data_9GGU
# 
_entry.id   9GGU 
# 
_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   9GGU         pdb_00009ggu 10.2210/pdb9ggu/pdb 
WWPDB D_1292140468 ?            ?                   
# 
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                        9GGU 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.content_type 
_pdbx_database_related.db_id 
_pdbx_database_related.db_name 
_pdbx_database_related.details 
unspecified 9GGY PDB . 
unspecified 9GH2 PDB . 
unspecified 9GGZ PDB . 
unspecified 9GH0 PDB . 
unspecified 9GH1 PDB . 
unspecified 9GGW PDB . 
unspecified 9GGX PDB . 
unspecified 9GGT PDB . 
unspecified 9GGV PDB . 
unspecified 9G0Y PDB . 
unspecified 9G4B PDB . 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexander.schuettelkopf@cancer.org.uk 
_pdbx_contact_author.name_first         Alexander 
_pdbx_contact_author.name_last          Schuettelkopf 
_pdbx_contact_author.name_mi            W. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9424-8730 
# 
_audit_author.name               'Schuettelkopf, A.W.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-9424-8730 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                9129 
_citation.page_last                 9161 
_citation.title                     
'Reversible Small Molecule Multivariant Ras Inhibitors Display Tunable Affinity for the Active and Inactive Forms of Ras.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02929 
_citation.pdbx_database_id_PubMed   40162713 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Parry, C.W.'        1  ? 
primary 'Pellicano, F.'      2  ? 
primary 'Schuttelkopf, A.W.' 3  ? 
primary 'Beyer, K.S.'        4  ? 
primary 'Bower, J.'          5  ? 
primary 'Bryson, A.'         6  ? 
primary 'Cameron, K.'        7  ? 
primary 'Cerutti, N.M.'      8  ? 
primary 'Clark, J.P.'        9  ? 
primary 'Davidson, S.C.'     10 ? 
primary 'Davies, K.'         11 ? 
primary 'Drysdale, M.J.'     12 ? 
primary 'Engelman, J.'       13 ? 
primary 'Estevan-Barber, A.' 14 ? 
primary 'Gohlke, A.'         15 ? 
primary 'Gray, C.H.'         16 ? 
primary 'Guthy, D.A.'        17 ? 
primary 'Hong, M.'           18 ? 
primary 'Hopkins, A.'        19 ? 
primary 'Hutchinson, L.D.'   20 ? 
primary 'Konczal, J.'        21 ? 
primary 'Maira, M.'          22 ? 
primary 'McArthur, D.'       23 ? 
primary 'Mezna, M.'          24 ? 
primary 'McKinnon, H.'       25 ? 
primary 'Nepravishta, R.'    26 ? 
primary 'Ostermann, N.'      27 ? 
primary 'Pasquali, C.C.'     28 ? 
primary 'Pollock, K.'        29 ? 
primary 'Pugliese, A.'       30 ? 
primary 'Rooney, N.'         31 ? 
primary 'Schmiedeberg, N.'   32 ? 
primary 'Shaw, P.'           33 ? 
primary 'Velez-Vega, C.'     34 ? 
primary 'West, C.'           35 ? 
primary 'West, R.'           36 ? 
primary 'Zecri, F.'          37 ? 
primary 'Taylor, J.B.'       38 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'GTPase KRas'                                                     19607.078 1   3.6.5.2 C118S ? ? 
2 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                                        443.201   1   ?       ?     ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                                   24.305    1   ?       ?     ? ? 
4 non-polymer syn 'N-(7-chloro-1,3-benzothiazol-2-yl)-2-hydroxy-benzenesulfonamide' 340.805   1   ?       ?     ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                    62.068    1   ?       ?     ? ? 
6 water       nat water                                                             18.015    119 ?       ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'K-Ras 2,Ki-Ras,c-K-ras,c-Ki-ras' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GGSMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEG
FLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFY
TLVREIRQYRLK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GGSMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEG
FLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFY
TLVREIRQYRLK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "GUANOSINE-5'-DIPHOSPHATE"                                        GDP   
3 'MAGNESIUM ION'                                                   MG    
4 'N-(7-chloro-1,3-benzothiazol-2-yl)-2-hydroxy-benzenesulfonamide' A1IMC 
5 1,2-ETHANEDIOL                                                    EDO   
6 water                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   GLY n 
1 3   SER n 
1 4   MET n 
1 5   THR n 
1 6   GLU n 
1 7   TYR n 
1 8   LYS n 
1 9   LEU n 
1 10  VAL n 
1 11  VAL n 
1 12  VAL n 
1 13  GLY n 
1 14  ALA n 
1 15  GLY n 
1 16  GLY n 
1 17  VAL n 
1 18  GLY n 
1 19  LYS n 
1 20  SER n 
1 21  ALA n 
1 22  LEU n 
1 23  THR n 
1 24  ILE n 
1 25  GLN n 
1 26  LEU n 
1 27  ILE n 
1 28  GLN n 
1 29  ASN n 
1 30  HIS n 
1 31  PHE n 
1 32  VAL n 
1 33  ASP n 
1 34  GLU n 
1 35  TYR n 
1 36  ASP n 
1 37  PRO n 
1 38  THR n 
1 39  ILE n 
1 40  GLU n 
1 41  ASP n 
1 42  SER n 
1 43  TYR n 
1 44  ARG n 
1 45  LYS n 
1 46  GLN n 
1 47  VAL n 
1 48  VAL n 
1 49  ILE n 
1 50  ASP n 
1 51  GLY n 
1 52  GLU n 
1 53  THR n 
1 54  CYS n 
1 55  LEU n 
1 56  LEU n 
1 57  ASP n 
1 58  ILE n 
1 59  LEU n 
1 60  ASP n 
1 61  THR n 
1 62  ALA n 
1 63  GLY n 
1 64  GLN n 
1 65  GLU n 
1 66  GLU n 
1 67  TYR n 
1 68  SER n 
1 69  ALA n 
1 70  MET n 
1 71  ARG n 
1 72  ASP n 
1 73  GLN n 
1 74  TYR n 
1 75  MET n 
1 76  ARG n 
1 77  THR n 
1 78  GLY n 
1 79  GLU n 
1 80  GLY n 
1 81  PHE n 
1 82  LEU n 
1 83  CYS n 
1 84  VAL n 
1 85  PHE n 
1 86  ALA n 
1 87  ILE n 
1 88  ASN n 
1 89  ASN n 
1 90  THR n 
1 91  LYS n 
1 92  SER n 
1 93  PHE n 
1 94  GLU n 
1 95  ASP n 
1 96  ILE n 
1 97  HIS n 
1 98  HIS n 
1 99  TYR n 
1 100 ARG n 
1 101 GLU n 
1 102 GLN n 
1 103 ILE n 
1 104 LYS n 
1 105 ARG n 
1 106 VAL n 
1 107 LYS n 
1 108 ASP n 
1 109 SER n 
1 110 GLU n 
1 111 ASP n 
1 112 VAL n 
1 113 PRO n 
1 114 MET n 
1 115 VAL n 
1 116 LEU n 
1 117 VAL n 
1 118 GLY n 
1 119 ASN n 
1 120 LYS n 
1 121 SER n 
1 122 ASP n 
1 123 LEU n 
1 124 PRO n 
1 125 SER n 
1 126 ARG n 
1 127 THR n 
1 128 VAL n 
1 129 ASP n 
1 130 THR n 
1 131 LYS n 
1 132 GLN n 
1 133 ALA n 
1 134 GLN n 
1 135 ASP n 
1 136 LEU n 
1 137 ALA n 
1 138 ARG n 
1 139 SER n 
1 140 TYR n 
1 141 GLY n 
1 142 ILE n 
1 143 PRO n 
1 144 PHE n 
1 145 ILE n 
1 146 GLU n 
1 147 THR n 
1 148 SER n 
1 149 ALA n 
1 150 LYS n 
1 151 THR n 
1 152 ARG n 
1 153 GLN n 
1 154 ARG n 
1 155 VAL n 
1 156 GLU n 
1 157 ASP n 
1 158 ALA n 
1 159 PHE n 
1 160 TYR n 
1 161 THR n 
1 162 LEU n 
1 163 VAL n 
1 164 ARG n 
1 165 GLU n 
1 166 ILE n 
1 167 ARG n 
1 168 GLN n 
1 169 TYR n 
1 170 ARG n 
1 171 LEU n 
1 172 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   172 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'KRAS, KRAS2, RASK2' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IMC non-polymer         . 'N-(7-chloro-1,3-benzothiazol-2-yl)-2-hydroxy-benzenesulfonamide' ?                 
'C13 H9 Cl N2 O3 S2' 340.805 
ALA   'L-peptide linking' y ALANINE                                                           ?                 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                          ?                 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                        ?                 'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                   ?                 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                          ?                 'C3 H7 N O2 S' 
121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                                                    'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068  
GDP   'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE"                                        ?                 
'C10 H15 N5 O11 P2'  443.201 
GLN   'L-peptide linking' y GLUTAMINE                                                         ?                 'C5 H10 N2 O3' 
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                   ?                 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                           ?                 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                         ?                 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                             ?                 'H2 O' 18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                        ?                 'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                           ?                 'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                            ?                 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                        ?                 'C5 H11 N O2 S' 
149.211 
MG    non-polymer         . 'MAGNESIUM ION'                                                   ?                 'Mg 2' 24.305  
PHE   'L-peptide linking' y PHENYLALANINE                                                     ?                 'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                           ?                 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                            ?                 'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                         ?                 'C4 H9 N O3' 
119.119 
TYR   'L-peptide linking' y TYROSINE                                                          ?                 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                            ?                 'C5 H11 N O2' 
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   GLY 2   -1  ?   ?   ?   A . n 
A 1 3   SER 3   0   ?   ?   ?   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 A1IMC 1   203 1    A1IMC DRG A . 
E 5 EDO   1   204 1    EDO   EDO A . 
F 6 HOH   1   301 144  HOH   HOH A . 
F 6 HOH   2   302 64   HOH   HOH A . 
F 6 HOH   3   303 49   HOH   HOH A . 
F 6 HOH   4   304 174  HOH   HOH A . 
F 6 HOH   5   305 170  HOH   HOH A . 
F 6 HOH   6   306 6    HOH   HOH A . 
F 6 HOH   7   307 88   HOH   HOH A . 
F 6 HOH   8   308 199  HOH   HOH A . 
F 6 HOH   9   309 173  HOH   HOH A . 
F 6 HOH   10  310 130  HOH   HOH A . 
F 6 HOH   11  311 7    HOH   HOH A . 
F 6 HOH   12  312 192  HOH   HOH A . 
F 6 HOH   13  313 16   HOH   HOH A . 
F 6 HOH   14  314 178  HOH   HOH A . 
F 6 HOH   15  315 171  HOH   HOH A . 
F 6 HOH   16  316 112  HOH   HOH A . 
F 6 HOH   17  317 140  HOH   HOH A . 
F 6 HOH   18  318 99   HOH   HOH A . 
F 6 HOH   19  319 197  HOH   HOH A . 
F 6 HOH   20  320 114  HOH   HOH A . 
F 6 HOH   21  321 119  HOH   HOH A . 
F 6 HOH   22  322 93   HOH   HOH A . 
F 6 HOH   23  323 203  HOH   HOH A . 
F 6 HOH   24  324 28   HOH   HOH A . 
F 6 HOH   25  325 143  HOH   HOH A . 
F 6 HOH   26  326 193  HOH   HOH A . 
F 6 HOH   27  327 196  HOH   HOH A . 
F 6 HOH   28  328 151  HOH   HOH A . 
F 6 HOH   29  329 48   HOH   HOH A . 
F 6 HOH   30  330 131  HOH   HOH A . 
F 6 HOH   31  331 113  HOH   HOH A . 
F 6 HOH   32  332 168  HOH   HOH A . 
F 6 HOH   33  333 21   HOH   HOH A . 
F 6 HOH   34  334 44   HOH   HOH A . 
F 6 HOH   35  335 138  HOH   HOH A . 
F 6 HOH   36  336 179  HOH   HOH A . 
F 6 HOH   37  337 147  HOH   HOH A . 
F 6 HOH   38  338 10   HOH   HOH A . 
F 6 HOH   39  339 141  HOH   HOH A . 
F 6 HOH   40  340 139  HOH   HOH A . 
F 6 HOH   41  341 3    HOH   HOH A . 
F 6 HOH   42  342 169  HOH   HOH A . 
F 6 HOH   43  343 187  HOH   HOH A . 
F 6 HOH   44  344 30   HOH   HOH A . 
F 6 HOH   45  345 26   HOH   HOH A . 
F 6 HOH   46  346 9    HOH   HOH A . 
F 6 HOH   47  347 92   HOH   HOH A . 
F 6 HOH   48  348 101  HOH   HOH A . 
F 6 HOH   49  349 5    HOH   HOH A . 
F 6 HOH   50  350 68   HOH   HOH A . 
F 6 HOH   51  351 31   HOH   HOH A . 
F 6 HOH   52  352 115  HOH   HOH A . 
F 6 HOH   53  353 40   HOH   HOH A . 
F 6 HOH   54  354 132  HOH   HOH A . 
F 6 HOH   55  355 41   HOH   HOH A . 
F 6 HOH   56  356 89   HOH   HOH A . 
F 6 HOH   57  357 149  HOH   HOH A . 
F 6 HOH   58  358 105  HOH   HOH A . 
F 6 HOH   59  359 213  HOH   HOH A . 
F 6 HOH   60  360 1    HOH   HOH A . 
F 6 HOH   61  361 98   HOH   HOH A . 
F 6 HOH   62  362 39   HOH   HOH A . 
F 6 HOH   63  363 91   HOH   HOH A . 
F 6 HOH   64  364 118  HOH   HOH A . 
F 6 HOH   65  365 166  HOH   HOH A . 
F 6 HOH   66  366 19   HOH   HOH A . 
F 6 HOH   67  367 157  HOH   HOH A . 
F 6 HOH   68  368 207  HOH   HOH A . 
F 6 HOH   69  369 102  HOH   HOH A . 
F 6 HOH   70  370 17   HOH   HOH A . 
F 6 HOH   71  371 188  HOH   HOH A . 
F 6 HOH   72  372 34   HOH   HOH A . 
F 6 HOH   73  373 159  HOH   HOH A . 
F 6 HOH   74  374 103  HOH   HOH A . 
F 6 HOH   75  375 176  HOH   HOH A . 
F 6 HOH   76  376 142  HOH   HOH A . 
F 6 HOH   77  377 210  HOH   HOH A . 
F 6 HOH   78  378 165  HOH   HOH A . 
F 6 HOH   79  379 154  HOH   HOH A . 
F 6 HOH   80  380 90   HOH   HOH A . 
F 6 HOH   81  381 116  HOH   HOH A . 
F 6 HOH   82  382 106  HOH   HOH A . 
F 6 HOH   83  383 59   HOH   HOH A . 
F 6 HOH   84  384 163  HOH   HOH A . 
F 6 HOH   85  385 164  HOH   HOH A . 
F 6 HOH   86  386 33   HOH   HOH A . 
F 6 HOH   87  387 183  HOH   HOH A . 
F 6 HOH   88  388 208  HOH   HOH A . 
F 6 HOH   89  389 96   HOH   HOH A . 
F 6 HOH   90  390 29   HOH   HOH A . 
F 6 HOH   91  391 185  HOH   HOH A . 
F 6 HOH   92  392 95   HOH   HOH A . 
F 6 HOH   93  393 198  HOH   HOH A . 
F 6 HOH   94  394 150  HOH   HOH A . 
F 6 HOH   95  395 209  HOH   HOH A . 
F 6 HOH   96  396 156  HOH   HOH A . 
F 6 HOH   97  397 66   HOH   HOH A . 
F 6 HOH   98  398 217  HOH   HOH A . 
F 6 HOH   99  399 153  HOH   HOH A . 
F 6 HOH   100 400 160  HOH   HOH A . 
F 6 HOH   101 401 145  HOH   HOH A . 
F 6 HOH   102 402 110  HOH   HOH A . 
F 6 HOH   103 403 35   HOH   HOH A . 
F 6 HOH   104 404 180  HOH   HOH A . 
F 6 HOH   105 405 38   HOH   HOH A . 
F 6 HOH   106 406 155  HOH   HOH A . 
F 6 HOH   107 407 172  HOH   HOH A . 
F 6 HOH   108 408 202  HOH   HOH A . 
F 6 HOH   109 409 206  HOH   HOH A . 
F 6 HOH   110 410 195  HOH   HOH A . 
F 6 HOH   111 411 190  HOH   HOH A . 
F 6 HOH   112 412 162  HOH   HOH A . 
F 6 HOH   113 413 148  HOH   HOH A . 
F 6 HOH   114 414 158  HOH   HOH A . 
F 6 HOH   115 415 200  HOH   HOH A . 
F 6 HOH   116 416 218  HOH   HOH A . 
F 6 HOH   117 417 212  HOH   HOH A . 
F 6 HOH   118 418 205  HOH   HOH A . 
F 6 HOH   119 419 214  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 0 A GLU 31 ? CG  ? A GLU 34 CG  
2 1 Y 0 A GLU 31 ? CD  ? A GLU 34 CD  
3 1 Y 0 A GLU 31 ? OE1 ? A GLU 34 OE1 
4 1 Y 0 A GLU 31 ? OE2 ? A GLU 34 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0258 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? xia2        ? ? ? 0.3.6.3  2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.22     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GGU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.050 
_cell.length_a_esd                 ? 
_cell.length_b                     40.240 
_cell.length_b_esd                 ? 
_cell.length_c                     110.940 
_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                         9GGU 
_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                   9GGU 
_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             2.11 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.68 
_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               0.327 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.2 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '25% PEG 8000, 300 mM LiCl, 100 mM bis-tris propane' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2014-07-02 
_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   0.87 
_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        0.87 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          15.103 
_reflns.entry_id                                       9GGU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.600 
_reflns.d_resolution_low                               26.170 
_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                                     22384 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.300 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.300 
_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                                0.064 
_reflns.pdbx_Rpim_I_all                                0.030 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       96255 
_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                              0.049 
_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 
1.600 1.640  ? 2.400  ? ? ? ? 1627 ? ? ? ? ? ? ? ? ? ? ? 4.300 ? ? ? 0.682 0.317 ? 1 1 ? ? ? 99.700 ? 0.539 ? ? ? ? ? ? ? ? ? 
7.160 26.170 ? 46.900 ? ? ? ? 278  ? ? ? ? ? ? ? ? ? ? ? 3.900 ? ? ? 0.031 0.015 ? 2 1 ? ? ? 93.200 ? 0.023 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.4000 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            -0.1700 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -0.2300 
_refine.B_iso_max                                60.510 
_refine.B_iso_mean                               22.2620 
_refine.B_iso_min                                10.420 
_refine.correlation_coeff_Fo_to_Fc               0.9640 
_refine.correlation_coeff_Fo_to_Fc_free          0.9540 
_refine.details                                  'U VALUES      : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GGU 
_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                            1.6000 
_refine.ls_d_res_low                             26.1700 
_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                     21228 
_refine.ls_number_reflns_R_free                  1118 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.6100 
_refine.ls_percent_reflns_R_free                 5.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1765 
_refine.ls_R_factor_R_free                       0.2077 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1750 
_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                       0.0920 
_refine.pdbx_overall_ESU_R_Free                  0.0920 
_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                             4.0950 
_refine.overall_SU_ML                            0.0630 
_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                       1.6000 
_refine_hist.d_res_low                        26.1700 
_refine_hist.number_atoms_solvent             119 
_refine_hist.number_atoms_total               1535 
_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           26.49 
_refine_hist.pdbx_B_iso_mean_solvent          31.60 
_refine_hist.pdbx_number_atoms_protein        1362 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.018  0.013  1463 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.035  0.018  1333 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 2.059  1.711  1985 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 2.366  1.615  3086 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 4.707  5.000  174  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 33.144 21.765 85   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.258 15.000 260  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 20.056 15.000 13   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.123  0.200  190  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  1633 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  320  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 1.362  1.407  687  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 1.363  1.406  686  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 2.007  2.108  861  ? r_mcangle_it           ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.6000 
_refine_ls_shell.d_res_low                        1.6410 
_refine_ls_shell.number_reflns_all                1621 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             100 
_refine_ls_shell.number_reflns_R_work             1521 
_refine_ls_shell.percent_reflns_obs               99.5700 
_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                  0.2530 
_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                  0.2650 
# 
_struct.entry_id                     9GGU 
_struct.title                        'Human KRas4A (GDP) in complex with compound 9' 
_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        9GGU 
_struct_keywords.text            'RAS, GTPase, inhibitor, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RASK_HUMAN 
_struct_ref.pdbx_db_accession          P01116 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLV
REIRQYRLK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9GGU 
_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 9GGU GLY A 1   ? UNP P01116 ?   ?   'expression tag'      -2  1 
1 9GGU GLY A 2   ? UNP P01116 ?   ?   'expression tag'      -1  2 
1 9GGU SER A 3   ? UNP P01116 ?   ?   'expression tag'      0   3 
1 9GGU 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)' 1590 ? 
1 MORE         -19  ? 
1 'SSA (A^2)'  8180 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 18  ? ASN A 29  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2 AA2 SER A 68  ? GLY A 78  ? SER A 65  GLY A 75  1 ? 11 
HELX_P HELX_P3 AA3 ASN A 89  ? ASP A 95  ? ASN A 86  ASP A 92  1 ? 7  
HELX_P HELX_P4 AA4 ASP A 95  ? ASP A 108 ? ASP A 92  ASP A 105 1 ? 14 
HELX_P HELX_P5 AA5 ASP A 129 ? GLY A 141 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P6 AA6 ARG A 154 ? ARG A 170 ? ARG A 151 ARG A 167 1 ? 17 
# 
_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 ? ? ? ? ? ? ? 2.060 ? ? 
metalc2 metalc ? ? B GDP .  O1B ? ? ? 1_555 C MG  . MG ? ? A GDP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc3 metalc ? ? C MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 306 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc4 metalc ? ? C MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 311 1_555 ? ? ? ? ? ? ? 2.133 ? ? 
metalc5 metalc ? ? C MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 319 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
metalc6 metalc ? ? C MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 349 1_555 ? ? ? ? ? ? ? 2.008 ? ? 
# 
_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 93.5  ? 
2  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 306 ? 1_555 81.4  ? 
3  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 306 ? 1_555 94.7  ? 
4  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 311 ? 1_555 93.9  ? 
5  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 311 ? 1_555 84.5  ? 
6  O   ? F HOH .  ? A HOH 306 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 311 ? 1_555 175.2 ? 
7  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 319 ? 1_555 90.9  ? 
8  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 319 ? 1_555 171.1 ? 
9  O   ? F HOH .  ? A HOH 306 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 319 ? 1_555 93.6  ? 
10 O   ? F HOH .  ? A HOH 311 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 319 ? 1_555 87.4  ? 
11 OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 349 ? 1_555 172.4 ? 
12 O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 349 ? 1_555 89.3  ? 
13 O   ? F HOH .  ? A HOH 306 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 349 ? 1_555 91.4  ? 
14 O   ? F HOH .  ? A HOH 311 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 349 ? 1_555 93.3  ? 
15 O   ? F HOH .  ? A HOH 319 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH . ? A HOH 349 ? 1_555 87.3  ? 
# 
_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 59  ? O LEU A 56  N LEU A 9   ? N LEU A 6   
AA1 3 4 N VAL A 10  ? N VAL A 7   O LEU A 82  ? O LEU A 79  
AA1 4 5 N 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                   9GGU 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             153 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE1 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             153 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.180 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            -0.072 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              92 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              92 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              92 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                123.73 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            5.43 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 31 ? ? -152.64 69.91  
2 1 ALA A 59 ? ? -108.10 -83.84 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -1.1065 
_pdbx_refine_tls.origin_y         17.9626 
_pdbx_refine_tls.origin_z         11.8148 
_pdbx_refine_tls.T[1][1]          0.0175 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0012 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0017 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0097 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0057 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0061 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.4806 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0791 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.1844 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.6867 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.2059 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.1709 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0258 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1006 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0612 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0177 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0019 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0417 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1056 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0249 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0238 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     204 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
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 
A1IMC NAP    N  Y N 1   
A1IMC CAO    C  Y N 2   
A1IMC CAN    C  Y N 3   
A1IMC CAM    C  Y N 4   
A1IMC CAL    C  Y N 5   
A1IMC CAK    C  Y N 6   
A1IMC CLAJ   CL N N 7   
A1IMC CAS    C  Y N 8   
A1IMC SAR    S  Y N 9   
A1IMC CAQ    C  Y N 10  
A1IMC NAT    N  N N 11  
A1IMC SAB    S  N N 12  
A1IMC OAA    O  N N 13  
A1IMC OAU    O  N N 14  
A1IMC CAC    C  Y N 15  
A1IMC CAH    C  Y N 16  
A1IMC CAG    C  Y N 17  
A1IMC CAF    C  Y N 18  
A1IMC CAE    C  Y N 19  
A1IMC CAD    C  Y N 20  
A1IMC OAI    O  N N 21  
A1IMC H1     H  N N 22  
A1IMC H2     H  N N 23  
A1IMC H3     H  N N 24  
A1IMC H4     H  N N 25  
A1IMC H5     H  N N 26  
A1IMC H6     H  N N 27  
A1IMC H7     H  N N 28  
A1IMC H8     H  N N 29  
A1IMC H9     H  N N 30  
ALA   N      N  N N 31  
ALA   CA     C  N S 32  
ALA   C      C  N N 33  
ALA   O      O  N N 34  
ALA   CB     C  N N 35  
ALA   OXT    O  N N 36  
ALA   H      H  N N 37  
ALA   H2     H  N N 38  
ALA   HA     H  N N 39  
ALA   HB1    H  N N 40  
ALA   HB2    H  N N 41  
ALA   HB3    H  N N 42  
ALA   HXT    H  N N 43  
ARG   N      N  N N 44  
ARG   CA     C  N S 45  
ARG   C      C  N N 46  
ARG   O      O  N N 47  
ARG   CB     C  N N 48  
ARG   CG     C  N N 49  
ARG   CD     C  N N 50  
ARG   NE     N  N N 51  
ARG   CZ     C  N N 52  
ARG   NH1    N  N N 53  
ARG   NH2    N  N N 54  
ARG   OXT    O  N N 55  
ARG   H      H  N N 56  
ARG   H2     H  N N 57  
ARG   HA     H  N N 58  
ARG   HB2    H  N N 59  
ARG   HB3    H  N N 60  
ARG   HG2    H  N N 61  
ARG   HG3    H  N N 62  
ARG   HD2    H  N N 63  
ARG   HD3    H  N N 64  
ARG   HE     H  N N 65  
ARG   HH11   H  N N 66  
ARG   HH12   H  N N 67  
ARG   HH21   H  N N 68  
ARG   HH22   H  N N 69  
ARG   HXT    H  N N 70  
ASN   N      N  N N 71  
ASN   CA     C  N S 72  
ASN   C      C  N N 73  
ASN   O      O  N N 74  
ASN   CB     C  N N 75  
ASN   CG     C  N N 76  
ASN   OD1    O  N N 77  
ASN   ND2    N  N N 78  
ASN   OXT    O  N N 79  
ASN   H      H  N N 80  
ASN   H2     H  N N 81  
ASN   HA     H  N N 82  
ASN   HB2    H  N N 83  
ASN   HB3    H  N N 84  
ASN   HD21   H  N N 85  
ASN   HD22   H  N N 86  
ASN   HXT    H  N N 87  
ASP   N      N  N N 88  
ASP   CA     C  N S 89  
ASP   C      C  N N 90  
ASP   O      O  N N 91  
ASP   CB     C  N N 92  
ASP   CG     C  N N 93  
ASP   OD1    O  N N 94  
ASP   OD2    O  N N 95  
ASP   OXT    O  N N 96  
ASP   H      H  N N 97  
ASP   H2     H  N N 98  
ASP   HA     H  N N 99  
ASP   HB2    H  N N 100 
ASP   HB3    H  N N 101 
ASP   HD2    H  N N 102 
ASP   HXT    H  N N 103 
CYS   N      N  N N 104 
CYS   CA     C  N R 105 
CYS   C      C  N N 106 
CYS   O      O  N N 107 
CYS   CB     C  N N 108 
CYS   SG     S  N N 109 
CYS   OXT    O  N N 110 
CYS   H      H  N N 111 
CYS   H2     H  N N 112 
CYS   HA     H  N N 113 
CYS   HB2    H  N N 114 
CYS   HB3    H  N N 115 
CYS   HG     H  N N 116 
CYS   HXT    H  N N 117 
EDO   C1     C  N N 118 
EDO   O1     O  N N 119 
EDO   C2     C  N N 120 
EDO   O2     O  N N 121 
EDO   H11    H  N N 122 
EDO   H12    H  N N 123 
EDO   HO1    H  N N 124 
EDO   H21    H  N N 125 
EDO   H22    H  N N 126 
EDO   HO2    H  N N 127 
GDP   PB     P  N N 128 
GDP   O1B    O  N N 129 
GDP   O2B    O  N N 130 
GDP   O3B    O  N N 131 
GDP   O3A    O  N N 132 
GDP   PA     P  N N 133 
GDP   O1A    O  N N 134 
GDP   O2A    O  N N 135 
GDP   "O5'"  O  N N 136 
GDP   "C5'"  C  N N 137 
GDP   "C4'"  C  N R 138 
GDP   "O4'"  O  N N 139 
GDP   "C3'"  C  N S 140 
GDP   "O3'"  O  N N 141 
GDP   "C2'"  C  N R 142 
GDP   "O2'"  O  N N 143 
GDP   "C1'"  C  N R 144 
GDP   N9     N  Y N 145 
GDP   C8     C  Y N 146 
GDP   N7     N  Y N 147 
GDP   C5     C  Y N 148 
GDP   C6     C  N N 149 
GDP   O6     O  N N 150 
GDP   N1     N  N N 151 
GDP   C2     C  N N 152 
GDP   N2     N  N N 153 
GDP   N3     N  N N 154 
GDP   C4     C  Y N 155 
GDP   HOB2   H  N N 156 
GDP   HOB3   H  N N 157 
GDP   HOA2   H  N N 158 
GDP   "H5'"  H  N N 159 
GDP   "H5''" H  N N 160 
GDP   "H4'"  H  N N 161 
GDP   "H3'"  H  N N 162 
GDP   "HO3'" H  N N 163 
GDP   "H2'"  H  N N 164 
GDP   "HO2'" H  N N 165 
GDP   "H1'"  H  N N 166 
GDP   H8     H  N N 167 
GDP   HN1    H  N N 168 
GDP   HN21   H  N N 169 
GDP   HN22   H  N N 170 
GLN   N      N  N N 171 
GLN   CA     C  N S 172 
GLN   C      C  N N 173 
GLN   O      O  N N 174 
GLN   CB     C  N N 175 
GLN   CG     C  N N 176 
GLN   CD     C  N N 177 
GLN   OE1    O  N N 178 
GLN   NE2    N  N N 179 
GLN   OXT    O  N N 180 
GLN   H      H  N N 181 
GLN   H2     H  N N 182 
GLN   HA     H  N N 183 
GLN   HB2    H  N N 184 
GLN   HB3    H  N N 185 
GLN   HG2    H  N N 186 
GLN   HG3    H  N N 187 
GLN   HE21   H  N N 188 
GLN   HE22   H  N N 189 
GLN   HXT    H  N N 190 
GLU   N      N  N N 191 
GLU   CA     C  N S 192 
GLU   C      C  N N 193 
GLU   O      O  N N 194 
GLU   CB     C  N N 195 
GLU   CG     C  N N 196 
GLU   CD     C  N N 197 
GLU   OE1    O  N N 198 
GLU   OE2    O  N N 199 
GLU   OXT    O  N N 200 
GLU   H      H  N N 201 
GLU   H2     H  N N 202 
GLU   HA     H  N N 203 
GLU   HB2    H  N N 204 
GLU   HB3    H  N N 205 
GLU   HG2    H  N N 206 
GLU   HG3    H  N N 207 
GLU   HE2    H  N N 208 
GLU   HXT    H  N N 209 
GLY   N      N  N N 210 
GLY   CA     C  N N 211 
GLY   C      C  N N 212 
GLY   O      O  N N 213 
GLY   OXT    O  N N 214 
GLY   H      H  N N 215 
GLY   H2     H  N N 216 
GLY   HA2    H  N N 217 
GLY   HA3    H  N N 218 
GLY   HXT    H  N N 219 
HIS   N      N  N N 220 
HIS   CA     C  N S 221 
HIS   C      C  N N 222 
HIS   O      O  N N 223 
HIS   CB     C  N N 224 
HIS   CG     C  Y N 225 
HIS   ND1    N  Y N 226 
HIS   CD2    C  Y N 227 
HIS   CE1    C  Y N 228 
HIS   NE2    N  Y N 229 
HIS   OXT    O  N N 230 
HIS   H      H  N N 231 
HIS   H2     H  N N 232 
HIS   HA     H  N N 233 
HIS   HB2    H  N N 234 
HIS   HB3    H  N N 235 
HIS   HD1    H  N N 236 
HIS   HD2    H  N N 237 
HIS   HE1    H  N N 238 
HIS   HE2    H  N N 239 
HIS   HXT    H  N N 240 
HOH   O      O  N N 241 
HOH   H1     H  N N 242 
HOH   H2     H  N N 243 
ILE   N      N  N N 244 
ILE   CA     C  N S 245 
ILE   C      C  N N 246 
ILE   O      O  N N 247 
ILE   CB     C  N S 248 
ILE   CG1    C  N N 249 
ILE   CG2    C  N N 250 
ILE   CD1    C  N N 251 
ILE   OXT    O  N N 252 
ILE   H      H  N N 253 
ILE   H2     H  N N 254 
ILE   HA     H  N N 255 
ILE   HB     H  N N 256 
ILE   HG12   H  N N 257 
ILE   HG13   H  N N 258 
ILE   HG21   H  N N 259 
ILE   HG22   H  N N 260 
ILE   HG23   H  N N 261 
ILE   HD11   H  N N 262 
ILE   HD12   H  N N 263 
ILE   HD13   H  N N 264 
ILE   HXT    H  N N 265 
LEU   N      N  N N 266 
LEU   CA     C  N S 267 
LEU   C      C  N N 268 
LEU   O      O  N N 269 
LEU   CB     C  N N 270 
LEU   CG     C  N N 271 
LEU   CD1    C  N N 272 
LEU   CD2    C  N N 273 
LEU   OXT    O  N N 274 
LEU   H      H  N N 275 
LEU   H2     H  N N 276 
LEU   HA     H  N N 277 
LEU   HB2    H  N N 278 
LEU   HB3    H  N N 279 
LEU   HG     H  N N 280 
LEU   HD11   H  N N 281 
LEU   HD12   H  N N 282 
LEU   HD13   H  N N 283 
LEU   HD21   H  N N 284 
LEU   HD22   H  N N 285 
LEU   HD23   H  N N 286 
LEU   HXT    H  N N 287 
LYS   N      N  N N 288 
LYS   CA     C  N S 289 
LYS   C      C  N N 290 
LYS   O      O  N N 291 
LYS   CB     C  N N 292 
LYS   CG     C  N N 293 
LYS   CD     C  N N 294 
LYS   CE     C  N N 295 
LYS   NZ     N  N N 296 
LYS   OXT    O  N N 297 
LYS   H      H  N N 298 
LYS   H2     H  N N 299 
LYS   HA     H  N N 300 
LYS   HB2    H  N N 301 
LYS   HB3    H  N N 302 
LYS   HG2    H  N N 303 
LYS   HG3    H  N N 304 
LYS   HD2    H  N N 305 
LYS   HD3    H  N N 306 
LYS   HE2    H  N N 307 
LYS   HE3    H  N N 308 
LYS   HZ1    H  N N 309 
LYS   HZ2    H  N N 310 
LYS   HZ3    H  N N 311 
LYS   HXT    H  N N 312 
MET   N      N  N N 313 
MET   CA     C  N S 314 
MET   C      C  N N 315 
MET   O      O  N N 316 
MET   CB     C  N N 317 
MET   CG     C  N N 318 
MET   SD     S  N N 319 
MET   CE     C  N N 320 
MET   OXT    O  N N 321 
MET   H      H  N N 322 
MET   H2     H  N N 323 
MET   HA     H  N N 324 
MET   HB2    H  N N 325 
MET   HB3    H  N N 326 
MET   HG2    H  N N 327 
MET   HG3    H  N N 328 
MET   HE1    H  N N 329 
MET   HE2    H  N N 330 
MET   HE3    H  N N 331 
MET   HXT    H  N N 332 
MG    MG     MG N N 333 
PHE   N      N  N N 334 
PHE   CA     C  N S 335 
PHE   C      C  N N 336 
PHE   O      O  N N 337 
PHE   CB     C  N N 338 
PHE   CG     C  Y N 339 
PHE   CD1    C  Y N 340 
PHE   CD2    C  Y N 341 
PHE   CE1    C  Y N 342 
PHE   CE2    C  Y N 343 
PHE   CZ     C  Y N 344 
PHE   OXT    O  N N 345 
PHE   H      H  N N 346 
PHE   H2     H  N N 347 
PHE   HA     H  N N 348 
PHE   HB2    H  N N 349 
PHE   HB3    H  N N 350 
PHE   HD1    H  N N 351 
PHE   HD2    H  N N 352 
PHE   HE1    H  N N 353 
PHE   HE2    H  N N 354 
PHE   HZ     H  N N 355 
PHE   HXT    H  N N 356 
PRO   N      N  N N 357 
PRO   CA     C  N S 358 
PRO   C      C  N N 359 
PRO   O      O  N N 360 
PRO   CB     C  N N 361 
PRO   CG     C  N N 362 
PRO   CD     C  N N 363 
PRO   OXT    O  N N 364 
PRO   H      H  N N 365 
PRO   HA     H  N N 366 
PRO   HB2    H  N N 367 
PRO   HB3    H  N N 368 
PRO   HG2    H  N N 369 
PRO   HG3    H  N N 370 
PRO   HD2    H  N N 371 
PRO   HD3    H  N N 372 
PRO   HXT    H  N N 373 
SER   N      N  N N 374 
SER   CA     C  N S 375 
SER   C      C  N N 376 
SER   O      O  N N 377 
SER   CB     C  N N 378 
SER   OG     O  N N 379 
SER   OXT    O  N N 380 
SER   H      H  N N 381 
SER   H2     H  N N 382 
SER   HA     H  N N 383 
SER   HB2    H  N N 384 
SER   HB3    H  N N 385 
SER   HG     H  N N 386 
SER   HXT    H  N N 387 
THR   N      N  N N 388 
THR   CA     C  N S 389 
THR   C      C  N N 390 
THR   O      O  N N 391 
THR   CB     C  N R 392 
THR   OG1    O  N N 393 
THR   CG2    C  N N 394 
THR   OXT    O  N N 395 
THR   H      H  N N 396 
THR   H2     H  N N 397 
THR   HA     H  N N 398 
THR   HB     H  N N 399 
THR   HG1    H  N N 400 
THR   HG21   H  N N 401 
THR   HG22   H  N N 402 
THR   HG23   H  N N 403 
THR   HXT    H  N N 404 
TYR   N      N  N N 405 
TYR   CA     C  N S 406 
TYR   C      C  N N 407 
TYR   O      O  N N 408 
TYR   CB     C  N N 409 
TYR   CG     C  Y N 410 
TYR   CD1    C  Y N 411 
TYR   CD2    C  Y N 412 
TYR   CE1    C  Y N 413 
TYR   CE2    C  Y N 414 
TYR   CZ     C  Y N 415 
TYR   OH     O  N N 416 
TYR   OXT    O  N N 417 
TYR   H      H  N N 418 
TYR   H2     H  N N 419 
TYR   HA     H  N N 420 
TYR   HB2    H  N N 421 
TYR   HB3    H  N N 422 
TYR   HD1    H  N N 423 
TYR   HD2    H  N N 424 
TYR   HE1    H  N N 425 
TYR   HE2    H  N N 426 
TYR   HH     H  N N 427 
TYR   HXT    H  N N 428 
VAL   N      N  N N 429 
VAL   CA     C  N S 430 
VAL   C      C  N N 431 
VAL   O      O  N N 432 
VAL   CB     C  N N 433 
VAL   CG1    C  N N 434 
VAL   CG2    C  N N 435 
VAL   OXT    O  N N 436 
VAL   H      H  N N 437 
VAL   H2     H  N N 438 
VAL   HA     H  N N 439 
VAL   HB     H  N N 440 
VAL   HG11   H  N N 441 
VAL   HG12   H  N N 442 
VAL   HG13   H  N N 443 
VAL   HG21   H  N N 444 
VAL   HG22   H  N N 445 
VAL   HG23   H  N N 446 
VAL   HXT    H  N N 447 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1IMC OAI   CAD    sing N N 1   
A1IMC CAE   CAD    doub Y N 2   
A1IMC CAE   CAF    sing Y N 3   
A1IMC CAD   CAC    sing Y N 4   
A1IMC CAF   CAG    doub Y N 5   
A1IMC OAU   SAB    doub N N 6   
A1IMC NAT   SAB    sing N N 7   
A1IMC NAT   CAQ    sing N N 8   
A1IMC CAC   SAB    sing N N 9   
A1IMC CAC   CAH    doub Y N 10  
A1IMC NAP   CAQ    doub Y N 11  
A1IMC NAP   CAO    sing Y N 12  
A1IMC SAB   OAA    doub N N 13  
A1IMC CAG   CAH    sing Y N 14  
A1IMC CAQ   SAR    sing Y N 15  
A1IMC CAN   CAO    sing Y N 16  
A1IMC CAN   CAM    doub Y N 17  
A1IMC CAO   CAS    doub Y N 18  
A1IMC CAM   CAL    sing Y N 19  
A1IMC SAR   CAS    sing Y N 20  
A1IMC CAS   CAK    sing Y N 21  
A1IMC CAL   CAK    doub Y N 22  
A1IMC CAK   CLAJ   sing N N 23  
A1IMC CAN   H1     sing N N 24  
A1IMC CAM   H2     sing N N 25  
A1IMC CAL   H3     sing N N 26  
A1IMC NAT   H4     sing N N 27  
A1IMC CAH   H5     sing N N 28  
A1IMC CAG   H6     sing N N 29  
A1IMC CAF   H7     sing N N 30  
A1IMC CAE   H8     sing N N 31  
A1IMC OAI   H9     sing N N 32  
ALA   N     CA     sing N N 33  
ALA   N     H      sing N N 34  
ALA   N     H2     sing N N 35  
ALA   CA    C      sing N N 36  
ALA   CA    CB     sing N N 37  
ALA   CA    HA     sing N N 38  
ALA   C     O      doub N N 39  
ALA   C     OXT    sing N N 40  
ALA   CB    HB1    sing N N 41  
ALA   CB    HB2    sing N N 42  
ALA   CB    HB3    sing N N 43  
ALA   OXT   HXT    sing N N 44  
ARG   N     CA     sing N N 45  
ARG   N     H      sing N N 46  
ARG   N     H2     sing N N 47  
ARG   CA    C      sing N N 48  
ARG   CA    CB     sing N N 49  
ARG   CA    HA     sing N N 50  
ARG   C     O      doub N N 51  
ARG   C     OXT    sing N N 52  
ARG   CB    CG     sing N N 53  
ARG   CB    HB2    sing N N 54  
ARG   CB    HB3    sing N N 55  
ARG   CG    CD     sing N N 56  
ARG   CG    HG2    sing N N 57  
ARG   CG    HG3    sing N N 58  
ARG   CD    NE     sing N N 59  
ARG   CD    HD2    sing N N 60  
ARG   CD    HD3    sing N N 61  
ARG   NE    CZ     sing N N 62  
ARG   NE    HE     sing N N 63  
ARG   CZ    NH1    sing N N 64  
ARG   CZ    NH2    doub N N 65  
ARG   NH1   HH11   sing N N 66  
ARG   NH1   HH12   sing N N 67  
ARG   NH2   HH21   sing N N 68  
ARG   NH2   HH22   sing N N 69  
ARG   OXT   HXT    sing N N 70  
ASN   N     CA     sing N N 71  
ASN   N     H      sing N N 72  
ASN   N     H2     sing N N 73  
ASN   CA    C      sing N N 74  
ASN   CA    CB     sing N N 75  
ASN   CA    HA     sing N N 76  
ASN   C     O      doub N N 77  
ASN   C     OXT    sing N N 78  
ASN   CB    CG     sing N N 79  
ASN   CB    HB2    sing N N 80  
ASN   CB    HB3    sing N N 81  
ASN   CG    OD1    doub N N 82  
ASN   CG    ND2    sing N N 83  
ASN   ND2   HD21   sing N N 84  
ASN   ND2   HD22   sing N N 85  
ASN   OXT   HXT    sing N N 86  
ASP   N     CA     sing N N 87  
ASP   N     H      sing N N 88  
ASP   N     H2     sing N N 89  
ASP   CA    C      sing N N 90  
ASP   CA    CB     sing N N 91  
ASP   CA    HA     sing N N 92  
ASP   C     O      doub N N 93  
ASP   C     OXT    sing N N 94  
ASP   CB    CG     sing N N 95  
ASP   CB    HB2    sing N N 96  
ASP   CB    HB3    sing N N 97  
ASP   CG    OD1    doub N N 98  
ASP   CG    OD2    sing N N 99  
ASP   OD2   HD2    sing N N 100 
ASP   OXT   HXT    sing N N 101 
CYS   N     CA     sing N N 102 
CYS   N     H      sing N N 103 
CYS   N     H2     sing N N 104 
CYS   CA    C      sing N N 105 
CYS   CA    CB     sing N N 106 
CYS   CA    HA     sing N N 107 
CYS   C     O      doub N N 108 
CYS   C     OXT    sing N N 109 
CYS   CB    SG     sing N N 110 
CYS   CB    HB2    sing N N 111 
CYS   CB    HB3    sing N N 112 
CYS   SG    HG     sing N N 113 
CYS   OXT   HXT    sing N N 114 
EDO   C1    O1     sing N N 115 
EDO   C1    C2     sing N N 116 
EDO   C1    H11    sing N N 117 
EDO   C1    H12    sing N N 118 
EDO   O1    HO1    sing N N 119 
EDO   C2    O2     sing N N 120 
EDO   C2    H21    sing N N 121 
EDO   C2    H22    sing N N 122 
EDO   O2    HO2    sing N N 123 
GDP   PB    O1B    doub N N 124 
GDP   PB    O2B    sing N N 125 
GDP   PB    O3B    sing N N 126 
GDP   PB    O3A    sing N N 127 
GDP   O2B   HOB2   sing N N 128 
GDP   O3B   HOB3   sing N N 129 
GDP   O3A   PA     sing N N 130 
GDP   PA    O1A    doub N N 131 
GDP   PA    O2A    sing N N 132 
GDP   PA    "O5'"  sing N N 133 
GDP   O2A   HOA2   sing N N 134 
GDP   "O5'" "C5'"  sing N N 135 
GDP   "C5'" "C4'"  sing N N 136 
GDP   "C5'" "H5'"  sing N N 137 
GDP   "C5'" "H5''" sing N N 138 
GDP   "C4'" "O4'"  sing N N 139 
GDP   "C4'" "C3'"  sing N N 140 
GDP   "C4'" "H4'"  sing N N 141 
GDP   "O4'" "C1'"  sing N N 142 
GDP   "C3'" "O3'"  sing N N 143 
GDP   "C3'" "C2'"  sing N N 144 
GDP   "C3'" "H3'"  sing N N 145 
GDP   "O3'" "HO3'" sing N N 146 
GDP   "C2'" "O2'"  sing N N 147 
GDP   "C2'" "C1'"  sing N N 148 
GDP   "C2'" "H2'"  sing N N 149 
GDP   "O2'" "HO2'" sing N N 150 
GDP   "C1'" N9     sing N N 151 
GDP   "C1'" "H1'"  sing N N 152 
GDP   N9    C8     sing Y N 153 
GDP   N9    C4     sing Y N 154 
GDP   C8    N7     doub Y N 155 
GDP   C8    H8     sing N N 156 
GDP   N7    C5     sing Y N 157 
GDP   C5    C6     sing N N 158 
GDP   C5    C4     doub Y N 159 
GDP   C6    O6     doub N N 160 
GDP   C6    N1     sing N N 161 
GDP   N1    C2     sing N N 162 
GDP   N1    HN1    sing N N 163 
GDP   C2    N2     sing N N 164 
GDP   C2    N3     doub N N 165 
GDP   N2    HN21   sing N N 166 
GDP   N2    HN22   sing N N 167 
GDP   N3    C4     sing N N 168 
GLN   N     CA     sing N N 169 
GLN   N     H      sing N N 170 
GLN   N     H2     sing N N 171 
GLN   CA    C      sing N N 172 
GLN   CA    CB     sing N N 173 
GLN   CA    HA     sing N N 174 
GLN   C     O      doub N N 175 
GLN   C     OXT    sing N N 176 
GLN   CB    CG     sing N N 177 
GLN   CB    HB2    sing N N 178 
GLN   CB    HB3    sing N N 179 
GLN   CG    CD     sing N N 180 
GLN   CG    HG2    sing N N 181 
GLN   CG    HG3    sing N N 182 
GLN   CD    OE1    doub N N 183 
GLN   CD    NE2    sing N N 184 
GLN   NE2   HE21   sing N N 185 
GLN   NE2   HE22   sing N N 186 
GLN   OXT   HXT    sing N N 187 
GLU   N     CA     sing N N 188 
GLU   N     H      sing N N 189 
GLU   N     H2     sing N N 190 
GLU   CA    C      sing N N 191 
GLU   CA    CB     sing N N 192 
GLU   CA    HA     sing N N 193 
GLU   C     O      doub N N 194 
GLU   C     OXT    sing N N 195 
GLU   CB    CG     sing N N 196 
GLU   CB    HB2    sing N N 197 
GLU   CB    HB3    sing N N 198 
GLU   CG    CD     sing N N 199 
GLU   CG    HG2    sing N N 200 
GLU   CG    HG3    sing N N 201 
GLU   CD    OE1    doub N N 202 
GLU   CD    OE2    sing N N 203 
GLU   OE2   HE2    sing N N 204 
GLU   OXT   HXT    sing N N 205 
GLY   N     CA     sing N N 206 
GLY   N     H      sing N N 207 
GLY   N     H2     sing N N 208 
GLY   CA    C      sing N N 209 
GLY   CA    HA2    sing N N 210 
GLY   CA    HA3    sing N N 211 
GLY   C     O      doub N N 212 
GLY   C     OXT    sing N N 213 
GLY   OXT   HXT    sing N N 214 
HIS   N     CA     sing N N 215 
HIS   N     H      sing N N 216 
HIS   N     H2     sing N N 217 
HIS   CA    C      sing N N 218 
HIS   CA    CB     sing N N 219 
HIS   CA    HA     sing N N 220 
HIS   C     O      doub N N 221 
HIS   C     OXT    sing N N 222 
HIS   CB    CG     sing N N 223 
HIS   CB    HB2    sing N N 224 
HIS   CB    HB3    sing N N 225 
HIS   CG    ND1    sing Y N 226 
HIS   CG    CD2    doub Y N 227 
HIS   ND1   CE1    doub Y N 228 
HIS   ND1   HD1    sing N N 229 
HIS   CD2   NE2    sing Y N 230 
HIS   CD2   HD2    sing N N 231 
HIS   CE1   NE2    sing Y N 232 
HIS   CE1   HE1    sing N N 233 
HIS   NE2   HE2    sing N N 234 
HIS   OXT   HXT    sing N N 235 
HOH   O     H1     sing N N 236 
HOH   O     H2     sing N N 237 
ILE   N     CA     sing N N 238 
ILE   N     H      sing N N 239 
ILE   N     H2     sing N N 240 
ILE   CA    C      sing N N 241 
ILE   CA    CB     sing N N 242 
ILE   CA    HA     sing N N 243 
ILE   C     O      doub N N 244 
ILE   C     OXT    sing N N 245 
ILE   CB    CG1    sing N N 246 
ILE   CB    CG2    sing N N 247 
ILE   CB    HB     sing N N 248 
ILE   CG1   CD1    sing N N 249 
ILE   CG1   HG12   sing N N 250 
ILE   CG1   HG13   sing N N 251 
ILE   CG2   HG21   sing N N 252 
ILE   CG2   HG22   sing N N 253 
ILE   CG2   HG23   sing N N 254 
ILE   CD1   HD11   sing N N 255 
ILE   CD1   HD12   sing N N 256 
ILE   CD1   HD13   sing N N 257 
ILE   OXT   HXT    sing N N 258 
LEU   N     CA     sing N N 259 
LEU   N     H      sing N N 260 
LEU   N     H2     sing N N 261 
LEU   CA    C      sing N N 262 
LEU   CA    CB     sing N N 263 
LEU   CA    HA     sing N N 264 
LEU   C     O      doub N N 265 
LEU   C     OXT    sing N N 266 
LEU   CB    CG     sing N N 267 
LEU   CB    HB2    sing N N 268 
LEU   CB    HB3    sing N N 269 
LEU   CG    CD1    sing N N 270 
LEU   CG    CD2    sing N N 271 
LEU   CG    HG     sing N N 272 
LEU   CD1   HD11   sing N N 273 
LEU   CD1   HD12   sing N N 274 
LEU   CD1   HD13   sing N N 275 
LEU   CD2   HD21   sing N N 276 
LEU   CD2   HD22   sing N N 277 
LEU   CD2   HD23   sing N N 278 
LEU   OXT   HXT    sing N N 279 
LYS   N     CA     sing N N 280 
LYS   N     H      sing N N 281 
LYS   N     H2     sing N N 282 
LYS   CA    C      sing N N 283 
LYS   CA    CB     sing N N 284 
LYS   CA    HA     sing N N 285 
LYS   C     O      doub N N 286 
LYS   C     OXT    sing N N 287 
LYS   CB    CG     sing N N 288 
LYS   CB    HB2    sing N N 289 
LYS   CB    HB3    sing N N 290 
LYS   CG    CD     sing N N 291 
LYS   CG    HG2    sing N N 292 
LYS   CG    HG3    sing N N 293 
LYS   CD    CE     sing N N 294 
LYS   CD    HD2    sing N N 295 
LYS   CD    HD3    sing N N 296 
LYS   CE    NZ     sing N N 297 
LYS   CE    HE2    sing N N 298 
LYS   CE    HE3    sing N N 299 
LYS   NZ    HZ1    sing N N 300 
LYS   NZ    HZ2    sing N N 301 
LYS   NZ    HZ3    sing N N 302 
LYS   OXT   HXT    sing N N 303 
MET   N     CA     sing N N 304 
MET   N     H      sing N N 305 
MET   N     H2     sing N N 306 
MET   CA    C      sing N N 307 
MET   CA    CB     sing N N 308 
MET   CA    HA     sing N N 309 
MET   C     O      doub N N 310 
MET   C     OXT    sing N N 311 
MET   CB    CG     sing N N 312 
MET   CB    HB2    sing N N 313 
MET   CB    HB3    sing N N 314 
MET   CG    SD     sing N N 315 
MET   CG    HG2    sing N N 316 
MET   CG    HG3    sing N N 317 
MET   SD    CE     sing N N 318 
MET   CE    HE1    sing N N 319 
MET   CE    HE2    sing N N 320 
MET   CE    HE3    sing N N 321 
MET   OXT   HXT    sing N N 322 
PHE   N     CA     sing N N 323 
PHE   N     H      sing N N 324 
PHE   N     H2     sing N N 325 
PHE   CA    C      sing N N 326 
PHE   CA    CB     sing N N 327 
PHE   CA    HA     sing N N 328 
PHE   C     O      doub N N 329 
PHE   C     OXT    sing N N 330 
PHE   CB    CG     sing N N 331 
PHE   CB    HB2    sing N N 332 
PHE   CB    HB3    sing N N 333 
PHE   CG    CD1    doub Y N 334 
PHE   CG    CD2    sing Y N 335 
PHE   CD1   CE1    sing Y N 336 
PHE   CD1   HD1    sing N N 337 
PHE   CD2   CE2    doub Y N 338 
PHE   CD2   HD2    sing N N 339 
PHE   CE1   CZ     doub Y N 340 
PHE   CE1   HE1    sing N N 341 
PHE   CE2   CZ     sing Y N 342 
PHE   CE2   HE2    sing N N 343 
PHE   CZ    HZ     sing N N 344 
PHE   OXT   HXT    sing N N 345 
PRO   N     CA     sing N N 346 
PRO   N     CD     sing N N 347 
PRO   N     H      sing N N 348 
PRO   CA    C      sing N N 349 
PRO   CA    CB     sing N N 350 
PRO   CA    HA     sing N N 351 
PRO   C     O      doub N N 352 
PRO   C     OXT    sing N N 353 
PRO   CB    CG     sing N N 354 
PRO   CB    HB2    sing N N 355 
PRO   CB    HB3    sing N N 356 
PRO   CG    CD     sing N N 357 
PRO   CG    HG2    sing N N 358 
PRO   CG    HG3    sing N N 359 
PRO   CD    HD2    sing N N 360 
PRO   CD    HD3    sing N N 361 
PRO   OXT   HXT    sing N N 362 
SER   N     CA     sing N N 363 
SER   N     H      sing N N 364 
SER   N     H2     sing N N 365 
SER   CA    C      sing N N 366 
SER   CA    CB     sing N N 367 
SER   CA    HA     sing N N 368 
SER   C     O      doub N N 369 
SER   C     OXT    sing N N 370 
SER   CB    OG     sing N N 371 
SER   CB    HB2    sing N N 372 
SER   CB    HB3    sing N N 373 
SER   OG    HG     sing N N 374 
SER   OXT   HXT    sing N N 375 
THR   N     CA     sing N N 376 
THR   N     H      sing N N 377 
THR   N     H2     sing N N 378 
THR   CA    C      sing N N 379 
THR   CA    CB     sing N N 380 
THR   CA    HA     sing N N 381 
THR   C     O      doub N N 382 
THR   C     OXT    sing N N 383 
THR   CB    OG1    sing N N 384 
THR   CB    CG2    sing N N 385 
THR   CB    HB     sing N N 386 
THR   OG1   HG1    sing N N 387 
THR   CG2   HG21   sing N N 388 
THR   CG2   HG22   sing N N 389 
THR   CG2   HG23   sing N N 390 
THR   OXT   HXT    sing N N 391 
TYR   N     CA     sing N N 392 
TYR   N     H      sing N N 393 
TYR   N     H2     sing N N 394 
TYR   CA    C      sing N N 395 
TYR   CA    CB     sing N N 396 
TYR   CA    HA     sing N N 397 
TYR   C     O      doub N N 398 
TYR   C     OXT    sing N N 399 
TYR   CB    CG     sing N N 400 
TYR   CB    HB2    sing N N 401 
TYR   CB    HB3    sing N N 402 
TYR   CG    CD1    doub Y N 403 
TYR   CG    CD2    sing Y N 404 
TYR   CD1   CE1    sing Y N 405 
TYR   CD1   HD1    sing N N 406 
TYR   CD2   CE2    doub Y N 407 
TYR   CD2   HD2    sing N N 408 
TYR   CE1   CZ     doub Y N 409 
TYR   CE1   HE1    sing N N 410 
TYR   CE2   CZ     sing Y N 411 
TYR   CE2   HE2    sing N N 412 
TYR   CZ    OH     sing N N 413 
TYR   OH    HH     sing N N 414 
TYR   OXT   HXT    sing N N 415 
VAL   N     CA     sing N N 416 
VAL   N     H      sing N N 417 
VAL   N     H2     sing N N 418 
VAL   CA    C      sing N N 419 
VAL   CA    CB     sing N N 420 
VAL   CA    HA     sing N N 421 
VAL   C     O      doub N N 422 
VAL   C     OXT    sing N N 423 
VAL   CB    CG1    sing N N 424 
VAL   CB    CG2    sing N N 425 
VAL   CB    HB     sing N N 426 
VAL   CG1   HG11   sing N N 427 
VAL   CG1   HG12   sing N N 428 
VAL   CG1   HG13   sing N N 429 
VAL   CG2   HG21   sing N N 430 
VAL   CG2   HG22   sing N N 431 
VAL   CG2   HG23   sing N N 432 
VAL   OXT   HXT    sing N N 433 
# 
_pdbx_audit_support.funding_organization   'Cancer Research UK' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'unreleased crystal structure' 
# 
_atom_sites.entry_id                    9GGU 
_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]   0.026991 
_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]   0.024851 
_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]   0.009014 
_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   ? -17.241 21.057 -4.827 1.00 41.48 ? 1   MET   A N     1 
ATOM   2    C  CA    . MET   A 1 4   ? -16.178 21.515 -3.901 1.00 37.03 ? 1   MET   A CA    1 
ATOM   3    C  C     . MET   A 1 4   ? -16.513 21.073 -2.473 1.00 31.24 ? 1   MET   A C     1 
ATOM   4    O  O     . MET   A 1 4   ? -17.624 21.238 -2.064 1.00 29.44 ? 1   MET   A O     1 
ATOM   5    C  CB    . MET   A 1 4   ? -16.128 23.037 -3.907 1.00 40.19 ? 1   MET   A CB    1 
ATOM   6    C  CG    . MET   A 1 4   ? -15.190 23.555 -2.915 1.00 43.70 ? 1   MET   A CG    1 
ATOM   7    S  SD    . MET   A 1 4   ? -13.787 24.122 -3.794 1.00 40.40 ? 1   MET   A SD    1 
ATOM   8    C  CE    . MET   A 1 4   ? -14.461 24.408 -5.426 1.00 41.68 ? 1   MET   A CE    1 
ATOM   9    N  N     . THR   A 1 5   ? -15.532 20.573 -1.737 1.00 25.06 ? 2   THR   A N     1 
ATOM   10   C  CA    . THR   A 1 5   ? -15.872 20.090 -0.387 1.00 22.83 ? 2   THR   A CA    1 
ATOM   11   C  C     . THR   A 1 5   ? -14.966 20.802 0.613  1.00 21.09 ? 2   THR   A C     1 
ATOM   12   O  O     . THR   A 1 5   ? -13.828 20.829 0.256  1.00 22.99 ? 2   THR   A O     1 
ATOM   13   C  CB    . THR   A 1 5   ? -15.634 18.587 -0.373 1.00 21.45 ? 2   THR   A CB    1 
ATOM   14   O  OG1   . THR   A 1 5   ? -16.477 18.050 -1.386 1.00 22.28 ? 2   THR   A OG1   1 
ATOM   15   C  CG2   . THR   A 1 5   ? -15.936 17.976 0.971  1.00 22.22 ? 2   THR   A CG2   1 
ATOM   16   N  N     A GLU   A 1 6   ? -15.335 21.256 1.681  0.50 19.98 ? 3   GLU   A N     1 
ATOM   17   N  N     B GLU   A 1 6   ? -15.338 21.273 1.670  0.50 20.19 ? 3   GLU   A N     1 
ATOM   18   C  CA    A GLU   A 1 6   ? -14.434 21.935 2.656  0.50 20.22 ? 3   GLU   A CA    1 
ATOM   19   C  CA    B GLU   A 1 6   ? -14.417 21.933 2.639  0.50 20.50 ? 3   GLU   A CA    1 
ATOM   20   C  C     A GLU   A 1 6   ? -13.897 20.941 3.707  0.50 18.71 ? 3   GLU   A C     1 
ATOM   21   C  C     B GLU   A 1 6   ? -13.895 20.940 3.685  0.50 18.87 ? 3   GLU   A C     1 
ATOM   22   O  O     A GLU   A 1 6   ? -14.645 20.072 4.135  0.50 19.71 ? 3   GLU   A O     1 
ATOM   23   O  O     B GLU   A 1 6   ? -14.657 20.090 4.131  0.50 19.98 ? 3   GLU   A O     1 
ATOM   24   C  CB    A GLU   A 1 6   ? -15.181 23.075 3.350  0.50 21.71 ? 3   GLU   A CB    1 
ATOM   25   C  CB    B GLU   A 1 6   ? -15.127 23.082 3.347  0.50 22.25 ? 3   GLU   A CB    1 
ATOM   26   C  CG    A GLU   A 1 6   ? -14.282 23.896 4.258  0.50 22.51 ? 3   GLU   A CG    1 
ATOM   27   C  CG    B GLU   A 1 6   ? -15.827 24.019 2.387  0.50 24.46 ? 3   GLU   A CG    1 
ATOM   28   C  CD    A GLU   A 1 6   ? -14.913 24.845 5.265  0.50 25.39 ? 3   GLU   A CD    1 
ATOM   29   C  CD    B GLU   A 1 6   ? -16.478 25.240 3.025  0.50 27.50 ? 3   GLU   A CD    1 
ATOM   30   O  OE1   A GLU   A 1 6   ? -14.248 25.822 5.652  0.50 27.26 ? 3   GLU   A OE1   1 
ATOM   31   O  OE1   B GLU   A 1 6   ? -17.514 25.698 2.506  0.50 29.12 ? 3   GLU   A OE1   1 
ATOM   32   O  OE2   A GLU   A 1 6   ? -16.042 24.594 5.684  0.50 29.08 ? 3   GLU   A OE2   1 
ATOM   33   O  OE2   B GLU   A 1 6   ? -15.929 25.740 4.021  0.50 31.72 ? 3   GLU   A OE2   1 
ATOM   34   N  N     . TYR   A 1 7   ? -12.648 21.125 4.105  1.00 15.83 ? 4   TYR   A N     1 
ATOM   35   C  CA    . TYR   A 1 7   ? -11.994 20.283 5.136  1.00 15.31 ? 4   TYR   A CA    1 
ATOM   36   C  C     . TYR   A 1 7   ? -11.274 21.222 6.102  1.00 14.75 ? 4   TYR   A C     1 
ATOM   37   O  O     . TYR   A 1 7   ? -10.387 21.890 5.676  1.00 15.38 ? 4   TYR   A O     1 
ATOM   38   C  CB    . TYR   A 1 7   ? -10.967 19.355 4.487  1.00 14.16 ? 4   TYR   A CB    1 
ATOM   39   C  CG    . TYR   A 1 7   ? -11.576 18.291 3.621  1.00 14.43 ? 4   TYR   A CG    1 
ATOM   40   C  CD1   . TYR   A 1 7   ? -11.851 18.504 2.288  1.00 15.35 ? 4   TYR   A CD1   1 
ATOM   41   C  CD2   . TYR   A 1 7   ? -11.929 17.077 4.157  1.00 14.51 ? 4   TYR   A CD2   1 
ATOM   42   C  CE1   . TYR   A 1 7   ? -12.427 17.518 1.514  1.00 15.84 ? 4   TYR   A CE1   1 
ATOM   43   C  CE2   . TYR   A 1 7   ? -12.526 16.087 3.404  1.00 15.40 ? 4   TYR   A CE2   1 
ATOM   44   C  CZ    . TYR   A 1 7   ? -12.788 16.310 2.074  1.00 16.35 ? 4   TYR   A CZ    1 
ATOM   45   O  OH    . TYR   A 1 7   ? -13.364 15.356 1.312  1.00 16.37 ? 4   TYR   A OH    1 
ATOM   46   N  N     . LYS   A 1 8   ? -11.709 21.236 7.349  1.00 14.08 ? 5   LYS   A N     1 
ATOM   47   C  CA    . LYS   A 1 8   ? -11.078 22.099 8.360  1.00 15.14 ? 5   LYS   A CA    1 
ATOM   48   C  C     . LYS   A 1 8   ? -10.014 21.291 9.108  1.00 14.42 ? 5   LYS   A C     1 
ATOM   49   O  O     . LYS   A 1 8   ? -10.339 20.348 9.836  1.00 14.05 ? 5   LYS   A O     1 
ATOM   50   C  CB    . LYS   A 1 8   ? -12.116 22.638 9.338  1.00 17.21 ? 5   LYS   A CB    1 
ATOM   51   C  CG    . LYS   A 1 8   ? -13.148 23.542 8.686  1.00 20.38 ? 5   LYS   A CG    1 
ATOM   52   C  CD    . LYS   A 1 8   ? -14.336 23.786 9.605  1.00 24.85 ? 5   LYS   A CD    1 
ATOM   53   C  CE    . LYS   A 1 8   ? -15.490 24.422 8.847  1.00 29.80 ? 5   LYS   A CE    1 
ATOM   54   N  NZ    . LYS   A 1 8   ? -15.163 25.838 8.544  1.00 32.85 ? 5   LYS   A NZ    1 
ATOM   55   N  N     . LEU   A 1 9   ? -8.762  21.692 8.954  1.00 13.61 ? 6   LEU   A N     1 
ATOM   56   C  CA    . LEU   A 1 9   ? -7.619  20.958 9.484  1.00 13.98 ? 6   LEU   A CA    1 
ATOM   57   C  C     . LEU   A 1 9   ? -6.941  21.830 10.516 1.00 13.55 ? 6   LEU   A C     1 
ATOM   58   O  O     . LEU   A 1 9   ? -6.861  23.041 10.310 1.00 15.78 ? 6   LEU   A O     1 
ATOM   59   C  CB    . LEU   A 1 9   ? -6.598  20.640 8.383  1.00 13.27 ? 6   LEU   A CB    1 
ATOM   60   C  CG    . LEU   A 1 9   ? -7.167  20.030 7.089  1.00 14.75 ? 6   LEU   A CG    1 
ATOM   61   C  CD1   . LEU   A 1 9   ? -6.055  19.633 6.128  1.00 15.14 ? 6   LEU   A CD1   1 
ATOM   62   C  CD2   . LEU   A 1 9   ? -8.049  18.824 7.367  1.00 14.99 ? 6   LEU   A CD2   1 
ATOM   63   N  N     . VAL   A 1 10  ? -6.501  21.212 11.614 1.00 12.99 ? 7   VAL   A N     1 
ATOM   64   C  CA    . VAL   A 1 10  ? -5.799  21.912 12.706 1.00 13.68 ? 7   VAL   A CA    1 
ATOM   65   C  C     . VAL   A 1 10  ? -4.445  21.243 12.973 1.00 13.17 ? 7   VAL   A C     1 
ATOM   66   O  O     . VAL   A 1 10  ? -4.382  19.995 13.138 1.00 14.09 ? 7   VAL   A O     1 
ATOM   67   C  CB    . VAL   A 1 10  ? -6.632  21.842 13.988 1.00 13.78 ? 7   VAL   A CB    1 
ATOM   68   C  CG1   . VAL   A 1 10  ? -5.931  22.589 15.112 1.00 15.79 ? 7   VAL   A CG1   1 
ATOM   69   C  CG2   . VAL   A 1 10  ? -8.014  22.426 13.730 1.00 14.67 ? 7   VAL   A CG2   1 
ATOM   70   N  N     . VAL   A 1 11  ? -3.378  22.045 12.952 1.00 12.41 ? 8   VAL   A N     1 
ATOM   71   C  CA    . VAL   A 1 11  ? -2.021  21.543 13.154 1.00 13.10 ? 8   VAL   A CA    1 
ATOM   72   C  C     . VAL   A 1 11  ? -1.616  21.846 14.593 1.00 13.65 ? 8   VAL   A C     1 
ATOM   73   O  O     . VAL   A 1 11  ? -1.620  23.007 14.979 1.00 14.70 ? 8   VAL   A O     1 
ATOM   74   C  CB    . VAL   A 1 11  ? -1.048  22.229 12.200 1.00 13.68 ? 8   VAL   A CB    1 
ATOM   75   C  CG1   . VAL   A 1 11  ? 0.338   21.602 12.323 1.00 13.49 ? 8   VAL   A CG1   1 
ATOM   76   C  CG2   . VAL   A 1 11  ? -1.542  22.144 10.758 1.00 14.03 ? 8   VAL   A CG2   1 
ATOM   77   N  N     . VAL   A 1 12  ? -1.382  20.794 15.367 1.00 13.69 ? 9   VAL   A N     1 
ATOM   78   C  CA    . VAL   A 1 12  ? -0.994  20.903 16.794 1.00 14.97 ? 9   VAL   A CA    1 
ATOM   79   C  C     . VAL   A 1 12  ? 0.346   20.208 17.007 1.00 14.14 ? 9   VAL   A C     1 
ATOM   80   O  O     . VAL   A 1 12  ? 0.755   19.486 16.174 1.00 14.12 ? 9   VAL   A O     1 
ATOM   81   C  CB    . VAL   A 1 12  ? -2.072  20.289 17.706 1.00 15.52 ? 9   VAL   A CB    1 
ATOM   82   C  CG1   . VAL   A 1 12  ? -3.415  20.943 17.463 1.00 15.70 ? 9   VAL   A CG1   1 
ATOM   83   C  CG2   . VAL   A 1 12  ? -2.175  18.781 17.532 1.00 15.53 ? 9   VAL   A CG2   1 
ATOM   84   N  N     . GLY   A 1 13  ? 0.976   20.538 18.117 1.00 14.41 ? 10  GLY   A N     1 
ATOM   85   C  CA    . GLY   A 1 13  ? 2.240   19.917 18.512 1.00 14.27 ? 10  GLY   A CA    1 
ATOM   86   C  C     . GLY   A 1 13  ? 3.032   20.860 19.392 1.00 15.85 ? 10  GLY   A C     1 
ATOM   87   O  O     . GLY   A 1 13  ? 2.757   22.003 19.369 1.00 15.88 ? 10  GLY   A O     1 
ATOM   88   N  N     . ALA   A 1 14  ? 4.099   20.374 20.003 1.00 15.36 ? 11  ALA   A N     1 
ATOM   89   C  CA    . ALA   A 1 14  ? 4.914   21.234 20.885 1.00 16.87 ? 11  ALA   A CA    1 
ATOM   90   C  C     . ALA   A 1 14  ? 5.581   22.393 20.128 1.00 16.98 ? 11  ALA   A C     1 
ATOM   91   O  O     . ALA   A 1 14  ? 5.797   22.328 18.958 1.00 17.00 ? 11  ALA   A O     1 
ATOM   92   C  CB    . ALA   A 1 14  ? 5.942   20.383 21.585 1.00 17.05 ? 11  ALA   A CB    1 
ATOM   93   N  N     . GLY   A 1 15  ? 5.868   23.481 20.837 1.00 17.91 ? 12  GLY   A N     1 
ATOM   94   C  CA    . GLY   A 1 15  ? 6.598   24.562 20.230 1.00 19.04 ? 12  GLY   A CA    1 
ATOM   95   C  C     . GLY   A 1 15  ? 7.894   24.083 19.592 1.00 18.47 ? 12  GLY   A C     1 
ATOM   96   O  O     . GLY   A 1 15  ? 8.652   23.284 20.153 1.00 18.94 ? 12  GLY   A O     1 
ATOM   97   N  N     . GLY   A 1 16  ? 8.142   24.571 18.387 1.00 17.65 ? 13  GLY   A N     1 
ATOM   98   C  CA    . GLY   A 1 16  ? 9.373   24.282 17.703 1.00 18.00 ? 13  GLY   A CA    1 
ATOM   99   C  C     . GLY   A 1 16  ? 9.392   23.040 16.828 1.00 18.30 ? 13  GLY   A C     1 
ATOM   100  O  O     . GLY   A 1 16  ? 10.420  22.733 16.222 1.00 17.90 ? 13  GLY   A O     1 
ATOM   101  N  N     . VAL   A 1 17  ? 8.298   22.285 16.774 1.00 15.61 ? 14  VAL   A N     1 
ATOM   102  C  CA    . VAL   A 1 17  ? 8.360   21.023 16.020 1.00 14.49 ? 14  VAL   A CA    1 
ATOM   103  C  C     . VAL   A 1 17  ? 8.266   21.229 14.509 1.00 14.55 ? 14  VAL   A C     1 
ATOM   104  O  O     . VAL   A 1 17  ? 8.642   20.337 13.757 1.00 13.92 ? 14  VAL   A O     1 
ATOM   105  C  CB    . VAL   A 1 17  ? 7.257   20.016 16.429 1.00 14.25 ? 14  VAL   A CB    1 
ATOM   106  C  CG1   . VAL   A 1 17  ? 7.429   19.569 17.872 1.00 13.65 ? 14  VAL   A CG1   1 
ATOM   107  C  CG2   . VAL   A 1 17  ? 5.871   20.550 16.141 1.00 14.61 ? 14  VAL   A CG2   1 
ATOM   108  N  N     . GLY   A 1 18  ? 7.696   22.352 14.082 1.00 15.48 ? 15  GLY   A N     1 
ATOM   109  C  CA    . GLY   A 1 18  ? 7.515   22.657 12.651 1.00 15.57 ? 15  GLY   A CA    1 
ATOM   110  C  C     . GLY   A 1 18  ? 6.099   22.816 12.146 1.00 15.53 ? 15  GLY   A C     1 
ATOM   111  O  O     . GLY   A 1 18  ? 5.876   22.717 10.946 1.00 14.98 ? 15  GLY   A O     1 
ATOM   112  N  N     . LYS   A 1 19  ? 5.157   23.151 13.022 1.00 15.79 ? 16  LYS   A N     1 
ATOM   113  C  CA    . LYS   A 1 19  ? 3.751   23.395 12.622 1.00 15.56 ? 16  LYS   A CA    1 
ATOM   114  C  C     . LYS   A 1 19  ? 3.668   24.496 11.551 1.00 17.01 ? 16  LYS   A C     1 
ATOM   115  O  O     . LYS   A 1 19  ? 3.013   24.334 10.499 1.00 16.84 ? 16  LYS   A O     1 
ATOM   116  C  CB    . LYS   A 1 19  ? 2.903   23.797 13.823 1.00 16.50 ? 16  LYS   A CB    1 
ATOM   117  C  CG    . LYS   A 1 19  ? 2.829   22.764 14.956 1.00 16.25 ? 16  LYS   A CG    1 
ATOM   118  C  CD    . LYS   A 1 19  ? 1.936   23.271 16.088 1.00 18.01 ? 16  LYS   A CD    1 
ATOM   119  C  CE    . LYS   A 1 19  ? 2.538   24.378 16.919 1.00 18.65 ? 16  LYS   A CE    1 
ATOM   120  N  NZ    . LYS   A 1 19  ? 3.831   24.100 17.627 1.00 18.46 ? 16  LYS   A NZ    1 
ATOM   121  N  N     . SER   A 1 20  ? 4.332   25.626 11.811 1.00 16.31 ? 17  SER   A N     1 
ATOM   122  C  CA    . SER   A 1 20  ? 4.262   26.758 10.901 1.00 16.01 ? 17  SER   A CA    1 
ATOM   123  C  C     . SER   A 1 20  ? 5.022   26.460 9.636  1.00 16.44 ? 17  SER   A C     1 
ATOM   124  O  O     . SER   A 1 20  ? 4.546   26.752 8.544  1.00 17.16 ? 17  SER   A O     1 
ATOM   125  C  CB    . SER   A 1 20  ? 4.844   28.028 11.547 1.00 17.17 ? 17  SER   A CB    1 
ATOM   126  O  OG    . SER   A 1 20  ? 4.033   28.399 12.657 1.00 17.74 ? 17  SER   A OG    1 
ATOM   127  N  N     . ALA   A 1 21  ? 6.208   25.882 9.781  1.00 15.36 ? 18  ALA   A N     1 
ATOM   128  C  CA    . ALA   A 1 21  ? 7.006   25.573 8.607  1.00 17.01 ? 18  ALA   A CA    1 
ATOM   129  C  C     . ALA   A 1 21  ? 6.282   24.582 7.674  1.00 16.12 ? 18  ALA   A C     1 
ATOM   130  O  O     . ALA   A 1 21  ? 6.335   24.734 6.456  1.00 16.53 ? 18  ALA   A O     1 
ATOM   131  C  CB    . ALA   A 1 21  ? 8.366   25.053 8.997  1.00 16.79 ? 18  ALA   A CB    1 
ATOM   132  N  N     . LEU   A 1 22  ? 5.614   23.566 8.244  1.00 16.18 ? 19  LEU   A N     1 
ATOM   133  C  CA    . LEU   A 1 22  ? 4.773   22.650 7.403  1.00 15.92 ? 19  LEU   A CA    1 
ATOM   134  C  C     . LEU   A 1 22  ? 3.624   23.365 6.696  1.00 16.37 ? 19  LEU   A C     1 
ATOM   135  O  O     . LEU   A 1 22  ? 3.339   23.134 5.508  1.00 17.46 ? 19  LEU   A O     1 
ATOM   136  C  CB    . LEU   A 1 22  ? 4.229   21.495 8.237  1.00 15.98 ? 19  LEU   A CB    1 
ATOM   137  C  CG    . LEU   A 1 22  ? 5.281   20.450 8.625  1.00 15.79 ? 19  LEU   A CG    1 
ATOM   138  C  CD1   . LEU   A 1 22  ? 4.729   19.567 9.740  1.00 15.54 ? 19  LEU   A CD1   1 
ATOM   139  C  CD2   . LEU   A 1 22  ? 5.754   19.612 7.434  1.00 17.25 ? 19  LEU   A CD2   1 
ATOM   140  N  N     . THR   A 1 23  ? 2.910   24.162 7.463  1.00 16.82 ? 20  THR   A N     1 
ATOM   141  C  CA    . THR   A 1 23  ? 1.744   24.867 6.927  1.00 16.52 ? 20  THR   A CA    1 
ATOM   142  C  C     . THR   A 1 23  ? 2.150   25.849 5.822  1.00 17.71 ? 20  THR   A C     1 
ATOM   143  O  O     . THR   A 1 23  ? 1.520   25.877 4.761  1.00 15.88 ? 20  THR   A O     1 
ATOM   144  C  CB    . THR   A 1 23  ? 0.963   25.605 8.027  1.00 16.31 ? 20  THR   A CB    1 
ATOM   145  O  OG1   . THR   A 1 23  ? 0.565   24.682 9.066  1.00 15.77 ? 20  THR   A OG1   1 
ATOM   146  C  CG2   . THR   A 1 23  ? -0.293  26.255 7.432  1.00 16.70 ? 20  THR   A CG2   1 
ATOM   147  N  N     . ILE   A 1 24  ? 3.224   26.592 6.047  1.00 18.56 ? 21  ILE   A N     1 
ATOM   148  C  CA    . ILE   A 1 24  ? 3.693   27.580 5.063  1.00 19.43 ? 21  ILE   A CA    1 
ATOM   149  C  C     . ILE   A 1 24  ? 4.254   26.897 3.827  1.00 19.92 ? 21  ILE   A C     1 
ATOM   150  O  O     . ILE   A 1 24  ? 4.040   27.368 2.700  1.00 21.14 ? 21  ILE   A O     1 
ATOM   151  C  CB    . ILE   A 1 24  ? 4.726   28.537 5.714  1.00 20.95 ? 21  ILE   A CB    1 
ATOM   152  C  CG1   . ILE   A 1 24  ? 4.006   29.375 6.776  1.00 22.15 ? 21  ILE   A CG1   1 
ATOM   153  C  CG2   . ILE   A 1 24  ? 5.441   29.392 4.674  1.00 22.80 ? 21  ILE   A CG2   1 
ATOM   154  C  CD1   . ILE   A 1 24  ? 4.929   29.986 7.798  1.00 25.46 ? 21  ILE   A CD1   1 
ATOM   155  N  N     . GLN   A 1 25  ? 4.952   25.770 4.005  1.00 18.46 ? 22  GLN   A N     1 
ATOM   156  C  CA    . GLN   A 1 25  ? 5.400   24.995 2.872  1.00 18.75 ? 22  GLN   A CA    1 
ATOM   157  C  C     . GLN   A 1 25  ? 4.254   24.567 1.986  1.00 20.27 ? 22  GLN   A C     1 
ATOM   158  O  O     . GLN   A 1 25  ? 4.315   24.737 0.768  1.00 20.17 ? 22  GLN   A O     1 
ATOM   159  C  CB    . GLN   A 1 25  ? 6.169   23.737 3.301  1.00 19.91 ? 22  GLN   A CB    1 
ATOM   160  C  CG    . GLN   A 1 25  ? 7.649   23.936 3.299  1.00 21.56 ? 22  GLN   A CG    1 
ATOM   161  C  CD    . GLN   A 1 25  ? 8.293   24.071 1.915  1.00 23.23 ? 22  GLN   A CD    1 
ATOM   162  O  OE1   . GLN   A 1 25  ? 7.648   24.432 0.903  1.00 23.23 ? 22  GLN   A OE1   1 
ATOM   163  N  NE2   . GLN   A 1 25  ? 9.577   23.823 1.880  1.00 22.77 ? 22  GLN   A NE2   1 
ATOM   164  N  N     . LEU   A 1 26  ? 3.226   24.008 2.586  1.00 19.17 ? 23  LEU   A N     1 
ATOM   165  C  CA    . LEU   A 1 26  ? 2.080   23.547 1.789  1.00 19.63 ? 23  LEU   A CA    1 
ATOM   166  C  C     . LEU   A 1 26  ? 1.440   24.718 1.032  1.00 22.84 ? 23  LEU   A C     1 
ATOM   167  O  O     . LEU   A 1 26  ? 1.187   24.590 -0.149 1.00 22.57 ? 23  LEU   A O     1 
ATOM   168  C  CB    . LEU   A 1 26  ? 1.054   22.928 2.741  1.00 20.31 ? 23  LEU   A CB    1 
ATOM   169  C  CG    . LEU   A 1 26  ? -0.192  22.416 2.035  1.00 22.44 ? 23  LEU   A CG    1 
ATOM   170  C  CD1   . LEU   A 1 26  ? 0.100   21.099 1.357  1.00 21.67 ? 23  LEU   A CD1   1 
ATOM   171  C  CD2   . LEU   A 1 26  ? -1.331  22.250 3.003  1.00 22.51 ? 23  LEU   A CD2   1 
ATOM   172  N  N     . ILE   A 1 27  ? 1.071   25.756 1.777  1.00 21.62 ? 24  ILE   A N     1 
ATOM   173  C  CA    . ILE   A 1 27  ? 0.345   26.936 1.238  1.00 24.84 ? 24  ILE   A CA    1 
ATOM   174  C  C     . ILE   A 1 27  ? 1.173   27.826 0.323  1.00 25.31 ? 24  ILE   A C     1 
ATOM   175  O  O     . ILE   A 1 27  ? 0.633   28.212 -0.702 1.00 27.64 ? 24  ILE   A O     1 
ATOM   176  C  CB    . ILE   A 1 27  ? -0.189  27.780 2.395  1.00 24.07 ? 24  ILE   A CB    1 
ATOM   177  C  CG1   . ILE   A 1 27  ? -1.166  26.989 3.248  1.00 23.51 ? 24  ILE   A CG1   1 
ATOM   178  C  CG2   . ILE   A 1 27  ? -0.825  29.066 1.882  1.00 28.87 ? 24  ILE   A CG2   1 
ATOM   179  C  CD1   . ILE   A 1 27  ? -2.387  26.526 2.532  1.00 25.20 ? 24  ILE   A CD1   1 
ATOM   180  N  N     . GLN   A 1 28  ? 2.377   28.166 0.742  1.00 23.87 ? 25  GLN   A N     1 
ATOM   181  C  CA    . GLN   A 1 28  ? 3.175   29.200 0.050  1.00 26.11 ? 25  GLN   A CA    1 
ATOM   182  C  C     . GLN   A 1 28  ? 4.440   28.643 -0.589 1.00 26.26 ? 25  GLN   A C     1 
ATOM   183  O  O     . GLN   A 1 28  ? 5.148   29.434 -1.125 1.00 26.66 ? 25  GLN   A O     1 
ATOM   184  C  CB    . GLN   A 1 28  ? 3.491   30.351 1.011  1.00 26.57 ? 25  GLN   A CB    1 
ATOM   185  C  CG    . GLN   A 1 28  ? 2.279   31.172 1.395  1.00 29.59 ? 25  GLN   A CG    1 
ATOM   186  C  CD    . GLN   A 1 28  ? 2.510   32.133 2.536  1.00 34.32 ? 25  GLN   A CD    1 
ATOM   187  O  OE1   . GLN   A 1 28  ? 3.615   32.512 2.848  1.00 33.01 ? 25  GLN   A OE1   1 
ATOM   188  N  NE2   . GLN   A 1 28  ? 1.427   32.561 3.145  1.00 37.76 ? 25  GLN   A NE2   1 
ATOM   189  N  N     . ASN   A 1 29  ? 4.720   27.345 -0.491 1.00 26.84 ? 26  ASN   A N     1 
ATOM   190  C  CA    . ASN   A 1 29  ? 5.890   26.740 -1.184 1.00 25.09 ? 26  ASN   A CA    1 
ATOM   191  C  C     . ASN   A 1 29  ? 7.241   27.380 -0.843 1.00 26.99 ? 26  ASN   A C     1 
ATOM   192  O  O     . ASN   A 1 29  ? 8.023   27.623 -1.743 1.00 30.22 ? 26  ASN   A O     1 
ATOM   193  C  CB    . ASN   A 1 29  ? 5.641   26.680 -2.690 1.00 27.07 ? 26  ASN   A CB    1 
ATOM   194  C  CG    . ASN   A 1 29  ? 6.662   25.898 -3.478 1.00 28.25 ? 26  ASN   A CG    1 
ATOM   195  O  OD1   . ASN   A 1 29  ? 7.328   25.033 -2.970 1.00 31.09 ? 26  ASN   A OD1   1 
ATOM   196  N  ND2   . ASN   A 1 29  ? 6.756   26.166 -4.763 1.00 32.59 ? 26  ASN   A ND2   1 
ATOM   197  N  N     . HIS   A 1 30  ? 7.486   27.658 0.426  1.00 23.95 ? 27  HIS   A N     1 
ATOM   198  C  CA    . HIS   A 1 30  ? 8.821   28.112 0.878  1.00 23.65 ? 27  HIS   A CA    1 
ATOM   199  C  C     . HIS   A 1 30  ? 8.996   27.638 2.323  1.00 21.85 ? 27  HIS   A C     1 
ATOM   200  O  O     . HIS   A 1 30  ? 8.020   27.435 2.996  1.00 21.41 ? 27  HIS   A O     1 
ATOM   201  C  CB    . HIS   A 1 30  ? 9.076   29.623 0.703  1.00 22.61 ? 27  HIS   A CB    1 
ATOM   202  C  CG    . HIS   A 1 30  ? 8.144   30.478 1.471  1.00 22.53 ? 27  HIS   A CG    1 
ATOM   203  N  ND1   . HIS   A 1 30  ? 8.515   31.132 2.596  1.00 24.07 ? 27  HIS   A ND1   1 
ATOM   204  C  CD2   . HIS   A 1 30  ? 6.847   30.742 1.292  1.00 25.62 ? 27  HIS   A CD2   1 
ATOM   205  C  CE1   . HIS   A 1 30  ? 7.479   31.753 3.087  1.00 27.31 ? 27  HIS   A CE1   1 
ATOM   206  N  NE2   . HIS   A 1 30  ? 6.455   31.544 2.305  1.00 26.16 ? 27  HIS   A NE2   1 
ATOM   207  N  N     . PHE   A 1 31  ? 10.235  27.457 2.694  1.00 23.48 ? 28  PHE   A N     1 
ATOM   208  C  CA    . PHE   A 1 31  ? 10.647  27.085 4.035  1.00 22.15 ? 28  PHE   A CA    1 
ATOM   209  C  C     . PHE   A 1 31  ? 10.998  28.303 4.875  1.00 23.82 ? 28  PHE   A C     1 
ATOM   210  O  O     . PHE   A 1 31  ? 11.866  29.110 4.496  1.00 26.17 ? 28  PHE   A O     1 
ATOM   211  C  CB    . PHE   A 1 31  ? 11.875  26.188 3.952  1.00 20.94 ? 28  PHE   A CB    1 
ATOM   212  C  CG    . PHE   A 1 31  ? 12.388  25.732 5.296  1.00 21.97 ? 28  PHE   A CG    1 
ATOM   213  C  CD1   . PHE   A 1 31  ? 11.542  25.083 6.188  1.00 20.05 ? 28  PHE   A CD1   1 
ATOM   214  C  CD2   . PHE   A 1 31  ? 13.704  25.962 5.690  1.00 21.48 ? 28  PHE   A CD2   1 
ATOM   215  C  CE1   . PHE   A 1 31  ? 12.003  24.654 7.406  1.00 20.91 ? 28  PHE   A CE1   1 
ATOM   216  C  CE2   . PHE   A 1 31  ? 14.168  25.548 6.930  1.00 22.14 ? 28  PHE   A CE2   1 
ATOM   217  C  CZ    . PHE   A 1 31  ? 13.313  24.873 7.787  1.00 19.56 ? 28  PHE   A CZ    1 
ATOM   218  N  N     . VAL   A 1 32  ? 10.374  28.402 6.045  1.00 23.71 ? 29  VAL   A N     1 
ATOM   219  C  CA    . VAL   A 1 32  ? 10.694  29.513 6.983  1.00 25.03 ? 29  VAL   A CA    1 
ATOM   220  C  C     . VAL   A 1 32  ? 11.674  29.044 8.061  1.00 28.06 ? 29  VAL   A C     1 
ATOM   221  O  O     . VAL   A 1 32  ? 11.400  28.076 8.733  1.00 25.49 ? 29  VAL   A O     1 
ATOM   222  C  CB    . VAL   A 1 32  ? 9.439   30.157 7.585  1.00 27.22 ? 29  VAL   A CB    1 
ATOM   223  C  CG1   . VAL   A 1 32  ? 8.695   30.946 6.553  1.00 28.02 ? 29  VAL   A CG1   1 
ATOM   224  C  CG2   . VAL   A 1 32  ? 8.503   29.169 8.262  1.00 28.34 ? 29  VAL   A CG2   1 
ATOM   225  N  N     . ASP   A 1 33  ? 12.796  29.760 8.150  1.00 33.15 ? 30  ASP   A N     1 
ATOM   226  C  CA    . ASP   A 1 33  ? 13.909  29.629 9.123  1.00 36.35 ? 30  ASP   A CA    1 
ATOM   227  C  C     . ASP   A 1 33  ? 13.561  30.061 10.543 1.00 35.41 ? 30  ASP   A C     1 
ATOM   228  O  O     . ASP   A 1 33  ? 14.075  29.432 11.450 1.00 39.06 ? 30  ASP   A O     1 
ATOM   229  C  CB    . ASP   A 1 33  ? 15.051  30.547 8.695  1.00 43.19 ? 30  ASP   A CB    1 
ATOM   230  C  CG    . ASP   A 1 33  ? 16.021  29.801 7.808  1.00 48.58 ? 30  ASP   A CG    1 
ATOM   231  O  OD1   . ASP   A 1 33  ? 15.782  28.608 7.591  1.00 53.03 ? 30  ASP   A OD1   1 
ATOM   232  O  OD2   . ASP   A 1 33  ? 17.068  30.370 7.508  1.00 53.17 ? 30  ASP   A OD2   1 
ATOM   233  N  N     . GLU   A 1 34  ? 12.784  31.120 10.731 1.00 38.40 ? 31  GLU   A N     1 
ATOM   234  C  CA    . GLU   A 1 34  ? 12.626  31.629 12.123 1.00 40.96 ? 31  GLU   A CA    1 
ATOM   235  C  C     . GLU   A 1 34  ? 11.282  32.327 12.265 1.00 41.51 ? 31  GLU   A C     1 
ATOM   236  O  O     . GLU   A 1 34  ? 11.183  33.540 12.492 1.00 45.33 ? 31  GLU   A O     1 
ATOM   237  C  CB    . GLU   A 1 34  ? 13.760  32.600 12.452 1.00 44.47 ? 31  GLU   A CB    1 
ATOM   238  C  CG    . GLU   A 1 34  ? 13.625  33.248 13.818 0.00 50.90 ? 31  GLU   A CG    1 
ATOM   239  C  CD    . GLU   A 1 34  ? 14.659  34.321 14.111 0.00 52.25 ? 31  GLU   A CD    1 
ATOM   240  O  OE1   . GLU   A 1 34  ? 15.431  34.662 13.193 0.00 52.81 ? 31  GLU   A OE1   1 
ATOM   241  O  OE2   . GLU   A 1 34  ? 14.689  34.814 15.256 0.00 52.81 ? 31  GLU   A OE2   1 
ATOM   242  N  N     . TYR   A 1 35  ? 10.266  31.524 12.223 1.00 33.61 ? 32  TYR   A N     1 
ATOM   243  C  CA    . TYR   A 1 35  ? 8.924   32.042 12.240 1.00 31.74 ? 32  TYR   A CA    1 
ATOM   244  C  C     . TYR   A 1 35  ? 8.444   32.268 13.665 1.00 30.16 ? 32  TYR   A C     1 
ATOM   245  O  O     . TYR   A 1 35  ? 8.416   31.340 14.463 1.00 30.69 ? 32  TYR   A O     1 
ATOM   246  C  CB    . TYR   A 1 35  ? 7.997   31.069 11.537 1.00 29.61 ? 32  TYR   A CB    1 
ATOM   247  C  CG    . TYR   A 1 35  ? 6.790   31.742 10.993 1.00 28.91 ? 32  TYR   A CG    1 
ATOM   248  C  CD1   . TYR   A 1 35  ? 6.905   32.591 9.916  1.00 31.18 ? 32  TYR   A CD1   1 
ATOM   249  C  CD2   . TYR   A 1 35  ? 5.541   31.542 11.552 1.00 26.56 ? 32  TYR   A CD2   1 
ATOM   250  C  CE1   . TYR   A 1 35  ? 5.812   33.234 9.397  1.00 32.40 ? 32  TYR   A CE1   1 
ATOM   251  C  CE2   . TYR   A 1 35  ? 4.428   32.165 11.038 1.00 28.59 ? 32  TYR   A CE2   1 
ATOM   252  C  CZ    . TYR   A 1 35  ? 4.574   33.016 9.954  1.00 31.86 ? 32  TYR   A CZ    1 
ATOM   253  O  OH    . TYR   A 1 35  ? 3.510   33.666 9.421  1.00 32.61 ? 32  TYR   A OH    1 
ATOM   254  N  N     . ASP   A 1 36  ? 8.051   33.499 13.964 1.00 31.99 ? 33  ASP   A N     1 
ATOM   255  C  CA    . ASP   A 1 36  ? 7.628   33.872 15.307 1.00 31.22 ? 33  ASP   A CA    1 
ATOM   256  C  C     . ASP   A 1 36  ? 6.713   32.787 15.875 1.00 31.44 ? 33  ASP   A C     1 
ATOM   257  O  O     . ASP   A 1 36  ? 5.670   32.488 15.272 1.00 30.50 ? 33  ASP   A O     1 
ATOM   258  C  CB    . ASP   A 1 36  ? 6.888   35.207 15.294 1.00 31.96 ? 33  ASP   A CB    1 
ATOM   259  C  CG    . ASP   A 1 36  ? 6.561   35.709 16.697 1.00 33.90 ? 33  ASP   A CG    1 
ATOM   260  O  OD1   . ASP   A 1 36  ? 6.202   34.911 17.583 1.00 35.06 ? 33  ASP   A OD1   1 
ATOM   261  O  OD2   . ASP   A 1 36  ? 6.655   36.923 16.921 1.00 40.07 ? 33  ASP   A OD2   1 
ATOM   262  N  N     . PRO   A 1 37  ? 7.103   32.194 17.018 1.00 29.73 ? 34  PRO   A N     1 
ATOM   263  C  CA    . PRO   A 1 37  ? 6.329   31.096 17.590 1.00 27.82 ? 34  PRO   A CA    1 
ATOM   264  C  C     . PRO   A 1 37  ? 4.924   31.453 18.091 1.00 27.74 ? 34  PRO   A C     1 
ATOM   265  O  O     . PRO   A 1 37  ? 4.132   30.545 18.372 1.00 27.01 ? 34  PRO   A O     1 
ATOM   266  C  CB    . PRO   A 1 37  ? 7.211   30.611 18.741 1.00 29.70 ? 34  PRO   A CB    1 
ATOM   267  C  CG    . PRO   A 1 37  ? 8.052   31.769 19.105 1.00 31.32 ? 34  PRO   A CG    1 
ATOM   268  C  CD    . PRO   A 1 37  ? 8.290   32.514 17.833 1.00 31.06 ? 34  PRO   A CD    1 
ATOM   269  N  N     . THR   A 1 38  ? 4.592   32.736 18.186 1.00 28.14 ? 35  THR   A N     1 
ATOM   270  C  CA    . THR   A 1 38  ? 3.279   33.139 18.703 1.00 29.48 ? 35  THR   A CA    1 
ATOM   271  C  C     . THR   A 1 38  ? 2.220   33.387 17.621 1.00 29.78 ? 35  THR   A C     1 
ATOM   272  O  O     . THR   A 1 38  ? 1.038   33.650 17.942 1.00 30.02 ? 35  THR   A O     1 
ATOM   273  C  CB    . THR   A 1 38  ? 3.415   34.388 19.628 1.00 29.80 ? 35  THR   A CB    1 
ATOM   274  O  OG1   . THR   A 1 38  ? 3.669   35.577 18.846 1.00 30.48 ? 35  THR   A OG1   1 
ATOM   275  C  CG2   . THR   A 1 38  ? 4.552   34.176 20.599 1.00 30.81 ? 35  THR   A CG2   1 
ATOM   276  N  N     . ILE   A 1 39  ? 2.620   33.361 16.349 1.00 26.37 ? 36  ILE   A N     1 
ATOM   277  C  CA    . ILE   A 1 39  ? 1.689   33.723 15.287 1.00 26.91 ? 36  ILE   A CA    1 
ATOM   278  C  C     . ILE   A 1 39  ? 0.789   32.522 15.043 1.00 23.35 ? 36  ILE   A C     1 
ATOM   279  O  O     . ILE   A 1 39  ? 1.281   31.403 14.868 1.00 22.33 ? 36  ILE   A O     1 
ATOM   280  C  CB    . ILE   A 1 39  ? 2.391   34.118 13.976 1.00 27.68 ? 36  ILE   A CB    1 
ATOM   281  C  CG1   . ILE   A 1 39  ? 3.319   35.301 14.221 1.00 29.58 ? 36  ILE   A CG1   1 
ATOM   282  C  CG2   . ILE   A 1 39  ? 1.348   34.441 12.898 1.00 29.29 ? 36  ILE   A CG2   1 
ATOM   283  C  CD1   . ILE   A 1 39  ? 4.037   35.757 12.972 1.00 30.77 ? 36  ILE   A CD1   1 
ATOM   284  N  N     . GLU   A 1 40  ? -0.521  32.765 15.104 1.00 23.49 ? 37  GLU   A N     1 
ATOM   285  C  CA    . GLU   A 1 40  ? -1.556  31.745 14.871 1.00 23.79 ? 37  GLU   A CA    1 
ATOM   286  C  C     . GLU   A 1 40  ? -2.477  32.280 13.780 1.00 24.63 ? 37  GLU   A C     1 
ATOM   287  O  O     . GLU   A 1 40  ? -3.125  33.313 13.970 1.00 26.26 ? 37  GLU   A O     1 
ATOM   288  C  CB    . GLU   A 1 40  ? -2.362  31.560 16.152 1.00 25.14 ? 37  GLU   A CB    1 
ATOM   289  C  CG    . GLU   A 1 40  ? -3.408  30.451 16.200 1.00 25.48 ? 37  GLU   A CG    1 
ATOM   290  C  CD    . GLU   A 1 40  ? -3.734  30.086 17.651 1.00 28.73 ? 37  GLU   A CD    1 
ATOM   291  O  OE1   . GLU   A 1 40  ? -3.140  29.138 18.215 1.00 24.00 ? 37  GLU   A OE1   1 
ATOM   292  O  OE2   . GLU   A 1 40  ? -4.549  30.806 18.273 1.00 34.55 ? 37  GLU   A OE2   1 
ATOM   293  N  N     . ASP   A 1 41  ? -2.541  31.595 12.642 1.00 24.48 ? 38  ASP   A N     1 
ATOM   294  C  CA    . ASP   A 1 41  ? -3.465  32.014 11.589 1.00 25.62 ? 38  ASP   A CA    1 
ATOM   295  C  C     . ASP   A 1 41  ? -4.045  30.825 10.883 1.00 22.63 ? 38  ASP   A C     1 
ATOM   296  O  O     . ASP   A 1 41  ? -3.535  29.703 11.025 1.00 21.32 ? 38  ASP   A O     1 
ATOM   297  C  CB    . ASP   A 1 41  ? -2.788  32.895 10.544 1.00 30.23 ? 38  ASP   A CB    1 
ATOM   298  C  CG    . ASP   A 1 41  ? -3.626  34.141 10.198 1.00 35.54 ? 38  ASP   A CG    1 
ATOM   299  O  OD1   . ASP   A 1 41  ? -4.892  34.074 10.064 1.00 33.94 ? 38  ASP   A OD1   1 
ATOM   300  O  OD2   . ASP   A 1 41  ? -2.996  35.198 10.078 1.00 42.88 ? 38  ASP   A OD2   1 
ATOM   301  N  N     . SER   A 1 42  ? -5.125  31.097 10.152 1.00 22.92 ? 39  SER   A N     1 
ATOM   302  C  CA    . SER   A 1 42  ? -5.698  30.118 9.248  1.00 21.28 ? 39  SER   A CA    1 
ATOM   303  C  C     . SER   A 1 42  ? -5.455  30.488 7.784  1.00 21.50 ? 39  SER   A C     1 
ATOM   304  O  O     . SER   A 1 42  ? -5.389  31.681 7.393  1.00 22.47 ? 39  SER   A O     1 
ATOM   305  C  CB    . SER   A 1 42  ? -7.191  29.917 9.510  1.00 22.08 ? 39  SER   A CB    1 
ATOM   306  O  OG    . SER   A 1 42  ? -7.927  31.098 9.250  1.00 26.83 ? 39  SER   A OG    1 
ATOM   307  N  N     . TYR   A 1 43  ? -5.315  29.431 6.979  1.00 19.35 ? 40  TYR   A N     1 
ATOM   308  C  CA    . TYR   A 1 43  ? -5.004  29.545 5.575  1.00 20.91 ? 40  TYR   A CA    1 
ATOM   309  C  C     . TYR   A 1 43  ? -5.965  28.682 4.779  1.00 20.00 ? 40  TYR   A C     1 
ATOM   310  O  O     . TYR   A 1 43  ? -6.180  27.527 5.106  1.00 19.25 ? 40  TYR   A O     1 
ATOM   311  C  CB    . TYR   A 1 43  ? -3.629  28.985 5.302  1.00 21.70 ? 40  TYR   A CB    1 
ATOM   312  C  CG    . TYR   A 1 43  ? -2.467  29.692 5.969  1.00 26.13 ? 40  TYR   A CG    1 
ATOM   313  C  CD1   . TYR   A 1 43  ? -2.091  29.388 7.263  1.00 26.24 ? 40  TYR   A CD1   1 
ATOM   314  C  CD2   . TYR   A 1 43  ? -1.695  30.602 5.252  1.00 31.77 ? 40  TYR   A CD2   1 
ATOM   315  C  CE1   . TYR   A 1 43  ? -0.977  29.992 7.849  1.00 30.78 ? 40  TYR   A CE1   1 
ATOM   316  C  CE2   . TYR   A 1 43  ? -0.600  31.232 5.835  1.00 33.58 ? 40  TYR   A CE2   1 
ATOM   317  C  CZ    . TYR   A 1 43  ? -0.251  30.920 7.135  1.00 34.05 ? 40  TYR   A CZ    1 
ATOM   318  O  OH    . TYR   A 1 43  ? 0.835   31.545 7.707  1.00 37.84 ? 40  TYR   A OH    1 
ATOM   319  N  N     . ARG   A 1 44  ? -6.543  29.262 3.764  1.00 20.90 ? 41  ARG   A N     1 
ATOM   320  C  CA    A ARG   A 1 44  ? -7.428  28.489 2.828  0.50 21.40 ? 41  ARG   A CA    1 
ATOM   321  C  CA    B ARG   A 1 44  ? -7.421  28.485 2.829  0.50 21.25 ? 41  ARG   A CA    1 
ATOM   322  C  C     . ARG   A 1 44  ? -6.834  28.362 1.365  1.00 21.40 ? 41  ARG   A C     1 
ATOM   323  O  O     . ARG   A 1 44  ? -6.167  29.256 0.753  1.00 26.30 ? 41  ARG   A O     1 
ATOM   324  C  CB    A ARG   A 1 44  ? -8.793  29.171 2.747  0.50 23.22 ? 41  ARG   A CB    1 
ATOM   325  C  CB    B ARG   A 1 44  ? -8.786  29.164 2.745  0.50 22.85 ? 41  ARG   A CB    1 
ATOM   326  C  CG    A ARG   A 1 44  ? -9.577  29.107 4.045  0.50 24.23 ? 41  ARG   A CG    1 
ATOM   327  C  CG    B ARG   A 1 44  ? -9.590  29.067 4.028  0.50 23.67 ? 41  ARG   A CG    1 
ATOM   328  C  CD    A ARG   A 1 44  ? -10.560 30.235 4.255  0.50 25.85 ? 41  ARG   A CD    1 
ATOM   329  C  CD    B ARG   A 1 44  ? -10.536 30.229 4.185  0.50 25.13 ? 41  ARG   A CD    1 
ATOM   330  N  NE    A ARG   A 1 44  ? -11.852 30.148 3.585  0.50 26.37 ? 41  ARG   A NE    1 
ATOM   331  N  NE    B ARG   A 1 44  ? -9.733  31.413 4.416  0.50 25.00 ? 41  ARG   A NE    1 
ATOM   332  C  CZ    A ARG   A 1 44  ? -12.852 29.326 3.902  0.50 25.97 ? 41  ARG   A CZ    1 
ATOM   333  C  CZ    B ARG   A 1 44  ? -9.057  31.656 5.532  0.50 26.12 ? 41  ARG   A CZ    1 
ATOM   334  N  NH1   A ARG   A 1 44  ? -12.727 28.447 4.883  0.50 25.16 ? 41  ARG   A NH1   1 
ATOM   335  N  NH1   B ARG   A 1 44  ? -9.089  30.784 6.523  0.50 25.46 ? 41  ARG   A NH1   1 
ATOM   336  N  NH2   A ARG   A 1 44  ? -13.984 29.384 3.233  0.50 24.19 ? 41  ARG   A NH2   1 
ATOM   337  N  NH2   B ARG   A 1 44  ? -8.350  32.764 5.651  0.50 26.96 ? 41  ARG   A NH2   1 
ATOM   338  N  N     . LYS   A 1 45  ? -6.921  27.131 0.871  1.00 20.25 ? 42  LYS   A N     1 
ATOM   339  C  CA    . LYS   A 1 45  ? -6.404  26.803 -0.444 1.00 21.97 ? 42  LYS   A CA    1 
ATOM   340  C  C     . LYS   A 1 45  ? -7.229  25.670 -1.026 1.00 19.49 ? 42  LYS   A C     1 
ATOM   341  O  O     . LYS   A 1 45  ? -7.512  24.711 -0.316 1.00 18.99 ? 42  LYS   A O     1 
ATOM   342  C  CB    . LYS   A 1 45  ? -4.963  26.342 -0.279 1.00 23.55 ? 42  LYS   A CB    1 
ATOM   343  C  CG    . LYS   A 1 45  ? -4.159  26.257 -1.563 1.00 28.83 ? 42  LYS   A CG    1 
ATOM   344  C  CD    . LYS   A 1 45  ? -3.030  25.235 -1.394 1.00 31.05 ? 42  LYS   A CD    1 
ATOM   345  C  CE    . LYS   A 1 45  ? -2.205  25.110 -2.662 1.00 33.67 ? 42  LYS   A CE    1 
ATOM   346  N  NZ    . LYS   A 1 45  ? -0.995  24.273 -2.420 1.00 33.28 ? 42  LYS   A NZ    1 
ATOM   347  N  N     . GLN   A 1 46  ? -7.512  25.744 -2.332 1.00 20.44 ? 43  GLN   A N     1 
ATOM   348  C  CA    . GLN   A 1 46  ? -8.201  24.681 -3.106 1.00 19.87 ? 43  GLN   A CA    1 
ATOM   349  C  C     . GLN   A 1 46  ? -7.149  23.760 -3.738 1.00 19.95 ? 43  GLN   A C     1 
ATOM   350  O  O     . GLN   A 1 46  ? -6.238  24.239 -4.372 1.00 21.47 ? 43  GLN   A O     1 
ATOM   351  C  CB    . GLN   A 1 46  ? -9.011  25.251 -4.276 1.00 24.06 ? 43  GLN   A CB    1 
ATOM   352  C  CG    . GLN   A 1 46  ? -10.467 25.597 -4.004 1.00 28.44 ? 43  GLN   A CG    1 
ATOM   353  C  CD    . GLN   A 1 46  ? -11.163 26.030 -5.275 1.00 28.23 ? 43  GLN   A CD    1 
ATOM   354  O  OE1   . GLN   A 1 46  ? -12.007 26.923 -5.270 1.00 36.55 ? 43  GLN   A OE1   1 
ATOM   355  N  NE2   . GLN   A 1 46  ? -10.807 25.394 -6.379 1.00 26.79 ? 43  GLN   A NE2   1 
ATOM   356  N  N     . VAL   A 1 47  ? -7.330  22.458 -3.579 1.00 17.50 ? 44  VAL   A N     1 
ATOM   357  C  CA    . VAL   A 1 47  ? -6.449  21.436 -4.157 1.00 17.98 ? 44  VAL   A CA    1 
ATOM   358  C  C     . VAL   A 1 47  ? -7.323  20.295 -4.679 1.00 18.67 ? 44  VAL   A C     1 
ATOM   359  O  O     . VAL   A 1 47  ? -8.473  20.193 -4.283 1.00 20.54 ? 44  VAL   A O     1 
ATOM   360  C  CB    . VAL   A 1 47  ? -5.483  20.830 -3.108 1.00 18.96 ? 44  VAL   A CB    1 
ATOM   361  C  CG1   . VAL   A 1 47  ? -4.531  21.878 -2.542 1.00 22.65 ? 44  VAL   A CG1   1 
ATOM   362  C  CG2   . VAL   A 1 47  ? -6.255  20.181 -1.985 1.00 20.20 ? 44  VAL   A CG2   1 
ATOM   363  N  N     . VAL   A 1 48  ? -6.779  19.436 -5.531 1.00 18.00 ? 45  VAL   A N     1 
ATOM   364  C  CA    . VAL   A 1 48  ? -7.527  18.254 -6.011 1.00 17.71 ? 45  VAL   A CA    1 
ATOM   365  C  C     . VAL   A 1 48  ? -6.896  17.003 -5.418 1.00 16.53 ? 45  VAL   A C     1 
ATOM   366  O  O     . VAL   A 1 48  ? -5.686  16.752 -5.534 1.00 16.94 ? 45  VAL   A O     1 
ATOM   367  C  CB    . VAL   A 1 48  ? -7.561  18.162 -7.531 1.00 18.58 ? 45  VAL   A CB    1 
ATOM   368  C  CG1   . VAL   A 1 48  ? -8.284  16.910 -7.981 1.00 19.13 ? 45  VAL   A CG1   1 
ATOM   369  C  CG2   . VAL   A 1 48  ? -8.276  19.363 -8.112 1.00 20.63 ? 45  VAL   A CG2   1 
ATOM   370  N  N     . ILE   A 1 49  ? -7.735  16.223 -4.733 1.00 14.03 ? 46  ILE   A N     1 
ATOM   371  C  CA    . ILE   A 1 49  ? -7.312  15.024 -4.048 1.00 13.98 ? 46  ILE   A CA    1 
ATOM   372  C  C     . ILE   A 1 49  ? -8.316  13.928 -4.425 1.00 13.92 ? 46  ILE   A C     1 
ATOM   373  O  O     . ILE   A 1 49  ? -9.499  14.057 -4.141 1.00 13.20 ? 46  ILE   A O     1 
ATOM   374  C  CB    . ILE   A 1 49  ? -7.315  15.213 -2.540 1.00 14.64 ? 46  ILE   A CB    1 
ATOM   375  C  CG1   . ILE   A 1 49  ? -6.438  16.398 -2.137 1.00 14.78 ? 46  ILE   A CG1   1 
ATOM   376  C  CG2   . ILE   A 1 49  ? -6.873  13.921 -1.839 1.00 13.56 ? 46  ILE   A CG2   1 
ATOM   377  C  CD1   . ILE   A 1 49  ? -6.646  16.838 -0.729 1.00 14.45 ? 46  ILE   A CD1   1 
ATOM   378  N  N     . ASP   A 1 50  ? -7.857  12.851 -5.062 1.00 14.01 ? 47  ASP   A N     1 
ATOM   379  C  CA    . ASP   A 1 50  ? -8.729  11.737 -5.459 1.00 14.46 ? 47  ASP   A CA    1 
ATOM   380  C  C     . ASP   A 1 50  ? -9.920  12.187 -6.309 1.00 14.20 ? 47  ASP   A C     1 
ATOM   381  O  O     . ASP   A 1 50  ? -11.044 11.700 -6.153 1.00 14.59 ? 47  ASP   A O     1 
ATOM   382  C  CB    . ASP   A 1 50  ? -9.225  10.902 -4.248 1.00 14.70 ? 47  ASP   A CB    1 
ATOM   383  C  CG    . ASP   A 1 50  ? -8.090  10.412 -3.376 1.00 14.37 ? 47  ASP   A CG    1 
ATOM   384  O  OD1   . ASP   A 1 50  ? -7.197  9.733  -3.945 1.00 15.92 ? 47  ASP   A OD1   1 
ATOM   385  O  OD2   . ASP   A 1 50  ? -8.056  10.743 -2.177 1.00 15.02 ? 47  ASP   A OD2   1 
ATOM   386  N  N     . GLY   A 1 51  ? -9.649  13.117 -7.204 1.00 14.04 ? 48  GLY   A N     1 
ATOM   387  C  CA    . GLY   A 1 51  ? -10.654 13.635 -8.146 1.00 15.47 ? 48  GLY   A CA    1 
ATOM   388  C  C     . GLY   A 1 51  ? -11.570 14.668 -7.540 1.00 15.08 ? 48  GLY   A C     1 
ATOM   389  O  O     . GLY   A 1 51  ? -12.374 15.191 -8.253 1.00 17.61 ? 48  GLY   A O     1 
ATOM   390  N  N     . GLU   A 1 52  ? -11.440 14.941 -6.249 1.00 15.15 ? 49  GLU   A N     1 
ATOM   391  C  CA    . GLU   A 1 52  ? -12.350 15.907 -5.598 1.00 15.35 ? 49  GLU   A CA    1 
ATOM   392  C  C     . GLU   A 1 52  ? -11.656 17.271 -5.489 1.00 15.50 ? 49  GLU   A C     1 
ATOM   393  O  O     . GLU   A 1 52  ? -10.530 17.297 -5.066 1.00 14.25 ? 49  GLU   A O     1 
ATOM   394  C  CB    . GLU   A 1 52  ? -12.706 15.438 -4.189 1.00 15.21 ? 49  GLU   A CB    1 
ATOM   395  C  CG    . GLU   A 1 52  ? -13.721 16.291 -3.467 1.00 16.30 ? 49  GLU   A CG    1 
ATOM   396  C  CD    . GLU   A 1 52  ? -14.161 15.714 -2.140 1.00 17.61 ? 49  GLU   A CD    1 
ATOM   397  O  OE1   . GLU   A 1 52  ? -13.326 15.370 -1.352 1.00 18.84 ? 49  GLU   A OE1   1 
ATOM   398  O  OE2   . GLU   A 1 52  ? -15.335 15.604 -1.932 1.00 20.76 ? 49  GLU   A OE2   1 
ATOM   399  N  N     . THR   A 1 53  ? -12.340 18.336 -5.898 1.00 16.25 ? 50  THR   A N     1 
ATOM   400  C  CA    . THR   A 1 53  ? -11.800 19.687 -5.646 1.00 16.93 ? 50  THR   A CA    1 
ATOM   401  C  C     . THR   A 1 53  ? -12.111 19.992 -4.187 1.00 17.06 ? 50  THR   A C     1 
ATOM   402  O  O     . THR   A 1 53  ? -13.245 20.023 -3.847 1.00 17.89 ? 50  THR   A O     1 
ATOM   403  C  CB    . THR   A 1 53  ? -12.402 20.724 -6.592 1.00 18.23 ? 50  THR   A CB    1 
ATOM   404  O  OG1   . THR   A 1 53  ? -12.062 20.323 -7.912 1.00 18.16 ? 50  THR   A OG1   1 
ATOM   405  C  CG2   . THR   A 1 53  ? -11.851 22.102 -6.300 1.00 19.31 ? 50  THR   A CG2   1 
ATOM   406  N  N     . CYS   A 1 54  ? -11.069 20.160 -3.387 1.00 16.09 ? 51  CYS   A N     1 
ATOM   407  C  CA    . CYS   A 1 54  ? -11.208 20.287 -1.922 1.00 16.84 ? 51  CYS   A CA    1 
ATOM   408  C  C     . CYS   A 1 54  ? -10.762 21.682 -1.485 1.00 16.95 ? 51  CYS   A C     1 
ATOM   409  O  O     . CYS   A 1 54  ? -9.758  22.134 -1.942 1.00 18.03 ? 51  CYS   A O     1 
ATOM   410  C  CB    . CYS   A 1 54  ? -10.252 19.331 -1.207 1.00 14.61 ? 51  CYS   A CB    1 
ATOM   411  S  SG    . CYS   A 1 54  ? -10.522 17.587 -1.586 1.00 17.82 ? 51  CYS   A SG    1 
ATOM   412  N  N     . LEU   A 1 55  ? -11.542 22.299 -0.613 1.00 17.37 ? 52  LEU   A N     1 
ATOM   413  C  CA    . LEU   A 1 55  ? -11.086 23.564 -0.021 1.00 19.21 ? 52  LEU   A CA    1 
ATOM   414  C  C     . LEU   A 1 55  ? -10.507 23.215 1.350  1.00 17.25 ? 52  LEU   A C     1 
ATOM   415  O  O     . LEU   A 1 55  ? -11.239 22.756 2.155  1.00 18.07 ? 52  LEU   A O     1 
ATOM   416  C  CB    . LEU   A 1 55  ? -12.248 24.555 0.073  1.00 21.51 ? 52  LEU   A CB    1 
ATOM   417  C  CG    . LEU   A 1 55  ? -11.947 25.841 0.833  1.00 23.98 ? 52  LEU   A CG    1 
ATOM   418  C  CD1   . LEU   A 1 55  ? -10.808 26.604 0.194  1.00 24.24 ? 52  LEU   A CD1   1 
ATOM   419  C  CD2   . LEU   A 1 55  ? -13.198 26.693 0.937  1.00 25.80 ? 52  LEU   A CD2   1 
ATOM   420  N  N     . LEU   A 1 56  ? -9.209  23.404 1.508  1.00 16.64 ? 53  LEU   A N     1 
ATOM   421  C  CA    . LEU   A 1 56  ? -8.562  23.142 2.806  1.00 15.99 ? 53  LEU   A CA    1 
ATOM   422  C  C     . LEU   A 1 56  ? -8.584  24.433 3.623  1.00 17.10 ? 53  LEU   A C     1 
ATOM   423  O  O     . LEU   A 1 56  ? -8.211  25.453 3.091  1.00 19.62 ? 53  LEU   A O     1 
ATOM   424  C  CB    . LEU   A 1 56  ? -7.122  22.704 2.582  1.00 16.42 ? 53  LEU   A CB    1 
ATOM   425  C  CG    . LEU   A 1 56  ? -6.894  21.518 1.648  1.00 18.19 ? 53  LEU   A CG    1 
ATOM   426  C  CD1   . LEU   A 1 56  ? -5.447  21.062 1.716  1.00 19.59 ? 53  LEU   A CD1   1 
ATOM   427  C  CD2   . LEU   A 1 56  ? -7.841  20.381 1.954  1.00 18.02 ? 53  LEU   A CD2   1 
ATOM   428  N  N     . ASP   A 1 57  ? -9.024  24.328 4.856  1.00 15.37 ? 54  ASP   A N     1 
ATOM   429  C  CA    . ASP   A 1 57  ? -8.990  25.490 5.770  1.00 16.51 ? 54  ASP   A CA    1 
ATOM   430  C  C     . ASP   A 1 57  ? -8.123  25.017 6.934  1.00 15.74 ? 54  ASP   A C     1 
ATOM   431  O  O     . ASP   A 1 57  ? -8.588  24.253 7.722  1.00 16.28 ? 54  ASP   A O     1 
ATOM   432  C  CB    . ASP   A 1 57  ? -10.395 25.875 6.185  1.00 19.24 ? 54  ASP   A CB    1 
ATOM   433  C  CG    . ASP   A 1 57  ? -10.459 27.134 7.015  1.00 22.26 ? 54  ASP   A CG    1 
ATOM   434  O  OD1   . ASP   A 1 57  ? -9.502  27.440 7.673  1.00 25.69 ? 54  ASP   A OD1   1 
ATOM   435  O  OD2   . ASP   A 1 57  ? -11.482 27.741 6.989  1.00 29.22 ? 54  ASP   A OD2   1 
ATOM   436  N  N     . ILE   A 1 58  ? -6.908  25.532 6.969  1.00 15.39 ? 55  ILE   A N     1 
ATOM   437  C  CA    . ILE   A 1 58  ? -5.904  24.996 7.910  1.00 14.93 ? 55  ILE   A CA    1 
ATOM   438  C  C     . ILE   A 1 58  ? -5.565  26.017 8.984  1.00 15.85 ? 55  ILE   A C     1 
ATOM   439  O  O     . ILE   A 1 58  ? -5.150  27.074 8.651  1.00 16.74 ? 55  ILE   A O     1 
ATOM   440  C  CB    . ILE   A 1 58  ? -4.649  24.648 7.101  1.00 15.83 ? 55  ILE   A CB    1 
ATOM   441  C  CG1   . ILE   A 1 58  ? -4.977  23.628 6.015  1.00 16.68 ? 55  ILE   A CG1   1 
ATOM   442  C  CG2   . ILE   A 1 58  ? -3.520  24.187 7.999  1.00 15.98 ? 55  ILE   A CG2   1 
ATOM   443  C  CD1   . ILE   A 1 58  ? -3.852  23.389 5.071  1.00 18.89 ? 55  ILE   A CD1   1 
ATOM   444  N  N     . LEU   A 1 59  ? -5.722  25.610 10.226 1.00 14.66 ? 56  LEU   A N     1 
ATOM   445  C  CA    . LEU   A 1 59  ? -5.272  26.474 11.352 1.00 15.62 ? 56  LEU   A CA    1 
ATOM   446  C  C     . LEU   A 1 59  ? -3.909  26.031 11.870 1.00 15.67 ? 56  LEU   A C     1 
ATOM   447  O  O     . LEU   A 1 59  ? -3.769  24.912 12.331 1.00 14.48 ? 56  LEU   A O     1 
ATOM   448  C  CB    . LEU   A 1 59  ? -6.291  26.436 12.477 1.00 16.96 ? 56  LEU   A CB    1 
ATOM   449  C  CG    . LEU   A 1 59  ? -5.948  27.266 13.699 1.00 18.41 ? 56  LEU   A CG    1 
ATOM   450  C  CD1   . LEU   A 1 59  ? -5.939  28.753 13.384 1.00 19.88 ? 56  LEU   A CD1   1 
ATOM   451  C  CD2   . LEU   A 1 59  ? -6.951  26.956 14.775 1.00 19.63 ? 56  LEU   A CD2   1 
ATOM   452  N  N     . ASP   A 1 60  ? -2.924  26.930 11.792 1.00 16.05 ? 57  ASP   A N     1 
ATOM   453  C  CA    . ASP   A 1 60  ? -1.578  26.710 12.309 1.00 17.45 ? 57  ASP   A CA    1 
ATOM   454  C  C     . ASP   A 1 60  ? -1.571  27.256 13.727 1.00 18.48 ? 57  ASP   A C     1 
ATOM   455  O  O     . ASP   A 1 60  ? -1.580  28.493 13.935 1.00 20.66 ? 57  ASP   A O     1 
ATOM   456  C  CB    . ASP   A 1 60  ? -0.567  27.423 11.415 1.00 18.75 ? 57  ASP   A CB    1 
ATOM   457  C  CG    . ASP   A 1 60  ? 0.822   27.438 11.982 1.00 19.60 ? 57  ASP   A CG    1 
ATOM   458  O  OD1   . ASP   A 1 60  ? 1.175   26.537 12.762 1.00 19.13 ? 57  ASP   A OD1   1 
ATOM   459  O  OD2   . ASP   A 1 60  ? 1.563   28.369 11.630 1.00 22.40 ? 57  ASP   A OD2   1 
ATOM   460  N  N     . THR   A 1 61  ? -1.630  26.354 14.704 1.00 18.62 ? 58  THR   A N     1 
ATOM   461  C  CA    . THR   A 1 61  ? -1.798  26.772 16.080 1.00 19.25 ? 58  THR   A CA    1 
ATOM   462  C  C     . THR   A 1 61  ? -0.473  27.207 16.688 1.00 19.74 ? 58  THR   A C     1 
ATOM   463  O  O     . THR   A 1 61  ? 0.605   26.706 16.333 1.00 19.72 ? 58  THR   A O     1 
ATOM   464  C  CB    . THR   A 1 61  ? -2.441  25.693 16.997 1.00 17.86 ? 58  THR   A CB    1 
ATOM   465  O  OG1   . THR   A 1 61  ? -1.562  24.585 17.160 1.00 16.30 ? 58  THR   A OG1   1 
ATOM   466  C  CG2   . THR   A 1 61  ? -3.798  25.225 16.433 1.00 17.91 ? 58  THR   A CG2   1 
ATOM   467  N  N     . ALA   A 1 62  ? -0.581  28.144 17.617 1.00 23.09 ? 59  ALA   A N     1 
ATOM   468  C  CA    . ALA   A 1 62  ? 0.586   28.714 18.305 1.00 23.22 ? 59  ALA   A CA    1 
ATOM   469  C  C     . ALA   A 1 62  ? 0.574   28.179 19.733 1.00 22.47 ? 59  ALA   A C     1 
ATOM   470  O  O     . ALA   A 1 62  ? 1.242   27.230 20.023 1.00 22.83 ? 59  ALA   A O     1 
ATOM   471  C  CB    . ALA   A 1 62  ? 0.524   30.233 18.297 1.00 25.93 ? 59  ALA   A CB    1 
ATOM   472  N  N     . GLY   A 1 63  ? -0.169  28.792 20.633 1.00 23.51 ? 60  GLY   A N     1 
ATOM   473  C  CA    . GLY   A 1 63  ? -0.145  28.305 22.020 1.00 24.87 ? 60  GLY   A CA    1 
ATOM   474  C  C     . GLY   A 1 63  ? -0.742  26.928 22.161 1.00 26.02 ? 60  GLY   A C     1 
ATOM   475  O  O     . GLY   A 1 63  ? -1.705  26.673 21.494 1.00 25.73 ? 60  GLY   A O     1 
ATOM   476  N  N     . GLN   A 1 64  ? -0.167  26.081 23.006 1.00 25.73 ? 61  GLN   A N     1 
ATOM   477  C  CA    . GLN   A 1 64  ? -0.703  24.706 23.168 1.00 26.60 ? 61  GLN   A CA    1 
ATOM   478  C  C     . GLN   A 1 64  ? -1.283  24.550 24.580 1.00 28.85 ? 61  GLN   A C     1 
ATOM   479  O  O     . GLN   A 1 64  ? -1.476  23.435 24.997 1.00 29.14 ? 61  GLN   A O     1 
ATOM   480  C  CB    . GLN   A 1 64  ? 0.346   23.633 22.829 1.00 24.91 ? 61  GLN   A CB    1 
ATOM   481  C  CG    . GLN   A 1 64  ? 1.013   23.755 21.465 1.00 23.13 ? 61  GLN   A CG    1 
ATOM   482  C  CD    . GLN   A 1 64  ? 0.117   23.619 20.259 1.00 21.66 ? 61  GLN   A CD    1 
ATOM   483  O  OE1   . GLN   A 1 64  ? -0.513  22.613 20.050 1.00 20.38 ? 61  GLN   A OE1   1 
ATOM   484  N  NE2   . GLN   A 1 64  ? 0.122   24.643 19.435 1.00 21.91 ? 61  GLN   A NE2   1 
ATOM   485  N  N     . GLU   A 1 65  ? -1.616  25.672 25.229 1.00 31.37 ? 62  GLU   A N     1 
ATOM   486  C  CA    . GLU   A 1 65  ? -2.115  25.705 26.639 1.00 32.12 ? 62  GLU   A CA    1 
ATOM   487  C  C     . GLU   A 1 65  ? -3.314  24.785 26.894 1.00 31.90 ? 62  GLU   A C     1 
ATOM   488  O  O     . GLU   A 1 65  ? -4.253  24.785 26.146 1.00 31.92 ? 62  GLU   A O     1 
ATOM   489  C  CB    . GLU   A 1 65  ? -2.471  27.127 27.080 1.00 36.78 ? 62  GLU   A CB    1 
ATOM   490  C  CG    . GLU   A 1 65  ? -1.448  28.192 26.703 1.00 41.53 ? 62  GLU   A CG    1 
ATOM   491  C  CD    . GLU   A 1 65  ? -1.684  29.006 25.428 1.00 43.60 ? 62  GLU   A CD    1 
ATOM   492  O  OE1   . GLU   A 1 65  ? -2.606  28.707 24.672 1.00 43.20 ? 62  GLU   A OE1   1 
ATOM   493  O  OE2   . GLU   A 1 65  ? -0.941  29.935 25.201 1.00 44.40 ? 62  GLU   A OE2   1 
ATOM   494  N  N     . GLU   A 1 66  ? -3.251  24.065 28.004 1.00 32.94 ? 63  GLU   A N     1 
ATOM   495  C  CA    . GLU   A 1 66  ? -4.351  23.234 28.487 1.00 35.15 ? 63  GLU   A CA    1 
ATOM   496  C  C     . GLU   A 1 66  ? -5.625  24.059 28.640 1.00 30.88 ? 63  GLU   A C     1 
ATOM   497  O  O     . GLU   A 1 66  ? -6.703  23.657 28.168 1.00 32.19 ? 63  GLU   A O     1 
ATOM   498  C  CB    . GLU   A 1 66  ? -3.960  22.600 29.828 1.00 38.38 ? 63  GLU   A CB    1 
ATOM   499  C  CG    . GLU   A 1 66  ? -5.045  21.774 30.514 1.00 43.73 ? 63  GLU   A CG    1 
ATOM   500  C  CD    . GLU   A 1 66  ? -5.312  20.433 29.857 1.00 46.25 ? 63  GLU   A CD    1 
ATOM   501  O  OE1   . GLU   A 1 66  ? -4.527  20.005 28.970 1.00 50.31 ? 63  GLU   A OE1   1 
ATOM   502  O  OE2   . GLU   A 1 66  ? -6.325  19.809 30.238 1.00 50.74 ? 63  GLU   A OE2   1 
ATOM   503  N  N     . TYR   A 1 67  ? -5.500  25.210 29.296 1.00 28.28 ? 64  TYR   A N     1 
ATOM   504  C  CA    . TYR   A 1 67  ? -6.649  26.024 29.645 1.00 27.15 ? 64  TYR   A CA    1 
ATOM   505  C  C     . TYR   A 1 67  ? -6.764  27.226 28.703 1.00 26.71 ? 64  TYR   A C     1 
ATOM   506  O  O     . TYR   A 1 67  ? -6.111  28.258 28.905 1.00 27.73 ? 64  TYR   A O     1 
ATOM   507  C  CB    . TYR   A 1 67  ? -6.551  26.458 31.108 1.00 27.70 ? 64  TYR   A CB    1 
ATOM   508  C  CG    . TYR   A 1 67  ? -6.541  25.261 32.030 1.00 27.87 ? 64  TYR   A CG    1 
ATOM   509  C  CD1   . TYR   A 1 67  ? -7.620  24.383 32.052 1.00 28.11 ? 64  TYR   A CD1   1 
ATOM   510  C  CD2   . TYR   A 1 67  ? -5.443  24.965 32.836 1.00 28.82 ? 64  TYR   A CD2   1 
ATOM   511  C  CE1   . TYR   A 1 67  ? -7.621  23.266 32.869 1.00 29.20 ? 64  TYR   A CE1   1 
ATOM   512  C  CE2   . TYR   A 1 67  ? -5.439  23.860 33.665 1.00 29.62 ? 64  TYR   A CE2   1 
ATOM   513  C  CZ    . TYR   A 1 67  ? -6.528  23.005 33.674 1.00 29.17 ? 64  TYR   A CZ    1 
ATOM   514  O  OH    . TYR   A 1 67  ? -6.552  21.889 34.490 1.00 30.88 ? 64  TYR   A OH    1 
ATOM   515  N  N     . SER   A 1 68  ? -7.590  27.070 27.668 1.00 23.20 ? 65  SER   A N     1 
ATOM   516  C  CA    . SER   A 1 68  ? -7.710  28.060 26.626 1.00 22.14 ? 65  SER   A CA    1 
ATOM   517  C  C     . SER   A 1 68  ? -9.083  27.935 25.956 1.00 21.69 ? 65  SER   A C     1 
ATOM   518  O  O     . SER   A 1 68  ? -9.349  26.949 25.266 1.00 20.50 ? 65  SER   A O     1 
ATOM   519  C  CB    . SER   A 1 68  ? -6.636  27.847 25.565 1.00 22.07 ? 65  SER   A CB    1 
ATOM   520  O  OG    . SER   A 1 68  ? -6.895  28.724 24.481 1.00 22.53 ? 65  SER   A OG    1 
ATOM   521  N  N     . ALA   A 1 69  ? -9.942  28.925 26.168 1.00 22.86 ? 66  ALA   A N     1 
ATOM   522  C  CA    . ALA   A 1 69  ? -11.254 28.916 25.536 1.00 24.51 ? 66  ALA   A CA    1 
ATOM   523  C  C     . ALA   A 1 69  ? -11.134 28.863 24.025 1.00 24.27 ? 66  ALA   A C     1 
ATOM   524  O  O     . ALA   A 1 69  ? -11.955 28.224 23.367 1.00 24.10 ? 66  ALA   A O     1 
ATOM   525  C  CB    . ALA   A 1 69  ? -12.046 30.134 25.943 1.00 25.91 ? 66  ALA   A CB    1 
ATOM   526  N  N     . MET   A 1 70  ? -10.128 29.533 23.478 1.00 24.88 ? 67  MET   A N     1 
ATOM   527  C  CA    . MET   A 1 70  ? -9.949  29.569 22.032 1.00 27.67 ? 67  MET   A CA    1 
ATOM   528  C  C     . MET   A 1 70  ? -9.546  28.224 21.469 1.00 25.49 ? 67  MET   A C     1 
ATOM   529  O  O     . MET   A 1 70  ? -10.082 27.808 20.423 1.00 23.46 ? 67  MET   A O     1 
ATOM   530  C  CB    . MET   A 1 70  ? -8.915  30.620 21.610 1.00 32.81 ? 67  MET   A CB    1 
ATOM   531  C  CG    . MET   A 1 70  ? -8.983  30.952 20.121 1.00 36.43 ? 67  MET   A CG    1 
ATOM   532  S  SD    . MET   A 1 70  ? -10.616 31.573 19.619 1.00 49.11 ? 67  MET   A SD    1 
ATOM   533  C  CE    . MET   A 1 70  ? -11.033 30.402 18.321 1.00 45.87 ? 67  MET   A CE    1 
ATOM   534  N  N     . ARG   A 1 71  ? -8.593  27.563 22.129 1.00 23.01 ? 68  ARG   A N     1 
ATOM   535  C  CA    . ARG   A 1 71  ? -8.214  26.183 21.785 1.00 21.88 ? 68  ARG   A CA    1 
ATOM   536  C  C     . ARG   A 1 71  ? -9.404  25.233 21.859 1.00 20.82 ? 68  ARG   A C     1 
ATOM   537  O  O     . ARG   A 1 71  ? -9.606  24.386 20.985 1.00 20.32 ? 68  ARG   A O     1 
ATOM   538  C  CB    . ARG   A 1 71  ? -7.077  25.675 22.683 1.00 22.69 ? 68  ARG   A CB    1 
ATOM   539  C  CG    . ARG   A 1 71  ? -6.401  24.399 22.204 1.00 25.14 ? 68  ARG   A CG    1 
ATOM   540  C  CD    . ARG   A 1 71  ? -4.956  24.381 22.697 1.00 28.30 ? 68  ARG   A CD    1 
ATOM   541  N  NE    . ARG   A 1 71  ? -4.287  23.081 22.655 1.00 30.03 ? 68  ARG   A NE    1 
ATOM   542  C  CZ    . ARG   A 1 71  ? -3.510  22.635 21.659 1.00 32.23 ? 68  ARG   A CZ    1 
ATOM   543  N  NH1   . ARG   A 1 71  ? -3.314  23.336 20.542 1.00 31.51 ? 68  ARG   A NH1   1 
ATOM   544  N  NH2   . ARG   A 1 71  ? -2.916  21.459 21.783 1.00 36.20 ? 68  ARG   A NH2   1 
ATOM   545  N  N     . ASP   A 1 72  ? -10.238 25.394 22.874 1.00 21.71 ? 69  ASP   A N     1 
ATOM   546  C  CA    . ASP   A 1 72  ? -11.439 24.531 22.907 1.00 22.82 ? 69  ASP   A CA    1 
ATOM   547  C  C     . ASP   A 1 72  ? -12.316 24.830 21.679 1.00 22.78 ? 69  ASP   A C     1 
ATOM   548  O  O     . ASP   A 1 72  ? -12.828 23.906 21.096 1.00 22.50 ? 69  ASP   A O     1 
ATOM   549  C  CB    . ASP   A 1 72  ? -12.256 24.746 24.173 1.00 26.81 ? 69  ASP   A CB    1 
ATOM   550  C  CG    . ASP   A 1 72  ? -11.623 24.190 25.431 1.00 32.40 ? 69  ASP   A CG    1 
ATOM   551  O  OD1   . ASP   A 1 72  ? -10.612 23.470 25.345 1.00 33.72 ? 69  ASP   A OD1   1 
ATOM   552  O  OD2   . ASP   A 1 72  ? -12.116 24.558 26.509 1.00 41.61 ? 69  ASP   A OD2   1 
ATOM   553  N  N     . GLN   A 1 73  ? -12.447 26.093 21.308 1.00 22.90 ? 70  GLN   A N     1 
ATOM   554  C  CA    . GLN   A 1 73  ? -13.349 26.417 20.182 1.00 24.97 ? 70  GLN   A CA    1 
ATOM   555  C  C     . GLN   A 1 73  ? -12.760 25.833 18.897 1.00 23.90 ? 70  GLN   A C     1 
ATOM   556  O  O     . GLN   A 1 73  ? -13.515 25.246 18.154 1.00 22.80 ? 70  GLN   A O     1 
ATOM   557  C  CB    . GLN   A 1 73  ? -13.608 27.917 20.067 1.00 29.51 ? 70  GLN   A CB    1 
ATOM   558  C  CG    . GLN   A 1 73  ? -14.788 28.292 19.171 1.00 33.19 ? 70  GLN   A CG    1 
ATOM   559  C  CD    . GLN   A 1 73  ? -15.984 27.390 19.340 1.00 38.45 ? 70  GLN   A CD    1 
ATOM   560  O  OE1   . GLN   A 1 73  ? -16.502 27.194 20.437 1.00 43.35 ? 70  GLN   A OE1   1 
ATOM   561  N  NE2   . GLN   A 1 73  ? -16.440 26.826 18.238 1.00 41.00 ? 70  GLN   A NE2   1 
ATOM   562  N  N     . TYR   A 1 74  ? -11.472 26.033 18.663 1.00 21.46 ? 71  TYR   A N     1 
ATOM   563  C  CA    . TYR   A 1 74  ? -10.881 25.473 17.424 1.00 22.42 ? 71  TYR   A CA    1 
ATOM   564  C  C     . TYR   A 1 74  ? -10.873 23.942 17.406 1.00 20.50 ? 71  TYR   A C     1 
ATOM   565  O  O     . TYR   A 1 74  ? -10.884 23.380 16.341 1.00 20.80 ? 71  TYR   A O     1 
ATOM   566  C  CB    . TYR   A 1 74  ? -9.658  26.236 16.937 1.00 22.90 ? 71  TYR   A CB    1 
ATOM   567  C  CG    . TYR   A 1 74  ? -8.381  26.060 17.703 1.00 22.68 ? 71  TYR   A CG    1 
ATOM   568  C  CD1   . TYR   A 1 74  ? -7.814  24.818 17.900 1.00 21.57 ? 71  TYR   A CD1   1 
ATOM   569  C  CD2   . TYR   A 1 74  ? -7.698  27.168 18.146 1.00 24.35 ? 71  TYR   A CD2   1 
ATOM   570  C  CE1   . TYR   A 1 74  ? -6.607  24.671 18.549 1.00 23.37 ? 71  TYR   A CE1   1 
ATOM   571  C  CE2   . TYR   A 1 74  ? -6.489  27.039 18.788 1.00 23.98 ? 71  TYR   A CE2   1 
ATOM   572  C  CZ    . TYR   A 1 74  ? -5.943  25.794 18.997 1.00 23.63 ? 71  TYR   A CZ    1 
ATOM   573  O  OH    . TYR   A 1 74  ? -4.754  25.687 19.629 1.00 24.75 ? 71  TYR   A OH    1 
ATOM   574  N  N     . MET   A 1 75  ? -10.760 23.299 18.548 1.00 19.09 ? 72  MET   A N     1 
ATOM   575  C  CA    . MET   A 1 75  ? -10.860 21.827 18.528 1.00 20.15 ? 72  MET   A CA    1 
ATOM   576  C  C     . MET   A 1 75  ? -12.312 21.443 18.212 1.00 22.18 ? 72  MET   A C     1 
ATOM   577  O  O     . MET   A 1 75  ? -12.486 20.468 17.540 1.00 21.41 ? 72  MET   A O     1 
ATOM   578  C  CB    . MET   A 1 75  ? -10.373 21.187 19.826 1.00 20.44 ? 72  MET   A CB    1 
ATOM   579  C  CG    . MET   A 1 75  ? -8.905  21.396 19.999 1.00 21.35 ? 72  MET   A CG    1 
ATOM   580  S  SD    . MET   A 1 75  ? -8.217  20.607 21.425 1.00 22.74 ? 72  MET   A SD    1 
ATOM   581  C  CE    . MET   A 1 75  ? -6.489  20.676 20.959 1.00 25.09 ? 72  MET   A CE    1 
ATOM   582  N  N     . ARG   A 1 76  ? -13.295 22.204 18.695 1.00 20.78 ? 73  ARG   A N     1 
ATOM   583  C  CA    . ARG   A 1 76  ? -14.687 21.959 18.307 1.00 21.72 ? 73  ARG   A CA    1 
ATOM   584  C  C     . ARG   A 1 76  ? -14.945 22.127 16.803 1.00 21.08 ? 73  ARG   A C     1 
ATOM   585  O  O     . ARG   A 1 76  ? -15.623 21.295 16.184 1.00 21.46 ? 73  ARG   A O     1 
ATOM   586  C  CB    . ARG   A 1 76  ? -15.656 22.823 19.139 1.00 24.15 ? 73  ARG   A CB    1 
ATOM   587  C  CG    . ARG   A 1 76  ? -15.809 22.294 20.555 1.00 27.99 ? 73  ARG   A CG    1 
ATOM   588  C  CD    . ARG   A 1 76  ? -16.999 22.878 21.288 1.00 33.54 ? 73  ARG   A CD    1 
ATOM   589  N  NE    . ARG   A 1 76  ? -16.815 24.290 21.613 1.00 38.61 ? 73  ARG   A NE    1 
ATOM   590  C  CZ    . ARG   A 1 76  ? -16.216 24.770 22.703 1.00 40.31 ? 73  ARG   A CZ    1 
ATOM   591  N  NH1   . ARG   A 1 76  ? -15.699 23.962 23.634 1.00 43.82 ? 73  ARG   A NH1   1 
ATOM   592  N  NH2   . ARG   A 1 76  ? -16.139 26.087 22.862 1.00 41.95 ? 73  ARG   A NH2   1 
ATOM   593  N  N     . THR   A 1 77  ? -14.371 23.166 16.216 1.00 19.68 ? 74  THR   A N     1 
ATOM   594  C  CA    . THR   A 1 77  ? -14.595 23.528 14.815 1.00 20.78 ? 74  THR   A CA    1 
ATOM   595  C  C     . THR   A 1 77  ? -13.762 22.653 13.877 1.00 20.08 ? 74  THR   A C     1 
ATOM   596  O  O     . THR   A 1 77  ? -14.226 22.284 12.797 1.00 19.36 ? 74  THR   A O     1 
ATOM   597  C  CB    . THR   A 1 77  ? -14.279 25.018 14.564 1.00 23.49 ? 74  THR   A CB    1 
ATOM   598  O  OG1   . THR   A 1 77  ? -15.170 25.809 15.370 1.00 26.40 ? 74  THR   A OG1   1 
ATOM   599  C  CG2   . THR   A 1 77  ? -14.468 25.374 13.093 1.00 23.74 ? 74  THR   A CG2   1 
ATOM   600  N  N     . GLY   A 1 78  ? -12.553 22.297 14.297 1.00 18.08 ? 75  GLY   A N     1 
ATOM   601  C  CA    . GLY   A 1 78  ? -11.656 21.489 13.447 1.00 17.15 ? 75  GLY   A CA    1 
ATOM   602  C  C     . GLY   A 1 78  ? -12.206 20.095 13.175 1.00 16.29 ? 75  GLY   A C     1 
ATOM   603  O  O     . GLY   A 1 78  ? -12.774 19.470 14.048 1.00 19.62 ? 75  GLY   A O     1 
ATOM   604  N  N     . GLU   A 1 79  ? -11.999 19.602 11.957 1.00 14.85 ? 76  GLU   A N     1 
ATOM   605  C  CA    . GLU   A 1 79  ? -12.482 18.270 11.592 1.00 15.26 ? 76  GLU   A CA    1 
ATOM   606  C  C     . GLU   A 1 79  ? -11.398 17.207 11.655 1.00 13.91 ? 76  GLU   A C     1 
ATOM   607  O  O     . GLU   A 1 79  ? -11.690 16.043 11.956 1.00 15.34 ? 76  GLU   A O     1 
ATOM   608  C  CB    . GLU   A 1 79  ? -13.093 18.326 10.202 1.00 16.14 ? 76  GLU   A CB    1 
ATOM   609  C  CG    . GLU   A 1 79  ? -14.364 19.164 10.136 1.00 17.73 ? 76  GLU   A CG    1 
ATOM   610  C  CD    . GLU   A 1 79  ? -14.876 19.281 8.716  1.00 22.28 ? 76  GLU   A CD    1 
ATOM   611  O  OE1   . GLU   A 1 79  ? -14.129 19.729 7.818  1.00 20.92 ? 76  GLU   A OE1   1 
ATOM   612  O  OE2   . GLU   A 1 79  ? -16.033 18.850 8.477  1.00 28.65 ? 76  GLU   A OE2   1 
ATOM   613  N  N     . GLY   A 1 80  ? -10.158 17.586 11.337 1.00 12.08 ? 77  GLY   A N     1 
ATOM   614  C  CA    . GLY   A 1 80  ? -9.048  16.675 11.444 1.00 12.14 ? 77  GLY   A CA    1 
ATOM   615  C  C     . GLY   A 1 80  ? -7.838  17.358 12.025 1.00 10.95 ? 77  GLY   A C     1 
ATOM   616  O  O     . GLY   A 1 80  ? -7.677  18.576 11.881 1.00 12.21 ? 77  GLY   A O     1 
ATOM   617  N  N     . PHE   A 1 81  ? -6.972  16.548 12.643 1.00 11.24 ? 78  PHE   A N     1 
ATOM   618  C  CA    . PHE   A 1 81  ? -5.826  17.062 13.431 1.00 11.41 ? 78  PHE   A CA    1 
ATOM   619  C  C     . PHE   A 1 81  ? -4.513  16.437 12.955 1.00 11.50 ? 78  PHE   A C     1 
ATOM   620  O  O     . PHE   A 1 81  ? -4.368  15.207 12.919 1.00 12.34 ? 78  PHE   A O     1 
ATOM   621  C  CB    . PHE   A 1 81  ? -6.110  16.786 14.906 1.00 12.27 ? 78  PHE   A CB    1 
ATOM   622  C  CG    . PHE   A 1 81  ? -7.364  17.482 15.366 1.00 12.45 ? 78  PHE   A CG    1 
ATOM   623  C  CD1   . PHE   A 1 81  ? -8.596  16.916 15.168 1.00 13.80 ? 78  PHE   A CD1   1 
ATOM   624  C  CD2   . PHE   A 1 81  ? -7.304  18.746 15.907 1.00 13.22 ? 78  PHE   A CD2   1 
ATOM   625  C  CE1   . PHE   A 1 81  ? -9.741  17.587 15.478 1.00 13.78 ? 78  PHE   A CE1   1 
ATOM   626  C  CE2   . PHE   A 1 81  ? -8.458  19.449 16.211 1.00 14.33 ? 78  PHE   A CE2   1 
ATOM   627  C  CZ    . PHE   A 1 81  ? -9.689  18.852 16.031 1.00 14.15 ? 78  PHE   A CZ    1 
ATOM   628  N  N     . LEU   A 1 82  ? -3.566  17.299 12.620 1.00 11.14 ? 79  LEU   A N     1 
ATOM   629  C  CA    . LEU   A 1 82  ? -2.206  16.856 12.268 1.00 12.48 ? 79  LEU   A CA    1 
ATOM   630  C  C     . LEU   A 1 82  ? -1.435  16.997 13.574 1.00 13.92 ? 79  LEU   A C     1 
ATOM   631  O  O     . LEU   A 1 82  ? -1.320  18.090 14.007 1.00 13.35 ? 79  LEU   A O     1 
ATOM   632  C  CB    . LEU   A 1 82  ? -1.634  17.814 11.222 1.00 15.51 ? 79  LEU   A CB    1 
ATOM   633  C  CG    . LEU   A 1 82  ? -0.674  17.192 10.231 1.00 17.00 ? 79  LEU   A CG    1 
ATOM   634  C  CD1   . LEU   A 1 82  ? -1.401  16.155 9.383  1.00 17.27 ? 79  LEU   A CD1   1 
ATOM   635  C  CD2   . LEU   A 1 82  ? -0.010  18.261 9.379  1.00 16.17 ? 79  LEU   A CD2   1 
ATOM   636  N  N     . CYS   A 1 83  ? -1.033  15.884 14.164 1.00 13.29 ? 80  CYS   A N     1 
ATOM   637  C  CA    . CYS   A 1 83  ? -0.331  15.863 15.468 1.00 13.77 ? 80  CYS   A CA    1 
ATOM   638  C  C     . CYS   A 1 83  ? 1.160   15.721 15.180 1.00 13.57 ? 80  CYS   A C     1 
ATOM   639  O  O     . CYS   A 1 83  ? 1.556   14.676 14.848 1.00 14.21 ? 80  CYS   A O     1 
ATOM   640  C  CB    . CYS   A 1 83  ? -0.863  14.740 16.346 1.00 15.26 ? 80  CYS   A CB    1 
ATOM   641  S  SG    . CYS   A 1 83  ? -2.587  15.059 16.821 1.00 20.17 ? 80  CYS   A SG    1 
ATOM   642  N  N     . VAL   A 1 84  ? 1.898   16.809 15.346 1.00 12.39 ? 81  VAL   A N     1 
ATOM   643  C  CA    . VAL   A 1 84  ? 3.304   16.855 14.883 1.00 12.49 ? 81  VAL   A CA    1 
ATOM   644  C  C     . VAL   A 1 84  ? 4.280   16.826 16.047 1.00 12.05 ? 81  VAL   A C     1 
ATOM   645  O  O     . VAL   A 1 84  ? 4.083   17.514 16.989 1.00 12.18 ? 81  VAL   A O     1 
ATOM   646  C  CB    . VAL   A 1 84  ? 3.550   18.138 14.078 1.00 12.29 ? 81  VAL   A CB    1 
ATOM   647  C  CG1   . VAL   A 1 84  ? 4.904   18.153 13.401 1.00 11.82 ? 81  VAL   A CG1   1 
ATOM   648  C  CG2   . VAL   A 1 84  ? 2.456   18.368 13.055 1.00 12.23 ? 81  VAL   A CG2   1 
ATOM   649  N  N     . PHE   A 1 85  ? 5.264   15.960 15.899 1.00 11.39 ? 82  PHE   A N     1 
ATOM   650  C  CA    . PHE   A 1 85  ? 6.445   15.950 16.788 1.00 12.10 ? 82  PHE   A CA    1 
ATOM   651  C  C     . PHE   A 1 85  ? 7.692   16.083 15.892 1.00 13.03 ? 82  PHE   A C     1 
ATOM   652  O  O     . PHE   A 1 85  ? 7.604   16.045 14.710 1.00 13.06 ? 82  PHE   A O     1 
ATOM   653  C  CB    . PHE   A 1 85  ? 6.478   14.693 17.660 1.00 12.49 ? 82  PHE   A CB    1 
ATOM   654  C  CG    . PHE   A 1 85  ? 6.782   13.413 16.943 1.00 12.13 ? 82  PHE   A CG    1 
ATOM   655  C  CD1   . PHE   A 1 85  ? 5.770   12.660 16.391 1.00 11.83 ? 82  PHE   A CD1   1 
ATOM   656  C  CD2   . PHE   A 1 85  ? 8.069   12.926 16.879 1.00 12.69 ? 82  PHE   A CD2   1 
ATOM   657  C  CE1   . PHE   A 1 85  ? 6.061   11.496 15.718 1.00 11.59 ? 82  PHE   A CE1   1 
ATOM   658  C  CE2   . PHE   A 1 85  ? 8.354   11.754 16.205 1.00 11.91 ? 82  PHE   A CE2   1 
ATOM   659  C  CZ    . PHE   A 1 85  ? 7.345   11.050 15.605 1.00 12.11 ? 82  PHE   A CZ    1 
ATOM   660  N  N     . ALA   A 1 86  ? 8.831   16.315 16.518 1.00 13.26 ? 83  ALA   A N     1 
ATOM   661  C  CA    . ALA   A 1 86  ? 10.078  16.341 15.767 1.00 14.52 ? 83  ALA   A CA    1 
ATOM   662  C  C     . ALA   A 1 86  ? 10.889  15.120 16.096 1.00 14.16 ? 83  ALA   A C     1 
ATOM   663  O  O     . ALA   A 1 86  ? 10.989  14.712 17.280 1.00 14.86 ? 83  ALA   A O     1 
ATOM   664  C  CB    . ALA   A 1 86  ? 10.860  17.601 16.074 1.00 14.34 ? 83  ALA   A CB    1 
ATOM   665  N  N     . ILE   A 1 87  ? 11.469  14.532 15.051 1.00 13.85 ? 84  ILE   A N     1 
ATOM   666  C  CA    . ILE   A 1 87  ? 12.143  13.249 15.235 1.00 13.45 ? 84  ILE   A CA    1 
ATOM   667  C  C     . ILE   A 1 87  ? 13.411  13.356 16.095 1.00 14.47 ? 84  ILE   A C     1 
ATOM   668  O  O     . ILE   A 1 87  ? 13.955  12.338 16.502 1.00 14.95 ? 84  ILE   A O     1 
ATOM   669  C  CB    . ILE   A 1 87  ? 12.495  12.531 13.919 1.00 13.91 ? 84  ILE   A CB    1 
ATOM   670  C  CG1   . ILE   A 1 87  ? 13.516  13.336 13.121 1.00 15.52 ? 84  ILE   A CG1   1 
ATOM   671  C  CG2   . ILE   A 1 87  ? 11.234  12.223 13.125 1.00 13.45 ? 84  ILE   A CG2   1 
ATOM   672  C  CD1   . ILE   A 1 87  ? 14.233  12.483 12.115 1.00 17.61 ? 84  ILE   A CD1   1 
ATOM   673  N  N     . ASN   A 1 88  ? 13.869  14.589 16.347 1.00 14.17 ? 85  ASN   A N     1 
ATOM   674  C  CA    . ASN   A 1 88  ? 15.020  14.847 17.208 1.00 16.33 ? 85  ASN   A CA    1 
ATOM   675  C  C     . ASN   A 1 88  ? 14.632  15.428 18.560 1.00 17.43 ? 85  ASN   A C     1 
ATOM   676  O  O     . ASN   A 1 88  ? 15.514  15.936 19.270 1.00 18.88 ? 85  ASN   A O     1 
ATOM   677  C  CB    . ASN   A 1 88  ? 16.018  15.799 16.527 1.00 16.21 ? 85  ASN   A CB    1 
ATOM   678  C  CG    . ASN   A 1 88  ? 15.470  17.206 16.369 1.00 17.50 ? 85  ASN   A CG    1 
ATOM   679  O  OD1   . ASN   A 1 88  ? 14.273  17.396 16.195 1.00 16.91 ? 85  ASN   A OD1   1 
ATOM   680  N  ND2   . ASN   A 1 88  ? 16.337  18.203 16.450 1.00 19.16 ? 85  ASN   A ND2   1 
ATOM   681  N  N     . ASN   A 1 89  ? 13.361  15.290 18.960 1.00 16.46 ? 86  ASN   A N     1 
ATOM   682  C  CA    . ASN   A 1 89  ? 12.890  15.891 20.227 1.00 17.95 ? 86  ASN   A CA    1 
ATOM   683  C  C     . ASN   A 1 89  ? 11.988  14.855 20.898 1.00 17.40 ? 86  ASN   A C     1 
ATOM   684  O  O     . ASN   A 1 89  ? 10.818  14.749 20.575 1.00 16.24 ? 86  ASN   A O     1 
ATOM   685  C  CB    . ASN   A 1 89  ? 12.162  17.224 19.961 1.00 18.62 ? 86  ASN   A CB    1 
ATOM   686  C  CG    . ASN   A 1 89  ? 11.554  17.876 21.214 1.00 22.02 ? 86  ASN   A CG    1 
ATOM   687  O  OD1   . ASN   A 1 89  ? 11.422  17.291 22.246 1.00 21.15 ? 86  ASN   A OD1   1 
ATOM   688  N  ND2   . ASN   A 1 89  ? 11.127  19.124 21.063 1.00 26.81 ? 86  ASN   A ND2   1 
ATOM   689  N  N     . THR   A 1 90  ? 12.540  14.061 21.810 1.00 18.25 ? 87  THR   A N     1 
ATOM   690  C  CA    . THR   A 1 90  ? 11.744  12.982 22.421 1.00 18.71 ? 87  THR   A CA    1 
ATOM   691  C  C     . THR   A 1 90  ? 10.546  13.527 23.213 1.00 17.55 ? 87  THR   A C     1 
ATOM   692  O  O     . THR   A 1 90  ? 9.448   12.953 23.209 1.00 17.40 ? 87  THR   A O     1 
ATOM   693  C  CB    . THR   A 1 90  ? 12.639  12.074 23.282 1.00 21.41 ? 87  THR   A CB    1 
ATOM   694  O  OG1   . THR   A 1 90  ? 13.581  11.399 22.427 1.00 23.23 ? 87  THR   A OG1   1 
ATOM   695  C  CG2   . THR   A 1 90  ? 11.828  11.047 24.027 1.00 22.56 ? 87  THR   A CG2   1 
ATOM   696  N  N     . LYS   A 1 91  ? 10.751  14.634 23.908 1.00 17.71 ? 88  LYS   A N     1 
ATOM   697  C  CA    . LYS   A 1 91  ? 9.673   15.281 24.669 1.00 19.49 ? 88  LYS   A CA    1 
ATOM   698  C  C     . LYS   A 1 91  ? 8.465   15.609 23.776 1.00 17.25 ? 88  LYS   A C     1 
ATOM   699  O  O     . LYS   A 1 91  ? 7.324   15.401 24.157 1.00 18.04 ? 88  LYS   A O     1 
ATOM   700  C  CB    . LYS   A 1 91  ? 10.184  16.549 25.354 1.00 21.71 ? 88  LYS   A CB    1 
ATOM   701  C  CG    . LYS   A 1 91  ? 9.117   17.253 26.172 1.00 26.79 ? 88  LYS   A CG    1 
ATOM   702  C  CD    . LYS   A 1 91  ? 9.650   18.418 26.991 1.00 32.04 ? 88  LYS   A CD    1 
ATOM   703  C  CE    . LYS   A 1 91  ? 8.537   19.103 27.778 1.00 34.93 ? 88  LYS   A CE    1 
ATOM   704  N  NZ    . LYS   A 1 91  ? 7.615   18.134 28.438 1.00 37.75 ? 88  LYS   A NZ    1 
ATOM   705  N  N     . SER   A 1 92  ? 8.718   16.127 22.586 1.00 15.45 ? 89  SER   A N     1 
ATOM   706  C  CA    . SER   A 1 92  ? 7.635   16.460 21.662 1.00 15.17 ? 89  SER   A CA    1 
ATOM   707  C  C     . SER   A 1 92  ? 6.853   15.213 21.267 1.00 14.73 ? 89  SER   A C     1 
ATOM   708  O  O     . SER   A 1 92  ? 5.644   15.275 21.063 1.00 14.12 ? 89  SER   A O     1 
ATOM   709  C  CB    . SER   A 1 92  ? 8.173   17.210 20.432 1.00 14.31 ? 89  SER   A CB    1 
ATOM   710  O  OG    . SER   A 1 92  ? 8.906   16.378 19.534 1.00 13.16 ? 89  SER   A OG    1 
ATOM   711  N  N     . PHE   A 1 93  ? 7.529   14.074 21.168 1.00 14.22 ? 90  PHE   A N     1 
ATOM   712  C  CA    . PHE   A 1 93  ? 6.842   12.799 20.912 1.00 15.43 ? 90  PHE   A CA    1 
ATOM   713  C  C     . PHE   A 1 93  ? 6.001   12.372 22.119 1.00 17.23 ? 90  PHE   A C     1 
ATOM   714  O  O     . PHE   A 1 93  ? 4.870   11.902 21.979 1.00 16.42 ? 90  PHE   A O     1 
ATOM   715  C  CB    . PHE   A 1 93  ? 7.884   11.738 20.544 1.00 15.35 ? 90  PHE   A CB    1 
ATOM   716  C  CG    . PHE   A 1 93  ? 7.332   10.368 20.273 1.00 14.87 ? 90  PHE   A CG    1 
ATOM   717  C  CD1   . PHE   A 1 93  ? 6.591   10.117 19.138 1.00 14.44 ? 90  PHE   A CD1   1 
ATOM   718  C  CD2   . PHE   A 1 93  ? 7.616   9.297  21.123 1.00 16.74 ? 90  PHE   A CD2   1 
ATOM   719  C  CE1   . PHE   A 1 93  ? 6.106   8.858  18.885 1.00 14.69 ? 90  PHE   A CE1   1 
ATOM   720  C  CE2   . PHE   A 1 93  ? 7.150   8.029  20.844 1.00 18.51 ? 90  PHE   A CE2   1 
ATOM   721  C  CZ    . PHE   A 1 93  ? 6.406   7.812  19.705 1.00 16.74 ? 90  PHE   A CZ    1 
ATOM   722  N  N     . GLU   A 1 94  ? 6.559   12.532 23.309 1.00 18.67 ? 91  GLU   A N     1 
ATOM   723  C  CA    . GLU   A 1 94  ? 5.819   12.221 24.544 1.00 21.77 ? 91  GLU   A CA    1 
ATOM   724  C  C     . GLU   A 1 94  ? 4.625   13.126 24.749 1.00 22.42 ? 91  GLU   A C     1 
ATOM   725  O  O     . GLU   A 1 94  ? 3.643   12.715 25.370 1.00 29.80 ? 91  GLU   A O     1 
ATOM   726  C  CB    . GLU   A 1 94  ? 6.753   12.312 25.740 1.00 22.41 ? 91  GLU   A CB    1 
ATOM   727  C  CG    . GLU   A 1 94  ? 7.743   11.197 25.741 1.00 23.58 ? 91  GLU   A CG    1 
ATOM   728  C  CD    . GLU   A 1 94  ? 8.533   11.174 27.035 1.00 27.29 ? 91  GLU   A CD    1 
ATOM   729  O  OE1   . GLU   A 1 94  ? 8.103   11.825 28.024 1.00 34.86 ? 91  GLU   A OE1   1 
ATOM   730  O  OE2   . GLU   A 1 94  ? 9.560   10.501 27.051 1.00 25.40 ? 91  GLU   A OE2   1 
ATOM   731  N  N     . ASP   A 1 95  ? 4.681   14.348 24.242 1.00 21.15 ? 92  ASP   A N     1 
ATOM   732  C  CA    . ASP   A 1 95  ? 3.568   15.288 24.352 1.00 21.41 ? 92  ASP   A CA    1 
ATOM   733  C  C     . ASP   A 1 95  ? 2.349   14.858 23.509 1.00 19.49 ? 92  ASP   A C     1 
ATOM   734  O  O     . ASP   A 1 95  ? 1.238   15.321 23.768 1.00 20.72 ? 92  ASP   A O     1 
ATOM   735  C  CB    . ASP   A 1 95  ? 3.965   16.708 23.909 1.00 23.70 ? 92  ASP   A CB    1 
ATOM   736  C  CG    . ASP   A 1 95  ? 4.961   17.425 24.852 1.00 28.72 ? 92  ASP   A CG    1 
ATOM   737  O  OD1   . ASP   A 1 95  ? 5.188   17.062 26.034 1.00 25.84 ? 92  ASP   A OD1   1 
ATOM   738  O  OD2   . ASP   A 1 95  ? 5.553   18.418 24.348 1.00 32.49 ? 92  ASP   A OD2   1 
ATOM   739  N  N     . ILE   A 1 96  ? 2.545   14.002 22.501 1.00 17.99 ? 93  ILE   A N     1 
ATOM   740  C  CA    . ILE   A 1 96  ? 1.466   13.666 21.556 1.00 17.11 ? 93  ILE   A CA    1 
ATOM   741  C  C     . ILE   A 1 96  ? 0.239   13.118 22.277 1.00 17.10 ? 93  ILE   A C     1 
ATOM   742  O  O     . ILE   A 1 96  ? -0.889  13.503 21.957 1.00 16.54 ? 93  ILE   A O     1 
ATOM   743  C  CB    . ILE   A 1 96  ? 1.957   12.646 20.502 1.00 16.20 ? 93  ILE   A CB    1 
ATOM   744  C  CG1   . ILE   A 1 96  ? 2.978   13.315 19.561 1.00 15.25 ? 93  ILE   A CG1   1 
ATOM   745  C  CG2   . ILE   A 1 96  ? 0.792   12.021 19.715 1.00 16.09 ? 93  ILE   A CG2   1 
ATOM   746  C  CD1   . ILE   A 1 96  ? 2.446   14.409 18.641 1.00 15.85 ? 93  ILE   A CD1   1 
ATOM   747  N  N     . HIS   A 1 97  ? 0.456   12.219 23.216 1.00 17.96 ? 94  HIS   A N     1 
ATOM   748  C  CA    . HIS   A 1 97  ? -0.667  11.588 23.949 1.00 20.56 ? 94  HIS   A CA    1 
ATOM   749  C  C     . HIS   A 1 97  ? -1.575  12.657 24.587 1.00 19.40 ? 94  HIS   A C     1 
ATOM   750  O  O     . HIS   A 1 97  ? -2.774  12.492 24.615 1.00 19.97 ? 94  HIS   A O     1 
ATOM   751  C  CB    . HIS   A 1 97  ? -0.052  10.622 24.965 1.00 25.56 ? 94  HIS   A CB    1 
ATOM   752  C  CG    . HIS   A 1 97  ? -1.012  9.979  25.892 1.00 32.40 ? 94  HIS   A CG    1 
ATOM   753  N  ND1   . HIS   A 1 97  ? -1.592  8.764  25.630 1.00 39.11 ? 94  HIS   A ND1   1 
ATOM   754  C  CD2   . HIS   A 1 97  ? -1.458  10.369 27.094 1.00 35.37 ? 94  HIS   A CD2   1 
ATOM   755  C  CE1   . HIS   A 1 97  ? -2.406  8.460  26.609 1.00 37.73 ? 94  HIS   A CE1   1 
ATOM   756  N  NE2   . HIS   A 1 97  ? -2.348  9.431  27.503 1.00 41.60 ? 94  HIS   A NE2   1 
ATOM   757  N  N     . HIS   A 1 98  ? -0.977  13.711 25.100 1.00 19.53 ? 95  HIS   A N     1 
ATOM   758  C  CA    . HIS   A 1 98  ? -1.713  14.746 25.802 1.00 22.23 ? 95  HIS   A CA    1 
ATOM   759  C  C     . HIS   A 1 98  ? -2.593  15.500 24.775 1.00 19.53 ? 95  HIS   A C     1 
ATOM   760  O  O     . HIS   A 1 98  ? -3.766  15.795 25.043 1.00 19.19 ? 95  HIS   A O     1 
ATOM   761  C  CB    . HIS   A 1 98  ? -0.708  15.687 26.464 1.00 27.19 ? 95  HIS   A CB    1 
ATOM   762  C  CG    . HIS   A 1 98  ? -1.286  16.647 27.449 1.00 36.54 ? 95  HIS   A CG    1 
ATOM   763  N  ND1   . HIS   A 1 98  ? -1.039  16.548 28.805 1.00 40.00 ? 95  HIS   A ND1   1 
ATOM   764  C  CD2   . HIS   A 1 98  ? -2.032  17.766 27.283 1.00 40.72 ? 95  HIS   A CD2   1 
ATOM   765  C  CE1   . HIS   A 1 98  ? -1.645  17.542 29.434 1.00 46.59 ? 95  HIS   A CE1   1 
ATOM   766  N  NE2   . HIS   A 1 98  ? -2.266  18.288 28.533 1.00 43.03 ? 95  HIS   A NE2   1 
ATOM   767  N  N     . TYR   A 1 99  ? -2.051  15.784 23.583 1.00 18.35 ? 96  TYR   A N     1 
ATOM   768  C  CA    . TYR   A 1 99  ? -2.860  16.450 22.537 1.00 18.93 ? 96  TYR   A CA    1 
ATOM   769  C  C     . TYR   A 1 99  ? -4.012  15.559 22.073 1.00 19.10 ? 96  TYR   A C     1 
ATOM   770  O  O     . TYR   A 1 99  ? -5.181  16.007 21.943 1.00 20.01 ? 96  TYR   A O     1 
ATOM   771  C  CB    . TYR   A 1 99  ? -1.943  16.924 21.359 1.00 19.21 ? 96  TYR   A CB    1 
ATOM   772  C  CG    . TYR   A 1 99  ? -0.786  17.865 21.786 1.00 23.61 ? 96  TYR   A CG    1 
ATOM   773  C  CD1   . TYR   A 1 99  ? -0.955  18.830 22.806 1.00 28.56 ? 96  TYR   A CD1   1 
ATOM   774  C  CD2   . TYR   A 1 99  ? 0.479   17.772 21.221 1.00 24.65 ? 96  TYR   A CD2   1 
ATOM   775  C  CE1   . TYR   A 1 99  ? 0.096   19.686 23.207 1.00 31.61 ? 96  TYR   A CE1   1 
ATOM   776  C  CE2   . TYR   A 1 99  ? 1.529   18.615 21.603 1.00 27.30 ? 96  TYR   A CE2   1 
ATOM   777  C  CZ    . TYR   A 1 99  ? 1.353   19.582 22.596 1.00 30.79 ? 96  TYR   A CZ    1 
ATOM   778  O  OH    . TYR   A 1 99  ? 2.404   20.436 22.993 1.00 28.97 ? 96  TYR   A OH    1 
ATOM   779  N  N     . ARG   A 1 100 ? -3.757  14.278 21.845 1.00 18.88 ? 97  ARG   A N     1 
ATOM   780  C  CA    . ARG   A 1 100 ? -4.847  13.374 21.509 1.00 20.34 ? 97  ARG   A CA    1 
ATOM   781  C  C     . ARG   A 1 100 ? -5.957  13.319 22.576 1.00 21.45 ? 97  ARG   A C     1 
ATOM   782  O  O     . ARG   A 1 100 ? -7.173  13.354 22.270 1.00 22.13 ? 97  ARG   A O     1 
ATOM   783  C  CB    . ARG   A 1 100 ? -4.320  11.990 21.215 1.00 21.34 ? 97  ARG   A CB    1 
ATOM   784  C  CG    . ARG   A 1 100 ? -5.381  11.046 20.728 1.00 22.99 ? 97  ARG   A CG    1 
ATOM   785  C  CD    . ARG   A 1 100 ? -4.771  9.781  20.157 1.00 25.59 ? 97  ARG   A CD    1 
ATOM   786  N  NE    . ARG   A 1 100 ? -5.761  8.708  20.076 1.00 25.30 ? 97  ARG   A NE    1 
ATOM   787  C  CZ    . ARG   A 1 100 ? -6.549  8.445  19.021 1.00 27.56 ? 97  ARG   A CZ    1 
ATOM   788  N  NH1   . ARG   A 1 100 ? -6.504  9.176  17.908 1.00 27.52 ? 97  ARG   A NH1   1 
ATOM   789  N  NH2   . ARG   A 1 100 ? -7.409  7.428  19.090 1.00 32.89 ? 97  ARG   A NH2   1 
ATOM   790  N  N     . GLU   A 1 101 ? -5.542  13.232 23.831 1.00 20.40 ? 98  GLU   A N     1 
ATOM   791  C  CA    . GLU   A 1 101 ? -6.490  13.209 24.941 1.00 23.11 ? 98  GLU   A CA    1 
ATOM   792  C  C     . GLU   A 1 101 ? -7.344  14.466 24.979 1.00 20.22 ? 98  GLU   A C     1 
ATOM   793  O  O     . GLU   A 1 101 ? -8.557  14.360 25.211 1.00 22.73 ? 98  GLU   A O     1 
ATOM   794  C  CB    . GLU   A 1 101 ? -5.747  13.020 26.268 1.00 25.32 ? 98  GLU   A CB    1 
ATOM   795  C  CG    . GLU   A 1 101 ? -5.248  11.607 26.480 1.00 30.23 ? 98  GLU   A CG    1 
ATOM   796  C  CD    . GLU   A 1 101 ? -6.346  10.577 26.303 1.00 37.72 ? 98  GLU   A CD    1 
ATOM   797  O  OE1   . GLU   A 1 101 ? -7.373  10.680 27.018 1.00 42.00 ? 98  GLU   A OE1   1 
ATOM   798  O  OE2   . GLU   A 1 101 ? -6.206  9.684  25.434 1.00 40.61 ? 98  GLU   A OE2   1 
ATOM   799  N  N     . GLN   A 1 102 ? -6.733  15.624 24.726 1.00 19.35 ? 99  GLN   A N     1 
ATOM   800  C  CA    . GLN   A 1 102 ? -7.447  16.917 24.735 1.00 21.11 ? 99  GLN   A CA    1 
ATOM   801  C  C     . GLN   A 1 102 ? -8.503  16.911 23.638 1.00 20.21 ? 99  GLN   A C     1 
ATOM   802  O  O     . GLN   A 1 102 ? -9.643  17.276 23.854 1.00 19.56 ? 99  GLN   A O     1 
ATOM   803  C  CB    . GLN   A 1 102 ? -6.554  18.116 24.507 1.00 22.17 ? 99  GLN   A CB    1 
ATOM   804  C  CG    . GLN   A 1 102 ? -5.584  18.482 25.626 1.00 28.70 ? 99  GLN   A CG    1 
ATOM   805  C  CD    . GLN   A 1 102 ? -4.664  19.660 25.263 1.00 31.38 ? 99  GLN   A CD    1 
ATOM   806  O  OE1   . GLN   A 1 102 ? -4.379  19.939 24.086 1.00 31.88 ? 99  GLN   A OE1   1 
ATOM   807  N  NE2   . GLN   A 1 102 ? -4.169  20.332 26.285 1.00 36.12 ? 99  GLN   A NE2   1 
ATOM   808  N  N     . ILE   A 1 103 ? -8.082  16.497 22.453 1.00 18.08 ? 100 ILE   A N     1 
ATOM   809  C  CA    . ILE   A 1 103 ? -9.005  16.476 21.301 1.00 18.05 ? 100 ILE   A CA    1 
ATOM   810  C  C     . ILE   A 1 103 ? -10.181 15.517 21.542 1.00 19.55 ? 100 ILE   A C     1 
ATOM   811  O  O     . ILE   A 1 103 ? -11.350 15.875 21.317 1.00 20.03 ? 100 ILE   A O     1 
ATOM   812  C  CB    . ILE   A 1 103 ? -8.272  16.127 20.007 1.00 17.94 ? 100 ILE   A CB    1 
ATOM   813  C  CG1   . ILE   A 1 103 ? -7.226  17.192 19.696 1.00 18.28 ? 100 ILE   A CG1   1 
ATOM   814  C  CG2   . ILE   A 1 103 ? -9.274  16.048 18.851 1.00 18.73 ? 100 ILE   A CG2   1 
ATOM   815  C  CD1   . ILE   A 1 103 ? -6.163  16.824 18.695 1.00 16.94 ? 100 ILE   A CD1   1 
ATOM   816  N  N     . LYS   A 1 104 ? -9.883  14.304 21.997 1.00 19.07 ? 101 LYS   A N     1 
ATOM   817  C  CA    . LYS   A 1 104 ? -10.930 13.321 22.322 1.00 20.59 ? 101 LYS   A CA    1 
ATOM   818  C  C     . LYS   A 1 104 ? -11.944 13.866 23.337 1.00 21.61 ? 101 LYS   A C     1 
ATOM   819  O  O     . LYS   A 1 104 ? -13.153 13.677 23.188 1.00 21.81 ? 101 LYS   A O     1 
ATOM   820  C  CB    . LYS   A 1 104 ? -10.320 12.035 22.865 1.00 23.34 ? 101 LYS   A CB    1 
ATOM   821  C  CG    . LYS   A 1 104 ? -9.697  11.178 21.765 1.00 25.06 ? 101 LYS   A CG    1 
ATOM   822  C  CD    . LYS   A 1 104 ? -8.798  10.089 22.328 1.00 29.07 ? 101 LYS   A CD    1 
ATOM   823  C  CE    . LYS   A 1 104 ? -9.587  8.948  22.926 1.00 33.68 ? 101 LYS   A CE    1 
ATOM   824  N  NZ    . LYS   A 1 104 ? -8.721  8.128  23.830 1.00 36.99 ? 101 LYS   A NZ    1 
ATOM   825  N  N     . ARG   A 1 105 ? -11.423 14.582 24.319 1.00 21.94 ? 102 ARG   A N     1 
ATOM   826  C  CA    . ARG   A 1 105 ? -12.306 15.151 25.363 1.00 24.10 ? 102 ARG   A CA    1 
ATOM   827  C  C     . ARG   A 1 105 ? -13.244 16.200 24.769 1.00 23.21 ? 102 ARG   A C     1 
ATOM   828  O  O     . ARG   A 1 105 ? -14.400 16.178 25.109 1.00 25.25 ? 102 ARG   A O     1 
ATOM   829  C  CB    . ARG   A 1 105 ? -11.490 15.721 26.522 1.00 26.90 ? 102 ARG   A CB    1 
ATOM   830  C  CG    . ARG   A 1 105 ? -12.326 16.565 27.464 1.00 31.69 ? 102 ARG   A CG    1 
ATOM   831  C  CD    . ARG   A 1 105 ? -11.606 17.049 28.706 1.00 36.51 ? 102 ARG   A CD    1 
ATOM   832  N  NE    . ARG   A 1 105 ? -10.159 17.098 28.643 1.00 40.41 ? 102 ARG   A NE    1 
ATOM   833  C  CZ    . ARG   A 1 105 ? -9.480  18.139 28.199 1.00 44.39 ? 102 ARG   A CZ    1 
ATOM   834  N  NH1   . ARG   A 1 105 ? -10.126 19.204 27.758 1.00 46.23 ? 102 ARG   A NH1   1 
ATOM   835  N  NH2   . ARG   A 1 105 ? -8.158  18.104 28.187 1.00 45.78 ? 102 ARG   A NH2   1 
ATOM   836  N  N     . VAL   A 1 106 ? -12.725 17.066 23.914 1.00 23.14 ? 103 VAL   A N     1 
ATOM   837  C  CA    . VAL   A 1 106 ? -13.519 18.145 23.312 1.00 23.58 ? 103 VAL   A CA    1 
ATOM   838  C  C     . VAL   A 1 106 ? -14.566 17.532 22.373 1.00 22.76 ? 103 VAL   A C     1 
ATOM   839  O  O     . VAL   A 1 106 ? -15.692 18.005 22.315 1.00 22.41 ? 103 VAL   A O     1 
ATOM   840  C  CB    . VAL   A 1 106 ? -12.629 19.135 22.529 1.00 25.67 ? 103 VAL   A CB    1 
ATOM   841  C  CG1   . VAL   A 1 106 ? -13.455 20.034 21.611 1.00 28.38 ? 103 VAL   A CG1   1 
ATOM   842  C  CG2   . VAL   A 1 106 ? -11.815 19.998 23.486 1.00 25.75 ? 103 VAL   A CG2   1 
ATOM   843  N  N     . LYS   A 1 107 ? -14.191 16.487 21.656 1.00 21.02 ? 104 LYS   A N     1 
ATOM   844  C  CA    . LYS   A 1 107 ? -15.114 15.833 20.706 1.00 21.51 ? 104 LYS   A CA    1 
ATOM   845  C  C     . LYS   A 1 107 ? -16.072 14.901 21.404 1.00 23.02 ? 104 LYS   A C     1 
ATOM   846  O  O     . LYS   A 1 107 ? -17.121 14.551 20.837 1.00 24.97 ? 104 LYS   A O     1 
ATOM   847  C  CB    . LYS   A 1 107 ? -14.359 15.009 19.653 1.00 19.75 ? 104 LYS   A CB    1 
ATOM   848  C  CG    . LYS   A 1 107 ? -13.517 15.818 18.701 1.00 19.32 ? 104 LYS   A CG    1 
ATOM   849  C  CD    . LYS   A 1 107 ? -14.316 16.867 17.947 1.00 20.50 ? 104 LYS   A CD    1 
ATOM   850  C  CE    . LYS   A 1 107 ? -13.424 17.563 16.932 1.00 19.32 ? 104 LYS   A CE    1 
ATOM   851  N  NZ    . LYS   A 1 107 ? -14.219 18.567 16.166 1.00 19.93 ? 104 LYS   A NZ    1 
ATOM   852  N  N     . ASP   A 1 108 ? -15.691 14.465 22.603 1.00 23.58 ? 105 ASP   A N     1 
ATOM   853  C  CA    . ASP   A 1 108 ? -16.496 13.449 23.326 1.00 26.60 ? 105 ASP   A CA    1 
ATOM   854  C  C     . ASP   A 1 108 ? -16.613 12.233 22.403 1.00 26.83 ? 105 ASP   A C     1 
ATOM   855  O  O     . ASP   A 1 108 ? -17.645 11.605 22.377 1.00 26.92 ? 105 ASP   A O     1 
ATOM   856  C  CB    . ASP   A 1 108 ? -17.823 14.012 23.854 1.00 29.77 ? 105 ASP   A CB    1 
ATOM   857  C  CG    . ASP   A 1 108 ? -18.679 12.975 24.525 1.00 35.04 ? 105 ASP   A CG    1 
ATOM   858  O  OD1   . ASP   A 1 108 ? -18.113 12.231 25.275 1.00 37.35 ? 105 ASP   A OD1   1 
ATOM   859  O  OD2   . ASP   A 1 108 ? -19.900 12.915 24.231 1.00 36.18 ? 105 ASP   A OD2   1 
ATOM   860  N  N     . SER   A 1 109 ? -15.546 11.942 21.659 1.00 26.66 ? 106 SER   A N     1 
ATOM   861  C  CA    . SER   A 1 109 ? -15.612 10.855 20.660 1.00 27.30 ? 106 SER   A CA    1 
ATOM   862  C  C     . SER   A 1 109 ? -14.276 10.137 20.516 1.00 32.49 ? 106 SER   A C     1 
ATOM   863  O  O     . SER   A 1 109 ? -13.281 10.778 20.701 1.00 32.08 ? 106 SER   A O     1 
ATOM   864  C  CB    . SER   A 1 109 ? -15.988 11.452 19.349 1.00 29.18 ? 106 SER   A CB    1 
ATOM   865  O  OG    . SER   A 1 109 ? -15.973 10.484 18.333 1.00 33.27 ? 106 SER   A OG    1 
ATOM   866  N  N     . GLU   A 1 110 ? -14.316 8.885  20.067 1.00 35.43 ? 107 GLU   A N     1 
ATOM   867  C  CA    . GLU   A 1 110 ? -13.068 8.165  19.720 1.00 38.20 ? 107 GLU   A CA    1 
ATOM   868  C  C     . GLU   A 1 110 ? -12.883 8.290  18.205 1.00 31.05 ? 107 GLU   A C     1 
ATOM   869  O  O     . GLU   A 1 110 ? -11.818 8.003  17.721 1.00 32.84 ? 107 GLU   A O     1 
ATOM   870  C  CB    . GLU   A 1 110 ? -13.149 6.716  20.184 1.00 45.00 ? 107 GLU   A CB    1 
ATOM   871  C  CG    . GLU   A 1 110 ? -12.899 6.576  21.666 1.00 48.93 ? 107 GLU   A CG    1 
ATOM   872  C  CD    . GLU   A 1 110 ? -13.237 5.185  22.153 1.00 57.10 ? 107 GLU   A CD    1 
ATOM   873  O  OE1   . GLU   A 1 110 ? -12.897 4.237  21.429 1.00 60.51 ? 107 GLU   A OE1   1 
ATOM   874  O  OE2   . GLU   A 1 110 ? -13.854 5.050  23.234 1.00 58.41 ? 107 GLU   A OE2   1 
ATOM   875  N  N     . ASP   A 1 111 ? -13.937 8.684  17.498 1.00 31.80 ? 108 ASP   A N     1 
ATOM   876  C  CA    . ASP   A 1 111 ? -13.883 8.856  16.041 1.00 32.02 ? 108 ASP   A CA    1 
ATOM   877  C  C     . ASP   A 1 111 ? -13.254 10.202 15.745 1.00 28.83 ? 108 ASP   A C     1 
ATOM   878  O  O     . ASP   A 1 111 ? -13.971 11.143 15.408 1.00 34.54 ? 108 ASP   A O     1 
ATOM   879  C  CB    . ASP   A 1 111 ? -15.310 8.846  15.424 1.00 32.36 ? 108 ASP   A CB    1 
ATOM   880  C  CG    . ASP   A 1 111 ? -15.900 7.447  15.291 1.00 36.64 ? 108 ASP   A CG    1 
ATOM   881  O  OD1   . ASP   A 1 111 ? -15.305 6.484  15.850 1.00 37.93 ? 108 ASP   A OD1   1 
ATOM   882  O  OD2   . ASP   A 1 111 ? -16.979 7.325  14.632 1.00 32.53 ? 108 ASP   A OD2   1 
ATOM   883  N  N     . VAL   A 1 112 ? -11.928 10.342 15.870 1.00 24.97 ? 109 VAL   A N     1 
ATOM   884  C  CA    . VAL   A 1 112 ? -11.328 11.625 15.530 1.00 20.75 ? 109 VAL   A CA    1 
ATOM   885  C  C     . VAL   A 1 112 ? -10.285 11.463 14.425 1.00 18.16 ? 109 VAL   A C     1 
ATOM   886  O  O     . VAL   A 1 112 ? -9.274  10.830 14.649 1.00 17.81 ? 109 VAL   A O     1 
ATOM   887  C  CB    . VAL   A 1 112 ? -10.670 12.334 16.734 1.00 21.79 ? 109 VAL   A CB    1 
ATOM   888  C  CG1   . VAL   A 1 112 ? -10.334 13.772 16.351 1.00 23.42 ? 109 VAL   A CG1   1 
ATOM   889  C  CG2   . VAL   A 1 112 ? -11.592 12.334 17.951 1.00 23.30 ? 109 VAL   A CG2   1 
ATOM   890  N  N     . PRO   A 1 113 ? -10.513 12.087 13.250 1.00 15.46 ? 110 PRO   A N     1 
ATOM   891  C  CA    . PRO   A 1 113 ? -9.508  12.007 12.191 1.00 14.21 ? 110 PRO   A CA    1 
ATOM   892  C  C     . PRO   A 1 113 ? -8.208  12.683 12.601 1.00 13.77 ? 110 PRO   A C     1 
ATOM   893  O  O     . PRO   A 1 113 ? -8.210  13.851 12.997 1.00 13.15 ? 110 PRO   A O     1 
ATOM   894  C  CB    . PRO   A 1 113 ? -10.144 12.789 11.024 1.00 14.53 ? 110 PRO   A CB    1 
ATOM   895  C  CG    . PRO   A 1 113 ? -11.622 12.733 11.289 1.00 15.76 ? 110 PRO   A CG    1 
ATOM   896  C  CD    . PRO   A 1 113 ? -11.724 12.788 12.793 1.00 15.79 ? 110 PRO   A CD    1 
ATOM   897  N  N     A MET   A 1 114 ? -7.121  11.908 12.618 0.50 13.15 ? 111 MET   A N     1 
ATOM   898  N  N     B MET   A 1 114 ? -7.102  11.962 12.436 0.50 13.18 ? 111 MET   A N     1 
ATOM   899  C  CA    A MET   A 1 114 ? -5.807  12.401 13.058 0.50 13.36 ? 111 MET   A CA    1 
ATOM   900  C  CA    B MET   A 1 114 ? -5.823  12.371 13.008 0.50 13.61 ? 111 MET   A CA    1 
ATOM   901  C  C     A MET   A 1 114 ? -4.744  11.723 12.201 0.50 12.89 ? 111 MET   A C     1 
ATOM   902  C  C     B MET   A 1 114 ? -4.729  11.700 12.205 0.50 13.10 ? 111 MET   A C     1 
ATOM   903  O  O     A MET   A 1 114 ? -4.933  10.580 11.755 0.50 13.09 ? 111 MET   A O     1 
ATOM   904  O  O     B MET   A 1 114 ? -4.882  10.539 11.800 0.50 13.41 ? 111 MET   A O     1 
ATOM   905  C  CB    A MET   A 1 114 ? -5.555  12.114 14.551 0.50 15.02 ? 111 MET   A CB    1 
ATOM   906  C  CB    B MET   A 1 114 ? -5.764  11.957 14.473 0.50 15.64 ? 111 MET   A CB    1 
ATOM   907  C  CG    A MET   A 1 114 ? -6.490  12.806 15.551 0.50 16.38 ? 111 MET   A CG    1 
ATOM   908  C  CG    B MET   A 1 114 ? -4.528  12.386 15.224 0.50 16.16 ? 111 MET   A CG    1 
ATOM   909  S  SD    A MET   A 1 114 ? -5.814  12.615 17.216 0.50 19.02 ? 111 MET   A SD    1 
ATOM   910  S  SD    B MET   A 1 114 ? -4.680  11.986 16.980 0.50 20.59 ? 111 MET   A SD    1 
ATOM   911  C  CE    A MET   A 1 114 ? -4.234  11.908 16.734 0.50 18.61 ? 111 MET   A CE    1 
ATOM   912  C  CE    B MET   A 1 114 ? -5.932  13.196 17.403 0.50 19.86 ? 111 MET   A CE    1 
ATOM   913  N  N     . VAL   A 1 115 ? -3.622  12.409 11.979 1.00 11.96 ? 112 VAL   A N     1 
ATOM   914  C  CA    . VAL   A 1 115 ? -2.427  11.801 11.378 1.00 12.03 ? 112 VAL   A CA    1 
ATOM   915  C  C     . VAL   A 1 115 ? -1.263  12.158 12.294 1.00 11.78 ? 112 VAL   A C     1 
ATOM   916  O  O     . VAL   A 1 115 ? -1.153  13.326 12.726 1.00 13.16 ? 112 VAL   A O     1 
ATOM   917  C  CB    . VAL   A 1 115 ? -2.212  12.336 9.966  1.00 13.78 ? 112 VAL   A CB    1 
ATOM   918  C  CG1   . VAL   A 1 115 ? -0.839  11.923 9.451  1.00 13.20 ? 112 VAL   A CG1   1 
ATOM   919  C  CG2   . VAL   A 1 115 ? -3.327  11.864 9.045  1.00 13.18 ? 112 VAL   A CG2   1 
ATOM   920  N  N     . LEU   A 1 116 ? -0.413  11.178 12.597 1.00 10.95 ? 113 LEU   A N     1 
ATOM   921  C  CA    . LEU   A 1 116 ? 0.802   11.423 13.389 1.00 11.50 ? 113 LEU   A CA    1 
ATOM   922  C  C     . LEU   A 1 116 ? 1.910   11.792 12.421 1.00 10.87 ? 113 LEU   A C     1 
ATOM   923  O  O     . LEU   A 1 116 ? 2.138   11.074 11.457 1.00 11.93 ? 113 LEU   A O     1 
ATOM   924  C  CB    . LEU   A 1 116 ? 1.188   10.185 14.167 1.00 12.28 ? 113 LEU   A CB    1 
ATOM   925  C  CG    . LEU   A 1 116 ? 2.406   10.290 15.062 1.00 12.66 ? 113 LEU   A CG    1 
ATOM   926  C  CD1   . LEU   A 1 116 ? 2.172   11.326 16.145 1.00 13.55 ? 113 LEU   A CD1   1 
ATOM   927  C  CD2   . LEU   A 1 116 ? 2.780   8.930  15.639 1.00 13.74 ? 113 LEU   A CD2   1 
ATOM   928  N  N     . VAL   A 1 117 ? 2.527   12.954 12.632 1.00 11.01 ? 114 VAL   A N     1 
ATOM   929  C  CA    . VAL   A 1 117 ? 3.605   13.430 11.753 1.00 10.96 ? 114 VAL   A CA    1 
ATOM   930  C  C     . VAL   A 1 117 ? 4.895   13.557 12.554 1.00 10.79 ? 114 VAL   A C     1 
ATOM   931  O  O     . VAL   A 1 117 ? 4.975   14.323 13.544 1.00 10.42 ? 114 VAL   A O     1 
ATOM   932  C  CB    . VAL   A 1 117 ? 3.265   14.780 11.153 1.00 11.63 ? 114 VAL   A CB    1 
ATOM   933  C  CG1   . VAL   A 1 117 ? 4.444   15.328 10.321 1.00 12.22 ? 114 VAL   A CG1   1 
ATOM   934  C  CG2   . VAL   A 1 117 ? 1.993   14.672 10.327 1.00 12.97 ? 114 VAL   A CG2   1 
ATOM   935  N  N     . GLY   A 1 118 ? 5.908   12.828 12.117 1.00 11.14 ? 115 GLY   A N     1 
ATOM   936  C  CA    . GLY   A 1 118 ? 7.287   13.015 12.639 1.00 11.91 ? 115 GLY   A CA    1 
ATOM   937  C  C     . GLY   A 1 118 ? 8.018   13.936 11.687 1.00 13.00 ? 115 GLY   A C     1 
ATOM   938  O  O     . GLY   A 1 118 ? 8.409   13.527 10.598 1.00 12.22 ? 115 GLY   A O     1 
ATOM   939  N  N     . ASN   A 1 119 ? 8.159   15.184 12.075 1.00 11.60 ? 116 ASN   A N     1 
ATOM   940  C  CA    . ASN   A 1 119 ? 8.809   16.192 11.234 1.00 11.86 ? 116 ASN   A CA    1 
ATOM   941  C  C     . ASN   A 1 119 ? 10.322  16.295 11.486 1.00 13.22 ? 116 ASN   A C     1 
ATOM   942  O  O     . ASN   A 1 119 ? 10.863  15.768 12.479 1.00 13.33 ? 116 ASN   A O     1 
ATOM   943  C  CB    . ASN   A 1 119 ? 8.075   17.533 11.390 1.00 12.96 ? 116 ASN   A CB    1 
ATOM   944  C  CG    . ASN   A 1 119 ? 8.542   18.613 10.382 1.00 13.77 ? 116 ASN   A CG    1 
ATOM   945  O  OD1   . ASN   A 1 119 ? 8.663   18.367 9.175  1.00 13.07 ? 116 ASN   A OD1   1 
ATOM   946  N  ND2   . ASN   A 1 119 ? 8.864   19.799 10.912 1.00 13.53 ? 116 ASN   A ND2   1 
ATOM   947  N  N     . LYS   A 1 120 ? 11.000  17.019 10.598 1.00 12.25 ? 117 LYS   A N     1 
ATOM   948  C  CA    . LYS   A 1 120 ? 12.463  17.205 10.615 1.00 13.68 ? 117 LYS   A CA    1 
ATOM   949  C  C     . LYS   A 1 120 ? 13.197  15.915 10.261 1.00 13.62 ? 117 LYS   A C     1 
ATOM   950  O  O     . LYS   A 1 120 ? 14.290  15.626 10.757 1.00 14.16 ? 117 LYS   A O     1 
ATOM   951  C  CB    . LYS   A 1 120 ? 12.976  17.812 11.927 1.00 13.70 ? 117 LYS   A CB    1 
ATOM   952  C  CG    . LYS   A 1 120 ? 12.173  18.999 12.390 1.00 14.09 ? 117 LYS   A CG    1 
ATOM   953  C  CD    . LYS   A 1 120 ? 12.861  19.805 13.476 1.00 14.16 ? 117 LYS   A CD    1 
ATOM   954  C  CE    . LYS   A 1 120 ? 12.001  20.909 14.063 1.00 15.69 ? 117 LYS   A CE    1 
ATOM   955  N  NZ    . LYS   A 1 120 ? 12.762  21.823 14.981 1.00 16.99 ? 117 LYS   A NZ    1 
ATOM   956  N  N     . SER   A 1 121 ? 12.630  15.179 9.301  1.00 13.73 ? 118 SER   A N     1 
ATOM   957  C  CA    . SER   A 1 121 ? 13.202  13.916 8.877  1.00 14.56 ? 118 SER   A CA    1 
ATOM   958  C  C     . SER   A 1 121 ? 14.559  14.108 8.199  1.00 15.03 ? 118 SER   A C     1 
ATOM   959  O  O     . SER   A 1 121 ? 15.277  13.153 8.015  1.00 18.35 ? 118 SER   A O     1 
ATOM   960  C  CB    . SER   A 1 121 ? 12.271  13.162 7.904  1.00 15.07 ? 118 SER   A CB    1 
ATOM   961  O  OG    . SER   A 1 121 ? 12.203  13.861 6.662  1.00 15.86 ? 118 SER   A OG    1 
ATOM   962  N  N     . ASP   A 1 122 ? 14.885  15.341 7.826  1.00 14.36 ? 119 ASP   A N     1 
ATOM   963  C  CA    . ASP   A 1 122 ? 16.178  15.698 7.227  1.00 16.10 ? 119 ASP   A CA    1 
ATOM   964  C  C     . ASP   A 1 122 ? 17.279  15.801 8.266  1.00 16.95 ? 119 ASP   A C     1 
ATOM   965  O  O     . ASP   A 1 122 ? 18.455  15.902 7.904  1.00 18.70 ? 119 ASP   A O     1 
ATOM   966  C  CB    . ASP   A 1 122 ? 16.063  17.032 6.482  1.00 17.32 ? 119 ASP   A CB    1 
ATOM   967  C  CG    . ASP   A 1 122 ? 15.669  18.170 7.400  1.00 17.47 ? 119 ASP   A CG    1 
ATOM   968  O  OD1   . ASP   A 1 122 ? 14.458  18.232 7.778  1.00 16.04 ? 119 ASP   A OD1   1 
ATOM   969  O  OD2   . ASP   A 1 122 ? 16.555  18.964 7.841  1.00 19.15 ? 119 ASP   A OD2   1 
ATOM   970  N  N     . LEU   A 1 123 ? 16.930  15.807 9.539  1.00 15.93 ? 120 LEU   A N     1 
ATOM   971  C  CA    . LEU   A 1 123 ? 17.987  15.934 10.560 1.00 16.89 ? 120 LEU   A CA    1 
ATOM   972  C  C     . LEU   A 1 123 ? 18.572  14.569 10.881 1.00 16.86 ? 120 LEU   A C     1 
ATOM   973  O  O     . LEU   A 1 123 ? 17.842  13.626 11.115 1.00 16.21 ? 120 LEU   A O     1 
ATOM   974  C  CB    . LEU   A 1 123 ? 17.426  16.563 11.831 1.00 16.74 ? 120 LEU   A CB    1 
ATOM   975  C  CG    . LEU   A 1 123 ? 17.021  18.024 11.655 1.00 18.55 ? 120 LEU   A CG    1 
ATOM   976  C  CD1   . LEU   A 1 123 ? 16.428  18.570 12.950 1.00 19.25 ? 120 LEU   A CD1   1 
ATOM   977  C  CD2   . LEU   A 1 123 ? 18.204  18.885 11.198 1.00 19.77 ? 120 LEU   A CD2   1 
ATOM   978  N  N     . PRO   A 1 124 ? 19.906  14.450 10.870 1.00 16.38 ? 121 PRO   A N     1 
ATOM   979  C  CA    . PRO   A 1 124 ? 20.512  13.103 11.012 1.00 16.67 ? 121 PRO   A CA    1 
ATOM   980  C  C     . PRO   A 1 124 ? 20.500  12.548 12.440 1.00 17.90 ? 121 PRO   A C     1 
ATOM   981  O  O     . PRO   A 1 124 ? 20.507  11.340 12.596 1.00 19.64 ? 121 PRO   A O     1 
ATOM   982  C  CB    . PRO   A 1 124 ? 21.944  13.313 10.549 1.00 17.24 ? 121 PRO   A CB    1 
ATOM   983  C  CG    . PRO   A 1 124 ? 22.188  14.764 10.764 1.00 17.87 ? 121 PRO   A CG    1 
ATOM   984  C  CD    . PRO   A 1 124 ? 20.898  15.487 10.552 1.00 16.85 ? 121 PRO   A CD    1 
ATOM   985  N  N     . SER   A 1 125 ? 20.486  13.407 13.458 1.00 16.65 ? 122 SER   A N     1 
ATOM   986  C  CA    . SER   A 1 125 ? 20.521  12.933 14.865 1.00 17.62 ? 122 SER   A CA    1 
ATOM   987  C  C     . SER   A 1 125 ? 19.122  12.634 15.431 1.00 17.14 ? 122 SER   A C     1 
ATOM   988  O  O     . SER   A 1 125 ? 18.691  13.295 16.315 1.00 18.45 ? 122 SER   A O     1 
ATOM   989  C  CB    . SER   A 1 125 ? 21.275  13.875 15.748 1.00 18.51 ? 122 SER   A CB    1 
ATOM   990  O  OG    . SER   A 1 125 ? 22.637  13.861 15.386 1.00 20.42 ? 122 SER   A OG    1 
ATOM   991  N  N     . ARG   A 1 126 ? 18.513  11.582 14.933 1.00 17.58 ? 123 ARG   A N     1 
ATOM   992  C  CA    . ARG   A 1 126 ? 17.177  11.146 15.385 1.00 17.19 ? 123 ARG   A CA    1 
ATOM   993  C  C     . ARG   A 1 126 ? 17.206  10.690 16.854 1.00 17.28 ? 123 ARG   A C     1 
ATOM   994  O  O     . ARG   A 1 126 ? 18.135  10.041 17.246 1.00 18.08 ? 123 ARG   A O     1 
ATOM   995  C  CB    . ARG   A 1 126 ? 16.824  9.967  14.481 1.00 17.56 ? 123 ARG   A CB    1 
ATOM   996  C  CG    . ARG   A 1 126 ? 15.509  9.295  14.794 1.00 17.47 ? 123 ARG   A CG    1 
ATOM   997  C  CD    . ARG   A 1 126 ? 15.382  8.087  13.903 1.00 17.11 ? 123 ARG   A CD    1 
ATOM   998  N  NE    . ARG   A 1 126 ? 15.140  8.462  12.542 1.00 17.77 ? 123 ARG   A NE    1 
ATOM   999  C  CZ    . ARG   A 1 126 ? 13.951  8.769  12.067 1.00 17.28 ? 123 ARG   A CZ    1 
ATOM   1000 N  NH1   . ARG   A 1 126 ? 12.894  8.770  12.861 1.00 18.45 ? 123 ARG   A NH1   1 
ATOM   1001 N  NH2   . ARG   A 1 126 ? 13.833  9.066  10.794 1.00 16.80 ? 123 ARG   A NH2   1 
ATOM   1002 N  N     . THR   A 1 127 ? 16.162  11.031 17.603 1.00 16.79 ? 124 THR   A N     1 
ATOM   1003 C  CA    . THR   A 1 127 ? 16.008  10.535 18.989 1.00 17.36 ? 124 THR   A CA    1 
ATOM   1004 C  C     . THR   A 1 127 ? 14.754  9.660  19.085 1.00 17.19 ? 124 THR   A C     1 
ATOM   1005 O  O     . THR   A 1 127 ? 14.637  8.968  20.032 1.00 18.29 ? 124 THR   A O     1 
ATOM   1006 C  CB    . THR   A 1 127 ? 16.010  11.669 20.015 1.00 18.12 ? 124 THR   A CB    1 
ATOM   1007 O  OG1   . THR   A 1 127 ? 14.910  12.533 19.781 1.00 17.96 ? 124 THR   A OG1   1 
ATOM   1008 C  CG2   . THR   A 1 127 ? 17.314  12.434 20.007 1.00 19.62 ? 124 THR   A CG2   1 
ATOM   1009 N  N     . VAL   A 1 128 ? 13.849  9.775  18.116 1.00 15.98 ? 125 VAL   A N     1 
ATOM   1010 C  CA    . VAL   A 1 128 ? 12.639  8.933  18.125 1.00 16.99 ? 125 VAL   A CA    1 
ATOM   1011 C  C     . VAL   A 1 128 ? 12.711  7.909  16.994 1.00 16.56 ? 125 VAL   A C     1 
ATOM   1012 O  O     . VAL   A 1 128 ? 12.665  8.252  15.811 1.00 16.25 ? 125 VAL   A O     1 
ATOM   1013 C  CB    . VAL   A 1 128 ? 11.368  9.798  17.975 1.00 16.51 ? 125 VAL   A CB    1 
ATOM   1014 C  CG1   . VAL   A 1 128 ? 10.097  8.933  18.071 1.00 16.75 ? 125 VAL   A CG1   1 
ATOM   1015 C  CG2   . VAL   A 1 128 ? 11.310  10.864 19.048 1.00 16.65 ? 125 VAL   A CG2   1 
ATOM   1016 N  N     . ASP   A 1 129 ? 12.773  6.640  17.373 1.00 19.66 ? 126 ASP   A N     1 
ATOM   1017 C  CA    . ASP   A 1 129 ? 12.846  5.545  16.403 1.00 21.47 ? 126 ASP   A CA    1 
ATOM   1018 C  C     . ASP   A 1 129 ? 11.580  5.500  15.594 1.00 21.17 ? 126 ASP   A C     1 
ATOM   1019 O  O     . ASP   A 1 129 ? 10.487  5.549  16.145 1.00 17.51 ? 126 ASP   A O     1 
ATOM   1020 C  CB    . ASP   A 1 129 ? 13.029  4.218  17.150 1.00 24.23 ? 126 ASP   A CB    1 
ATOM   1021 C  CG    . ASP   A 1 129 ? 13.523  3.085  16.261 1.00 29.48 ? 126 ASP   A CG    1 
ATOM   1022 O  OD1   . ASP   A 1 129 ? 13.039  2.918  15.124 1.00 31.72 ? 126 ASP   A OD1   1 
ATOM   1023 O  OD2   . ASP   A 1 129 ? 14.408  2.323  16.737 1.00 40.25 ? 126 ASP   A OD2   1 
ATOM   1024 N  N     . THR   A 1 130 ? 11.708  5.391  14.274 1.00 22.36 ? 127 THR   A N     1 
ATOM   1025 C  CA    . THR   A 1 130 ? 10.521  5.253  13.431 1.00 22.84 ? 127 THR   A CA    1 
ATOM   1026 C  C     . THR   A 1 130 ? 9.629   4.084  13.892 1.00 21.58 ? 127 THR   A C     1 
ATOM   1027 O  O     . THR   A 1 130 ? 8.397   4.189  13.837 1.00 21.53 ? 127 THR   A O     1 
ATOM   1028 C  CB    . THR   A 1 130 ? 10.930  5.130  11.951 1.00 26.34 ? 127 THR   A CB    1 
ATOM   1029 O  OG1   . THR   A 1 130 ? 11.780  6.235  11.629 1.00 29.66 ? 127 THR   A OG1   1 
ATOM   1030 C  CG2   . THR   A 1 130 ? 9.764   5.236  11.065 1.00 29.27 ? 127 THR   A CG2   1 
ATOM   1031 N  N     . LYS   A 1 131 ? 10.232  3.001  14.387 1.00 21.56 ? 128 LYS   A N     1 
ATOM   1032 C  CA    . LYS   A 1 131 ? 9.480   1.847  14.915 1.00 25.23 ? 128 LYS   A CA    1 
ATOM   1033 C  C     . LYS   A 1 131 ? 8.533   2.194  16.056 1.00 21.75 ? 128 LYS   A C     1 
ATOM   1034 O  O     . LYS   A 1 131 ? 7.392   1.689  16.120 1.00 23.03 ? 128 LYS   A O     1 
ATOM   1035 C  CB    . LYS   A 1 131 ? 10.435  0.760  15.403 1.00 30.16 ? 128 LYS   A CB    1 
ATOM   1036 C  CG    . LYS   A 1 131 ? 11.282  0.136  14.312 1.00 36.83 ? 128 LYS   A CG    1 
ATOM   1037 C  CD    . LYS   A 1 131 ? 10.409  -0.545 13.274 1.00 41.28 ? 128 LYS   A CD    1 
ATOM   1038 C  CE    . LYS   A 1 131 ? 10.148  0.335  12.063 1.00 39.47 ? 128 LYS   A CE    1 
ATOM   1039 N  NZ    . LYS   A 1 131 ? 9.182   -0.376 11.181 1.00 43.08 ? 128 LYS   A NZ    1 
ATOM   1040 N  N     . GLN   A 1 132 ? 9.019   3.032  16.955 1.00 20.05 ? 129 GLN   A N     1 
ATOM   1041 C  CA    . GLN   A 1 132 ? 8.243   3.442  18.111 1.00 20.03 ? 129 GLN   A CA    1 
ATOM   1042 C  C     . GLN   A 1 132 ? 7.088   4.316  17.683 1.00 17.64 ? 129 GLN   A C     1 
ATOM   1043 O  O     . GLN   A 1 132 ? 5.952   4.172  18.153 1.00 16.47 ? 129 GLN   A O     1 
ATOM   1044 C  CB    . GLN   A 1 132 ? 9.124   4.206  19.113 1.00 22.39 ? 129 GLN   A CB    1 
ATOM   1045 C  CG    . GLN   A 1 132 ? 10.058  3.315  19.912 1.00 27.18 ? 129 GLN   A CG    1 
ATOM   1046 C  CD    . GLN   A 1 132 ? 10.632  4.026  21.134 1.00 33.15 ? 129 GLN   A CD    1 
ATOM   1047 O  OE1   . GLN   A 1 132 ? 10.257  5.167  21.456 1.00 41.16 ? 129 GLN   A OE1   1 
ATOM   1048 N  NE2   . GLN   A 1 132 ? 11.505  3.355  21.833 1.00 36.85 ? 129 GLN   A NE2   1 
ATOM   1049 N  N     . ALA   A 1 133 ? 7.358   5.214  16.743 1.00 15.66 ? 130 ALA   A N     1 
ATOM   1050 C  CA    . ALA   A 1 133 ? 6.302   6.093  16.245 1.00 15.00 ? 130 ALA   A CA    1 
ATOM   1051 C  C     . ALA   A 1 133 ? 5.223   5.306  15.483 1.00 13.37 ? 130 ALA   A C     1 
ATOM   1052 O  O     . ALA   A 1 133 ? 4.014   5.542  15.648 1.00 13.71 ? 130 ALA   A O     1 
ATOM   1053 C  CB    . ALA   A 1 133 ? 6.921   7.181  15.375 1.00 15.32 ? 130 ALA   A CB    1 
ATOM   1054 N  N     . GLN   A 1 134 ? 5.660   4.332  14.669 1.00 13.58 ? 131 GLN   A N     1 
ATOM   1055 C  CA    . GLN   A 1 134 ? 4.712   3.423  14.011 1.00 14.32 ? 131 GLN   A CA    1 
ATOM   1056 C  C     . GLN   A 1 134 ? 3.865   2.677  15.038 1.00 14.64 ? 131 GLN   A C     1 
ATOM   1057 O  O     . GLN   A 1 134 ? 2.679   2.505  14.829 1.00 16.24 ? 131 GLN   A O     1 
ATOM   1058 C  CB    . GLN   A 1 134 ? 5.414   2.428  13.085 1.00 15.06 ? 131 GLN   A CB    1 
ATOM   1059 C  CG    . GLN   A 1 134 ? 5.984   3.061  11.840 1.00 14.66 ? 131 GLN   A CG    1 
ATOM   1060 C  CD    . GLN   A 1 134 ? 6.608   2.037  10.918 1.00 16.13 ? 131 GLN   A CD    1 
ATOM   1061 O  OE1   . GLN   A 1 134 ? 7.070   1.001  11.361 1.00 18.60 ? 131 GLN   A OE1   1 
ATOM   1062 N  NE2   . GLN   A 1 134 ? 6.590   2.311  9.616  1.00 16.36 ? 131 GLN   A NE2   1 
ATOM   1063 N  N     . ASP   A 1 135 ? 4.481   2.195  16.108 1.00 16.37 ? 132 ASP   A N     1 
ATOM   1064 C  CA    . ASP   A 1 135 ? 3.744   1.479  17.143 1.00 17.15 ? 132 ASP   A CA    1 
ATOM   1065 C  C     . ASP   A 1 135 ? 2.716   2.395  17.801 1.00 16.24 ? 132 ASP   A C     1 
ATOM   1066 O  O     . ASP   A 1 135 ? 1.592   1.980  18.038 1.00 15.98 ? 132 ASP   A O     1 
ATOM   1067 C  CB    . ASP   A 1 135 ? 4.702   0.934  18.197 1.00 19.39 ? 132 ASP   A CB    1 
ATOM   1068 C  CG    . ASP   A 1 135 ? 3.971   0.268  19.338 1.00 23.38 ? 132 ASP   A CG    1 
ATOM   1069 O  OD1   . ASP   A 1 135 ? 3.194   -0.690 19.083 1.00 26.34 ? 132 ASP   A OD1   1 
ATOM   1070 O  OD2   . ASP   A 1 135 ? 4.183   0.704  20.499 1.00 24.43 ? 132 ASP   A OD2   1 
ATOM   1071 N  N     . LEU   A 1 136 ? 3.098   3.632  18.086 1.00 15.25 ? 133 LEU   A N     1 
ATOM   1072 C  CA    . LEU   A 1 136 ? 2.162   4.559  18.706 1.00 15.55 ? 133 LEU   A CA    1 
ATOM   1073 C  C     . LEU   A 1 136 ? 0.968   4.797  17.771 1.00 15.27 ? 133 LEU   A C     1 
ATOM   1074 O  O     . LEU   A 1 136 ? -0.198  4.729  18.168 1.00 14.49 ? 133 LEU   A O     1 
ATOM   1075 C  CB    . LEU   A 1 136 ? 2.861   5.873  19.066 1.00 15.88 ? 133 LEU   A CB    1 
ATOM   1076 C  CG    . LEU   A 1 136 ? 1.975   6.870  19.818 1.00 17.35 ? 133 LEU   A CG    1 
ATOM   1077 C  CD1   . LEU   A 1 136 ? 1.652   6.362  21.213 1.00 17.77 ? 133 LEU   A CD1   1 
ATOM   1078 C  CD2   . LEU   A 1 136 ? 2.609   8.259  19.858 1.00 17.44 ? 133 LEU   A CD2   1 
ATOM   1079 N  N     . ALA   A 1 137 ? 1.257   5.057  16.515 1.00 14.57 ? 134 ALA   A N     1 
ATOM   1080 C  CA    . ALA   A 1 137 ? 0.174   5.331  15.588 1.00 13.29 ? 134 ALA   A CA    1 
ATOM   1081 C  C     . ALA   A 1 137 ? -0.755  4.087  15.467 1.00 14.91 ? 134 ALA   A C     1 
ATOM   1082 O  O     . ALA   A 1 137 ? -1.976  4.210  15.374 1.00 16.35 ? 134 ALA   A O     1 
ATOM   1083 C  CB    . ALA   A 1 137 ? 0.754   5.714  14.229 1.00 13.26 ? 134 ALA   A CB    1 
ATOM   1084 N  N     . ARG   A 1 138 ? -0.166  2.889  15.466 1.00 15.55 ? 135 ARG   A N     1 
ATOM   1085 C  CA    . ARG   A 1 138 ? -0.948  1.648  15.381 1.00 17.30 ? 135 ARG   A CA    1 
ATOM   1086 C  C     . ARG   A 1 138 ? -1.887  1.555  16.594 1.00 17.73 ? 135 ARG   A C     1 
ATOM   1087 O  O     . ARG   A 1 138 ? -3.079  1.222  16.459 1.00 17.48 ? 135 ARG   A O     1 
ATOM   1088 C  CB    . ARG   A 1 138 ? -0.008  0.440  15.303 1.00 20.48 ? 135 ARG   A CB    1 
ATOM   1089 C  CG    . ARG   A 1 138 ? -0.596  -0.849 14.752 1.00 27.40 ? 135 ARG   A CG    1 
ATOM   1090 C  CD    . ARG   A 1 138 ? 0.508   -1.668 14.030 1.00 29.55 ? 135 ARG   A CD    1 
ATOM   1091 N  NE    . ARG   A 1 138 ? 1.757   -1.679 14.783 1.00 33.94 ? 135 ARG   A NE    1 
ATOM   1092 C  CZ    . ARG   A 1 138 ? 2.970   -1.347 14.325 1.00 34.11 ? 135 ARG   A CZ    1 
ATOM   1093 N  NH1   . ARG   A 1 138 ? 4.004   -1.423 15.150 1.00 38.73 ? 135 ARG   A NH1   1 
ATOM   1094 N  NH2   . ARG   A 1 138 ? 3.178   -0.980 13.062 1.00 35.70 ? 135 ARG   A NH2   1 
ATOM   1095 N  N     . SER   A 1 139 ? -1.362  1.911  17.764 1.00 17.23 ? 136 SER   A N     1 
ATOM   1096 C  CA    . SER   A 1 139 ? -2.170  1.861  18.987 1.00 18.57 ? 136 SER   A CA    1 
ATOM   1097 C  C     . SER   A 1 139 ? -3.366  2.817  18.957 1.00 19.29 ? 136 SER   A C     1 
ATOM   1098 O  O     . SER   A 1 139 ? -4.425  2.525  19.550 1.00 19.73 ? 136 SER   A O     1 
ATOM   1099 C  CB    . SER   A 1 139 ? -1.315  2.058  20.260 1.00 20.18 ? 136 SER   A CB    1 
ATOM   1100 O  OG    . SER   A 1 139 ? -0.985  3.411  20.435 1.00 21.89 ? 136 SER   A OG    1 
ATOM   1101 N  N     . TYR   A 1 140 ? -3.194  3.935  18.259 1.00 16.97 ? 137 TYR   A N     1 
ATOM   1102 C  CA    . TYR   A 1 140 ? -4.239  4.953  18.083 1.00 17.44 ? 137 TYR   A CA    1 
ATOM   1103 C  C     . TYR   A 1 140 ? -5.147  4.676  16.899 1.00 17.02 ? 137 TYR   A C     1 
ATOM   1104 O  O     . TYR   A 1 140 ? -6.220  5.254  16.791 1.00 20.76 ? 137 TYR   A O     1 
ATOM   1105 C  CB    . TYR   A 1 140 ? -3.619  6.328  17.917 1.00 17.39 ? 137 TYR   A CB    1 
ATOM   1106 C  CG    . TYR   A 1 140 ? -2.883  6.899  19.104 1.00 19.66 ? 137 TYR   A CG    1 
ATOM   1107 C  CD1   . TYR   A 1 140 ? -3.094  6.455  20.400 1.00 20.49 ? 137 TYR   A CD1   1 
ATOM   1108 C  CD2   . TYR   A 1 140 ? -2.000  7.934  18.914 1.00 18.84 ? 137 TYR   A CD2   1 
ATOM   1109 C  CE1   . TYR   A 1 140 ? -2.398  7.037  21.469 1.00 21.58 ? 137 TYR   A CE1   1 
ATOM   1110 C  CE2   . TYR   A 1 140 ? -1.305  8.504  19.950 1.00 19.72 ? 137 TYR   A CE2   1 
ATOM   1111 C  CZ    . TYR   A 1 140 ? -1.517  8.072  21.222 1.00 20.82 ? 137 TYR   A CZ    1 
ATOM   1112 O  OH    . TYR   A 1 140 ? -0.807  8.684  22.236 1.00 23.40 ? 137 TYR   A OH    1 
ATOM   1113 N  N     . GLY   A 1 141 ? -4.732  3.768  16.025 1.00 16.74 ? 138 GLY   A N     1 
ATOM   1114 C  CA    . GLY   A 1 141 ? -5.424  3.521  14.779 1.00 15.94 ? 138 GLY   A CA    1 
ATOM   1115 C  C     . GLY   A 1 141 ? -5.376  4.633  13.778 1.00 15.74 ? 138 GLY   A C     1 
ATOM   1116 O  O     . GLY   A 1 141 ? -6.348  4.866  13.055 1.00 17.57 ? 138 GLY   A O     1 
ATOM   1117 N  N     . ILE   A 1 142 ? -4.231  5.306  13.709 1.00 14.07 ? 139 ILE   A N     1 
ATOM   1118 C  CA    . ILE   A 1 142 ? -4.033  6.440  12.799 1.00 13.66 ? 139 ILE   A CA    1 
ATOM   1119 C  C     . ILE   A 1 142 ? -2.807  6.257  11.918 1.00 13.05 ? 139 ILE   A C     1 
ATOM   1120 O  O     . ILE   A 1 142 ? -1.906  5.498  12.290 1.00 13.19 ? 139 ILE   A O     1 
ATOM   1121 C  CB    . ILE   A 1 142 ? -3.907  7.768  13.572 1.00 14.17 ? 139 ILE   A CB    1 
ATOM   1122 C  CG1   . ILE   A 1 142 ? -2.626  7.838  14.397 1.00 13.96 ? 139 ILE   A CG1   1 
ATOM   1123 C  CG2   . ILE   A 1 142 ? -5.152  7.948  14.438 1.00 14.25 ? 139 ILE   A CG2   1 
ATOM   1124 C  CD1   . ILE   A 1 142 ? -2.457  9.141  15.160 1.00 14.44 ? 139 ILE   A CD1   1 
ATOM   1125 N  N     . PRO   A 1 143 ? -2.793  6.939  10.749 1.00 12.83 ? 140 PRO   A N     1 
ATOM   1126 C  CA    . PRO   A 1 143 ? -1.594  6.952  9.917  1.00 11.75 ? 140 PRO   A CA    1 
ATOM   1127 C  C     . PRO   A 1 143 ? -0.415  7.657  10.569 1.00 11.59 ? 140 PRO   A C     1 
ATOM   1128 O  O     . PRO   A 1 143 ? -0.593  8.522  11.423 1.00 13.17 ? 140 PRO   A O     1 
ATOM   1129 C  CB    . PRO   A 1 143 ? -2.046  7.688  8.641  1.00 12.70 ? 140 PRO   A CB    1 
ATOM   1130 C  CG    . PRO   A 1 143 ? -3.525  7.598  8.631  1.00 13.38 ? 140 PRO   A CG    1 
ATOM   1131 C  CD    . PRO   A 1 143 ? -3.908  7.617  10.062 1.00 12.54 ? 140 PRO   A CD    1 
ATOM   1132 N  N     . PHE   A 1 144 ? 0.783   7.242  10.173 1.00 10.61 ? 141 PHE   A N     1 
ATOM   1133 C  CA    . PHE   A 1 144 ? 2.041   7.852  10.569 1.00 11.32 ? 141 PHE   A CA    1 
ATOM   1134 C  C     . PHE   A 1 144 ? 2.839   8.179  9.317  1.00 11.43 ? 141 PHE   A C     1 
ATOM   1135 O  O     . PHE   A 1 144 ? 3.043   7.314  8.472  1.00 12.15 ? 141 PHE   A O     1 
ATOM   1136 C  CB    . PHE   A 1 144 ? 2.882   6.897  11.416 1.00 11.76 ? 141 PHE   A CB    1 
ATOM   1137 C  CG    . PHE   A 1 144 ? 4.276   7.433  11.717 1.00 12.54 ? 141 PHE   A CG    1 
ATOM   1138 C  CD1   . PHE   A 1 144 ? 4.434   8.685  12.299 1.00 12.61 ? 141 PHE   A CD1   1 
ATOM   1139 C  CD2   . PHE   A 1 144 ? 5.406   6.706  11.387 1.00 14.09 ? 141 PHE   A CD2   1 
ATOM   1140 C  CE1   . PHE   A 1 144 ? 5.685   9.223  12.532 1.00 12.90 ? 141 PHE   A CE1   1 
ATOM   1141 C  CE2   . PHE   A 1 144 ? 6.652   7.224  11.659 1.00 14.07 ? 141 PHE   A CE2   1 
ATOM   1142 C  CZ    . PHE   A 1 144 ? 6.791   8.467  12.237 1.00 12.45 ? 141 PHE   A CZ    1 
ATOM   1143 N  N     . ILE   A 1 145 ? 3.297   9.426  9.237  1.00 11.41 ? 142 ILE   A N     1 
ATOM   1144 C  CA    . ILE   A 1 145 ? 4.100   9.959  8.121  1.00 11.53 ? 142 ILE   A CA    1 
ATOM   1145 C  C     . ILE   A 1 145 ? 5.292   10.767 8.678  1.00 11.38 ? 142 ILE   A C     1 
ATOM   1146 O  O     . ILE   A 1 145 ? 5.101   11.576 9.584  1.00 11.82 ? 142 ILE   A O     1 
ATOM   1147 C  CB    . ILE   A 1 145 ? 3.239   10.866 7.238  1.00 10.77 ? 142 ILE   A CB    1 
ATOM   1148 C  CG1   . ILE   A 1 145 ? 2.163   10.012 6.547  1.00 11.47 ? 142 ILE   A CG1   1 
ATOM   1149 C  CG2   . ILE   A 1 145 ? 4.100   11.585 6.198  1.00 10.66 ? 142 ILE   A CG2   1 
ATOM   1150 C  CD1   . ILE   A 1 145 ? 1.118   10.787 5.815  1.00 11.20 ? 142 ILE   A CD1   1 
ATOM   1151 N  N     . GLU   A 1 146 ? 6.488   10.541 8.146  1.00 11.60 ? 143 GLU   A N     1 
ATOM   1152 C  CA    . GLU   A 1 146 ? 7.642   11.408 8.490  1.00 11.12 ? 143 GLU   A CA    1 
ATOM   1153 C  C     . GLU   A 1 146 ? 7.775   12.451 7.370  1.00 12.80 ? 143 GLU   A C     1 
ATOM   1154 O  O     . GLU   A 1 146 ? 7.792   12.082 6.234  1.00 12.07 ? 143 GLU   A O     1 
ATOM   1155 C  CB    . GLU   A 1 146 ? 8.942   10.636 8.694  1.00 13.17 ? 143 GLU   A CB    1 
ATOM   1156 C  CG    . GLU   A 1 146 ? 8.933   9.871  9.983  1.00 14.00 ? 143 GLU   A CG    1 
ATOM   1157 C  CD    . GLU   A 1 146 ? 10.275  9.343  10.471 1.00 19.08 ? 143 GLU   A CD    1 
ATOM   1158 O  OE1   . GLU   A 1 146 ? 11.249  9.550  9.789  1.00 21.34 ? 143 GLU   A OE1   1 
ATOM   1159 O  OE2   . GLU   A 1 146 ? 10.320  8.782  11.524 1.00 16.75 ? 143 GLU   A OE2   1 
ATOM   1160 N  N     . THR   A 1 147 ? 7.922   13.707 7.768  1.00 11.34 ? 144 THR   A N     1 
ATOM   1161 C  CA    . THR   A 1 147 ? 8.032   14.802 6.795  1.00 12.17 ? 144 THR   A CA    1 
ATOM   1162 C  C     . THR   A 1 147 ? 9.263   15.657 7.046  1.00 13.39 ? 144 THR   A C     1 
ATOM   1163 O  O     . THR   A 1 147 ? 9.858   15.552 8.065  1.00 12.47 ? 144 THR   A O     1 
ATOM   1164 C  CB    . THR   A 1 147 ? 6.915   15.829 7.015  1.00 13.02 ? 144 THR   A CB    1 
ATOM   1165 O  OG1   . THR   A 1 147 ? 6.953   16.270 8.371  1.00 11.95 ? 144 THR   A OG1   1 
ATOM   1166 C  CG2   . THR   A 1 147 ? 5.557   15.248 6.705  1.00 12.99 ? 144 THR   A CG2   1 
ATOM   1167 N  N     . SER   A 1 148 ? 9.618   16.407 6.021  1.00 12.31 ? 145 SER   A N     1 
ATOM   1168 C  CA    . SER   A 1 148 ? 10.635  17.467 6.153  1.00 13.73 ? 145 SER   A CA    1 
ATOM   1169 C  C     . SER   A 1 148 ? 10.058  18.756 5.556  1.00 13.93 ? 145 SER   A C     1 
ATOM   1170 O  O     . SER   A 1 148 ? 9.839   18.806 4.369  1.00 14.64 ? 145 SER   A O     1 
ATOM   1171 C  CB    . SER   A 1 148 ? 11.933  17.115 5.512  1.00 15.03 ? 145 SER   A CB    1 
ATOM   1172 O  OG    . SER   A 1 148 ? 12.839  18.196 5.642  1.00 16.36 ? 145 SER   A OG    1 
ATOM   1173 N  N     . ALA   A 1 149 ? 9.715   19.708 6.418  1.00 14.08 ? 146 ALA   A N     1 
ATOM   1174 C  CA    . ALA   A 1 149 ? 9.344   21.064 5.952  1.00 15.50 ? 146 ALA   A CA    1 
ATOM   1175 C  C     . ALA   A 1 149 ? 10.477  21.737 5.176  1.00 18.11 ? 146 ALA   A C     1 
ATOM   1176 O  O     . ALA   A 1 149 ? 10.244  22.569 4.284  1.00 20.29 ? 146 ALA   A O     1 
ATOM   1177 C  CB    . ALA   A 1 149 ? 8.911   21.917 7.137  1.00 16.45 ? 146 ALA   A CB    1 
ATOM   1178 N  N     . LYS   A 1 150 ? 11.709  21.374 5.505  1.00 16.88 ? 147 LYS   A N     1 
ATOM   1179 C  CA    . LYS   A 1 150 ? 12.862  22.017 4.921  1.00 20.44 ? 147 LYS   A CA    1 
ATOM   1180 C  C     . LYS   A 1 150 ? 13.011  21.571 3.477  1.00 22.82 ? 147 LYS   A C     1 
ATOM   1181 O  O     . LYS   A 1 150 ? 13.216  22.410 2.610  1.00 25.55 ? 147 LYS   A O     1 
ATOM   1182 C  CB    . LYS   A 1 150 ? 14.120  21.714 5.695  1.00 20.79 ? 147 LYS   A CB    1 
ATOM   1183 C  CG    . LYS   A 1 150 ? 15.368  22.477 5.209  1.00 24.48 ? 147 LYS   A CG    1 
ATOM   1184 C  CD    . LYS   A 1 150 ? 16.557  22.215 6.117  1.00 26.72 ? 147 LYS   A CD    1 
ATOM   1185 C  CE    . LYS   A 1 150 ? 17.749  23.100 5.792  1.00 31.77 ? 147 LYS   A CE    1 
ATOM   1186 N  NZ    . LYS   A 1 150 ? 18.667  23.075 6.962  1.00 36.09 ? 147 LYS   A NZ    1 
ATOM   1187 N  N     . THR   A 1 151 ? 12.855  20.274 3.219  1.00 21.96 ? 148 THR   A N     1 
ATOM   1188 C  CA    . THR   A 1 151 ? 12.960  19.756 1.837  1.00 22.05 ? 148 THR   A CA    1 
ATOM   1189 C  C     . THR   A 1 151 ? 11.639  19.542 1.121  1.00 20.79 ? 148 THR   A C     1 
ATOM   1190 O  O     . THR   A 1 151 ? 11.649  19.217 -0.085 1.00 22.22 ? 148 THR   A O     1 
ATOM   1191 C  CB    . THR   A 1 151 ? 13.665  18.414 1.807  1.00 21.88 ? 148 THR   A CB    1 
ATOM   1192 O  OG1   . THR   A 1 151 ? 12.778  17.410 2.334  1.00 22.75 ? 148 THR   A OG1   1 
ATOM   1193 C  CG2   . THR   A 1 151 ? 14.940  18.484 2.587  1.00 24.05 ? 148 THR   A CG2   1 
ATOM   1194 N  N     . ARG   A 1 152 ? 10.528  19.706 1.849  1.00 18.55 ? 149 ARG   A N     1 
ATOM   1195 C  CA    . ARG   A 1 152 ? 9.172   19.492 1.376  1.00 19.65 ? 149 ARG   A CA    1 
ATOM   1196 C  C     . ARG   A 1 152 ? 8.774   17.999 1.292  1.00 19.85 ? 149 ARG   A C     1 
ATOM   1197 O  O     . ARG   A 1 152 ? 7.643   17.656 0.854  1.00 23.45 ? 149 ARG   A O     1 
ATOM   1198 C  CB    . ARG   A 1 152 ? 8.908   20.264 0.047  1.00 21.04 ? 149 ARG   A CB    1 
ATOM   1199 C  CG    . ARG   A 1 152 ? 7.580   20.980 0.071  1.00 24.04 ? 149 ARG   A CG    1 
ATOM   1200 C  CD    . ARG   A 1 152 ? 7.326   21.883 -1.132 1.00 24.05 ? 149 ARG   A CD    1 
ATOM   1201 N  NE    . ARG   A 1 152 ? 5.979   22.443 -1.000 1.00 24.85 ? 149 ARG   A NE    1 
ATOM   1202 C  CZ    . ARG   A 1 152 ? 4.898   21.907 -1.551 1.00 29.89 ? 149 ARG   A CZ    1 
ATOM   1203 N  NH1   . ARG   A 1 152 ? 4.987   20.792 -2.253 1.00 32.36 ? 149 ARG   A NH1   1 
ATOM   1204 N  NH2   . ARG   A 1 152 ? 3.713   22.475 -1.391 1.00 34.93 ? 149 ARG   A NH2   1 
ATOM   1205 N  N     . GLN   A 1 153 ? 9.610   17.111 1.847  1.00 14.98 ? 150 GLN   A N     1 
ATOM   1206 C  CA    . GLN   A 1 153 ? 9.364   15.668 1.765  1.00 14.58 ? 150 GLN   A CA    1 
ATOM   1207 C  C     . GLN   A 1 153 ? 8.068   15.322 2.500  1.00 13.88 ? 150 GLN   A C     1 
ATOM   1208 O  O     . GLN   A 1 153 ? 7.921   15.604 3.710  1.00 12.47 ? 150 GLN   A O     1 
ATOM   1209 C  CB    . GLN   A 1 153 ? 10.513  14.861 2.389  1.00 15.86 ? 150 GLN   A CB    1 
ATOM   1210 C  CG    . GLN   A 1 153 ? 10.577  13.426 1.874  1.00 17.69 ? 150 GLN   A CG    1 
ATOM   1211 C  CD    . GLN   A 1 153 ? 11.170  13.376 0.466  1.00 20.02 ? 150 GLN   A CD    1 
ATOM   1212 O  OE1   . GLN   A 1 153 ? 12.305  13.757 0.276  1.00 22.91 ? 150 GLN   A OE1   1 
ATOM   1213 N  NE2   . GLN   A 1 153 ? 10.389  12.968 -0.506 1.00 22.37 ? 150 GLN   A NE2   1 
ATOM   1214 N  N     . ARG   A 1 154 ? 7.132   14.746 1.749  1.00 12.90 ? 151 ARG   A N     1 
ATOM   1215 C  CA    . ARG   A 1 154 ? 5.827   14.267 2.262  1.00 12.17 ? 151 ARG   A CA    1 
ATOM   1216 C  C     . ARG   A 1 154 ? 4.894   15.328 2.881  1.00 12.62 ? 151 ARG   A C     1 
ATOM   1217 O  O     . ARG   A 1 154 ? 3.978   15.004 3.653  1.00 11.79 ? 151 ARG   A O     1 
ATOM   1218 C  CB    . ARG   A 1 154 ? 6.008   13.066 3.178  1.00 11.46 ? 151 ARG   A CB    1 
ATOM   1219 C  CG    . ARG   A 1 154 ? 6.678   11.895 2.488  1.00 12.97 ? 151 ARG   A CG    1 
ATOM   1220 C  CD    . ARG   A 1 154 ? 6.368   10.586 3.190  1.00 14.09 ? 151 ARG   A CD    1 
ATOM   1221 N  NE    . ARG   A 1 154 ? 5.061   10.081 2.876  1.00 14.56 ? 151 ARG   A NE    1 
ATOM   1222 C  CZ    . ARG   A 1 154 ? 4.500   9.044  3.484  1.00 14.29 ? 151 ARG   A CZ    1 
ATOM   1223 N  NH1   . ARG   A 1 154 ? 3.279   8.681  3.118  1.00 14.87 ? 151 ARG   A NH1   1 
ATOM   1224 N  NH2   . ARG   A 1 154 ? 5.148   8.413  4.453  1.00 14.36 ? 151 ARG   A NH2   1 
ATOM   1225 N  N     . VAL   A 1 155 ? 5.129   16.603 2.530  1.00 12.72 ? 152 VAL   A N     1 
ATOM   1226 C  CA    . VAL   A 1 155 ? 4.317   17.689 3.082  1.00 13.64 ? 152 VAL   A CA    1 
ATOM   1227 C  C     . VAL   A 1 155 ? 2.878   17.582 2.562  1.00 13.19 ? 152 VAL   A C     1 
ATOM   1228 O  O     . VAL   A 1 155 ? 1.938   17.523 3.351  1.00 13.65 ? 152 VAL   A O     1 
ATOM   1229 C  CB    . VAL   A 1 155 ? 4.925   19.089 2.847  1.00 15.21 ? 152 VAL   A CB    1 
ATOM   1230 C  CG1   . VAL   A 1 155 ? 3.938   20.140 3.325  1.00 16.18 ? 152 VAL   A CG1   1 
ATOM   1231 C  CG2   . VAL   A 1 155 ? 6.252   19.201 3.614  1.00 16.11 ? 152 VAL   A CG2   1 
ATOM   1232 N  N     . GLU   A 1 156 ? 2.723   17.539 1.235  1.00 13.82 ? 153 GLU   A N     1 
ATOM   1233 C  CA    . GLU   A 1 156 ? 1.375   17.346 0.663  1.00 14.76 ? 153 GLU   A CA    1 
ATOM   1234 C  C     . GLU   A 1 156 ? 0.792   16.001 1.142  1.00 13.22 ? 153 GLU   A C     1 
ATOM   1235 O  O     . GLU   A 1 156 ? -0.347  15.961 1.517  1.00 14.29 ? 153 GLU   A O     1 
ATOM   1236 C  CB    . GLU   A 1 156 ? 1.418   17.468 -0.856 1.00 17.96 ? 153 GLU   A CB    1 
ATOM   1237 C  CG    . GLU   A 1 156 ? 1.907   18.827 -1.343 1.00 20.88 ? 153 GLU   A CG    1 
ATOM   1238 C  CD    . GLU   A 1 156 ? 1.736   19.047 -2.839 1.00 29.03 ? 153 GLU   A CD    1 
ATOM   1239 O  OE1   . GLU   A 1 156 ? 2.667   18.864 -3.541 1.00 33.95 ? 153 GLU   A OE1   1 
ATOM   1240 O  OE2   . GLU   A 1 156 ? 0.661   19.441 -3.252 1.00 37.54 ? 153 GLU   A OE2   1 
ATOM   1241 N  N     . ASP   A 1 157 ? 1.595   14.946 1.194  1.00 13.98 ? 154 ASP   A N     1 
ATOM   1242 C  CA    . ASP   A 1 157 ? 1.066   13.628 1.632  1.00 14.06 ? 154 ASP   A CA    1 
ATOM   1243 C  C     . ASP   A 1 157 ? 0.474   13.715 3.049  1.00 13.04 ? 154 ASP   A C     1 
ATOM   1244 O  O     . ASP   A 1 157 ? -0.538  13.124 3.288  1.00 13.52 ? 154 ASP   A O     1 
ATOM   1245 C  CB    . ASP   A 1 157 ? 2.189   12.607 1.804  1.00 16.04 ? 154 ASP   A CB    1 
ATOM   1246 C  CG    . ASP   A 1 157 ? 2.557   11.782 0.596  1.00 22.74 ? 154 ASP   A CG    1 
ATOM   1247 O  OD1   . ASP   A 1 157 ? 1.865   11.893 -0.426 1.00 23.33 ? 154 ASP   A OD1   1 
ATOM   1248 O  OD2   . ASP   A 1 157 ? 3.526   11.055 0.687  1.00 24.12 ? 154 ASP   A OD2   1 
ATOM   1249 N  N     . ALA   A 1 158 ? 1.135   14.424 3.961  1.00 11.67 ? 155 ALA   A N     1 
ATOM   1250 C  CA    . ALA   A 1 158 ? 0.613   14.490 5.341  1.00 11.59 ? 155 ALA   A CA    1 
ATOM   1251 C  C     . ALA   A 1 158 ? -0.760  15.144 5.374  1.00 11.18 ? 155 ALA   A C     1 
ATOM   1252 O  O     . ALA   A 1 158 ? -1.618  14.605 6.014  1.00 12.58 ? 155 ALA   A O     1 
ATOM   1253 C  CB    . ALA   A 1 158 ? 1.578   15.221 6.245  1.00 13.34 ? 155 ALA   A CB    1 
ATOM   1254 N  N     . PHE   A 1 159 ? -0.879  16.299 4.723  1.00 11.74 ? 156 PHE   A N     1 
ATOM   1255 C  CA    . PHE   A 1 159 ? -2.168  17.024 4.769  1.00 11.92 ? 156 PHE   A CA    1 
ATOM   1256 C  C     . PHE   A 1 159 ? -3.243  16.250 3.990  1.00 11.77 ? 156 PHE   A C     1 
ATOM   1257 O  O     . PHE   A 1 159 ? -4.421  16.187 4.418  1.00 12.42 ? 156 PHE   A O     1 
ATOM   1258 C  CB    . PHE   A 1 159 ? -2.024  18.443 4.244  1.00 12.06 ? 156 PHE   A CB    1 
ATOM   1259 C  CG    . PHE   A 1 159 ? -1.351  19.391 5.196  1.00 12.62 ? 156 PHE   A CG    1 
ATOM   1260 C  CD1   . PHE   A 1 159 ? -2.080  20.023 6.195  1.00 13.26 ? 156 PHE   A CD1   1 
ATOM   1261 C  CD2   . PHE   A 1 159 ? 0.012   19.634 5.098  1.00 13.32 ? 156 PHE   A CD2   1 
ATOM   1262 C  CE1   . PHE   A 1 159 ? -1.452  20.917 7.067  1.00 14.58 ? 156 PHE   A CE1   1 
ATOM   1263 C  CE2   . PHE   A 1 159 ? 0.650   20.509 5.975  1.00 15.40 ? 156 PHE   A CE2   1 
ATOM   1264 C  CZ    . PHE   A 1 159 ? -0.096  21.167 6.944  1.00 13.77 ? 156 PHE   A CZ    1 
ATOM   1265 N  N     . TYR   A 1 160 ? -2.861  15.715 2.833  1.00 12.00 ? 157 TYR   A N     1 
ATOM   1266 C  CA    . TYR   A 1 160 ? -3.835  14.992 1.984  1.00 12.36 ? 157 TYR   A CA    1 
ATOM   1267 C  C     . TYR   A 1 160 ? -4.269  13.684 2.649  1.00 12.38 ? 157 TYR   A C     1 
ATOM   1268 O  O     . TYR   A 1 160 ? -5.362  13.277 2.488  1.00 12.29 ? 157 TYR   A O     1 
ATOM   1269 C  CB    . TYR   A 1 160 ? -3.275  14.716 0.597  1.00 13.46 ? 157 TYR   A CB    1 
ATOM   1270 C  CG    . TYR   A 1 160 ? -2.993  15.934 -0.232 1.00 14.45 ? 157 TYR   A CG    1 
ATOM   1271 C  CD1   . TYR   A 1 160 ? -3.111  17.207 0.275  1.00 14.85 ? 157 TYR   A CD1   1 
ATOM   1272 C  CD2   . TYR   A 1 160 ? -2.556  15.792 -1.522 1.00 15.88 ? 157 TYR   A CD2   1 
ATOM   1273 C  CE1   . TYR   A 1 160 ? -2.818  18.310 -0.500 1.00 17.57 ? 157 TYR   A CE1   1 
ATOM   1274 C  CE2   . TYR   A 1 160 ? -2.251  16.877 -2.314 1.00 18.63 ? 157 TYR   A CE2   1 
ATOM   1275 C  CZ    . TYR   A 1 160 ? -2.375  18.141 -1.793 1.00 18.89 ? 157 TYR   A CZ    1 
ATOM   1276 O  OH    . TYR   A 1 160 ? -2.085  19.195 -2.594 1.00 24.65 ? 157 TYR   A OH    1 
ATOM   1277 N  N     . THR   A 1 161 ? -3.351  13.058 3.379  1.00 11.28 ? 158 THR   A N     1 
ATOM   1278 C  CA    . THR   A 1 161 ? -3.715  11.840 4.137  1.00 10.69 ? 158 THR   A CA    1 
ATOM   1279 C  C     . THR   A 1 161 ? -4.786  12.216 5.174  1.00 11.82 ? 158 THR   A C     1 
ATOM   1280 O  O     . THR   A 1 161 ? -5.702  11.469 5.348  1.00 12.24 ? 158 THR   A O     1 
ATOM   1281 C  CB    . THR   A 1 161 ? -2.466  11.169 4.722  1.00 11.66 ? 158 THR   A CB    1 
ATOM   1282 O  OG1   . THR   A 1 161 ? -1.673  10.712 3.636  1.00 11.86 ? 158 THR   A OG1   1 
ATOM   1283 C  CG2   . THR   A 1 161 ? -2.802  10.039 5.664  1.00 12.29 ? 158 THR   A CG2   1 
ATOM   1284 N  N     . LEU   A 1 162 ? -4.644  13.365 5.831  1.00 10.55 ? 159 LEU   A N     1 
ATOM   1285 C  CA    . LEU   A 1 162 ? -5.664  13.771 6.832  1.00 11.69 ? 159 LEU   A CA    1 
ATOM   1286 C  C     . LEU   A 1 162 ? -7.030  14.005 6.154  1.00 11.90 ? 159 LEU   A C     1 
ATOM   1287 O  O     . LEU   A 1 162 ? -8.008  13.628 6.708  1.00 13.02 ? 159 LEU   A O     1 
ATOM   1288 C  CB    . LEU   A 1 162 ? -5.160  15.016 7.569  1.00 11.82 ? 159 LEU   A CB    1 
ATOM   1289 C  CG    . LEU   A 1 162 ? -6.062  15.567 8.668  1.00 11.03 ? 159 LEU   A CG    1 
ATOM   1290 C  CD1   . LEU   A 1 162 ? -6.354  14.520 9.715  1.00 11.62 ? 159 LEU   A CD1   1 
ATOM   1291 C  CD2   . LEU   A 1 162 ? -5.359  16.730 9.303  1.00 12.23 ? 159 LEU   A CD2   1 
ATOM   1292 N  N     . VAL   A 1 163 ? -7.035  14.671 5.013  1.00 11.15 ? 160 VAL   A N     1 
ATOM   1293 C  CA    . VAL   A 1 163 ? -8.270  14.816 4.236  1.00 12.19 ? 160 VAL   A CA    1 
ATOM   1294 C  C     . VAL   A 1 163 ? -8.934  13.463 3.980  1.00 13.09 ? 160 VAL   A C     1 
ATOM   1295 O  O     . VAL   A 1 163 ? -10.145 13.265 4.195  1.00 12.64 ? 160 VAL   A O     1 
ATOM   1296 C  CB    . VAL   A 1 163 ? -8.001  15.561 2.912  1.00 12.42 ? 160 VAL   A CB    1 
ATOM   1297 C  CG1   . VAL   A 1 163 ? -9.201  15.478 1.974  1.00 14.57 ? 160 VAL   A CG1   1 
ATOM   1298 C  CG2   . VAL   A 1 163 ? -7.613  17.002 3.174  1.00 14.01 ? 160 VAL   A CG2   1 
ATOM   1299 N  N     . ARG   A 1 164 ? -8.149  12.510 3.506  1.00 12.22 ? 161 ARG   A N     1 
ATOM   1300 C  CA    . ARG   A 1 164 ? -8.660  11.139 3.296  1.00 13.02 ? 161 ARG   A CA    1 
ATOM   1301 C  C     . ARG   A 1 164 ? -9.247  10.516 4.562  1.00 13.32 ? 161 ARG   A C     1 
ATOM   1302 O  O     . ARG   A 1 164 ? -10.297 9.853  4.499  1.00 13.98 ? 161 ARG   A O     1 
ATOM   1303 C  CB    . ARG   A 1 164 ? -7.548  10.249 2.747  1.00 13.28 ? 161 ARG   A CB    1 
ATOM   1304 C  CG    . ARG   A 1 164 ? -7.171  10.644 1.311  1.00 14.46 ? 161 ARG   A CG    1 
ATOM   1305 C  CD    . ARG   A 1 164 ? -5.920  9.946  0.827  1.00 15.48 ? 161 ARG   A CD    1 
ATOM   1306 N  NE    . ARG   A 1 164 ? -5.805  9.994  -0.637 1.00 16.61 ? 161 ARG   A NE    1 
ATOM   1307 C  CZ    . ARG   A 1 164 ? -4.753  9.533  -1.327 1.00 21.58 ? 161 ARG   A CZ    1 
ATOM   1308 N  NH1   . ARG   A 1 164 ? -3.664  9.083  -0.692 1.00 23.42 ? 161 ARG   A NH1   1 
ATOM   1309 N  NH2   . ARG   A 1 164 ? -4.778  9.505  -2.672 1.00 22.46 ? 161 ARG   A NH2   1 
ATOM   1310 N  N     . GLU   A 1 165 ? -8.622  10.757 5.710  1.00 12.63 ? 162 GLU   A N     1 
ATOM   1311 C  CA    . GLU   A 1 165 ? -9.123  10.230 6.979  1.00 12.68 ? 162 GLU   A CA    1 
ATOM   1312 C  C     . GLU   A 1 165 ? -10.486 10.877 7.271  1.00 12.84 ? 162 GLU   A C     1 
ATOM   1313 O  O     . GLU   A 1 165 ? -11.418 10.181 7.695  1.00 15.69 ? 162 GLU   A O     1 
ATOM   1314 C  CB    . GLU   A 1 165 ? -8.178  10.485 8.152  1.00 12.84 ? 162 GLU   A CB    1 
ATOM   1315 C  CG    . GLU   A 1 165 ? -6.888  9.676  8.089  1.00 14.14 ? 162 GLU   A CG    1 
ATOM   1316 C  CD    . GLU   A 1 165 ? -7.133  8.176  8.237  1.00 16.17 ? 162 GLU   A CD    1 
ATOM   1317 O  OE1   . GLU   A 1 165 ? -7.587  7.729  9.309  1.00 19.13 ? 162 GLU   A OE1   1 
ATOM   1318 O  OE2   . GLU   A 1 165 ? -6.827  7.411  7.293  1.00 19.29 ? 162 GLU   A OE2   1 
ATOM   1319 N  N     . ILE   A 1 166 ? -10.580 12.177 7.088  1.00 13.56 ? 163 ILE   A N     1 
ATOM   1320 C  CA    . ILE   A 1 166 ? -11.882 12.861 7.318  1.00 14.28 ? 163 ILE   A CA    1 
ATOM   1321 C  C     . ILE   A 1 166 ? -12.964 12.322 6.383  1.00 15.97 ? 163 ILE   A C     1 
ATOM   1322 O  O     . ILE   A 1 166 ? -14.096 11.952 6.814  1.00 16.53 ? 163 ILE   A O     1 
ATOM   1323 C  CB    . ILE   A 1 166 ? -11.798 14.384 7.138  1.00 14.75 ? 163 ILE   A CB    1 
ATOM   1324 C  CG1   . ILE   A 1 166 ? -10.910 15.025 8.216  1.00 14.82 ? 163 ILE   A CG1   1 
ATOM   1325 C  CG2   . ILE   A 1 166 ? -13.206 15.024 7.154  1.00 14.95 ? 163 ILE   A CG2   1 
ATOM   1326 C  CD1   . ILE   A 1 166 ? -10.402 16.373 7.802  1.00 14.64 ? 163 ILE   A CD1   1 
ATOM   1327 N  N     . ARG   A 1 167 ? -12.616 12.227 5.098  1.00 15.46 ? 164 ARG   A N     1 
ATOM   1328 C  CA    . ARG   A 1 167 ? -13.586 11.803 4.104  1.00 18.01 ? 164 ARG   A CA    1 
ATOM   1329 C  C     . ARG   A 1 167 ? -14.132 10.446 4.509  1.00 18.58 ? 164 ARG   A C     1 
ATOM   1330 O  O     . ARG   A 1 167 ? -15.360 10.209 4.414  1.00 20.89 ? 164 ARG   A O     1 
ATOM   1331 C  CB    . ARG   A 1 167 ? -12.929 11.817 2.694  1.00 16.66 ? 164 ARG   A CB    1 
ATOM   1332 C  CG    . ARG   A 1 167 ? -13.911 11.675 1.568  1.00 20.69 ? 164 ARG   A CG    1 
ATOM   1333 C  CD    . ARG   A 1 167 ? -13.121 11.350 0.331  1.00 20.06 ? 164 ARG   A CD    1 
ATOM   1334 N  NE    . ARG   A 1 167 ? -12.475 12.523 -0.261 1.00 17.93 ? 164 ARG   A NE    1 
ATOM   1335 C  CZ    . ARG   A 1 167 ? -11.236 12.553 -0.781 1.00 18.05 ? 164 ARG   A CZ    1 
ATOM   1336 N  NH1   . ARG   A 1 167 ? -10.842 13.648 -1.416 1.00 17.94 ? 164 ARG   A NH1   1 
ATOM   1337 N  NH2   . ARG   A 1 167 ? -10.384 11.524 -0.695 1.00 16.17 ? 164 ARG   A NH2   1 
ATOM   1338 N  N     . GLN   A 1 168 ? -13.269 9.545  4.981  1.00 19.23 ? 165 GLN   A N     1 
ATOM   1339 C  CA    . GLN   A 1 168 ? -13.679 8.239  5.402  1.00 22.98 ? 165 GLN   A CA    1 
ATOM   1340 C  C     . GLN   A 1 168 ? -14.548 8.205  6.649  1.00 22.37 ? 165 GLN   A C     1 
ATOM   1341 O  O     . GLN   A 1 168 ? -15.542 7.482  6.705  1.00 21.40 ? 165 GLN   A O     1 
ATOM   1342 C  CB    . GLN   A 1 168 ? -12.495 7.328  5.628  1.00 26.38 ? 165 GLN   A CB    1 
ATOM   1343 C  CG    . GLN   A 1 168 ? -11.794 6.955  4.331  1.00 29.90 ? 165 GLN   A CG    1 
ATOM   1344 C  CD    . GLN   A 1 168 ? -10.411 6.413  4.582  1.00 33.75 ? 165 GLN   A CD    1 
ATOM   1345 O  OE1   . GLN   A 1 168 ? -10.204 5.639  5.525  1.00 36.52 ? 165 GLN   A OE1   1 
ATOM   1346 N  NE2   . GLN   A 1 168 ? -9.439  6.825  3.753  1.00 27.44 ? 165 GLN   A NE2   1 
ATOM   1347 N  N     . TYR   A 1 169 ? -14.140 8.927  7.674  1.00 18.27 ? 166 TYR   A N     1 
ATOM   1348 C  CA    . TYR   A 1 169 ? -14.976 9.030  8.863  1.00 17.52 ? 166 TYR   A CA    1 
ATOM   1349 C  C     . TYR   A 1 169 ? -16.381 9.580  8.579  1.00 18.09 ? 166 TYR   A C     1 
ATOM   1350 O  O     . TYR   A 1 169 ? -17.333 9.230  9.307  1.00 19.75 ? 166 TYR   A O     1 
ATOM   1351 C  CB    . TYR   A 1 169 ? -14.248 9.893  9.898  1.00 18.03 ? 166 TYR   A CB    1 
ATOM   1352 C  CG    . TYR   A 1 169 ? -13.366 9.101  10.832 1.00 19.50 ? 166 TYR   A CG    1 
ATOM   1353 C  CD1   . TYR   A 1 169 ? -13.916 8.317  11.839 1.00 22.76 ? 166 TYR   A CD1   1 
ATOM   1354 C  CD2   . TYR   A 1 169 ? -11.993 9.106  10.704 1.00 20.61 ? 166 TYR   A CD2   1 
ATOM   1355 C  CE1   . TYR   A 1 169 ? -13.114 7.607  12.724 1.00 25.36 ? 166 TYR   A CE1   1 
ATOM   1356 C  CE2   . TYR   A 1 169 ? -11.184 8.397  11.565 1.00 22.90 ? 166 TYR   A CE2   1 
ATOM   1357 C  CZ    . TYR   A 1 169 ? -11.741 7.678  12.597 1.00 26.06 ? 166 TYR   A CZ    1 
ATOM   1358 O  OH    . TYR   A 1 169 ? -10.950 6.956  13.449 1.00 29.56 ? 166 TYR   A OH    1 
ATOM   1359 N  N     . ARG   A 1 170 ? -16.537 10.398 7.545  1.00 18.30 ? 167 ARG   A N     1 
ATOM   1360 C  CA    . ARG   A 1 170 ? -17.863 10.973 7.172  1.00 20.07 ? 167 ARG   A CA    1 
ATOM   1361 C  C     . ARG   A 1 170 ? -18.801 9.857  6.714  1.00 22.44 ? 167 ARG   A C     1 
ATOM   1362 O  O     . ARG   A 1 170 ? -20.029 10.012 6.788  1.00 21.10 ? 167 ARG   A O     1 
ATOM   1363 C  CB    . ARG   A 1 170 ? -17.750 12.089 6.079  1.00 19.88 ? 167 ARG   A CB    1 
ATOM   1364 C  CG    . ARG   A 1 170 ? -17.123 13.418 6.494  1.00 19.78 ? 167 ARG   A CG    1 
ATOM   1365 C  CD    . ARG   A 1 170 ? -17.123 14.469 5.388  1.00 21.06 ? 167 ARG   A CD    1 
ATOM   1366 N  NE    . ARG   A 1 170 ? -16.625 15.777 5.857  1.00 22.54 ? 167 ARG   A NE    1 
ATOM   1367 C  CZ    . ARG   A 1 170 ? -15.884 16.628 5.145  1.00 24.24 ? 167 ARG   A CZ    1 
ATOM   1368 N  NH1   . ARG   A 1 170 ? -15.567 16.358 3.880  1.00 26.88 ? 167 ARG   A NH1   1 
ATOM   1369 N  NH2   . ARG   A 1 170 ? -15.482 17.790 5.688  1.00 26.36 ? 167 ARG   A NH2   1 
ATOM   1370 N  N     . LEU   A 1 171 ? -18.259 8.712  6.290  1.00 22.99 ? 168 LEU   A N     1 
ATOM   1371 C  CA    . LEU   A 1 171 ? -19.083 7.537  5.929  1.00 26.04 ? 168 LEU   A CA    1 
ATOM   1372 C  C     . LEU   A 1 171 ? -19.391 6.577  7.068  1.00 27.03 ? 168 LEU   A C     1 
ATOM   1373 O  O     . LEU   A 1 171 ? -20.189 5.641  6.893  1.00 30.11 ? 168 LEU   A O     1 
ATOM   1374 C  CB    . LEU   A 1 171 ? -18.426 6.731  4.787  1.00 27.40 ? 168 LEU   A CB    1 
ATOM   1375 C  CG    . LEU   A 1 171 ? -18.225 7.474  3.473  1.00 28.86 ? 168 LEU   A CG    1 
ATOM   1376 C  CD1   . LEU   A 1 171 ? -17.577 6.506  2.470  1.00 32.23 ? 168 LEU   A CD1   1 
ATOM   1377 C  CD2   . LEU   A 1 171 ? -19.478 8.126  2.880  1.00 30.68 ? 168 LEU   A CD2   1 
ATOM   1378 N  N     . LYS   A 1 172 ? -18.786 6.793  8.233  1.00 29.57 ? 169 LYS   A N     1 
ATOM   1379 C  CA    . LYS   A 1 172 ? -18.936 5.915  9.379  1.00 27.62 ? 169 LYS   A CA    1 
ATOM   1380 C  C     . LYS   A 1 172 ? -19.935 6.537  10.366 1.00 27.31 ? 169 LYS   A C     1 
ATOM   1381 O  O     . LYS   A 1 172 ? -20.790 5.843  10.914 1.00 28.55 ? 169 LYS   A O     1 
ATOM   1382 C  CB    . LYS   A 1 172 ? -17.586 5.696  10.056 1.00 30.24 ? 169 LYS   A CB    1 
ATOM   1383 C  CG    . LYS   A 1 172 ? -17.638 4.769  11.270 1.00 34.27 ? 169 LYS   A CG    1 
ATOM   1384 C  CD    . LYS   A 1 172 ? -16.456 5.004  12.200 1.00 35.86 ? 169 LYS   A CD    1 
ATOM   1385 C  CE    . LYS   A 1 172 ? -16.572 4.184  13.474 1.00 38.32 ? 169 LYS   A CE    1 
ATOM   1386 N  NZ    . LYS   A 1 172 ? -15.253 4.079  14.168 1.00 40.69 ? 169 LYS   A NZ    1 
ATOM   1387 O  OXT   . LYS   A 1 172 ? -19.929 7.752  10.590 1.00 22.44 ? 169 LYS   A OXT   1 
HETATM 1388 P  PB    . GDP   B 2 .   ? 6.285   25.646 15.418 1.00 16.29 ? 201 GDP   A PB    1 
HETATM 1389 O  O1B   . GDP   B 2 .   ? 5.468   26.525 14.529 1.00 16.59 ? 201 GDP   A O1B   1 
HETATM 1390 O  O2B   . GDP   B 2 .   ? 5.890   24.204 15.615 1.00 16.25 ? 201 GDP   A O2B   1 
HETATM 1391 O  O3B   . GDP   B 2 .   ? 6.596   26.342 16.736 1.00 18.89 ? 201 GDP   A O3B   1 
HETATM 1392 O  O3A   . GDP   B 2 .   ? 7.707   25.494 14.660 1.00 16.00 ? 201 GDP   A O3A   1 
HETATM 1393 P  PA    . GDP   B 2 .   ? 8.320   26.337 13.402 1.00 17.72 ? 201 GDP   A PA    1 
HETATM 1394 O  O1A   . GDP   B 2 .   ? 7.685   25.923 12.113 1.00 17.12 ? 201 GDP   A O1A   1 
HETATM 1395 O  O2A   . GDP   B 2 .   ? 8.401   27.824 13.706 1.00 19.41 ? 201 GDP   A O2A   1 
HETATM 1396 O  "O5'" . GDP   B 2 .   ? 9.762   25.674 13.342 1.00 16.44 ? 201 GDP   A "O5'" 1 
HETATM 1397 C  "C5'" . GDP   B 2 .   ? 10.721  25.722 14.433 1.00 17.13 ? 201 GDP   A "C5'" 1 
HETATM 1398 C  "C4'" . GDP   B 2 .   ? 12.165  25.709 13.956 1.00 17.73 ? 201 GDP   A "C4'" 1 
HETATM 1399 O  "O4'" . GDP   B 2 .   ? 12.480  24.414 13.380 1.00 17.90 ? 201 GDP   A "O4'" 1 
HETATM 1400 C  "C3'" . GDP   B 2 .   ? 12.443  26.751 12.885 1.00 18.66 ? 201 GDP   A "C3'" 1 
HETATM 1401 O  "O3'" . GDP   B 2 .   ? 13.789  27.228 13.052 1.00 20.52 ? 201 GDP   A "O3'" 1 
HETATM 1402 C  "C2'" . GDP   B 2 .   ? 12.309  25.985 11.567 1.00 17.37 ? 201 GDP   A "C2'" 1 
HETATM 1403 O  "O2'" . GDP   B 2 .   ? 13.081  26.554 10.490 1.00 19.54 ? 201 GDP   A "O2'" 1 
HETATM 1404 C  "C1'" . GDP   B 2 .   ? 12.791  24.601 12.007 1.00 17.43 ? 201 GDP   A "C1'" 1 
HETATM 1405 N  N9    . GDP   B 2 .   ? 12.135  23.534 11.232 1.00 16.49 ? 201 GDP   A N9    1 
HETATM 1406 C  C8    . GDP   B 2 .   ? 10.815  23.359 11.005 1.00 16.23 ? 201 GDP   A C8    1 
HETATM 1407 N  N7    . GDP   B 2 .   ? 10.627  22.267 10.265 1.00 16.02 ? 201 GDP   A N7    1 
HETATM 1408 C  C5    . GDP   B 2 .   ? 11.829  21.736 9.995  1.00 14.65 ? 201 GDP   A C5    1 
HETATM 1409 C  C6    . GDP   B 2 .   ? 12.335  20.598 9.226  1.00 15.68 ? 201 GDP   A C6    1 
HETATM 1410 O  O6    . GDP   B 2 .   ? 11.567  19.825 8.617  1.00 14.39 ? 201 GDP   A O6    1 
HETATM 1411 N  N1    . GDP   B 2 .   ? 13.667  20.418 9.214  1.00 15.22 ? 201 GDP   A N1    1 
HETATM 1412 C  C2    . GDP   B 2 .   ? 14.527  21.260 9.827  1.00 17.14 ? 201 GDP   A C2    1 
HETATM 1413 N  N2    . GDP   B 2 .   ? 15.839  21.064 9.786  1.00 17.62 ? 201 GDP   A N2    1 
HETATM 1414 N  N3    . GDP   B 2 .   ? 14.143  22.310 10.557 1.00 16.57 ? 201 GDP   A N3    1 
HETATM 1415 C  C4    . GDP   B 2 .   ? 12.813  22.576 10.629 1.00 15.89 ? 201 GDP   A C4    1 
HETATM 1416 MG MG    . MG    C 3 .   ? 4.428   28.315 14.677 1.00 16.62 2 202 MG    A MG    1 
HETATM 1417 N  NAP   . A1IMC D 4 .   ? -9.153  31.527 12.350 1.00 45.79 ? 203 A1IMC A NAP   1 
HETATM 1418 C  CAO   . A1IMC D 4 .   ? -8.214  31.910 13.240 1.00 45.08 ? 203 A1IMC A CAO   1 
HETATM 1419 C  CAN   . A1IMC D 4 .   ? -7.214  32.873 13.093 1.00 47.08 ? 203 A1IMC A CAN   1 
HETATM 1420 C  CAM   . A1IMC D 4 .   ? -6.332  33.136 14.132 1.00 47.37 ? 203 A1IMC A CAM   1 
HETATM 1421 C  CAL   . A1IMC D 4 .   ? -6.438  32.444 15.337 1.00 46.49 ? 203 A1IMC A CAL   1 
HETATM 1422 C  CAK   . A1IMC D 4 .   ? -7.433  31.482 15.498 1.00 42.85 ? 203 A1IMC A CAK   1 
HETATM 1423 CL CLAJ  . A1IMC D 4 .   ? -7.552  30.620 16.989 1.00 48.77 ? 203 A1IMC A CLAJ  1 
HETATM 1424 C  CAS   . A1IMC D 4 .   ? -8.312  31.222 14.460 1.00 43.03 ? 203 A1IMC A CAS   1 
HETATM 1425 S  SAR   . A1IMC D 4 .   ? -9.624  30.130 14.359 1.00 42.81 ? 203 A1IMC A SAR   1 
HETATM 1426 C  CAQ   . A1IMC D 4 .   ? -10.005 30.564 12.756 1.00 42.90 ? 203 A1IMC A CAQ   1 
HETATM 1427 N  NAT   . A1IMC D 4 .   ? -10.999 30.063 12.024 1.00 42.59 ? 203 A1IMC A NAT   1 
HETATM 1428 S  SAB   . A1IMC D 4 .   ? -11.954 28.771 12.424 1.00 37.76 ? 203 A1IMC A SAB   1 
HETATM 1429 O  OAA   . A1IMC D 4 .   ? -12.354 28.765 13.895 1.00 45.59 ? 203 A1IMC A OAA   1 
HETATM 1430 O  OAU   . A1IMC D 4 .   ? -13.165 28.758 11.515 1.00 39.17 ? 203 A1IMC A OAU   1 
HETATM 1431 C  CAC   . A1IMC D 4 .   ? -11.059 27.270 12.030 1.00 34.22 ? 203 A1IMC A CAC   1 
HETATM 1432 C  CAH   . A1IMC D 4 .   ? -10.952 26.263 12.991 1.00 32.43 ? 203 A1IMC A CAH   1 
HETATM 1433 C  CAG   . A1IMC D 4 .   ? -10.272 25.095 12.698 1.00 26.70 ? 203 A1IMC A CAG   1 
HETATM 1434 C  CAF   . A1IMC D 4 .   ? -9.692  24.888 11.436 1.00 26.43 ? 203 A1IMC A CAF   1 
HETATM 1435 C  CAE   . A1IMC D 4 .   ? -9.798  25.869 10.476 1.00 28.04 ? 203 A1IMC A CAE   1 
HETATM 1436 C  CAD   . A1IMC D 4 .   ? -10.481 27.058 10.778 1.00 31.25 ? 203 A1IMC A CAD   1 
HETATM 1437 O  OAI   . A1IMC D 4 .   ? -10.591 28.028 9.850  1.00 32.34 ? 203 A1IMC A OAI   1 
HETATM 1438 C  C1    . EDO   E 5 .   ? -4.479  11.526 -6.126 1.00 27.96 ? 204 EDO   A C1    1 
HETATM 1439 O  O1    . EDO   E 5 .   ? -5.142  12.619 -5.563 1.00 24.56 ? 204 EDO   A O1    1 
HETATM 1440 C  C2    . EDO   E 5 .   ? -5.441  10.441 -6.611 1.00 27.22 ? 204 EDO   A C2    1 
HETATM 1441 O  O2    . EDO   E 5 .   ? -6.255  11.053 -7.555 1.00 28.61 ? 204 EDO   A O2    1 
HETATM 1442 O  O     . HOH   F 6 .   ? -4.219  9.728  24.018 1.00 36.49 ? 301 HOH   A O     1 
HETATM 1443 O  O     . HOH   F 6 .   ? -3.714  27.927 20.302 1.00 26.50 ? 302 HOH   A O     1 
HETATM 1444 O  O     . HOH   F 6 .   ? -8.471  7.071  13.181 1.00 25.38 ? 303 HOH   A O     1 
HETATM 1445 O  O     . HOH   F 6 .   ? 8.452   11.305 30.453 1.00 31.10 ? 304 HOH   A O     1 
HETATM 1446 O  O     . HOH   F 6 .   ? 7.377   20.124 24.798 1.00 40.56 ? 305 HOH   A O     1 
HETATM 1447 O  O     . HOH   F 6 .   ? 2.571   27.431 14.690 1.00 19.62 ? 306 HOH   A O     1 
HETATM 1448 O  O     . HOH   F 6 .   ? -3.748  14.652 -4.884 1.00 26.67 ? 307 HOH   A O     1 
HETATM 1449 O  O     . HOH   F 6 .   ? 10.273  8.573  25.497 1.00 34.33 ? 308 HOH   A O     1 
HETATM 1450 O  O     . HOH   F 6 .   ? 8.135   -1.956 9.430  1.00 32.64 ? 309 HOH   A O     1 
HETATM 1451 O  O     . HOH   F 6 .   ? -8.433  6.006  15.675 1.00 35.37 ? 310 HOH   A O     1 
HETATM 1452 O  O     . HOH   F 6 .   ? 6.353   29.214 14.487 1.00 20.97 ? 311 HOH   A O     1 
HETATM 1453 O  O     . HOH   F 6 .   ? 17.208  16.119 21.231 1.00 40.43 ? 312 HOH   A O     1 
HETATM 1454 O  O     . HOH   F 6 .   ? -6.857  13.517 -8.197 1.00 21.50 ? 313 HOH   A O     1 
HETATM 1455 O  O     . HOH   F 6 .   ? 10.974  31.754 3.250  1.00 34.28 ? 314 HOH   A O     1 
HETATM 1456 O  O     . HOH   F 6 .   ? 7.219   22.988 -4.611 1.00 45.53 ? 315 HOH   A O     1 
HETATM 1457 O  O     . HOH   F 6 .   ? -16.665 21.852 11.896 1.00 33.09 ? 316 HOH   A O     1 
HETATM 1458 O  O     . HOH   F 6 .   ? -4.992  31.130 20.859 1.00 42.65 ? 317 HOH   A O     1 
HETATM 1459 O  O     . HOH   F 6 .   ? 2.644   -2.448 17.174 1.00 50.96 ? 318 HOH   A O     1 
HETATM 1460 O  O     . HOH   F 6 .   ? 3.660   30.236 14.942 1.00 22.12 ? 319 HOH   A O     1 
HETATM 1461 O  O     . HOH   F 6 .   ? -16.272 13.715 -0.316 1.00 30.80 ? 320 HOH   A O     1 
HETATM 1462 O  O     . HOH   F 6 .   ? -14.565 27.938 23.950 1.00 36.74 ? 321 HOH   A O     1 
HETATM 1463 O  O     . HOH   F 6 .   ? 1.022   32.712 10.093 1.00 31.94 ? 322 HOH   A O     1 
HETATM 1464 O  O     . HOH   F 6 .   ? -8.950  24.941 -8.240 1.00 48.52 ? 323 HOH   A O     1 
HETATM 1465 O  O     . HOH   F 6 .   ? -17.497 8.731  12.417 1.00 20.59 ? 324 HOH   A O     1 
HETATM 1466 O  O     . HOH   F 6 .   ? -4.054  0.156  14.208 1.00 36.02 ? 325 HOH   A O     1 
HETATM 1467 O  O     . HOH   F 6 .   ? 19.029  19.616 7.041  1.00 28.40 ? 326 HOH   A O     1 
HETATM 1468 O  O     . HOH   F 6 .   ? 23.564  15.963 13.995 1.00 22.26 ? 327 HOH   A O     1 
HETATM 1469 O  O     . HOH   F 6 .   ? -0.823  3.101  11.731 1.00 30.36 ? 328 HOH   A O     1 
HETATM 1470 O  O     . HOH   F 6 .   ? -7.319  9.057  11.642 1.00 16.21 ? 329 HOH   A O     1 
HETATM 1471 O  O     . HOH   F 6 .   ? -8.475  8.701  16.101 1.00 28.32 ? 330 HOH   A O     1 
HETATM 1472 O  O     . HOH   F 6 .   ? -16.182 14.356 2.179  1.00 36.87 ? 331 HOH   A O     1 
HETATM 1473 O  O     . HOH   F 6 .   ? 6.294   -1.279 12.578 1.00 31.35 ? 332 HOH   A O     1 
HETATM 1474 O  O     . HOH   F 6 .   ? -17.489 20.573 14.370 1.00 26.47 ? 333 HOH   A O     1 
HETATM 1475 O  O     . HOH   F 6 .   ? 3.520   6.554  5.916  1.00 14.74 ? 334 HOH   A O     1 
HETATM 1476 O  O     . HOH   F 6 .   ? -5.721  7.603  22.550 1.00 33.74 ? 335 HOH   A O     1 
HETATM 1477 O  O     . HOH   F 6 .   ? 10.999  20.479 18.718 1.00 37.96 ? 336 HOH   A O     1 
HETATM 1478 O  O     . HOH   F 6 .   ? -3.162  25.894 30.487 1.00 37.62 ? 337 HOH   A O     1 
HETATM 1479 O  O     . HOH   F 6 .   ? 7.927   26.829 5.780  1.00 19.65 ? 338 HOH   A O     1 
HETATM 1480 O  O     . HOH   F 6 .   ? -4.444  33.695 5.831  1.00 49.70 ? 339 HOH   A O     1 
HETATM 1481 O  O     . HOH   F 6 .   ? -5.735  8.205  4.928  1.00 30.85 ? 340 HOH   A O     1 
HETATM 1482 O  O     . HOH   F 6 .   ? 13.494  19.859 17.090 1.00 18.01 ? 341 HOH   A O     1 
HETATM 1483 O  O     . HOH   F 6 .   ? 6.697   -0.974 15.317 1.00 33.16 ? 342 HOH   A O     1 
HETATM 1484 O  O     . HOH   F 6 .   ? 13.933  14.932 2.210  1.00 28.21 ? 343 HOH   A O     1 
HETATM 1485 O  O     . HOH   F 6 .   ? 15.579  10.618 9.018  1.00 16.46 ? 344 HOH   A O     1 
HETATM 1486 O  O     . HOH   F 6 .   ? -17.674 15.199 18.224 1.00 19.48 ? 345 HOH   A O     1 
HETATM 1487 O  O     . HOH   F 6 .   ? 8.847   27.854 17.193 1.00 22.80 ? 346 HOH   A O     1 
HETATM 1488 O  O     . HOH   F 6 .   ? 0.455   30.869 11.931 1.00 30.27 ? 347 HOH   A O     1 
HETATM 1489 O  O     . HOH   F 6 .   ? 10.351  29.393 14.851 1.00 39.38 ? 348 HOH   A O     1 
HETATM 1490 O  O     . HOH   F 6 .   ? 4.553   28.192 16.677 1.00 21.76 ? 349 HOH   A O     1 
HETATM 1491 O  O     . HOH   F 6 .   ? 3.040   10.411 23.412 1.00 22.80 ? 350 HOH   A O     1 
HETATM 1492 O  O     . HOH   F 6 .   ? 14.238  13.886 4.788  1.00 25.28 ? 351 HOH   A O     1 
HETATM 1493 O  O     . HOH   F 6 .   ? -15.843 14.524 26.800 1.00 34.45 ? 352 HOH   A O     1 
HETATM 1494 O  O     . HOH   F 6 .   ? 5.219   17.465 -0.477 1.00 20.63 ? 353 HOH   A O     1 
HETATM 1495 O  O     . HOH   F 6 .   ? -8.215  7.459  -5.182 1.00 14.80 ? 354 HOH   A O     1 
HETATM 1496 O  O     . HOH   F 6 .   ? -2.785  8.741  2.012  1.00 23.73 ? 355 HOH   A O     1 
HETATM 1497 O  O     . HOH   F 6 .   ? 3.792   26.291 19.365 1.00 26.43 ? 356 HOH   A O     1 
HETATM 1498 O  O     . HOH   F 6 .   ? -1.938  18.756 -5.354 1.00 39.55 ? 357 HOH   A O     1 
HETATM 1499 O  O     . HOH   F 6 .   ? -18.510 9.155  21.315 1.00 42.52 ? 358 HOH   A O     1 
HETATM 1500 O  O     . HOH   F 6 .   ? -16.758 19.360 17.884 1.00 38.61 ? 359 HOH   A O     1 
HETATM 1501 O  O     . HOH   F 6 .   ? 4.477   17.544 19.777 1.00 15.15 ? 360 HOH   A O     1 
HETATM 1502 O  O     . HOH   F 6 .   ? -21.391 10.519 24.077 1.00 40.20 ? 361 HOH   A O     1 
HETATM 1503 O  O     . HOH   F 6 .   ? 7.261   14.416 -1.055 1.00 21.60 ? 362 HOH   A O     1 
HETATM 1504 O  O     . HOH   F 6 .   ? 9.499   20.110 23.154 1.00 35.25 ? 363 HOH   A O     1 
HETATM 1505 O  O     . HOH   F 6 .   ? -14.552 20.533 -9.241 1.00 32.49 ? 364 HOH   A O     1 
HETATM 1506 O  O     . HOH   F 6 .   ? 5.358   28.391 -5.825 1.00 39.68 ? 365 HOH   A O     1 
HETATM 1507 O  O     . HOH   F 6 .   ? -15.043 18.091 -6.775 1.00 20.38 ? 366 HOH   A O     1 
HETATM 1508 O  O     . HOH   F 6 .   ? 1.529   2.544  12.214 1.00 31.10 ? 367 HOH   A O     1 
HETATM 1509 O  O     . HOH   F 6 .   ? -6.743  5.118  10.137 1.00 39.19 ? 368 HOH   A O     1 
HETATM 1510 O  O     . HOH   F 6 .   ? -21.761 14.396 22.631 1.00 27.20 ? 369 HOH   A O     1 
HETATM 1511 O  O     . HOH   F 6 .   ? -15.098 15.971 -8.687 1.00 21.01 ? 370 HOH   A O     1 
HETATM 1512 O  O     . HOH   F 6 .   ? 14.852  24.718 2.028  1.00 35.90 ? 371 HOH   A O     1 
HETATM 1513 O  O     . HOH   F 6 .   ? 14.344  5.069  13.123 1.00 23.75 ? 372 HOH   A O     1 
HETATM 1514 O  O     . HOH   F 6 .   ? 1.992   1.914  21.962 1.00 42.55 ? 373 HOH   A O     1 
HETATM 1515 O  O     . HOH   F 6 .   ? -21.362 11.681 4.819  1.00 25.97 ? 374 HOH   A O     1 
HETATM 1516 O  O     . HOH   F 6 .   ? 10.300  7.450  23.256 1.00 41.25 ? 375 HOH   A O     1 
HETATM 1517 O  O     . HOH   F 6 .   ? -4.636  29.171 22.642 1.00 34.09 ? 376 HOH   A O     1 
HETATM 1518 O  O     . HOH   F 6 .   ? -3.772  23.498 -5.731 1.00 43.79 ? 377 HOH   A O     1 
HETATM 1519 O  O     . HOH   F 6 .   ? 5.309   12.149 -1.340 1.00 29.17 ? 378 HOH   A O     1 
HETATM 1520 O  O     . HOH   F 6 .   ? 0.740   4.938  8.381  1.00 17.23 ? 379 HOH   A O     1 
HETATM 1521 O  O     . HOH   F 6 .   ? 8.778   23.186 23.069 1.00 37.44 ? 380 HOH   A O     1 
HETATM 1522 O  O     . HOH   F 6 .   ? -15.708 21.720 6.375  1.00 27.78 ? 381 HOH   A O     1 
HETATM 1523 O  O     . HOH   F 6 .   ? -18.189 20.955 2.270  1.00 27.11 ? 382 HOH   A O     1 
HETATM 1524 O  O     . HOH   F 6 .   ? 15.289  22.603 13.714 1.00 26.87 ? 383 HOH   A O     1 
HETATM 1525 O  O     . HOH   F 6 .   ? 3.566   29.992 21.210 1.00 38.87 ? 384 HOH   A O     1 
HETATM 1526 O  O     . HOH   F 6 .   ? 4.775   23.724 23.563 1.00 29.80 ? 385 HOH   A O     1 
HETATM 1527 O  O     . HOH   F 6 .   ? 9.850   8.949  14.431 1.00 20.56 ? 386 HOH   A O     1 
HETATM 1528 O  O     . HOH   F 6 .   ? 12.831  6.104  20.275 1.00 34.60 ? 387 HOH   A O     1 
HETATM 1529 O  O     . HOH   F 6 .   ? -6.073  27.172 -4.703 1.00 37.99 ? 388 HOH   A O     1 
HETATM 1530 O  O     . HOH   F 6 .   ? 15.878  25.386 14.086 1.00 31.07 ? 389 HOH   A O     1 
HETATM 1531 O  O     . HOH   F 6 .   ? 17.513  10.673 10.988 1.00 17.37 ? 390 HOH   A O     1 
HETATM 1532 O  O     . HOH   F 6 .   ? 13.548  23.694 17.167 1.00 33.91 ? 391 HOH   A O     1 
HETATM 1533 O  O     . HOH   F 6 .   ? 16.769  21.036 15.608 1.00 28.86 ? 392 HOH   A O     1 
HETATM 1534 O  O     . HOH   F 6 .   ? 11.592  13.473 -3.195 1.00 36.09 ? 393 HOH   A O     1 
HETATM 1535 O  O     . HOH   F 6 .   ? -1.406  35.514 15.901 1.00 32.27 ? 394 HOH   A O     1 
HETATM 1536 O  O     . HOH   F 6 .   ? -1.746  31.324 20.951 1.00 38.47 ? 395 HOH   A O     1 
HETATM 1537 O  O     . HOH   F 6 .   ? 1.519   6.424  4.026  1.00 33.94 ? 396 HOH   A O     1 
HETATM 1538 O  O     . HOH   F 6 .   ? 13.446  15.880 24.387 1.00 23.92 ? 397 HOH   A O     1 
HETATM 1539 O  O     . HOH   F 6 .   ? -16.940 7.418  19.933 1.00 40.65 ? 398 HOH   A O     1 
HETATM 1540 O  O     . HOH   F 6 .   ? 0.252   -1.048 18.561 1.00 38.90 ? 399 HOH   A O     1 
HETATM 1541 O  O     . HOH   F 6 .   ? 2.598   -2.790 21.169 1.00 52.99 ? 400 HOH   A O     1 
HETATM 1542 O  O     . HOH   F 6 .   ? -4.140  20.200 -6.820 1.00 31.52 ? 401 HOH   A O     1 
HETATM 1543 O  O     . HOH   F 6 .   ? -17.046 11.887 2.497  1.00 32.37 ? 402 HOH   A O     1 
HETATM 1544 O  O     . HOH   F 6 .   ? 4.111   14.866 -0.564 1.00 17.33 ? 403 HOH   A O     1 
HETATM 1545 O  O     . HOH   F 6 .   ? 11.710  12.711 27.182 1.00 38.49 ? 404 HOH   A O     1 
HETATM 1546 O  O     . HOH   F 6 .   ? 7.883   11.228 -0.991 1.00 17.53 ? 405 HOH   A O     1 
HETATM 1547 O  O     . HOH   F 6 .   ? 1.373   8.774  0.520  1.00 28.82 ? 406 HOH   A O     1 
HETATM 1548 O  O     . HOH   F 6 .   ? 7.817   35.893 11.908 1.00 40.55 ? 407 HOH   A O     1 
HETATM 1549 O  O     . HOH   F 6 .   ? -1.246  8.101  -2.576 1.00 25.90 ? 408 HOH   A O     1 
HETATM 1550 O  O     . HOH   F 6 .   ? -18.002 19.397 4.339  1.00 40.41 ? 409 HOH   A O     1 
HETATM 1551 O  O     . HOH   F 6 .   ? 20.752  16.807 13.678 1.00 14.82 ? 410 HOH   A O     1 
HETATM 1552 O  O     . HOH   F 6 .   ? 16.421  4.752  15.156 1.00 44.67 ? 411 HOH   A O     1 
HETATM 1553 O  O     . HOH   F 6 .   ? 3.092   2.074  10.269 1.00 40.84 ? 412 HOH   A O     1 
HETATM 1554 O  O     . HOH   F 6 .   ? -2.835  28.350 30.706 1.00 36.87 ? 413 HOH   A O     1 
HETATM 1555 O  O     . HOH   F 6 .   ? 1.683   31.710 22.456 1.00 41.01 ? 414 HOH   A O     1 
HETATM 1556 O  O     . HOH   F 6 .   ? 12.891  8.461  26.363 1.00 39.35 ? 415 HOH   A O     1 
HETATM 1557 O  O     . HOH   F 6 .   ? 17.910  21.831 18.055 1.00 47.17 ? 416 HOH   A O     1 
HETATM 1558 O  O     . HOH   F 6 .   ? 12.637  26.245 17.649 1.00 42.01 ? 417 HOH   A O     1 
HETATM 1559 O  O     . HOH   F 6 .   ? -20.916 8.427  22.327 1.00 45.86 ? 418 HOH   A O     1 
HETATM 1560 O  O     . HOH   F 6 .   ? -18.861 22.623 10.446 1.00 40.45 ? 419 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   ? 0.5012 0.5677 0.5073 0.0603  -0.0667 -0.0019 1   MET   A N     
2    C  CA    . MET   A 4   ? 0.4518 0.5012 0.4541 0.0573  -0.0604 0.0013  1   MET   A CA    
3    C  C     . MET   A 4   ? 0.3729 0.4260 0.3879 0.0550  -0.0552 -0.0046 1   MET   A C     
4    O  O     . MET   A 4   ? 0.3434 0.4063 0.3690 0.0597  -0.0570 -0.0081 1   MET   A O     
5    C  CB    . MET   A 4   ? 0.4982 0.5338 0.4948 0.0646  -0.0632 0.0083  1   MET   A CB    
6    C  CG    . MET   A 4   ? 0.5488 0.5684 0.5433 0.0618  -0.0576 0.0101  1   MET   A CG    
7    S  SD    . MET   A 4   ? 0.5178 0.5216 0.4954 0.0580  -0.0572 0.0194  1   MET   A SD    
8    C  CE    . MET   A 4   ? 0.5343 0.5453 0.5040 0.0639  -0.0655 0.0248  1   MET   A CE    
9    N  N     . THR   A 5   ? 0.2977 0.3434 0.3111 0.0481  -0.0488 -0.0052 2   THR   A N     
10   C  CA    . THR   A 5   ? 0.2642 0.3147 0.2886 0.0457  -0.0437 -0.0101 2   THR   A CA    
11   C  C     . THR   A 5   ? 0.2484 0.2844 0.2685 0.0452  -0.0393 -0.0077 2   THR   A C     
12   O  O     . THR   A 5   ? 0.2791 0.3048 0.2897 0.0415  -0.0380 -0.0040 2   THR   A O     
13   C  CB    . THR   A 5   ? 0.2432 0.3006 0.2712 0.0374  -0.0407 -0.0139 2   THR   A CB    
14   O  OG1   . THR   A 5   ? 0.2481 0.3187 0.2799 0.0381  -0.0457 -0.0169 2   THR   A OG1   
15   C  CG2   . THR   A 5   ? 0.2479 0.3103 0.2861 0.0339  -0.0353 -0.0174 2   THR   A CG2   
16   N  N     A GLU   A 6   ? 0.2325 0.2684 0.2584 0.0479  -0.0370 -0.0099 3   GLU   A N     
17   N  N     B GLU   A 6   ? 0.2352 0.2710 0.2611 0.0480  -0.0371 -0.0098 3   GLU   A N     
18   C  CA    A GLU   A 6   ? 0.2414 0.2638 0.2629 0.0472  -0.0332 -0.0086 3   GLU   A CA    
19   C  CA    B GLU   A 6   ? 0.2451 0.2674 0.2664 0.0471  -0.0332 -0.0086 3   GLU   A CA    
20   C  C     A GLU   A 6   ? 0.2205 0.2458 0.2445 0.0401  -0.0268 -0.0112 3   GLU   A C     
21   C  C     B GLU   A 6   ? 0.2226 0.2478 0.2465 0.0401  -0.0269 -0.0111 3   GLU   A C     
22   O  O     A GLU   A 6   ? 0.2260 0.2643 0.2588 0.0382  -0.0249 -0.0147 3   GLU   A O     
23   O  O     B GLU   A 6   ? 0.2294 0.2677 0.2622 0.0383  -0.0250 -0.0147 3   GLU   A O     
24   C  CB    A GLU   A 6   ? 0.2592 0.2801 0.2856 0.0553  -0.0344 -0.0108 3   GLU   A CB    
25   C  CB    B GLU   A 6   ? 0.2663 0.2867 0.2924 0.0551  -0.0343 -0.0107 3   GLU   A CB    
26   C  CG    A GLU   A 6   ? 0.2758 0.2821 0.2974 0.0550  -0.0315 -0.0105 3   GLU   A CG    
27   C  CG    B GLU   A 6   ? 0.2952 0.3136 0.3204 0.0634  -0.0412 -0.0081 3   GLU   A CG    
28   C  CD    A GLU   A 6   ? 0.3106 0.3161 0.3378 0.0621  -0.0312 -0.0152 3   GLU   A CD    
29   C  CD    B GLU   A 6   ? 0.3336 0.3478 0.3636 0.0727  -0.0430 -0.0105 3   GLU   A CD    
30   O  OE1   A GLU   A 6   ? 0.3410 0.3314 0.3633 0.0636  -0.0313 -0.0147 3   GLU   A OE1   
31   O  OE1   B GLU   A 6   ? 0.3503 0.3708 0.3852 0.0808  -0.0482 -0.0108 3   GLU   A OE1   
32   O  OE2   A GLU   A 6   ? 0.3491 0.3697 0.3860 0.0659  -0.0307 -0.0199 3   GLU   A OE2   
33   O  OE2   B GLU   A 6   ? 0.3906 0.3954 0.4194 0.0722  -0.0395 -0.0124 3   GLU   A OE2   
34   N  N     . TYR   A 7   ? 0.1904 0.2039 0.2072 0.0364  -0.0240 -0.0090 4   TYR   A N     
35   C  CA    . TYR   A 7   ? 0.1830 0.1979 0.2008 0.0304  -0.0185 -0.0104 4   TYR   A CA    
36   C  C     . TYR   A 7   ? 0.1807 0.1853 0.1944 0.0314  -0.0165 -0.0106 4   TYR   A C     
37   O  O     . TYR   A 7   ? 0.1949 0.1879 0.2016 0.0308  -0.0178 -0.0075 4   TYR   A O     
38   C  CB    . TYR   A 7   ? 0.1711 0.1831 0.1838 0.0242  -0.0176 -0.0081 4   TYR   A CB    
39   C  CG    . TYR   A 7   ? 0.1699 0.1916 0.1867 0.0224  -0.0194 -0.0094 4   TYR   A CG    
40   C  CD1   . TYR   A 7   ? 0.1823 0.2051 0.1958 0.0246  -0.0241 -0.0083 4   TYR   A CD1   
41   C  CD2   . TYR   A 7   ? 0.1657 0.1956 0.1898 0.0182  -0.0167 -0.0120 4   TYR   A CD2   
42   C  CE1   . TYR   A 7   ? 0.1839 0.2166 0.2015 0.0228  -0.0261 -0.0109 4   TYR   A CE1   
43   C  CE2   . TYR   A 7   ? 0.1726 0.2108 0.2017 0.0159  -0.0186 -0.0142 4   TYR   A CE2   
44   C  CZ    . TYR   A 7   ? 0.1850 0.2252 0.2111 0.0183  -0.0235 -0.0143 4   TYR   A CZ    
45   O  OH    . TYR   A 7   ? 0.1808 0.2297 0.2117 0.0161  -0.0259 -0.0177 4   TYR   A OH    
46   N  N     . LYS   A 8   ? 0.1687 0.1791 0.1873 0.0326  -0.0134 -0.0143 5   LYS   A N     
47   C  CA    . LYS   A 8   ? 0.1860 0.1882 0.2010 0.0337  -0.0117 -0.0160 5   LYS   A CA    
48   C  C     . LYS   A 8   ? 0.1781 0.1802 0.1897 0.0271  -0.0077 -0.0152 5   LYS   A C     
49   O  O     . LYS   A 8   ? 0.1687 0.1811 0.1842 0.0247  -0.0044 -0.0162 5   LYS   A O     
50   C  CB    . LYS   A 8   ? 0.2076 0.2174 0.2287 0.0395  -0.0106 -0.0214 5   LYS   A CB    
51   C  CG    . LYS   A 8   ? 0.2465 0.2561 0.2717 0.0475  -0.0151 -0.0227 5   LYS   A CG    
52   C  CD    . LYS   A 8   ? 0.2960 0.3185 0.3297 0.0534  -0.0134 -0.0288 5   LYS   A CD    
53   C  CE    . LYS   A 8   ? 0.3555 0.3816 0.3953 0.0616  -0.0182 -0.0299 5   LYS   A CE    
54   N  NZ    . LYS   A 8   ? 0.4015 0.4100 0.4368 0.0677  -0.0226 -0.0295 5   LYS   A NZ    
55   N  N     . LEU   A 9   ? 0.1738 0.1647 0.1786 0.0243  -0.0081 -0.0131 6   LEU   A N     
56   C  CA    . LEU   A 9   ? 0.1796 0.1703 0.1813 0.0186  -0.0053 -0.0119 6   LEU   A CA    
57   C  C     . LEU   A 9   ? 0.1772 0.1622 0.1756 0.0189  -0.0045 -0.0147 6   LEU   A C     
58   O  O     . LEU   A 9   ? 0.2092 0.1845 0.2057 0.0215  -0.0069 -0.0157 6   LEU   A O     
59   C  CB    . LEU   A 9   ? 0.1740 0.1590 0.1713 0.0146  -0.0065 -0.0079 6   LEU   A CB    
60   C  CG    . LEU   A 9   ? 0.1910 0.1797 0.1897 0.0148  -0.0084 -0.0059 6   LEU   A CG    
61   C  CD1   . LEU   A 9   ? 0.1988 0.1839 0.1926 0.0109  -0.0087 -0.0028 6   LEU   A CD1   
62   C  CD2   . LEU   A 9   ? 0.1881 0.1880 0.1935 0.0142  -0.0069 -0.0075 6   LEU   A CD2   
63   N  N     . VAL   A 10  ? 0.1683 0.1591 0.1660 0.0163  -0.0015 -0.0158 7   VAL   A N     
64   C  CA    . VAL   A 10  ? 0.1792 0.1669 0.1735 0.0162  -0.0009 -0.0193 7   VAL   A CA    
65   C  C     . VAL   A 10  ? 0.1740 0.1618 0.1647 0.0108  0.0002  -0.0169 7   VAL   A C     
66   O  O     . VAL   A 10  ? 0.1828 0.1778 0.1745 0.0087  0.0021  -0.0141 7   VAL   A O     
67   C  CB    . VAL   A 10  ? 0.1765 0.1746 0.1726 0.0192  0.0017  -0.0236 7   VAL   A CB    
68   C  CG1   . VAL   A 10  ? 0.2040 0.1999 0.1959 0.0194  0.0019  -0.0284 7   VAL   A CG1   
69   C  CG2   . VAL   A 10  ? 0.1852 0.1858 0.1864 0.0251  0.0009  -0.0265 7   VAL   A CG2   
70   N  N     . VAL   A 11  ? 0.1682 0.1477 0.1556 0.0087  -0.0014 -0.0178 8   VAL   A N     
71   C  CA    . VAL   A 11  ? 0.1773 0.1579 0.1623 0.0041  -0.0009 -0.0161 8   VAL   A CA    
72   C  C     . VAL   A 11  ? 0.1838 0.1683 0.1665 0.0042  -0.0004 -0.0206 8   VAL   A C     
73   O  O     . VAL   A 11  ? 0.1993 0.1782 0.1811 0.0054  -0.0018 -0.0255 8   VAL   A O     
74   C  CB    . VAL   A 11  ? 0.1883 0.1596 0.1719 0.0007  -0.0028 -0.0143 8   VAL   A CB    
75   C  CG1   . VAL   A 11  ? 0.1848 0.1601 0.1675 -0.0038 -0.0021 -0.0128 8   VAL   A CG1   
76   C  CG2   . VAL   A 11  ? 0.1938 0.1614 0.1780 0.0014  -0.0036 -0.0102 8   VAL   A CG2   
77   N  N     . VAL   A 12  ? 0.1815 0.1754 0.1633 0.0033  0.0014  -0.0191 9   VAL   A N     
78   C  CA    . VAL   A 12  ? 0.1967 0.1970 0.1750 0.0036  0.0018  -0.0227 9   VAL   A CA    
79   C  C     . VAL   A 12  ? 0.1855 0.1893 0.1622 0.0002  0.0012  -0.0200 9   VAL   A C     
80   O  O     . VAL   A 12  ? 0.1851 0.1876 0.1638 -0.0015 0.0012  -0.0156 9   VAL   A O     
81   C  CB    . VAL   A 12  ? 0.2004 0.2111 0.1783 0.0065  0.0047  -0.0227 9   VAL   A CB    
82   C  CG1   . VAL   A 12  ? 0.2021 0.2117 0.1830 0.0104  0.0053  -0.0258 9   VAL   A CG1   
83   C  CG2   . VAL   A 12  ? 0.1982 0.2142 0.1776 0.0049  0.0066  -0.0157 9   VAL   A CG2   
84   N  N     . GLY   A 13  ? 0.1886 0.1971 0.1618 -0.0001 0.0002  -0.0238 10  GLY   A N     
85   C  CA    . GLY   A 13  ? 0.1854 0.1994 0.1572 -0.0024 -0.0010 -0.0218 10  GLY   A CA    
86   C  C     . GLY   A 13  ? 0.2057 0.2218 0.1748 -0.0036 -0.0034 -0.0284 10  GLY   A C     
87   O  O     . GLY   A 13  ? 0.2082 0.2178 0.1775 -0.0036 -0.0043 -0.0339 10  GLY   A O     
88   N  N     . ALA   A 14  ? 0.1974 0.2214 0.1649 -0.0049 -0.0050 -0.0276 11  ALA   A N     
89   C  CA    . ALA   A 14  ? 0.2160 0.2437 0.1812 -0.0064 -0.0079 -0.0347 11  ALA   A CA    
90   C  C     . ALA   A 14  ? 0.2191 0.2372 0.1887 -0.0109 -0.0099 -0.0389 11  ALA   A C     
91   O  O     . ALA   A 14  ? 0.2201 0.2318 0.1940 -0.0132 -0.0093 -0.0349 11  ALA   A O     
92   C  CB    . ALA   A 14  ? 0.2151 0.2544 0.1784 -0.0066 -0.0097 -0.0322 11  ALA   A CB    
93   N  N     . GLY   A 15  ? 0.2316 0.2489 0.2000 -0.0123 -0.0123 -0.0472 12  GLY   A N     
94   C  CA    . GLY   A 15  ? 0.2475 0.2554 0.2205 -0.0177 -0.0144 -0.0508 12  GLY   A CA    
95   C  C     . GLY   A 15  ? 0.2372 0.2497 0.2148 -0.0225 -0.0152 -0.0465 12  GLY   A C     
96   O  O     . GLY   A 15  ? 0.2390 0.2644 0.2161 -0.0221 -0.0163 -0.0452 12  GLY   A O     
97   N  N     . GLY   A 16  ? 0.2286 0.2314 0.2108 -0.0267 -0.0145 -0.0438 13  GLY   A N     
98   C  CA    . GLY   A 16  ? 0.2296 0.2375 0.2168 -0.0317 -0.0146 -0.0405 13  GLY   A CA    
99   C  C     . GLY   A 16  ? 0.2316 0.2439 0.2199 -0.0296 -0.0120 -0.0326 13  GLY   A C     
100  O  O     . GLY   A 16  ? 0.2230 0.2413 0.2159 -0.0330 -0.0117 -0.0303 13  GLY   A O     
101  N  N     . VAL   A 17  ? 0.1991 0.2098 0.1840 -0.0240 -0.0101 -0.0290 14  VAL   A N     
102  C  CA    . VAL   A 17  ? 0.1831 0.1980 0.1695 -0.0220 -0.0082 -0.0227 14  VAL   A CA    
103  C  C     . VAL   A 17  ? 0.1856 0.1930 0.1743 -0.0244 -0.0062 -0.0191 14  VAL   A C     
104  O  O     . VAL   A 17  ? 0.1754 0.1873 0.1663 -0.0239 -0.0049 -0.0154 14  VAL   A O     
105  C  CB    . VAL   A 17  ? 0.1807 0.1969 0.1637 -0.0161 -0.0068 -0.0197 14  VAL   A CB    
106  C  CG1   . VAL   A 17  ? 0.1711 0.1968 0.1507 -0.0135 -0.0083 -0.0212 14  VAL   A CG1   
107  C  CG2   . VAL   A 17  ? 0.1891 0.1958 0.1701 -0.0143 -0.0054 -0.0200 14  VAL   A CG2   
108  N  N     . GLY   A 18  ? 0.2015 0.1974 0.1891 -0.0263 -0.0062 -0.0201 15  GLY   A N     
109  C  CA    . GLY   A 18  ? 0.2051 0.1934 0.1933 -0.0284 -0.0047 -0.0159 15  GLY   A CA    
110  C  C     . GLY   A 18  ? 0.2086 0.1877 0.1939 -0.0244 -0.0042 -0.0139 15  GLY   A C     
111  O  O     . GLY   A 18  ? 0.2028 0.1786 0.1877 -0.0249 -0.0030 -0.0096 15  GLY   A O     
112  N  N     . LYS   A 19  ? 0.2135 0.1893 0.1970 -0.0206 -0.0051 -0.0173 16  LYS   A N     
113  C  CA    . LYS   A 19  ? 0.2135 0.1820 0.1956 -0.0163 -0.0048 -0.0163 16  LYS   A CA    
114  C  C     . LYS   A 19  ? 0.2362 0.1923 0.2180 -0.0186 -0.0058 -0.0139 16  LYS   A C     
115  O  O     . LYS   A 19  ? 0.2354 0.1883 0.2162 -0.0168 -0.0053 -0.0096 16  LYS   A O     
116  C  CB    . LYS   A 19  ? 0.2260 0.1942 0.2068 -0.0122 -0.0055 -0.0217 16  LYS   A CB    
117  C  CG    . LYS   A 19  ? 0.2192 0.1995 0.1988 -0.0097 -0.0044 -0.0230 16  LYS   A CG    
118  C  CD    . LYS   A 19  ? 0.2417 0.2231 0.2194 -0.0057 -0.0046 -0.0286 16  LYS   A CD    
119  C  CE    . LYS   A 19  ? 0.2512 0.2297 0.2278 -0.0074 -0.0068 -0.0358 16  LYS   A CE    
120  N  NZ    . LYS   A 19  ? 0.2463 0.2331 0.2221 -0.0110 -0.0080 -0.0374 16  LYS   A NZ    
121  N  N     . SER   A 20  ? 0.2294 0.1783 0.2120 -0.0228 -0.0073 -0.0166 17  SER   A N     
122  C  CA    . SER   A 20  ? 0.2304 0.1653 0.2125 -0.0253 -0.0084 -0.0135 17  SER   A CA    
123  C  C     . SER   A 20  ? 0.2352 0.1725 0.2170 -0.0302 -0.0067 -0.0067 17  SER   A C     
124  O  O     . SER   A 20  ? 0.2474 0.1778 0.2267 -0.0296 -0.0067 -0.0013 17  SER   A O     
125  C  CB    . SER   A 20  ? 0.2476 0.1731 0.2316 -0.0295 -0.0106 -0.0184 17  SER   A CB    
126  O  OG    . SER   A 20  ? 0.2557 0.1788 0.2395 -0.0241 -0.0122 -0.0257 17  SER   A OG    
127  N  N     . ALA   A 21  ? 0.2172 0.1654 0.2012 -0.0346 -0.0053 -0.0071 18  ALA   A N     
128  C  CA    . ALA   A 21  ? 0.2365 0.1895 0.2205 -0.0392 -0.0031 -0.0016 18  ALA   A CA    
129  C  C     . ALA   A 21  ? 0.2247 0.1821 0.2058 -0.0344 -0.0017 0.0023  18  ALA   A C     
130  O  O     . ALA   A 21  ? 0.2313 0.1869 0.2097 -0.0364 -0.0006 0.0077  18  ALA   A O     
131  C  CB    . ALA   A 21  ? 0.2279 0.1940 0.2160 -0.0435 -0.0020 -0.0037 18  ALA   A CB    
132  N  N     . LEU   A 22  ? 0.2233 0.1869 0.2047 -0.0286 -0.0017 -0.0003 19  LEU   A N     
133  C  CA    . LEU   A 22  ? 0.2196 0.1861 0.1990 -0.0243 -0.0010 0.0024  19  LEU   A CA    
134  C  C     . LEU   A 22  ? 0.2298 0.1863 0.2060 -0.0216 -0.0025 0.0052  19  LEU   A C     
135  O  O     . LEU   A 22  ? 0.2443 0.2016 0.2177 -0.0210 -0.0022 0.0091  19  LEU   A O     
136  C  CB    . LEU   A 22  ? 0.2174 0.1909 0.1987 -0.0195 -0.0008 -0.0006 19  LEU   A CB    
137  C  CG    . LEU   A 22  ? 0.2105 0.1949 0.1947 -0.0206 0.0004  -0.0018 19  LEU   A CG    
138  C  CD1   . LEU   A 22  ? 0.2056 0.1940 0.1910 -0.0164 0.0001  -0.0039 19  LEU   A CD1   
139  C  CD2   . LEU   A 22  ? 0.2269 0.2173 0.2114 -0.0211 0.0020  0.0004  19  LEU   A CD2   
140  N  N     . THR   A 23  ? 0.2379 0.1864 0.2146 -0.0190 -0.0044 0.0026  20  THR   A N     
141  C  CA    . THR   A 23  ? 0.2379 0.1770 0.2126 -0.0150 -0.0064 0.0046  20  THR   A CA    
142  C  C     . THR   A 23  ? 0.2574 0.1870 0.2287 -0.0188 -0.0072 0.0107  20  THR   A C     
143  O  O     . THR   A 23  ? 0.2359 0.1635 0.2038 -0.0165 -0.0081 0.0153  20  THR   A O     
144  C  CB    . THR   A 23  ? 0.2368 0.1695 0.2135 -0.0109 -0.0083 -0.0004 20  THR   A CB    
145  O  OG1   . THR   A 23  ? 0.2257 0.1687 0.2047 -0.0078 -0.0071 -0.0050 20  THR   A OG1   
146  C  CG2   . THR   A 23  ? 0.2448 0.1692 0.2204 -0.0054 -0.0107 0.0015  20  THR   A CG2   
147  N  N     . ILE   A 24  ? 0.2695 0.1942 0.2416 -0.0251 -0.0067 0.0109  21  ILE   A N     
148  C  CA    . ILE   A 24  ? 0.2849 0.1997 0.2538 -0.0302 -0.0070 0.0177  21  ILE   A CA    
149  C  C     . ILE   A 24  ? 0.2889 0.2135 0.2543 -0.0333 -0.0043 0.0233  21  ILE   A C     
150  O  O     . ILE   A 24  ? 0.3080 0.2272 0.2682 -0.0340 -0.0047 0.0303  21  ILE   A O     
151  C  CB    . ILE   A 24  ? 0.3054 0.2131 0.2777 -0.0373 -0.0071 0.0158  21  ILE   A CB    
152  C  CG1   . ILE   A 24  ? 0.3238 0.2196 0.2984 -0.0331 -0.0103 0.0098  21  ILE   A CG1   
153  C  CG2   . ILE   A 24  ? 0.3323 0.2321 0.3021 -0.0447 -0.0063 0.0238  21  ILE   A CG2   
154  C  CD1   . ILE   A 24  ? 0.3651 0.2582 0.3441 -0.0388 -0.0108 0.0039  21  ILE   A CD1   
155  N  N     . GLN   A 25  ? 0.2647 0.2040 0.2325 -0.0345 -0.0017 0.0202  22  GLN   A N     
156  C  CA    . GLN   A 25  ? 0.2658 0.2160 0.2307 -0.0360 0.0009  0.0237  22  GLN   A CA    
157  C  C     . GLN   A 25  ? 0.2865 0.2371 0.2466 -0.0302 -0.0005 0.0260  22  GLN   A C     
158  O  O     . GLN   A 25  ? 0.2868 0.2383 0.2411 -0.0317 0.0002  0.0317  22  GLN   A O     
159  C  CB    . GLN   A 25  ? 0.2739 0.2392 0.2432 -0.0361 0.0032  0.0187  22  GLN   A CB    
160  C  CG    . GLN   A 25  ? 0.2916 0.2636 0.2638 -0.0433 0.0057  0.0191  22  GLN   A CG    
161  C  CD    . GLN   A 25  ? 0.3123 0.2899 0.2805 -0.0480 0.0087  0.0249  22  GLN   A CD    
162  O  OE1   . GLN   A 25  ? 0.3163 0.2886 0.2778 -0.0471 0.0083  0.0305  22  GLN   A OE1   
163  N  NE2   . GLN   A 25  ? 0.3011 0.2906 0.2734 -0.0530 0.0117  0.0239  22  GLN   A NE2   
164  N  N     . LEU   A 26  ? 0.2715 0.2227 0.2340 -0.0239 -0.0023 0.0216  23  LEU   A N     
165  C  CA    . LEU   A 26  ? 0.2778 0.2310 0.2371 -0.0186 -0.0040 0.0228  23  LEU   A CA    
166  C  C     . LEU   A 26  ? 0.3240 0.2659 0.2781 -0.0173 -0.0068 0.0290  23  LEU   A C     
167  O  O     . LEU   A 26  ? 0.3214 0.2665 0.2698 -0.0165 -0.0073 0.0333  23  LEU   A O     
168  C  CB    . LEU   A 26  ? 0.2841 0.2392 0.2484 -0.0130 -0.0054 0.0172  23  LEU   A CB    
169  C  CG    . LEU   A 26  ? 0.3103 0.2689 0.2735 -0.0078 -0.0075 0.0173  23  LEU   A CG    
170  C  CD1   . LEU   A 26  ? 0.2968 0.2669 0.2596 -0.0085 -0.0059 0.0156  23  LEU   A CD1   
171  C  CD2   . LEU   A 26  ? 0.3095 0.2678 0.2779 -0.0030 -0.0090 0.0130  23  LEU   A CD2   
172  N  N     . ILE   A 27  ? 0.3119 0.2415 0.2681 -0.0161 -0.0089 0.0286  24  ILE   A N     
173  C  CA    . ILE   A 27  ? 0.3583 0.2745 0.3108 -0.0133 -0.0124 0.0342  24  ILE   A CA    
174  C  C     . ILE   A 27  ? 0.3689 0.2773 0.3155 -0.0195 -0.0118 0.0428  24  ILE   A C     
175  O  O     . ILE   A 27  ? 0.4017 0.3063 0.3422 -0.0172 -0.0140 0.0495  24  ILE   A O     
176  C  CB    . ILE   A 27  ? 0.3508 0.2555 0.3082 -0.0100 -0.0148 0.0298  24  ILE   A CB    
177  C  CG1   . ILE   A 27  ? 0.3392 0.2523 0.3018 -0.0037 -0.0152 0.0224  24  ILE   A CG1   
178  C  CG2   . ILE   A 27  ? 0.4180 0.3067 0.3724 -0.0068 -0.0187 0.0355  24  ILE   A CG2   
179  C  CD1   . ILE   A 27  ? 0.3590 0.2779 0.3207 0.0027  -0.0175 0.0235  24  ILE   A CD1   
180  N  N     . GLN   A 28  ? 0.3505 0.2571 0.2993 -0.0270 -0.0091 0.0427  25  GLN   A N     
181  C  CA    . GLN   A 28  ? 0.3834 0.2804 0.3281 -0.0343 -0.0083 0.0512  25  GLN   A CA    
182  C  C     . GLN   A 28  ? 0.3814 0.2921 0.3242 -0.0420 -0.0034 0.0537  25  GLN   A C     
183  O  O     . GLN   A 28  ? 0.3893 0.2944 0.3295 -0.0490 -0.0020 0.0608  25  GLN   A O     
184  C  CB    . GLN   A 28  ? 0.3928 0.2739 0.3426 -0.0376 -0.0097 0.0493  25  GLN   A CB    
185  C  CG    . GLN   A 28  ? 0.4362 0.3014 0.3868 -0.0300 -0.0147 0.0483  25  GLN   A CG    
186  C  CD    . GLN   A 28  ? 0.4987 0.3498 0.4554 -0.0319 -0.0163 0.0429  25  GLN   A CD    
187  O  OE1   . GLN   A 28  ? 0.4820 0.3308 0.4415 -0.0405 -0.0145 0.0425  25  GLN   A OE1   
188  N  NE2   . GLN   A 28  ? 0.5444 0.3865 0.5037 -0.0236 -0.0200 0.0382  25  GLN   A NE2   
189  N  N     . ASN   A 29  ? 0.3823 0.3102 0.3274 -0.0406 -0.0009 0.0479  26  ASN   A N     
190  C  CA    . ASN   A 29  ? 0.3555 0.2984 0.2992 -0.0465 0.0038  0.0495  26  ASN   A CA    
191  C  C     . ASN   A 29  ? 0.3783 0.3208 0.3262 -0.0561 0.0067  0.0508  26  ASN   A C     
192  O  O     . ASN   A 29  ? 0.4187 0.3665 0.3631 -0.0625 0.0100  0.0571  26  ASN   A O     
193  C  CB    . ASN   A 29  ? 0.3825 0.3298 0.3164 -0.0460 0.0045  0.0569  26  ASN   A CB    
194  C  CG    . ASN   A 29  ? 0.3919 0.3576 0.3237 -0.0501 0.0094  0.0569  26  ASN   A CG    
195  O  OD1   . ASN   A 29  ? 0.4219 0.3992 0.3600 -0.0505 0.0117  0.0499  26  ASN   A OD1   
196  N  ND2   . ASN   A 29  ? 0.4489 0.4181 0.3714 -0.0523 0.0109  0.0648  26  ASN   A ND2   
197  N  N     . HIS   A 30  ? 0.3391 0.2764 0.2945 -0.0573 0.0054  0.0449  27  HIS   A N     
198  C  CA    . HIS   A 30  ? 0.3323 0.2724 0.2937 -0.0665 0.0078  0.0441  27  HIS   A CA    
199  C  C     . HIS   A 30  ? 0.3055 0.2498 0.2747 -0.0641 0.0064  0.0341  27  HIS   A C     
200  O  O     . HIS   A 30  ? 0.3018 0.2407 0.2712 -0.0569 0.0035  0.0298  27  HIS   A O     
201  C  CB    . HIS   A 30  ? 0.3252 0.2482 0.2859 -0.0740 0.0070  0.0509  27  HIS   A CB    
202  C  CG    . HIS   A 30  ? 0.3304 0.2336 0.2922 -0.0698 0.0021  0.0487  27  HIS   A CG    
203  N  ND1   . HIS   A 30  ? 0.3503 0.2453 0.3190 -0.0732 0.0003  0.0429  27  HIS   A ND1   
204  C  CD2   . HIS   A 30  ? 0.3750 0.2663 0.3322 -0.0618 -0.0015 0.0506  27  HIS   A CD2   
205  C  CE1   . HIS   A 30  ? 0.3969 0.2757 0.3650 -0.0671 -0.0039 0.0408  27  HIS   A CE1   
206  N  NE2   . HIS   A 30  ? 0.3854 0.2618 0.3470 -0.0600 -0.0051 0.0457  27  HIS   A NE2   
207  N  N     . PHE   A 31  ? 0.3204 0.2760 0.2958 -0.0701 0.0088  0.0312  28  PHE   A N     
208  C  CA    . PHE   A 31  ? 0.2992 0.2606 0.2817 -0.0692 0.0074  0.0227  28  PHE   A CA    
209  C  C     . PHE   A 31  ? 0.3228 0.2725 0.3098 -0.0751 0.0051  0.0204  28  PHE   A C     
210  O  O     . PHE   A 31  ? 0.3524 0.3001 0.3418 -0.0846 0.0066  0.0242  28  PHE   A O     
211  C  CB    . PHE   A 31  ? 0.2753 0.2575 0.2629 -0.0720 0.0107  0.0203  28  PHE   A CB    
212  C  CG    . PHE   A 31  ? 0.2833 0.2735 0.2778 -0.0706 0.0089  0.0122  28  PHE   A CG    
213  C  CD1   . PHE   A 31  ? 0.2600 0.2483 0.2535 -0.0622 0.0062  0.0075  28  PHE   A CD1   
214  C  CD2   . PHE   A 31  ? 0.2711 0.2718 0.2732 -0.0778 0.0097  0.0096  28  PHE   A CD2   
215  C  CE1   . PHE   A 31  ? 0.2666 0.2628 0.2651 -0.0607 0.0044  0.0011  28  PHE   A CE1   
216  C  CE2   . PHE   A 31  ? 0.2747 0.2838 0.2825 -0.0759 0.0074  0.0024  28  PHE   A CE2   
217  C  CZ    . PHE   A 31  ? 0.2437 0.2504 0.2490 -0.0671 0.0047  -0.0015 28  PHE   A CZ    
218  N  N     . VAL   A 32  ? 0.3231 0.2663 0.3115 -0.0701 0.0016  0.0138  29  VAL   A N     
219  C  CA    . VAL   A 32  ? 0.3419 0.2744 0.3348 -0.0750 -0.0011 0.0092  29  VAL   A CA    
220  C  C     . VAL   A 32  ? 0.3731 0.3205 0.3726 -0.0773 -0.0015 0.0014  29  VAL   A C     
221  O  O     . VAL   A 32  ? 0.3374 0.2946 0.3366 -0.0704 -0.0022 -0.0031 29  VAL   A O     
222  C  CB    . VAL   A 32  ? 0.3763 0.2916 0.3665 -0.0685 -0.0049 0.0060  29  VAL   A CB    
223  C  CG1   . VAL   A 32  ? 0.3936 0.2922 0.3788 -0.0680 -0.0054 0.0140  29  VAL   A CG1   
224  C  CG2   . VAL   A 32  ? 0.3888 0.3111 0.3770 -0.0582 -0.0058 0.0011  29  VAL   A CG2   
225  N  N     . ASP   A 33  ? 0.4350 0.3839 0.4406 -0.0873 -0.0013 0.0006  30  ASP   A N     
226  C  CA    . ASP   A 33  ? 0.4685 0.4311 0.4818 -0.0917 -0.0024 -0.0067 30  ASP   A CA    
227  C  C     . ASP   A 33  ? 0.4582 0.4145 0.4726 -0.0889 -0.0070 -0.0161 30  ASP   A C     
228  O  O     . ASP   A 33  ? 0.4985 0.4696 0.5159 -0.0871 -0.0084 -0.0223 30  ASP   A O     
229  C  CB    . ASP   A 33  ? 0.5529 0.5153 0.5727 -0.1047 -0.0011 -0.0043 30  ASP   A CB    
230  C  CG    . ASP   A 33  ? 0.6135 0.5959 0.6364 -0.1085 0.0036  0.0004  30  ASP   A CG    
231  O  OD1   . ASP   A 33  ? 0.6670 0.6611 0.6868 -0.1004 0.0051  0.0008  30  ASP   A OD1   
232  O  OD2   . ASP   A 33  ? 0.6676 0.6553 0.6971 -0.1193 0.0054  0.0020  30  ASP   A OD2   
233  N  N     . GLU   A 34  ? 0.5037 0.4395 0.5159 -0.0885 -0.0095 -0.0174 31  GLU   A N     
234  C  CA    . GLU   A 34  ? 0.5369 0.4684 0.5508 -0.0869 -0.0139 -0.0281 31  GLU   A CA    
235  C  C     . GLU   A 34  ? 0.5524 0.4635 0.5613 -0.0803 -0.0160 -0.0293 31  GLU   A C     
236  O  O     . GLU   A 34  ? 0.6058 0.4997 0.6169 -0.0839 -0.0187 -0.0328 31  GLU   A O     
237  C  CB    . GLU   A 34  ? 0.5793 0.5091 0.6012 -0.0984 -0.0157 -0.0325 31  GLU   A CB    
238  C  CG    . GLU   A 34  ? 0.6620 0.5864 0.6855 -0.0974 -0.0205 -0.0445 31  GLU   A CG    
239  C  CD    . GLU   A 34  ? 0.6777 0.5976 0.7098 -0.1095 -0.0230 -0.0498 31  GLU   A CD    
240  O  OE1   . GLU   A 34  ? 0.6835 0.6026 0.7206 -0.1195 -0.0205 -0.0427 31  GLU   A OE1   
241  O  OE2   . GLU   A 34  ? 0.6848 0.6029 0.7188 -0.1093 -0.0273 -0.0611 31  GLU   A OE2   
242  N  N     . TYR   A 35  ? 0.4532 0.3675 0.4565 -0.0705 -0.0150 -0.0277 32  TYR   A N     
243  C  CA    . TYR   A 35  ? 0.4361 0.3345 0.4353 -0.0631 -0.0166 -0.0282 32  TYR   A CA    
244  C  C     . TYR   A 35  ? 0.4162 0.3144 0.4152 -0.0577 -0.0195 -0.0396 32  TYR   A C     
245  O  O     . TYR   A 35  ? 0.4182 0.3323 0.4155 -0.0533 -0.0191 -0.0435 32  TYR   A O     
246  C  CB    . TYR   A 35  ? 0.4092 0.3125 0.4032 -0.0553 -0.0142 -0.0217 32  TYR   A CB    
247  C  CG    . TYR   A 35  ? 0.4071 0.2932 0.3980 -0.0500 -0.0155 -0.0185 32  TYR   A CG    
248  C  CD1   . TYR   A 35  ? 0.4410 0.3125 0.4314 -0.0548 -0.0156 -0.0108 32  TYR   A CD1   
249  C  CD2   . TYR   A 35  ? 0.3784 0.2638 0.3670 -0.0402 -0.0165 -0.0228 32  TYR   A CD2   
250  C  CE1   . TYR   A 35  ? 0.4626 0.3181 0.4502 -0.0491 -0.0175 -0.0073 32  TYR   A CE1   
251  C  CE2   . TYR   A 35  ? 0.4095 0.2806 0.3963 -0.0345 -0.0181 -0.0201 32  TYR   A CE2   
252  C  CZ    . TYR   A 35  ? 0.4563 0.3119 0.4425 -0.0387 -0.0189 -0.0123 32  TYR   A CZ    
253  O  OH    . TYR   A 35  ? 0.4712 0.3122 0.4555 -0.0326 -0.0211 -0.0090 32  TYR   A OH    
254  N  N     . ASP   A 36  ? 0.4451 0.3252 0.4453 -0.0578 -0.0226 -0.0446 33  ASP   A N     
255  C  CA    . ASP   A 36  ? 0.4356 0.3151 0.4356 -0.0529 -0.0254 -0.0568 33  ASP   A CA    
256  C  C     . ASP   A 36  ? 0.4353 0.3292 0.4302 -0.0428 -0.0238 -0.0583 33  ASP   A C     
257  O  O     . ASP   A 36  ? 0.4254 0.3159 0.4176 -0.0362 -0.0222 -0.0529 33  ASP   A O     
258  C  CB    . ASP   A 36  ? 0.4524 0.3082 0.4535 -0.0505 -0.0285 -0.0606 33  ASP   A CB    
259  C  CG    . ASP   A 36  ? 0.4771 0.3324 0.4785 -0.0460 -0.0316 -0.0752 33  ASP   A CG    
260  O  OD1   . ASP   A 36  ? 0.4874 0.3597 0.4851 -0.0398 -0.0306 -0.0803 33  ASP   A OD1   
261  O  OD2   . ASP   A 36  ? 0.5600 0.3976 0.5650 -0.0487 -0.0350 -0.0816 33  ASP   A OD2   
262  N  N     . PRO   A 37  ? 0.4084 0.3189 0.4022 -0.0418 -0.0241 -0.0652 34  PRO   A N     
263  C  CA    . PRO   A 37  ? 0.3810 0.3060 0.3699 -0.0335 -0.0221 -0.0653 34  PRO   A CA    
264  C  C     . PRO   A 37  ? 0.3829 0.3022 0.3690 -0.0244 -0.0223 -0.0706 34  PRO   A C     
265  O  O     . PRO   A 37  ? 0.3710 0.3015 0.3537 -0.0179 -0.0200 -0.0688 34  PRO   A O     
266  C  CB    . PRO   A 37  ? 0.3993 0.3415 0.3875 -0.0355 -0.0233 -0.0715 34  PRO   A CB    
267  C  CG    . PRO   A 37  ? 0.4210 0.3554 0.4135 -0.0425 -0.0269 -0.0794 34  PRO   A CG    
268  C  CD    . PRO   A 37  ? 0.4219 0.3391 0.4190 -0.0487 -0.0267 -0.0728 34  PRO   A CD    
269  N  N     . THR   A 38  ? 0.3928 0.2953 0.3811 -0.0237 -0.0251 -0.0769 35  THR   A N     
270  C  CA    . THR   A 38  ? 0.4117 0.3100 0.3983 -0.0142 -0.0254 -0.0834 35  THR   A CA    
271  C  C     . THR   A 38  ? 0.4194 0.3050 0.4071 -0.0091 -0.0248 -0.0764 35  THR   A C     
272  O  O     . THR   A 38  ? 0.4232 0.3070 0.4106 -0.0002 -0.0249 -0.0810 35  THR   A O     
273  C  CB    . THR   A 38  ? 0.4186 0.3069 0.4069 -0.0142 -0.0292 -0.0970 35  THR   A CB    
274  O  OG1   . THR   A 38  ? 0.4334 0.2980 0.4267 -0.0187 -0.0321 -0.0957 35  THR   A OG1   
275  C  CG2   . THR   A 38  ? 0.4273 0.3288 0.4147 -0.0201 -0.0305 -0.1037 35  THR   A CG2   
276  N  N     . ILE   A 39  ? 0.3784 0.2560 0.3674 -0.0142 -0.0244 -0.0657 36  ILE   A N     
277  C  CA    . ILE   A 39  ? 0.3895 0.2541 0.3789 -0.0096 -0.0248 -0.0589 36  ILE   A CA    
278  C  C     . ILE   A 39  ? 0.3402 0.2199 0.3273 -0.0034 -0.0217 -0.0540 36  ILE   A C     
279  O  O     . ILE   A 39  ? 0.3232 0.2168 0.3086 -0.0067 -0.0191 -0.0489 36  ILE   A O     
280  C  CB    . ILE   A 39  ? 0.4031 0.2549 0.3936 -0.0172 -0.0253 -0.0486 36  ILE   A CB    
281  C  CG1   . ILE   A 39  ? 0.4312 0.2678 0.4251 -0.0249 -0.0282 -0.0530 36  ILE   A CG1   
282  C  CG2   . ILE   A 39  ? 0.4277 0.2677 0.4173 -0.0113 -0.0262 -0.0411 36  ILE   A CG2   
283  C  CD1   . ILE   A 39  ? 0.4500 0.2742 0.4450 -0.0335 -0.0282 -0.0422 36  ILE   A CD1   
284  N  N     . GLU   A 40  ? 0.3426 0.2197 0.3303 0.0058  -0.0222 -0.0565 37  GLU   A N     
285  C  CA    . GLU   A 40  ? 0.3421 0.2327 0.3291 0.0118  -0.0197 -0.0527 37  GLU   A CA    
286  C  C     . GLU   A 40  ? 0.3562 0.2348 0.3449 0.0170  -0.0217 -0.0473 37  GLU   A C     
287  O  O     . GLU   A 40  ? 0.3799 0.2467 0.3711 0.0230  -0.0245 -0.0525 37  GLU   A O     
288  C  CB    . GLU   A 40  ? 0.3551 0.2580 0.3421 0.0186  -0.0183 -0.0622 37  GLU   A CB    
289  C  CG    . GLU   A 40  ? 0.3537 0.2735 0.3409 0.0237  -0.0150 -0.0596 37  GLU   A CG    
290  C  CD    . GLU   A 40  ? 0.3902 0.3257 0.3757 0.0269  -0.0125 -0.0680 37  GLU   A CD    
291  O  OE1   . GLU   A 40  ? 0.3270 0.2756 0.3093 0.0228  -0.0101 -0.0664 37  GLU   A OE1   
292  O  OE2   . GLU   A 40  ? 0.4635 0.3984 0.4508 0.0339  -0.0130 -0.0766 37  GLU   A OE2   
293  N  N     . ASP   A 41  ? 0.3536 0.2354 0.3410 0.0153  -0.0207 -0.0374 38  ASP   A N     
294  C  CA    . ASP   A 41  ? 0.3707 0.2437 0.3589 0.0208  -0.0231 -0.0318 38  ASP   A CA    
295  C  C     . ASP   A 41  ? 0.3284 0.2155 0.3159 0.0224  -0.0212 -0.0257 38  ASP   A C     
296  O  O     . ASP   A 41  ? 0.3078 0.2083 0.2938 0.0178  -0.0180 -0.0242 38  ASP   A O     
297  C  CB    . ASP   A 41  ? 0.4361 0.2902 0.4224 0.0158  -0.0257 -0.0243 38  ASP   A CB    
298  C  CG    . ASP   A 41  ? 0.5087 0.3446 0.4971 0.0231  -0.0302 -0.0243 38  ASP   A CG    
299  O  OD1   . ASP   A 41  ? 0.4863 0.3263 0.4769 0.0326  -0.0315 -0.0253 38  ASP   A OD1   
300  O  OD2   . ASP   A 41  ? 0.6079 0.4251 0.5964 0.0191  -0.0326 -0.0235 38  ASP   A OD2   
301  N  N     . SER   A 42  ? 0.3326 0.2165 0.3215 0.0292  -0.0235 -0.0228 39  SER   A N     
302  C  CA    . SER   A 42  ? 0.3083 0.2034 0.2967 0.0304  -0.0228 -0.0167 39  SER   A CA    
303  C  C     . SER   A 42  ? 0.3160 0.2005 0.3004 0.0284  -0.0254 -0.0069 39  SER   A C     
304  O  O     . SER   A 42  ? 0.3345 0.2015 0.3179 0.0297  -0.0288 -0.0042 39  SER   A O     
305  C  CB    . SER   A 42  ? 0.3134 0.2186 0.3069 0.0395  -0.0233 -0.0209 39  SER   A CB    
306  O  OG    . SER   A 42  ? 0.3769 0.2697 0.3728 0.0472  -0.0276 -0.0218 39  SER   A OG    
307  N  N     . TYR   A 43  ? 0.2860 0.1814 0.2679 0.0251  -0.0238 -0.0016 40  TYR   A N     
308  C  CA    . TYR   A 43  ? 0.3092 0.1992 0.2858 0.0225  -0.0254 0.0077  40  TYR   A CA    
309  C  C     . TYR   A 43  ? 0.2934 0.1961 0.2703 0.0267  -0.0263 0.0099  40  TYR   A C     
310  O  O     . TYR   A 43  ? 0.2782 0.1957 0.2577 0.0260  -0.0237 0.0065  40  TYR   A O     
311  C  CB    . TYR   A 43  ? 0.3195 0.2127 0.2923 0.0130  -0.0221 0.0110  40  TYR   A CB    
312  C  CG    . TYR   A 43  ? 0.3788 0.2624 0.3517 0.0067  -0.0210 0.0092  40  TYR   A CG    
313  C  CD1   . TYR   A 43  ? 0.3770 0.2666 0.3533 0.0053  -0.0189 0.0014  40  TYR   A CD1   
314  C  CD2   . TYR   A 43  ? 0.4560 0.3258 0.4253 0.0015  -0.0221 0.0158  40  TYR   A CD2   
315  C  CE1   . TYR   A 43  ? 0.4368 0.3193 0.4135 -0.0010 -0.0184 -0.0009 40  TYR   A CE1   
316  C  CE2   . TYR   A 43  ? 0.4811 0.3430 0.4517 -0.0054 -0.0212 0.0138  40  TYR   A CE2   
317  C  CZ    . TYR   A 43  ? 0.4835 0.3522 0.4580 -0.0065 -0.0196 0.0049  40  TYR   A CZ    
318  O  OH    . TYR   A 43  ? 0.5332 0.3953 0.5094 -0.0135 -0.0193 0.0022  40  TYR   A OH    
319  N  N     . ARG   A 44  ? 0.3078 0.2042 0.2821 0.0309  -0.0303 0.0157  41  ARG   A N     
320  C  CA    A ARG   A 44  ? 0.3101 0.2191 0.2840 0.0346  -0.0320 0.0181  41  ARG   A CA    
321  C  CA    B ARG   A 44  ? 0.3082 0.2171 0.2821 0.0346  -0.0320 0.0181  41  ARG   A CA    
322  C  C     . ARG   A 44  ? 0.3134 0.2212 0.2784 0.0304  -0.0329 0.0272  41  ARG   A C     
323  O  O     . ARG   A 44  ? 0.3821 0.2763 0.3408 0.0275  -0.0340 0.0345  41  ARG   A O     
324  C  CB    A ARG   A 44  ? 0.3324 0.2393 0.3105 0.0448  -0.0368 0.0170  41  ARG   A CB    
325  C  CB    B ARG   A 44  ? 0.3277 0.2347 0.3058 0.0448  -0.0368 0.0170  41  ARG   A CB    
326  C  CG    A ARG   A 44  ? 0.3399 0.2536 0.3271 0.0499  -0.0356 0.0075  41  ARG   A CG    
327  C  CG    B ARG   A 44  ? 0.3326 0.2468 0.3198 0.0498  -0.0355 0.0075  41  ARG   A CG    
328  C  CD    A ARG   A 44  ? 0.3616 0.2672 0.3533 0.0599  -0.0400 0.0052  41  ARG   A CD    
329  C  CD    B ARG   A 44  ? 0.3527 0.2581 0.3440 0.0597  -0.0401 0.0057  41  ARG   A CD    
330  N  NE    A ARG   A 44  ? 0.3639 0.2788 0.3594 0.0682  -0.0442 0.0061  41  ARG   A NE    
331  N  NE    B ARG   A 44  ? 0.3592 0.2435 0.3472 0.0581  -0.0411 0.0075  41  ARG   A NE    
332  C  CZ    A ARG   A 44  ? 0.3497 0.2839 0.3529 0.0715  -0.0432 0.0005  41  ARG   A CZ    
333  C  CZ    B ARG   A 44  ? 0.3746 0.2538 0.3640 0.0545  -0.0380 0.0014  41  ARG   A CZ    
334  N  NH1   A ARG   A 44  ? 0.3343 0.2803 0.3414 0.0670  -0.0377 -0.0056 41  ARG   A NH1   
335  N  NH1   B ARG   A 44  ? 0.3601 0.2542 0.3532 0.0525  -0.0336 -0.0058 41  ARG   A NH1   
336  N  NH2   A ARG   A 44  ? 0.3233 0.2655 0.3305 0.0790  -0.0478 0.0014  41  ARG   A NH2   
337  N  NH2   B ARG   A 44  ? 0.3926 0.2520 0.3797 0.0524  -0.0395 0.0029  41  ARG   A NH2   
338  N  N     . LYS   A 45  ? 0.2940 0.2171 0.2584 0.0285  -0.0314 0.0263  42  LYS   A N     
339  C  CA    . LYS   A 45  ? 0.3174 0.2438 0.2736 0.0248  -0.0315 0.0328  42  LYS   A CA    
340  C  C     . LYS   A 45  ? 0.2800 0.2227 0.2377 0.0274  -0.0328 0.0299  42  LYS   A C     
341  O  O     . LYS   A 45  ? 0.2680 0.2207 0.2327 0.0269  -0.0305 0.0230  42  LYS   A O     
342  C  CB    . LYS   A 45  ? 0.3380 0.2653 0.2916 0.0160  -0.0265 0.0329  42  LYS   A CB    
343  C  CG    . LYS   A 45  ? 0.4074 0.3365 0.3517 0.0112  -0.0256 0.0399  42  LYS   A CG    
344  C  CD    . LYS   A 45  ? 0.4321 0.3707 0.3769 0.0045  -0.0205 0.0366  42  LYS   A CD    
345  C  CE    . LYS   A 45  ? 0.4667 0.4098 0.4027 0.0000  -0.0189 0.0426  42  LYS   A CE    
346  N  NZ    . LYS   A 45  ? 0.4585 0.4099 0.3961 -0.0061 -0.0139 0.0391  42  LYS   A NZ    
347  N  N     . GLN   A 46  ? 0.2934 0.2390 0.2442 0.0293  -0.0362 0.0354  43  GLN   A N     
348  C  CA    . GLN   A 46  ? 0.2808 0.2424 0.2319 0.0310  -0.0380 0.0326  43  GLN   A CA    
349  C  C     . GLN   A 46  ? 0.2814 0.2501 0.2266 0.0241  -0.0343 0.0326  43  GLN   A C     
350  O  O     . GLN   A 46  ? 0.3054 0.2687 0.2418 0.0205  -0.0331 0.0390  43  GLN   A O     
351  C  CB    . GLN   A 46  ? 0.3355 0.2981 0.2807 0.0369  -0.0443 0.0383  43  GLN   A CB    
352  C  CG    . GLN   A 46  ? 0.3873 0.3529 0.3404 0.0457  -0.0494 0.0356  43  GLN   A CG    
353  C  CD    . GLN   A 46  ? 0.3859 0.3545 0.3322 0.0516  -0.0560 0.0417  43  GLN   A CD    
354  O  OE1   . GLN   A 46  ? 0.4922 0.4556 0.4408 0.0595  -0.0610 0.0443  43  GLN   A OE1   
355  N  NE2   . GLN   A 46  ? 0.3675 0.3452 0.3052 0.0483  -0.0563 0.0438  43  GLN   A NE2   
356  N  N     . VAL   A 47  ? 0.2444 0.2254 0.1950 0.0226  -0.0327 0.0254  44  VAL   A N     
357  C  CA    . VAL   A 47  ? 0.2492 0.2380 0.1960 0.0174  -0.0296 0.0233  44  VAL   A CA    
358  C  C     . VAL   A 47  ? 0.2521 0.2546 0.2025 0.0193  -0.0321 0.0171  44  VAL   A C     
359  O  O     . VAL   A 47  ? 0.2721 0.2783 0.2302 0.0231  -0.0349 0.0138  44  VAL   A O     
360  C  CB    . VAL   A 47  ? 0.2604 0.2477 0.2124 0.0124  -0.0242 0.0193  44  VAL   A CB    
361  C  CG1   . VAL   A 47  ? 0.3120 0.2872 0.2615 0.0095  -0.0217 0.0241  44  VAL   A CG1   
362  C  CG2   . VAL   A 47  ? 0.2713 0.2618 0.2343 0.0140  -0.0238 0.0130  44  VAL   A CG2   
363  N  N     . VAL   A 48  ? 0.2425 0.2532 0.1882 0.0165  -0.0311 0.0147  45  VAL   A N     
364  C  CA    . VAL   A 48  ? 0.2333 0.2564 0.1832 0.0174  -0.0335 0.0073  45  VAL   A CA    
365  C  C     . VAL   A 48  ? 0.2154 0.2406 0.1719 0.0131  -0.0292 0.0005  45  VAL   A C     
366  O  O     . VAL   A 48  ? 0.2225 0.2464 0.1748 0.0098  -0.0253 0.0008  45  VAL   A O     
367  C  CB    . VAL   A 48  ? 0.2448 0.2767 0.1843 0.0185  -0.0367 0.0082  45  VAL   A CB    
368  C  CG1   . VAL   A 48  ? 0.2459 0.2904 0.1907 0.0188  -0.0394 -0.0011 45  VAL   A CG1   
369  C  CG2   . VAL   A 48  ? 0.2737 0.3034 0.2067 0.0235  -0.0418 0.0157  45  VAL   A CG2   
370  N  N     . ILE   A 49  ? 0.1790 0.2076 0.1465 0.0132  -0.0299 -0.0052 46  ILE   A N     
371  C  CA    . ILE   A 49  ? 0.1758 0.2046 0.1507 0.0096  -0.0264 -0.0108 46  ILE   A CA    
372  C  C     . ILE   A 49  ? 0.1696 0.2075 0.1518 0.0095  -0.0296 -0.0180 46  ILE   A C     
373  O  O     . ILE   A 49  ? 0.1570 0.1987 0.1460 0.0112  -0.0323 -0.0189 46  ILE   A O     
374  C  CB    . ILE   A 49  ? 0.1840 0.2060 0.1662 0.0088  -0.0234 -0.0093 46  ILE   A CB    
375  C  CG1   . ILE   A 49  ? 0.1909 0.2039 0.1669 0.0088  -0.0212 -0.0030 46  ILE   A CG1   
376  C  CG2   . ILE   A 49  ? 0.1681 0.1899 0.1573 0.0053  -0.0202 -0.0138 46  ILE   A CG2   
377  C  CD1   . ILE   A 49  ? 0.1866 0.1940 0.1685 0.0092  -0.0193 -0.0021 46  ILE   A CD1   
378  N  N     . ASP   A 50  ? 0.1695 0.2115 0.1512 0.0074  -0.0293 -0.0239 47  ASP   A N     
379  C  CA    . ASP   A 50  ? 0.1702 0.2198 0.1594 0.0064  -0.0325 -0.0319 47  ASP   A CA    
380  C  C     . ASP   A 50  ? 0.1642 0.2233 0.1520 0.0094  -0.0384 -0.0326 47  ASP   A C     
381  O  O     . ASP   A 50  ? 0.1637 0.2290 0.1615 0.0088  -0.0412 -0.0371 47  ASP   A O     
382  C  CB    . ASP   A 50  ? 0.1698 0.2163 0.1726 0.0032  -0.0306 -0.0345 47  ASP   A CB    
383  C  CG    . ASP   A 50  ? 0.1681 0.2056 0.1722 0.0009  -0.0255 -0.0333 47  ASP   A CG    
384  O  OD1   . ASP   A 50  ? 0.1891 0.2260 0.1900 0.0002  -0.0246 -0.0371 47  ASP   A OD1   
385  O  OD2   . ASP   A 50  ? 0.1769 0.2090 0.1846 0.0003  -0.0226 -0.0289 47  ASP   A OD2   
386  N  N     . GLY   A 51  ? 0.1656 0.2265 0.1413 0.0126  -0.0402 -0.0279 48  GLY   A N     
387  C  CA    . GLY   A 51  ? 0.1819 0.2522 0.1537 0.0165  -0.0465 -0.0274 48  GLY   A CA    
388  C  C     . GLY   A 51  ? 0.1762 0.2446 0.1523 0.0203  -0.0487 -0.0218 48  GLY   A C     
389  O  O     . GLY   A 51  ? 0.2067 0.2824 0.1800 0.0245  -0.0541 -0.0205 48  GLY   A O     
390  N  N     . GLU   A 52  ? 0.1778 0.2374 0.1606 0.0193  -0.0446 -0.0191 49  GLU   A N     
391  C  CA    . GLU   A 52  ? 0.1789 0.2375 0.1668 0.0236  -0.0463 -0.0153 49  GLU   A CA    
392  C  C     . GLU   A 52  ? 0.1879 0.2347 0.1662 0.0263  -0.0451 -0.0064 49  GLU   A C     
393  O  O     . GLU   A 52  ? 0.1763 0.2143 0.1508 0.0230  -0.0403 -0.0042 49  GLU   A O     
394  C  CB    . GLU   A 52  ? 0.1733 0.2305 0.1743 0.0210  -0.0425 -0.0181 49  GLU   A CB    
395  C  CG    . GLU   A 52  ? 0.1842 0.2431 0.1921 0.0256  -0.0439 -0.0162 49  GLU   A CG    
396  C  CD    . GLU   A 52  ? 0.1959 0.2569 0.2163 0.0225  -0.0398 -0.0194 49  GLU   A CD    
397  O  OE1   . GLU   A 52  ? 0.2142 0.2674 0.2341 0.0187  -0.0347 -0.0186 49  GLU   A OE1   
398  O  OE2   . GLU   A 52  ? 0.2289 0.3004 0.2594 0.0240  -0.0418 -0.0225 49  GLU   A OE2   
399  N  N     . THR   A 53  ? 0.1984 0.2454 0.1735 0.0323  -0.0498 -0.0017 50  THR   A N     
400  C  CA    . THR   A 53  ? 0.2139 0.2472 0.1819 0.0348  -0.0489 0.0067  50  THR   A CA    
401  C  C     . THR   A 53  ? 0.2140 0.2418 0.1924 0.0356  -0.0460 0.0052  50  THR   A C     
402  O  O     . THR   A 53  ? 0.2192 0.2540 0.2066 0.0394  -0.0485 0.0021  50  THR   A O     
403  C  CB    . THR   A 53  ? 0.2328 0.2664 0.1936 0.0414  -0.0553 0.0130  50  THR   A CB    
404  O  OG1   . THR   A 53  ? 0.2331 0.2738 0.1833 0.0400  -0.0573 0.0138  50  THR   A OG1   
405  C  CG2   . THR   A 53  ? 0.2540 0.2711 0.2086 0.0434  -0.0544 0.0217  50  THR   A CG2   
406  N  N     . CYS   A 54  ? 0.2058 0.2230 0.1826 0.0318  -0.0407 0.0068  51  CYS   A N     
407  C  CA    . CYS   A 54  ? 0.2137 0.2269 0.1991 0.0316  -0.0372 0.0044  51  CYS   A CA    
408  C  C     . CYS   A 54  ? 0.2213 0.2202 0.2023 0.0341  -0.0369 0.0096  51  CYS   A C     
409  O  O     . CYS   A 54  ? 0.2410 0.2312 0.2130 0.0316  -0.0360 0.0147  51  CYS   A O     
410  C  CB    . CYS   A 54  ? 0.1853 0.1973 0.1726 0.0250  -0.0315 0.0015  51  CYS   A CB    
411  S  SG    . CYS   A 54  ? 0.2199 0.2443 0.2128 0.0208  -0.0311 -0.0050 51  CYS   A SG    
412  N  N     . LEU   A 55  ? 0.2248 0.2223 0.2129 0.0389  -0.0376 0.0078  52  LEU   A N     
413  C  CA    . LEU   A 55  ? 0.2540 0.2366 0.2393 0.0409  -0.0371 0.0110  52  LEU   A CA    
414  C  C     . LEU   A 55  ? 0.2283 0.2093 0.2179 0.0367  -0.0315 0.0068  52  LEU   A C     
415  O  O     . LEU   A 55  ? 0.2331 0.2226 0.2309 0.0380  -0.0300 0.0017  52  LEU   A O     
416  C  CB    . LEU   A 55  ? 0.2820 0.2633 0.2718 0.0499  -0.0417 0.0109  52  LEU   A CB    
417  C  CG    . LEU   A 55  ? 0.3189 0.2844 0.3081 0.0529  -0.0414 0.0120  52  LEU   A CG    
418  C  CD1   . LEU   A 55  ? 0.3310 0.2805 0.3094 0.0494  -0.0419 0.0198  52  LEU   A CD1   
419  C  CD2   . LEU   A 55  ? 0.3396 0.3055 0.3350 0.0630  -0.0462 0.0105  52  LEU   A CD2   
420  N  N     . LEU   A 56  ? 0.2258 0.1973 0.2092 0.0315  -0.0286 0.0093  53  LEU   A N     
421  C  CA    . LEU   A 56  ? 0.2170 0.1871 0.2035 0.0278  -0.0239 0.0057  53  LEU   A CA    
422  C  C     . LEU   A 56  ? 0.2345 0.1934 0.2217 0.0312  -0.0245 0.0050  53  LEU   A C     
423  O  O     . LEU   A 56  ? 0.2723 0.2191 0.2542 0.0320  -0.0268 0.0096  53  LEU   A O     
424  C  CB    . LEU   A 56  ? 0.2254 0.1924 0.2061 0.0207  -0.0209 0.0081  53  LEU   A CB    
425  C  CG    . LEU   A 56  ? 0.2455 0.2215 0.2243 0.0176  -0.0204 0.0083  53  LEU   A CG    
426  C  CD1   . LEU   A 56  ? 0.2649 0.2393 0.2402 0.0115  -0.0168 0.0091  53  LEU   A CD1   
427  C  CD2   . LEU   A 56  ? 0.2367 0.2245 0.2234 0.0185  -0.0202 0.0034  53  LEU   A CD2   
428  N  N     . ASP   A 57  ? 0.2090 0.1724 0.2024 0.0329  -0.0223 -0.0006 54  ASP   A N     
429  C  CA    . ASP   A 57  ? 0.2265 0.1801 0.2208 0.0362  -0.0226 -0.0033 54  ASP   A CA    
430  C  C     . ASP   A 57  ? 0.2161 0.1717 0.2103 0.0309  -0.0180 -0.0067 54  ASP   A C     
431  O  O     . ASP   A 57  ? 0.2177 0.1846 0.2164 0.0310  -0.0154 -0.0105 54  ASP   A O     
432  C  CB    . ASP   A 57  ? 0.2567 0.2162 0.2582 0.0444  -0.0244 -0.0078 54  ASP   A CB    
433  C  CG    . ASP   A 57  ? 0.2980 0.2469 0.3008 0.0492  -0.0253 -0.0118 54  ASP   A CG    
434  O  OD1   . ASP   A 57  ? 0.3451 0.2861 0.3447 0.0452  -0.0233 -0.0131 54  ASP   A OD1   
435  O  OD2   . ASP   A 57  ? 0.3845 0.3341 0.3919 0.0571  -0.0281 -0.0141 54  ASP   A OD2   
436  N  N     . ILE   A 58  ? 0.2170 0.1618 0.2061 0.0264  -0.0176 -0.0047 55  ILE   A N     
437  C  CA    . ILE   A 58  ? 0.2103 0.1582 0.1986 0.0208  -0.0139 -0.0071 55  ILE   A CA    
438  C  C     . ILE   A 58  ? 0.2247 0.1645 0.2131 0.0217  -0.0139 -0.0118 55  ILE   A C     
439  O  O     . ILE   A 58  ? 0.2411 0.1677 0.2272 0.0212  -0.0162 -0.0103 55  ILE   A O     
440  C  CB    . ILE   A 58  ? 0.2244 0.1694 0.2078 0.0142  -0.0132 -0.0021 55  ILE   A CB    
441  C  CG1   . ILE   A 58  ? 0.2324 0.1857 0.2154 0.0138  -0.0133 0.0012  55  ILE   A CG1   
442  C  CG2   . ILE   A 58  ? 0.2254 0.1734 0.2083 0.0091  -0.0102 -0.0042 55  ILE   A CG2   
443  C  CD1   . ILE   A 58  ? 0.2627 0.2143 0.2406 0.0085  -0.0126 0.0057  55  ILE   A CD1   
444  N  N     . LEU   A 59  ? 0.2059 0.1544 0.1966 0.0223  -0.0114 -0.0172 56  LEU   A N     
445  C  CA    . LEU   A 59  ? 0.2202 0.1630 0.2102 0.0225  -0.0113 -0.0231 56  LEU   A CA    
446  C  C     . LEU   A 59  ? 0.2213 0.1660 0.2082 0.0156  -0.0094 -0.0230 56  LEU   A C     
447  O  O     . LEU   A 59  ? 0.2022 0.1586 0.1892 0.0137  -0.0068 -0.0225 56  LEU   A O     
448  C  CB    . LEU   A 59  ? 0.2328 0.1854 0.2263 0.0281  -0.0098 -0.0299 56  LEU   A CB    
449  C  CG    . LEU   A 59  ? 0.2526 0.2017 0.2450 0.0292  -0.0097 -0.0376 56  LEU   A CG    
450  C  CD1   . LEU   A 59  ? 0.2770 0.2085 0.2699 0.0323  -0.0136 -0.0400 56  LEU   A CD1   
451  C  CD2   . LEU   A 59  ? 0.2624 0.2259 0.2575 0.0343  -0.0070 -0.0436 56  LEU   A CD2   
452  N  N     . ASP   A 60  ? 0.2306 0.1637 0.2154 0.0118  -0.0111 -0.0231 57  ASP   A N     
453  C  CA    . ASP   A 60  ? 0.2483 0.1835 0.2313 0.0054  -0.0100 -0.0240 57  ASP   A CA    
454  C  C     . ASP   A 60  ? 0.2609 0.1972 0.2440 0.0072  -0.0102 -0.0325 57  ASP   A C     
455  O  O     . ASP   A 60  ? 0.2923 0.2167 0.2760 0.0084  -0.0126 -0.0370 57  ASP   A O     
456  C  CB    . ASP   A 60  ? 0.2691 0.1926 0.2507 -0.0003 -0.0115 -0.0197 57  ASP   A CB    
457  C  CG    . ASP   A 60  ? 0.2793 0.2048 0.2606 -0.0070 -0.0110 -0.0217 57  ASP   A CG    
458  O  OD1   . ASP   A 60  ? 0.2692 0.2072 0.2504 -0.0076 -0.0093 -0.0238 57  ASP   A OD1   
459  O  OD2   . ASP   A 60  ? 0.3183 0.2330 0.2998 -0.0117 -0.0125 -0.0208 57  ASP   A OD2   
460  N  N     . THR   A 61  ? 0.2583 0.2086 0.2407 0.0078  -0.0078 -0.0349 58  THR   A N     
461  C  CA    . THR   A 61  ? 0.2652 0.2198 0.2465 0.0105  -0.0076 -0.0432 58  THR   A CA    
462  C  C     . THR   A 61  ? 0.2727 0.2251 0.2522 0.0052  -0.0091 -0.0470 58  THR   A C     
463  O  O     . THR   A 61  ? 0.2720 0.2264 0.2510 -0.0005 -0.0090 -0.0426 58  THR   A O     
464  C  CB    . THR   A 61  ? 0.2423 0.2138 0.2226 0.0133  -0.0043 -0.0439 58  THR   A CB    
465  O  OG1   . THR   A 61  ? 0.2204 0.2002 0.1986 0.0087  -0.0030 -0.0393 58  THR   A OG1   
466  C  CG2   . THR   A 61  ? 0.2403 0.2160 0.2240 0.0177  -0.0028 -0.0408 58  THR   A CG2   
467  N  N     . ALA   A 62  ? 0.3163 0.2657 0.2953 0.0075  -0.0106 -0.0560 59  ALA   A N     
468  C  CA    . ALA   A 62  ? 0.3190 0.2664 0.2968 0.0026  -0.0127 -0.0618 59  ALA   A CA    
469  C  C     . ALA   A 62  ? 0.3054 0.2690 0.2791 0.0047  -0.0114 -0.0675 59  ALA   A C     
470  O  O     . ALA   A 62  ? 0.3071 0.2819 0.2786 0.0018  -0.0104 -0.0637 59  ALA   A O     
471  C  CB    . ALA   A 62  ? 0.3582 0.2887 0.3384 0.0033  -0.0160 -0.0687 59  ALA   A CB    
472  N  N     . GLY   A 63  ? 0.3185 0.2838 0.2909 0.0102  -0.0115 -0.0765 60  GLY   A N     
473  C  CA    . GLY   A 63  ? 0.3319 0.3142 0.2990 0.0120  -0.0101 -0.0817 60  GLY   A CA    
474  C  C     . GLY   A 63  ? 0.3422 0.3394 0.3070 0.0139  -0.0060 -0.0741 60  GLY   A C     
475  O  O     . GLY   A 63  ? 0.3380 0.3336 0.3060 0.0169  -0.0040 -0.0698 60  GLY   A O     
476  N  N     . GLN   A 64  ? 0.3356 0.3467 0.2953 0.0121  -0.0051 -0.0724 61  GLN   A N     
477  C  CA    . GLN   A 64  ? 0.3431 0.3670 0.3007 0.0132  -0.0012 -0.0640 61  GLN   A CA    
478  C  C     . GLN   A 64  ? 0.3683 0.4081 0.3196 0.0171  0.0013  -0.0689 61  GLN   A C     
479  O  O     . GLN   A 64  ? 0.3693 0.4208 0.3172 0.0169  0.0041  -0.0621 61  GLN   A O     
480  C  CB    . GLN   A 64  ? 0.3209 0.3475 0.2782 0.0084  -0.0018 -0.0551 61  GLN   A CB    
481  C  CG    . GLN   A 64  ? 0.3008 0.3146 0.2636 0.0044  -0.0037 -0.0507 61  GLN   A CG    
482  C  CD    . GLN   A 64  ? 0.2831 0.2891 0.2507 0.0057  -0.0021 -0.0457 61  GLN   A CD    
483  O  OE1   . GLN   A 64  ? 0.2649 0.2764 0.2332 0.0068  0.0005  -0.0397 61  GLN   A OE1   
484  N  NE2   . GLN   A 64  ? 0.2896 0.2822 0.2606 0.0050  -0.0041 -0.0479 61  GLN   A NE2   
485  N  N     . GLU   A 65  ? 0.4010 0.4402 0.3509 0.0207  0.0003  -0.0805 62  GLU   A N     
486  C  CA    . GLU   A 65  ? 0.4073 0.4629 0.3501 0.0248  0.0026  -0.0874 62  GLU   A CA    
487  C  C     . GLU   A 65  ? 0.4002 0.4696 0.3422 0.0277  0.0084  -0.0814 62  GLU   A C     
488  O  O     . GLU   A 65  ? 0.3997 0.4649 0.3482 0.0298  0.0103  -0.0790 62  GLU   A O     
489  C  CB    . GLU   A 65  ? 0.4677 0.5185 0.4112 0.0293  0.0008  -0.1020 62  GLU   A CB    
490  C  CG    . GLU   A 65  ? 0.5325 0.5664 0.4790 0.0259  -0.0049 -0.1085 62  GLU   A CG    
491  C  CD    . GLU   A 65  ? 0.5629 0.5755 0.5182 0.0259  -0.0070 -0.1078 62  GLU   A CD    
492  O  OE1   . GLU   A 65  ? 0.5573 0.5675 0.5168 0.0287  -0.0046 -0.1018 62  GLU   A OE1   
493  O  OE2   . GLU   A 65  ? 0.5769 0.5756 0.5346 0.0229  -0.0112 -0.1132 62  GLU   A OE2   
494  N  N     . GLU   A 66  ? 0.4104 0.4969 0.3441 0.0276  0.0108  -0.0793 63  GLU   A N     
495  C  CA    . GLU   A 66  ? 0.4339 0.5359 0.3657 0.0295  0.0168  -0.0740 63  GLU   A CA    
496  C  C     . GLU   A 66  ? 0.3772 0.4834 0.3126 0.0356  0.0197  -0.0834 63  GLU   A C     
497  O  O     . GLU   A 66  ? 0.3906 0.5003 0.3323 0.0368  0.0235  -0.0788 63  GLU   A O     
498  C  CB    . GLU   A 66  ? 0.4728 0.5924 0.3929 0.0288  0.0184  -0.0719 63  GLU   A CB    
499  C  CG    . GLU   A 66  ? 0.5358 0.6736 0.4523 0.0299  0.0252  -0.0661 63  GLU   A CG    
500  C  CD    . GLU   A 66  ? 0.5667 0.7027 0.4878 0.0256  0.0278  -0.0509 63  GLU   A CD    
501  O  OE1   . GLU   A 66  ? 0.6214 0.7435 0.5466 0.0222  0.0242  -0.0444 63  GLU   A OE1   
502  O  OE2   . GLU   A 66  ? 0.6194 0.7683 0.5401 0.0256  0.0336  -0.0459 63  GLU   A OE2   
503  N  N     . TYR   A 67  ? 0.3452 0.4517 0.2776 0.0395  0.0176  -0.0971 64  TYR   A N     
504  C  CA    . TYR   A 67  ? 0.3280 0.4407 0.2631 0.0466  0.0202  -0.1079 64  TYR   A CA    
505  C  C     . TYR   A 67  ? 0.3262 0.4182 0.2705 0.0498  0.0158  -0.1154 64  TYR   A C     
506  O  O     . TYR   A 67  ? 0.3429 0.4244 0.2860 0.0507  0.0112  -0.1257 64  TYR   A O     
507  C  CB    . TYR   A 67  ? 0.3330 0.4617 0.2579 0.0499  0.0211  -0.1191 64  TYR   A CB    
508  C  CG    . TYR   A 67  ? 0.3314 0.4812 0.2465 0.0472  0.0257  -0.1102 64  TYR   A CG    
509  C  CD1   . TYR   A 67  ? 0.3292 0.4926 0.2462 0.0472  0.0324  -0.1015 64  TYR   A CD1   
510  C  CD2   . TYR   A 67  ? 0.3451 0.5009 0.2493 0.0440  0.0231  -0.1092 64  TYR   A CD2   
511  C  CE1   . TYR   A 67  ? 0.3402 0.5211 0.2482 0.0440  0.0367  -0.0916 64  TYR   A CE1   
512  C  CE2   . TYR   A 67  ? 0.3522 0.5263 0.2468 0.0418  0.0270  -0.0995 64  TYR   A CE2   
513  C  CZ    . TYR   A 67  ? 0.3421 0.5278 0.2384 0.0416  0.0339  -0.0902 64  TYR   A CZ    
514  O  OH    . TYR   A 67  ? 0.3614 0.5639 0.2481 0.0388  0.0380  -0.0791 64  TYR   A OH    
515  N  N     . SER   A 68  ? 0.2807 0.3667 0.2341 0.0512  0.0170  -0.1097 65  SER   A N     
516  C  CA    . SER   A 68  ? 0.2712 0.3368 0.2330 0.0539  0.0127  -0.1133 65  SER   A CA    
517  C  C     . SER   A 68  ? 0.2614 0.3307 0.2322 0.0587  0.0154  -0.1107 65  SER   A C     
518  O  O     . SER   A 68  ? 0.2443 0.3163 0.2182 0.0550  0.0174  -0.0993 65  SER   A O     
519  C  CB    . SER   A 68  ? 0.2758 0.3235 0.2391 0.0469  0.0086  -0.1043 65  SER   A CB    
520  O  OG    . SER   A 68  ? 0.2854 0.3144 0.2564 0.0494  0.0050  -0.1056 65  SER   A OG    
521  N  N     . ALA   A 69  ? 0.2745 0.3443 0.2497 0.0672  0.0153  -0.1219 66  ALA   A N     
522  C  CA    . ALA   A 69  ? 0.2906 0.3650 0.2755 0.0728  0.0171  -0.1206 66  ALA   A CA    
523  C  C     . ALA   A 69  ? 0.2915 0.3476 0.2828 0.0703  0.0131  -0.1112 66  ALA   A C     
524  O  O     . ALA   A 69  ? 0.2851 0.3479 0.2825 0.0706  0.0150  -0.1043 66  ALA   A O     
525  C  CB    . ALA   A 69  ? 0.3067 0.3815 0.2961 0.0833  0.0163  -0.1352 66  ALA   A CB    
526  N  N     . MET   A 70  ? 0.3072 0.3413 0.2969 0.0676  0.0077  -0.1112 67  MET   A N     
527  C  CA    . MET   A 70  ? 0.3468 0.3636 0.3411 0.0652  0.0039  -0.1023 67  MET   A CA    
528  C  C     . MET   A 70  ? 0.3181 0.3397 0.3107 0.0571  0.0058  -0.0893 67  MET   A C     
529  O  O     . MET   A 70  ? 0.2912 0.3112 0.2891 0.0570  0.0053  -0.0820 67  MET   A O     
530  C  CB    . MET   A 70  ? 0.4204 0.4130 0.4133 0.0632  -0.0019 -0.1048 67  MET   A CB    
531  C  CG    . MET   A 70  ? 0.4705 0.4452 0.4684 0.0631  -0.0059 -0.0971 67  MET   A CG    
532  S  SD    . MET   A 70  ? 0.6277 0.6032 0.6350 0.0750  -0.0070 -0.1006 67  MET   A SD    
533  C  CE    . MET   A 70  ? 0.5837 0.5651 0.5940 0.0712  -0.0061 -0.0863 67  MET   A CE    
534  N  N     . ARG   A 71  ? 0.2873 0.3144 0.2726 0.0507  0.0073  -0.0868 68  ARG   A N     
535  C  CA    . ARG   A 71  ? 0.2715 0.3046 0.2551 0.0437  0.0094  -0.0752 68  ARG   A CA    
536  C  C     . ARG   A 71  ? 0.2510 0.3013 0.2388 0.0449  0.0142  -0.0710 68  ARG   A C     
537  O  O     . ARG   A 71  ? 0.2435 0.2935 0.2350 0.0416  0.0146  -0.0623 68  ARG   A O     
538  C  CB    . ARG   A 71  ? 0.2828 0.3211 0.2581 0.0383  0.0101  -0.0742 68  ARG   A CB    
539  C  CG    . ARG   A 71  ? 0.3141 0.3531 0.2879 0.0314  0.0108  -0.0626 68  ARG   A CG    
540  C  CD    . ARG   A 71  ? 0.3573 0.3934 0.3247 0.0269  0.0085  -0.0629 68  ARG   A CD    
541  N  NE    . ARG   A 71  ? 0.3784 0.4194 0.3432 0.0217  0.0095  -0.0532 68  ARG   A NE    
542  C  CZ    . ARG   A 71  ? 0.4086 0.4403 0.3756 0.0175  0.0075  -0.0465 68  ARG   A CZ    
543  N  NH1   . ARG   A 71  ? 0.4028 0.4203 0.3741 0.0169  0.0046  -0.0470 68  ARG   A NH1   
544  N  NH2   . ARG   A 71  ? 0.4579 0.4949 0.4227 0.0140  0.0083  -0.0390 68  ARG   A NH2   
545  N  N     . ASP   A 72  ? 0.2570 0.3231 0.2447 0.0496  0.0179  -0.0777 69  ASP   A N     
546  C  CA    . ASP   A 72  ? 0.2634 0.3470 0.2566 0.0501  0.0228  -0.0736 69  ASP   A CA    
547  C  C     . ASP   A 72  ? 0.2615 0.3391 0.2648 0.0539  0.0204  -0.0727 69  ASP   A C     
548  O  O     . ASP   A 72  ? 0.2543 0.3380 0.2626 0.0507  0.0220  -0.0653 69  ASP   A O     
549  C  CB    . ASP   A 72  ? 0.3077 0.4112 0.2997 0.0550  0.0277  -0.0816 69  ASP   A CB    
550  C  CG    . ASP   A 72  ? 0.3782 0.4932 0.3596 0.0511  0.0311  -0.0806 69  ASP   A CG    
551  O  OD1   . ASP   A 72  ? 0.3989 0.5077 0.3747 0.0445  0.0298  -0.0726 69  ASP   A OD1   
552  O  OD2   . ASP   A 72  ? 0.4908 0.6210 0.4690 0.0555  0.0346  -0.0887 69  ASP   A OD2   
553  N  N     . GLN   A 73  ? 0.2662 0.3316 0.2723 0.0605  0.0162  -0.0799 70  GLN   A N     
554  C  CA    . GLN   A 73  ? 0.2907 0.3518 0.3061 0.0652  0.0135  -0.0788 70  GLN   A CA    
555  C  C     . GLN   A 73  ? 0.2814 0.3300 0.2967 0.0590  0.0103  -0.0684 70  GLN   A C     
556  O  O     . GLN   A 73  ? 0.2632 0.3180 0.2849 0.0588  0.0105  -0.0637 70  GLN   A O     
557  C  CB    . GLN   A 73  ? 0.3512 0.4003 0.3696 0.0743  0.0092  -0.0881 70  GLN   A CB    
558  C  CG    . GLN   A 73  ? 0.3942 0.4441 0.4228 0.0817  0.0067  -0.0884 70  GLN   A CG    
559  C  CD    . GLN   A 73  ? 0.4501 0.5247 0.4861 0.0823  0.0115  -0.0870 70  GLN   A CD    
560  O  OE1   . GLN   A 73  ? 0.5057 0.5992 0.5423 0.0840  0.0169  -0.0926 70  GLN   A OE1   
561  N  NE2   . GLN   A 73  ? 0.4802 0.5557 0.5220 0.0805  0.0097  -0.0797 70  GLN   A NE2   
562  N  N     . TYR   A 74  ? 0.2581 0.2907 0.2667 0.0543  0.0075  -0.0658 71  TYR   A N     
563  C  CA    . TYR   A 74  ? 0.2738 0.2961 0.2820 0.0487  0.0050  -0.0564 71  TYR   A CA    
564  C  C     . TYR   A 74  ? 0.2455 0.2795 0.2538 0.0421  0.0086  -0.0489 71  TYR   A C     
565  O  O     . TYR   A 74  ? 0.2498 0.2802 0.2604 0.0394  0.0070  -0.0427 71  TYR   A O     
566  C  CB    . TYR   A 74  ? 0.2883 0.2905 0.2915 0.0461  0.0008  -0.0556 71  TYR   A CB    
567  C  CG    . TYR   A 74  ? 0.2884 0.2888 0.2846 0.0404  0.0017  -0.0561 71  TYR   A CG    
568  C  CD1   . TYR   A 74  ? 0.2726 0.2811 0.2657 0.0342  0.0043  -0.0500 71  TYR   A CD1   
569  C  CD2   . TYR   A 74  ? 0.3142 0.3035 0.3073 0.0413  -0.0009 -0.0626 71  TYR   A CD2   
570  C  CE1   . TYR   A 74  ? 0.2979 0.3052 0.2849 0.0296  0.0043  -0.0502 71  TYR   A CE1   
571  C  CE2   . TYR   A 74  ? 0.3118 0.3003 0.2991 0.0358  -0.0008 -0.0633 71  TYR   A CE2   
572  C  CZ    . TYR   A 74  ? 0.3051 0.3034 0.2893 0.0303  0.0017  -0.0571 71  TYR   A CZ    
573  O  OH    . TYR   A 74  ? 0.3210 0.3195 0.2999 0.0258  0.0012  -0.0580 71  TYR   A OH    
574  N  N     . MET   A 75  ? 0.2247 0.2709 0.2296 0.0396  0.0129  -0.0493 72  MET   A N     
575  C  CA    . MET   A 75  ? 0.2346 0.2906 0.2406 0.0336  0.0161  -0.0416 72  MET   A CA    
576  C  C     . MET   A 75  ? 0.2528 0.3217 0.2682 0.0357  0.0181  -0.0413 72  MET   A C     
577  O  O     . MET   A 75  ? 0.2413 0.3118 0.2603 0.0313  0.0184  -0.0352 72  MET   A O     
578  C  CB    . MET   A 75  ? 0.2372 0.3028 0.2367 0.0302  0.0201  -0.0404 72  MET   A CB    
579  C  CG    . MET   A 75  ? 0.2551 0.3095 0.2467 0.0274  0.0174  -0.0399 72  MET   A CG    
580  S  SD    . MET   A 75  ? 0.2719 0.3371 0.2550 0.0238  0.0207  -0.0374 72  MET   A SD    
581  C  CE    . MET   A 75  ? 0.3084 0.3583 0.2867 0.0199  0.0160  -0.0349 72  MET   A CE    
582  N  N     . ARG   A 76  ? 0.2306 0.3088 0.2502 0.0424  0.0194  -0.0485 73  ARG   A N     
583  C  CA    . ARG   A 76  ? 0.2346 0.3261 0.2646 0.0450  0.0207  -0.0490 73  ARG   A CA    
584  C  C     . ARG   A 76  ? 0.2279 0.3097 0.2634 0.0465  0.0154  -0.0466 73  ARG   A C     
585  O  O     . ARG   A 76  ? 0.2277 0.3177 0.2702 0.0437  0.0157  -0.0427 73  ARG   A O     
586  C  CB    . ARG   A 76  ? 0.2597 0.3643 0.2937 0.0531  0.0230  -0.0584 73  ARG   A CB    
587  C  CG    . ARG   A 76  ? 0.3035 0.4259 0.3341 0.0506  0.0298  -0.0594 73  ARG   A CG    
588  C  CD    . ARG   A 76  ? 0.3655 0.5067 0.4021 0.0580  0.0334  -0.0681 73  ARG   A CD    
589  N  NE    . ARG   A 76  ? 0.4334 0.5663 0.4673 0.0668  0.0304  -0.0786 73  ARG   A NE    
590  C  CZ    . ARG   A 76  ? 0.4579 0.5910 0.4829 0.0683  0.0320  -0.0846 73  ARG   A CZ    
591  N  NH1   . ARG   A 76  ? 0.5021 0.6442 0.5187 0.0618  0.0365  -0.0805 73  ARG   A NH1   
592  N  NH2   . ARG   A 76  ? 0.4819 0.6057 0.5063 0.0765  0.0286  -0.0950 73  ARG   A NH2   
593  N  N     . THR   A 77  ? 0.2170 0.2815 0.2490 0.0503  0.0103  -0.0484 74  THR   A N     
594  C  CA    . THR   A 77  ? 0.2332 0.2880 0.2685 0.0529  0.0048  -0.0460 74  THR   A CA    
595  C  C     . THR   A 77  ? 0.2284 0.2747 0.2599 0.0453  0.0033  -0.0381 74  THR   A C     
596  O  O     . THR   A 77  ? 0.2174 0.2649 0.2532 0.0450  0.0007  -0.0349 74  THR   A O     
597  C  CB    . THR   A 77  ? 0.2740 0.3121 0.3065 0.0596  0.0001  -0.0500 74  THR   A CB    
598  O  OG1   . THR   A 77  ? 0.3063 0.3529 0.3437 0.0679  0.0012  -0.0586 74  THR   A OG1   
599  C  CG2   . THR   A 77  ? 0.2799 0.3077 0.3143 0.0621  -0.0056 -0.0458 74  THR   A CG2   
600  N  N     . GLY   A 78  ? 0.2079 0.2474 0.2318 0.0396  0.0048  -0.0355 75  GLY   A N     
601  C  CA    . GLY   A 78  ? 0.1999 0.2316 0.2202 0.0331  0.0035  -0.0289 75  GLY   A CA    
602  C  C     . GLY   A 78  ? 0.1835 0.2263 0.2091 0.0285  0.0056  -0.0251 75  GLY   A C     
603  O  O     . GLY   A 78  ? 0.2203 0.2758 0.2494 0.0270  0.0098  -0.0256 75  GLY   A O     
604  N  N     . GLU   A 79  ? 0.1668 0.2044 0.1929 0.0259  0.0028  -0.0214 76  GLU   A N     
605  C  CA    . GLU   A 79  ? 0.1674 0.2135 0.1991 0.0212  0.0040  -0.0187 76  GLU   A CA    
606  C  C     . GLU   A 79  ? 0.1534 0.1942 0.1808 0.0147  0.0055  -0.0144 76  GLU   A C     
607  O  O     . GLU   A 79  ? 0.1679 0.2156 0.1995 0.0102  0.0081  -0.0123 76  GLU   A O     
608  C  CB    . GLU   A 79  ? 0.1771 0.2233 0.2128 0.0231  -0.0004 -0.0187 76  GLU   A CB    
609  C  CG    . GLU   A 79  ? 0.1922 0.2468 0.2346 0.0300  -0.0022 -0.0226 76  GLU   A CG    
610  C  CD    . GLU   A 79  ? 0.2490 0.3034 0.2940 0.0324  -0.0075 -0.0221 76  GLU   A CD    
611  O  OE1   . GLU   A 79  ? 0.2384 0.2803 0.2761 0.0331  -0.0111 -0.0195 76  GLU   A OE1   
612  O  OE2   . GLU   A 79  ? 0.3220 0.3901 0.3763 0.0330  -0.0081 -0.0240 76  GLU   A OE2   
613  N  N     . GLY   A 80  ? 0.1367 0.1656 0.1567 0.0142  0.0038  -0.0131 77  GLY   A N     
614  C  CA    . GLY   A 80  ? 0.1402 0.1647 0.1565 0.0093  0.0049  -0.0097 77  GLY   A CA    
615  C  C     . GLY   A 80  ? 0.1300 0.1471 0.1389 0.0095  0.0050  -0.0100 77  GLY   A C     
616  O  O     . GLY   A 80  ? 0.1489 0.1600 0.1549 0.0126  0.0031  -0.0123 77  GLY   A O     
617  N  N     . PHE   A 81  ? 0.1346 0.1517 0.1409 0.0061  0.0068  -0.0074 78  PHE   A N     
618  C  CA    . PHE   A 81  ? 0.1401 0.1533 0.1401 0.0059  0.0070  -0.0080 78  PHE   A CA    
619  C  C     . PHE   A 81  ? 0.1438 0.1518 0.1415 0.0028  0.0060  -0.0051 78  PHE   A C     
620  O  O     . PHE   A 81  ? 0.1531 0.1629 0.1528 0.0006  0.0069  -0.0020 78  PHE   A O     
621  C  CB    . PHE   A 81  ? 0.1485 0.1703 0.1475 0.0060  0.0101  -0.0081 78  PHE   A CB    
622  C  CG    . PHE   A 81  ? 0.1475 0.1764 0.1493 0.0096  0.0115  -0.0120 78  PHE   A CG    
623  C  CD1   . PHE   A 81  ? 0.1596 0.1966 0.1681 0.0095  0.0131  -0.0112 78  PHE   A CD1   
624  C  CD2   . PHE   A 81  ? 0.1588 0.1862 0.1575 0.0133  0.0108  -0.0173 78  PHE   A CD2   
625  C  CE1   . PHE   A 81  ? 0.1555 0.2004 0.1678 0.0134  0.0142  -0.0154 78  PHE   A CE1   
626  C  CE2   . PHE   A 81  ? 0.1697 0.2031 0.1717 0.0178  0.0117  -0.0220 78  PHE   A CE2   
627  C  CZ    . PHE   A 81  ? 0.1618 0.2052 0.1708 0.0181  0.0136  -0.0209 78  PHE   A CZ    
628  N  N     . LEU   A 82  ? 0.1427 0.1441 0.1366 0.0027  0.0041  -0.0063 79  LEU   A N     
629  C  CA    . LEU   A 82  ? 0.1612 0.1597 0.1531 0.0001  0.0035  -0.0044 79  LEU   A CA    
630  C  C     . LEU   A 82  ? 0.1796 0.1810 0.1684 -0.0003 0.0040  -0.0052 79  LEU   A C     
631  O  O     . LEU   A 82  ? 0.1738 0.1733 0.1602 0.0004  0.0033  -0.0085 79  LEU   A O     
632  C  CB    . LEU   A 82  ? 0.2026 0.1942 0.1925 -0.0006 0.0015  -0.0051 79  LEU   A CB    
633  C  CG    . LEU   A 82  ? 0.2217 0.2125 0.2116 -0.0029 0.0011  -0.0031 79  LEU   A CG    
634  C  CD1   . LEU   A 82  ? 0.2235 0.2163 0.2165 -0.0024 0.0012  -0.0020 79  LEU   A CD1   
635  C  CD2   . LEU   A 82  ? 0.2141 0.1993 0.2011 -0.0044 -0.0001 -0.0029 79  LEU   A CD2   
636  N  N     . CYS   A 83  ? 0.1701 0.1759 0.1590 -0.0012 0.0050  -0.0023 80  CYS   A N     
637  C  CA    . CYS   A 83  ? 0.1759 0.1863 0.1611 -0.0011 0.0052  -0.0024 80  CYS   A CA    
638  C  C     . CYS   A 83  ? 0.1739 0.1831 0.1585 -0.0026 0.0034  -0.0019 80  CYS   A C     
639  O  O     . CYS   A 83  ? 0.1812 0.1907 0.1681 -0.0028 0.0033  0.0012  80  CYS   A O     
640  C  CB    . CYS   A 83  ? 0.1928 0.2091 0.1780 -0.0008 0.0072  0.0017  80  CYS   A CB    
641  S  SG    . CYS   A 83  ? 0.2527 0.2743 0.2393 0.0005  0.0100  0.0003  80  CYS   A SG    
642  N  N     . VAL   A 84  ? 0.1600 0.1681 0.1425 -0.0036 0.0019  -0.0055 81  VAL   A N     
643  C  CA    . VAL   A 84  ? 0.1610 0.1692 0.1446 -0.0057 0.0004  -0.0056 81  VAL   A CA    
644  C  C     . VAL   A 84  ? 0.1538 0.1689 0.1353 -0.0058 -0.0010 -0.0067 81  VAL   A C     
645  O  O     . VAL   A 84  ? 0.1558 0.1729 0.1340 -0.0054 -0.0015 -0.0099 81  VAL   A O     
646  C  CB    . VAL   A 84  ? 0.1604 0.1623 0.1441 -0.0081 -0.0004 -0.0084 81  VAL   A CB    
647  C  CG1   . VAL   A 84  ? 0.1534 0.1567 0.1391 -0.0112 -0.0011 -0.0080 81  VAL   A CG1   
648  C  CG2   . VAL   A 84  ? 0.1615 0.1572 0.1460 -0.0072 0.0003  -0.0074 81  VAL   A CG2   
649  N  N     . PHE   A 85  ? 0.1433 0.1623 0.1270 -0.0057 -0.0018 -0.0043 82  PHE   A N     
650  C  CA    . PHE   A 85  ? 0.1501 0.1769 0.1329 -0.0058 -0.0041 -0.0054 82  PHE   A CA    
651  C  C     . PHE   A 85  ? 0.1596 0.1883 0.1471 -0.0081 -0.0050 -0.0066 82  PHE   A C     
652  O  O     . PHE   A 85  ? 0.1606 0.1849 0.1507 -0.0093 -0.0036 -0.0059 82  PHE   A O     
653  C  CB    . PHE   A 85  ? 0.1538 0.1859 0.1351 -0.0024 -0.0045 -0.0008 82  PHE   A CB    
654  C  CG    . PHE   A 85  ? 0.1481 0.1788 0.1339 -0.0006 -0.0044 0.0035  82  PHE   A CG    
655  C  CD1   . PHE   A 85  ? 0.1459 0.1702 0.1332 0.0002  -0.0024 0.0065  82  PHE   A CD1   
656  C  CD2   . PHE   A 85  ? 0.1523 0.1885 0.1414 0.0007  -0.0065 0.0038  82  PHE   A CD2   
657  C  CE1   . PHE   A 85  ? 0.1422 0.1641 0.1341 0.0019  -0.0026 0.0091  82  PHE   A CE1   
658  C  CE2   . PHE   A 85  ? 0.1415 0.1758 0.1353 0.0033  -0.0065 0.0065  82  PHE   A CE2   
659  C  CZ    . PHE   A 85  ? 0.1462 0.1726 0.1413 0.0038  -0.0046 0.0089  82  PHE   A CZ    
660  N  N     . ALA   A 86  ? 0.1596 0.1962 0.1479 -0.0091 -0.0073 -0.0088 83  ALA   A N     
661  C  CA    . ALA   A 86  ? 0.1721 0.2137 0.1660 -0.0113 -0.0079 -0.0098 83  ALA   A CA    
662  C  C     . ALA   A 86  ? 0.1637 0.2139 0.1604 -0.0073 -0.0095 -0.0074 83  ALA   A C     
663  O  O     . ALA   A 86  ? 0.1717 0.2272 0.1656 -0.0044 -0.0117 -0.0062 83  ALA   A O     
664  C  CB    . ALA   A 86  ? 0.1684 0.2133 0.1632 -0.0163 -0.0095 -0.0148 83  ALA   A CB    
665  N  N     . ILE   A 87  ? 0.1574 0.2094 0.1595 -0.0067 -0.0085 -0.0066 84  ILE   A N     
666  C  CA    . ILE   A 87  ? 0.1490 0.2074 0.1549 -0.0015 -0.0101 -0.0044 84  ILE   A CA    
667  C  C     . ILE   A 87  ? 0.1566 0.2281 0.1651 -0.0008 -0.0136 -0.0062 84  ILE   A C     
668  O  O     . ILE   A 87  ? 0.1599 0.2370 0.1709 0.0046  -0.0159 -0.0039 84  ILE   A O     
669  C  CB    . ILE   A 87  ? 0.1529 0.2112 0.1644 0.0000  -0.0083 -0.0045 84  ILE   A CB    
670  C  CG1   . ILE   A 87  ? 0.1691 0.2355 0.1851 -0.0045 -0.0072 -0.0083 84  ILE   A CG1   
671  C  CG2   . ILE   A 87  ? 0.1518 0.1984 0.1608 0.0001  -0.0057 -0.0028 84  ILE   A CG2   
672  C  CD1   . ILE   A 87  ? 0.1914 0.2639 0.2138 -0.0015 -0.0060 -0.0094 84  ILE   A CD1   
673  N  N     . ASN   A 88  ? 0.1512 0.2273 0.1598 -0.0062 -0.0143 -0.0105 85  ASN   A N     
674  C  CA    . ASN   A 88  ? 0.1731 0.2628 0.1844 -0.0065 -0.0181 -0.0135 85  ASN   A CA    
675  C  C     . ASN   A 88  ? 0.1892 0.2795 0.1934 -0.0070 -0.0207 -0.0151 85  ASN   A C     
676  O  O     . ASN   A 88  ? 0.2033 0.3047 0.2092 -0.0088 -0.0242 -0.0191 85  ASN   A O     
677  C  CB    . ASN   A 88  ? 0.1669 0.2638 0.1851 -0.0132 -0.0175 -0.0182 85  ASN   A CB    
678  C  CG    . ASN   A 88  ? 0.1874 0.2751 0.2024 -0.0204 -0.0160 -0.0211 85  ASN   A CG    
679  O  OD1   . ASN   A 88  ? 0.1862 0.2608 0.1953 -0.0200 -0.0140 -0.0193 85  ASN   A OD1   
680  N  ND2   . ASN   A 88  ? 0.2047 0.2990 0.2242 -0.0268 -0.0172 -0.0257 85  ASN   A ND2   
681  N  N     . ASN   A 89  ? 0.1827 0.2633 0.1795 -0.0051 -0.0192 -0.0123 86  ASN   A N     
682  C  CA    . ASN   A 89  ? 0.2035 0.2856 0.1928 -0.0054 -0.0210 -0.0146 86  ASN   A CA    
683  C  C     . ASN   A 89  ? 0.1997 0.2790 0.1824 0.0001  -0.0203 -0.0081 86  ASN   A C     
684  O  O     . ASN   A 89  ? 0.1892 0.2586 0.1693 0.0001  -0.0170 -0.0057 86  ASN   A O     
685  C  CB    . ASN   A 89  ? 0.2159 0.2886 0.2030 -0.0105 -0.0189 -0.0195 86  ASN   A CB    
686  C  CG    . ASN   A 89  ? 0.2612 0.3350 0.2406 -0.0101 -0.0202 -0.0234 86  ASN   A CG    
687  O  OD1   . ASN   A 89  ? 0.2498 0.3304 0.2236 -0.0061 -0.0217 -0.0212 86  ASN   A OD1   
688  N  ND2   . ASN   A 89  ? 0.3245 0.3908 0.3034 -0.0141 -0.0195 -0.0291 86  ASN   A ND2   
689  N  N     . THR   A 90  ? 0.2081 0.2966 0.1887 0.0045  -0.0236 -0.0047 87  THR   A N     
690  C  CA    . THR   A 90  ? 0.2169 0.3023 0.1916 0.0092  -0.0229 0.0032  87  THR   A CA    
691  C  C     . THR   A 90  ? 0.2060 0.2890 0.1717 0.0080  -0.0207 0.0026  87  THR   A C     
692  O  O     . THR   A 90  ? 0.2074 0.2834 0.1702 0.0090  -0.0174 0.0079  87  THR   A O     
693  C  CB    . THR   A 90  ? 0.2480 0.3438 0.2216 0.0146  -0.0275 0.0079  87  THR   A CB    
694  O  OG1   . THR   A 90  ? 0.2675 0.3644 0.2506 0.0170  -0.0288 0.0088  87  THR   A OG1   
695  C  CG2   . THR   A 90  ? 0.2662 0.3584 0.2326 0.0185  -0.0267 0.0171  87  THR   A CG2   
696  N  N     . LYS   A 91  ? 0.2072 0.2967 0.1691 0.0057  -0.0224 -0.0046 88  LYS   A N     
697  C  CA    . LYS   A 91  ? 0.2327 0.3215 0.1865 0.0050  -0.0203 -0.0073 88  LYS   A CA    
698  C  C     . LYS   A 91  ? 0.2078 0.2839 0.1639 0.0030  -0.0155 -0.0078 88  LYS   A C     
699  O  O     . LYS   A 91  ? 0.2200 0.2942 0.1713 0.0042  -0.0124 -0.0051 88  LYS   A O     
700  C  CB    . LYS   A 91  ? 0.2591 0.3553 0.2104 0.0025  -0.0233 -0.0173 88  LYS   A CB    
701  C  CG    . LYS   A 91  ? 0.3261 0.4227 0.2692 0.0028  -0.0213 -0.0218 88  LYS   A CG    
702  C  CD    . LYS   A 91  ? 0.3909 0.4954 0.3309 0.0009  -0.0250 -0.0326 88  LYS   A CD    
703  C  CE    . LYS   A 91  ? 0.4301 0.5352 0.3621 0.0021  -0.0227 -0.0382 88  LYS   A CE    
704  N  NZ    . LYS   A 91  ? 0.4668 0.5769 0.3907 0.0062  -0.0193 -0.0299 88  LYS   A NZ    
705  N  N     . SER   A 92  ? 0.1850 0.2535 0.1484 -0.0001 -0.0149 -0.0109 89  SER   A N     
706  C  CA    . SER   A 92  ? 0.1846 0.2416 0.1502 -0.0016 -0.0111 -0.0112 89  SER   A CA    
707  C  C     . SER   A 92  ? 0.1802 0.2328 0.1466 0.0007  -0.0084 -0.0032 89  SER   A C     
708  O  O     . SER   A 92  ? 0.1746 0.2218 0.1401 0.0007  -0.0053 -0.0024 89  SER   A O     
709  C  CB    . SER   A 92  ? 0.1736 0.2241 0.1460 -0.0055 -0.0113 -0.0148 89  SER   A CB    
710  O  OG    . SER   A 92  ? 0.1571 0.2078 0.1352 -0.0054 -0.0114 -0.0109 89  SER   A OG    
711  N  N     . PHE   A 93  ? 0.1722 0.2270 0.1410 0.0028  -0.0098 0.0023  90  PHE   A N     
712  C  CA    . PHE   A 93  ? 0.1889 0.2386 0.1589 0.0048  -0.0077 0.0099  90  PHE   A CA    
713  C  C     . PHE   A 93  ? 0.2128 0.2663 0.1755 0.0063  -0.0063 0.0146  90  PHE   A C     
714  O  O     . PHE   A 93  ? 0.2041 0.2529 0.1670 0.0058  -0.0031 0.0184  90  PHE   A O     
715  C  CB    . PHE   A 93  ? 0.1860 0.2364 0.1609 0.0074  -0.0101 0.0137  90  PHE   A CB    
716  C  CG    . PHE   A 93  ? 0.1816 0.2250 0.1587 0.0095  -0.0088 0.0210  90  PHE   A CG    
717  C  CD1   . PHE   A 93  ? 0.1775 0.2117 0.1594 0.0079  -0.0062 0.0206  90  PHE   A CD1   
718  C  CD2   . PHE   A 93  ? 0.2053 0.2508 0.1800 0.0131  -0.0107 0.0283  90  PHE   A CD2   
719  C  CE1   . PHE   A 93  ? 0.1821 0.2093 0.1669 0.0092  -0.0054 0.0263  90  PHE   A CE1   
720  C  CE2   . PHE   A 93  ? 0.2296 0.2665 0.2073 0.0145  -0.0098 0.0350  90  PHE   A CE2   
721  C  CZ    . PHE   A 93  ? 0.2084 0.2361 0.1917 0.0123  -0.0071 0.0334  90  PHE   A CZ    
722  N  N     . GLU   A 94  ? 0.2299 0.2934 0.1863 0.0079  -0.0088 0.0145  91  GLU   A N     
723  C  CA    . GLU   A 94  ? 0.2699 0.3395 0.2176 0.0092  -0.0072 0.0190  91  GLU   A CA    
724  C  C     . GLU   A 94  ? 0.2790 0.3491 0.2236 0.0074  -0.0035 0.0140  91  GLU   A C     
725  O  O     . GLU   A 94  ? 0.3730 0.4461 0.3132 0.0077  -0.0002 0.0186  91  GLU   A O     
726  C  CB    . GLU   A 94  ? 0.2763 0.3582 0.2170 0.0115  -0.0113 0.0188  91  GLU   A CB    
727  C  CG    . GLU   A 94  ? 0.2901 0.3727 0.2332 0.0147  -0.0149 0.0259  91  GLU   A CG    
728  C  CD    . GLU   A 94  ? 0.3353 0.4315 0.2702 0.0178  -0.0192 0.0272  91  GLU   A CD    
729  O  OE1   . GLU   A 94  ? 0.4313 0.5361 0.3571 0.0173  -0.0185 0.0241  91  GLU   A OE1   
730  O  OE2   . GLU   A 94  ? 0.3096 0.4084 0.2472 0.0211  -0.0234 0.0310  91  GLU   A OE2   
731  N  N     . ASP   A 95  ? 0.2629 0.3303 0.2103 0.0057  -0.0039 0.0048  92  ASP   A N     
732  C  CA    . ASP   A 95  ? 0.2670 0.3338 0.2128 0.0051  -0.0009 -0.0010 92  ASP   A CA    
733  C  C     . ASP   A 95  ? 0.2434 0.3027 0.1943 0.0044  0.0030  0.0026  92  ASP   A C     
734  O  O     . ASP   A 95  ? 0.2588 0.3202 0.2084 0.0047  0.0061  -0.0001 92  ASP   A O     
735  C  CB    . ASP   A 95  ? 0.2965 0.3591 0.2449 0.0035  -0.0029 -0.0111 92  ASP   A CB    
736  C  CG    . ASP   A 95  ? 0.3589 0.4299 0.3026 0.0035  -0.0068 -0.0176 92  ASP   A CG    
737  O  OD1   . ASP   A 95  ? 0.3211 0.4034 0.2573 0.0055  -0.0079 -0.0161 92  ASP   A OD1   
738  O  OD2   . ASP   A 95  ? 0.4069 0.4730 0.3547 0.0010  -0.0090 -0.0245 92  ASP   A OD2   
739  N  N     . ILE   A 96  ? 0.2249 0.2765 0.1821 0.0035  0.0028  0.0077  93  ILE   A N     
740  C  CA    . ILE   A 96  ? 0.2141 0.2588 0.1771 0.0024  0.0058  0.0097  93  ILE   A CA    
741  C  C     . ILE   A 96  ? 0.2131 0.2630 0.1738 0.0023  0.0096  0.0142  93  ILE   A C     
742  O  O     . ILE   A 96  ? 0.2051 0.2548 0.1687 0.0018  0.0123  0.0117  93  ILE   A O     
743  C  CB    . ILE   A 96  ? 0.2031 0.2401 0.1724 0.0017  0.0046  0.0142  93  ILE   A CB    
744  C  CG1   . ILE   A 96  ? 0.1913 0.2242 0.1639 0.0012  0.0019  0.0091  93  ILE   A CG1   
745  C  CG2   . ILE   A 96  ? 0.2017 0.2333 0.1765 0.0004  0.0073  0.0170  93  ILE   A CG2   
746  C  CD1   . ILE   A 96  ? 0.1999 0.2274 0.1751 -0.0002 0.0027  0.0035  93  ILE   A CD1   
747  N  N     . HIS   A 97  ? 0.2237 0.2790 0.1796 0.0027  0.0099  0.0213  94  HIS   A N     
748  C  CA    . HIS   A 97  ? 0.2555 0.3168 0.2090 0.0016  0.0142  0.0273  94  HIS   A CA    
749  C  C     . HIS   A 97  ? 0.2388 0.3096 0.1887 0.0024  0.0172  0.0206  94  HIS   A C     
750  O  O     . HIS   A 97  ? 0.2440 0.3184 0.1964 0.0011  0.0213  0.0220  94  HIS   A O     
751  C  CB    . HIS   A 97  ? 0.3195 0.3852 0.2665 0.0024  0.0132  0.0362  94  HIS   A CB    
752  C  CG    . HIS   A 97  ? 0.4051 0.4783 0.3477 0.0008  0.0176  0.0439  94  HIS   A CG    
753  N  ND1   . HIS   A 97  ? 0.4904 0.5578 0.4378 -0.0022 0.0199  0.0532  94  HIS   A ND1   
754  C  CD2   . HIS   A 97  ? 0.4412 0.5279 0.3749 0.0014  0.0204  0.0438  94  HIS   A CD2   
755  C  CE1   . HIS   A 97  ? 0.4715 0.5485 0.4136 -0.0040 0.0242  0.0591  94  HIS   A CE1   
756  N  NE2   . HIS   A 97  ? 0.5192 0.6088 0.4526 -0.0016 0.0248  0.0534  94  HIS   A NE2   
757  N  N     . HIS   A 98  ? 0.2408 0.3160 0.1853 0.0045  0.0150  0.0130  95  HIS   A N     
758  C  CA    . HIS   A 98  ? 0.2734 0.3575 0.2138 0.0062  0.0173  0.0054  95  HIS   A CA    
759  C  C     . HIS   A 98  ? 0.2386 0.3161 0.1872 0.0065  0.0184  -0.0009 95  HIS   A C     
760  O  O     . HIS   A 98  ? 0.2317 0.3160 0.1813 0.0075  0.0222  -0.0034 95  HIS   A O     
761  C  CB    . HIS   A 98  ? 0.3371 0.4250 0.2710 0.0081  0.0134  -0.0024 95  HIS   A CB    
762  C  CG    . HIS   A 98  ? 0.4539 0.5526 0.3816 0.0106  0.0153  -0.0108 95  HIS   A CG    
763  N  ND1   . HIS   A 98  ? 0.4967 0.6092 0.4137 0.0120  0.0155  -0.0105 95  HIS   A ND1   
764  C  CD2   . HIS   A 98  ? 0.5063 0.6041 0.4367 0.0125  0.0165  -0.0206 95  HIS   A CD2   
765  C  CE1   . HIS   A 98  ? 0.5789 0.6993 0.4922 0.0145  0.0172  -0.0204 95  HIS   A CE1   
766  N  NE2   . HIS   A 98  ? 0.5339 0.6452 0.4559 0.0151  0.0178  -0.0267 95  HIS   A NE2   
767  N  N     . TYR   A 99  ? 0.2258 0.2910 0.1804 0.0057  0.0152  -0.0029 96  TYR   A N     
768  C  CA    . TYR   A 99  ? 0.2330 0.2915 0.1948 0.0063  0.0157  -0.0074 96  TYR   A CA    
769  C  C     . TYR   A 99  ? 0.2326 0.2926 0.2004 0.0049  0.0191  -0.0018 96  TYR   A C     
770  O  O     . TYR   A 99  ? 0.2416 0.3054 0.2132 0.0063  0.0214  -0.0053 96  TYR   A O     
771  C  CB    . TYR   A 99  ? 0.2395 0.2854 0.2050 0.0053  0.0117  -0.0097 96  TYR   A CB    
772  C  CG    . TYR   A 99  ? 0.2970 0.3418 0.2582 0.0055  0.0083  -0.0157 96  TYR   A CG    
773  C  CD1   . TYR   A 99  ? 0.3595 0.4101 0.3157 0.0077  0.0083  -0.0232 96  TYR   A CD1   
774  C  CD2   . TYR   A 99  ? 0.3116 0.3508 0.2742 0.0034  0.0051  -0.0145 96  TYR   A CD2   
775  C  CE1   . TYR   A 99  ? 0.3995 0.4490 0.3526 0.0072  0.0048  -0.0296 96  TYR   A CE1   
776  C  CE2   . TYR   A 99  ? 0.3460 0.3852 0.3061 0.0026  0.0020  -0.0201 96  TYR   A CE2   
777  C  CZ    . TYR   A 99  ? 0.3902 0.4340 0.3456 0.0042  0.0015  -0.0278 96  TYR   A CZ    
778  O  OH    . TYR   A 99  ? 0.3678 0.4117 0.3214 0.0027  -0.0021 -0.0343 96  TYR   A OH    
779  N  N     . ARG   A 100 ? 0.2301 0.2876 0.1996 0.0021  0.0193  0.0065  97  ARG   A N     
780  C  CA    . ARG   A 100 ? 0.2460 0.3051 0.2217 -0.0002 0.0224  0.0116  97  ARG   A CA    
781  C  C     . ARG   A 100 ? 0.2561 0.3291 0.2299 -0.0004 0.0274  0.0127  97  ARG   A C     
782  O  O     . ARG   A 100 ? 0.2609 0.3387 0.2412 -0.0010 0.0302  0.0114  97  ARG   A O     
783  C  CB    . ARG   A 100 ? 0.2600 0.3129 0.2377 -0.0031 0.0216  0.0200  97  ARG   A CB    
784  C  CG    . ARG   A 100 ? 0.2786 0.3310 0.2640 -0.0065 0.0241  0.0245  97  ARG   A CG    
785  C  CD    . ARG   A 100 ? 0.3137 0.3560 0.3026 -0.0087 0.0221  0.0307  97  ARG   A CD    
786  N  NE    . ARG   A 100 ? 0.3077 0.3504 0.3032 -0.0131 0.0249  0.0364  97  ARG   A NE    
787  C  CZ    . ARG   A 100 ? 0.3344 0.3739 0.3390 -0.0154 0.0249  0.0342  97  ARG   A CZ    
788  N  NH1   . ARG   A 100 ? 0.3341 0.3698 0.3416 -0.0132 0.0222  0.0269  97  ARG   A NH1   
789  N  NH2   . ARG   A 100 ? 0.3995 0.4399 0.4104 -0.0202 0.0274  0.0395  97  ARG   A NH2   
790  N  N     . GLU   A 101 ? 0.2430 0.3241 0.2079 0.0002  0.0285  0.0149  98  GLU   A N     
791  C  CA    . GLU   A 101 ? 0.2734 0.3699 0.2347 0.0001  0.0337  0.0160  98  GLU   A CA    
792  C  C     . GLU   A 101 ? 0.2338 0.3373 0.1971 0.0038  0.0352  0.0055  98  GLU   A C     
793  O  O     . GLU   A 101 ? 0.2606 0.3750 0.2279 0.0032  0.0399  0.0057  98  GLU   A O     
794  C  CB    . GLU   A 101 ? 0.3027 0.4071 0.2521 0.0008  0.0338  0.0195  98  GLU   A CB    
795  C  CG    . GLU   A 101 ? 0.3669 0.4674 0.3143 -0.0025 0.0335  0.0321  98  GLU   A CG    
796  C  CD    . GLU   A 101 ? 0.4590 0.5611 0.4132 -0.0073 0.0381  0.0403  98  GLU   A CD    
797  O  OE1   . GLU   A 101 ? 0.5089 0.6252 0.4617 -0.0084 0.0435  0.0408  98  GLU   A OE1   
798  O  OE2   . GLU   A 101 ? 0.4972 0.5871 0.4586 -0.0101 0.0364  0.0456  98  GLU   A OE2   
799  N  N     . GLN   A 102 ? 0.2255 0.3226 0.1871 0.0075  0.0313  -0.0034 99  GLN   A N     
800  C  CA    . GLN   A 102 ? 0.2458 0.3466 0.2095 0.0120  0.0318  -0.0142 99  GLN   A CA    
801  C  C     . GLN   A 102 ? 0.2317 0.3296 0.2065 0.0121  0.0325  -0.0146 99  GLN   A C     
802  O  O     . GLN   A 102 ? 0.2187 0.3271 0.1976 0.0145  0.0357  -0.0187 99  GLN   A O     
803  C  CB    . GLN   A 102 ? 0.2635 0.3542 0.2247 0.0150  0.0269  -0.0227 99  GLN   A CB    
804  C  CG    . GLN   A 102 ? 0.3481 0.4433 0.2990 0.0159  0.0253  -0.0262 99  GLN   A CG    
805  C  CD    . GLN   A 102 ? 0.3861 0.4695 0.3366 0.0174  0.0200  -0.0347 99  GLN   A CD    
806  O  OE1   . GLN   A 102 ? 0.3951 0.4647 0.3516 0.0164  0.0171  -0.0345 99  GLN   A OE1   
807  N  NE2   . GLN   A 102 ? 0.4466 0.5359 0.3897 0.0192  0.0188  -0.0419 99  GLN   A NE2   
808  N  N     . ILE   A 103 ? 0.2074 0.2922 0.1871 0.0097  0.0293  -0.0108 100 ILE   A N     
809  C  CA    . ILE   A 103 ? 0.2047 0.2865 0.1944 0.0098  0.0290  -0.0113 100 ILE   A CA    
810  C  C     . ILE   A 103 ? 0.2176 0.3119 0.2133 0.0067  0.0338  -0.0063 100 ILE   A C     
811  O  O     . ILE   A 103 ? 0.2186 0.3210 0.2215 0.0087  0.0355  -0.0102 100 ILE   A O     
812  C  CB    . ILE   A 103 ? 0.2073 0.2743 0.1999 0.0076  0.0247  -0.0082 100 ILE   A CB    
813  C  CG1   . ILE   A 103 ? 0.2168 0.2727 0.2050 0.0100  0.0205  -0.0133 100 ILE   A CG1   
814  C  CG2   . ILE   A 103 ? 0.2146 0.2805 0.2167 0.0077  0.0241  -0.0088 100 ILE   A CG2   
815  C  CD1   . ILE   A 103 ? 0.2038 0.2475 0.1921 0.0074  0.0170  -0.0099 100 ILE   A CD1   
816  N  N     . LYS   A 104 ? 0.2118 0.3077 0.2051 0.0017  0.0358  0.0024  101 LYS   A N     
817  C  CA    . LYS   A 104 ? 0.2254 0.3326 0.2242 -0.0029 0.0408  0.0085  101 LYS   A CA    
818  C  C     . LYS   A 104 ? 0.2322 0.3584 0.2304 -0.0006 0.0461  0.0045  101 LYS   A C     
819  O  O     . LYS   A 104 ? 0.2282 0.3653 0.2353 -0.0020 0.0495  0.0042  101 LYS   A O     
820  C  CB    . LYS   A 104 ? 0.2627 0.3672 0.2570 -0.0081 0.0420  0.0191  101 LYS   A CB    
821  C  CG    . LYS   A 104 ? 0.2883 0.3767 0.2872 -0.0111 0.0380  0.0235  101 LYS   A CG    
822  C  CD    . LYS   A 104 ? 0.3429 0.4257 0.3360 -0.0140 0.0378  0.0329  101 LYS   A CD    
823  C  CE    . LYS   A 104 ? 0.3981 0.4876 0.3941 -0.0199 0.0426  0.0422  101 LYS   A CE    
824  N  NZ    . LYS   A 104 ? 0.4440 0.5304 0.4313 -0.0212 0.0426  0.0519  101 LYS   A NZ    
825  N  N     . ARG   A 105 ? 0.2382 0.3689 0.2264 0.0033  0.0465  0.0004  102 ARG   A N     
826  C  CA    . ARG   A 105 ? 0.2598 0.4099 0.2461 0.0063  0.0516  -0.0048 102 ARG   A CA    
827  C  C     . ARG   A 105 ? 0.2444 0.3979 0.2396 0.0119  0.0510  -0.0150 102 ARG   A C     
828  O  O     . ARG   A 105 ? 0.2627 0.4331 0.2637 0.0123  0.0559  -0.0166 102 ARG   A O     
829  C  CB    . ARG   A 105 ? 0.2984 0.4524 0.2712 0.0096  0.0515  -0.0083 102 ARG   A CB    
830  C  CG    . ARG   A 105 ? 0.3535 0.5263 0.3243 0.0145  0.0559  -0.0172 102 ARG   A CG    
831  C  CD    . ARG   A 105 ? 0.4169 0.5965 0.3738 0.0174  0.0561  -0.0213 102 ARG   A CD    
832  N  NE    . ARG   A 105 ? 0.4738 0.6385 0.4231 0.0169  0.0502  -0.0201 102 ARG   A NE    
833  C  CZ    . ARG   A 105 ? 0.5285 0.6804 0.4777 0.0208  0.0446  -0.0292 102 ARG   A CZ    
834  N  NH1   . ARG   A 105 ? 0.5501 0.7003 0.5060 0.0259  0.0438  -0.0395 102 ARG   A NH1   
835  N  NH2   . ARG   A 105 ? 0.5518 0.6928 0.4949 0.0195  0.0397  -0.0276 102 ARG   A NH2   
836  N  N     . VAL   A 106 ? 0.2482 0.3865 0.2445 0.0161  0.0451  -0.0211 103 VAL   A N     
837  C  CA    . VAL   A 106 ? 0.2510 0.3898 0.2550 0.0225  0.0434  -0.0303 103 VAL   A CA    
838  C  C     . VAL   A 106 ? 0.2351 0.3780 0.2517 0.0200  0.0441  -0.0269 103 VAL   A C     
839  O  O     . VAL   A 106 ? 0.2240 0.3789 0.2487 0.0241  0.0458  -0.0325 103 VAL   A O     
840  C  CB    . VAL   A 106 ? 0.2849 0.4039 0.2867 0.0263  0.0366  -0.0354 103 VAL   A CB    
841  C  CG1   . VAL   A 106 ? 0.3172 0.4331 0.3281 0.0322  0.0338  -0.0418 103 VAL   A CG1   
842  C  CG2   . VAL   A 106 ? 0.2898 0.4070 0.2815 0.0296  0.0357  -0.0420 103 VAL   A CG2   
843  N  N     . LYS   A 107 ? 0.2154 0.3492 0.2341 0.0136  0.0426  -0.0186 104 LYS   A N     
844  C  CA    . LYS   A 107 ? 0.2165 0.3536 0.2473 0.0104  0.0425  -0.0159 104 LYS   A CA    
845  C  C     . LYS   A 107 ? 0.2276 0.3831 0.2639 0.0049  0.0490  -0.0111 104 LYS   A C     
846  O  O     . LYS   A 107 ? 0.2455 0.4097 0.2936 0.0029  0.0499  -0.0111 104 LYS   A O     
847  C  CB    . LYS   A 107 ? 0.1995 0.3200 0.2309 0.0054  0.0383  -0.0098 104 LYS   A CB    
848  C  CG    . LYS   A 107 ? 0.2009 0.3042 0.2288 0.0095  0.0320  -0.0135 104 LYS   A CG    
849  C  CD    . LYS   A 107 ? 0.2133 0.3180 0.2477 0.0159  0.0291  -0.0205 104 LYS   A CD    
850  C  CE    . LYS   A 107 ? 0.2058 0.2922 0.2361 0.0186  0.0231  -0.0220 104 LYS   A CE    
851  N  NZ    . LYS   A 107 ? 0.2116 0.2981 0.2476 0.0252  0.0197  -0.0275 104 LYS   A NZ    
852  N  N     . ASP   A 108 ? 0.2356 0.3972 0.2632 0.0020  0.0534  -0.0063 105 ASP   A N     
853  C  CA    . ASP   A 108 ? 0.2671 0.4452 0.2985 -0.0048 0.0603  0.0008  105 ASP   A CA    
854  C  C     . ASP   A 108 ? 0.2700 0.4394 0.3101 -0.0127 0.0587  0.0084  105 ASP   A C     
855  O  O     . ASP   A 108 ? 0.2636 0.4455 0.3139 -0.0179 0.0625  0.0111  105 ASP   A O     
856  C  CB    . ASP   A 108 ? 0.2969 0.4989 0.3354 -0.0016 0.0656  -0.0055 105 ASP   A CB    
857  C  CG    . ASP   A 108 ? 0.3560 0.5761 0.3995 -0.0098 0.0730  0.0023  105 ASP   A CG    
858  O  OD1   . ASP   A 108 ? 0.3887 0.6071 0.4234 -0.0149 0.0757  0.0111  105 ASP   A OD1   
859  O  OD2   . ASP   A 108 ? 0.3607 0.5963 0.4176 -0.0110 0.0758  -0.0002 105 ASP   A OD2   
860  N  N     . SER   A 109 ? 0.2759 0.4248 0.3123 -0.0134 0.0531  0.0108  106 SER   A N     
861  C  CA    . SER   A 109 ? 0.2845 0.4236 0.3293 -0.0197 0.0508  0.0158  106 SER   A CA    
862  C  C     . SER   A 109 ? 0.3590 0.4794 0.3962 -0.0221 0.0475  0.0221  106 SER   A C     
863  O  O     . SER   A 109 ? 0.3596 0.4723 0.3872 -0.0173 0.0449  0.0198  106 SER   A O     
864  C  CB    . SER   A 109 ? 0.3070 0.4420 0.3597 -0.0159 0.0457  0.0084  106 SER   A CB    
865  O  OG    . SER   A 109 ? 0.3596 0.4851 0.4193 -0.0213 0.0428  0.0115  106 SER   A OG    
866  N  N     . GLU   A 110 ? 0.3965 0.5097 0.4398 -0.0290 0.0471  0.0286  107 GLU   A N     
867  C  CA    . GLU   A 110 ? 0.4396 0.5340 0.4778 -0.0302 0.0432  0.0333  107 GLU   A CA    
868  C  C     . GLU   A 110 ? 0.3509 0.4342 0.3948 -0.0284 0.0375  0.0273  107 GLU   A C     
869  O  O     . GLU   A 110 ? 0.3796 0.4486 0.4194 -0.0274 0.0337  0.0282  107 GLU   A O     
870  C  CB    . GLU   A 110 ? 0.5258 0.6172 0.5666 -0.0381 0.0460  0.0439  107 GLU   A CB    
871  C  CG    . GLU   A 110 ? 0.5766 0.6753 0.6073 -0.0388 0.0505  0.0515  107 GLU   A CG    
872  C  CD    . GLU   A 110 ? 0.6792 0.7766 0.7136 -0.0474 0.0540  0.0631  107 GLU   A CD    
873  O  OE1   . GLU   A 110 ? 0.7258 0.8076 0.7656 -0.0508 0.0507  0.0662  107 GLU   A OE1   
874  O  OE2   . GLU   A 110 ? 0.6918 0.8036 0.7238 -0.0508 0.0601  0.0690  107 GLU   A OE2   
875  N  N     . ASP   A 111 ? 0.3546 0.4460 0.4077 -0.0281 0.0370  0.0215  108 ASP   A N     
876  C  CA    . ASP   A 111 ? 0.3585 0.4418 0.4163 -0.0262 0.0315  0.0158  108 ASP   A CA    
877  C  C     . ASP   A 111 ? 0.3221 0.4012 0.3720 -0.0182 0.0283  0.0100  108 ASP   A C     
878  O  O     . ASP   A 111 ? 0.3908 0.4774 0.4440 -0.0140 0.0273  0.0042  108 ASP   A O     
879  C  CB    . ASP   A 111 ? 0.3544 0.4501 0.4251 -0.0282 0.0316  0.0117  108 ASP   A CB    
880  C  CG    . ASP   A 111 ? 0.4049 0.5015 0.4857 -0.0373 0.0331  0.0161  108 ASP   A CG    
881  O  OD1   . ASP   A 111 ? 0.4251 0.5131 0.5029 -0.0420 0.0349  0.0235  108 ASP   A OD1   
882  O  OD2   . ASP   A 111 ? 0.3459 0.4519 0.4384 -0.0397 0.0322  0.0122  108 ASP   A OD2   
883  N  N     . VAL   A 112 ? 0.2803 0.3479 0.3206 -0.0161 0.0264  0.0115  109 VAL   A N     
884  C  CA    . VAL   A 112 ? 0.2305 0.2933 0.2645 -0.0098 0.0234  0.0062  109 VAL   A CA    
885  C  C     . VAL   A 112 ? 0.2032 0.2521 0.2346 -0.0094 0.0189  0.0057  109 VAL   A C     
886  O  O     . VAL   A 112 ? 0.2028 0.2442 0.2299 -0.0111 0.0186  0.0094  109 VAL   A O     
887  C  CB    . VAL   A 112 ? 0.2463 0.3108 0.2707 -0.0068 0.0252  0.0062  109 VAL   A CB    
888  C  CG1   . VAL   A 112 ? 0.2697 0.3299 0.2901 -0.0008 0.0221  -0.0003 109 VAL   A CG1   
889  C  CG2   . VAL   A 112 ? 0.2600 0.3397 0.2854 -0.0075 0.0305  0.0072  109 VAL   A CG2   
890  N  N     . PRO   A 113 ? 0.1692 0.2156 0.2027 -0.0067 0.0153  0.0012  110 PRO   A N     
891  C  CA    . PRO   A 113 ? 0.1582 0.1934 0.1882 -0.0063 0.0116  0.0006  110 PRO   A CA    
892  C  C     . PRO   A 113 ? 0.1579 0.1863 0.1789 -0.0040 0.0111  0.0010  110 PRO   A C     
893  O  O     . PRO   A 113 ? 0.1510 0.1806 0.1682 -0.0005 0.0111  -0.0016 110 PRO   A O     
894  C  CB    . PRO   A 113 ? 0.1611 0.1974 0.1936 -0.0032 0.0082  -0.0037 110 PRO   A CB    
895  C  CG    . PRO   A 113 ? 0.1697 0.2183 0.2107 -0.0035 0.0098  -0.0052 110 PRO   A CG    
896  C  CD    . PRO   A 113 ? 0.1686 0.2234 0.2080 -0.0039 0.0144  -0.0032 110 PRO   A CD    
897  N  N     A MET   A 114 ? 0.1531 0.1751 0.1714 -0.0059 0.0107  0.0039  111 MET   A N     
898  N  N     B MET   A 114 ? 0.1537 0.1750 0.1720 -0.0057 0.0103  0.0034  111 MET   A N     
899  C  CA    A MET   A 114 ? 0.1598 0.1772 0.1707 -0.0044 0.0102  0.0043  111 MET   A CA    
900  C  CA    B MET   A 114 ? 0.1629 0.1802 0.1740 -0.0045 0.0101  0.0043  111 MET   A CA    
901  C  C     A MET   A 114 ? 0.1564 0.1666 0.1669 -0.0053 0.0081  0.0050  111 MET   A C     
902  C  C     B MET   A 114 ? 0.1591 0.1692 0.1696 -0.0054 0.0081  0.0051  111 MET   A C     
903  O  O     A MET   A 114 ? 0.1579 0.1663 0.1732 -0.0074 0.0079  0.0063  111 MET   A O     
904  O  O     B MET   A 114 ? 0.1620 0.1702 0.1772 -0.0075 0.0079  0.0065  111 MET   A O     
905  C  CB    A MET   A 114 ? 0.1806 0.2022 0.1881 -0.0050 0.0128  0.0077  111 MET   A CB    
906  C  CB    B MET   A 114 ? 0.1877 0.2098 0.1966 -0.0054 0.0130  0.0079  111 MET   A CB    
907  C  CG    A MET   A 114 ? 0.1950 0.2257 0.2017 -0.0036 0.0155  0.0062  111 MET   A CG    
908  C  CG    B MET   A 114 ? 0.1973 0.2178 0.1989 -0.0040 0.0124  0.0083  111 MET   A CG    
909  S  SD    A MET   A 114 ? 0.2293 0.2649 0.2285 -0.0037 0.0177  0.0098  111 MET   A SD    
910  S  SD    B MET   A 114 ? 0.2520 0.2807 0.2495 -0.0046 0.0157  0.0127  111 MET   A SD    
911  C  CE    A MET   A 114 ? 0.2281 0.2538 0.2252 -0.0045 0.0146  0.0127  111 MET   A CE    
912  C  CE    B MET   A 114 ? 0.2397 0.2773 0.2375 -0.0023 0.0178  0.0074  111 MET   A CE    
913  N  N     . VAL   A 115 ? 0.1474 0.1540 0.1530 -0.0040 0.0067  0.0037  112 VAL   A N     
914  C  CA    . VAL   A 115 ? 0.1500 0.1522 0.1550 -0.0044 0.0053  0.0042  112 VAL   A CA    
915  C  C     . VAL   A 115 ? 0.1481 0.1510 0.1485 -0.0037 0.0054  0.0052  112 VAL   A C     
916  O  O     . VAL   A 115 ? 0.1665 0.1705 0.1631 -0.0030 0.0053  0.0034  112 VAL   A O     
917  C  CB    . VAL   A 115 ? 0.1732 0.1728 0.1775 -0.0039 0.0035  0.0013  112 VAL   A CB    
918  C  CG1   . VAL   A 115 ? 0.1670 0.1646 0.1700 -0.0040 0.0028  0.0010  112 VAL   A CG1   
919  C  CG2   . VAL   A 115 ? 0.1639 0.1642 0.1726 -0.0044 0.0027  -0.0002 112 VAL   A CG2   
920  N  N     . LEU   A 116 ? 0.1376 0.1396 0.1386 -0.0036 0.0051  0.0077  113 LEU   A N     
921  C  CA    . LEU   A 116 ? 0.1452 0.1494 0.1425 -0.0027 0.0044  0.0085  113 LEU   A CA    
922  C  C     . LEU   A 116 ? 0.1374 0.1406 0.1349 -0.0026 0.0030  0.0057  113 LEU   A C     
923  O  O     . LEU   A 116 ? 0.1505 0.1515 0.1512 -0.0023 0.0025  0.0050  113 LEU   A O     
924  C  CB    . LEU   A 116 ? 0.1546 0.1590 0.1530 -0.0019 0.0042  0.0131  113 LEU   A CB    
925  C  CG    . LEU   A 116 ? 0.1593 0.1676 0.1542 -0.0003 0.0028  0.0143  113 LEU   A CG    
926  C  CD1   . LEU   A 116 ? 0.1706 0.1844 0.1598 -0.0005 0.0035  0.0133  113 LEU   A CD1   
927  C  CD2   . LEU   A 116 ? 0.1729 0.1799 0.1692 0.0014  0.0020  0.0199  113 LEU   A CD2   
928  N  N     . VAL   A 117 ? 0.1397 0.1447 0.1339 -0.0032 0.0024  0.0035  114 VAL   A N     
929  C  CA    . VAL   A 117 ? 0.1389 0.1442 0.1333 -0.0043 0.0017  0.0014  114 VAL   A CA    
930  C  C     . VAL   A 117 ? 0.1352 0.1457 0.1290 -0.0043 0.0006  0.0012  114 VAL   A C     
931  O  O     . VAL   A 117 ? 0.1309 0.1434 0.1217 -0.0049 0.0001  0.0002  114 VAL   A O     
932  C  CB    . VAL   A 117 ? 0.1493 0.1514 0.1413 -0.0060 0.0017  -0.0006 114 VAL   A CB    
933  C  CG1   . VAL   A 117 ? 0.1564 0.1596 0.1483 -0.0083 0.0015  -0.0017 114 VAL   A CG1   
934  C  CG2   . VAL   A 117 ? 0.1671 0.1657 0.1599 -0.0054 0.0021  -0.0004 114 VAL   A CG2   
935  N  N     . GLY   A 118 ? 0.1376 0.1512 0.1346 -0.0033 0.0001  0.0012  115 GLY   A N     
936  C  CA    . GLY   A 118 ? 0.1445 0.1653 0.1425 -0.0034 -0.0013 0.0002  115 GLY   A CA    
937  C  C     . GLY   A 118 ? 0.1574 0.1802 0.1562 -0.0068 -0.0007 -0.0025 115 GLY   A C     
938  O  O     . GLY   A 118 ? 0.1461 0.1705 0.1476 -0.0066 0.0003  -0.0032 115 GLY   A O     
939  N  N     . ASN   A 119 ? 0.1405 0.1631 0.1371 -0.0101 -0.0011 -0.0041 116 ASN   A N     
940  C  CA    . ASN   A 119 ? 0.1434 0.1666 0.1407 -0.0146 -0.0004 -0.0057 116 ASN   A CA    
941  C  C     . ASN   A 119 ? 0.1557 0.1893 0.1572 -0.0165 -0.0012 -0.0075 116 ASN   A C     
942  O  O     . ASN   A 119 ? 0.1544 0.1946 0.1575 -0.0141 -0.0032 -0.0080 116 ASN   A O     
943  C  CB    . ASN   A 119 ? 0.1613 0.1763 0.1549 -0.0173 -0.0005 -0.0065 116 ASN   A CB    
944  C  CG    . ASN   A 119 ? 0.1724 0.1847 0.1662 -0.0225 0.0004  -0.0064 116 ASN   A CG    
945  O  OD1   . ASN   A 119 ? 0.1633 0.1763 0.1572 -0.0232 0.0021  -0.0045 116 ASN   A OD1   
946  N  ND2   . ASN   A 119 ? 0.1704 0.1798 0.1638 -0.0264 -0.0007 -0.0084 116 ASN   A ND2   
947  N  N     . LYS   A 120 ? 0.1422 0.1779 0.1454 -0.0213 0.0002  -0.0081 117 LYS   A N     
948  C  CA    . LYS   A 120 ? 0.1546 0.2020 0.1632 -0.0244 0.0000  -0.0100 117 LYS   A CA    
949  C  C     . LYS   A 120 ? 0.1488 0.2065 0.1624 -0.0199 0.0004  -0.0104 117 LYS   A C     
950  O  O     . LYS   A 120 ? 0.1499 0.2193 0.1688 -0.0191 -0.0010 -0.0122 117 LYS   A O     
951  C  CB    . LYS   A 120 ? 0.1532 0.2046 0.1628 -0.0263 -0.0029 -0.0128 117 LYS   A CB    
952  C  CG    . LYS   A 120 ? 0.1634 0.2037 0.1684 -0.0293 -0.0037 -0.0138 117 LYS   A CG    
953  C  CD    . LYS   A 120 ? 0.1622 0.2071 0.1688 -0.0328 -0.0065 -0.0181 117 LYS   A CD    
954  C  CE    . LYS   A 120 ? 0.1870 0.2203 0.1889 -0.0344 -0.0077 -0.0206 117 LYS   A CE    
955  N  NZ    . LYS   A 120 ? 0.2013 0.2387 0.2054 -0.0390 -0.0106 -0.0262 117 LYS   A NZ    
956  N  N     . SER   A 121 ? 0.1518 0.2058 0.1641 -0.0169 0.0023  -0.0092 118 SER   A N     
957  C  CA    . SER   A 121 ? 0.1581 0.2198 0.1753 -0.0119 0.0026  -0.0104 118 SER   A CA    
958  C  C     . SER   A 121 ? 0.1574 0.2333 0.1803 -0.0144 0.0045  -0.0128 118 SER   A C     
959  O  O     . SER   A 121 ? 0.1946 0.2796 0.2230 -0.0097 0.0044  -0.0149 118 SER   A O     
960  C  CB    . SER   A 121 ? 0.1678 0.2223 0.1825 -0.0088 0.0040  -0.0100 118 SER   A CB    
961  O  OG    . SER   A 121 ? 0.1787 0.2335 0.1906 -0.0130 0.0069  -0.0100 118 SER   A OG    
962  N  N     . ASP   A 122 ? 0.1488 0.2263 0.1707 -0.0218 0.0062  -0.0123 119 ASP   A N     
963  C  CA    . ASP   A 122 ? 0.1639 0.2561 0.1916 -0.0262 0.0086  -0.0139 119 ASP   A CA    
964  C  C     . ASP   A 122 ? 0.1684 0.2725 0.2033 -0.0269 0.0060  -0.0164 119 ASP   A C     
965  O  O     . ASP   A 122 ? 0.1829 0.3027 0.2250 -0.0296 0.0076  -0.0185 119 ASP   A O     
966  C  CB    . ASP   A 122 ? 0.1821 0.2700 0.2061 -0.0349 0.0113  -0.0112 119 ASP   A CB    
967  C  CG    . ASP   A 122 ? 0.1883 0.2657 0.2097 -0.0396 0.0089  -0.0102 119 ASP   A CG    
968  O  OD1   . ASP   A 122 ? 0.1770 0.2402 0.1924 -0.0368 0.0071  -0.0089 119 ASP   A OD1   
969  O  OD2   . ASP   A 122 ? 0.2059 0.2897 0.2321 -0.0458 0.0083  -0.0115 119 ASP   A OD2   
970  N  N     . LEU   A 123 ? 0.1578 0.2566 0.1911 -0.0248 0.0021  -0.0164 120 LEU   A N     
971  C  CA    . LEU   A 123 ? 0.1636 0.2750 0.2031 -0.0254 -0.0011 -0.0191 120 LEU   A CA    
972  C  C     . LEU   A 123 ? 0.1580 0.2796 0.2029 -0.0165 -0.0032 -0.0202 120 LEU   A C     
973  O  O     . LEU   A 123 ? 0.1538 0.2668 0.1952 -0.0097 -0.0044 -0.0183 120 LEU   A O     
974  C  CB    . LEU   A 123 ? 0.1662 0.2692 0.2007 -0.0267 -0.0046 -0.0192 120 LEU   A CB    
975  C  CG    . LEU   A 123 ? 0.1936 0.2868 0.2246 -0.0352 -0.0034 -0.0192 120 LEU   A CG    
976  C  CD1   . LEU   A 123 ? 0.2066 0.2922 0.2327 -0.0352 -0.0069 -0.0208 120 LEU   A CD1   
977  C  CD2   . LEU   A 123 ? 0.2028 0.3071 0.2411 -0.0438 -0.0019 -0.0211 120 LEU   A CD2   
978  N  N     . PRO   A 124 ? 0.1426 0.2827 0.1969 -0.0166 -0.0037 -0.0233 121 PRO   A N     
979  C  CA    . PRO   A 124 ? 0.1410 0.2909 0.2015 -0.0069 -0.0057 -0.0246 121 PRO   A CA    
980  C  C     . PRO   A 124 ? 0.1571 0.3065 0.2165 -0.0007 -0.0116 -0.0233 121 PRO   A C     
981  O  O     . PRO   A 124 ? 0.1788 0.3275 0.2399 0.0083  -0.0135 -0.0221 121 PRO   A O     
982  C  CB    . PRO   A 124 ? 0.1372 0.3090 0.2087 -0.0095 -0.0043 -0.0287 121 PRO   A CB    
983  C  CG    . PRO   A 124 ? 0.1445 0.3186 0.2159 -0.0208 -0.0037 -0.0292 121 PRO   A CG    
984  C  CD    . PRO   A 124 ? 0.1423 0.2953 0.2028 -0.0255 -0.0019 -0.0258 121 PRO   A CD    
985  N  N     . SER   A 125 ? 0.1422 0.2918 0.1987 -0.0052 -0.0144 -0.0234 122 SER   A N     
986  C  CA    . SER   A 125 ? 0.1546 0.3061 0.2087 0.0005  -0.0201 -0.0220 122 SER   A CA    
987  C  C     . SER   A 125 ? 0.1584 0.2914 0.2015 0.0032  -0.0205 -0.0173 122 SER   A C     
988  O  O     . SER   A 125 ? 0.1782 0.3077 0.2151 0.0003  -0.0222 -0.0172 122 SER   A O     
989  C  CB    . SER   A 125 ? 0.1610 0.3247 0.2176 -0.0047 -0.0235 -0.0256 122 SER   A CB    
990  O  OG    . SER   A 125 ? 0.1745 0.3584 0.2430 -0.0055 -0.0239 -0.0295 122 SER   A OG    
991  N  N     . ARG   A 126 ? 0.1676 0.2910 0.2094 0.0090  -0.0190 -0.0140 123 ARG   A N     
992  C  CA    . ARG   A 126 ? 0.1710 0.2781 0.2039 0.0114  -0.0189 -0.0091 123 ARG   A CA    
993  C  C     . ARG   A 126 ? 0.1727 0.2823 0.2016 0.0162  -0.0237 -0.0055 123 ARG   A C     
994  O  O     . ARG   A 126 ? 0.1776 0.2976 0.2116 0.0217  -0.0273 -0.0051 123 ARG   A O     
995  C  CB    . ARG   A 126 ? 0.1775 0.2768 0.2129 0.0167  -0.0170 -0.0074 123 ARG   A CB    
996  C  CG    . ARG   A 126 ? 0.1839 0.2673 0.2127 0.0191  -0.0167 -0.0023 123 ARG   A CG    
997  C  CD    . ARG   A 126 ? 0.1799 0.2570 0.2132 0.0243  -0.0157 -0.0020 123 ARG   A CD    
998  N  NE    . ARG   A 126 ? 0.1885 0.2636 0.2230 0.0205  -0.0116 -0.0060 123 ARG   A NE    
999  C  CZ    . ARG   A 126 ? 0.1879 0.2516 0.2171 0.0167  -0.0090 -0.0051 123 ARG   A CZ    
1000 N  NH1   . ARG   A 126 ? 0.2080 0.2621 0.2311 0.0158  -0.0096 -0.0009 123 ARG   A NH1   
1001 N  NH2   . ARG   A 126 ? 0.1816 0.2451 0.2115 0.0139  -0.0058 -0.0085 123 ARG   A NH2   
1002 N  N     . THR   A 127 ? 0.1725 0.2731 0.1922 0.0143  -0.0236 -0.0028 124 THR   A N     
1003 C  CA    . THR   A 127 ? 0.1813 0.2835 0.1949 0.0188  -0.0274 0.0018  124 THR   A CA    
1004 C  C     . THR   A 127 ? 0.1858 0.2733 0.1939 0.0216  -0.0255 0.0084  124 THR   A C     
1005 O  O     . THR   A 127 ? 0.2013 0.2888 0.2051 0.0259  -0.0281 0.0141  124 THR   A O     
1006 C  CB    . THR   A 127 ? 0.1907 0.2993 0.1984 0.0144  -0.0293 -0.0014 124 THR   A CB    
1007 O  OG1   . THR   A 127 ? 0.1941 0.2920 0.1964 0.0089  -0.0255 -0.0031 124 THR   A OG1   
1008 C  CG2   . THR   A 127 ? 0.2023 0.3263 0.2168 0.0113  -0.0318 -0.0079 124 THR   A CG2   
1009 N  N     . VAL   A 128 ? 0.1744 0.2504 0.1825 0.0184  -0.0212 0.0078  125 VAL   A N     
1010 C  CA    . VAL   A 128 ? 0.1928 0.2556 0.1972 0.0201  -0.0193 0.0135  125 VAL   A CA    
1011 C  C     . VAL   A 128 ? 0.1871 0.2433 0.1986 0.0232  -0.0182 0.0137  125 VAL   A C     
1012 O  O     . VAL   A 128 ? 0.1827 0.2371 0.1977 0.0205  -0.0155 0.0091  125 VAL   A O     
1013 C  CB    . VAL   A 128 ? 0.1911 0.2463 0.1901 0.0145  -0.0156 0.0122  125 VAL   A CB    
1014 C  CG1   . VAL   A 128 ? 0.1987 0.2428 0.1950 0.0155  -0.0136 0.0180  125 VAL   A CG1   
1015 C  CG2   . VAL   A 128 ? 0.1929 0.2545 0.1853 0.0118  -0.0166 0.0102  125 VAL   A CG2   
1016 N  N     . ASP   A 129 ? 0.2274 0.2792 0.2403 0.0291  -0.0204 0.0192  126 ASP   A N     
1017 C  CA    . ASP   A 129 ? 0.2505 0.2948 0.2705 0.0330  -0.0201 0.0187  126 ASP   A CA    
1018 C  C     . ASP   A 129 ? 0.2511 0.2833 0.2700 0.0289  -0.0162 0.0181  126 ASP   A C     
1019 O  O     . ASP   A 129 ? 0.2087 0.2343 0.2221 0.0260  -0.0149 0.0224  126 ASP   A O     
1020 C  CB    . ASP   A 129 ? 0.2868 0.3260 0.3080 0.0399  -0.0237 0.0259  126 ASP   A CB    
1021 C  CG    . ASP   A 129 ? 0.3520 0.3858 0.3824 0.0460  -0.0248 0.0239  126 ASP   A CG    
1022 O  OD1   . ASP   A 129 ? 0.3816 0.4084 0.4153 0.0441  -0.0219 0.0194  126 ASP   A OD1   
1023 O  OD2   . ASP   A 129 ? 0.4861 0.5229 0.5203 0.0534  -0.0290 0.0266  126 ASP   A OD2   
1024 N  N     . THR   A 130 ? 0.2648 0.2956 0.2891 0.0288  -0.0144 0.0125  127 THR   A N     
1025 C  CA    . THR   A 130 ? 0.2747 0.2948 0.2983 0.0254  -0.0115 0.0114  127 THR   A CA    
1026 C  C     . THR   A 130 ? 0.2630 0.2704 0.2868 0.0270  -0.0122 0.0174  127 THR   A C     
1027 O  O     . THR   A 130 ? 0.2656 0.2660 0.2866 0.0227  -0.0101 0.0190  127 THR   A O     
1028 C  CB    . THR   A 130 ? 0.3166 0.3386 0.3457 0.0262  -0.0100 0.0043  127 THR   A CB    
1029 O  OG1   . THR   A 130 ? 0.3545 0.3889 0.3833 0.0237  -0.0090 0.0002  127 THR   A OG1   
1030 C  CG2   . THR   A 130 ? 0.3569 0.3710 0.3842 0.0223  -0.0075 0.0023  127 THR   A CG2   
1031 N  N     . LYS   A 131 ? 0.2625 0.2670 0.2898 0.0330  -0.0154 0.0212  128 LYS   A N     
1032 C  CA    . LYS   A 131 ? 0.3133 0.3044 0.3410 0.0341  -0.0163 0.0285  128 LYS   A CA    
1033 C  C     . LYS   A 131 ? 0.2722 0.2622 0.2920 0.0297  -0.0150 0.0360  128 LYS   A C     
1034 O  O     . LYS   A 131 ? 0.2917 0.2719 0.3113 0.0263  -0.0132 0.0399  128 LYS   A O     
1035 C  CB    . LYS   A 131 ? 0.3751 0.3638 0.4071 0.0420  -0.0206 0.0324  128 LYS   A CB    
1036 C  CG    . LYS   A 131 ? 0.4567 0.4449 0.4979 0.0478  -0.0220 0.0250  128 LYS   A CG    
1037 C  CD    . LYS   A 131 ? 0.5159 0.4909 0.5615 0.0458  -0.0202 0.0211  128 LYS   A CD    
1038 C  CE    . LYS   A 131 ? 0.4910 0.4726 0.5361 0.0412  -0.0167 0.0121  128 LYS   A CE    
1039 N  NZ    . LYS   A 131 ? 0.5397 0.5088 0.5883 0.0391  -0.0157 0.0088  128 LYS   A NZ    
1040 N  N     . GLN   A 132 ? 0.2489 0.2502 0.2628 0.0296  -0.0158 0.0373  129 GLN   A N     
1041 C  CA    . GLN   A 132 ? 0.2508 0.2541 0.2563 0.0262  -0.0145 0.0434  129 GLN   A CA    
1042 C  C     . GLN   A 132 ? 0.2214 0.2242 0.2246 0.0198  -0.0104 0.0396  129 GLN   A C     
1043 O  O     . GLN   A 132 ? 0.2089 0.2078 0.2090 0.0164  -0.0080 0.0442  129 GLN   A O     
1044 C  CB    . GLN   A 132 ? 0.2781 0.2950 0.2778 0.0280  -0.0169 0.0436  129 GLN   A CB    
1045 C  CG    . GLN   A 132 ? 0.3381 0.3567 0.3380 0.0347  -0.0215 0.0499  129 GLN   A CG    
1046 C  CD    . GLN   A 132 ? 0.4116 0.4443 0.4038 0.0356  -0.0240 0.0514  129 GLN   A CD    
1047 O  OE1   . GLN   A 132 ? 0.5125 0.5522 0.4990 0.0310  -0.0220 0.0475  129 GLN   A OE1   
1048 N  NE2   . GLN   A 132 ? 0.4573 0.4937 0.4491 0.0419  -0.0287 0.0567  129 GLN   A NE2   
1049 N  N     . ALA   A 133 ? 0.1943 0.2013 0.1995 0.0182  -0.0094 0.0314  130 ALA   A N     
1050 C  CA    . ALA   A 133 ? 0.1869 0.1930 0.1902 0.0131  -0.0061 0.0278  130 ALA   A CA    
1051 C  C     . ALA   A 133 ? 0.1681 0.1640 0.1758 0.0112  -0.0044 0.0284  130 ALA   A C     
1052 O  O     . ALA   A 133 ? 0.1735 0.1679 0.1795 0.0074  -0.0020 0.0298  130 ALA   A O     
1053 C  CB    . ALA   A 133 ? 0.1887 0.2005 0.1930 0.0119  -0.0059 0.0202  130 ALA   A CB    
1054 N  N     . GLN   A 134 ? 0.1707 0.1605 0.1849 0.0139  -0.0058 0.0268  131 GLN   A N     
1055 C  CA    . GLN   A 134 ? 0.1818 0.1613 0.2011 0.0121  -0.0050 0.0269  131 GLN   A CA    
1056 C  C     . GLN   A 134 ? 0.1882 0.1618 0.2065 0.0101  -0.0043 0.0356  131 GLN   A C     
1057 O  O     . GLN   A 134 ? 0.2091 0.1787 0.2293 0.0057  -0.0022 0.0362  131 GLN   A O     
1058 C  CB    . GLN   A 134 ? 0.1907 0.1643 0.2171 0.0162  -0.0071 0.0231  131 GLN   A CB    
1059 C  CG    . GLN   A 134 ? 0.1832 0.1629 0.2109 0.0169  -0.0067 0.0142  131 GLN   A CG    
1060 C  CD    . GLN   A 134 ? 0.2010 0.1761 0.2357 0.0214  -0.0084 0.0093  131 GLN   A CD    
1061 O  OE1   . GLN   A 134 ? 0.2331 0.2020 0.2717 0.0258  -0.0107 0.0123  131 GLN   A OE1   
1062 N  NE2   . GLN   A 134 ? 0.2025 0.1805 0.2385 0.0207  -0.0073 0.0015  131 GLN   A NE2   
1063 N  N     . ASP   A 135 ? 0.2109 0.1845 0.2265 0.0133  -0.0061 0.0426  132 ASP   A N     
1064 C  CA    . ASP   A 135 ? 0.2232 0.1918 0.2368 0.0112  -0.0052 0.0524  132 ASP   A CA    
1065 C  C     . ASP   A 135 ? 0.2110 0.1878 0.2184 0.0062  -0.0015 0.0539  132 ASP   A C     
1066 O  O     . ASP   A 135 ? 0.2085 0.1818 0.2171 0.0017  0.0011  0.0583  132 ASP   A O     
1067 C  CB    . ASP   A 135 ? 0.2526 0.2216 0.2627 0.0163  -0.0083 0.0601  132 ASP   A CB    
1068 C  CG    . ASP   A 135 ? 0.3057 0.2707 0.3118 0.0137  -0.0071 0.0717  132 ASP   A CG    
1069 O  OD1   . ASP   A 135 ? 0.3454 0.2984 0.3569 0.0105  -0.0060 0.0757  132 ASP   A OD1   
1070 O  OD2   . ASP   A 135 ? 0.3189 0.2933 0.3162 0.0146  -0.0071 0.0770  132 ASP   A OD2   
1071 N  N     . LEU   A 136 ? 0.1967 0.1845 0.1982 0.0069  -0.0013 0.0498  133 LEU   A N     
1072 C  CA    . LEU   A 136 ? 0.1997 0.1955 0.1956 0.0033  0.0020  0.0497  133 LEU   A CA    
1073 C  C     . LEU   A 136 ? 0.1954 0.1886 0.1963 -0.0009 0.0046  0.0451  133 LEU   A C     
1074 O  O     . LEU   A 136 ? 0.1848 0.1798 0.1858 -0.0047 0.0077  0.0482  133 LEU   A O     
1075 C  CB    . LEU   A 136 ? 0.2024 0.2087 0.1922 0.0050  0.0011  0.0445  133 LEU   A CB    
1076 C  CG    . LEU   A 136 ? 0.2203 0.2350 0.2041 0.0025  0.0041  0.0433  133 LEU   A CG    
1077 C  CD1   . LEU   A 136 ? 0.2262 0.2455 0.2036 0.0023  0.0054  0.0520  133 LEU   A CD1   
1078 C  CD2   . LEU   A 136 ? 0.2203 0.2421 0.2003 0.0035  0.0029  0.0358  133 LEU   A CD2   
1079 N  N     . ALA   A 137 ? 0.1859 0.1763 0.1914 -0.0002 0.0034  0.0379  134 ALA   A N     
1080 C  CA    . ALA   A 137 ? 0.1687 0.1579 0.1783 -0.0035 0.0051  0.0333  134 ALA   A CA    
1081 C  C     . ALA   A 137 ? 0.1895 0.1713 0.2057 -0.0068 0.0061  0.0374  134 ALA   A C     
1082 O  O     . ALA   A 137 ? 0.2061 0.1901 0.2249 -0.0108 0.0084  0.0371  134 ALA   A O     
1083 C  CB    . ALA   A 137 ? 0.1679 0.1556 0.1802 -0.0019 0.0034  0.0257  134 ALA   A CB    
1084 N  N     . ARG   A 138 ? 0.1996 0.1723 0.2191 -0.0052 0.0041  0.0411  135 ARG   A N     
1085 C  CA    . ARG   A 138 ? 0.2225 0.1858 0.2490 -0.0089 0.0045  0.0453  135 ARG   A CA    
1086 C  C     . ARG   A 138 ? 0.2275 0.1950 0.2513 -0.0132 0.0080  0.0538  135 ARG   A C     
1087 O  O     . ARG   A 138 ? 0.2227 0.1897 0.2518 -0.0188 0.0103  0.0549  135 ARG   A O     
1088 C  CB    . ARG   A 138 ? 0.2654 0.2171 0.2955 -0.0052 0.0013  0.0481  135 ARG   A CB    
1089 C  CG    . ARG   A 138 ? 0.3544 0.2929 0.3939 -0.0083 0.0005  0.0487  135 ARG   A CG    
1090 C  CD    . ARG   A 138 ? 0.3834 0.3118 0.4276 -0.0024 -0.0035 0.0446  135 ARG   A CD    
1091 N  NE    . ARG   A 138 ? 0.4401 0.3700 0.4794 0.0040  -0.0056 0.0491  135 ARG   A NE    
1092 C  CZ    . ARG   A 138 ? 0.4411 0.3754 0.4796 0.0103  -0.0079 0.0432  135 ARG   A CZ    
1093 N  NH1   . ARG   A 138 ? 0.5000 0.4368 0.5349 0.0156  -0.0100 0.0483  135 ARG   A NH1   
1094 N  NH2   . ARG   A 138 ? 0.4593 0.3966 0.5007 0.0113  -0.0081 0.0327  135 ARG   A NH2   
1095 N  N     . SER   A 139 ? 0.2219 0.1955 0.2372 -0.0109 0.0084  0.0594  136 SER   A N     
1096 C  CA    . SER   A 139 ? 0.2382 0.2182 0.2492 -0.0146 0.0121  0.0677  136 SER   A CA    
1097 C  C     . SER   A 139 ? 0.2435 0.2347 0.2546 -0.0182 0.0160  0.0632  136 SER   A C     
1098 O  O     . SER   A 139 ? 0.2472 0.2429 0.2595 -0.0232 0.0198  0.0685  136 SER   A O     
1099 C  CB    . SER   A 139 ? 0.2601 0.2459 0.2607 -0.0108 0.0113  0.0739  136 SER   A CB    
1100 O  OG    . SER   A 139 ? 0.2800 0.2773 0.2743 -0.0081 0.0113  0.0671  136 SER   A OG    
1101 N  N     . TYR   A 140 ? 0.2129 0.2088 0.2231 -0.0157 0.0150  0.0537  137 TYR   A N     
1102 C  CA    . TYR   A 140 ? 0.2154 0.2210 0.2264 -0.0175 0.0176  0.0482  137 TYR   A CA    
1103 C  C     . TYR   A 140 ? 0.2078 0.2102 0.2286 -0.0207 0.0175  0.0436  137 TYR   A C     
1104 O  O     . TYR   A 140 ? 0.2517 0.2622 0.2750 -0.0226 0.0198  0.0405  137 TYR   A O     
1105 C  CB    . TYR   A 140 ? 0.2148 0.2256 0.2202 -0.0132 0.0161  0.0409  137 TYR   A CB    
1106 C  CG    . TYR   A 140 ? 0.2447 0.2620 0.2405 -0.0103 0.0161  0.0429  137 TYR   A CG    
1107 C  CD1   . TYR   A 140 ? 0.2550 0.2777 0.2457 -0.0114 0.0185  0.0506  137 TYR   A CD1   
1108 C  CD2   . TYR   A 140 ? 0.2351 0.2539 0.2267 -0.0069 0.0138  0.0367  137 TYR   A CD2   
1109 C  CE1   . TYR   A 140 ? 0.2695 0.2998 0.2505 -0.0084 0.0179  0.0512  137 TYR   A CE1   
1110 C  CE2   . TYR   A 140 ? 0.2467 0.2721 0.2303 -0.0045 0.0132  0.0370  137 TYR   A CE2   
1111 C  CZ    . TYR   A 140 ? 0.2605 0.2921 0.2385 -0.0050 0.0150  0.0437  137 TYR   A CZ    
1112 O  OH    . TYR   A 140 ? 0.2935 0.3329 0.2628 -0.0024 0.0139  0.0430  137 TYR   A OH    
1113 N  N     . GLY   A 141 ? 0.2061 0.1973 0.2324 -0.0209 0.0147  0.0427  138 GLY   A N     
1114 C  CA    . GLY   A 141 ? 0.1942 0.1824 0.2290 -0.0233 0.0136  0.0368  138 GLY   A CA    
1115 C  C     . GLY   A 141 ? 0.1907 0.1831 0.2242 -0.0204 0.0120  0.0280  138 GLY   A C     
1116 O  O     . GLY   A 141 ? 0.2108 0.2071 0.2495 -0.0224 0.0120  0.0236  138 GLY   A O     
1117 N  N     . ILE   A 142 ? 0.1720 0.1639 0.1989 -0.0158 0.0103  0.0259  139 ILE   A N     
1118 C  CA    . ILE   A 142 ? 0.1666 0.1615 0.1910 -0.0132 0.0088  0.0189  139 ILE   A CA    
1119 C  C     . ILE   A 142 ? 0.1611 0.1503 0.1846 -0.0103 0.0061  0.0156  139 ILE   A C     
1120 O  O     . ILE   A 142 ? 0.1645 0.1488 0.1877 -0.0088 0.0052  0.0186  139 ILE   A O     
1121 C  CB    . ILE   A 142 ? 0.1730 0.1750 0.1903 -0.0110 0.0101  0.0186  139 ILE   A CB    
1122 C  CG1   . ILE   A 142 ? 0.1726 0.1739 0.1837 -0.0086 0.0095  0.0213  139 ILE   A CG1   
1123 C  CG2   . ILE   A 142 ? 0.1710 0.1809 0.1895 -0.0133 0.0133  0.0209  139 ILE   A CG2   
1124 C  CD1   . ILE   A 142 ? 0.1788 0.1868 0.1832 -0.0068 0.0102  0.0197  139 ILE   A CD1   
1125 N  N     . PRO   A 143 ? 0.1580 0.1484 0.1810 -0.0092 0.0047  0.0097  140 PRO   A N     
1126 C  CA    . PRO   A 143 ? 0.1458 0.1337 0.1670 -0.0066 0.0028  0.0063  140 PRO   A CA    
1127 C  C     . PRO   A 143 ? 0.1449 0.1353 0.1603 -0.0043 0.0030  0.0078  140 PRO   A C     
1128 O  O     . PRO   A 143 ? 0.1649 0.1592 0.1763 -0.0045 0.0041  0.0095  140 PRO   A O     
1129 C  CB    . PRO   A 143 ? 0.1572 0.1478 0.1777 -0.0067 0.0018  0.0011  140 PRO   A CB    
1130 C  CG    . PRO   A 143 ? 0.1636 0.1564 0.1883 -0.0091 0.0022  0.0009  140 PRO   A CG    
1131 C  CD    . PRO   A 143 ? 0.1524 0.1472 0.1769 -0.0103 0.0046  0.0061  140 PRO   A CD    
1132 N  N     . PHE   A 144 ? 0.1328 0.1216 0.1486 -0.0021 0.0017  0.0064  141 PHE   A N     
1133 C  CA    . PHE   A 144 ? 0.1418 0.1344 0.1537 -0.0001 0.0014  0.0066  141 PHE   A CA    
1134 C  C     . PHE   A 144 ? 0.1426 0.1373 0.1544 0.0007  0.0008  0.0017  141 PHE   A C     
1135 O  O     . PHE   A 144 ? 0.1512 0.1437 0.1666 0.0021  0.0001  -0.0011 141 PHE   A O     
1136 C  CB    . PHE   A 144 ? 0.1474 0.1385 0.1609 0.0023  0.0003  0.0103  141 PHE   A CB    
1137 C  CG    . PHE   A 144 ? 0.1561 0.1531 0.1672 0.0045  -0.0006 0.0095  141 PHE   A CG    
1138 C  CD1   . PHE   A 144 ? 0.1569 0.1593 0.1630 0.0030  -0.0001 0.0093  141 PHE   A CD1   
1139 C  CD2   . PHE   A 144 ? 0.1744 0.1721 0.1891 0.0079  -0.0021 0.0081  141 PHE   A CD2   
1140 C  CE1   . PHE   A 144 ? 0.1589 0.1675 0.1638 0.0040  -0.0012 0.0080  141 PHE   A CE1   
1141 C  CE2   . PHE   A 144 ? 0.1719 0.1771 0.1856 0.0095  -0.0030 0.0071  141 PHE   A CE2   
1142 C  CZ    . PHE   A 144 ? 0.1511 0.1619 0.1601 0.0071  -0.0026 0.0071  141 PHE   A CZ    
1143 N  N     . ILE   A 145 ? 0.1423 0.1412 0.1498 -0.0002 0.0012  0.0007  142 ILE   A N     
1144 C  CA    . ILE   A 145 ? 0.1431 0.1456 0.1494 -0.0004 0.0014  -0.0026 142 ILE   A CA    
1145 C  C     . ILE   A 145 ? 0.1401 0.1478 0.1445 -0.0010 0.0015  -0.0021 142 ILE   A C     
1146 O  O     . ILE   A 145 ? 0.1466 0.1542 0.1482 -0.0023 0.0015  -0.0005 142 ILE   A O     
1147 C  CB    . ILE   A 145 ? 0.1350 0.1364 0.1380 -0.0024 0.0018  -0.0038 142 ILE   A CB    
1148 C  CG1   . ILE   A 145 ? 0.1438 0.1424 0.1496 -0.0020 0.0012  -0.0055 142 ILE   A CG1   
1149 C  CG2   . ILE   A 145 ? 0.1332 0.1387 0.1333 -0.0035 0.0024  -0.0055 142 ILE   A CG2   
1150 C  CD1   . ILE   A 145 ? 0.1413 0.1397 0.1445 -0.0032 0.0007  -0.0061 142 ILE   A CD1   
1151 N  N     . GLU   A 146 ? 0.1404 0.1535 0.1469 0.0000  0.0017  -0.0042 143 GLU   A N     
1152 C  CA    . GLU   A 146 ? 0.1323 0.1521 0.1381 -0.0017 0.0018  -0.0044 143 GLU   A CA    
1153 C  C     . GLU   A 146 ? 0.1540 0.1755 0.1569 -0.0053 0.0034  -0.0057 143 GLU   A C     
1154 O  O     . GLU   A 146 ? 0.1441 0.1673 0.1473 -0.0047 0.0044  -0.0075 143 GLU   A O     
1155 C  CB    . GLU   A 146 ? 0.1542 0.1812 0.1649 0.0014  0.0010  -0.0057 143 GLU   A CB    
1156 C  CG    . GLU   A 146 ? 0.1648 0.1901 0.1769 0.0046  -0.0010 -0.0028 143 GLU   A CG    
1157 C  CD    . GLU   A 146 ? 0.2249 0.2584 0.2415 0.0082  -0.0027 -0.0033 143 GLU   A CD    
1158 O  OE1   . GLU   A 146 ? 0.2497 0.2915 0.2695 0.0080  -0.0020 -0.0065 143 GLU   A OE1   
1159 O  OE2   . GLU   A 146 ? 0.1957 0.2282 0.2126 0.0110  -0.0048 -0.0001 143 GLU   A OE2   
1160 N  N     . THR   A 147 ? 0.1365 0.1576 0.1367 -0.0089 0.0035  -0.0046 144 THR   A N     
1161 C  CA    . THR   A 147 ? 0.1481 0.1690 0.1452 -0.0129 0.0048  -0.0042 144 THR   A CA    
1162 C  C     . THR   A 147 ? 0.1612 0.1879 0.1596 -0.0170 0.0053  -0.0044 144 THR   A C     
1163 O  O     . THR   A 147 ? 0.1473 0.1780 0.1486 -0.0166 0.0041  -0.0054 144 THR   A O     
1164 C  CB    . THR   A 147 ? 0.1634 0.1751 0.1562 -0.0144 0.0041  -0.0024 144 THR   A CB    
1165 O  OG1   . THR   A 147 ? 0.1502 0.1605 0.1433 -0.0147 0.0028  -0.0028 144 THR   A OG1   
1166 C  CG2   . THR   A 147 ? 0.1651 0.1718 0.1567 -0.0114 0.0035  -0.0022 144 THR   A CG2   
1167 N  N     . SER   A 148 ? 0.1477 0.1759 0.1442 -0.0211 0.0071  -0.0034 145 SER   A N     
1168 C  CA    . SER   A 148 ? 0.1639 0.1960 0.1619 -0.0270 0.0078  -0.0029 145 SER   A CA    
1169 C  C     . SER   A 148 ? 0.1714 0.1938 0.1641 -0.0313 0.0083  0.0005  145 SER   A C     
1170 O  O     . SER   A 148 ? 0.1816 0.2039 0.1708 -0.0320 0.0099  0.0028  145 SER   A O     
1171 C  CB    . SER   A 148 ? 0.1744 0.2201 0.1767 -0.0286 0.0101  -0.0042 145 SER   A CB    
1172 O  OG    . SER   A 148 ? 0.1893 0.2387 0.1937 -0.0355 0.0109  -0.0035 145 SER   A OG    
1173 N  N     . ALA   A 149 ? 0.1764 0.1902 0.1683 -0.0332 0.0064  0.0005  146 ALA   A N     
1174 C  CA    . ALA   A 149 ? 0.1992 0.2023 0.1872 -0.0375 0.0063  0.0038  146 ALA   A CA    
1175 C  C     . ALA   A 149 ? 0.2303 0.2382 0.2194 -0.0449 0.0087  0.0064  146 ALA   A C     
1176 O  O     . ALA   A 149 ? 0.2617 0.2626 0.2465 -0.0483 0.0095  0.0112  146 ALA   A O     
1177 C  CB    . ALA   A 149 ? 0.2143 0.2081 0.2025 -0.0378 0.0036  0.0016  146 ALA   A CB    
1178 N  N     . LYS   A 150 ? 0.2085 0.2292 0.2036 -0.0473 0.0097  0.0038  147 LYS   A N     
1179 C  CA    . LYS   A 150 ? 0.2504 0.2781 0.2483 -0.0552 0.0123  0.0058  147 LYS   A CA    
1180 C  C     . LYS   A 150 ? 0.2791 0.3143 0.2738 -0.0552 0.0160  0.0090  147 LYS   A C     
1181 O  O     . LYS   A 150 ? 0.3155 0.3485 0.3070 -0.0614 0.0182  0.0141  147 LYS   A O     
1182 C  CB    . LYS   A 150 ? 0.2473 0.2891 0.2536 -0.0572 0.0121  0.0013  147 LYS   A CB    
1183 C  CG    . LYS   A 150 ? 0.2894 0.3401 0.3006 -0.0668 0.0149  0.0030  147 LYS   A CG    
1184 C  CD    . LYS   A 150 ? 0.3096 0.3753 0.3302 -0.0683 0.0137  -0.0023 147 LYS   A CD    
1185 C  CE    . LYS   A 150 ? 0.3686 0.4431 0.3955 -0.0792 0.0161  -0.0012 147 LYS   A CE    
1186 N  NZ    . LYS   A 150 ? 0.4166 0.5022 0.4526 -0.0807 0.0132  -0.0073 147 LYS   A NZ    
1187 N  N     . THR   A 151 ? 0.2655 0.3086 0.2604 -0.0485 0.0164  0.0062  148 THR   A N     
1188 C  CA    . THR   A 151 ? 0.2649 0.3165 0.2563 -0.0476 0.0197  0.0076  148 THR   A CA    
1189 C  C     . THR   A 151 ? 0.2548 0.2970 0.2381 -0.0431 0.0187  0.0097  148 THR   A C     
1190 O  O     . THR   A 151 ? 0.2721 0.3211 0.2510 -0.0426 0.0210  0.0108  148 THR   A O     
1191 C  CB    . THR   A 151 ? 0.2558 0.3226 0.2529 -0.0426 0.0209  0.0021  148 THR   A CB    
1192 O  OG1   . THR   A 151 ? 0.2690 0.3296 0.2659 -0.0347 0.0179  -0.0010 148 THR   A OG1   
1193 C  CG2   . THR   A 151 ? 0.2765 0.3545 0.2826 -0.0455 0.0212  -0.0006 148 THR   A CG2   
1194 N  N     . ARG   A 152 ? 0.2314 0.2603 0.2131 -0.0398 0.0151  0.0096  149 ARG   A N     
1195 C  CA    . ARG   A 152 ? 0.2500 0.2707 0.2260 -0.0351 0.0133  0.0107  149 ARG   A CA    
1196 C  C     . ARG   A 152 ? 0.2500 0.2763 0.2279 -0.0285 0.0127  0.0058  149 ARG   A C     
1197 O  O     . ARG   A 152 ? 0.2984 0.3199 0.2727 -0.0247 0.0111  0.0057  149 ARG   A O     
1198 C  CB    . ARG   A 152 ? 0.2711 0.2892 0.2390 -0.0381 0.0145  0.0167  149 ARG   A CB    
1199 C  CG    . ARG   A 152 ? 0.3155 0.3191 0.2787 -0.0360 0.0112  0.0200  149 ARG   A CG    
1200 C  CD    . ARG   A 152 ? 0.3200 0.3193 0.2747 -0.0387 0.0115  0.0274  149 ARG   A CD    
1201 N  NE    . ARG   A 152 ? 0.3356 0.3215 0.2872 -0.0348 0.0075  0.0295  149 ARG   A NE    
1202 C  CZ    . ARG   A 152 ? 0.4003 0.3870 0.3485 -0.0291 0.0054  0.0287  149 ARG   A CZ    
1203 N  NH1   . ARG   A 152 ? 0.4279 0.4266 0.3749 -0.0270 0.0067  0.0253  149 ARG   A NH1   
1204 N  NH2   . ARG   A 152 ? 0.4682 0.4442 0.4148 -0.0254 0.0017  0.0305  149 ARG   A NH2   
1205 N  N     . GLN   A 153 ? 0.1832 0.2182 0.1676 -0.0267 0.0134  0.0016  150 GLN   A N     
1206 C  CA    . GLN   A 153 ? 0.1759 0.2148 0.1631 -0.0207 0.0128  -0.0030 150 GLN   A CA    
1207 C  C     . GLN   A 153 ? 0.1707 0.1989 0.1578 -0.0170 0.0097  -0.0033 150 GLN   A C     
1208 O  O     . GLN   A 153 ? 0.1538 0.1770 0.1431 -0.0171 0.0083  -0.0026 150 GLN   A O     
1209 C  CB    . GLN   A 153 ? 0.1864 0.2348 0.1812 -0.0188 0.0133  -0.0068 150 GLN   A CB    
1210 C  CG    . GLN   A 153 ? 0.2068 0.2608 0.2045 -0.0130 0.0135  -0.0117 150 GLN   A CG    
1211 C  CD    . GLN   A 153 ? 0.2334 0.2986 0.2286 -0.0139 0.0168  -0.0136 150 GLN   A CD    
1212 O  OE1   . GLN   A 153 ? 0.2656 0.3418 0.2631 -0.0170 0.0195  -0.0135 150 GLN   A OE1   
1213 N  NE2   . GLN   A 153 ? 0.2653 0.3288 0.2557 -0.0118 0.0166  -0.0152 150 GLN   A NE2   
1214 N  N     . ARG   A 154 ? 0.1598 0.1860 0.1444 -0.0141 0.0089  -0.0045 151 ARG   A N     
1215 C  CA    . ARG   A 154 ? 0.1528 0.1711 0.1384 -0.0110 0.0064  -0.0051 151 ARG   A CA    
1216 C  C     . ARG   A 154 ? 0.1622 0.1717 0.1454 -0.0122 0.0049  -0.0017 151 ARG   A C     
1217 O  O     . ARG   A 154 ? 0.1525 0.1575 0.1379 -0.0101 0.0034  -0.0022 151 ARG   A O     
1218 C  CB    . ARG   A 154 ? 0.1415 0.1603 0.1336 -0.0079 0.0058  -0.0079 151 ARG   A CB    
1219 C  CG    . ARG   A 154 ? 0.1574 0.1829 0.1526 -0.0051 0.0066  -0.0123 151 ARG   A CG    
1220 C  CD    . ARG   A 154 ? 0.1709 0.1926 0.1720 -0.0014 0.0049  -0.0144 151 ARG   A CD    
1221 N  NE    . ARG   A 154 ? 0.1789 0.1947 0.1798 -0.0006 0.0034  -0.0155 151 ARG   A NE    
1222 C  CZ    . ARG   A 154 ? 0.1755 0.1858 0.1814 0.0013  0.0020  -0.0162 151 ARG   A CZ    
1223 N  NH1   . ARG   A 154 ? 0.1841 0.1903 0.1905 0.0010  0.0007  -0.0174 151 ARG   A NH1   
1224 N  NH2   . ARG   A 154 ? 0.1754 0.1846 0.1857 0.0032  0.0017  -0.0151 151 ARG   A NH2   
1225 N  N     . VAL   A 155 ? 0.1658 0.1729 0.1447 -0.0156 0.0054  0.0018  152 VAL   A N     
1226 C  CA    . VAL   A 155 ? 0.1812 0.1789 0.1581 -0.0160 0.0037  0.0043  152 VAL   A CA    
1227 C  C     . VAL   A 155 ? 0.1773 0.1716 0.1522 -0.0127 0.0016  0.0046  152 VAL   A C     
1228 O  O     . VAL   A 155 ? 0.1836 0.1742 0.1610 -0.0103 0.0002  0.0036  152 VAL   A O     
1229 C  CB    . VAL   A 155 ? 0.2036 0.1972 0.1772 -0.0206 0.0042  0.0082  152 VAL   A CB    
1230 C  CG1   . VAL   A 155 ? 0.2201 0.2026 0.1921 -0.0196 0.0019  0.0099  152 VAL   A CG1   
1231 C  CG2   . VAL   A 155 ? 0.2121 0.2101 0.1897 -0.0242 0.0057  0.0068  152 VAL   A CG2   
1232 N  N     . GLU   A 156 ? 0.1858 0.1830 0.1562 -0.0126 0.0014  0.0058  153 GLU   A N     
1233 C  CA    . GLU   A 156 ? 0.1985 0.1947 0.1675 -0.0092 -0.0011 0.0053  153 GLU   A CA    
1234 C  C     . GLU   A 156 ? 0.1760 0.1752 0.1512 -0.0067 -0.0017 0.0005  153 GLU   A C     
1235 O  O     . GLU   A 156 ? 0.1894 0.1864 0.1672 -0.0047 -0.0035 -0.0001 153 GLU   A O     
1236 C  CB    . GLU   A 156 ? 0.2400 0.2405 0.2020 -0.0095 -0.0014 0.0071  153 GLU   A CB    
1237 C  CG    . GLU   A 156 ? 0.2806 0.2768 0.2360 -0.0126 -0.0009 0.0136  153 GLU   A CG    
1238 C  CD    . GLU   A 156 ? 0.3853 0.3857 0.3321 -0.0125 -0.0016 0.0170  153 GLU   A CD    
1239 O  OE1   . GLU   A 156 ? 0.4463 0.4541 0.3897 -0.0151 0.0012  0.0175  153 GLU   A OE1   
1240 O  OE2   . GLU   A 156 ? 0.4952 0.4922 0.4389 -0.0095 -0.0049 0.0191  153 GLU   A OE2   
1241 N  N     . ASP   A 157 ? 0.1829 0.1870 0.1612 -0.0070 0.0000  -0.0027 154 ASP   A N     
1242 C  CA    . ASP   A 157 ? 0.1816 0.1865 0.1662 -0.0051 -0.0007 -0.0066 154 ASP   A CA    
1243 C  C     . ASP   A 157 ? 0.1688 0.1692 0.1576 -0.0047 -0.0009 -0.0053 154 ASP   A C     
1244 O  O     . ASP   A 157 ? 0.1738 0.1737 0.1664 -0.0037 -0.0020 -0.0065 154 ASP   A O     
1245 C  CB    . ASP   A 157 ? 0.2042 0.2127 0.1924 -0.0048 0.0009  -0.0094 154 ASP   A CB    
1246 C  CG    . ASP   A 157 ? 0.2874 0.3017 0.2749 -0.0036 0.0011  -0.0139 154 ASP   A CG    
1247 O  OD1   . ASP   A 157 ? 0.2955 0.3118 0.2792 -0.0033 -0.0003 -0.0150 154 ASP   A OD1   
1248 O  OD2   . ASP   A 157 ? 0.3028 0.3202 0.2934 -0.0026 0.0024  -0.0165 154 ASP   A OD2   
1249 N  N     . ALA   A 158 ? 0.1523 0.1506 0.1404 -0.0059 0.0002  -0.0031 155 ALA   A N     
1250 C  CA    . ALA   A 158 ? 0.1512 0.1469 0.1422 -0.0053 0.0002  -0.0024 155 ALA   A CA    
1251 C  C     . ALA   A 158 ? 0.1469 0.1403 0.1376 -0.0039 -0.0011 -0.0019 155 ALA   A C     
1252 O  O     . ALA   A 158 ? 0.1629 0.1575 0.1576 -0.0030 -0.0011 -0.0026 155 ALA   A O     
1253 C  CB    . ALA   A 158 ? 0.1741 0.1689 0.1638 -0.0067 0.0011  -0.0013 155 ALA   A CB    
1254 N  N     . PHE   A 159 ? 0.1563 0.1468 0.1428 -0.0039 -0.0022 -0.0004 156 PHE   A N     
1255 C  CA    . PHE   A 159 ? 0.1593 0.1475 0.1460 -0.0014 -0.0040 -0.0001 156 PHE   A CA    
1256 C  C     . PHE   A 159 ? 0.1549 0.1478 0.1444 0.0002  -0.0056 -0.0017 156 PHE   A C     
1257 O  O     . PHE   A 159 ? 0.1609 0.1561 0.1548 0.0021  -0.0064 -0.0028 156 PHE   A O     
1258 C  CB    . PHE   A 159 ? 0.1648 0.1470 0.1464 -0.0012 -0.0053 0.0026  156 PHE   A CB    
1259 C  CG    . PHE   A 159 ? 0.1741 0.1507 0.1548 -0.0026 -0.0045 0.0030  156 PHE   A CG    
1260 C  CD1   . PHE   A 159 ? 0.1825 0.1561 0.1653 -0.0001 -0.0051 0.0012  156 PHE   A CD1   
1261 C  CD2   . PHE   A 159 ? 0.1841 0.1595 0.1624 -0.0065 -0.0032 0.0042  156 PHE   A CD2   
1262 C  CE1   . PHE   A 159 ? 0.2013 0.1696 0.1831 -0.0014 -0.0048 0.0003  156 PHE   A CE1   
1263 C  CE2   . PHE   A 159 ? 0.2120 0.1827 0.1902 -0.0084 -0.0029 0.0037  156 PHE   A CE2   
1264 C  CZ    . PHE   A 159 ? 0.1924 0.1589 0.1720 -0.0058 -0.0039 0.0015  156 PHE   A CZ    
1265 N  N     . TYR   A 160 ? 0.1577 0.1533 0.1449 -0.0006 -0.0062 -0.0023 157 TYR   A N     
1266 C  CA    . TYR   A 160 ? 0.1599 0.1605 0.1494 0.0005  -0.0083 -0.0049 157 TYR   A CA    
1267 C  C     . TYR   A 160 ? 0.1566 0.1598 0.1539 -0.0004 -0.0075 -0.0079 157 TYR   A C     
1268 O  O     . TYR   A 160 ? 0.1527 0.1596 0.1546 0.0000  -0.0091 -0.0098 157 TYR   A O     
1269 C  CB    . TYR   A 160 ? 0.1745 0.1782 0.1587 0.0001  -0.0091 -0.0058 157 TYR   A CB    
1270 C  CG    . TYR   A 160 ? 0.1904 0.1923 0.1664 0.0005  -0.0101 -0.0016 157 TYR   A CG    
1271 C  CD1   . TYR   A 160 ? 0.1983 0.1936 0.1723 0.0012  -0.0104 0.0025  157 TYR   A CD1   
1272 C  CD2   . TYR   A 160 ? 0.2090 0.2154 0.1788 0.0001  -0.0105 -0.0017 157 TYR   A CD2   
1273 C  CE1   . TYR   A 160 ? 0.2365 0.2280 0.2030 0.0011  -0.0114 0.0074  157 TYR   A CE1   
1274 C  CE2   . TYR   A 160 ? 0.2473 0.2520 0.2086 -0.0001 -0.0110 0.0035  157 TYR   A CE2   
1275 C  CZ    . TYR   A 160 ? 0.2538 0.2502 0.2137 0.0001  -0.0115 0.0086  157 TYR   A CZ    
1276 O  OH    . TYR   A 160 ? 0.3306 0.3236 0.2823 -0.0005 -0.0122 0.0147  157 TYR   A OH    
1277 N  N     . THR   A 161 ? 0.1428 0.1441 0.1416 -0.0020 -0.0051 -0.0078 158 THR   A N     
1278 C  CA    . THR   A 161 ? 0.1328 0.1346 0.1388 -0.0031 -0.0042 -0.0090 158 THR   A CA    
1279 C  C     . THR   A 161 ? 0.1455 0.1486 0.1550 -0.0029 -0.0036 -0.0074 158 THR   A C     
1280 O  O     . THR   A 161 ? 0.1478 0.1537 0.1635 -0.0041 -0.0037 -0.0085 158 THR   A O     
1281 C  CB    . THR   A 161 ? 0.1459 0.1452 0.1521 -0.0038 -0.0024 -0.0083 158 THR   A CB    
1282 O  OG1   . THR   A 161 ? 0.1487 0.1489 0.1531 -0.0035 -0.0029 -0.0111 158 THR   A OG1   
1283 C  CG2   . THR   A 161 ? 0.1522 0.1500 0.1647 -0.0050 -0.0014 -0.0075 158 THR   A CG2   
1284 N  N     . LEU   A 162 ? 0.1312 0.1327 0.1371 -0.0016 -0.0028 -0.0054 159 LEU   A N     
1285 C  CA    . LEU   A 162 ? 0.1436 0.1480 0.1527 -0.0006 -0.0019 -0.0050 159 LEU   A CA    
1286 C  C     . LEU   A 162 ? 0.1433 0.1526 0.1562 0.0010  -0.0041 -0.0068 159 LEU   A C     
1287 O  O     . LEU   A 162 ? 0.1536 0.1685 0.1727 0.0006  -0.0032 -0.0074 159 LEU   A O     
1288 C  CB    . LEU   A 162 ? 0.1479 0.1489 0.1522 0.0009  -0.0012 -0.0040 159 LEU   A CB    
1289 C  CG    . LEU   A 162 ? 0.1360 0.1406 0.1426 0.0028  0.0000  -0.0047 159 LEU   A CG    
1290 C  CD1   . LEU   A 162 ? 0.1404 0.1501 0.1510 0.0007  0.0028  -0.0037 159 LEU   A CD1   
1291 C  CD2   . LEU   A 162 ? 0.1545 0.1543 0.1560 0.0040  0.0002  -0.0050 159 LEU   A CD2   
1292 N  N     . VAL   A 163 ? 0.1356 0.1436 0.1446 0.0029  -0.0069 -0.0071 160 VAL   A N     
1293 C  CA    . VAL   A 163 ? 0.1457 0.1594 0.1581 0.0051  -0.0100 -0.0088 160 VAL   A CA    
1294 C  C     . VAL   A 163 ? 0.1525 0.1725 0.1724 0.0022  -0.0103 -0.0117 160 VAL   A C     
1295 O  O     . VAL   A 163 ? 0.1418 0.1692 0.1691 0.0023  -0.0108 -0.0133 160 VAL   A O     
1296 C  CB    . VAL   A 163 ? 0.1518 0.1630 0.1571 0.0072  -0.0132 -0.0078 160 VAL   A CB    
1297 C  CG1   . VAL   A 163 ? 0.1755 0.1942 0.1839 0.0094  -0.0171 -0.0098 160 VAL   A CG1   
1298 C  CG2   . VAL   A 163 ? 0.1763 0.1802 0.1758 0.0098  -0.0134 -0.0047 160 VAL   A CG2   
1299 N  N     . ARG   A 164 ? 0.1427 0.1600 0.1614 -0.0004 -0.0100 -0.0127 161 ARG   A N     
1300 C  CA    . ARG   A 164 ? 0.1493 0.1699 0.1756 -0.0037 -0.0105 -0.0160 161 ARG   A CA    
1301 C  C     . ARG   A 164 ? 0.1498 0.1722 0.1840 -0.0066 -0.0076 -0.0145 161 ARG   A C     
1302 O  O     . ARG   A 164 ? 0.1533 0.1817 0.1961 -0.0091 -0.0083 -0.0167 161 ARG   A O     
1303 C  CB    . ARG   A 164 ? 0.1551 0.1708 0.1789 -0.0052 -0.0104 -0.0177 161 ARG   A CB    
1304 C  CG    . ARG   A 164 ? 0.1718 0.1891 0.1886 -0.0031 -0.0131 -0.0200 161 ARG   A CG    
1305 C  CD    . ARG   A 164 ? 0.1870 0.2008 0.2004 -0.0037 -0.0122 -0.0220 161 ARG   A CD    
1306 N  NE    . ARG   A 164 ? 0.2016 0.2199 0.2096 -0.0024 -0.0149 -0.0256 161 ARG   A NE    
1307 C  CZ    . ARG   A 164 ? 0.2660 0.2841 0.2698 -0.0021 -0.0142 -0.0285 161 ARG   A CZ    
1308 N  NH1   . ARG   A 164 ? 0.2906 0.3039 0.2955 -0.0025 -0.0113 -0.0277 161 ARG   A NH1   
1309 N  NH2   . ARG   A 164 ? 0.2769 0.3010 0.2754 -0.0009 -0.0165 -0.0324 161 ARG   A NH2   
1310 N  N     . GLU   A 165 ? 0.1432 0.1619 0.1748 -0.0065 -0.0044 -0.0108 162 GLU   A N     
1311 C  CA    . GLU   A 165 ? 0.1412 0.1624 0.1783 -0.0091 -0.0011 -0.0084 162 GLU   A CA    
1312 C  C     . GLU   A 165 ? 0.1382 0.1693 0.1803 -0.0079 -0.0009 -0.0093 162 GLU   A C     
1313 O  O     . GLU   A 165 ? 0.1694 0.2070 0.2199 -0.0113 0.0006  -0.0092 162 GLU   A O     
1314 C  CB    . GLU   A 165 ? 0.1464 0.1634 0.1781 -0.0086 0.0018  -0.0045 162 GLU   A CB    
1315 C  CG    . GLU   A 165 ? 0.1664 0.1756 0.1953 -0.0096 0.0018  -0.0032 162 GLU   A CG    
1316 C  CD    . GLU   A 165 ? 0.1905 0.1975 0.2264 -0.0135 0.0024  -0.0023 162 GLU   A CD    
1317 O  OE1   . GLU   A 165 ? 0.2263 0.2352 0.2655 -0.0160 0.0050  0.0016  162 GLU   A OE1   
1318 O  OE2   . GLU   A 165 ? 0.2306 0.2336 0.2687 -0.0142 0.0003  -0.0053 162 GLU   A OE2   
1319 N  N     . ILE   A 166 ? 0.1485 0.1805 0.1861 -0.0032 -0.0023 -0.0101 163 ILE   A N     
1320 C  CA    . ILE   A 166 ? 0.1526 0.1944 0.1956 -0.0005 -0.0025 -0.0118 163 ILE   A CA    
1321 C  C     . ILE   A 166 ? 0.1685 0.2186 0.2198 -0.0018 -0.0055 -0.0150 163 ILE   A C     
1322 O  O     . ILE   A 166 ? 0.1687 0.2297 0.2296 -0.0038 -0.0042 -0.0161 163 ILE   A O     
1323 C  CB    . ILE   A 166 ? 0.1615 0.2006 0.1985 0.0056  -0.0045 -0.0123 163 ILE   A CB    
1324 C  CG1   . ILE   A 166 ? 0.1666 0.1994 0.1972 0.0067  -0.0017 -0.0105 163 ILE   A CG1   
1325 C  CG2   . ILE   A 166 ? 0.1581 0.2080 0.2021 0.0097  -0.0058 -0.0149 163 ILE   A CG2   
1326 C  CD1   . ILE   A 166 ? 0.1693 0.1943 0.1928 0.0111  -0.0041 -0.0105 163 ILE   A CD1   
1327 N  N     . ARG   A 167 ? 0.1643 0.2108 0.2121 -0.0012 -0.0095 -0.0167 164 ARG   A N     
1328 C  CA    . ARG   A 167 ? 0.1917 0.2466 0.2461 -0.0019 -0.0133 -0.0206 164 ARG   A CA    
1329 C  C     . ARG   A 167 ? 0.1939 0.2534 0.2589 -0.0086 -0.0113 -0.0219 164 ARG   A C     
1330 O  O     . ARG   A 167 ? 0.2157 0.2871 0.2909 -0.0101 -0.0125 -0.0246 164 ARG   A O     
1331 C  CB    . ARG   A 167 ? 0.1786 0.2287 0.2255 -0.0005 -0.0174 -0.0223 164 ARG   A CB    
1332 C  CG    . ARG   A 167 ? 0.2249 0.2849 0.2763 0.0004  -0.0225 -0.0266 164 ARG   A CG    
1333 C  CD    . ARG   A 167 ? 0.2211 0.2767 0.2646 0.0003  -0.0254 -0.0286 164 ARG   A CD    
1334 N  NE    . ARG   A 167 ? 0.1996 0.2504 0.2312 0.0053  -0.0270 -0.0252 164 ARG   A NE    
1335 C  CZ    . ARG   A 167 ? 0.2070 0.2502 0.2287 0.0051  -0.0262 -0.0238 164 ARG   A CZ    
1336 N  NH1   . ARG   A 167 ? 0.2097 0.2502 0.2215 0.0090  -0.0279 -0.0202 164 ARG   A NH1   
1337 N  NH2   . ARG   A 167 ? 0.1846 0.2232 0.2065 0.0013  -0.0238 -0.0257 164 ARG   A NH2   
1338 N  N     . GLN   A 168 ? 0.2055 0.2562 0.2691 -0.0127 -0.0086 -0.0197 165 GLN   A N     
1339 C  CA    . GLN   A 168 ? 0.2494 0.3012 0.3225 -0.0194 -0.0067 -0.0197 165 GLN   A CA    
1340 C  C     . GLN   A 168 ? 0.2364 0.2967 0.3167 -0.0221 -0.0023 -0.0166 165 GLN   A C     
1341 O  O     . GLN   A 168 ? 0.2177 0.2862 0.3092 -0.0273 -0.0019 -0.0179 165 GLN   A O     
1342 C  CB    . GLN   A 168 ? 0.2980 0.3369 0.3674 -0.0220 -0.0052 -0.0175 165 GLN   A CB    
1343 C  CG    . GLN   A 168 ? 0.3459 0.3788 0.4114 -0.0209 -0.0091 -0.0221 165 GLN   A CG    
1344 C  CD    . GLN   A 168 ? 0.4005 0.4213 0.4604 -0.0207 -0.0075 -0.0199 165 GLN   A CD    
1345 O  OE1   . GLN   A 168 ? 0.4362 0.4517 0.4995 -0.0239 -0.0047 -0.0161 165 GLN   A OE1   
1346 N  NE2   . GLN   A 168 ? 0.3247 0.3418 0.3760 -0.0169 -0.0093 -0.0220 165 GLN   A NE2   
1347 N  N     . TYR   A 169 ? 0.1870 0.2461 0.2611 -0.0192 0.0011  -0.0126 166 TYR   A N     
1348 C  CA    . TYR   A 169 ? 0.1721 0.2417 0.2518 -0.0209 0.0057  -0.0102 166 TYR   A CA    
1349 C  C     . TYR   A 169 ? 0.1711 0.2566 0.2597 -0.0191 0.0044  -0.0142 166 TYR   A C     
1350 O  O     . TYR   A 169 ? 0.1849 0.2826 0.2828 -0.0229 0.0080  -0.0133 166 TYR   A O     
1351 C  CB    . TYR   A 169 ? 0.1830 0.2492 0.2530 -0.0167 0.0087  -0.0070 166 TYR   A CB    
1352 C  CG    . TYR   A 169 ? 0.2056 0.2639 0.2714 -0.0204 0.0121  -0.0013 166 TYR   A CG    
1353 C  CD1   . TYR   A 169 ? 0.2431 0.3075 0.3144 -0.0259 0.0166  0.0031  166 TYR   A CD1   
1354 C  CD2   . TYR   A 169 ? 0.2270 0.2725 0.2837 -0.0186 0.0108  0.0001  166 TYR   A CD2   
1355 C  CE1   . TYR   A 169 ? 0.2800 0.3369 0.3465 -0.0287 0.0193  0.0094  166 TYR   A CE1   
1356 C  CE2   . TYR   A 169 ? 0.2593 0.2984 0.3123 -0.0210 0.0132  0.0054  166 TYR   A CE2   
1357 C  CZ    . TYR   A 169 ? 0.2962 0.3405 0.3535 -0.0257 0.0173  0.0103  166 TYR   A CZ    
1358 O  OH    . TYR   A 169 ? 0.3441 0.3817 0.3972 -0.0277 0.0192  0.0166  166 TYR   A OH    
1359 N  N     . ARG   A 170 ? 0.1741 0.2608 0.2606 -0.0134 -0.0005 -0.0183 167 ARG   A N     
1360 C  CA    . ARG   A 170 ? 0.1883 0.2907 0.2836 -0.0102 -0.0029 -0.0224 167 ARG   A CA    
1361 C  C     . ARG   A 170 ? 0.2107 0.3230 0.3191 -0.0171 -0.0041 -0.0252 167 ARG   A C     
1362 O  O     . ARG   A 170 ? 0.1845 0.3135 0.3039 -0.0171 -0.0042 -0.0279 167 ARG   A O     
1363 C  CB    . ARG   A 170 ? 0.1890 0.2887 0.2777 -0.0020 -0.0088 -0.0250 167 ARG   A CB    
1364 C  CG    . ARG   A 170 ? 0.1938 0.2857 0.2722 0.0052  -0.0083 -0.0231 167 ARG   A CG    
1365 C  CD    . ARG   A 170 ? 0.2128 0.3016 0.2858 0.0124  -0.0143 -0.0244 167 ARG   A CD    
1366 N  NE    . ARG   A 170 ? 0.2369 0.3175 0.3019 0.0189  -0.0137 -0.0227 167 ARG   A NE    
1367 C  CZ    . ARG   A 170 ? 0.2658 0.3345 0.3207 0.0229  -0.0171 -0.0209 167 ARG   A CZ    
1368 N  NH1   . ARG   A 170 ? 0.3019 0.3672 0.3524 0.0221  -0.0212 -0.0203 167 ARG   A NH1   
1369 N  NH2   . ARG   A 170 ? 0.2973 0.3579 0.3465 0.0279  -0.0165 -0.0198 167 ARG   A NH2   
1370 N  N     . LEU   A 171 ? 0.2207 0.3235 0.3293 -0.0233 -0.0049 -0.0250 168 LEU   A N     
1371 C  CA    . LEU   A 171 ? 0.2525 0.3624 0.3744 -0.0314 -0.0060 -0.0279 168 LEU   A CA    
1372 C  C     . LEU   A 171 ? 0.2617 0.3735 0.3918 -0.0400 0.0001  -0.0234 168 LEU   A C     
1373 O  O     . LEU   A 171 ? 0.2942 0.4128 0.4371 -0.0478 -0.0002 -0.0254 168 LEU   A O     
1374 C  CB    . LEU   A 171 ? 0.2745 0.3730 0.3937 -0.0337 -0.0106 -0.0315 168 LEU   A CB    
1375 C  CG    . LEU   A 171 ? 0.2954 0.3940 0.4071 -0.0267 -0.0169 -0.0361 168 LEU   A CG    
1376 C  CD1   . LEU   A 171 ? 0.3421 0.4310 0.4516 -0.0299 -0.0204 -0.0403 168 LEU   A CD1   
1377 C  CD2   . LEU   A 171 ? 0.3101 0.4265 0.4290 -0.0232 -0.0212 -0.0405 168 LEU   A CD2   
1378 N  N     . LYS   A 172 ? 0.2981 0.4045 0.4209 -0.0391 0.0054  -0.0171 169 LYS   A N     
1379 C  CA    . LYS   A 172 ? 0.2716 0.3785 0.3993 -0.0469 0.0114  -0.0109 169 LYS   A CA    
1380 C  C     . LYS   A 172 ? 0.2595 0.3854 0.3926 -0.0462 0.0164  -0.0096 169 LYS   A C     
1381 O  O     . LYS   A 172 ? 0.2679 0.4047 0.4121 -0.0540 0.0204  -0.0072 169 LYS   A O     
1382 C  CB    . LYS   A 172 ? 0.3145 0.4045 0.4300 -0.0460 0.0138  -0.0047 169 LYS   A CB    
1383 C  CG    . LYS   A 172 ? 0.3649 0.4539 0.4833 -0.0536 0.0197  0.0034  169 LYS   A CG    
1384 C  CD    . LYS   A 172 ? 0.3930 0.4716 0.4979 -0.0500 0.0223  0.0096  169 LYS   A CD    
1385 C  CE    . LYS   A 172 ? 0.4234 0.5029 0.5296 -0.0567 0.0282  0.0187  169 LYS   A CE    
1386 N  NZ    . LYS   A 172 ? 0.4621 0.5282 0.5557 -0.0539 0.0290  0.0248  169 LYS   A NZ    
1387 O  OXT   . LYS   A 172 ? 0.1982 0.3294 0.3252 -0.0379 0.0165  -0.0113 169 LYS   A OXT   
1388 P  PB    . GDP   B .   ? 0.2216 0.1915 0.2058 -0.0265 -0.0106 -0.0336 201 GDP   A PB    
1389 O  O1B   . GDP   B .   ? 0.2305 0.1853 0.2147 -0.0258 -0.0106 -0.0316 201 GDP   A O1B   
1390 O  O2B   . GDP   B .   ? 0.2180 0.1992 0.2004 -0.0218 -0.0087 -0.0300 201 GDP   A O2B   
1391 O  O3B   . GDP   B .   ? 0.2542 0.2259 0.2378 -0.0271 -0.0132 -0.0423 201 GDP   A O3B   
1392 O  O3A   . GDP   B .   ? 0.2152 0.1895 0.2033 -0.0335 -0.0103 -0.0300 201 GDP   A O3A   
1393 P  PA    . GDP   B .   ? 0.2390 0.2040 0.2301 -0.0406 -0.0097 -0.0260 201 GDP   A PA    
1394 O  O1A   . GDP   B .   ? 0.2335 0.1946 0.2226 -0.0385 -0.0075 -0.0187 201 GDP   A O1A   
1395 O  O2A   . GDP   B .   ? 0.2644 0.2162 0.2569 -0.0447 -0.0122 -0.0306 201 GDP   A O2A   
1396 O  "O5'" . GDP   B .   ? 0.2165 0.1964 0.2118 -0.0453 -0.0091 -0.0251 201 GDP   A "O5'" 
1397 C  "C5'" . GDP   B .   ? 0.2208 0.2109 0.2190 -0.0478 -0.0114 -0.0311 201 GDP   A "C5'" 
1398 C  "C4'" . GDP   B .   ? 0.2232 0.2229 0.2277 -0.0551 -0.0108 -0.0300 201 GDP   A "C4'" 
1399 O  "O4'" . GDP   B .   ? 0.2211 0.2327 0.2265 -0.0520 -0.0085 -0.0252 201 GDP   A "O4'" 
1400 C  "C3'" . GDP   B .   ? 0.2378 0.2266 0.2447 -0.0628 -0.0094 -0.0265 201 GDP   A "C3'" 
1401 O  "O3'" . GDP   B .   ? 0.2562 0.2531 0.2703 -0.0714 -0.0103 -0.0294 201 GDP   A "O3'" 
1402 C  "C2'" . GDP   B .   ? 0.2210 0.2126 0.2264 -0.0613 -0.0057 -0.0187 201 GDP   A "C2'" 
1403 O  "O2'" . GDP   B .   ? 0.2476 0.2385 0.2562 -0.0695 -0.0034 -0.0141 201 GDP   A "O2'" 
1404 C  "C1'" . GDP   B .   ? 0.2153 0.2246 0.2225 -0.0565 -0.0055 -0.0198 201 GDP   A "C1'" 
1405 N  N9    . GDP   B .   ? 0.2041 0.2146 0.2078 -0.0504 -0.0031 -0.0150 201 GDP   A N9    
1406 C  C8    . GDP   B .   ? 0.2059 0.2065 0.2042 -0.0450 -0.0027 -0.0128 201 GDP   A C8    
1407 N  N7    . GDP   B .   ? 0.2017 0.2076 0.1992 -0.0412 -0.0007 -0.0095 201 GDP   A N7    
1408 C  C5    . GDP   B .   ? 0.1785 0.1975 0.1807 -0.0435 0.0005  -0.0095 201 GDP   A C5    
1409 C  C6    . GDP   B .   ? 0.1871 0.2171 0.1916 -0.0411 0.0027  -0.0079 201 GDP   A C6    
1410 O  O6    . GDP   B .   ? 0.1727 0.2001 0.1741 -0.0363 0.0038  -0.0058 201 GDP   A O6    
1411 N  N1    . GDP   B .   ? 0.1747 0.2183 0.1854 -0.0442 0.0032  -0.0094 201 GDP   A N1    
1412 C  C2    . GDP   B .   ? 0.1962 0.2438 0.2111 -0.0501 0.0019  -0.0121 201 GDP   A C2    
1413 N  N2    . GDP   B .   ? 0.1946 0.2578 0.2169 -0.0532 0.0024  -0.0139 201 GDP   A N2    
1414 N  N3    . GDP   B .   ? 0.1931 0.2305 0.2062 -0.0531 -0.0004 -0.0141 201 GDP   A N3    
1415 C  C4    . GDP   B .   ? 0.1915 0.2142 0.1981 -0.0496 -0.0010 -0.0129 201 GDP   A C4    
1416 MG MG    . MG    C .   ? 0.2378 0.1719 0.2218 -0.0231 -0.0133 -0.0373 202 MG    A MG    
1417 N  NAP   . A1IMC D .   ? 0.6082 0.5179 0.6136 0.0589  -0.0236 -0.0465 203 A1IMC A NAP   
1418 C  CAO   . A1IMC D .   ? 0.6022 0.5060 0.6048 0.0545  -0.0226 -0.0519 203 A1IMC A CAO   
1419 C  CAN   . A1IMC D .   ? 0.6349 0.5189 0.6350 0.0503  -0.0254 -0.0514 203 A1IMC A CAN   
1420 C  CAM   . A1IMC D .   ? 0.6398 0.5220 0.6379 0.0458  -0.0244 -0.0585 203 A1IMC A CAM   
1421 C  CAL   . A1IMC D .   ? 0.6228 0.5233 0.6203 0.0461  -0.0205 -0.0656 203 A1IMC A CAL   
1422 C  CAK   . A1IMC D .   ? 0.5696 0.4894 0.5691 0.0503  -0.0173 -0.0650 203 A1IMC A CAK   
1423 CL CLAJ  . A1IMC D .   ? 0.6377 0.5800 0.6354 0.0500  -0.0122 -0.0718 203 A1IMC A CLAJ  
1424 C  CAS   . A1IMC D .   ? 0.5703 0.4916 0.5730 0.0541  -0.0184 -0.0585 203 A1IMC A CAS   
1425 S  SAR   . A1IMC D .   ? 0.5587 0.5018 0.5660 0.0585  -0.0154 -0.0568 203 A1IMC A SAR   
1426 C  CAQ   . A1IMC D .   ? 0.5635 0.4940 0.5724 0.0613  -0.0203 -0.0486 203 A1IMC A CAQ   
1427 N  NAT   . A1IMC D .   ? 0.5550 0.4951 0.5680 0.0651  -0.0209 -0.0449 203 A1IMC A NAT   
1428 S  SAB   . A1IMC D .   ? 0.4838 0.4493 0.5018 0.0656  -0.0166 -0.0462 203 A1IMC A SAB   
1429 O  OAA   . A1IMC D .   ? 0.5778 0.5560 0.5983 0.0685  -0.0125 -0.0555 203 A1IMC A OAA   
1430 O  OAU   . A1IMC D .   ? 0.4974 0.4689 0.5217 0.0721  -0.0195 -0.0440 203 A1IMC A OAU   
1431 C  CAC   . A1IMC D .   ? 0.4384 0.4105 0.4516 0.0543  -0.0134 -0.0383 203 A1IMC A CAC   
1432 C  CAH   . A1IMC D .   ? 0.4109 0.3973 0.4240 0.0501  -0.0084 -0.0401 203 A1IMC A CAH   
1433 C  CAG   . A1IMC D .   ? 0.3381 0.3282 0.3483 0.0424  -0.0064 -0.0343 203 A1IMC A CAG   
1434 C  CAF   . A1IMC D .   ? 0.3384 0.3200 0.3457 0.0387  -0.0090 -0.0276 203 A1IMC A CAF   
1435 C  CAE   . A1IMC D .   ? 0.3633 0.3325 0.3698 0.0423  -0.0134 -0.0256 203 A1IMC A CAE   
1436 C  CAD   . A1IMC D .   ? 0.4048 0.3684 0.4142 0.0500  -0.0158 -0.0304 203 A1IMC A CAD   
1437 O  OAI   . A1IMC D .   ? 0.4234 0.3733 0.4319 0.0539  -0.0206 -0.0274 203 A1IMC A OAI   
1438 C  C1    . EDO   E .   ? 0.3505 0.3922 0.3195 0.0038  -0.0212 -0.0296 204 EDO   A C1    
1439 O  O1    . EDO   E .   ? 0.3088 0.3463 0.2779 0.0047  -0.0222 -0.0227 204 EDO   A O1    
1440 C  C2    . EDO   E .   ? 0.3372 0.3846 0.3123 0.0040  -0.0250 -0.0383 204 EDO   A C2    
1441 O  O2    . EDO   E .   ? 0.3545 0.4094 0.3234 0.0060  -0.0294 -0.0373 204 EDO   A O2    
1442 O  O     . HOH   F .   ? 0.4516 0.5191 0.4158 -0.0067 0.0268  0.0416  301 HOH   A O     
1443 O  O     . HOH   F .   ? 0.3501 0.3299 0.3269 0.0264  -0.0046 -0.0727 302 HOH   A O     
1444 O  O     . HOH   F .   ? 0.3018 0.3212 0.3413 -0.0217 0.0152  0.0172  303 HOH   A O     
1445 O  O     . HOH   F .   ? 0.3828 0.5104 0.2883 0.0226  -0.0227 0.0321  304 HOH   A O     
1446 O  O     . HOH   F .   ? 0.5071 0.5775 0.4567 -0.0036 -0.0162 -0.0389 305 HOH   A O     
1447 O  O     . HOH   F .   ? 0.2748 0.2143 0.2563 -0.0125 -0.0113 -0.0354 306 HOH   A O     
1448 O  O     . HOH   F .   ? 0.3425 0.3688 0.3019 0.0036  -0.0174 -0.0090 307 HOH   A O     
1449 O  O     . HOH   F .   ? 0.4228 0.5057 0.3759 0.0255  -0.0249 0.0406  308 HOH   A O     
1450 O  O     . HOH   F .   ? 0.4107 0.3601 0.4694 0.0390  -0.0160 -0.0012 309 HOH   A O     
1451 O  O     . HOH   F .   ? 0.4285 0.4514 0.4639 -0.0263 0.0216  0.0314  310 HOH   A O     
1452 O  O     . HOH   F .   ? 0.2927 0.2226 0.2813 -0.0356 -0.0151 -0.0383 311 HOH   A O     
1453 O  O     . HOH   F .   ? 0.4668 0.5954 0.4739 -0.0072 -0.0335 -0.0248 312 HOH   A O     
1454 O  O     . HOH   F .   ? 0.2693 0.3248 0.2229 0.0105  -0.0330 -0.0223 313 HOH   A O     
1455 O  O     . HOH   F .   ? 0.4721 0.3769 0.4534 -0.0924 0.0041  0.0398  314 HOH   A O     
1456 O  O     . HOH   F .   ? 0.5980 0.6029 0.5290 -0.0439 0.0146  0.0447  315 HOH   A O     
1457 O  O     . HOH   F .   ? 0.3767 0.4494 0.4310 0.0507  -0.0012 -0.0373 316 HOH   A O     
1458 O  O     . HOH   F .   ? 0.5607 0.5161 0.5438 0.0408  -0.0104 -0.0966 317 HOH   A O     
1459 O  O     . HOH   F .   ? 0.6596 0.5867 0.6899 0.0087  -0.0077 0.0695  318 HOH   A O     
1460 O  O     . HOH   F .   ? 0.3145 0.2262 0.2997 -0.0207 -0.0170 -0.0446 319 HOH   A O     
1461 O  O     . HOH   F .   ? 0.3446 0.4276 0.3980 0.0140  -0.0355 -0.0296 320 HOH   A O     
1462 O  O     . HOH   F .   ? 0.4284 0.5289 0.4388 0.0818  0.0233  -0.1109 321 HOH   A O     
1463 O  O     . HOH   F .   ? 0.4592 0.3122 0.4421 -0.0123 -0.0219 -0.0159 322 HOH   A O     
1464 O  O     . HOH   F .   ? 0.6490 0.6309 0.5638 0.0378  -0.0522 0.0529  323 HOH   A O     
1465 O  O     . HOH   F .   ? 0.1923 0.3005 0.2895 -0.0296 0.0221  -0.0020 324 HOH   A O     
1466 O  O     . HOH   F .   ? 0.4558 0.4100 0.5026 -0.0238 0.0078  0.0437  325 HOH   A O     
1467 O  O     . HOH   F .   ? 0.3083 0.4220 0.3489 -0.0577 0.0128  -0.0135 326 HOH   A O     
1468 O  O     . HOH   F .   ? 0.1910 0.3856 0.2692 -0.0256 -0.0171 -0.0354 327 HOH   A O     
1469 O  O     . HOH   F .   ? 0.3845 0.3524 0.4166 -0.0067 0.0017  0.0198  328 HOH   A O     
1470 O  O     . HOH   F .   ? 0.1901 0.2056 0.2201 -0.0133 0.0100  0.0077  329 HOH   A O     
1471 O  O     . HOH   F .   ? 0.3380 0.3749 0.3630 -0.0177 0.0221  0.0223  330 HOH   A O     
1472 O  O     . HOH   F .   ? 0.4216 0.4992 0.4800 0.0143  -0.0261 -0.0252 331 HOH   A O     
1473 O  O     . HOH   F .   ? 0.4007 0.3448 0.4455 0.0275  -0.0139 0.0252  332 HOH   A O     
1474 O  O     . HOH   F .   ? 0.2800 0.3847 0.3410 0.0445  0.0119  -0.0405 333 HOH   A O     
1475 O  O     . HOH   F .   ? 0.1823 0.1766 0.2009 0.0042  -0.0007 -0.0116 334 HOH   A O     
1476 O  O     . HOH   F .   ? 0.4148 0.4690 0.3983 -0.0156 0.0299  0.0520  335 HOH   A O     
1477 O  O     . HOH   F .   ? 0.4693 0.5160 0.4570 -0.0226 -0.0155 -0.0302 336 HOH   A O     
1478 O  O     . HOH   F .   ? 0.4683 0.5733 0.3877 0.0352  0.0090  -0.1074 337 HOH   A O     
1479 O  O     . HOH   F .   ? 0.2746 0.2181 0.2541 -0.0510 0.0001  0.0135  338 HOH   A O     
1480 O  O     . HOH   F .   ? 0.6938 0.5239 0.6704 0.0245  -0.0343 0.0101  339 HOH   A O     
1481 O  O     . HOH   F .   ? 0.3804 0.3827 0.4093 -0.0094 -0.0042 -0.0129 340 HOH   A O     
1482 O  O     . HOH   F .   ? 0.2065 0.2683 0.2093 -0.0285 -0.0154 -0.0273 341 HOH   A O     
1483 O  O     . HOH   F .   ? 0.4254 0.3762 0.4584 0.0289  -0.0153 0.0439  342 HOH   A O     
1484 O  O     . HOH   F .   ? 0.3273 0.4094 0.3350 -0.0238 0.0188  -0.0108 343 HOH   A O     
1485 O  O     . HOH   F .   ? 0.1677 0.2542 0.2035 0.0056  -0.0006 -0.0159 344 HOH   A O     
1486 O  O     . HOH   F .   ? 0.1758 0.3259 0.2384 0.0082  0.0390  -0.0181 345 HOH   A O     
1487 O  O     . HOH   F .   ? 0.3015 0.2723 0.2923 -0.0407 -0.0178 -0.0510 346 HOH   A O     
1488 O  O     . HOH   F .   ? 0.4271 0.3123 0.4107 -0.0055 -0.0180 -0.0276 347 HOH   A O     
1489 O  O     . HOH   F .   ? 0.5145 0.4663 0.5154 -0.0582 -0.0168 -0.0420 348 HOH   A O     
1490 O  O     . HOH   F .   ? 0.2993 0.2459 0.2814 -0.0204 -0.0146 -0.0485 349 HOH   A O     
1491 O  O     . HOH   F .   ? 0.2863 0.3382 0.2417 0.0060  0.0023  0.0323  350 HOH   A O     
1492 O  O     . HOH   F .   ? 0.2878 0.3670 0.3058 -0.0163 0.0124  -0.0138 351 HOH   A O     
1493 O  O     . HOH   F .   ? 0.3668 0.5738 0.3685 0.0023  0.0701  -0.0035 352 HOH   A O     
1494 O  O     . HOH   F .   ? 0.2685 0.2817 0.2337 -0.0188 0.0071  0.0071  353 HOH   A O     
1495 O  O     . HOH   F .   ? 0.1683 0.2135 0.1805 -0.0029 -0.0305 -0.0542 354 HOH   A O     
1496 O  O     . HOH   F .   ? 0.2957 0.2984 0.3077 -0.0039 -0.0064 -0.0202 355 HOH   A O     
1497 O  O     . HOH   F .   ? 0.3501 0.3306 0.3235 -0.0103 -0.0121 -0.0550 356 HOH   A O     
1498 O  O     . HOH   F .   ? 0.5195 0.5278 0.4555 -0.0002 -0.0140 0.0166  357 HOH   A O     
1499 O  O     . HOH   F .   ? 0.4559 0.6334 0.5263 -0.0359 0.0635  0.0243  358 HOH   A O     
1500 O  O     . HOH   F .   ? 0.4308 0.5563 0.4800 0.0344  0.0279  -0.0387 359 HOH   A O     
1501 O  O     . HOH   F .   ? 0.1913 0.2242 0.1602 -0.0029 -0.0032 -0.0130 360 HOH   A O     
1502 O  O     . HOH   F .   ? 0.3990 0.6516 0.4767 -0.0321 0.0839  0.0164  361 HOH   A O     
1503 O  O     . HOH   F .   ? 0.2687 0.3079 0.2441 -0.0140 0.0117  -0.0066 362 HOH   A O     
1504 O  O     . HOH   F .   ? 0.4361 0.5031 0.4001 -0.0104 -0.0198 -0.0372 363 HOH   A O     
1505 O  O     . HOH   F .   ? 0.4052 0.4695 0.3597 0.0522  -0.0722 0.0114  364 HOH   A O     
1506 O  O     . HOH   F .   ? 0.5538 0.4920 0.4619 -0.0511 0.0042  0.0842  365 HOH   A O     
1507 O  O     . HOH   F .   ? 0.2375 0.3110 0.2257 0.0406  -0.0619 -0.0088 366 HOH   A O     
1508 O  O     . HOH   F .   ? 0.3958 0.3605 0.4254 0.0017  -0.0015 0.0220  367 HOH   A O     
1509 O  O     . HOH   F .   ? 0.4831 0.4775 0.5286 -0.0212 0.0061  0.0086  368 HOH   A O     
1510 O  O     . HOH   F .   ? 0.2335 0.4842 0.3157 0.0009  0.0706  -0.0187 369 HOH   A O     
1511 O  O     . HOH   F .   ? 0.2395 0.3349 0.2241 0.0343  -0.0666 -0.0217 370 HOH   A O     
1512 O  O     . HOH   F .   ? 0.4455 0.4775 0.4408 -0.0821 0.0223  0.0227  371 HOH   A O     
1513 O  O     . HOH   F .   ? 0.2705 0.3225 0.3094 0.0368  -0.0166 0.0024  372 HOH   A O     
1514 O  O     . HOH   F .   ? 0.5472 0.5377 0.5318 0.0041  0.0018  0.0821  373 HOH   A O     
1515 O  O     . HOH   F .   ? 0.2391 0.3855 0.3622 -0.0028 -0.0166 -0.0368 374 HOH   A O     
1516 O  O     . HOH   F .   ? 0.5112 0.5743 0.4819 0.0261  -0.0225 0.0411  375 HOH   A O     
1517 O  O     . HOH   F .   ? 0.4432 0.4360 0.4161 0.0368  -0.0035 -0.0951 376 HOH   A O     
1518 O  O     . HOH   F .   ? 0.5900 0.5620 0.5118 0.0078  -0.0251 0.0437  377 HOH   A O     
1519 O  O     . HOH   F .   ? 0.3650 0.3986 0.3448 -0.0054 0.0067  -0.0161 378 HOH   A O     
1520 O  O     . HOH   F .   ? 0.2164 0.1949 0.2433 -0.0009 -0.0009 0.0000  379 HOH   A O     
1521 O  O     . HOH   F .   ? 0.4699 0.5174 0.4354 -0.0168 -0.0207 -0.0555 380 HOH   A O     
1522 O  O     . HOH   F .   ? 0.3238 0.3658 0.3658 0.0488  -0.0214 -0.0212 381 HOH   A O     
1523 O  O     . HOH   F .   ? 0.3030 0.3725 0.3545 0.0560  -0.0397 -0.0195 382 HOH   A O     
1524 O  O     . HOH   F .   ? 0.3164 0.3694 0.3351 -0.0531 -0.0092 -0.0269 383 HOH   A O     
1525 O  O     . HOH   F .   ? 0.5150 0.4728 0.4890 -0.0089 -0.0198 -0.0853 384 HOH   A O     
1526 O  O     . HOH   F .   ? 0.3808 0.4152 0.3363 -0.0045 -0.0124 -0.0586 385 HOH   A O     
1527 O  O     . HOH   F .   ? 0.2466 0.2794 0.2552 0.0118  -0.0082 0.0084  386 HOH   A O     
1528 O  O     . HOH   F .   ? 0.4187 0.4776 0.4185 0.0345  -0.0267 0.0324  387 HOH   A O     
1529 O  O     . HOH   F .   ? 0.5286 0.4596 0.4552 0.0235  -0.0379 0.0564  388 HOH   A O     
1530 O  O     . HOH   F .   ? 0.3726 0.4116 0.3963 -0.0697 -0.0120 -0.0342 389 HOH   A O     
1531 O  O     . HOH   F .   ? 0.1691 0.2769 0.2140 0.0087  -0.0068 -0.0166 390 HOH   A O     
1532 O  O     . HOH   F .   ? 0.4142 0.4549 0.4192 -0.0458 -0.0176 -0.0404 391 HOH   A O     
1533 O  O     . HOH   F .   ? 0.3293 0.4135 0.3536 -0.0453 -0.0153 -0.0322 392 HOH   A O     
1534 O  O     . HOH   F .   ? 0.4340 0.5229 0.4145 -0.0162 0.0243  -0.0160 393 HOH   A O     
1535 O  O     . HOH   F .   ? 0.4632 0.3061 0.4568 0.0152  -0.0295 -0.0736 394 HOH   A O     
1536 O  O     . HOH   F .   ? 0.5139 0.4564 0.4914 0.0218  -0.0153 -0.0946 395 HOH   A O     
1537 O  O     . HOH   F .   ? 0.4260 0.4191 0.4446 0.0012  -0.0021 -0.0183 396 HOH   A O     
1538 O  O     . HOH   F .   ? 0.2757 0.3877 0.2455 0.0018  -0.0316 -0.0175 397 HOH   A O     
1539 O  O     . HOH   F .   ? 0.4458 0.5835 0.5152 -0.0435 0.0548  0.0335  398 HOH   A O     
1540 O  O     . HOH   F .   ? 0.5040 0.4503 0.5236 -0.0050 0.0019  0.0770  399 HOH   A O     
1541 O  O     . HOH   F .   ? 0.6899 0.6267 0.6967 0.0083  -0.0063 0.1037  400 HOH   A O     
1542 O  O     . HOH   F .   ? 0.4219 0.4285 0.3472 0.0083  -0.0244 0.0256  401 HOH   A O     
1543 O  O     . HOH   F .   ? 0.3541 0.4445 0.4314 0.0011  -0.0233 -0.0308 402 HOH   A O     
1544 O  O     . HOH   F .   ? 0.2226 0.2413 0.1947 -0.0106 0.0048  -0.0034 403 HOH   A O     
1545 O  O     . HOH   F .   ? 0.4671 0.5856 0.4099 0.0178  -0.0316 0.0096  404 HOH   A O     
1546 O  O     . HOH   F .   ? 0.2097 0.2579 0.1984 -0.0037 0.0111  -0.0214 405 HOH   A O     
1547 O  O     . HOH   F .   ? 0.3614 0.3717 0.3621 0.0000  -0.0021 -0.0244 406 HOH   A O     
1548 O  O     . HOH   F .   ? 0.5686 0.4010 0.5712 -0.0667 -0.0247 -0.0306 407 HOH   A O     
1549 O  O     . HOH   F .   ? 0.3225 0.3425 0.3192 0.0004  -0.0094 -0.0370 408 HOH   A O     
1550 O  O     . HOH   F .   ? 0.4651 0.5441 0.5264 0.0443  -0.0276 -0.0242 409 HOH   A O     
1551 O  O     . HOH   F .   ? 0.1197 0.2685 0.1750 -0.0296 -0.0128 -0.0287 410 HOH   A O     
1552 O  O     . HOH   F .   ? 0.5270 0.6002 0.5701 0.0464  -0.0254 0.0068  411 HOH   A O     
1553 O  O     . HOH   F .   ? 0.5179 0.4811 0.5528 0.0082  -0.0046 0.0097  412 HOH   A O     
1554 O  O     . HOH   F .   ? 0.4635 0.5507 0.3867 0.0396  0.0019  -0.1337 413 HOH   A O     
1555 O  O     . HOH   F .   ? 0.5459 0.4936 0.5186 0.0039  -0.0213 -0.1052 414 HOH   A O     
1556 O  O     . HOH   F .   ? 0.4779 0.5837 0.4333 0.0335  -0.0365 0.0385  415 HOH   A O     
1557 O  O     . HOH   F .   ? 0.5544 0.6567 0.5810 -0.0480 -0.0246 -0.0442 416 HOH   A O     
1558 O  O     . HOH   F .   ? 0.5263 0.5411 0.5288 -0.0521 -0.0201 -0.0504 417 HOH   A O     
1559 O  O     . HOH   F .   ? 0.4776 0.6976 0.5674 -0.0472 0.0764  0.0285  418 HOH   A O     
1560 O  O     . HOH   F .   ? 0.4593 0.5474 0.5302 0.0636  -0.0092 -0.0413 419 HOH   A O     
# 
