68  ? 0.1720 0.2150 0.1562 0.0202  -0.0476 -0.0566 65  SER   A O     
502  C  CB    . SER   A 68  ? 0.1857 0.2301 0.1245 0.0456  -0.0420 -0.0324 65  SER   A CB    
503  O  OG    . SER   A 68  ? 0.2287 0.2205 0.1425 0.0190  -0.0453 -0.0106 65  SER   A OG    
504  N  N     . ALA   A 69  ? 0.1152 0.2416 0.1578 0.0187  -0.0277 -0.0800 66  ALA   A N     
505  C  CA    . ALA   A 69  ? 0.1409 0.2472 0.1833 -0.0003 -0.0580 -0.0940 66  ALA   A CA    
506  C  C     . ALA   A 69  ? 0.1865 0.2296 0.1925 0.0365  -0.0336 -0.1077 66  ALA   A C     
507  O  O     . ALA   A 69  ? 0.1752 0.2741 0.1842 0.0599  -0.0735 -0.1073 66  ALA   A O     
508  C  CB    . ALA   A 69  ? 0.1635 0.2859 0.2127 0.0196  -0.0244 -0.1234 66  ALA   A CB    
509  N  N     . MET   A 70  ? 0.1868 0.2173 0.1615 0.0516  -0.0698 -0.0679 67  MET   A N     
510  C  CA    . MET   A 70  ? 0.2231 0.2296 0.1603 0.0527  -0.0511 -0.0661 67  MET   A CA    
511  C  C     . MET   A 70  ? 0.1874 0.2293 0.1544 0.0598  -0.0619 -0.0697 67  MET   A C     
512  O  O     . MET   A 70  ? 0.1691 0.2287 0.1442 0.0488  -0.0533 -0.0584 67  MET   A O     
513  C  CB    . MET   A 70  ? 0.3417 0.2834 0.2136 0.0175  -0.0065 -0.0610 67  MET   A CB    
514  C  CG    . MET   A 70  ? 0.4480 0.2932 0.2849 0.0503  -0.0552 -0.0766 67  MET   A CG    
515  S  SD    . MET   A 70  ? 0.4771 0.4420 0.4532 0.1767  -0.0707 -0.1409 67  MET   A SD    
516  C  CE    . MET   A 70  ? 0.3924 0.4290 0.4284 0.1564  0.0668  -0.0922 67  MET   A CE    
517  N  N     . ARG   A 71  ? 0.1725 0.2023 0.1465 0.0382  -0.0548 -0.0741 68  ARG   A N     
518  C  CA    . ARG   A 71  ? 0.1572 0.2005 0.1578 0.0282  -0.0374 -0.0709 68  ARG   A CA    
519  C  C     . ARG   A 71  ? 0.1164 0.2008 0.1393 0.0485  -0.0265 -0.0556 68  ARG   A C     
520  O  O     . ARG   A 71  ? 0.1232 0.2039 0.1639 0.0226  -0.0238 -0.0657 68  ARG   A O     
521  C  CB    . ARG   A 71  ? 0.1476 0.2393 0.1880 0.0454  -0.0377 -0.0582 68  ARG   A CB    
522  C  CG    . ARG   A 71  ? 0.2797 0.2551 0.2424 0.0622  -0.0152 -0.0673 68  ARG   A CG    
523  C  CD    . ARG   A 71  ? 0.2953 0.4002 0.3352 0.0320  -0.0434 -0.0488 68  ARG   A CD    
524  N  NE    . ARG   A 71  ? 0.2779 0.4311 0.4771 0.0676  0.0696  -0.0798 68  ARG   A NE    
525  C  CZ    . ARG   A 71  ? 0.2926 0.3078 0.5214 0.0508  -0.0288 -0.0485 68  ARG   A CZ    
526  N  NH1   . ARG   A 71  ? 0.1581 0.3071 0.4832 0.0394  -0.0827 0.0400  68  ARG   A NH1   
527  N  NH2   . ARG   A 71  ? 0.4109 0.4042 0.5074 -0.1756 -0.1607 0.0329  68  ARG   A NH2   
528  N  N     . ASP   A 72  ? 0.1107 0.2186 0.1401 0.0489  -0.0343 -0.0603 69  ASP   A N     
529  C  CA    . ASP   A 72  ? 0.1152 0.2683 0.1517 0.0259  -0.0186 -0.0696 69  ASP   A CA    
530  C  C     . ASP   A 72  ? 0.1312 0.2527 0.1417 0.0427  -0.0099 -0.0759 69  ASP   A C     
531  O  O     . ASP   A 72  ? 0.1131 0.2702 0.1693 0.0197  -0.0003 -0.0810 69  ASP   A O     
532  C  CB    . ASP   A 72  ? 0.1828 0.3055 0.1667 0.0383  0.0178  -0.0730 69  ASP   A CB    
533  C  CG    . ASP   A 72  ? 0.2997 0.4349 0.2169 0.0538  0.0014  -0.0117 69  ASP   A CG    
534  O  OD1   . ASP   A 72  ? 0.3189 0.4770 0.3272 0.0820  0.0091  -0.0110 69  ASP   A OD1   
535  O  OD2   . ASP   A 72  ? 0.3954 0.5414 0.2649 0.0606  0.0463  -0.0538 69  ASP   A OD2   
536  N  N     . GLN   A 73  ? 0.1691 0.2398 0.1490 0.0484  -0.0393 -0.0829 70  GLN   A N     
537  C  CA    . GLN   A 73  ? 0.0907 0.2618 0.1806 0.0584  -0.0377 -0.0848 70  GLN   A CA    
538  C  C     . GLN   A 73  ? 0.1430 0.2067 0.1643 0.0331  -0.0445 -0.0747 70  GLN   A C     
539  O  O     . GLN   A 73  ? 0.1257 0.2503 0.1792 0.0383  -0.0351 -0.1052 70  GLN   A O     
540  C  CB    . GLN   A 73  ? 0.1698 0.2612 0.2034 0.0788  -0.0371 -0.0956 70  GLN   A CB    
541  C  CG    . GLN   A 73  ? 0.2033 0.2519 0.2268 0.1007  -0.0498 -0.0610 70  GLN   A CG    
542  C  CD    . GLN   A 73  ? 0.2100 0.3835 0.2921 0.0664  -0.0218 -0.1087 70  GLN   A CD    
543  O  OE1   . GLN   A 73  ? 0.2560 0.5427 0.2972 0.0568  -0.0119 -0.1134 70  GLN   A OE1   
544  N  NE2   . GLN   A 73  ? 0.2432 0.4359 0.2707 0.0392  -0.0413 -0.1022 70  GLN   A NE2   
545  N  N     . TYR   A 74  ? 0.1516 0.2119 0.1509 0.0300  -0.0433 -0.0794 71  TYR   A N     
546  C  CA    . TYR   A 74  ? 0.1076 0.2312 0.1574 0.0281  -0.0338 -0.0661 71  TYR   A CA    
547  C  C     . TYR   A 74  ? 0.1160 0.2311 0.1489 0.0189  -0.0085 -0.0717 71  TYR   A C     
548  O  O     . TYR   A 74  ? 0.1036 0.2365 0.1506 0.0129  -0.0197 -0.0747 71  TYR   A O     
549  C  CB    . TYR   A 74  ? 0.1420 0.2311 0.1566 0.0123  -0.0465 -0.0580 71  TYR   A CB    
550  C  CG    . TYR   A 74  ? 0.1245 0.2235 0.1379 0.0217  -0.0216 -0.0618 71  TYR   A CG    
551  C  CD1   . TYR   A 74  ? 0.1246 0.2118 0.1658 -0.0043 -0.0314 -0.0395 71  TYR   A CD1   
552  C  CD2   . TYR   A 74  ? 0.1649 0.2274 0.1378 0.0161  -0.0205 -0.0715 71  TYR   A CD2   
553  C  CE1   . TYR   A 74  ? 0.0906 0.2207 0.1687 0.0130  0.0063  -0.0384 71  TYR   A CE1   
554  C  CE2   . TYR   A 74  ? 0.1734 0.2371 0.1544 -0.0250 -0.0385 -0.0613 71  TYR   A CE2   
555  C  CZ    . TYR   A 74  ? 0.1170 0.2474 0.1905 -0.0092 -0.0175 -0.0454 71  TYR   A CZ    
556  O  OH    . TYR   A 74  ? 0.1260 0.2705 0.1894 0.0172  -0.0219 -0.0538 71  TYR   A OH    
557  N  N     . MET   A 75  ? 0.0817 0.2265 0.1518 0.0116  -0.0254 -0.0720 72  MET   A N     
558  C  CA    . MET   A 75  ? 0.0823 0.2277 0.1989 0.0332  -0.0102 -0.0818 72  MET   A CA    
559  C  C     . MET   A 75  ? 0.0861 0.2143 0.1908 0.0317  -0.0171 -0.0861 72  MET   A C     
560  O  O     . MET   A 75  ? 0.1158 0.2374 0.2436 0.0057  -0.0300 -0.1130 72  MET   A O     
561  C  CB    . MET   A 75  ? 0.0904 0.2416 0.1883 0.0302  -0.0011 -0.0777 72  MET   A CB    
562  C  CG    . MET   A 75  ? 0.0978 0.2173 0.1942 0.0282  -0.0136 -0.0533 72  MET   A CG    
563  S  SD    . MET   A 75  ? 0.1348 0.2375 0.2032 0.0213  -0.0322 -0.0424 72  MET   A SD    
564  C  CE    . MET   A 75  ? 0.1336 0.2554 0.2433 0.0084  -0.0651 -0.0174 72  MET   A CE    
565  N  N     . ARG   A 76  ? 0.0833 0.2610 0.1874 0.0429  -0.0190 -0.0965 73  ARG   A N     
566  C  CA    . ARG   A 76  ? 0.0791 0.2459 0.2188 0.0269  -0.0147 -0.0555 73  ARG   A CA    
567  C  C     . ARG   A 76  ? 0.1099 0.2475 0.2200 0.0232  -0.0115 -0.0766 73  ARG   A C     
568  O  O     . ARG   A 76  ? 0.1289 0.2932 0.2063 0.0139  -0.0361 -0.0841 73  ARG   A O     
569  C  CB    . ARG   A 76  ? 0.0816 0.2800 0.2182 0.0173  0.0009  -0.0700 73  ARG   A CB    
570  C  CG    . ARG   A 76  ? 0.1219 0.3415 0.2327 0.0167  0.0135  -0.0463 73  ARG   A CG    
571  C  CD    . ARG   A 76  ? 0.1015 0.4321 0.3108 0.0380  0.0263  -0.0428 73  ARG   A CD    
572  N  NE    . ARG   A 76  ? 0.2899 0.4714 0.4174 -0.0189 -0.0251 -0.0577 73  ARG   A NE    
573  C  CZ    . ARG   A 76  ? 0.2321 0.5265 0.3960 0.0485  -0.0519 -0.0315 73  ARG   A CZ    
574  N  NH1   . ARG   A 76  ? 0.2982 0.6247 0.4605 0.0758  0.0242  0.0650  73  ARG   A NH1   
575  N  NH2   . ARG   A 76  ? 0.1780 0.5336 0.4225 -0.0020 0.0398  -0.0638 73  ARG   A NH2   
576  N  N     . THR   A 77  ? 0.0967 0.2316 0.1904 0.0191  -0.0179 -0.0819 74  THR   A N     
577  C  CA    . THR   A 77  ? 0.0691 0.2395 0.2022 0.0261  -0.0333 -0.0768 74  THR   A CA    
578  C  C     . THR   A 77  ? 0.1013 0.2314 0.1819 0.0189  -0.0291 -0.0737 74  THR   A C     
579  O  O     . THR   A 77  ? 0.1135 0.2473 0.1833 0.0280  -0.0461 -0.0710 74  THR   A O     
580  C  CB    . THR   A 77  ? 0.1300 0.2439 0.2016 0.0489  -0.0143 -0.0618 74  THR   A CB    
581  O  OG1   . THR   A 77  ? 0.2055 0.2759 0.2089 0.1046  -0.0380 -0.0952 74  THR   A OG1   
582  C  CG2   . THR   A 77  ? 0.1558 0.2541 0.2185 0.0491  -0.0234 -0.0488 74  THR   A CG2   
583  N  N     . GLY   A 78  ? 0.0926 0.2170 0.1693 0.0219  -0.0155 -0.0844 75  GLY   A N     
584  C  CA    . GLY   A 78  ? 0.0795 0.2111 0.1660 0.0144  0.0036  -0.0566 75  GLY   A CA    
585  C  C     . GLY   A 78  ? 0.0691 0.2090 0.1537 0.0112  -0.0037 -0.0625 75  GLY   A C     
586  O  O     . GLY   A 78  ? 0.1094 0.2431 0.1669 -0.0128 -0.0005 -0.0577 75  GLY   A O     
587  N  N     . GLU   A 79  ? 0.0808 0.1751 0.1493 0.0158  -0.0136 -0.0444 76  GLU   A N     
588  C  CA    . GLU   A 79  ? 0.0673 0.1876 0.1416 0.0093  -0.0104 -0.0482 76  GLU   A CA    
589  C  C     . GLU   A 79  ? 0.0839 0.1659 0.1287 0.0122  0.0006  -0.0337 76  GLU   A C     
590  O  O     . GLU   A 79  ? 0.0940 0.1702 0.1871 0.0015  0.0174  -0.0212 76  GLU   A O     
591  C  CB    . GLU   A 79  ? 0.0957 0.1833 0.1616 0.0174  -0.0365 -0.0277 76  GLU   A CB    
592  C  CG    . GLU   A 79  ? 0.0808 0.2034 0.2257 0.0087  -0.0039 -0.0006 76  GLU   A CG    
593  C  CD    . GLU   A 79  ? 0.1252 0.3508 0.2495 0.0517  -0.0293 0.0810  76  GLU   A CD    
594  O  OE1   . GLU   A 79  ? 0.1144 0.2823 0.2342 -0.0367 -0.0512 0.0038  76  GLU   A OE1   
595  O  OE2   . GLU   A 79  ? 0.3434 0.5754 0.4377 -0.1897 -0.0026 0.0512  76  GLU   A OE2   
596  N  N     . GLY   A 80  ? 0.0789 0.1583 0.1213 0.0184  -0.0146 -0.0284 77  GLY   A N     
597  C  CA    . GLY   A 80  ? 0.0696 0.1587 0.1017 0.0137  -0.0125 -0.0351 77  GLY   A CA    
598  C  C     . GLY   A 80  ? 0.0700 0.1424 0.1031 0.0175  -0.0167 -0.0345 77  GLY   A C     
599  O  O     . GLY   A 80  ? 0.0593 0.1532 0.1340 0.0162  -0.0116 -0.0207 77  GLY   A O     
600  N  N     . PHE   A 81  ? 0.0779 0.1298 0.1088 0.0133  -0.0222 -0.0241 78  PHE   A N     
601  C  CA    . PHE   A 81  ? 0.0779 0.1439 0.1117 0.0002  -0.0128 -0.0344 78  PHE   A CA    
602  C  C     . PHE   A 81  ? 0.0729 0.1483 0.1050 -0.0078 -0.0094 -0.0285 78  PHE   A C     
603  O  O     . PHE   A 81  ? 0.0691 0.1461 0.1458 0.0056  -0.0063 -0.0156 78  PHE   A O     
604  C  CB    . PHE   A 81  ? 0.0716 0.1642 0.1122 0.0171  -0.0249 -0.0131 78  PHE   A CB    
605  C  CG    . PHE   A 81  ? 0.0811 0.1802 0.1123 0.0154  -0.0040 -0.0273 78  PHE   A CG    
606  C  CD1   . PHE   A 81  ? 0.0854 0.1890 0.1184 0.0126  -0.0159 -0.0171 78  PHE   A CD1   
607  C  CD2   . PHE   A 81  ? 0.0522 0.1845 0.1179 0.0054  -0.0113 -0.0323 78  PHE   A CD2   
608  C  CE1   . PHE   A 81  ? 0.1006 0.2114 0.1433 0.0102  0.0215  -0.0357 78  PHE   A CE1   
609  C  CE2   . PHE   A 81  ? 0.0931 0.1824 0.1251 0.0217  0.0198  -0.0287 78  PHE   A CE2   
610  C  CZ    . PHE   A 81  ? 0.1027 0.2092 0.1408 0.0175  0.0102  -0.0375 78  PHE   A CZ    
611  N  N     . LEU   A 82  ? 0.0788 0.1247 0.1123 0.0034  -0.0144 -0.0160 79  LEU   A N     
612  C  CA    . LEU   A 82  ? 0.0797 0.1391 0.1066 -0.0123 -0.0023 -0.0317 79  LEU   A CA    
613  C  C     . LEU   A 82  ? 0.0573 0.1425 0.1172 0.0003  -0.0098 -0.0252 79  LEU   A C     
614  O  O     . LEU   A 82  ? 0.1225 0.1476 0.1283 0.0102  -0.0529 -0.0325 79  LEU   A O     
615  C  CB    . LEU   A 82  ? 0.1584 0.1476 0.1226 -0.0214 0.0204  -0.0238 79  LEU   A CB    
616  C  CG    . LEU   A 82  ? 0.2005 0.1608 0.1530 -0.0102 0.0316  -0.0412 79  LEU   A CG    
617  C  CD1   . LEU   A 82  ? 0.2121 0.1590 0.1016 0.0240  0.0000  -0.0383 79  LEU   A CD1   
618  C  CD2   . LEU   A 82  ? 0.2033 0.1696 0.1792 0.0062  0.0697  -0.0281 79  LEU   A CD2   
619  N  N     . CYS   A 83  ? 0.0745 0.1374 0.1096 -0.0027 -0.0061 -0.0270 80  CYS   A N     
620  C  CA    . CYS   A 83  ? 0.0722 0.1521 0.1080 0.0120  -0.0049 -0.0271 80  CYS   A CA    
621  C  C     . CYS   A 83  ? 0.0650 0.1339 0.1015 0.0019  -0.0101 -0.0183 80  CYS   A C     
622  O  O     . CYS   A 83  ? 0.0573 0.1330 0.1187 -0.0032 -0.0095 -0.0177 80  CYS   A O     
623  C  CB    . CYS   A 83  ? 0.0697 0.1745 0.1408 0.0016  -0.0062 -0.0080 80  CYS   A CB    
624  S  SG    . CYS   A 83  ? 0.0838 0.2439 0.2313 -0.0054 0.0483  -0.0066 80  CYS   A SG    
625  N  N     . VAL   A 84  ? 0.0652 0.1211 0.0979 0.0056  -0.0047 -0.0174 81  VAL   A N     
626  C  CA    . VAL   A 84  ? 0.0589 0.1286 0.0880 0.0083  -0.0093 -0.0210 81  VAL   A CA    
627  C  C     . VAL   A 84  ? 0.0669 0.1356 0.0809 0.0016  -0.0076 -0.0167 81  VAL   A C     
628  O  O     . VAL   A 84  ? 0.0711 0.1459 0.0803 -0.0017 -0.0049 -0.0180 81  VAL   A O     
629  C  CB    . VAL   A 84  ? 0.0678 0.1272 0.1022 -0.0055 -0.0175 -0.0194 81  VAL   A CB    
630  C  CG1   . VAL   A 84  ? 0.0730 0.1360 0.1055 -0.0064 -0.0117 -0.0180 81  VAL   A CG1   
631  C  CG2   . VAL   A 84  ? 0.0901 0.1367 0.1041 0.0073  -0.0244 -0.0073 81  VAL   A CG2   
632  N  N     . PHE   A 85  ? 0.0486 0.1434 0.0889 -0.0059 -0.0066 -0.0183 82  PHE   A N     
633  C  CA    . PHE   A 85  ? 0.0534 0.1527 0.0881 -0.0155 -0.0082 -0.0181 82  PHE   A CA    
634  C  C     . PHE   A 85  ? 0.0636 0.1544 0.0819 -0.0112 -0.0006 -0.0148 82  PHE   A C     
635  O  O     . PHE   A 85  ? 0.0707 0.1659 0.0838 0.0003  -0.0078 -0.0089 82  PHE   A O     
636  C  CB    . PHE   A 85  ? 0.0603 0.1664 0.0815 -0.0037 -0.0080 -0.0046 82  PHE   A CB    
637  C  CG    . PHE   A 85  ? 0.0711 0.1547 0.0884 0.0037  -0.0056 0.0046  82  PHE   A CG    
638  C  CD1   . PHE   A 85  ? 0.0688 0.1528 0.0927 0.0039  -0.0061 0.0116  82  PHE   A CD1   
639  C  CD2   . PHE   A 85  ? 0.0541 0.1834 0.0930 -0.0046 -0.0053 0.0056  82  PHE   A CD2   
640  C  CE1   . PHE   A 85  ? 0.0563 0.1484 0.1081 -0.0084 -0.0168 0.0112  82  PHE   A CE1   
641  C  CE2   . PHE   A 85  ? 0.0451 0.1731 0.0987 0.0118  0.0028  0.0163  82  PHE   A CE2   
642  C  CZ    . PHE   A 85  ? 0.0701 0.1713 0.1011 0.0061  -0.0043 0.0161  82  PHE   A CZ    
643  N  N     . ALA   A 86  ? 0.0505 0.1878 0.0785 -0.0100 0.0058  -0.0077 83  ALA   A N     
644  C  CA    . ALA   A 86  ? 0.0613 0.1840 0.0944 -0.0113 0.0205  -0.0275 83  ALA   A CA    
645  C  C     . ALA   A 86  ? 0.0648 0.1850 0.0938 -0.0041 0.0059  -0.0243 83  ALA   A C     
646  O  O     . ALA   A 86  ? 0.0579 0.1872 0.0975 0.0006  0.0107  -0.0198 83  ALA   A O     
647  C  CB    . ALA   A 86  ? 0.0669 0.1929 0.1113 -0.0201 -0.0045 -0.0181 83  ALA   A CB    
648  N  N     . ILE   A 87  ? 0.0801 0.1769 0.0902 -0.0002 0.0175  -0.0125 84  ILE   A N     
649  C  CA    . ILE   A 87  ? 0.0929 0.1806 0.1042 -0.0085 0.0024  -0.0170 84  ILE   A CA    
650  C  C     . ILE   A 87  ? 0.0764 0.1934 0.1237 0.0151  0.0017  -0.0181 84  ILE   A C     
651  O  O     . ILE   A 87  ? 0.0696 0.2023 0.1310 0.0042  0.0040  -0.0022 84  ILE   A O     
652  C  CB    . ILE   A 87  ? 0.0838 0.1892 0.1111 0.0106  0.0014  -0.0206 84  ILE   A CB    
653  C  CG1   . ILE   A 87  ? 0.0740 0.2185 0.1253 0.0084  0.0111  -0.0042 84  ILE   A CG1   
654  C  CG2   . ILE   A 87  ? 0.1142 0.1882 0.1079 0.0077  -0.0224 -0.0252 84  ILE   A CG2   
655  C  CD1   . ILE   A 87  ? 0.1465 0.2398 0.1365 0.0342  0.0304  -0.0005 84  ILE   A CD1   
656  N  N     . ASN   A 88  ? 0.0752 0.2011 0.1160 -0.0015 0.0008  -0.0052 85  ASN   A N     
657  C  CA    . ASN   A 88  ? 0.0720 0.2188 0.1514 -0.0018 -0.0086 -0.0206 85  ASN   A CA    
658  C  C     . ASN   A 88  ? 0.0706 0.2411 0.1348 -0.0195 -0.0187 -0.0125 85  ASN   A C     
659  O  O     . ASN   A 88  ? 0.0767 0.2912 0.1536 -0.0220 -0.0239 -0.0375 85  ASN   A O     
660  C  CB    . ASN   A 88  ? 0.0476 0.2492 0.1430 -0.0157 -0.0091 -0.0247 85  ASN   A CB    
661  C  CG    . ASN   A 88  ? 0.0610 0.2427 0.1537 -0.0305 -0.0018 -0.0360 85  ASN   A CG    
662  O  OD1   . ASN   A 88  ? 0.0623 0.2339 0.1666 -0.0278 -0.0069 -0.0073 85  ASN   A OD1   
663  N  ND2   . ASN   A 88  ? 0.0932 0.2442 0.1998 -0.0363 -0.0291 -0.0441 85  ASN   A ND2   
664  N  N     . ASN   A 89  ? 0.0705 0.2395 0.1203 -0.0375 -0.0174 -0.0181 86  ASN   A N     
665  C  CA    . ASN   A 89  ? 0.1111 0.2388 0.1130 -0.0242 -0.0305 -0.0222 86  ASN   A CA    
666  C  C     . ASN   A 89  ? 0.0833 0.2291 0.0996 0.0048  -0.0126 -0.0099 86  ASN   A C     
667  O  O     . ASN   A 89  ? 0.0894 0.2094 0.0989 0.0128  -0.0269 -0.0034 86  ASN   A O     
668  C  CB    . ASN   A 89  ? 0.1331 0.2418 0.1342 -0.0252 0.0130  -0.0003 86  ASN   A CB    
669  C  CG    . ASN   A 89  ? 0.2643 0.2077 0.1864 -0.0313 0.0288  -0.0371 86  ASN   A CG    
670  O  OD1   . ASN   A 89  ? 0.1535 0.2503 0.1395 -0.0451 0.0269  -0.0442 86  ASN   A OD1   
671  N  ND2   . ASN   A 89  ? 0.1335 0.2801 0.3012 0.0081  -0.0003 -0.0219 86  ASN   A ND2   
672  N  N     . THR   A 90  ? 0.1037 0.2440 0.1122 0.0183  -0.0257 0.0017  87  THR   A N     
673  C  CA    . THR   A 90  ? 0.1499 0.2276 0.1158 0.0146  -0.0191 0.0028  87  THR   A CA    
674  C  C     . THR   A 90  ? 0.1163 0.2302 0.0934 -0.0114 -0.0240 0.0181  87  THR   A C     
675  O  O     . THR   A 90  ? 0.1092 0.2315 0.1272 0.0003  -0.0329 0.0226  87  THR   A O     
676  C  CB    . THR   A 90  ? 0.1533 0.2942 0.1741 0.0512  -0.0033 0.0306  87  THR   A CB    
677  O  OG1   . THR   A 90  ? 0.1752 0.3679 0.2097 0.0555  0.0017  -0.0237 87  THR   A OG1   
678  C  CG2   . THR   A 90  ? 0.2164 0.2873 0.2349 0.0088  -0.0059 0.0405  87  THR   A CG2   
679  N  N     . LYS   A 91  ? 0.1298 0.2290 0.1058 -0.0137 -0.0208 0.0015  88  LYS   A N     
680  C  CA    . LYS   A 91  ? 0.1293 0.2604 0.0945 0.0023  -0.0192 0.0032  88  LYS   A CA    
681  C  C     . LYS   A 91  ? 0.1134 0.2381 0.0882 0.0009  -0.0103 -0.0032 88  LYS   A C     
682  O  O     . LYS   A 91  ? 0.1296 0.2590 0.0946 0.0023  0.0070  0.0089  88  LYS   A O     
683  C  CB    . LYS   A 91  ? 0.1147 0.2851 0.1226 0.0195  -0.0467 -0.0252 88  LYS   A CB    
684  C  CG    . LYS   A 91  ? 0.1763 0.3653 0.2031 0.0419  -0.0111 -0.0741 88  LYS   A CG    
685  C  CD    . LYS   A 91  ? 0.3452 0.4476 0.2562 0.0393  0.0442  -0.0508 88  LYS   A CD    
686  C  CE    . LYS   A 91  ? 0.3203 0.5578 0.2283 0.0560  0.0485  -0.0758 88  LYS   A CE    
687  N  NZ    . LYS   A 91  ? 0.3534 0.5206 0.3922 0.0705  -0.0001 -0.0964 88  LYS   A NZ    
688  N  N     . SER   A 92  ? 0.0998 0.2104 0.0821 -0.0099 -0.0110 -0.0161 89  SER   A N     
689  C  CA    . SER   A 92  ? 0.0948 0.1842 0.0957 0.0061  -0.0089 -0.0173 89  SER   A CA    
690  C  C     . SER   A 92  ? 0.0857 0.1887 0.0880 -0.0029 -0.0066 -0.0092 89  SER   A C     
691  O  O     . SER   A 92  ? 0.0834 0.1966 0.1115 0.0023  0.0041  -0.0130 89  SER   A O     
692  C  CB    . SER   A 92  ? 0.1147 0.1839 0.0961 -0.0116 -0.0084 -0.0122 89  SER   A CB    
693  O  OG    . SER   A 92  ? 0.0924 0.1949 0.0817 -0.0138 -0.0133 -0.0133 89  SER   A OG    
694  N  N     . PHE   A 93  ? 0.0864 0.1855 0.0923 0.0097  -0.0077 0.0152  90  PHE   A N     
695  C  CA    . PHE   A 93  ? 0.1122 0.1831 0.1030 0.0152  0.0011  0.0240  90  PHE   A CA    
696  C  C     . PHE   A 93  ? 0.0810 0.2257 0.1123 0.0002  -0.0056 0.0304  90  PHE   A C     
697  O  O     . PHE   A 93  ? 0.0701 0.2198 0.1091 0.0104  0.0179  0.0201  90  PHE   A O     
698  C  CB    . PHE   A 93  ? 0.0850 0.1791 0.1057 0.0094  -0.0035 0.0228  90  PHE   A CB    
699  C  CG    . PHE   A 93  ? 0.0962 0.1840 0.1079 -0.0030 0.0004  0.0203  90  PHE   A CG    
700  C  CD1   . PHE   A 93  ? 0.0669 0.1779 0.1015 0.0130  0.0139  0.0201  90  PHE   A CD1   
701  C  CD2   . PHE   A 93  ? 0.1593 0.1898 0.1256 -0.0018 -0.0123 0.0233  90  PHE   A CD2   
702  C  CE1   . PHE   A 93  ? 0.1222 0.1914 0.1009 -0.0008 -0.0133 0.0174  90  PHE   A CE1   
703  C  CE2   . PHE   A 93  ? 0.2312 0.1891 0.1406 -0.0193 -0.0380 0.0433  90  PHE   A CE2   
704  C  CZ    . PHE   A 93  ? 0.1540 0.1606 0.1270 -0.0034 0.0048  0.0121  90  PHE   A CZ    
705  N  N     . GLU   A 94  ? 0.1264 0.2477 0.1052 -0.0163 -0.0078 0.0466  91  GLU   A N     
706  C  CA    . GLU   A 94  ? 0.2037 0.2491 0.1112 -0.0216 0.0117  0.0373  91  GLU   A CA    
707  C  C     . GLU   A 94  ? 0.1668 0.2749 0.1132 -0.0385 0.0293  0.0225  91  GLU   A C     
708  O  O     . GLU   A 94  ? 0.2333 0.3405 0.1816 -0.0625 0.1024  0.0069  91  GLU   A O     
709  C  CB    . GLU   A 94  ? 0.2577 0.2812 0.1066 -0.0339 -0.0084 0.0351  91  GLU   A CB    
710  C  CG    . GLU   A 94  ? 0.2546 0.2599 0.1671 -0.0464 0.0082  0.0523  91  GLU   A CG    
711  C  CD    . GLU   A 94  ? 0.2125 0.3763 0.1870 -0.0097 0.0178  0.0773  91  GLU   A CD    
712  O  OE1   . GLU   A 94  ? 0.3870 0.4486 0.2362 0.1200  -0.0821 0.0266  91  GLU   A OE1   
713  O  OE2   . GLU   A 94  ? 0.2340 0.2861 0.2199 0.0132  0.0032  0.1046  91  GLU   A OE2   
714  N  N     . ASP   A 95  ? 0.1710 0.2511 0.1006 -0.0295 0.0356  -0.0140 92  ASP   A N     
715  C  CA    . ASP   A 95  ? 0.1830 0.2747 0.1469 -0.0123 0.0501  -0.0385 92  ASP   A CA    
716  C  C     . ASP   A 95  ? 0.1726 0.2568 0.1145 -0.0062 0.0519  -0.0207 92  ASP   A C     
717  O  O     . ASP   A 95  ? 0.1882 0.2581 0.1406 -0.0082 0.0691  -0.0091 92  ASP   A O     
718  C  CB    . ASP   A 95  ? 0.2576 0.2574 0.1863 0.0072  0.0477  -0.0317 92  ASP   A CB    
719  C  CG    . ASP   A 95  ? 0.2754 0.3129 0.1820 -0.0316 0.0738  -0.0522 92  ASP   A CG    
720  O  OD1   . ASP   A 95  ? 0.2963 0.3285 0.1851 -0.0385 0.0800  -0.0621 92  ASP   A OD1   
721  O  OD2   . ASP   A 95  ? 0.5206 0.3441 0.2509 -0.0529 0.0741  0.0173  92  ASP   A OD2   
722  N  N     . ILE   A 96  ? 0.1383 0.2320 0.1086 -0.0197 0.0289  -0.0137 93  ILE   A N     
723  C  CA    . ILE   A 96  ? 0.1272 0.1970 0.1202 0.0041  0.0162  0.0013  93  ILE   A CA    
724  C  C     . ILE   A 96  ? 0.1068 0.2212 0.1011 0.0236  0.0118  0.0014  93  ILE   A C     
725  O  O     . ILE   A 96  ? 0.1043 0.2297 0.1148 0.0314  0.0243  0.0232  93  ILE   A O     
726  C  CB    . ILE   A 96  ? 0.0956 0.2262 0.1034 0.0094  0.0220  0.0011  93  ILE   A CB    
727  C  CG1   . ILE   A 96  ? 0.0849 0.2065 0.0992 0.0121  0.0214  -0.0128 93  ILE   A CG1   
728  C  CG2   . ILE   A 96  ? 0.1118 0.1923 0.1296 -0.0033 0.0190  0.0001  93  ILE   A CG2   
729  C  CD1   . ILE   A 96  ? 0.1108 0.2419 0.1080 -0.0082 0.0045  0.0175  93  ILE   A CD1   
730  N  N     . HIS   A 97  ? 0.0999 0.2146 0.1199 0.0185  0.0061  0.0104  94  HIS   A N     
731  C  CA    . HIS   A 97  ? 0.1150 0.2248 0.1417 0.0158  0.0267  0.0155  94  HIS   A CA    
732  C  C     . HIS   A 97  ? 0.1113 0.2210 0.1266 0.0217  0.0243  0.0327  94  HIS   A C     
733  O  O     . HIS   A 97  ? 0.1097 0.2712 0.1373 0.0049  0.0170  0.0240  94  HIS   A O     
734  C  CB    . HIS   A 97  ? 0.1344 0.2397 0.1690 0.0100  0.0439  0.0365  94  HIS   A CB    
735  C  CG    . HIS   A 97  ? 0.1733 0.2952 0.1947 0.0182  0.0250  0.0068  94  HIS   A CG    
736  N  ND1   . HIS   A 97  ? 0.2203 0.3117 0.2179 -0.0356 -0.0016 0.0201  94  HIS   A ND1   
737  C  CD2   . HIS   A 97  ? 0.2287 0.3534 0.1877 0.0435  0.0372  0.0136  94  HIS   A CD2   
738  C  CE1   . HIS   A 97  ? 0.2483 0.3407 0.1955 0.0066  0.0161  0.0198  94  HIS   A CE1   
739  N  NE2   . HIS   A 97  ? 0.2630 0.4057 0.2192 -0.0249 0.0134  0.0601  94  HIS   A NE2   
740  N  N     . HIS   A 98  ? 0.0883 0.2251 0.1290 0.0244  0.0205  0.0221  95  HIS   A N     
741  C  CA    . HIS   A 98  ? 0.1299 0.2367 0.1124 0.0120  0.0232  0.0021  95  HIS   A CA    
742  C  C     . HIS   A 98  ? 0.1061 0.2424 0.1193 0.0080  0.0243  0.0035  95  HIS   A C     
743  O  O     . HIS   A 98  ? 0.0993 0.2584 0.1384 0.0312  0.0119  0.0176  95  HIS   A O     
744  C  CB    . HIS   A 98  ? 0.1462 0.2945 0.1502 0.0093  0.0012  -0.0354 95  HIS   A CB    
745  C  CG    . HIS   A 98  ? 0.1700 0.3893 0.1646 0.0014  -0.0183 -0.0106 95  HIS   A CG    
746  N  ND1   . HIS   A 98  ? 0.2196 0.4878 0.1682 0.0426  0.0035  0.0228  95  HIS   A ND1   
747  C  CD2   . HIS   A 98  ? 0.1775 0.4744 0.2305 0.0287  -0.0234 0.0204  95  HIS   A CD2   
748  C  CE1   . HIS   A 98  ? 0.2376 0.4563 0.2219 0.0618  -0.0109 0.0523  95  HIS   A CE1   
749  N  NE2   . HIS   A 98  ? 0.1893 0.5016 0.2280 0.0002  -0.0676 0.0147  95  HIS   A NE2   
750  N  N     . TYR   A 99  ? 0.0992 0.2461 0.1291 0.0059  0.0158  0.0225  96  TYR   A N     
751  C  CA    . TYR   A 99  ? 0.1432 0.2350 0.1381 0.0456  0.0244  0.0290  96  TYR   A CA    
752  C  C     . TYR   A 99  ? 0.1173 0.2690 0.1198 0.0477  0.0134  0.0135  96  TYR   A C     
753  O  O     . TYR   A 99  ? 0.1201 0.2987 0.1194 0.0650  0.0027  0.0043  96  TYR   A O     
754  C  CB    . TYR   A 99  ? 0.1573 0.2610 0.1533 0.0803  0.0327  0.0487  96  TYR   A CB    
755  C  CG    . TYR   A 99  ? 0.1875 0.2223 0.1796 0.0716  0.0883  0.0288  96  TYR   A CG    
756  C  CD1   . TYR   A 99  ? 0.2390 0.2377 0.2352 0.0783  0.0532  -0.0032 96  TYR   A CD1   
757  C  CD2   . TYR   A 99  ? 0.1850 0.2219 0.2117 0.0516  0.0513  0.0235  96  TYR   A CD2   
758  C  CE1   . TYR   A 99  ? 0.2601 0.2612 0.2032 0.0301  0.0757  0.0244  96  TYR   A CE1   
759  C  CE2   . TYR   A 99  ? 0.2632 0.2021 0.1995 0.0392  0.0800  0.0109  96  TYR   A CE2   
760  C  CZ    . TYR   A 99  ? 0.2494 0.2104 0.2624 0.0299  0.0780  0.0075  96  TYR   A CZ    
761  O  OH    . TYR   A 99  ? 0.1748 0.2651 0.2773 0.0019  0.0566  0.0179  96  TYR   A OH    
762  N  N     . ARG   A 100 ? 0.1400 0.2742 0.1427 0.0767  -0.0089 -0.0021 97  ARG   A N     
763  C  CA    . ARG   A 100 ? 0.1599 0.3007 0.1404 0.0540  0.0064  -0.0362 97  ARG   A CA    
764  C  C     . ARG   A 100 ? 0.1166 0.2696 0.1503 0.0367  -0.0040 -0.0405 97  ARG   A C     
765  O  O     . ARG   A 100 ? 0.1072 0.3197 0.1757 0.0350  0.0004  -0.0477 97  ARG   A O     
766  C  CB    . ARG   A 100 ? 0.1712 0.2788 0.1887 0.0166  0.0216  -0.0314 97  ARG   A CB    
767  C  CG    . ARG   A 100 ? 0.1121 0.3081 0.2316 0.0295  0.0290  -0.0472 97  ARG   A CG    
768  C  CD    . ARG   A 100 ? 0.2127 0.2896 0.2710 0.0110  0.0439  -0.0673 97  ARG   A CD    
769  N  NE    . ARG   A 100 ? 0.2432 0.2882 0.2973 -0.0032 0.0473  -0.0338 97  ARG   A NE    
770  C  CZ    . ARG   A 100 ? 0.2720 0.3067 0.3244 0.0155  0.0218  -0.0232 97  ARG   A CZ    
771  N  NH1   . ARG   A 100 ? 0.3359 0.2927 0.2999 0.0139  0.0409  -0.0334 97  ARG   A NH1   
772  N  NH2   . ARG   A 100 ? 0.3548 0.3397 0.4274 -0.0521 0.0284  -0.0196 97  ARG   A NH2   
773  N  N     . GLU   A 101 ? 0.1031 0.3050 0.1397 0.0227  0.0233  0.0055  98  GLU   A N     
774  C  CA    . GLU   A 101 ? 0.1359 0.3177 0.1516 0.0106  0.0417  0.0033  98  GLU   A CA    
775  C  C     . GLU   A 101 ? 0.1064 0.3177 0.1203 0.0180  0.0086  -0.0068 98  GLU   A C     
776  O  O     . GLU   A 101 ? 0.1028 0.3455 0.1608 0.0029  0.0111  -0.0236 98  GLU   A O     
777  C  CB    . GLU   A 101 ? 0.1305 0.3565 0.1625 0.0330  0.0418  0.0504  98  GLU   A CB    
778  C  CG    . GLU   A 101 ? 0.2118 0.3828 0.2734 0.0456  0.0595  0.0613  98  GLU   A CG    
779  C  CD    . GLU   A 101 ? 0.3534 0.4450 0.4258 -0.0327 0.0572  0.0565  98  GLU   A CD    
780  O  OE1   . GLU   A 101 ? 0.3996 0.5589 0.4589 -0.0190 0.1097  0.1163  98  GLU   A OE1   
781  O  OE2   . GLU   A 101 ? 0.6085 0.4519 0.6567 0.0345  0.0695  -0.0119 98  GLU   A OE2   
782  N  N     . GLN   A 102 ? 0.1019 0.3044 0.1242 0.0256  0.0093  -0.0180 99  GLN   A N     
783  C  CA    . GLN   A 102 ? 0.1162 0.3040 0.1544 0.0178  -0.0072 -0.0505 99  GLN   A CA    
784  C  C     . GLN   A 102 ? 0.1072 0.2853 0.1386 0.0538  0.0014  -0.0525 99  GLN   A C     
785  O  O     . GLN   A 102 ? 0.0887 0.2801 0.1571 0.0249  0.0087  -0.0522 99  GLN   A O     
786  C  CB    . GLN   A 102 ? 0.1093 0.3280 0.1773 0.0093  0.0279  -0.0615 99  GLN   A CB    
787  C  CG    . GLN   A 102 ? 0.1507 0.3154 0.2057 -0.0279 0.0072  -0.0565 99  GLN   A CG    
788  C  CD    . GLN   A 102 ? 0.2013 0.3231 0.2242 -0.0559 -0.0029 -0.0606 99  GLN   A CD    
789  O  OE1   . GLN   A 102 ? 0.2829 0.4155 0.2332 -0.0314 -0.0250 0.0032  99  GLN   A OE1   
790  N  NE2   . GLN   A 102 ? 0.3785 0.4546 0.2777 -0.0803 -0.1052 -0.0569 99  GLN   A NE2   
791  N  N     . ILE   A 103 ? 0.0856 0.2575 0.1218 0.0372  -0.0142 -0.0432 100 ILE   A N     
792  C  CA    . ILE   A 103 ? 0.1212 0.2276 0.1212 0.0140  -0.0290 -0.0391 100 ILE   A CA    
793  C  C     . ILE   A 103 ? 0.1123 0.2501 0.1307 0.0220  -0.0181 -0.0367 100 ILE   A C     
794  O  O     . ILE   A 103 ? 0.0895 0.2783 0.1616 0.0066  0.0030  -0.0413 100 ILE   A O     
795  C  CB    . ILE   A 103 ? 0.1101 0.1962 0.1322 0.0216  -0.0192 -0.0165 100 ILE   A CB    
796  C  CG1   . ILE   A 103 ? 0.1137 0.1835 0.1542 0.0265  -0.0219 0.0022  100 ILE   A CG1   
797  C  CG2   . ILE   A 103 ? 0.1024 0.2439 0.1463 0.0071  -0.0198 -0.0346 100 ILE   A CG2   
798  C  CD1   . ILE   A 103 ? 0.1155 0.2040 0.1590 0.0131  -0.0084 -0.0079 100 ILE   A CD1   
799  N  N     . LYS   A 104 ? 0.0906 0.2687 0.1498 0.0332  -0.0130 -0.0266 101 LYS   A N     
800  C  CA    . LYS   A 104 ? 0.1624 0.2419 0.1735 0.0096  0.0287  -0.0469 101 LYS   A CA    
801  C  C     . LYS   A 104 ? 0.1144 0.2723 0.1606 0.0028  0.0157  -0.0200 101 LYS   A C     
802  O  O     . LYS   A 104 ? 0.1092 0.2843 0.1890 -0.0098 0.0244  -0.0218 101 LYS   A O     
803  C  CB    . LYS   A 104 ? 0.1600 0.2671 0.2154 0.0113  0.0419  0.0006  101 LYS   A CB    
804  C  CG    . LYS   A 104 ? 0.2284 0.2880 0.2432 0.0255  0.0302  -0.0397 101 LYS   A CG    
805  C  CD    . LYS   A 104 ? 0.3773 0.3182 0.3888 0.0714  0.0073  0.0046  101 LYS   A CD    
806  C  CE    . LYS   A 104 ? 0.3934 0.4067 0.4299 0.0516  -0.0111 0.0004  101 LYS   A CE    
807  N  NZ    . LYS   A 104 ? 0.4509 0.4703 0.5221 0.0888  0.0923  0.0860  101 LYS   A NZ    
808  N  N     . ARG   A 105 ? 0.0853 0.2818 0.1566 0.0064  0.0110  -0.0189 102 ARG   A N     
809  C  CA    . ARG   A 105 ? 0.1061 0.3454 0.1586 -0.0022 0.0405  -0.0232 102 ARG   A CA    
810  C  C     . ARG   A 105 ? 0.1001 0.3014 0.1770 -0.0205 0.0228  -0.0563 102 ARG   A C     
811  O  O     . ARG   A 105 ? 0.0932 0.3312 0.2053 -0.0182 0.0200  -0.0490 102 ARG   A O     
812  C  CB    . ARG   A 105 ? 0.1520 0.3937 0.1937 -0.0047 0.0326  -0.0709 102 ARG   A CB    
813  C  CG    . ARG   A 105 ? 0.1858 0.4939 0.2305 0.0284  0.0452  -0.0893 102 ARG   A CG    
814  C  CD    . ARG   A 105 ? 0.3183 0.5134 0.2250 -0.0058 0.0149  -0.0808 102 ARG   A CD    
815  N  NE    . ARG   A 105 ? 0.3910 0.6188 0.3203 -0.0715 0.0377  -0.0232 102 ARG   A NE    
816  C  CZ    . ARG   A 105 ? 0.4469 0.6262 0.4318 -0.0460 0.0085  0.0408  102 ARG   A CZ    
817  N  NH1   . ARG   A 105 ? 0.6134 0.5991 0.5245 0.0123  0.0377  0.0132  102 ARG   A NH1   
818  N  NH2   . ARG   A 105 ? 0.5638 0.6045 0.2959 -0.1370 -0.0027 -0.0328 102 ARG   A NH2   
819  N  N     . VAL   A 106 ? 0.1023 0.2889 0.1686 0.0160  0.0167  -0.0554 103 VAL   A N     
820  C  CA    . VAL   A 106 ? 0.1115 0.3126 0.1780 0.0218  0.0001  -0.0580 103 VAL   A CA    
821  C  C     . VAL   A 106 ? 0.0772 0.3210 0.2177 0.0357  -0.0167 -0.0521 103 VAL   A C     
822  O  O     . VAL   A 106 ? 0.0734 0.3365 0.2474 0.0338  -0.0028 -0.0343 103 VAL   A O     
823  C  CB    . VAL   A 106 ? 0.1053 0.2878 0.2570 0.0233  -0.0190 -0.0482 103 VAL   A CB    
824  C  CG1   . VAL   A 106 ? 0.1519 0.3227 0.2678 0.0691  -0.0271 -0.0610 103 VAL   A CG1   
825  C  CG2   . VAL   A 106 ? 0.1073 0.2446 0.2631 0.0252  -0.0095 -0.0501 103 VAL   A CG2   
826  N  N     . LYS   A 107 ? 0.0861 0.2903 0.1866 0.0093  -0.0288 -0.0313 104 LYS   A N     
827  C  CA    . LYS   A 107 ? 0.0791 0.3548 0.1721 -0.0022 -0.0150 -0.0390 104 LYS   A CA    
828  C  C     . LYS   A 107 ? 0.0660 0.3895 0.1941 0.0155  0.0283  -0.0249 104 LYS   A C     
829  O  O     . LYS   A 107 ? 0.1095 0.4065 0.2439 -0.0418 -0.0091 -0.0267 104 LYS   A O     
830  C  CB    . LYS   A 107 ? 0.1216 0.3035 0.1854 0.0160  -0.0104 -0.0328 104 LYS   A CB    
831  C  CG    . LYS   A 107 ? 0.1387 0.3218 0.1674 -0.0052 -0.0239 -0.0247 104 LYS   A CG    
832  C  CD    . LYS   A 107 ? 0.1144 0.2781 0.1640 -0.0192 0.0093  -0.0471 104 LYS   A CD    
833  C  CE    . LYS   A 107 ? 0.1367 0.2487 0.1664 -0.0220 0.0230  -0.0551 104 LYS   A CE    
834  N  NZ    . LYS   A 107 ? 0.1612 0.2435 0.2013 -0.0102 0.0111  -0.0637 104 LYS   A NZ    
835  N  N     . ASP   A 108 ? 0.1169 0.3877 0.1749 -0.0073 0.0156  -0.0419 105 ASP   A N     
836  C  CA    . ASP   A 108 ? 0.1429 0.3713 0.2020 -0.0245 0.0267  -0.0385 105 ASP   A CA    
837  C  C     . ASP   A 108 ? 0.1009 0.3057 0.2282 0.0031  0.0289  -0.0048 105 ASP   A C     
838  O  O     . ASP   A 108 ? 0.1134 0.4340 0.2563 -0.0370 0.0661  -0.0506 105 ASP   A O     
839  C  CB    . ASP   A 108 ? 0.1378 0.4029 0.2558 -0.0389 0.0584  -0.0433 105 ASP   A CB    
840  C  CG    . ASP   A 108 ? 0.1917 0.4562 0.2031 0.0079  0.0631  0.0470  105 ASP   A CG    
841  O  OD1   . ASP   A 108 ? 0.2628 0.5566 0.2197 0.0398  -0.0130 0.0613  105 ASP   A OD1   
842  O  OD2   . ASP   A 108 ? 0.1906 0.5424 0.3676 0.0701  0.0473  -0.0066 105 ASP   A OD2   
843  N  N     . SER   A 109 ? 0.1362 0.3353 0.2536 -0.0144 0.0559  -0.0573 106 SER   A N     
844  C  CA    . SER   A 109 ? 0.1018 0.3261 0.2527 -0.0049 0.0143  -0.0495 106 SER   A CA    
845  C  C     . SER   A 109 ? 0.0988 0.3222 0.2760 -0.0044 0.0287  -0.0098 106 SER   A C     
846  O  O     . SER   A 109 ? 0.0822 0.4642 0.2987 -0.0141 0.0108  -0.0397 106 SER   A O     
847  C  CB    . SER   A 109 ? 0.1402 0.4136 0.2217 -0.0277 0.0035  -0.0744 106 SER   A CB    
848  O  OG    . SER   A 109 ? 0.1380 0.4314 0.2904 -0.0004 0.0049  -0.1149 106 SER   A OG    
849  N  N     . GLU   A 110 ? 0.1896 0.2968 0.3828 -0.0505 0.0314  0.0106  107 GLU   A N     
850  C  CA    . GLU   A 110 ? 0.2519 0.3328 0.4325 0.0054  0.0258  0.0226  107 GLU   A CA    
851  C  C     . GLU   A 110 ? 0.1758 0.2840 0.4043 0.0229  0.0275  -0.0106 107 GLU   A C     
852  O  O     . GLU   A 110 ? 0.2254 0.3119 0.4690 0.0518  0.0665  -0.0409 107 GLU   A O     
853  C  CB    . GLU   A 110 ? 0.3960 0.3424 0.4235 0.0112  0.0000  0.0779  107 GLU   A CB    
854  C  CG    . GLU   A 110 ? 0.5008 0.3789 0.4158 -0.0059 -0.0184 0.1007  107 GLU   A CG    
855  C  CD    . GLU   A 110 ? 0.5136 0.4904 0.5374 -0.0063 -0.0509 0.0486  107 GLU   A CD    
856  O  OE1   . GLU   A 110 ? 0.6448 0.7277 0.6255 0.0381  0.0235  0.0714  107 GLU   A OE1   
857  O  OE2   . GLU   A 110 ? 0.7299 0.6969 0.5683 0.0195  -0.1389 0.0876  107 GLU   A OE2   
858  N  N     . ASP   A 111 ? 0.1757 0.3442 0.3119 0.0047  0.0437  -0.0322 108 ASP   A N     
859  C  CA    . ASP   A 111 ? 0.1615 0.3246 0.3154 -0.0038 0.0470  0.0050  108 ASP   A CA    
860  C  C     . ASP   A 111 ? 0.1307 0.2980 0.3143 0.0097  0.0725  -0.0360 108 ASP   A C     
861  O  O     . ASP   A 111 ? 0.1606 0.3430 0.5919 0.0259  0.0257  0.0203  108 ASP   A O     
862  C  CB    . ASP   A 111 ? 0.1689 0.2743 0.2957 -0.0217 0.0559  -0.0045 108 ASP   A CB    
863  C  CG    . ASP   A 111 ? 0.1631 0.3200 0.3213 -0.0600 0.0042  0.0104  108 ASP   A CG    
864  O  OD1   . ASP   A 111 ? 0.1832 0.3289 0.4487 -0.0179 0.0043  0.0265  108 ASP   A OD1   
865  O  OD2   . ASP   A 111 ? 0.1849 0.3397 0.3696 -0.0470 -0.0407 0.0032  108 ASP   A OD2   
866  N  N     . VAL   A 112 ? 0.1448 0.2546 0.2138 -0.0207 0.0562  -0.0390 109 VAL   A N     
867  C  CA    . VAL   A 112 ? 0.1551 0.2421 0.1525 0.0059  0.0478  -0.0127 109 VAL   A CA    
868  C  C     . VAL   A 112 ? 0.1174 0.2073 0.1467 0.0055  0.0307  -0.0210 109 VAL   A C     
869  O  O     . VAL   A 112 ? 0.1100 0.2209 0.1841 -0.0060 0.0154  0.0177  109 VAL   A O     
870  C  CB    . VAL   A 112 ? 0.2453 0.2798 0.1965 -0.0780 0.0505  -0.0524 109 VAL   A CB    
871  C  CG1   . VAL   A 112 ? 0.4135 0.2892 0.2383 -0.0865 0.0795  -0.0489 109 VAL   A CG1   
872  C  CG2   . VAL   A 112 ? 0.2986 0.2956 0.1942 -0.0376 0.0653  -0.0718 109 VAL   A CG2   
873  N  N     . PRO   A 113 ? 0.0864 0.1825 0.1445 -0.0214 0.0189  -0.0257 110 PRO   A N     
874  C  CA    . PRO   A 113 ? 0.0563 0.1775 0.1467 -0.0091 0.0049  -0.0298 110 PRO   A CA    
875  C  C     . PRO   A 113 ? 0.0595 0.1580 0.1380 -0.0001 -0.0088 -0.0244 110 PRO   A C     
876  O  O     . PRO   A 113 ? 0.0640 0.1600 0.1442 0.0001  0.0005  -0.0213 110 PRO   A O     
877  C  CB    . PRO   A 113 ? 0.0647 0.1934 0.1389 0.0129  0.0011  -0.0384 110 PRO   A CB    
878  C  CG    . PRO   A 113 ? 0.0656 0.2190 0.1695 0.0094  0.0039  -0.0310 110 PRO   A CG    
879  C  CD    . PRO   A 113 ? 0.0762 0.2232 0.1626 -0.0085 0.0221  -0.0309 110 PRO   A CD    
880  N  N     A MET   A 114 ? 0.0633 0.1579 0.1403 0.0043  -0.0082 -0.0192 111 MET   A N     
881  N  N     B MET   A 114 ? 0.0587 0.1461 0.1462 -0.0034 -0.0016 -0.0240 111 MET   A N     
882  C  CA    A MET   A 114 ? 0.0702 0.1641 0.1408 -0.0013 -0.0125 -0.0208 111 MET   A CA    
883  C  CA    B MET   A 114 ? 0.0712 0.1427 0.1302 0.0051  -0.0193 -0.0257 111 MET   A CA    
884  C  C     A MET   A 114 ? 0.0601 0.1429 0.1250 -0.0064 -0.0187 -0.0161 111 MET   A C     
885  C  C     B MET   A 114 ? 0.0546 0.1392 0.1255 -0.0034 -0.0208 -0.0237 111 MET   A C     
886  O  O     A MET   A 114 ? 0.0852 0.1372 0.1538 -0.0098 0.0018  -0.0131 111 MET   A O     
887  O  O     B MET   A 114 ? 0.0480 0.1406 0.1669 -0.0045 -0.0110 -0.0286 111 MET   A O     
888  C  CB    A MET   A 114 ? 0.1142 0.1992 0.1402 -0.0043 0.0144  -0.0092 111 MET   A CB    
889  C  CB    B MET   A 114 ? 0.0946 0.1499 0.1247 0.0133  -0.0014 -0.0373 111 MET   A CB    
890  C  CG    A MET   A 114 ? 0.1354 0.2402 0.1513 -0.0024 0.0258  -0.0206 111 MET   A CG    
891  C  CG    B MET   A 114 ? 0.1215 0.1720 0.1204 0.0167  -0.0251 -0.0375 111 MET   A CG    
892  S  SD    A MET   A 114 ? 0.1585 0.3139 0.1710 0.0168  -0.0001 -0.0230 111 MET   A SD    
893  S  SD    B MET   A 114 ? 0.1467 0.2238 0.1253 0.0157  -0.0229 -0.0420 111 MET   A SD    
894  C  CE    A MET   A 114 ? 0.1663 0.2791 0.1677 0.0362  -0.0124 -0.0310 111 MET   A CE    
895  C  CE    B MET   A 114 ? 0.1435 0.1825 0.1489 0.0038  -0.0114 -0.0220 111 MET   A CE    
896  N  N     . VAL   A 115 ? 0.0591 0.1424 0.1152 -0.0036 -0.0124 -0.0264 112 VAL   A N     
897  C  CA    . VAL   A 115 ? 0.0753 0.1246 0.1016 -0.0006 -0.0111 -0.0257 112 VAL   A CA    
898  C  C     . VAL   A 115 ? 0.0501 0.1313 0.0944 -0.0035 0.0062  -0.0139 112 VAL   A C     
899  O  O     . VAL   A 115 ? 0.0588 0.1400 0.1182 0.0043  -0.0086 -0.0224 112 VAL   A O     
900  C  CB    . VAL   A 115 ? 0.0957 0.1281 0.1031 -0.0054 -0.0122 -0.0174 112 VAL   A CB    
901  C  CG1   . VAL   A 115 ? 0.0915 0.1601 0.0978 -0.0166 0.0027  -0.0102 112 VAL   A CG1   
902  C  CG2   . VAL   A 115 ? 0.0969 0.1580 0.1113 0.0054  -0.0208 -0.0193 112 VAL   A CG2   
903  N  N     . LEU   A 116 ? 0.0389 0.1332 0.0981 -0.0070 0.0140  -0.0099 113 LEU   A N     
904  C  CA    . LEU   A 116 ? 0.0441 0.1410 0.1126 -0.0031 -0.0001 -0.0083 113 LEU   A CA    
905  C  C     . LEU   A 116 ? 0.0485 0.1259 0.0951 0.0115  -0.0009 -0.0065 113 LEU   A C     
906  O  O     . LEU   A 116 ? 0.0518 0.1234 0.1137 -0.0031 0.0002  -0.0208 113 LEU   A O     
907  C  CB    . LEU   A 116 ? 0.0705 0.1412 0.0941 -0.0011 0.0157  -0.0077 113 LEU   A CB    
908  C  CG    . LEU   A 116 ? 0.0807 0.1437 0.1043 -0.0004 0.0054  -0.0112 113 LEU   A CG    
909  C  CD1   . LEU   A 116 ? 0.0880 0.1671 0.1050 -0.0111 0.0180  -0.0174 113 LEU   A CD1   
910  C  CD2   . LEU   A 116 ? 0.1025 0.1534 0.1132 -0.0190 -0.0192 -0.0026 113 LEU   A CD2   
911  N  N     . VAL   A 117 ? 0.0673 0.1292 0.0843 0.0043  0.0020  -0.0076 114 VAL   A N     
912  C  CA    . VAL   A 117 ? 0.0673 0.1286 0.0851 -0.0100 -0.0048 -0.0096 114 VAL   A CA    
913  C  C     . VAL   A 117 ? 0.0577 0.1154 0.0930 -0.0025 -0.0028 -0.0015 114 VAL   A C     
914  O  O     . VAL   A 117 ? 0.0524 0.1404 0.0937 -0.0081 0.0032  -0.0092 114 VAL   A O     
915  C  CB    . VAL   A 117 ? 0.0679 0.1376 0.0966 -0.0075 -0.0099 -0.0050 114 VAL   A CB    
916  C  CG1   . VAL   A 117 ? 0.0898 0.1474 0.0880 0.0029  0.0017  -0.0023 114 VAL   A CG1   
917  C  CG2   . VAL   A 117 ? 0.1057 0.1500 0.1280 -0.0029 -0.0460 -0.0071 114 VAL   A CG2   
918  N  N     . GLY   A 118 ? 0.0692 0.1193 0.0772 0.0062  -0.0071 -0.0002 115 GLY   A N     
919  C  CA    . GLY   A 118 ? 0.0687 0.1313 0.0755 0.0054  -0.0077 -0.0011 115 GLY   A CA    
920  C  C     . GLY   A 118 ? 0.0667 0.1411 0.0835 0.0061  -0.0030 -0.0003 115 GLY   A C     
921  O  O     . GLY   A 118 ? 0.0774 0.1535 0.0865 -0.0044 0.0026  -0.0105 115 GLY   A O     
922  N  N     . ASN   A 119 ? 0.0711 0.1485 0.0729 -0.0016 -0.0055 -0.0053 116 ASN   A N     
923  C  CA    . ASN   A 119 ? 0.0614 0.1644 0.0779 -0.0131 0.0109  -0.0165 116 ASN   A CA    
924  C  C     . ASN   A 119 ? 0.0650 0.1734 0.0782 -0.0129 0.0111  -0.0161 116 ASN   A C     
925  O  O     . ASN   A 119 ? 0.0829 0.1729 0.0979 -0.0149 -0.0080 -0.0131 116 ASN   A O     
926  C  CB    . ASN   A 119 ? 0.0848 0.1561 0.0816 -0.0179 0.0099  -0.0164 116 ASN   A CB    
927  C  CG    . ASN   A 119 ? 0.0828 0.1505 0.0929 -0.0186 0.0001  -0.0119 116 ASN   A CG    
928  O  OD1   . ASN   A 119 ? 0.1080 0.1636 0.0840 -0.0381 -0.0032 -0.0074 116 ASN   A OD1   
929  N  ND2   . ASN   A 119 ? 0.1029 0.1577 0.0968 -0.0339 -0.0095 -0.0110 116 ASN   A ND2   
930  N  N     . LYS   A 120 ? 0.0634 0.1695 0.1004 -0.0239 0.0069  -0.0077 117 LYS   A N     
931  C  CA    . LYS   A 120 ? 0.0635 0.2019 0.1005 -0.0354 0.0110  -0.0211 117 LYS   A CA    
932  C  C     . LYS   A 120 ? 0.0826 0.2011 0.0868 -0.0244 0.0063  -0.0193 117 LYS   A C     
933  O  O     . LYS   A 120 ? 0.0702 0.1985 0.1246 -0.0207 -0.0050 -0.0330 117 LYS   A O     
934  C  CB    . LYS   A 120 ? 0.0936 0.1953 0.1161 -0.0429 0.0149  -0.0380 117 LYS   A CB    
935  C  CG    . LYS   A 120 ? 0.0834 0.1896 0.0921 -0.0324 -0.0038 -0.0254 117 LYS   A CG    
936  C  CD    . LYS   A 120 ? 0.0959 0.1829 0.1244 -0.0583 0.0060  -0.0356 117 LYS   A CD    
937  C  CE    . LYS   A 120 ? 0.1080 0.1985 0.1248 -0.0365 -0.0140 -0.0288 117 LYS   A CE    
938  N  NZ    . LYS   A 120 ? 0.1089 0.2099 0.1271 -0.0337 -0.0091 -0.0393 117 LYS   A NZ    
939  N  N     . SER   A 121 ? 0.0626 0.2002 0.1031 -0.0122 -0.0057 -0.0259 118 SER   A N     
940  C  CA    . SER   A 121 ? 0.0863 0.2039 0.1382 -0.0036 0.0146  -0.0288 118 SER   A CA    
941  C  C     . SER   A 121 ? 0.0753 0.2460 0.1294 -0.0120 0.0017  -0.0533 118 SER   A C     
942  O  O     . SER   A 121 ? 0.0685 0.2833 0.1570 -0.0015 0.0009  -0.0582 118 SER   A O     
943  C  CB    . SER   A 121 ? 0.0805 0.2178 0.1486 -0.0187 0.0119  -0.0286 118 SER   A CB    
944  O  OG    . SER   A 121 ? 0.1025 0.2043 0.1320 -0.0248 0.0109  -0.0423 118 SER   A OG    
945  N  N     . ASP   A 122 ? 0.0654 0.2466 0.1210 -0.0178 -0.0032 -0.0421 119 ASP   A N     
946  C  CA    . ASP   A 122 ? 0.0874 0.2443 0.1379 -0.0258 0.0228  -0.0566 119 ASP   A CA    
947  C  C     . ASP   A 122 ? 0.0625 0.2685 0.1523 -0.0145 0.0272  -0.0501 119 ASP   A C     
948  O  O     . ASP   A 122 ? 0.0663 0.3916 0.1653 -0.0402 0.0346  -0.0688 119 ASP   A O     
949  C  CB    . ASP   A 122 ? 0.1110 0.2643 0.1280 -0.0574 0.0496  -0.0327 119 ASP   A CB    
950  C  CG    . ASP   A 122 ? 0.0846 0.2563 0.1687 -0.0454 0.0411  -0.0366 119 ASP   A CG    
951  O  OD1   . ASP   A 122 ? 0.0852 0.2637 0.1432 -0.0467 0.0350  -0.0462 119 ASP   A OD1   
952  O  OD2   . ASP   A 122 ? 0.0912 0.2534 0.2351 -0.0533 0.0501  -0.0426 119 ASP   A OD2   
953  N  N     . LEU   A 123 ? 0.0692 0.2760 0.1430 -0.0123 0.0047  -0.0779 120 LEU   A N     
954  C  CA    . LEU   A 123 ? 0.0635 0.2459 0.1753 -0.0039 -0.0079 -0.0677 120 LEU   A CA    
955  C  C     . LEU   A 123 ? 0.0406 0.2482 0.1674 -0.0093 0.0114  -0.0482 120 LEU   A C     
956  O  O     . LEU   A 123 ? 0.0708 0.2681 0.2003 -0.0323 0.0270  -0.0502 120 LEU   A O     
957  C  CB    . LEU   A 123 ? 0.0443 0.2823 0.1507 -0.0226 -0.0073 -0.0616 120 LEU   A CB    
958  C  CG    . LEU   A 123 ? 0.0916 0.2765 0.1927 -0.0234 0.0071  -0.0740 120 LEU   A CG    
959  C  CD1   . LEU   A 123 ? 0.0954 0.2932 0.1802 -0.0142 -0.0041 -0.0823 120 LEU   A CD1   
960  C  CD2   . LEU   A 123 ? 0.1320 0.2494 0.2348 -0.0499 -0.0051 -0.0772 120 LEU   A CD2   
961  N  N     . PRO   A 124 ? 0.0390 0.2595 0.1860 -0.0155 0.0043  -0.0693 121 PRO   A N     
962  C  CA    . PRO   A 124 ? 0.0686 0.2402 0.1562 -0.0200 -0.0031 -0.0649 121 PRO   A CA    
963  C  C     . PRO   A 124 ? 0.0721 0.2193 0.1827 -0.0179 -0.0037 -0.0479 121 PRO   A C     
964  O  O     . PRO   A 124 ? 0.1329 0.2317 0.2079 -0.0054 0.0244  -0.0330 121 PRO   A O     
965  C  CB    . PRO   A 124 ? 0.0685 0.2742 0.1903 0.0065  0.0145  -0.0716 121 PRO   A CB    
966  C  CG    . PRO   A 124 ? 0.0355 0.2949 0.1808 -0.0378 0.0086  -0.0462 121 PRO   A CG    
967  C  CD    . PRO   A 124 ? 0.0423 0.3010 0.1766 -0.0296 -0.0042 -0.0509 121 PRO   A CD    
968  N  N     . SER   A 125 ? 0.0786 0.2311 0.1654 0.0034  0.0255  -0.0481 122 SER   A N     
969  C  CA    . SER   A 125 ? 0.0833 0.2379 0.1858 -0.0028 0.0092  -0.0455 122 SER   A CA    
970  C  C     . SER   A 125 ? 0.0567 0.2593 0.1728 0.0212  -0.0145 -0.0506 122 SER   A C     
971  O  O     . SER   A 125 ? 0.0891 0.2746 0.1784 -0.0031 0.0148  -0.0546 122 SER   A O     
972  C  CB    . SER   A 125 ? 0.0701 0.2658 0.1932 -0.0175 0.0198  -0.0605 122 SER   A CB    
973  O  OG    . SER   A 125 ? 0.0548 0.3107 0.2152 -0.0023 -0.0126 -0.0401 122 SER   A OG    
974  N  N     . ARG   A 126 ? 0.0576 0.2744 0.1537 0.0047  -0.0029 -0.0366 123 ARG   A N     
975  C  CA    . ARG   A 126 ? 0.0641 0.2370 0.1635 0.0079  -0.0083 -0.0039 123 ARG   A CA    
976  C  C     . ARG   A 126 ? 0.0513 0.2632 0.1660 0.0102  -0.0030 -0.0128 123 ARG   A C     
977  O  O     . ARG   A 126 ? 0.0803 0.2913 0.1875 0.0367  -0.0091 -0.0063 123 ARG   A O     
978  C  CB    . ARG   A 126 ? 0.0909 0.2488 0.1503 -0.0015 -0.0033 -0.0098 123 ARG   A CB    
979  C  CG    . ARG   A 126 ? 0.0771 0.2465 0.1361 0.0138  -0.0102 -0.0125 123 ARG   A CG    
980  C  CD    . ARG   A 126 ? 0.0618 0.2306 0.1756 0.0110  -0.0035 -0.0076 123 ARG   A CD    
981  N  NE    . ARG   A 126 ? 0.0729 0.2361 0.1573 -0.0019 0.0064  -0.0095 123 ARG   A NE    
982  C  CZ    . ARG   A 126 ? 0.0875 0.2443 0.1460 0.0200  0.0038  -0.0082 123 ARG   A CZ    
983  N  NH1   . ARG   A 126 ? 0.1094 0.2501 0.1120 0.0351  -0.0009 0.0052  123 ARG   A NH1   
984  N  NH2   . ARG   A 126 ? 0.0923 0.2681 0.1452 0.0052  0.0207  -0.0127 123 ARG   A NH2   
985  N  N     . THR   A 127 ? 0.0508 0.2416 0.1433 0.0138  -0.0164 -0.0131 124 THR   A N     
986  C  CA    . THR   A 127 ? 0.0628 0.2653 0.1399 0.0161  -0.0290 -0.0057 124 THR   A CA    
987  C  C     . THR   A 127 ? 0.0791 0.2703 0.1257 0.0109  -0.0282 0.0088  124 THR   A C     
988  O  O     . THR   A 127 ? 0.1124 0.3268 0.1720 -0.0201 -0.0570 0.0543  124 THR   A O     
989  C  CB    . THR   A 127 ? 0.0960 0.3013 0.1517 0.0044  -0.0089 -0.0344 124 THR   A CB    
990  O  OG1   . THR   A 127 ? 0.1085 0.2804 0.1334 0.0032  -0.0089 -0.0063 124 THR   A OG1   
991  C  CG2   . THR   A 127 ? 0.1044 0.3590 0.1909 -0.0192 0.0023  -0.0332 124 THR   A CG2   
992  N  N     . VAL   A 128 ? 0.0624 0.2531 0.1254 0.0132  -0.0202 -0.0028 125 VAL   A N     
993  C  CA    . VAL   A 128 ? 0.0539 0.2421 0.1231 0.0227  0.0011  0.0085  125 VAL   A CA    
994  C  C     . VAL   A 128 ? 0.0862 0.2133 0.1354 -0.0056 -0.0111 0.0174  125 VAL   A C     
995  O  O     . VAL   A 128 ? 0.0755 0.2120 0.1266 0.0105  0.0098  0.0041  125 VAL   A O     
996  C  CB    . VAL   A 128 ? 0.0582 0.2223 0.1340 0.0119  -0.0111 0.0117  125 VAL   A CB    
997  C  CG1   . VAL   A 128 ? 0.0766 0.2021 0.1428 0.0033  0.0105  0.0095  125 VAL   A CG1   
998  C  CG2   . VAL   A 128 ? 0.0456 0.2526 0.1702 0.0187  -0.0012 -0.0125 125 VAL   A CG2   
999  N  N     . ASP   A 129 ? 0.1139 0.2115 0.1795 0.0408  -0.0217 0.0191  126 ASP   A N     
1000 C  CA    . ASP   A 129 ? 0.1304 0.2381 0.1773 0.0331  -0.0342 0.0036  126 ASP   A CA    
1001 C  C     . ASP   A 129 ? 0.1122 0.2208 0.1685 0.0391  -0.0122 0.0065  126 ASP   A C     
1002 O  O     . ASP   A 129 ? 0.1145 0.1984 0.1636 0.0306  -0.0047 -0.0070 126 ASP   A O     
1003 C  CB    . ASP   A 129 ? 0.1483 0.2485 0.2630 0.0326  -0.0405 0.0345  126 ASP   A CB    
1004 C  CG    . ASP   A 129 ? 0.3258 0.2678 0.3393 0.0734  -0.0600 0.0074  126 ASP   A CG    
1005 O  OD1   . ASP   A 129 ? 0.3035 0.3277 0.4059 0.0643  -0.0640 -0.0506 126 ASP   A OD1   
1006 O  OD2   . ASP   A 129 ? 0.3345 0.4743 0.5421 0.1871  -0.0905 -0.0189 126 ASP   A OD2   
1007 N  N     A THR   A 130 ? 0.1261 0.2279 0.1748 0.0511  -0.0065 -0.0215 127 THR   A N     
1008 N  N     B THR   A 130 ? 0.1096 0.2267 0.1735 0.0484  -0.0261 -0.0306 127 THR   A N     
1009 C  CA    A THR   A 130 ? 0.1257 0.2552 0.1686 0.0589  -0.0031 -0.0187 127 THR   A CA    
1010 C  CA    B THR   A 130 ? 0.1121 0.2487 0.1669 0.0597  -0.0246 -0.0352 127 THR   A CA    
1011 C  C     A THR   A 130 ? 0.1320 0.2724 0.1578 0.0521  -0.0010 -0.0290 127 THR   A C     
1012 C  C     B THR   A 130 ? 0.1271 0.2697 0.1727 0.0495  -0.0159 -0.0378 127 THR   A C     
1013 O  O     A THR   A 130 ? 0.1254 0.2941 0.1508 0.0410  0.0076  -0.0169 127 THR   A O     
1014 O  O     B THR   A 130 ? 0.1226 0.2690 0.1998 0.0277  -0.0315 -0.0593 127 THR   A O     
1015 C  CB    A THR   A 130 ? 0.1851 0.2750 0.1855 0.0408  0.0508  0.0115  127 THR   A CB    
1016 C  CB    B THR   A 130 ? 0.1426 0.2526 0.1792 0.0473  -0.0084 -0.0193 127 THR   A CB    
1017 O  OG1   A THR   A 130 ? 0.1920 0.2830 0.1854 0.0344  0.0477  0.0176  127 THR   A OG1   
1018 O  OG1   B THR   A 130 ? 0.1876 0.2487 0.1917 0.0618  -0.0211 0.0093  127 THR   A OG1   
1019 C  CG2   A THR   A 130 ? 0.1905 0.2515 0.2200 0.0303  0.0629  -0.0290 127 THR   A CG2   
1020 C  CG2   B THR   A 130 ? 0.1263 0.2358 0.1681 0.0107  -0.0255 -0.0399 127 THR   A CG2   
1021 N  N     . LYS   A 131 ? 0.1122 0.2484 0.2118 0.0405  0.0139  -0.0384 128 LYS   A N     
1022 C  CA    . LYS   A 131 ? 0.1391 0.2429 0.3021 0.0347  0.0270  -0.0481 128 LYS   A CA    
1023 C  C     . LYS   A 131 ? 0.1289 0.1999 0.2247 0.0198  -0.0256 -0.0219 128 LYS   A C     
1024 O  O     . LYS   A 131 ? 0.1482 0.1948 0.2350 0.0163  0.0029  0.0009  128 LYS   A O     
1025 C  CB    . LYS   A 131 ? 0.1969 0.2428 0.4380 0.0496  0.0641  -0.0261 128 LYS   A CB    
1026 C  CG    . LYS   A 131 ? 0.3084 0.3302 0.4851 0.0772  0.1210  -0.0588 128 LYS   A CG    
1027 C  CD    . LYS   A 131 ? 0.5036 0.3492 0.5522 0.0991  0.0726  -0.0885 128 LYS   A CD    
1028 C  CE    . LYS   A 131 ? 0.5700 0.3833 0.6024 0.1747  0.0713  -0.1751 128 LYS   A CE    
1029 N  NZ    . LYS   A 131 ? 0.5622 0.5933 0.6583 0.0831  0.1218  -0.1600 128 LYS   A NZ    
1030 N  N     . GLN   A 132 ? 0.1528 0.2028 0.1871 0.0215  -0.0093 -0.0071 129 GLN   A N     
1031 C  CA    . GLN   A 132 ? 0.1489 0.1949 0.1485 0.0128  -0.0128 0.0265  129 GLN   A CA    
1032 C  C     . GLN   A 132 ? 0.1395 0.1689 0.1211 -0.0046 -0.0161 0.0047  129 GLN   A C     
1033 O  O     . GLN   A 132 ? 0.1431 0.1874 0.1281 0.0059  0.0039  0.0086  129 GLN   A O     
1034 C  CB    . GLN   A 132 ? 0.1966 0.2879 0.1642 -0.0005 -0.0301 0.0113  129 GLN   A CB    
1035 C  CG    . GLN   A 132 ? 0.2050 0.3659 0.2236 0.0169  -0.0148 0.0655  129 GLN   A CG    
1036 C  CD    . GLN   A 132 ? 0.3422 0.4549 0.2956 0.0083  -0.0618 0.0233  129 GLN   A CD    
1037 O  OE1   . GLN   A 132 ? 0.5184 0.4198 0.4323 -0.1028 -0.0660 0.0386  129 GLN   A OE1   
1038 N  NE2   . GLN   A 132 ? 0.3830 0.6513 0.3318 0.0156  -0.1634 0.0744  129 GLN   A NE2   
1039 N  N     . ALA   A 133 ? 0.0977 0.1740 0.1391 0.0045  -0.0116 0.0105  130 ALA   A N     
1040 C  CA    . ALA   A 133 ? 0.1163 0.1593 0.1073 0.0143  -0.0002 0.0045  130 ALA   A CA    
1041 C  C     . ALA   A 133 ? 0.1189 0.1433 0.1061 0.0093  0.0112  0.0110  130 ALA   A C     
1042 O  O     . ALA   A 133 ? 0.1131 0.1476 0.1112 0.0065  0.0086  0.0015  130 ALA   A O     
1043 C  CB    . ALA   A 133 ? 0.1182 0.1733 0.1400 0.0022  -0.0132 0.0171  130 ALA   A CB    
1044 N  N     . GLN   A 134 ? 0.1067 0.1538 0.1190 0.0085  0.0101  0.0003  131 GLN   A N     
1045 C  CA    . GLN   A 134 ? 0.1300 0.1630 0.1302 0.0041  0.0083  -0.0026 131 GLN   A CA    
1046 C  C     . GLN   A 134 ? 0.1215 0.1662 0.1279 0.0057  0.0082  0.0037  131 GLN   A C     
1047 O  O     . GLN   A 134 ? 0.1153 0.1710 0.1378 -0.0064 0.0116  -0.0105 131 GLN   A O     
1048 C  CB    . GLN   A 134 ? 0.1279 0.1640 0.1112 0.0240  -0.0128 -0.0017 131 GLN   A CB    
1049 C  CG    . GLN   A 134 ? 0.1513 0.1632 0.1263 0.0017  0.0063  -0.0098 131 GLN   A CG    
1050 C  CD    . GLN   A 134 ? 0.1943 0.1848 0.1434 0.0159  0.0456  -0.0063 131 GLN   A CD    
1051 O  OE1   . GLN   A 134 ? 0.2283 0.2138 0.2162 0.0552  0.0913  0.0153  131 GLN   A OE1   
1052 N  NE2   . GLN   A 134 ? 0.2158 0.1913 0.1418 0.0406  0.0375  -0.0009 131 GLN   A NE2   
1053 N  N     . ASP   A 135 ? 0.1586 0.1409 0.1186 0.0201  0.0122  -0.0016 132 ASP   A N     
1054 C  CA    . ASP   A 135 ? 0.1459 0.1473 0.1478 0.0062  0.0125  0.0029  132 ASP   A CA    
1055 C  C     . ASP   A 135 ? 0.1225 0.1604 0.1291 0.0126  0.0050  0.0135  132 ASP   A C     
1056 O  O     . ASP   A 135 ? 0.1395 0.1694 0.1488 -0.0066 0.0159  0.0110  132 ASP   A O     
1057 C  CB    . ASP   A 135 ? 0.1839 0.1503 0.1752 0.0202  -0.0020 0.0124  132 ASP   A CB    
1058 C  CG    . ASP   A 135 ? 0.2497 0.2037 0.1798 -0.0125 0.0077  0.0141  132 ASP   A CG    
1059 O  OD1   . ASP   A 135 ? 0.3132 0.2367 0.2860 -0.0538 -0.0737 0.0519  132 ASP   A OD1   
1060 O  OD2   . ASP   A 135 ? 0.3886 0.3224 0.1834 -0.0864 -0.0040 0.0098  132 ASP   A OD2   
1061 N  N     . LEU   A 136 ? 0.1534 0.1628 0.1231 0.0099  0.0375  0.0085  133 LEU   A N     
1062 C  CA    . LEU   A 136 ? 0.1471 0.1634 0.1093 0.0143  0.0334  0.0135  133 LEU   A CA    
1063 C  C     . LEU   A 136 ? 0.1288 0.1675 0.1240 -0.0031 0.0319  0.0045  133 LEU   A C     
1064 O  O     . LEU   A 136 ? 0.1293 0.1753 0.1240 -0.0001 0.0421  0.0187  133 LEU   A O     
1065 C  CB    . LEU   A 136 ? 0.1371 0.1889 0.1131 0.0086  0.0126  -0.0041 133 LEU   A CB    
1066 C  CG    . LEU   A 136 ? 0.1585 0.1954 0.1407 0.0246  0.0190  -0.0045 133 LEU   A CG    
1067 C  CD1   . LEU   A 136 ? 0.1703 0.2163 0.1330 0.0139  0.0579  -0.0258 133 LEU   A CD1   
1068 C  CD2   . LEU   A 136 ? 0.1745 0.1995 0.1635 0.0227  0.0183  -0.0018 133 LEU   A CD2   
1069 N  N     . ALA   A 137 ? 0.1059 0.1635 0.1131 -0.0108 0.0205  -0.0073 134 ALA   A N     
1070 C  CA    . ALA   A 137 ? 0.1058 0.1530 0.1176 -0.0064 0.0201  0.0118  134 ALA   A CA    
1071 C  C     . ALA   A 137 ? 0.0922 0.1673 0.1057 -0.0157 0.0233  -0.0021 134 ALA   A C     
1072 O  O     . ALA   A 137 ? 0.0901 0.1627 0.1665 -0.0074 0.0440  0.0170  134 ALA   A O     
1073 C  CB    . ALA   A 137 ? 0.1037 0.1660 0.1141 -0.0217 0.0196  0.0057  134 ALA   A CB    
1074 N  N     . ARG   A 138 ? 0.1115 0.1756 0.1560 -0.0010 0.0301  -0.0160 135 ARG   A N     
1075 C  CA    . ARG   A 138 ? 0.1352 0.1761 0.1614 -0.0078 0.0412  -0.0182 135 ARG   A CA    
1076 C  C     . ARG   A 138 ? 0.1386 0.1494 0.1684 -0.0248 0.0400  0.0120  135 ARG   A C     
1077 O  O     . ARG   A 138 ? 0.1423 0.1674 0.2283 -0.0231 0.0360  0.0035  135 ARG   A O     
1078 C  CB    . ARG   A 138 ? 0.1518 0.2225 0.1709 0.0325  0.0422  -0.0109 135 ARG   A CB    
1079 C  CG    . ARG   A 138 ? 0.2289 0.2470 0.2469 -0.0208 0.0402  0.0230  135 ARG   A CG    
1080 C  CD    . ARG   A 138 ? 0.2688 0.2539 0.2978 -0.0046 0.0011  -0.0436 135 ARG   A CD    
1081 N  NE    . ARG   A 138 ? 0.3023 0.2201 0.3445 -0.0021 0.0108  0.0069  135 ARG   A NE    
1082 C  CZ    . ARG   A 138 ? 0.3147 0.3066 0.4485 0.0245  0.0216  -0.0350 135 ARG   A CZ    
1083 N  NH1   . ARG   A 138 ? 0.4645 0.1875 0.3893 0.0433  0.0134  -0.0828 135 ARG   A NH1   
1084 N  NH2   . ARG   A 138 ? 0.4087 0.2492 0.5186 0.0185  0.1063  -0.0106 135 ARG   A NH2   
1085 N  N     . SER   A 139 ? 0.1123 0.1741 0.1644 -0.0043 0.0412  0.0133  136 SER   A N     
1086 C  CA    . SER   A 139 ? 0.1468 0.1967 0.1635 -0.0068 0.0495  0.0402  136 SER   A CA    
1087 C  C     . SER   A 139 ? 0.1435 0.1918 0.1635 -0.0095 0.0540  0.0121  136 SER   A C     
1088 O  O     . SER   A 139 ? 0.1683 0.2304 0.2237 -0.0115 0.0842  0.0414  136 SER   A O     
1089 C  CB    . SER   A 139 ? 0.1619 0.2135 0.1624 0.0116  0.0349  0.0537  136 SER   A CB    
1090 O  OG    . SER   A 139 ? 0.2376 0.2453 0.1800 -0.0104 0.0347  0.0189  136 SER   A OG    
1091 N  N     . TYR   A 140 ? 0.1539 0.1762 0.1557 -0.0038 0.0531  0.0044  137 TYR   A N     
1092 C  CA    . TYR   A 140 ? 0.1610 0.1723 0.1624 -0.0100 0.0500  0.0060  137 TYR   A CA    
1093 C  C     . TYR   A 140 ? 0.1357 0.1918 0.1618 0.0054  0.0580  0.0032  137 TYR   A C     
1094 O  O     . TYR   A 140 ? 0.1709 0.2094 0.2261 0.0360  0.0691  0.0004  137 TYR   A O     
1095 C  CB    . TYR   A 140 ? 0.1800 0.1798 0.1588 -0.0092 0.0459  0.0180  137 TYR   A CB    
1096 C  CG    . TYR   A 140 ? 0.1681 0.1747 0.1873 -0.0033 0.0307  0.0040  137 TYR   A CG    
1097 C  CD1   . TYR   A 140 ? 0.2235 0.1956 0.1755 0.0010  0.0233  0.0123  137 TYR   A CD1   
1098 C  CD2   . TYR   A 140 ? 0.1574 0.2094 0.2247 -0.0226 0.0380  0.0134  137 TYR   A CD2   
1099 C  CE1   . TYR   A 140 ? 0.2485 0.2302 0.1632 0.0414  0.0003  -0.0085 137 TYR   A CE1   
1100 C  CE2   . TYR   A 140 ? 0.1773 0.2166 0.2693 -0.0205 0.0056  -0.0086 137 TYR   A CE2   
1101 C  CZ    . TYR   A 140 ? 0.1999 0.2237 0.2258 0.0571  -0.0088 -0.0397 137 TYR   A CZ    
1102 O  OH    . TYR   A 140 ? 0.2854 0.2477 0.2730 0.0453  -0.0377 -0.0864 137 TYR   A OH    
1103 N  N     . GLY   A 141 ? 0.1297 0.1521 0.1589 -0.0292 0.0419  -0.0026 138 GLY   A N     
1104 C  CA    . GLY   A 141 ? 0.1278 0.1751 0.1722 -0.0234 0.0435  0.0021  138 GLY   A CA    
1105 C  C     . GLY   A 141 ? 0.0972 0.1719 0.1598 -0.0255 0.0267  0.0078  138 GLY   A C     
1106 O  O     . GLY   A 141 ? 0.1070 0.2098 0.2151 -0.0247 0.0028  0.0270  138 GLY   A O     
1107 N  N     . ILE   A 142 ? 0.0826 0.1575 0.1684 -0.0098 0.0268  0.0082  139 ILE   A N     
1108 C  CA    . ILE   A 142 ? 0.0639 0.1596 0.1477 0.0041  0.0156  0.0079  139 ILE   A CA    
1109 C  C     . ILE   A 142 ? 0.0756 0.1227 0.1503 -0.0144 0.0218  -0.0125 139 ILE   A C     
1110 O  O     . ILE   A 142 ? 0.1099 0.1380 0.1399 0.0016  0.0080  0.0020  139 ILE   A O     
1111 C  CB    . ILE   A 142 ? 0.0974 0.1562 0.1568 -0.0106 0.0372  0.0069  139 ILE   A CB    
1112 C  CG1   . ILE   A 142 ? 0.0992 0.1728 0.1407 -0.0075 0.0377  -0.0143 139 ILE   A CG1   
1113 C  CG2   . ILE   A 142 ? 0.1103 0.1961 0.1588 -0.0147 0.0433  -0.0004 139 ILE   A CG2   
1114 C  CD1   . ILE   A 142 ? 0.1386 0.1885 0.1587 -0.0242 0.0579  -0.0293 139 ILE   A CD1   
1115 N  N     . PRO   A 143 ? 0.0776 0.1272 0.1513 -0.0222 0.0073  -0.0030 140 PRO   A N     
1116 C  CA    . PRO   A 143 ? 0.0770 0.1375 0.1340 -0.0007 0.0023  -0.0170 140 PRO   A CA    
1117 C  C     . PRO   A 143 ? 0.0777 0.1315 0.1020 -0.0045 0.0078  -0.0054 140 PRO   A C     
1118 O  O     . PRO   A 143 ? 0.0731 0.1422 0.1245 0.0014  0.0127  -0.0175 140 PRO   A O     
1119 C  CB    . PRO   A 143 ? 0.0954 0.1513 0.1358 -0.0095 -0.0073 -0.0102 140 PRO   A CB    
1120 C  CG    . PRO   A 143 ? 0.0972 0.1680 0.1300 -0.0050 -0.0050 -0.0219 140 PRO   A CG    
1121 C  CD    . PRO   A 143 ? 0.0810 0.1399 0.1395 -0.0122 0.0113  -0.0119 140 PRO   A CD    
1122 N  N     . PHE   A 144 ? 0.0774 0.1234 0.1147 -0.0086 0.0184  -0.0147 141 PHE   A N     
1123 C  CA    . PHE   A 144 ? 0.0747 0.1212 0.1012 -0.0007 0.0100  -0.0104 141 PHE   A CA    
1124 C  C     . PHE   A 144 ? 0.0561 0.1170 0.1045 0.0104  0.0094  -0.0037 141 PHE   A C     
1125 O  O     . PHE   A 144 ? 0.0908 0.1288 0.0990 0.0040  0.0152  -0.0130 141 PHE   A O     
1126 C  CB    . PHE   A 144 ? 0.0870 0.1369 0.1025 0.0090  0.0049  0.0035  141 PHE   A CB    
1127 C  CG    . PHE   A 144 ? 0.0922 0.1400 0.1005 0.0057  0.0004  0.0078  141 PHE   A CG    
1128 C  CD1   . PHE   A 144 ? 0.1075 0.1469 0.1077 -0.0072 0.0094  0.0058  141 PHE   A CD1   
1129 C  CD2   . PHE   A 144 ? 0.1159 0.1732 0.1272 0.0239  0.0022  -0.0160 141 PHE   A CD2   
1130 C  CE1   . PHE   A 144 ? 0.1103 0.1690 0.1165 -0.0059 -0.0090 0.0128  141 PHE   A CE1   
1131 C  CE2   . PHE   A 144 ? 0.0920 0.2219 0.1192 0.0288  0.0061  0.0000  141 PHE   A CE2   
1132 C  CZ    . PHE   A 144 ? 0.0862 0.2032 0.1089 -0.0048 -0.0046 0.0221  141 PHE   A CZ    
1133 N  N     . ILE   A 145 ? 0.0804 0.1253 0.0878 0.0055  0.0084  -0.0035 142 ILE   A N     
1134 C  CA    . ILE   A 145 ? 0.0869 0.1328 0.0823 -0.0073 -0.0102 -0.0028 142 ILE   A CA    
1135 C  C     . ILE   A 145 ? 0.0589 0.1395 0.0848 -0.0125 0.0081  0.0037  142 ILE   A C     
1136 O  O     . ILE   A 145 ? 0.0608 0.1537 0.1039 -0.0114 0.0150  -0.0200 142 ILE   A O     
1137 C  CB    . ILE   A 145 ? 0.0775 0.1230 0.1016 -0.0035 -0.0061 0.0028  142 ILE   A CB    
1138 C  CG1   . ILE   A 145 ? 0.0817 0.1391 0.1120 -0.0091 -0.0096 -0.0024 142 ILE   A CG1   
1139 C  CG2   . ILE   A 145 ? 0.1066 0.1222 0.1018 -0.0008 0.0112  -0.0017 142 ILE   A CG2   
1140 C  CD1   . ILE   A 145 ? 0.1092 0.1522 0.1166 0.0051  -0.0188 -0.0010 142 ILE   A CD1   
1141 N  N     . GLU   A 146 ? 0.0659 0.1325 0.0923 -0.0070 0.0128  -0.0121 143 GLU   A N     
1142 C  CA    . GLU   A 146 ? 0.0602 0.1449 0.0852 -0.0029 0.0014  -0.0070 143 GLU   A CA    
1143 C  C     . GLU   A 146 ? 0.0667 0.1473 0.0916 -0.0200 0.0111  -0.0131 143 GLU   A C     
1144 O  O     . GLU   A 146 ? 0.0722 0.1631 0.0943 -0.0115 0.0135  -0.0103 143 GLU   A O     
1145 C  CB    . GLU   A 146 ? 0.0491 0.1759 0.1069 -0.0018 0.0068  -0.0128 143 GLU   A CB    
1146 C  CG    . GLU   A 146 ? 0.0745 0.1734 0.1363 -0.0038 0.0099  0.0040  143 GLU   A CG    
1147 C  CD    . GLU   A 146 ? 0.0832 0.2227 0.1428 0.0084  0.0065  0.0269  143 GLU   A CD    
1148 O  OE1   . GLU   A 146 ? 0.1128 0.3642 0.2014 0.0325  0.0437  0.0952  143 GLU   A OE1   
1149 O  OE2   . GLU   A 146 ? 0.0867 0.2653 0.1370 0.0299  0.0094  0.0351  143 GLU   A OE2   
1150 N  N     . THR   A 147 ? 0.0921 0.1383 0.0853 -0.0130 0.0032  -0.0105 144 THR   A N     
1151 C  CA    . THR   A 147 ? 0.0755 0.1532 0.0741 -0.0177 0.0013  -0.0087 144 THR   A CA    
1152 C  C     . THR   A 147 ? 0.0906 0.1652 0.0804 -0.0304 -0.0053 -0.0139 144 THR   A C     
1153 O  O     . THR   A 147 ? 0.0797 0.1726 0.0892 -0.0245 0.0001  -0.0093 144 THR   A O     
1154 C  CB    . THR   A 147 ? 0.0879 0.1438 0.0857 -0.0159 -0.0065 0.0029  144 THR   A CB    
1155 O  OG1   . THR   A 147 ? 0.0854 0.1506 0.0852 -0.0125 -0.0038 -0.0082 144 THR   A OG1   
1156 C  CG2   . THR   A 147 ? 0.0835 0.1542 0.0937 -0.0245 0.0045  -0.0189 144 THR   A CG2   
1157 N  N     . SER   A 148 ? 0.0918 0.1608 0.0903 -0.0379 0.0046  -0.0103 145 SER   A N     
1158 C  CA    . SER   A 148 ? 0.0812 0.1723 0.1073 -0.0356 0.0105  -0.0303 145 SER   A CA    
1159 C  C     . SER   A 148 ? 0.1254 0.1659 0.0932 -0.0585 0.0146  -0.0108 145 SER   A C     
1160 O  O     . SER   A 148 ? 0.1506 0.1888 0.0924 -0.0522 0.0187  -0.0094 145 SER   A O     
1161 C  CB    . SER   A 148 ? 0.0727 0.2095 0.1229 -0.0361 0.0090  -0.0193 145 SER   A CB    
1162 O  OG    . SER   A 148 ? 0.1349 0.2149 0.1529 -0.0671 0.0427  -0.0208 145 SER   A OG    
1163 N  N     . ALA   A 149 ? 0.1642 0.1543 0.1026 -0.0410 -0.0001 -0.0168 146 ALA   A N     
1164 C  CA    . ALA   A 149 ? 0.1834 0.1496 0.1248 -0.0478 -0.0089 -0.0141 146 ALA   A CA    
1165 C  C     . ALA   A 149 ? 0.1932 0.1924 0.1448 -0.0405 0.0084  0.0004  146 ALA   A C     
1166 O  O     . ALA   A 149 ? 0.2805 0.2253 0.1805 -0.0490 0.0128  0.0583  146 ALA   A O     
1167 C  CB    . ALA   A 149 ? 0.1808 0.1857 0.1432 -0.0098 -0.0098 -0.0237 146 ALA   A CB    
1168 N  N     . LYS   A 150 ? 0.1596 0.1831 0.1557 -0.0589 0.0272  -0.0092 147 LYS   A N     
1169 C  CA    . LYS   A 150 ? 0.1863 0.2108 0.2043 -0.0595 0.0523  0.0194  147 LYS   A CA    
1170 C  C     . LYS   A 150 ? 0.1989 0.2305 0.1994 -0.0650 0.0550  0.0236  147 LYS   A C     
1171 O  O     . LYS   A 150 ? 0.3003 0.2608 0.2256 -0.0443 0.0786  0.0523  147 LYS   A O     
1172 C  CB    . LYS   A 150 ? 0.1493 0.2348 0.2608 -0.0458 0.0592  0.0173  147 LYS   A CB    
1173 C  CG    . LYS   A 150 ? 0.1751 0.2476 0.3170 -0.0524 0.0675  0.0504  147 LYS   A CG    
1174 C  CD    . LYS   A 150 ? 0.1573 0.3022 0.3954 -0.0418 0.0343  0.0741  147 LYS   A CD    
1175 C  CE    . LYS   A 150 ? 0.1929 0.3420 0.4750 -0.0968 0.0156  0.0679  147 LYS   A CE    
1176 N  NZ    . LYS   A 150 ? 0.2489 0.3954 0.5539 -0.0518 -0.0376 0.0612  147 LYS   A NZ    
1177 N  N     . THR   A 151 ? 0.2048 0.2340 0.1685 -0.0613 0.0586  0.0134  148 THR   A N     
1178 C  CA    . THR   A 151 ? 0.2172 0.2880 0.1651 -0.0395 0.0736  0.0144  148 THR   A CA    
1179 C  C     . THR   A 151 ? 0.2374 0.2489 0.1956 -0.0544 0.0691  -0.0084 148 THR   A C     
1180 O  O     . THR   A 151 ? 0.3428 0.3820 0.1875 -0.1030 0.1025  -0.0254 148 THR   A O     
1181 C  CB    . THR   A 151 ? 0.1989 0.3073 0.1634 -0.0265 0.0731  0.0060  148 THR   A CB    
1182 O  OG1   . THR   A 151 ? 0.2656 0.2737 0.1846 -0.0257 0.0877  0.0063  148 THR   A OG1   
1183 C  CG2   . THR   A 151 ? 0.1896 0.3065 0.1695 -0.0641 0.0640  -0.0135 148 THR   A CG2   
1184 N  N     . ARG   A 152 ? 0.2329 0.2459 0.1545 -0.0091 0.0584  0.0649  149 ARG   A N     
1185 C  CA    . ARG   A 152 ? 0.2545 0.2595 0.1505 0.0047  0.0190  0.0137  149 ARG   A CA    
1186 C  C     . ARG   A 152 ? 0.1477 0.2858 0.1680 -0.0108 -0.0112 -0.0046 149 ARG   A C     
1187 O  O     . ARG   A 152 ? 0.1592 0.2774 0.1935 -0.0073 0.0025  -0.0217 149 ARG   A O     
1188 C  CB    . ARG   A 152 ? 0.2638 0.2890 0.1583 -0.0106 0.0399  0.0405  149 ARG   A CB    
1189 C  CG    . ARG   A 152 ? 0.3388 0.3056 0.2324 0.0454  0.0541  0.0433  149 ARG   A CG    
1190 C  CD    . ARG   A 152 ? 0.4353 0.2666 0.2333 -0.0406 -0.0105 0.0390  149 ARG   A CD    
1191 N  NE    . ARG   A 152 ? 0.4411 0.3323 0.1918 -0.0543 0.0342  0.0799  149 ARG   A NE    
1192 C  CZ    . ARG   A 152 ? 0.4735 0.2510 0.2557 -0.0622 0.0278  0.0464  149 ARG   A CZ    
1193 N  NH1   . ARG   A 152 ? 0.4431 0.3891 0.2588 -0.1068 0.0456  -0.0774 149 ARG   A NH1   
1194 N  NH2   . ARG   A 152 ? 0.5014 0.3868 0.2874 -0.0684 0.0676  -0.0094 149 ARG   A NH2   
1195 N  N     . GLN   A 153 ? 0.1413 0.2135 0.1268 -0.0367 0.0022  -0.0250 150 GLN   A N     
1196 C  CA    . GLN   A 153 ? 0.1117 0.2118 0.1088 -0.0153 0.0306  -0.0537 150 GLN   A CA    
1197 C  C     . GLN   A 153 ? 0.1044 0.1646 0.0916 -0.0172 0.0020  -0.0180 150 GLN   A C     
1198 O  O     . GLN   A 153 ? 0.0940 0.1895 0.0863 -0.0280 -0.0050 -0.0140 150 GLN   A O     
1199 C  CB    . GLN   A 153 ? 0.0767 0.2403 0.1465 -0.0172 0.0418  -0.0293 150 GLN   A CB    
1200 C  CG    . GLN   A 153 ? 0.1416 0.2413 0.1826 -0.0221 0.0082  -0.0226 150 GLN   A CG    
1201 C  CD    . GLN   A 153 ? 0.2171 0.2636 0.1987 -0.0178 0.0343  -0.0720 150 GLN   A CD    
1202 O  OE1   . GLN   A 153 ? 0.2438 0.3145 0.2521 -0.0119 0.0895  0.0084  150 GLN   A OE1   
1203 N  NE2   . GLN   A 153 ? 0.1787 0.2043 0.2361 -0.0113 0.0346  -0.0558 150 GLN   A NE2   
1204 N  N     . ARG   A 154 ? 0.0989 0.1673 0.0734 -0.0204 0.0126  -0.0083 151 ARG   A N     
1205 C  CA    . ARG   A 154 ? 0.0853 0.1720 0.0831 -0.0219 -0.0055 -0.0136 151 ARG   A CA    
1206 C  C     . ARG   A 154 ? 0.0940 0.1583 0.0921 -0.0202 0.0062  0.0011  151 ARG   A C     
1207 O  O     . ARG   A 154 ? 0.0771 0.1553 0.1018 -0.0079 -0.0030 0.0011  151 ARG   A O     
1208 C  CB    . ARG   A 154 ? 0.0750 0.1749 0.0933 -0.0106 0.0154  -0.0081 151 ARG   A CB    
1209 C  CG    . ARG   A 154 ? 0.1059 0.1928 0.1025 0.0102  0.0117  -0.0041 151 ARG   A CG    
1210 C  CD    . ARG   A 154 ? 0.1223 0.1674 0.1042 0.0363  0.0060  -0.0046 151 ARG   A CD    
1211 N  NE    . ARG   A 154 ? 0.1519 0.1496 0.1427 0.0172  -0.0150 -0.0084 151 ARG   A NE    
1212 C  CZ    . ARG   A 154 ? 0.1520 0.1410 0.1399 0.0082  -0.0067 -0.0267 151 ARG   A CZ    
1213 N  NH1   . ARG   A 154 ? 0.1600 0.1681 0.1378 -0.0068 -0.0139 -0.0250 151 ARG   A NH1   
1214 N  NH2   . ARG   A 154 ? 0.1344 0.1489 0.1478 0.0084  0.0146  -0.0176 151 ARG   A NH2   
1215 N  N     . VAL   A 155 ? 0.0943 0.1570 0.0919 -0.0169 0.0014  -0.0113 152 VAL   A N     
1216 C  CA    . VAL   A 155 ? 0.1031 0.1608 0.1326 -0.0157 0.0127  -0.0187 152 VAL   A CA    
1217 C  C     . VAL   A 155 ? 0.1045 0.1369 0.1188 0.0029  0.0135  -0.0123 152 VAL   A C     
1218 O  O     . VAL   A 155 ? 0.0866 0.1526 0.1086 -0.0080 -0.0076 -0.0087 152 VAL   A O     
1219 C  CB    . VAL   A 155 ? 0.1391 0.1676 0.1773 -0.0274 0.0013  -0.0031 152 VAL   A CB    
1220 C  CG1   . VAL   A 155 ? 0.1792 0.1638 0.2027 -0.0309 0.0206  -0.0145 152 VAL   A CG1   
1221 C  CG2   . VAL   A 155 ? 0.1277 0.1643 0.2216 -0.0323 0.0005  -0.0190 152 VAL   A CG2   
1222 N  N     . GLU   A 156 ? 0.1167 0.1660 0.1097 -0.0061 0.0177  0.0024  153 GLU   A N     
1223 C  CA    . GLU   A 156 ? 0.1254 0.1947 0.1041 0.0011  0.0129  -0.0070 153 GLU   A CA    
1224 C  C     . GLU   A 156 ? 0.1039 0.1823 0.0842 -0.0119 -0.0133 -0.0196 153 GLU   A C     
1225 O  O     . GLU   A 156 ? 0.0940 0.1993 0.1163 0.0060  -0.0217 0.0062  153 GLU   A O     
1226 C  CB    . GLU   A 156 ? 0.1908 0.2149 0.1058 0.0150  0.0036  0.0158  153 GLU   A CB    
1227 C  CG    . GLU   A 156 ? 0.2438 0.2208 0.1983 0.0293  0.0347  0.0181  153 GLU   A CG    
1228 C  CD    . GLU   A 156 ? 0.3900 0.3606 0.2121 0.0121  0.0288  0.0180  153 GLU   A CD    
1229 O  OE1   . GLU   A 156 ? 0.4596 0.6020 0.2245 -0.0352 0.1297  -0.0754 153 GLU   A OE1   
1230 O  OE2   . GLU   A 156 ? 0.5367 0.5649 0.3092 0.1471  -0.0306 0.0059  153 GLU   A OE2   
1231 N  N     . ASP   A 157 ? 0.1092 0.1817 0.0965 -0.0074 -0.0195 -0.0148 154 ASP   A N     
1232 C  CA    . ASP   A 157 ? 0.0864 0.1673 0.0952 0.0001  -0.0232 -0.0357 154 ASP   A CA    
1233 C  C     . ASP   A 157 ? 0.0643 0.1469 0.1035 -0.0072 -0.0171 -0.0219 154 ASP   A C     
1234 O  O     . ASP   A 157 ? 0.0701 0.1599 0.1130 -0.0127 -0.0110 -0.0201 154 ASP   A O     
1235 C  CB    . ASP   A 157 ? 0.0927 0.1943 0.1206 0.0164  -0.0270 -0.0221 154 ASP   A CB    
1236 C  CG    . ASP   A 157 ? 0.1542 0.2203 0.1405 0.0302  -0.0299 -0.0395 154 ASP   A CG    
1237 O  OD1   . ASP   A 157 ? 0.1757 0.3232 0.1336 0.0293  -0.0320 -0.0478 154 ASP   A OD1   
1238 O  OD2   . ASP   A 157 ? 0.1636 0.2429 0.1603 0.0347  -0.0276 -0.0386 154 ASP   A OD2   
1239 N  N     . ALA   A 158 ? 0.0672 0.1481 0.0899 -0.0169 -0.0066 -0.0184 155 ALA   A N     
1240 C  CA    . ALA   A 158 ? 0.1020 0.1402 0.0894 -0.0086 -0.0082 -0.0004 155 ALA   A CA    
1241 C  C     . ALA   A 158 ? 0.1127 0.1366 0.0805 -0.0009 -0.0027 -0.0095 155 ALA   A C     
1242 O  O     . ALA   A 158 ? 0.1194 0.1274 0.1029 0.0080  0.0025  -0.0043 155 ALA   A O     
1243 C  CB    . ALA   A 158 ? 0.1139 0.1609 0.0975 0.0076  -0.0350 -0.0076 155 ALA   A CB    
1244 N  N     . PHE   A 159 ? 0.0882 0.1292 0.0955 0.0028  -0.0044 -0.0172 156 PHE   A N     
1245 C  CA    . PHE   A 159 ? 0.0949 0.1392 0.1074 0.0104  -0.0074 -0.0164 156 PHE   A CA    
1246 C  C     . PHE   A 159 ? 0.0876 0.1397 0.0996 0.0164  -0.0132 -0.0120 156 PHE   A C     
1247 O  O     . PHE   A 159 ? 0.0877 0.1408 0.1188 0.0121  -0.0126 -0.0144 156 PHE   A O     
1248 C  CB    . PHE   A 159 ? 0.1212 0.1360 0.1148 0.0124  -0.0191 -0.0179 156 PHE   A CB    
1249 C  CG    . PHE   A 159 ? 0.1104 0.1375 0.1346 0.0147  -0.0201 -0.0253 156 PHE   A CG    
1250 C  CD1   . PHE   A 159 ? 0.1326 0.1637 0.1428 0.0230  -0.0133 -0.0387 156 PHE   A CD1   
1251 C  CD2   . PHE   A 159 ? 0.1178 0.1437 0.1174 0.0057  -0.0187 -0.0142 156 PHE   A CD2   
1252 C  CE1   . PHE   A 159 ? 0.1732 0.1600 0.1523 0.0160  -0.0146 -0.0437 156 PHE   A CE1   
1253 C  CE2   . PHE   A 159 ? 0.1614 0.1393 0.1245 0.0000  -0.0264 -0.0121 156 PHE   A CE2   
1254 C  CZ    . PHE   A 159 ? 0.1743 0.1467 0.1300 0.0110  -0.0334 -0.0251 156 PHE   A CZ    
1255 N  N     . TYR   A 160 ? 0.0994 0.1351 0.1022 0.0239  -0.0234 -0.0189 157 TYR   A N     
1256 C  CA    . TYR   A 160 ? 0.1076 0.1501 0.0988 0.0174  -0.0243 -0.0151 157 TYR   A CA    
1257 C  C     . TYR   A 160 ? 0.0797 0.1417 0.1012 0.0070  -0.0261 -0.0299 157 TYR   A C     
1258 O  O     . TYR   A 160 ? 0.0794 0.1617 0.1174 0.0057  -0.0321 -0.0372 157 TYR   A O     
1259 C  CB    . TYR   A 160 ? 0.0948 0.1757 0.0999 0.0090  -0.0325 -0.0258 157 TYR   A CB    
1260 C  CG    . TYR   A 160 ? 0.1008 0.2001 0.1116 0.0374  -0.0140 -0.0001 157 TYR   A CG    
1261 C  CD1   . TYR   A 160 ? 0.1771 0.1943 0.1202 0.0287  -0.0321 0.0128  157 TYR   A CD1   
1262 C  CD2   . TYR   A 160 ? 0.1769 0.2351 0.1192 0.0347  0.0260  0.0260  157 TYR   A CD2   
1263 C  CE1   . TYR   A 160 ? 0.1697 0.2110 0.1937 0.0199  -0.0461 0.0459  157 TYR   A CE1   
1264 C  CE2   . TYR   A 160 ? 0.2627 0.2562 0.1750 0.0455  0.0202  0.0734  157 TYR   A CE2   
1265 C  CZ    . TYR   A 160 ? 0.2315 0.2501 0.2173 0.0333  0.0348  0.0724  157 TYR   A CZ    
1266 O  OH    . TYR   A 160 ? 0.4080 0.2481 0.3117 0.0345  0.0210  0.1224  157 TYR   A OH    
1267 N  N     . THR   A 161 ? 0.0810 0.1412 0.1052 0.0053  -0.0197 -0.0170 158 THR   A N     
1268 C  CA    . THR   A 161 ? 0.0695 0.1363 0.1052 0.0030  -0.0178 -0.0251 158 THR   A CA    
1269 C  C     . THR   A 161 ? 0.0872 0.1308 0.1115 -0.0012 -0.0131 -0.0278 158 THR   A C     
1270 O  O     . THR   A 161 ? 0.0934 0.1379 0.1135 -0.0101 -0.0123 -0.0339 158 THR   A O     
1271 C  CB    . THR   A 161 ? 0.0657 0.1306 0.1119 0.0074  -0.0109 -0.0292 158 THR   A CB    
1272 O  OG1   . THR   A 161 ? 0.0735 0.1393 0.1192 0.0145  -0.0046 -0.0273 158 THR   A OG1   
1273 C  CG2   . THR   A 161 ? 0.0883 0.1375 0.1296 0.0043  -0.0263 -0.0172 158 THR   A CG2   
1274 N  N     . LEU   A 162 ? 0.0829 0.1339 0.0945 0.0068  -0.0142 -0.0262 159 LEU   A N     
1275 C  CA    . LEU   A 162 ? 0.0778 0.1472 0.1064 0.0090  -0.0124 -0.0279 159 LEU   A CA    
1276 C  C     . LEU   A 162 ? 0.0831 0.1404 0.1106 0.0094  -0.0190 -0.0296 159 LEU   A C     
1277 O  O     . LEU   A 162 ? 0.0949 0.1784 0.1171 0.0117  -0.0161 -0.0371 159 LEU   A O     
1278 C  CB    . LEU   A 162 ? 0.0584 0.1533 0.1020 0.0167  -0.0197 -0.0269 159 LEU   A CB    
1279 C  CG    . LEU   A 162 ? 0.0837 0.1502 0.0962 0.0278  -0.0177 -0.0259 159 LEU   A CG    
1280 C  CD1   . LEU   A 162 ? 0.0794 0.1652 0.0961 0.0169  -0.0180 -0.0225 159 LEU   A CD1   
1281 C  CD2   . LEU   A 162 ? 0.0591 0.1471 0.1265 0.0223  0.0062  -0.0370 159 LEU   A CD2   
1282 N  N     . VAL   A 163 ? 0.0648 0.1572 0.1177 0.0205  -0.0136 -0.0316 160 VAL   A N     
1283 C  CA    . VAL   A 163 ? 0.0678 0.1956 0.1390 0.0341  -0.0197 -0.0428 160 VAL   A CA    
1284 C  C     . VAL   A 163 ? 0.0605 0.2008 0.0982 0.0168  -0.0050 -0.0393 160 VAL   A C     
1285 O  O     . VAL   A 163 ? 0.0533 0.2164 0.1268 0.0242  -0.0045 -0.0399 160 VAL   A O     
1286 C  CB    . VAL   A 163 ? 0.0940 0.1868 0.1278 0.0446  -0.0237 -0.0441 160 VAL   A CB    
1287 C  CG1   . VAL   A 163 ? 0.1180 0.2299 0.1439 0.0357  -0.0405 -0.0362 160 VAL   A CG1   
1288 C  CG2   . VAL   A 163 ? 0.1553 0.1861 0.1460 0.0472  -0.0575 -0.0414 160 VAL   A CG2   
1289 N  N     . ARG   A 164 ? 0.0622 0.1897 0.1195 0.0090  -0.0074 -0.0555 161 ARG   A N     
1290 C  CA    . ARG   A 164 ? 0.0562 0.2042 0.1261 0.0068  -0.0197 -0.0522 161 ARG   A CA    
1291 C  C     . ARG   A 164 ? 0.0439 0.2073 0.1420 -0.0124 -0.0052 -0.0544 161 ARG   A C     
1292 O  O     . ARG   A 164 ? 0.0628 0.2338 0.1790 -0.0243 0.0009  -0.0613 161 ARG   A O     
1293 C  CB    . ARG   A 164 ? 0.0629 0.1837 0.1170 0.0132  -0.0153 -0.0319 161 ARG   A CB    
1294 C  CG    . ARG   A 164 ? 0.0900 0.1990 0.1048 0.0037  -0.0222 -0.0375 161 ARG   A CG    
1295 C  CD    . ARG   A 164 ? 0.1108 0.2355 0.1387 0.0258  -0.0098 -0.0324 161 ARG   A CD    
1296 N  NE    . ARG   A 164 ? 0.0788 0.2988 0.1400 0.0411  -0.0196 -0.0219 161 ARG   A NE    
1297 C  CZ    . ARG   A 164 ? 0.1081 0.4169 0.1767 0.0498  0.0012  -0.0536 161 ARG   A CZ    
1298 N  NH1   . ARG   A 164 ? 0.1332 0.4556 0.1560 0.0916  0.0035  -0.0579 161 ARG   A NH1   
1299 N  NH2   . ARG   A 164 ? 0.1363 0.5287 0.1730 0.0759  0.0035  -0.0611 161 ARG   A NH2   
1300 N  N     . GLU   A 165 ? 0.0772 0.1779 0.1336 -0.0210 -0.0120 -0.0269 162 GLU   A N     
1301 C  CA    . GLU   A 165 ? 0.0649 0.1689 0.1456 -0.0199 0.0031  -0.0302 162 GLU   A CA    
1302 C  C     . GLU   A 165 ? 0.0711 0.1958 0.1388 -0.0061 -0.0046 -0.0352 162 GLU   A C     
1303 O  O     . GLU   A 165 ? 0.0894 0.2005 0.1641 -0.0175 0.0135  -0.0474 162 GLU   A O     
1304 C  CB    . GLU   A 165 ? 0.0846 0.1740 0.1402 0.0000  -0.0002 -0.0255 162 GLU   A CB    
1305 C  CG    . GLU   A 165 ? 0.1111 0.1794 0.1663 0.0181  0.0118  -0.0107 162 GLU   A CG    
1306 C  CD    . GLU   A 165 ? 0.1041 0.1820 0.1851 0.0044  -0.0122 -0.0205 162 GLU   A CD    
1307 O  OE1   . GLU   A 165 ? 0.1845 0.1996 0.1943 -0.0485 0.0213  -0.0285 162 GLU   A OE1   
1308 O  OE2   . GLU   A 165 ? 0.2187 0.1900 0.2468 0.0109  0.0175  -0.0537 162 GLU   A OE2   
1309 N  N     . ILE   A 166 ? 0.0763 0.2062 0.1156 0.0065  0.0024  -0.0411 163 ILE   A N     
1310 C  CA    . ILE   A 166 ? 0.0596 0.2443 0.1207 0.0147  -0.0072 -0.0464 163 ILE   A CA    
1311 C  C     . ILE   A 166 ? 0.0908 0.3011 0.1206 0.0043  -0.0184 -0.0609 163 ILE   A C     
1312 O  O     . ILE   A 166 ? 0.0639 0.3424 0.1544 -0.0008 0.0015  -0.1043 163 ILE   A O     
1313 C  CB    . ILE   A 166 ? 0.0727 0.2492 0.1193 0.0283  0.0000  -0.0424 163 ILE   A CB    
1314 C  CG1   . ILE   A 166 ? 0.0973 0.2353 0.1123 0.0509  -0.0139 -0.0496 163 ILE   A CG1   
1315 C  CG2   . ILE   A 166 ? 0.0866 0.2812 0.1299 0.0497  0.0094  -0.0376 163 ILE   A CG2   
1316 C  CD1   . ILE   A 166 ? 0.1396 0.2222 0.1047 0.0520  -0.0180 -0.0540 163 ILE   A CD1   
1317 N  N     . ARG   A 167 ? 0.0562 0.3451 0.1319 0.0238  -0.0198 -0.0820 164 ARG   A N     
1318 C  CA    . ARG   A 167 ? 0.0457 0.3795 0.1310 0.0157  -0.0115 -0.0916 164 ARG   A CA    
1319 C  C     . ARG   A 167 ? 0.1179 0.4140 0.1644 -0.0638 0.0290  -0.1272 164 ARG   A C     
1320 O  O     . ARG   A 167 ? 0.0740 0.5290 0.2144 -0.0376 0.0245  -0.1733 164 ARG   A O     
1321 C  CB    . ARG   A 167 ? 0.1301 0.3403 0.1175 0.0033  0.0009  -0.0516 164 ARG   A CB    
1322 C  CG    . ARG   A 167 ? 0.0537 0.2659 0.1963 -0.0082 -0.0206 -0.0363 164 ARG   A CG    
1323 C  CD    . ARG   A 167 ? 0.1747 0.2849 0.1933 0.0021  0.0914  0.0037  164 ARG   A CD    
1324 N  NE    . ARG   A 167 ? 0.1408 0.2021 0.1996 0.0362  0.0438  -0.0078 164 ARG   A NE    
1325 C  CZ    . ARG   A 167 ? 0.1273 0.2185 0.1470 0.0033  0.0154  -0.0350 164 ARG   A CZ    
1326 N  NH1   . ARG   A 167 ? 0.1185 0.2279 0.1655 0.0120  0.0127  -0.0181 164 ARG   A NH1   
1327 N  NH2   . ARG   A 167 ? 0.1139 0.2277 0.1303 -0.0128 -0.0124 -0.0443 164 ARG   A NH2   
1328 N  N     . GLN   A 168 ? 0.1215 0.3700 0.1985 -0.0512 0.0347  -0.1434 165 GLN   A N     
1329 C  CA    . GLN   A 168 ? 0.1687 0.3600 0.2784 -0.0907 0.0769  -0.1670 165 GLN   A CA    
1330 C  C     . GLN   A 168 ? 0.0849 0.3827 0.2390 -0.0667 0.0231  -0.1851 165 GLN   A C     
1331 O  O     . GLN   A 168 ? 0.1138 0.4442 0.3319 -0.1140 0.0917  -0.2514 165 GLN   A O     
1332 C  CB    . GLN   A 168 ? 0.1575 0.3530 0.4326 -0.0473 0.1388  -0.1908 165 GLN   A CB    
1333 C  CG    . GLN   A 168 ? 0.3839 0.4443 0.4175 -0.0595 0.1942  -0.1597 165 GLN   A CG    
1334 C  CD    . GLN   A 168 ? 0.4174 0.4814 0.5445 0.0346  0.2637  -0.0551 165 GLN   A CD    
1335 O  OE1   . GLN   A 168 ? 0.4447 0.5448 0.6793 -0.1095 0.2756  -0.0431 165 GLN   A OE1   
1336 N  NE2   . GLN   A 168 ? 0.5697 0.5158 0.6366 0.0507  0.1693  0.0074  165 GLN   A NE2   
1337 N  N     . TYR   A 169 ? 0.0848 0.3232 0.2249 -0.0416 0.0437  -0.1578 166 TYR   A N     
1338 C  CA    . TYR   A 169 ? 0.0978 0.3189 0.2220 -0.0500 0.0522  -0.1413 166 TYR   A CA    
1339 C  C     . TYR   A 169 ? 0.0875 0.3078 0.2241 -0.0601 0.0494  -0.1342 166 TYR   A C     
1340 O  O     . TYR   A 169 ? 0.0943 0.3782 0.2415 -0.0491 0.0770  -0.1507 166 TYR   A O     
1341 C  CB    . TYR   A 169 ? 0.1120 0.2825 0.2152 -0.0174 0.0245  -0.1208 166 TYR   A CB    
1342 C  CG    . TYR   A 169 ? 0.1079 0.2677 0.2516 -0.0292 0.0486  -0.0764 166 TYR   A CG    
1343 C  CD1   . TYR   A 169 ? 0.1009 0.3064 0.3277 -0.0677 0.0183  -0.0259 166 TYR   A CD1   
1344 C  CD2   . TYR   A 169 ? 0.1056 0.2717 0.2687 -0.0287 0.0389  -0.0469 166 TYR   A CD2   
1345 C  CE1   . TYR   A 169 ? 0.2049 0.2949 0.2681 -0.0255 0.0446  -0.0276 166 TYR   A CE1   
1346 C  CE2   . TYR   A 169 ? 0.1328 0.2528 0.3216 -0.0376 0.0257  -0.0121 166 TYR   A CE2   
1347 C  CZ    . TYR   A 169 ? 0.2014 0.3251 0.3299 -0.0305 0.0415  0.0197  166 TYR   A CZ    
1348 O  OH    . TYR   A 169 ? 0.1615 0.3630 0.3962 -0.0187 0.0403  0.0420  166 TYR   A OH    
1349 N  N     . ARG   A 170 ? 0.0267 0.3755 0.2207 -0.0160 0.0393  -0.1246 167 ARG   A N     
1350 C  CA    . ARG   A 170 ? 0.0268 0.4272 0.2410 -0.0095 0.0196  -0.1121 167 ARG   A CA    
1351 C  C     . ARG   A 170 ? 0.0867 0.4323 0.2162 0.0014  0.0331  -0.1684 167 ARG   A C     
1352 O  O     . ARG   A 170 ? 0.0710 0.4798 0.2136 -0.0154 0.0224  -0.1638 167 ARG   A O     
1353 C  CB    . ARG   A 170 ? 0.0627 0.4690 0.2822 -0.0281 -0.0050 -0.0786 167 ARG   A CB    
1354 C  CG    . ARG   A 170 ? 0.1904 0.3845 0.3367 0.0497  0.0301  -0.0254 167 ARG   A CG    
1355 C  CD    . ARG   A 170 ? 0.1476 0.4021 0.3042 0.0816  0.0314  -0.0455 167 ARG   A CD    
1356 N  NE    . ARG   A 170 ? 0.1697 0.4300 0.3161 -0.0240 0.0230  0.0222  167 ARG   A NE    
1357 C  CZ    . ARG   A 170 ? 0.2240 0.3449 0.2463 0.0454  -0.0242 0.0358  167 ARG   A CZ    
1358 N  NH1   . ARG   A 170 ? 0.1731 0.5262 0.2934 0.0077  0.0014  -0.0576 167 ARG   A NH1   
1359 N  NH2   . ARG   A 170 ? 0.2163 0.4416 0.3225 -0.0094 -0.0837 -0.0271 167 ARG   A NH2   
1360 N  N     . LEU   A 171 ? 0.0633 0.4207 0.2696 -0.0271 -0.0057 -0.1925 168 LEU   A N     
1361 C  CA    . LEU   A 171 ? 0.1360 0.3875 0.2450 -0.0380 -0.0018 -0.1680 168 LEU   A CA    
1362 C  C     . LEU   A 171 ? 0.2183 0.3743 0.3527 -0.0666 0.0164  -0.1276 168 LEU   A C     
1363 O  O     . LEU   A 171 ? 0.1872 0.4325 0.4239 -0.0894 0.0648  -0.1639 168 LEU   A O     
1364 C  CB    . LEU   A 171 ? 0.1882 0.4019 0.2928 -0.0410 0.0509  -0.1667 168 LEU   A CB    
1365 C  CG    . LEU   A 171 ? 0.1878 0.5029 0.2302 -0.0149 0.0177  -0.1375 168 LEU   A CG    
1366 C  CD1   . LEU   A 171 ? 0.2900 0.5216 0.2534 0.0612  -0.0401 -0.1609 168 LEU   A CD1   
1367 C  CD2   . LEU   A 171 ? 0.2378 0.4567 0.2739 -0.0147 -0.0002 -0.1228 168 LEU   A CD2   
1368 N  N     . LYS   A 172 ? 0.1086 0.3707 0.3290 -0.0316 0.0654  -0.1527 169 LYS   A N     
1369 C  CA    . LYS   A 172 ? 0.2241 0.3399 0.3288 -0.0295 0.0780  -0.1769 169 LYS   A CA    
1370 C  C     . LYS   A 172 ? 0.1750 0.3519 0.3801 -0.0424 0.0799  -0.1846 169 LYS   A C     
1371 O  O     . LYS   A 172 ? 0.3004 0.3378 0.4404 -0.0725 0.1380  -0.1653 169 LYS   A O     
1372 C  CB    . LYS   A 172 ? 0.2593 0.3478 0.3951 0.0080  0.0209  -0.1696 169 LYS   A CB    
1373 C  CG    . LYS   A 172 ? 0.2753 0.3502 0.4625 -0.0547 -0.0507 -0.1149 169 LYS   A CG    
1374 C  CD    . LYS   A 172 ? 0.2514 0.4583 0.5010 -0.1122 -0.0507 -0.1016 169 LYS   A CD    
1375 C  CE    . LYS   A 172 ? 0.3664 0.5523 0.5069 -0.1382 -0.0490 -0.0759 169 LYS   A CE    
1376 N  NZ    . LYS   A 172 ? 0.4422 0.5963 0.5804 -0.1187 -0.1047 -0.0728 169 LYS   A NZ    
1377 O  OXT   . LYS   A 172 ? 0.1036 0.3552 0.3258 -0.0153 0.0468  -0.1859 169 LYS   A OXT   
1378 P  PB    . GDP   B .   ? 0.1344 0.1607 0.1275 -0.0273 -0.0166 -0.0297 201 GDP   A PB    
1379 O  O1B   . GDP   B .   ? 0.1536 0.1450 0.1312 -0.0273 -0.0163 -0.0161 201 GDP   A O1B   
1380 O  O2B   . GDP   B .   ? 0.1185 0.1641 0.1325 -0.0111 -0.0114 -0.0015 201 GDP   A O2B   
1381 O  O3B   . GDP   B .   ? 0.1067 0.1768 0.1344 -0.0365 -0.0139 -0.0301 201 GDP   A O3B   
1382 O  O3A   . GDP   B .   ? 0.1089 0.1581 0.1315 -0.0090 -0.0393 -0.0240 201 GDP   A O3A   
1383 P  PA    . GDP   B .   ? 0.1411 0.1736 0.1485 -0.0438 0.0000  -0.0234 201 GDP   A PA    
1384 O  O1A   . GDP   B .   ? 0.2048 0.1849 0.1285 -0.0479 -0.0124 0.0023  201 GDP   A O1A   
1385 O  O2A   . GDP   B .   ? 0.1775 0.1675 0.2429 -0.0404 0.0367  -0.0358 201 GDP   A O2A   
1386 O  "O5'" . GDP   B .   ? 0.1601 0.1598 0.1355 -0.0514 -0.0201 -0.0110 201 GDP   A "O5'" 
1387 C  "C5'" . GDP   B .   ? 0.1285 0.1776 0.1560 -0.0516 -0.0105 -0.0221 201 GDP   A "C5'" 
1388 C  "C4'" . GDP   B .   ? 0.1290 0.2010 0.1575 -0.0583 0.0012  -0.0491 201 GDP   A "C4'" 
1389 O  "O4'" . GDP   B .   ? 0.1334 0.2087 0.1527 -0.0557 -0.0042 -0.0534 201 GDP   A "O4'" 
1390 C  "C3'" . GDP   B .   ? 0.1575 0.2067 0.1809 -0.0748 0.0132  -0.0388 201 GDP   A "C3'" 
1391 O  "O3'" . GDP   B .   ? 0.1696 0.2436 0.2216 -0.0860 -0.0012 -0.0567 201 GDP   A "O3'" 
1392 C  "C2'" . GDP   B .   ? 0.1409 0.2074 0.1643 -0.0714 0.0132  -0.0310 201 GDP   A "C2'" 
1393 O  "O2'" . GDP   B .   ? 0.2417 0.2974 0.2147 -0.1187 0.0678  -0.0260 201 GDP   A "O2'" 
1394 C  "C1'" . GDP   B .   ? 0.1478 0.2004 0.1630 -0.0440 0.0213  -0.0532 201 GDP   A "C1'" 
1395 N  N9    . GDP   B .   ? 0.1305 0.1985 0.1308 -0.0418 0.0119  -0.0327 201 GDP   A N9    
1396 C  C8    . GDP   B .   ? 0.1274 0.1696 0.1313 -0.0435 0.0177  -0.0142 201 GDP   A C8    
1397 N  N7    . GDP   B .   ? 0.1175 0.1737 0.1336 -0.0433 0.0258  -0.0182 201 GDP   A N7    
1398 C  C5    . GDP   B .   ? 0.1197 0.1619 0.1456 -0.0372 0.0145  -0.0145 201 GDP   A C5    
1399 C  C6    . GDP   B .   ? 0.1172 0.1758 0.1428 -0.0499 0.0327  -0.0255 201 GDP   A C6    
1400 O  O6    . GDP   B .   ? 0.1190 0.1859 0.1184 -0.0388 0.0037  -0.0178 201 GDP   A O6    
1401 N  N1    . GDP   B .   ? 0.1167 0.2060 0.1433 -0.0507 0.0231  -0.0397 201 GDP   A N1    
1402 C  C2    . GDP   B .   ? 0.1257 0.2240 0.1531 -0.0648 0.0377  -0.0476 201 GDP   A C2    
1403 N  N2    . GDP   B .   ? 0.1277 0.2332 0.2240 -0.0613 0.0180  -0.0495 201 GDP   A N2    
1404 N  N3    . GDP   B .   ? 0.1112 0.2042 0.1341 -0.0309 0.0101  -0.0303 201 GDP   A N3    
1405 C  C4    . GDP   B .   ? 0.1106 0.1870 0.1444 -0.0501 0.0211  -0.0086 201 GDP   A C4    
1406 MG MG    . MG    C .   ? 0.1331 0.1327 0.1345 -0.0185 -0.0249 -0.0305 202 MG    A MG    
1407 C  C1    . EDO   D .   ? 0.1885 0.4173 0.3455 0.0089  0.0038  -0.0967 203 EDO   A C1    
1408 O  O1    . EDO   D .   ? 0.0650 0.3858 0.3227 -0.0152 -0.0123 -0.0638 203 EDO   A O1    
1409 C  C2    . EDO   D .   ? 0.1251 0.3712 0.3645 0.0499  0.0003  -0.0667 203 EDO   A C2    
1410 O  O2    . EDO   D .   ? 0.1430 0.4669 0.2966 0.0267  -0.0199 -0.0808 203 EDO   A O2    
1411 C  C1    . EDO   E .   ? 0.3988 0.3565 0.3602 -0.1196 -0.0160 -0.0556 204 EDO   A C1    
1412 O  O1    . EDO   E .   ? 0.4671 0.3512 0.4419 -0.1083 -0.0443 -0.0490 204 EDO   A O1    
1413 C  C2    . EDO   E .   ? 0.3159 0.4138 0.3412 -0.0290 -0.0585 0.0005  204 EDO   A C2    
1414 O  O2    . EDO   E .   ? 0.2451 0.3602 0.3407 -0.1050 -0.0623 0.0243  204 EDO   A O2    
1415 C  C1    . EDO   F .   ? 0.2243 0.2963 0.2551 0.0007  0.0109  0.0046  205 EDO   A C1    
1416 O  O1    . EDO   F .   ? 0.1461 0.2660 0.1484 0.0206  0.0085  0.0328  205 EDO   A O1    
1417 C  C2    . EDO   F .   ? 0.3442 0.2708 0.2323 0.0022  0.0386  0.0511  205 EDO   A C2    
1418 O  O2    . EDO   F .   ? 0.4205 0.3691 0.2074 0.0305  0.0356  0.1031  205 EDO   A O2    
1419 O  OAR   . A1IIU G .   ? 0.2737 0.2167 0.3593 0.0928  -0.0224 -0.1004 206 A1IIU A OAR   
1420 C  CAQ   . A1IIU G .   ? 0.2140 0.1848 0.2851 0.0570  -0.0425 -0.0777 206 A1IIU A CAQ   
1421 C  CAG   . A1IIU G .   ? 0.2179 0.1815 0.2442 0.0589  -0.0635 -0.0705 206 A1IIU A CAG   
1422 C  CAH   . A1IIU G .   ? 0.1945 0.2356 0.2485 0.0621  -0.0626 -0.0792 206 A1IIU A CAH   
1423 C  CAF   . A1IIU G .   ? 0.2278 0.1876 0.2514 0.0544  -0.0696 -0.0616 206 A1IIU A CAF   
1424 O  OAP   . A1IIU G .   ? 0.2202 0.2155 0.2929 0.0291  -0.0116 -0.0601 206 A1IIU A OAP   
1425 C  CAE   . A1IIU G .   ? 0.2098 0.1975 0.2364 0.0468  -0.0017 -0.0808 206 A1IIU A CAE   
1426 C  CAD   . A1IIU G .   ? 0.2297 0.2396 0.2361 0.0449  -0.0510 -0.0890 206 A1IIU A CAD   
1427 C  CAC   . A1IIU G .   ? 0.1867 0.2435 0.2289 0.0484  -0.0124 -0.0772 206 A1IIU A CAC   
1428 S  SAB   . A1IIU G .   ? 0.2208 0.2645 0.2460 0.0532  -0.0459 -0.1150 206 A1IIU A SAB   
1429 O  OAA   . A1IIU G .   ? 0.2053 0.2620 0.2681 0.0308  -0.0239 -0.1179 206 A1IIU A OAA   
1430 O  OAI   . A1IIU G .   ? 0.2102 0.2822 0.3003 0.0375  -0.0042 -0.1288 206 A1IIU A OAI   
1431 N  NAJ   . A1IIU G .   ? 0.2181 0.2353 0.2378 0.0796  -0.0281 -0.0600 206 A1IIU A NAJ   
1432 C  CAK   . A1IIU G .   ? 0.2245 0.2307 0.2198 0.0685  -0.0734 -0.0793 206 A1IIU A CAK   
1433 S  SAL   . A1IIU G .   ? 0.1734 0.2315 0.2255 0.0611  -0.0518 -0.0879 206 A1IIU A SAL   
1434 C  CAM   . A1IIU G .   ? 0.1526 0.1838 0.2246 0.0424  -0.0433 -0.0741 206 A1IIU A CAM   
1435 C  CAN   . A1IIU G .   ? 0.1258 0.1806 0.2150 0.0195  -0.0333 -0.0824 206 A1IIU A CAN   
1436 CL CLAO  . A1IIU G .   ? 0.1532 0.2009 0.2372 0.0466  -0.0500 -0.0606 206 A1IIU A CLAO  
1437 C  CAV   . A1IIU G .   ? 0.1239 0.2228 0.2007 0.0492  -0.0490 -0.0671 206 A1IIU A CAV   
1438 C  CAU   . A1IIU G .   ? 0.2292 0.2293 0.1745 0.0337  -0.0533 -0.0895 206 A1IIU A CAU   
1439 C  CAT   . A1IIU G .   ? 0.1753 0.1962 0.2141 0.0310  -0.0498 -0.0487 206 A1IIU A CAT   
1440 O  OAS   . A1IIU G .   ? 0.2427 0.2066 0.2230 0.0000  -0.0140 -0.0760 206 A1IIU A OAS   
1441 C  CAW   . A1IIU G .   ? 0.1818 0.1690 0.2096 0.0305  -0.0551 -0.0796 206 A1IIU A CAW   
1442 N  NBJ   . A1IIU G .   ? 0.2142 0.1943 0.2199 0.0760  -0.0806 -0.0822 206 A1IIU A NBJ   
1443 C  CBI   . A1IIU G .   ? 0.2232 0.2063 0.2476 0.0306  -0.0472 -0.0740 206 A1IIU A CBI   
1444 C  CBH   . A1IIU G .   ? 0.2387 0.2342 0.3129 0.0281  0.0011  -0.0702 206 A1IIU A CBH   
1445 C  CBG   . A1IIU G .   ? 0.2170 0.2996 0.2869 0.0741  0.0152  -0.0737 206 A1IIU A CBG   
1446 C  CBF   . A1IIU G .   ? 0.2520 0.2045 0.2954 0.0506  -0.0140 -0.1108 206 A1IIU A CBF   
1447 C  CBE   . A1IIU G .   ? 0.2198 0.2134 0.2855 0.0555  -0.0123 -0.0638 206 A1IIU A CBE   
1448 N  NAX   . A1IIU G .   ? 0.2577 0.2020 0.2751 0.0519  -0.0311 -0.0717 206 A1IIU A NAX   
1449 C  CAY   . A1IIU G .   ? 0.2792 0.2160 0.3431 0.0497  -0.0222 -0.0610 206 A1IIU A CAY   
1450 C  CAZ   . A1IIU G .   ? 0.2620 0.2504 0.3794 0.0448  -0.0264 -0.0221 206 A1IIU A CAZ   
1451 C  CBA   . A1IIU G .   ? 0.2145 0.2655 0.4562 0.0331  -0.0145 -0.0168 206 A1IIU A CBA   
1452 N  NBB   . A1IIU G .   ? 0.2417 0.2057 0.4500 0.0137  0.0121  0.0016  206 A1IIU A NBB   
1453 C  CBC   . A1IIU G .   ? 0.3096 0.2103 0.3388 -0.0033 -0.0089 -0.0162 206 A1IIU A CBC   
1454 C  CBD   . A1IIU G .   ? 0.2711 0.2042 0.3304 -0.0146 -0.0436 -0.0502 206 A1IIU A CBD   
1455 O  O     . HOH   H .   ? 0.1112 0.3966 0.2107 -0.0326 0.0091  -0.0130 301 HOH   A O     
1456 O  O     . HOH   H .   ? 0.2981 0.3141 0.3955 0.0605  0.1540  0.0483  302 HOH   A O     
1457 O  O     . HOH   H .   ? 0.1562 0.6136 0.4183 0.0248  0.0123  0.1160  303 HOH   A O     
1458 O  O     . HOH   H .   ? 0.1623 0.2577 0.2549 -0.0055 -0.0292 -0.0568 304 HOH   A O     
1459 O  O     . HOH   H .   ? 0.1805 0.3434 0.4038 -0.0790 0.0251  0.0910  305 HOH   A O     
1460 O  O     . HOH   H .   ? 0.6072 0.5700 0.3402 -0.1817 -0.0616 -0.1148 306 HOH   A O     
1461 O  O     . HOH   H .   ? 0.1227 0.2370 0.2055 -0.0085 0.0077  -0.0451 307 HOH   A O     
1462 O  O     . HOH   H .   ? 0.1140 0.1861 0.1868 -0.0305 0.0128  -0.0236 308 HOH   A O     
1463 O  O     . HOH   H .   ? 0.2384 0.5934 0.3335 0.1207  0.0161  -0.0691 309 HOH   A O     
1464 O  O     . HOH   H .   ? 0.1346 0.1869 0.1702 -0.0124 -0.0362 -0.0558 310 HOH   A O     
1465 O  O     . HOH   H .   ? 0.3823 0.3542 0.2144 0.0591  -0.1143 0.0496  311 HOH   A O     
1466 O  O     . HOH   H .   ? 0.3407 0.2935 0.4477 0.0886  -0.0869 0.0242  312 HOH   A O     
1467 O  O     . HOH   H .   ? 0.3899 0.6903 0.2551 -0.1627 -0.0777 0.0570  313 HOH   A O     
1468 O  O     . HOH   H .   ? 0.5021 0.3621 0.4027 0.1940  -0.1979 -0.1471 314 HOH   A O     
1469 O  O     . HOH   H .   ? 0.3655 0.4387 0.8601 -0.0434 -0.0257 -0.0028 315 HOH   A O     
1470 O  O     . HOH   H .   ? 0.4148 0.2371 0.2838 -0.0366 0.0977  -0.0275 316 HOH   A O     
1471 O  O     . HOH   H .   ? 0.0996 0.3492 0.2833 0.0026  0.0133  -0.1122 317 HOH   A O     
1472 O  O     . HOH   H .   ? 0.5654 0.6101 0.2333 0.0532  -0.0427 0.0610  318 HOH   A O     
1473 O  O     . HOH   H .   ? 0.5019 0.3940 0.3495 -0.1110 0.0165  0.0043  319 HOH   A O     
1474 O  O     . HOH   H .   ? 0.2290 0.5305 0.4142 -0.0674 -0.1051 0.0449  320 HOH   A O     
1475 O  O     . HOH   H .   ? 0.1748 0.1939 0.1719 -0.0347 -0.0102 -0.0415 321 HOH   A O     
1476 O  O     . HOH   H .   ? 0.1259 0.2715 0.1498 -0.0300 -0.0140 -0.0463 322 HOH   A O     
1477 O  O     . HOH   H .   ? 0.3067 0.3146 0.3779 -0.0099 0.0130  0.0413  323 HOH   A O     
1478 O  O     . HOH   H .   ? 0.5003 0.3443 0.4606 0.1151  0.1422  0.2010  324 HOH   A O     
1479 O  O     . HOH   H .   ? 0.1573 0.4056 0.2556 0.0488  -0.0735 -0.1295 325 HOH   A O     
1480 O  O     . HOH   H .   ? 0.2665 0.1838 0.2590 0.0109  -0.0757 -0.0311 326 HOH   A O     
1481 O  O     . HOH   H .   ? 0.1258 0.2176 0.1319 0.0462  -0.0137 -0.0363 327 HOH   A O     
1482 O  O     . HOH   H .   ? 0.5176 0.4716 0.5939 -0.0049 0.1698  -0.0819 328 HOH   A O     
1483 O  O     . HOH   H .   ? 0.0835 0.3087 0.1586 -0.0354 0.0204  -0.0708 329 HOH   A O     
1484 O  O     . HOH   H .   ? 0.1835 0.1888 0.1429 -0.0384 -0.0247 -0.0365 330 HOH   A O     
1485 O  O     . HOH   H .   ? 0.2252 0.2239 0.3132 -0.0261 0.0183  -0.1143 331 HOH   A O     
1486 O  O     . HOH   H .   ? 0.1001 0.3497 0.2259 -0.0312 -0.0074 -0.0751 332 HOH   A O     
1487 O  O     . HOH   H .   ? 0.5031 0.5339 0.3526 0.0195  -0.0050 0.1029  333 HOH   A O     
1488 O  O     . HOH   H .   ? 0.2793 0.6785 0.8516 0.0530  0.0238  -0.2064 334 HOH   A O     
1489 O  O     . HOH   H .   ? 0.1549 0.3528 0.3096 -0.0068 0.0042  -0.0128 335 HOH   A O     
1490 O  O     . HOH   H .   ? 0.3822 0.4549 0.4249 0.0792  -0.0252 0.0086  336 HOH   A O     
1491 O  O     . HOH   H .   ? 0.1679 0.6629 0.4045 -0.0892 0.0268  0.0405  337 HOH   A O     
1492 O  O     . HOH   H .   ? 0.1800 0.1723 0.1190 -0.0044 0.0260  -0.0226 338 HOH   A O     
1493 O  O     . HOH   H .   ? 0.2083 0.2097 0.2981 -0.0584 -0.0299 -0.0881 339 HOH   A O     
1494 O  O     . HOH   H .   ? 0.4848 0.3528 0.4059 0.0473  -0.1587 -0.0019 340 HOH   A O     
1495 O  O     . HOH   H .   ? 0.2672 0.2102 0.1563 -0.0772 0.0152  0.0093  341 HOH   A O     
1496 O  O     . HOH   H .   ? 0.1902 0.6212 0.4059 0.0296  0.0325  0.1713  342 HOH   A O     
1497 O  O     . HOH   H .   ? 0.8085 0.5128 0.3452 0.2873  0.0763  0.1161  343 HOH   A O     
1498 O  O     . HOH   H .   ? 0.3596 0.7155 0.4174 -0.1175 0.0595  -0.0364 344 HOH   A O     
1499 O  O     . HOH   H .   ? 0.2430 0.5374 0.3258 0.0046  -0.0107 -0.0116 345 HOH   A O     
1500 O  O     . HOH   H .   ? 0.2308 0.3915 0.3834 -0.0743 -0.1598 0.0392  346 HOH   A O     
1501 O  O     . HOH   H .   ? 0.2587 0.4041 0.5004 -0.0100 -0.0720 -0.2054 347 HOH   A O     
1502 O  O     . HOH   H .   ? 0.5175 0.4941 0.4761 0.0686  0.1399  0.0668  348 HOH   A O     
1503 O  O     . HOH   H .   ? 0.3323 0.5285 0.3689 -0.1034 -0.1397 -0.0178 349 HOH   A O     
1504 O  O     . HOH   H .   ? 0.4188 0.2575 0.3125 -0.0187 0.1256  -0.0421 350 HOH   A O     
1505 O  O     . HOH   H .   ? 0.1025 0.1809 0.1078 0.0145  -0.0019 -0.0275 351 HOH   A O     
1506 O  O     . HOH   H .   ? 0.2061 0.3402 0.2857 0.0195  0.0327  -0.0832 352 HOH   A O     
1507 O  O     . HOH   H .   ? 0.2356 0.2597 0.1747 -0.0020 0.0526  0.0278  353 HOH   A O     
1508 O  O     . HOH   H .   ? 0.1285 0.5068 0.2174 -0.0283 0.0545  -0.0508 354 HOH   A O     
1509 O  O     . HOH   H .   ? 0.2496 0.3975 0.2247 0.0011  -0.0089 -0.0465 355 HOH   A O     
1510 O  O     . HOH   H .   ? 0.3592 0.6804 0.4423 0.0982  0.1704  0.0712  356 HOH   A O     
1511 O  O     . HOH   H .   ? 0.1825 0.1981 0.2536 -0.0112 -0.0982 -0.0102 357 HOH   A O     
1512 O  O     . HOH   H .   ? 1.1036 0.5692 0.4666 -0.1374 -0.1084 -0.1098 358 HOH   A O     
1513 O  O     . HOH   H .   ? 0.2195 0.3910 0.3440 -0.0707 -0.0572 0.0162  359 HOH   A O     
1514 O  O     . HOH   H .   ? 0.3289 0.4266 0.2858 -0.0962 0.0501  0.0431  360 HOH   A O     
1515 O  O     . HOH   H .   ? 0.5802 0.6163 0.7494 -0.0622 -0.0959 -0.0611 361 HOH   A O     
1516 O  O     . HOH   H .   ? 0.2174 0.2672 0.1976 0.0105  -0.0047 -0.0704 362 HOH   A O     
1517 O  O     . HOH   H .   ? 0.1280 0.5142 0.4548 -0.0230 0.0075  0.0964  363 HOH   A O     
1518 O  O     . HOH   H .   ? 0.2896 0.4005 0.4699 0.0819  -0.1761 -0.0202 364 HOH   A O     
1519 O  O     . HOH   H .   ? 0.2810 0.6917 0.5194 0.1416  -0.0768 0.0360  365 HOH   A O     
1520 O  O     . HOH   H .   ? 0.3102 0.6014 0.4497 -0.0012 0.1110  0.2219  366 HOH   A O     
1521 O  O     . HOH   H .   ? 0.3395 0.5570 0.3199 0.1161  -0.0585 -0.1965 367 HOH   A O     
1522 O  O     . HOH   H .   ? 0.2205 0.1583 0.1622 -0.0028 -0.0463 -0.0229 368 HOH   A O     
1523 O  O     . HOH   H .   ? 0.3568 0.6109 0.2194 -0.0834 -0.1023 0.0281  369 HOH   A O     
1524 O  O     . HOH   H .   ? 0.2427 0.2172 0.4601 0.0374  -0.2066 -0.0885 370 HOH   A O     
1525 O  O     . HOH   H .   ? 0.4444 0.3227 0.2900 0.0452  0.0522  -0.0060 371 HOH   A O     
1526 O  O     . HOH   H .   ? 0.0880 0.2635 0.1596 -0.0042 0.0087  -0.0424 372 HOH   A O     
1527 O  O     . HOH   H .   ? 0.2707 0.7386 0.4610 -0.1348 0.0849  -0.0882 373 HOH   A O     
1528 O  O     . HOH   H .   ? 0.3504 0.4369 0.3745 -0.0152 -0.0338 -0.0447 374 HOH   A O     
1529 O  O     . HOH   H .   ? 0.1174 0.4587 0.4162 -0.0263 -0.0472 -0.0816 375 HOH   A O     
1530 O  O     . HOH   H .   ? 0.3246 0.4007 0.3824 -0.1001 -0.0189 0.0288  376 HOH   A O     
1531 O  O     . HOH   H .   ? 0.2717 0.6266 0.4423 0.0516  -0.0152 0.0037  377 HOH   A O     
1532 O  O     . HOH   H .   ? 0.1468 0.3091 0.3382 -0.0093 0.0478  -0.1063 378 HOH   A O     
1533 O  O     . HOH   H .   ? 0.2205 0.4533 0.1878 0.0254  0.0077  -0.0456 379 HOH   A O     
1534 O  O     . HOH   H .   ? 0.3457 0.4177 0.5570 0.0114  0.1312  -0.0739 380 HOH   A O     
1535 O  O     . HOH   H .   ? 0.3103 0.7137 0.6285 -0.0831 0.0228  -0.2381 381 HOH   A O     
1536 O  O     . HOH   H .   ? 0.1624 0.4373 0.4035 -0.0438 0.0579  -0.1669 382 HOH   A O     
1537 O  O     . HOH   H .   ? 0.4310 0.2742 0.5339 0.0771  -0.0272 -0.1667 383 HOH   A O     
1538 O  O     . HOH   H .   ? 0.4730 0.4250 0.5593 -0.1095 0.2679  -0.0969 384 HOH   A O     
1539 O  O     . HOH   H .   ? 0.2701 0.3021 0.5362 -0.0145 -0.1339 0.0017  385 HOH   A O     
1540 O  O     . HOH   H .   ? 0.4201 0.5905 0.9126 0.0703  0.2559  -0.3734 386 HOH   A O     
1541 O  O     . HOH   H .   ? 0.8148 0.3433 0.3810 -0.0715 -0.0270 0.0725  387 HOH   A O     
1542 O  O     . HOH   H .   ? 0.2275 0.7779 0.4277 0.2459  -0.0071 0.0204  388 HOH   A O     
1543 O  O     . HOH   H .   ? 0.1699 0.4370 0.2055 -0.0303 -0.0253 -0.0639 389 HOH   A O     
1544 O  O     . HOH   H .   ? 0.1601 0.2667 0.2003 0.0233  0.0073  0.0227  390 HOH   A O     
1545 O  O     . HOH   H .   ? 0.5654 0.8600 0.4461 -0.0052 -0.0511 0.2338  391 HOH   A O     
1546 O  O     . HOH   H .   ? 0.1262 0.2625 0.3643 -0.0159 0.0403  -0.1632 392 HOH   A O     
1547 O  O     . HOH   H .   ? 0.0815 0.4905 0.2646 0.0071  0.0118  0.0160  393 HOH   A O     
1548 O  O     . HOH   H .   ? 0.4023 0.2582 0.3814 0.0865  0.0366  -0.0712 394 HOH   A O     
1549 O  O     . HOH   H .   ? 0.8511 0.9883 0.9783 0.7492  0.4129  0.3513  395 HOH   A O     
1550 O  O     . HOH   H .   ? 0.1291 0.2292 0.1479 -0.0113 -0.0074 0.0101  396 HOH   A O     
1551 O  O     . HOH   H .   ? 0.1074 0.5451 0.2868 -0.0767 0.0012  -0.1181 397 HOH   A O     
1552 O  O     . HOH   H .   ? 0.1636 0.2509 0.2393 -0.0043 0.0557  -0.0279 398 HOH   A O     
1553 O  O     . HOH   H .   ? 0.3972 0.6784 0.5535 -0.1910 -0.1599 -0.0002 399 HOH   A O     
1554 O  O     . HOH   H .   ? 0.3859 0.5434 0.9176 0.0561  -0.1820 0.2009  400 HOH   A O     
1555 O  O     . HOH   H .   ? 0.4156 0.4843 0.5735 -0.1633 -0.0892 0.2464  401 HOH   A O     
1556 O  O     . HOH   H .   ? 0.6142 0.3222 0.6226 0.0089  0.0958  -0.1192 402 HOH   A O     
1557 O  O     . HOH   H .   ? 0.3730 0.5067 0.4149 -0.0528 -0.1557 -0.1725 403 HOH   A O     
1558 O  O     . HOH   H .   ? 0.3316 0.5702 0.6202 0.1240  -0.0290 -0.0926 404 HOH   A O     
1559 O  O     . HOH   H .   ? 0.7354 0.3983 0.8791 -0.0809 -0.1839 0.1411  405 HOH   A O     
1560 O  O     . HOH   H .   ? 0.5349 0.3722 0.4060 0.1754  -0.1827 -0.1378 406 HOH   A O     
1561 O  O     . HOH   H .   ? 0.7543 0.5292 0.6202 -0.1964 0.2093  -0.0808 407 HOH   A O     
1562 O  O     . HOH   H .   ? 0.3802 0.7208 0.4985 0.1862  0.0900  0.2255  408 HOH   A O     
1563 O  O     . HOH   H .   ? 0.6115 0.7790 0.2668 0.0635  -0.0354 0.0670  409 HOH   A O     
1564 O  O     . HOH   H .   ? 0.2188 0.2521 0.3561 -0.0150 0.0435  -0.0453 410 HOH   A O     
1565 O  O     . HOH   H .   ? 0.2305 0.3343 0.2939 -0.1000 -0.0031 -0.0179 411 HOH   A O     
1566 O  O     . HOH   H .   ? 0.5602 0.7899 0.6879 0.1306  0.5559  -0.1741 412 HOH   A O     
1567 O  O     . HOH   H .   ? 0.2125 0.7304 0.2465 0.1225  -0.0329 -0.1192 413 HOH   A O     
1568 O  O     . HOH   H .   ? 0.3490 0.5264 0.1895 -0.0254 0.0228  -0.1378 414 HOH   A O     
1569 O  O     . HOH   H .   ? 0.6065 0.6192 0.5136 0.1142  0.0462  0.0597  415 HOH   A O     
1570 O  O     . HOH   H .   ? 0.7981 0.2943 0.5260 -0.0449 0.1089  -0.0072 416 HOH   A O     
1571 O  O     . HOH   H .   ? 0.4297 0.3559 0.3562 0.0570  -0.0281 0.0137  417 HOH   A O     
1572 O  O     . HOH   H .   ? 0.3044 0.5309 0.6695 0.0428  -0.1643 -0.1286 418 HOH   A O     
1573 O  O     . HOH   H .   ? 0.0729 0.4673 0.1835 0.0073  -0.0606 0.0504  419 HOH   A O     
1574 O  O     . HOH   H .   ? 0.9432 0.5578 0.4901 -0.1154 -0.1507 0.2488  420 HOH   A O     
1575 O  O     . HOH   H .   ? 0.3231 0.4407 0.9036 -0.0108 -0.1522 -0.2218 421 HOH   A O     
1576 O  O     . HOH   H .   ? 0.3531 0.7773 0.4031 -0.1824 0.0661  -0.3097 422 HOH   A O     
1577 O  O     . HOH   H .   ? 0.7484 0.7637 0.8280 -0.2373 -0.7393 -0.0044 423 HOH   A O     
1578 O  O     . HOH   H .   ? 0.5165 0.4420 0.4516 0.0016  -0.1031 -0.1607 424 HOH   A O     
1579 O  O     . HOH   H .   ? 0.3082 0.5103 0.5873 -0.0305 -0.0850 0.1551  425 HOH   A O     
1580 O  O     . HOH   H .   ? 0.3852 0.5506 0.6085 -0.0701 0.0632  0.0210  426 HOH   A O     
1581 O  O     . HOH   H .   ? 0.7391 0.6192 0.6663 -0.1246 -0.3193 0.2066  427 HOH   A O     
1582 O  O     . HOH   H .   ? 0.6525 0.3966 0.2450 -0.2700 0.1045  -0.0905 428 HOH   A O     
1583 O  O     . HOH   H .   ? 0.6674 0.4243 0.6401 -0.0348 -0.2286 0.0709  429 HOH   A O     
1584 O  O     . HOH   H .   ? 0.5025 0.3483 0.5793 -0.1669 -0.0102 -0.0082 430 HOH   A O     
# 
