data_9GGV
# 
_entry.id   9GGV 
# 
_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   9GGV         pdb_00009ggv 10.2210/pdb9ggv/pdb 
WWPDB D_1292140522 ?            ?                   
# 
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                        9GGV 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.content_type 
_pdbx_database_related.db_id 
_pdbx_database_related.db_name 
_pdbx_database_related.details 
unspecified 9GGY PDB . 
unspecified 9GH2 PDB . 
unspecified 9GGZ PDB . 
unspecified 9GH0 PDB . 
unspecified 9GH1 PDB . 
unspecified 9GGW PDB . 
unspecified 9GGX PDB . 
unspecified 9GGU PDB . 
unspecified 9GGT PDB . 
unspecified 9G4B PDB . 
unspecified 9G0Y PDB . 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexander.schuettelkopf@cancer.org.uk 
_pdbx_contact_author.name_first         Alexander 
_pdbx_contact_author.name_last          Schuettelkopf 
_pdbx_contact_author.name_mi            W. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9424-8730 
# 
_audit_author.name               'Schuettelkopf, A.W.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-9424-8730 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                9129 
_citation.page_last                 9161 
_citation.title                     
'Reversible Small Molecule Multivariant Ras Inhibitors Display Tunable Affinity for the Active and Inactive Forms of Ras.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02929 
_citation.pdbx_database_id_PubMed   40162713 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Parry, C.W.'        1  ? 
primary 'Pellicano, F.'      2  ? 
primary 'Schuttelkopf, A.W.' 3  ? 
primary 'Beyer, K.S.'        4  ? 
primary 'Bower, J.'          5  ? 
primary 'Bryson, A.'         6  ? 
primary 'Cameron, K.'        7  ? 
primary 'Cerutti, N.M.'      8  ? 
primary 'Clark, J.P.'        9  ? 
primary 'Davidson, S.C.'     10 ? 
primary 'Davies, K.'         11 ? 
primary 'Drysdale, M.J.'     12 ? 
primary 'Engelman, J.'       13 ? 
primary 'Estevan-Barber, A.' 14 ? 
primary 'Gohlke, A.'         15 ? 
primary 'Gray, C.H.'         16 ? 
primary 'Guthy, D.A.'        17 ? 
primary 'Hong, M.'           18 ? 
primary 'Hopkins, A.'        19 ? 
primary 'Hutchinson, L.D.'   20 ? 
primary 'Konczal, J.'        21 ? 
primary 'Maira, M.'          22 ? 
primary 'McArthur, D.'       23 ? 
primary 'Mezna, M.'          24 ? 
primary 'McKinnon, H.'       25 ? 
primary 'Nepravishta, R.'    26 ? 
primary 'Ostermann, N.'      27 ? 
primary 'Pasquali, C.C.'     28 ? 
primary 'Pollock, K.'        29 ? 
primary 'Pugliese, A.'       30 ? 
primary 'Rooney, N.'         31 ? 
primary 'Schmiedeberg, N.'   32 ? 
primary 'Shaw, P.'           33 ? 
primary 'Velez-Vega, C.'     34 ? 
primary 'West, C.'           35 ? 
primary 'West, R.'           36 ? 
primary 'Zecri, F.'          37 ? 
primary 'Taylor, J.B.'       38 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'GTPase KRas' 19607.078 1   3.6.5.2 C118S ? ? 
2 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE" 443.201   1   ?       ?     ? ? 
3 non-polymer syn 'MAGNESIUM ION' 24.305    1   ?       ?     ? ? 
4 non-polymer syn 1,2-ETHANEDIOL 62.068    2   ?       ?     ? ? 
5 non-polymer syn 
'5-[(7-chloranyl-3-ethyl-4-oxidanyl-1,3-benzothiazol-2-yl)sulfamoyl]-~{N}-(2-hydroxyethyl)-2-oxidanyl-~{N}-piperidin-4-yl-benzamide' 
556.075   1   ?       ?     ? ? 
6 water       nat water 18.015    136 ?       ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'K-Ras 2,Ki-Ras,c-K-ras,c-Ki-ras' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GGSMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEG
FLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFY
TLVREIRQYRLK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GGSMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEG
FLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFY
TLVREIRQYRLK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "GUANOSINE-5'-DIPHOSPHATE" GDP   
3 'MAGNESIUM ION' MG    
4 1,2-ETHANEDIOL EDO   
5 
'5-[(7-chloranyl-3-ethyl-4-oxidanyl-1,3-benzothiazol-2-yl)sulfamoyl]-~{N}-(2-hydroxyethyl)-2-oxidanyl-~{N}-piperidin-4-yl-benzamide' 
A1IK9 
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 
A1IK9 non-polymer         . 
'5-[(7-chloranyl-3-ethyl-4-oxidanyl-1,3-benzothiazol-2-yl)sulfamoyl]-~{N}-(2-hydroxyethyl)-2-oxidanyl-~{N}-piperidin-4-yl-benzamide' 
?                 'C23 H28 Cl N4 O6 S2 1' 556.075 
ALA   'L-peptide linking' y ALANINE ?                 'C3 H7 N O2'            89.093  
ARG   'L-peptide linking' y ARGININE ?                 'C6 H15 N4 O2 1'        175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                 'C4 H8 N2 O3'           132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'            133.103 
CYS   'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'          121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'              62.068  
GDP   'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE" ?                 'C10 H15 N5 O11 P2'     443.201 
GLN   'L-peptide linking' y GLUTAMINE ?                 'C5 H10 N2 O3'          146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'            147.129 
GLY   'peptide linking'   y GLYCINE ?                 'C2 H5 N O2'            75.067  
HIS   'L-peptide linking' y HISTIDINE ?                 'C6 H10 N3 O2 1'        156.162 
HOH   non-polymer         . WATER ?                 'H2 O'                  18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                 'C6 H13 N O2'           131.173 
LEU   'L-peptide linking' y LEUCINE ?                 'C6 H13 N O2'           131.173 
LYS   'L-peptide linking' y LYSINE ?                 'C6 H15 N2 O2 1'        147.195 
MET   'L-peptide linking' y METHIONINE ?                 'C5 H11 N O2 S'         149.211 
MG    non-polymer         . 'MAGNESIUM ION' ?                 'Mg 2'                  24.305  
PHE   'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'           165.189 
PRO   'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'            115.130 
SER   'L-peptide linking' y SERINE ?                 'C3 H7 N O3'            105.093 
THR   'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'            119.119 
TYR   'L-peptide linking' y TYROSINE ?                 'C9 H11 N O3'           181.189 
VAL   'L-peptide linking' y VALINE ?                 'C5 H11 N O2'           117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   GLY 2   -1  ?   ?   ?   A . n 
A 1 3   SER 3   0   0   SER SER A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   THR 5   2   2   THR THR A . n 
A 1 6   GLU 6   3   3   GLU GLU A . n 
A 1 7   TYR 7   4   4   TYR TYR A . n 
A 1 8   LYS 8   5   5   LYS LYS A . n 
A 1 9   LEU 9   6   6   LEU LEU A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  VAL 11  8   8   VAL VAL A . n 
A 1 12  VAL 12  9   9   VAL VAL A . n 
A 1 13  GLY 13  10  10  GLY GLY A . n 
A 1 14  ALA 14  11  11  ALA ALA A . n 
A 1 15  GLY 15  12  12  GLY GLY A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  VAL 17  14  14  VAL VAL A . n 
A 1 18  GLY 18  15  15  GLY GLY A . n 
A 1 19  LYS 19  16  16  LYS LYS A . n 
A 1 20  SER 20  17  17  SER SER A . n 
A 1 21  ALA 21  18  18  ALA ALA A . n 
A 1 22  LEU 22  19  19  LEU LEU A . n 
A 1 23  THR 23  20  20  THR THR A . n 
A 1 24  ILE 24  21  21  ILE ILE A . n 
A 1 25  GLN 25  22  22  GLN GLN A . n 
A 1 26  LEU 26  23  23  LEU LEU A . n 
A 1 27  ILE 27  24  24  ILE ILE A . n 
A 1 28  GLN 28  25  25  GLN GLN A . n 
A 1 29  ASN 29  26  26  ASN ASN A . n 
A 1 30  HIS 30  27  27  HIS HIS A . n 
A 1 31  PHE 31  28  28  PHE PHE A . n 
A 1 32  VAL 32  29  29  VAL VAL A . n 
A 1 33  ASP 33  30  30  ASP ASP A . n 
A 1 34  GLU 34  31  31  GLU GLU A . n 
A 1 35  TYR 35  32  32  TYR TYR A . n 
A 1 36  ASP 36  33  33  ASP ASP A . n 
A 1 37  PRO 37  34  34  PRO PRO A . n 
A 1 38  THR 38  35  35  THR THR A . n 
A 1 39  ILE 39  36  36  ILE ILE A . n 
A 1 40  GLU 40  37  37  GLU GLU A . n 
A 1 41  ASP 41  38  38  ASP ASP A . n 
A 1 42  SER 42  39  39  SER SER A . n 
A 1 43  TYR 43  40  40  TYR TYR A . n 
A 1 44  ARG 44  41  41  ARG ARG A . n 
A 1 45  LYS 45  42  42  LYS LYS A . n 
A 1 46  GLN 46  43  43  GLN GLN A . n 
A 1 47  VAL 47  44  44  VAL VAL A . n 
A 1 48  VAL 48  45  45  VAL VAL A . n 
A 1 49  ILE 49  46  46  ILE ILE A . n 
A 1 50  ASP 50  47  47  ASP ASP A . n 
A 1 51  GLY 51  48  48  GLY GLY A . n 
A 1 52  GLU 52  49  49  GLU GLU A . n 
A 1 53  THR 53  50  50  THR THR A . n 
A 1 54  CYS 54  51  51  CYS CYS A . n 
A 1 55  LEU 55  52  52  LEU LEU A . n 
A 1 56  LEU 56  53  53  LEU LEU A . n 
A 1 57  ASP 57  54  54  ASP ASP A . n 
A 1 58  ILE 58  55  55  ILE ILE A . n 
A 1 59  LEU 59  56  56  LEU LEU A . n 
A 1 60  ASP 60  57  57  ASP ASP A . n 
A 1 61  THR 61  58  58  THR THR A . n 
A 1 62  ALA 62  59  59  ALA ALA A . n 
A 1 63  GLY 63  60  60  GLY GLY A . n 
A 1 64  GLN 64  61  61  GLN GLN A . n 
A 1 65  GLU 65  62  62  GLU GLU A . n 
A 1 66  GLU 66  63  63  GLU GLU A . n 
A 1 67  TYR 67  64  64  TYR TYR A . n 
A 1 68  SER 68  65  65  SER SER A . n 
A 1 69  ALA 69  66  66  ALA ALA A . n 
A 1 70  MET 70  67  67  MET MET A . n 
A 1 71  ARG 71  68  68  ARG ARG A . n 
A 1 72  ASP 72  69  69  ASP ASP A . n 
A 1 73  GLN 73  70  70  GLN GLN A . n 
A 1 74  TYR 74  71  71  TYR TYR A . n 
A 1 75  MET 75  72  72  MET MET A . n 
A 1 76  ARG 76  73  73  ARG ARG A . n 
A 1 77  THR 77  74  74  THR THR A . n 
A 1 78  GLY 78  75  75  GLY GLY A . n 
A 1 79  GLU 79  76  76  GLU GLU A . n 
A 1 80  GLY 80  77  77  GLY GLY A . n 
A 1 81  PHE 81  78  78  PHE PHE A . n 
A 1 82  LEU 82  79  79  LEU LEU A . n 
A 1 83  CYS 83  80  80  CYS CYS A . n 
A 1 84  VAL 84  81  81  VAL VAL A . n 
A 1 85  PHE 85  82  82  PHE PHE A . n 
A 1 86  ALA 86  83  83  ALA ALA A . n 
A 1 87  ILE 87  84  84  ILE ILE A . n 
A 1 88  ASN 88  85  85  ASN ASN A . n 
A 1 89  ASN 89  86  86  ASN ASN A . n 
A 1 90  THR 90  87  87  THR THR A . n 
A 1 91  LYS 91  88  88  LYS LYS A . n 
A 1 92  SER 92  89  89  SER SER A . n 
A 1 93  PHE 93  90  90  PHE PHE A . n 
A 1 94  GLU 94  91  91  GLU GLU A . n 
A 1 95  ASP 95  92  92  ASP ASP A . n 
A 1 96  ILE 96  93  93  ILE ILE A . n 
A 1 97  HIS 97  94  94  HIS HIS A . n 
A 1 98  HIS 98  95  95  HIS HIS A . n 
A 1 99  TYR 99  96  96  TYR TYR A . n 
A 1 100 ARG 100 97  97  ARG ARG A . n 
A 1 101 GLU 101 98  98  GLU GLU A . n 
A 1 102 GLN 102 99  99  GLN GLN A . n 
A 1 103 ILE 103 100 100 ILE ILE A . n 
A 1 104 LYS 104 101 101 LYS LYS A . n 
A 1 105 ARG 105 102 102 ARG ARG A . n 
A 1 106 VAL 106 103 103 VAL VAL A . n 
A 1 107 LYS 107 104 104 LYS LYS A . n 
A 1 108 ASP 108 105 105 ASP ASP A . n 
A 1 109 SER 109 106 106 SER SER A . n 
A 1 110 GLU 110 107 107 GLU GLU A . n 
A 1 111 ASP 111 108 108 ASP ASP A . n 
A 1 112 VAL 112 109 109 VAL VAL A . n 
A 1 113 PRO 113 110 110 PRO PRO A . n 
A 1 114 MET 114 111 111 MET MET A . n 
A 1 115 VAL 115 112 112 VAL VAL A . n 
A 1 116 LEU 116 113 113 LEU LEU A . n 
A 1 117 VAL 117 114 114 VAL VAL A . n 
A 1 118 GLY 118 115 115 GLY GLY A . n 
A 1 119 ASN 119 116 116 ASN ASN A . n 
A 1 120 LYS 120 117 117 LYS LYS A . n 
A 1 121 SER 121 118 118 SER SER A . n 
A 1 122 ASP 122 119 119 ASP ASP A . n 
A 1 123 LEU 123 120 120 LEU LEU A . n 
A 1 124 PRO 124 121 121 PRO PRO A . n 
A 1 125 SER 125 122 122 SER SER A . n 
A 1 126 ARG 126 123 123 ARG ARG A . n 
A 1 127 THR 127 124 124 THR THR A . n 
A 1 128 VAL 128 125 125 VAL VAL A . n 
A 1 129 ASP 129 126 126 ASP ASP A . n 
A 1 130 THR 130 127 127 THR THR A . n 
A 1 131 LYS 131 128 128 LYS LYS A . n 
A 1 132 GLN 132 129 129 GLN GLN A . n 
A 1 133 ALA 133 130 130 ALA ALA A . n 
A 1 134 GLN 134 131 131 GLN GLN A . n 
A 1 135 ASP 135 132 132 ASP ASP A . n 
A 1 136 LEU 136 133 133 LEU LEU A . n 
A 1 137 ALA 137 134 134 ALA ALA A . n 
A 1 138 ARG 138 135 135 ARG ARG A . n 
A 1 139 SER 139 136 136 SER SER A . n 
A 1 140 TYR 140 137 137 TYR TYR A . n 
A 1 141 GLY 141 138 138 GLY GLY A . n 
A 1 142 ILE 142 139 139 ILE ILE A . n 
A 1 143 PRO 143 140 140 PRO PRO A . n 
A 1 144 PHE 144 141 141 PHE PHE A . n 
A 1 145 ILE 145 142 142 ILE ILE A . n 
A 1 146 GLU 146 143 143 GLU GLU A . n 
A 1 147 THR 147 144 144 THR THR A . n 
A 1 148 SER 148 145 145 SER SER A . n 
A 1 149 ALA 149 146 146 ALA ALA A . n 
A 1 150 LYS 150 147 147 LYS LYS A . n 
A 1 151 THR 151 148 148 THR THR A . n 
A 1 152 ARG 152 149 149 ARG ARG A . n 
A 1 153 GLN 153 150 150 GLN GLN A . n 
A 1 154 ARG 154 151 151 ARG ARG A . n 
A 1 155 VAL 155 152 152 VAL VAL A . n 
A 1 156 GLU 156 153 153 GLU GLU A . n 
A 1 157 ASP 157 154 154 ASP ASP A . n 
A 1 158 ALA 158 155 155 ALA ALA A . n 
A 1 159 PHE 159 156 156 PHE PHE A . n 
A 1 160 TYR 160 157 157 TYR TYR A . n 
A 1 161 THR 161 158 158 THR THR A . n 
A 1 162 LEU 162 159 159 LEU LEU A . n 
A 1 163 VAL 163 160 160 VAL VAL A . n 
A 1 164 ARG 164 161 161 ARG ARG A . n 
A 1 165 GLU 165 162 162 GLU GLU A . n 
A 1 166 ILE 166 163 163 ILE ILE A . n 
A 1 167 ARG 167 164 164 ARG ARG A . n 
A 1 168 GLN 168 165 165 GLN GLN A . n 
A 1 169 TYR 169 166 166 TYR TYR A . n 
A 1 170 ARG 170 167 167 ARG ARG A . n 
A 1 171 LEU 171 168 168 LEU LEU A . n 
A 1 172 LYS 172 169 169 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 GDP   1   201 1000 GDP   GDP A . 
C 3 MG    1   202 1001 MG    MG  A . 
D 4 EDO   1   203 1    EDO   EDO A . 
E 4 EDO   1   204 2    EDO   EDO A . 
F 5 A1IK9 1   205 1    A1IK9 DRG A . 
G 6 HOH   1   301 129  HOH   HOH A . 
G 6 HOH   2   302 279  HOH   HOH A . 
G 6 HOH   3   303 49   HOH   HOH A . 
G 6 HOH   4   304 235  HOH   HOH A . 
G 6 HOH   5   305 64   HOH   HOH A . 
G 6 HOH   6   306 190  HOH   HOH A . 
G 6 HOH   7   307 7    HOH   HOH A . 
G 6 HOH   8   308 195  HOH   HOH A . 
G 6 HOH   9   309 117  HOH   HOH A . 
G 6 HOH   10  310 258  HOH   HOH A . 
G 6 HOH   11  311 6    HOH   HOH A . 
G 6 HOH   12  312 197  HOH   HOH A . 
G 6 HOH   13  313 149  HOH   HOH A . 
G 6 HOH   14  314 207  HOH   HOH A . 
G 6 HOH   15  315 144  HOH   HOH A . 
G 6 HOH   16  316 16   HOH   HOH A . 
G 6 HOH   17  317 148  HOH   HOH A . 
G 6 HOH   18  318 48   HOH   HOH A . 
G 6 HOH   19  319 155  HOH   HOH A . 
G 6 HOH   20  320 183  HOH   HOH A . 
G 6 HOH   21  321 126  HOH   HOH A . 
G 6 HOH   22  322 213  HOH   HOH A . 
G 6 HOH   23  323 162  HOH   HOH A . 
G 6 HOH   24  324 154  HOH   HOH A . 
G 6 HOH   25  325 289  HOH   HOH A . 
G 6 HOH   26  326 68   HOH   HOH A . 
G 6 HOH   27  327 204  HOH   HOH A . 
G 6 HOH   28  328 10   HOH   HOH A . 
G 6 HOH   29  329 231  HOH   HOH A . 
G 6 HOH   30  330 160  HOH   HOH A . 
G 6 HOH   31  331 41   HOH   HOH A . 
G 6 HOH   32  332 233  HOH   HOH A . 
G 6 HOH   33  333 121  HOH   HOH A . 
G 6 HOH   34  334 12   HOH   HOH A . 
G 6 HOH   35  335 106  HOH   HOH A . 
G 6 HOH   36  336 127  HOH   HOH A . 
G 6 HOH   37  337 211  HOH   HOH A . 
G 6 HOH   38  338 234  HOH   HOH A . 
G 6 HOH   39  339 168  HOH   HOH A . 
G 6 HOH   40  340 276  HOH   HOH A . 
G 6 HOH   41  341 3    HOH   HOH A . 
G 6 HOH   42  342 77   HOH   HOH A . 
G 6 HOH   43  343 288  HOH   HOH A . 
G 6 HOH   44  344 109  HOH   HOH A . 
G 6 HOH   45  345 208  HOH   HOH A . 
G 6 HOH   46  346 132  HOH   HOH A . 
G 6 HOH   47  347 269  HOH   HOH A . 
G 6 HOH   48  348 139  HOH   HOH A . 
G 6 HOH   49  349 150  HOH   HOH A . 
G 6 HOH   50  350 31   HOH   HOH A . 
G 6 HOH   51  351 4    HOH   HOH A . 
G 6 HOH   52  352 28   HOH   HOH A . 
G 6 HOH   53  353 44   HOH   HOH A . 
G 6 HOH   54  354 169  HOH   HOH A . 
G 6 HOH   55  355 264  HOH   HOH A . 
G 6 HOH   56  356 243  HOH   HOH A . 
G 6 HOH   57  357 175  HOH   HOH A . 
G 6 HOH   58  358 110  HOH   HOH A . 
G 6 HOH   59  359 275  HOH   HOH A . 
G 6 HOH   60  360 124  HOH   HOH A . 
G 6 HOH   61  361 87   HOH   HOH A . 
G 6 HOH   62  362 210  HOH   HOH A . 
G 6 HOH   63  363 270  HOH   HOH A . 
G 6 HOH   64  364 133  HOH   HOH A . 
G 6 HOH   65  365 107  HOH   HOH A . 
G 6 HOH   66  366 191  HOH   HOH A . 
G 6 HOH   67  367 194  HOH   HOH A . 
G 6 HOH   68  368 128  HOH   HOH A . 
G 6 HOH   69  369 278  HOH   HOH A . 
G 6 HOH   70  370 274  HOH   HOH A . 
G 6 HOH   71  371 193  HOH   HOH A . 
G 6 HOH   72  372 167  HOH   HOH A . 
G 6 HOH   73  373 40   HOH   HOH A . 
G 6 HOH   74  374 172  HOH   HOH A . 
G 6 HOH   75  375 1    HOH   HOH A . 
G 6 HOH   76  376 108  HOH   HOH A . 
G 6 HOH   77  377 173  HOH   HOH A . 
G 6 HOH   78  378 203  HOH   HOH A . 
G 6 HOH   79  379 123  HOH   HOH A . 
G 6 HOH   80  380 205  HOH   HOH A . 
G 6 HOH   81  381 222  HOH   HOH A . 
G 6 HOH   82  382 39   HOH   HOH A . 
G 6 HOH   83  383 111  HOH   HOH A . 
G 6 HOH   84  384 29   HOH   HOH A . 
G 6 HOH   85  385 228  HOH   HOH A . 
G 6 HOH   86  386 17   HOH   HOH A . 
G 6 HOH   87  387 215  HOH   HOH A . 
G 6 HOH   88  388 229  HOH   HOH A . 
G 6 HOH   89  389 209  HOH   HOH A . 
G 6 HOH   90  390 202  HOH   HOH A . 
G 6 HOH   91  391 171  HOH   HOH A . 
G 6 HOH   92  392 19   HOH   HOH A . 
G 6 HOH   93  393 161  HOH   HOH A . 
G 6 HOH   94  394 143  HOH   HOH A . 
G 6 HOH   95  395 170  HOH   HOH A . 
G 6 HOH   96  396 179  HOH   HOH A . 
G 6 HOH   97  397 196  HOH   HOH A . 
G 6 HOH   98  398 232  HOH   HOH A . 
G 6 HOH   99  399 217  HOH   HOH A . 
G 6 HOH   100 400 221  HOH   HOH A . 
G 6 HOH   101 401 116  HOH   HOH A . 
G 6 HOH   102 402 33   HOH   HOH A . 
G 6 HOH   103 403 283  HOH   HOH A . 
G 6 HOH   104 404 227  HOH   HOH A . 
G 6 HOH   105 405 187  HOH   HOH A . 
G 6 HOH   106 406 189  HOH   HOH A . 
G 6 HOH   107 407 140  HOH   HOH A . 
G 6 HOH   108 408 284  HOH   HOH A . 
G 6 HOH   109 409 122  HOH   HOH A . 
G 6 HOH   110 410 238  HOH   HOH A . 
G 6 HOH   111 411 225  HOH   HOH A . 
G 6 HOH   112 412 182  HOH   HOH A . 
G 6 HOH   113 413 198  HOH   HOH A . 
G 6 HOH   114 414 230  HOH   HOH A . 
G 6 HOH   115 415 181  HOH   HOH A . 
G 6 HOH   116 416 113  HOH   HOH A . 
G 6 HOH   117 417 212  HOH   HOH A . 
G 6 HOH   118 418 223  HOH   HOH A . 
G 6 HOH   119 419 114  HOH   HOH A . 
G 6 HOH   120 420 85   HOH   HOH A . 
G 6 HOH   121 421 224  HOH   HOH A . 
G 6 HOH   122 422 38   HOH   HOH A . 
G 6 HOH   123 423 35   HOH   HOH A . 
G 6 HOH   124 424 272  HOH   HOH A . 
G 6 HOH   125 425 281  HOH   HOH A . 
G 6 HOH   126 426 286  HOH   HOH A . 
G 6 HOH   127 427 165  HOH   HOH A . 
G 6 HOH   128 428 268  HOH   HOH A . 
G 6 HOH   129 429 178  HOH   HOH A . 
G 6 HOH   130 430 277  HOH   HOH A . 
G 6 HOH   131 431 285  HOH   HOH A . 
G 6 HOH   132 432 180  HOH   HOH A . 
G 6 HOH   133 433 220  HOH   HOH A . 
G 6 HOH   134 434 177  HOH   HOH A . 
G 6 HOH   135 435 201  HOH   HOH A . 
G 6 HOH   136 436 176  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0258 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.5.17   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                     9GGV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     36.959 
_cell.length_a_esd                 ? 
_cell.length_b                     40.278 
_cell.length_b_esd                 ? 
_cell.length_c                     110.665 
_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                         9GGV 
_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                   9GGV 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.44 
_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               0.100 
_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              ? 
_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    '27.5% PEG 8000, 400 mM LiCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-03-05 
_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   0.97949 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97949 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GGV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.190 
_reflns.d_resolution_low                               27.670 
_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                                     52205 
_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                           97.000 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.900 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.600 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           21 
_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                                0.043 
_reflns.pdbx_Rpim_I_all                                0.017 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       310446 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.039 
_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 
1.190 1.220  ? ? ? ? ? ? 2905 ? ? ? ? ? ? ? ? ? ? ? 3.600 ? ? ? 0.795 0.401 ? 1 1 0.599 ? ? 75.800 ? 0.680 ? ? ? ? ? ? ? ? ? 
5.320 27.670 ? ? ? ? ? ? 687  ? ? ? ? ? ? ? ? ? ? ? 5.500 ? ? ? 0.024 0.010 ? 2 1 0.999 ? ? 97.500 ? 0.022 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.1500 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            0.0400 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.1100 
_refine.B_iso_max                                61.790 
_refine.B_iso_mean                               16.2440 
_refine.B_iso_min                                7.420 
_refine.correlation_coeff_Fo_to_Fc               0.9750 
_refine.correlation_coeff_Fo_to_Fc_free          0.9670 
_refine.details                                  
'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GGV 
_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                            1.1900 
_refine.ls_d_res_low                             27.6700 
_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                     49566 
_refine.ls_number_reflns_R_free                  2571 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.7400 
_refine.ls_percent_reflns_R_free                 4.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1549 
_refine.ls_R_factor_R_free                       0.1776 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1538 
_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                       0.0400 
_refine.pdbx_overall_ESU_R_Free                  0.0390 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.2950 
_refine.overall_SU_ML                            0.0260 
_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                       1.1900 
_refine_hist.d_res_low                        27.6700 
_refine_hist.number_atoms_solvent             136 
_refine_hist.number_atoms_total               1577 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       170 
_refine_hist.pdbx_B_iso_mean_ligand           19.93 
_refine_hist.pdbx_B_iso_mean_solvent          28.51 
_refine_hist.pdbx_number_atoms_protein        1368 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         73 
_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  1488 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.035  0.018  1348 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 2.069  1.725  2018 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 2.364  1.641  3127 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 4.889  5.000  173  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 31.966 22.118 85   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.399 15.000 258  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 18.424 15.000 12   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.131  0.200  191  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  1645 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.020  316  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 1.720  1.428  689  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 1.717  1.426  688  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 2.102  2.155  863  ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 2.396  3.000  2836 ? r_rigid_bond_restr     ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.1900 
_refine_ls_shell.d_res_low                        1.2210 
_refine_ls_shell.number_reflns_all                2896 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             139 
_refine_ls_shell.number_reflns_R_work             2757 
_refine_ls_shell.percent_reflns_obs               74.4500 
_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                  0.3040 
_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                  0.3270 
# 
_struct.entry_id                     9GGV 
_struct.title                        'Human KRas4A (GDP) in complex with compound 14' 
_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        9GGV 
_struct_keywords.text            'RAS, GTPase, inhibitor, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G 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              9GGV 
_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 9GGV GLY A 1   ? UNP P01116 ?   ?   'expression tag'      -2  1 
1 9GGV GLY A 2   ? UNP P01116 ?   ?   'expression tag'      -1  2 
1 9GGV SER A 3   ? UNP P01116 ?   ?   'expression tag'      0   3 
1 9GGV SER A 121 ? UNP P01116 CYS 118 'engineered mutation' 118 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1170 ? 
1 MORE         -15  ? 
1 'SSA (A^2)'  8310 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 18  ? ASN A 29  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2 AA2 SER A 68  ? GLY A 78  ? SER A 65  GLY A 75  1 ? 11 
HELX_P HELX_P3 AA3 ASN A 89  ? ASP A 108 ? ASN A 86  ASP A 105 1 ? 20 
HELX_P HELX_P4 AA4 ASP A 129 ? GLY A 141 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P5 AA5 ARG A 154 ? LEU A 171 ? ARG A 151 LEU A 168 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A SER 20 OG  ? ? ? 1_555 C MG  . MG ? ? A SER 17  A MG  202 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
metalc2 metalc ? ? B GDP .  O1B ? ? ? 1_555 C MG  . MG ? ? A GDP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.131 ? ? 
metalc3 metalc ? ? C MG  .  MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 307 1_555 ? ? ? ? ? ? ? 2.137 ? ? 
metalc4 metalc ? ? C MG  .  MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 311 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc5 metalc ? ? C MG  .  MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 340 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc6 metalc ? ? C MG  .  MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 347 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
# 
_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 93.7  ? 
2  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 307 ? 1_555 92.4  ? 
3  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 307 ? 1_555 84.8  ? 
4  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 311 ? 1_555 81.9  ? 
5  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 311 ? 1_555 96.2  ? 
6  O   ? G HOH .  ? A HOH 307 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 311 ? 1_555 174.2 ? 
7  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 340 ? 1_555 172.2 ? 
8  O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 340 ? 1_555 88.1  ? 
9  O   ? G HOH .  ? A HOH 307 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 340 ? 1_555 95.3  ? 
10 O   ? G HOH .  ? A HOH 311 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 340 ? 1_555 90.4  ? 
11 OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 347 ? 1_555 90.2  ? 
12 O1B ? B GDP .  ? A GDP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 347 ? 1_555 170.2 ? 
13 O   ? G HOH .  ? A HOH 307 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 347 ? 1_555 86.0  ? 
14 O   ? G HOH .  ? A HOH 311 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 347 ? 1_555 93.2  ? 
15 O   ? G HOH .  ? A HOH 340 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH . ? A HOH 347 ? 1_555 89.3  ? 
# 
_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 55  ? O LEU A 52  N THR A 5   ? N THR A 2   
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                   9GGV 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 68 ? ? CZ A ARG 68 ? ? NH1 A ARG 68 ? ? 126.69 120.30 6.39  0.50 N 
2 1 NE A ARG 68 ? ? CZ A ARG 68 ? ? NH2 A ARG 68 ? ? 113.72 120.30 -6.58 0.50 N 
3 1 CB A TYR 96 ? B CG A TYR 96 ? B CD1 A TYR 96 ? B 117.21 121.00 -3.79 0.60 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  ? ? -158.61 68.11  
2 1 ALA A 59  ? ? -105.43 -83.85 
3 1 LYS A 117 ? ? 71.28   38.98  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY -2 ? A GLY 1 
2 1 Y 1 A GLY -1 ? A GLY 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1IK9 CBF    C  N N 1   
A1IK9 CBG    C  N N 2   
A1IK9 NBH    N  N N 3   
A1IK9 CBI    C  N N 4   
A1IK9 CBJ    C  N N 5   
A1IK9 CBE    C  N N 6   
A1IK9 NAC    N  N N 7   
A1IK9 CAD    C  N N 8   
A1IK9 CAE    C  N N 9   
A1IK9 OAF    O  N N 10  
A1IK9 CAB    C  N N 11  
A1IK9 OAA    O  N N 12  
A1IK9 CAY    C  Y N 13  
A1IK9 CAZ    C  Y N 14  
A1IK9 CAX    C  Y N 15  
A1IK9 OAW    O  N N 16  
A1IK9 CBC    C  Y N 17  
A1IK9 CBB    C  Y N 18  
A1IK9 CBA    C  Y N 19  
A1IK9 SAH    S  N N 20  
A1IK9 OAG    O  N N 21  
A1IK9 OBD    O  N N 22  
A1IK9 NAI    N  N N 23  
A1IK9 CAJ    C  Y N 24  
A1IK9 SAK    S  Y N 25  
A1IK9 CAL    C  Y N 26  
A1IK9 CAM    C  Y N 27  
A1IK9 CLAR   CL N N 28  
A1IK9 CAN    C  Y N 29  
A1IK9 CAO    C  Y N 30  
A1IK9 CAP    C  Y N 31  
A1IK9 OAQ    O  N N 32  
A1IK9 CAS    C  Y N 33  
A1IK9 NAV    N  Y N 34  
A1IK9 CAU    C  N N 35  
A1IK9 CAT    C  N N 36  
A1IK9 H1     H  N N 37  
A1IK9 H2     H  N N 38  
A1IK9 H3     H  N N 39  
A1IK9 H4     H  N N 40  
A1IK9 H5     H  N N 41  
A1IK9 H7     H  N N 42  
A1IK9 H8     H  N N 43  
A1IK9 H9     H  N N 44  
A1IK9 H10    H  N N 45  
A1IK9 H11    H  N N 46  
A1IK9 H12    H  N N 47  
A1IK9 H13    H  N N 48  
A1IK9 H14    H  N N 49  
A1IK9 H15    H  N N 50  
A1IK9 H16    H  N N 51  
A1IK9 H17    H  N N 52  
A1IK9 H18    H  N N 53  
A1IK9 H19    H  N N 54  
A1IK9 H20    H  N N 55  
A1IK9 H21    H  N N 56  
A1IK9 H22    H  N N 57  
A1IK9 H23    H  N N 58  
A1IK9 H24    H  N N 59  
A1IK9 H25    H  N N 60  
A1IK9 H26    H  N N 61  
A1IK9 H27    H  N N 62  
A1IK9 H28    H  N N 63  
A1IK9 H29    H  N N 64  
ALA   N      N  N N 65  
ALA   CA     C  N S 66  
ALA   C      C  N N 67  
ALA   O      O  N N 68  
ALA   CB     C  N N 69  
ALA   OXT    O  N N 70  
ALA   H      H  N N 71  
ALA   H2     H  N N 72  
ALA   HA     H  N N 73  
ALA   HB1    H  N N 74  
ALA   HB2    H  N N 75  
ALA   HB3    H  N N 76  
ALA   HXT    H  N N 77  
ARG   N      N  N N 78  
ARG   CA     C  N S 79  
ARG   C      C  N N 80  
ARG   O      O  N N 81  
ARG   CB     C  N N 82  
ARG   CG     C  N N 83  
ARG   CD     C  N N 84  
ARG   NE     N  N N 85  
ARG   CZ     C  N N 86  
ARG   NH1    N  N N 87  
ARG   NH2    N  N N 88  
ARG   OXT    O  N N 89  
ARG   H      H  N N 90  
ARG   H2     H  N N 91  
ARG   HA     H  N N 92  
ARG   HB2    H  N N 93  
ARG   HB3    H  N N 94  
ARG   HG2    H  N N 95  
ARG   HG3    H  N N 96  
ARG   HD2    H  N N 97  
ARG   HD3    H  N N 98  
ARG   HE     H  N N 99  
ARG   HH11   H  N N 100 
ARG   HH12   H  N N 101 
ARG   HH21   H  N N 102 
ARG   HH22   H  N N 103 
ARG   HXT    H  N N 104 
ASN   N      N  N N 105 
ASN   CA     C  N S 106 
ASN   C      C  N N 107 
ASN   O      O  N N 108 
ASN   CB     C  N N 109 
ASN   CG     C  N N 110 
ASN   OD1    O  N N 111 
ASN   ND2    N  N N 112 
ASN   OXT    O  N N 113 
ASN   H      H  N N 114 
ASN   H2     H  N N 115 
ASN   HA     H  N N 116 
ASN   HB2    H  N N 117 
ASN   HB3    H  N N 118 
ASN   HD21   H  N N 119 
ASN   HD22   H  N N 120 
ASN   HXT    H  N N 121 
ASP   N      N  N N 122 
ASP   CA     C  N S 123 
ASP   C      C  N N 124 
ASP   O      O  N N 125 
ASP   CB     C  N N 126 
ASP   CG     C  N N 127 
ASP   OD1    O  N N 128 
ASP   OD2    O  N N 129 
ASP   OXT    O  N N 130 
ASP   H      H  N N 131 
ASP   H2     H  N N 132 
ASP   HA     H  N N 133 
ASP   HB2    H  N N 134 
ASP   HB3    H  N N 135 
ASP   HD2    H  N N 136 
ASP   HXT    H  N N 137 
CYS   N      N  N N 138 
CYS   CA     C  N R 139 
CYS   C      C  N N 140 
CYS   O      O  N N 141 
CYS   CB     C  N N 142 
CYS   SG     S  N N 143 
CYS   OXT    O  N N 144 
CYS   H      H  N N 145 
CYS   H2     H  N N 146 
CYS   HA     H  N N 147 
CYS   HB2    H  N N 148 
CYS   HB3    H  N N 149 
CYS   HG     H  N N 150 
CYS   HXT    H  N N 151 
EDO   C1     C  N N 152 
EDO   O1     O  N N 153 
EDO   C2     C  N N 154 
EDO   O2     O  N N 155 
EDO   H11    H  N N 156 
EDO   H12    H  N N 157 
EDO   HO1    H  N N 158 
EDO   H21    H  N N 159 
EDO   H22    H  N N 160 
EDO   HO2    H  N N 161 
GDP   PB     P  N N 162 
GDP   O1B    O  N N 163 
GDP   O2B    O  N N 164 
GDP   O3B    O  N N 165 
GDP   O3A    O  N N 166 
GDP   PA     P  N N 167 
GDP   O1A    O  N N 168 
GDP   O2A    O  N N 169 
GDP   "O5'"  O  N N 170 
GDP   "C5'"  C  N N 171 
GDP   "C4'"  C  N R 172 
GDP   "O4'"  O  N N 173 
GDP   "C3'"  C  N S 174 
GDP   "O3'"  O  N N 175 
GDP   "C2'"  C  N R 176 
GDP   "O2'"  O  N N 177 
GDP   "C1'"  C  N R 178 
GDP   N9     N  Y N 179 
GDP   C8     C  Y N 180 
GDP   N7     N  Y N 181 
GDP   C5     C  Y N 182 
GDP   C6     C  N N 183 
GDP   O6     O  N N 184 
GDP   N1     N  N N 185 
GDP   C2     C  N N 186 
GDP   N2     N  N N 187 
GDP   N3     N  N N 188 
GDP   C4     C  Y N 189 
GDP   HOB2   H  N N 190 
GDP   HOB3   H  N N 191 
GDP   HOA2   H  N N 192 
GDP   "H5'"  H  N N 193 
GDP   "H5''" H  N N 194 
GDP   "H4'"  H  N N 195 
GDP   "H3'"  H  N N 196 
GDP   "HO3'" H  N N 197 
GDP   "H2'"  H  N N 198 
GDP   "HO2'" H  N N 199 
GDP   "H1'"  H  N N 200 
GDP   H8     H  N N 201 
GDP   HN1    H  N N 202 
GDP   HN21   H  N N 203 
GDP   HN22   H  N N 204 
GLN   N      N  N N 205 
GLN   CA     C  N S 206 
GLN   C      C  N N 207 
GLN   O      O  N N 208 
GLN   CB     C  N N 209 
GLN   CG     C  N N 210 
GLN   CD     C  N N 211 
GLN   OE1    O  N N 212 
GLN   NE2    N  N N 213 
GLN   OXT    O  N N 214 
GLN   H      H  N N 215 
GLN   H2     H  N N 216 
GLN   HA     H  N N 217 
GLN   HB2    H  N N 218 
GLN   HB3    H  N N 219 
GLN   HG2    H  N N 220 
GLN   HG3    H  N N 221 
GLN   HE21   H  N N 222 
GLN   HE22   H  N N 223 
GLN   HXT    H  N N 224 
GLU   N      N  N N 225 
GLU   CA     C  N S 226 
GLU   C      C  N N 227 
GLU   O      O  N N 228 
GLU   CB     C  N N 229 
GLU   CG     C  N N 230 
GLU   CD     C  N N 231 
GLU   OE1    O  N N 232 
GLU   OE2    O  N N 233 
GLU   OXT    O  N N 234 
GLU   H      H  N N 235 
GLU   H2     H  N N 236 
GLU   HA     H  N N 237 
GLU   HB2    H  N N 238 
GLU   HB3    H  N N 239 
GLU   HG2    H  N N 240 
GLU   HG3    H  N N 241 
GLU   HE2    H  N N 242 
GLU   HXT    H  N N 243 
GLY   N      N  N N 244 
GLY   CA     C  N N 245 
GLY   C      C  N N 246 
GLY   O      O  N N 247 
GLY   OXT    O  N N 248 
GLY   H      H  N N 249 
GLY   H2     H  N N 250 
GLY   HA2    H  N N 251 
GLY   HA3    H  N N 252 
GLY   HXT    H  N N 253 
HIS   N      N  N N 254 
HIS   CA     C  N S 255 
HIS   C      C  N N 256 
HIS   O      O  N N 257 
HIS   CB     C  N N 258 
HIS   CG     C  Y N 259 
HIS   ND1    N  Y N 260 
HIS   CD2    C  Y N 261 
HIS   CE1    C  Y N 262 
HIS   NE2    N  Y N 263 
HIS   OXT    O  N N 264 
HIS   H      H  N N 265 
HIS   H2     H  N N 266 
HIS   HA     H  N N 267 
HIS   HB2    H  N N 268 
HIS   HB3    H  N N 269 
HIS   HD1    H  N N 270 
HIS   HD2    H  N N 271 
HIS   HE1    H  N N 272 
HIS   HE2    H  N N 273 
HIS   HXT    H  N N 274 
HOH   O      O  N N 275 
HOH   H1     H  N N 276 
HOH   H2     H  N N 277 
ILE   N      N  N N 278 
ILE   CA     C  N S 279 
ILE   C      C  N N 280 
ILE   O      O  N N 281 
ILE   CB     C  N S 282 
ILE   CG1    C  N N 283 
ILE   CG2    C  N N 284 
ILE   CD1    C  N N 285 
ILE   OXT    O  N N 286 
ILE   H      H  N N 287 
ILE   H2     H  N N 288 
ILE   HA     H  N N 289 
ILE   HB     H  N N 290 
ILE   HG12   H  N N 291 
ILE   HG13   H  N N 292 
ILE   HG21   H  N N 293 
ILE   HG22   H  N N 294 
ILE   HG23   H  N N 295 
ILE   HD11   H  N N 296 
ILE   HD12   H  N N 297 
ILE   HD13   H  N N 298 
ILE   HXT    H  N N 299 
LEU   N      N  N N 300 
LEU   CA     C  N S 301 
LEU   C      C  N N 302 
LEU   O      O  N N 303 
LEU   CB     C  N N 304 
LEU   CG     C  N N 305 
LEU   CD1    C  N N 306 
LEU   CD2    C  N N 307 
LEU   OXT    O  N N 308 
LEU   H      H  N N 309 
LEU   H2     H  N N 310 
LEU   HA     H  N N 311 
LEU   HB2    H  N N 312 
LEU   HB3    H  N N 313 
LEU   HG     H  N N 314 
LEU   HD11   H  N N 315 
LEU   HD12   H  N N 316 
LEU   HD13   H  N N 317 
LEU   HD21   H  N N 318 
LEU   HD22   H  N N 319 
LEU   HD23   H  N N 320 
LEU   HXT    H  N N 321 
LYS   N      N  N N 322 
LYS   CA     C  N S 323 
LYS   C      C  N N 324 
LYS   O      O  N N 325 
LYS   CB     C  N N 326 
LYS   CG     C  N N 327 
LYS   CD     C  N N 328 
LYS   CE     C  N N 329 
LYS   NZ     N  N N 330 
LYS   OXT    O  N N 331 
LYS   H      H  N N 332 
LYS   H2     H  N N 333 
LYS   HA     H  N N 334 
LYS   HB2    H  N N 335 
LYS   HB3    H  N N 336 
LYS   HG2    H  N N 337 
LYS   HG3    H  N N 338 
LYS   HD2    H  N N 339 
LYS   HD3    H  N N 340 
LYS   HE2    H  N N 341 
LYS   HE3    H  N N 342 
LYS   HZ1    H  N N 343 
LYS   HZ2    H  N N 344 
LYS   HZ3    H  N N 345 
LYS   HXT    H  N N 346 
MET   N      N  N N 347 
MET   CA     C  N S 348 
MET   C      C  N N 349 
MET   O      O  N N 350 
MET   CB     C  N N 351 
MET   CG     C  N N 352 
MET   SD     S  N N 353 
MET   CE     C  N N 354 
MET   OXT    O  N N 355 
MET   H      H  N N 356 
MET   H2     H  N N 357 
MET   HA     H  N N 358 
MET   HB2    H  N N 359 
MET   HB3    H  N N 360 
MET   HG2    H  N N 361 
MET   HG3    H  N N 362 
MET   HE1    H  N N 363 
MET   HE2    H  N N 364 
MET   HE3    H  N N 365 
MET   HXT    H  N N 366 
MG    MG     MG N N 367 
PHE   N      N  N N 368 
PHE   CA     C  N S 369 
PHE   C      C  N N 370 
PHE   O      O  N N 371 
PHE   CB     C  N N 372 
PHE   CG     C  Y N 373 
PHE   CD1    C  Y N 374 
PHE   CD2    C  Y N 375 
PHE   CE1    C  Y N 376 
PHE   CE2    C  Y N 377 
PHE   CZ     C  Y N 378 
PHE   OXT    O  N N 379 
PHE   H      H  N N 380 
PHE   H2     H  N N 381 
PHE   HA     H  N N 382 
PHE   HB2    H  N N 383 
PHE   HB3    H  N N 384 
PHE   HD1    H  N N 385 
PHE   HD2    H  N N 386 
PHE   HE1    H  N N 387 
PHE   HE2    H  N N 388 
PHE   HZ     H  N N 389 
PHE   HXT    H  N N 390 
PRO   N      N  N N 391 
PRO   CA     C  N S 392 
PRO   C      C  N N 393 
PRO   O      O  N N 394 
PRO   CB     C  N N 395 
PRO   CG     C  N N 396 
PRO   CD     C  N N 397 
PRO   OXT    O  N N 398 
PRO   H      H  N N 399 
PRO   HA     H  N N 400 
PRO   HB2    H  N N 401 
PRO   HB3    H  N N 402 
PRO   HG2    H  N N 403 
PRO   HG3    H  N N 404 
PRO   HD2    H  N N 405 
PRO   HD3    H  N N 406 
PRO   HXT    H  N N 407 
SER   N      N  N N 408 
SER   CA     C  N S 409 
SER   C      C  N N 410 
SER   O      O  N N 411 
SER   CB     C  N N 412 
SER   OG     O  N N 413 
SER   OXT    O  N N 414 
SER   H      H  N N 415 
SER   H2     H  N N 416 
SER   HA     H  N N 417 
SER   HB2    H  N N 418 
SER   HB3    H  N N 419 
SER   HG     H  N N 420 
SER   HXT    H  N N 421 
THR   N      N  N N 422 
THR   CA     C  N S 423 
THR   C      C  N N 424 
THR   O      O  N N 425 
THR   CB     C  N R 426 
THR   OG1    O  N N 427 
THR   CG2    C  N N 428 
THR   OXT    O  N N 429 
THR   H      H  N N 430 
THR   H2     H  N N 431 
THR   HA     H  N N 432 
THR   HB     H  N N 433 
THR   HG1    H  N N 434 
THR   HG21   H  N N 435 
THR   HG22   H  N N 436 
THR   HG23   H  N N 437 
THR   HXT    H  N N 438 
TYR   N      N  N N 439 
TYR   CA     C  N S 440 
TYR   C      C  N N 441 
TYR   O      O  N N 442 
TYR   CB     C  N N 443 
TYR   CG     C  Y N 444 
TYR   CD1    C  Y N 445 
TYR   CD2    C  Y N 446 
TYR   CE1    C  Y N 447 
TYR   CE2    C  Y N 448 
TYR   CZ     C  Y N 449 
TYR   OH     O  N N 450 
TYR   OXT    O  N N 451 
TYR   H      H  N N 452 
TYR   H2     H  N N 453 
TYR   HA     H  N N 454 
TYR   HB2    H  N N 455 
TYR   HB3    H  N N 456 
TYR   HD1    H  N N 457 
TYR   HD2    H  N N 458 
TYR   HE1    H  N N 459 
TYR   HE2    H  N N 460 
TYR   HH     H  N N 461 
TYR   HXT    H  N N 462 
VAL   N      N  N N 463 
VAL   CA     C  N S 464 
VAL   C      C  N N 465 
VAL   O      O  N N 466 
VAL   CB     C  N N 467 
VAL   CG1    C  N N 468 
VAL   CG2    C  N N 469 
VAL   OXT    O  N N 470 
VAL   H      H  N N 471 
VAL   H2     H  N N 472 
VAL   HA     H  N N 473 
VAL   HB     H  N N 474 
VAL   HG11   H  N N 475 
VAL   HG12   H  N N 476 
VAL   HG13   H  N N 477 
VAL   HG21   H  N N 478 
VAL   HG22   H  N N 479 
VAL   HG23   H  N N 480 
VAL   HXT    H  N N 481 
# 
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 
A1IK9 OAQ   CAP    sing N N 1   
A1IK9 CAO   CAP    doub Y N 2   
A1IK9 CAO   CAN    sing Y N 3   
A1IK9 CAP   CAS    sing Y N 4   
A1IK9 CAN   CAM    doub Y N 5   
A1IK9 CAU   CAT    sing N N 6   
A1IK9 CAU   NAV    sing N N 7   
A1IK9 CAS   NAV    sing Y N 8   
A1IK9 CAS   CAL    doub Y N 9   
A1IK9 NAV   CAJ    doub Y N 10  
A1IK9 OAF   CAE    sing N N 11  
A1IK9 CAM   CAL    sing Y N 12  
A1IK9 CAM   CLAR   sing N N 13  
A1IK9 CAL   SAK    sing Y N 14  
A1IK9 CAE   CAD    sing N N 15  
A1IK9 CAJ   NAI    sing N N 16  
A1IK9 CAJ   SAK    sing Y N 17  
A1IK9 CBG   CBF    sing N N 18  
A1IK9 CBG   NBH    sing N N 19  
A1IK9 CBF   CBE    sing N N 20  
A1IK9 NAI   SAH    sing N N 21  
A1IK9 CAD   NAC    sing N N 22  
A1IK9 NBH   CBI    sing N N 23  
A1IK9 CBE   NAC    sing N N 24  
A1IK9 CBE   CBJ    sing N N 25  
A1IK9 NAC   CAB    sing N N 26  
A1IK9 SAH   OBD    doub N N 27  
A1IK9 SAH   CBA    sing N N 28  
A1IK9 SAH   OAG    doub N N 29  
A1IK9 CBJ   CBI    sing N N 30  
A1IK9 CAZ   CBA    doub Y N 31  
A1IK9 CAZ   CAY    sing Y N 32  
A1IK9 CAB   CAY    sing N N 33  
A1IK9 CAB   OAA    doub N N 34  
A1IK9 CBA   CBB    sing Y N 35  
A1IK9 CAY   CAX    doub Y N 36  
A1IK9 CBB   CBC    doub Y N 37  
A1IK9 CAX   CBC    sing Y N 38  
A1IK9 CAX   OAW    sing N N 39  
A1IK9 CBF   H1     sing N N 40  
A1IK9 CBF   H2     sing N N 41  
A1IK9 CBG   H3     sing N N 42  
A1IK9 CBG   H4     sing N N 43  
A1IK9 NBH   H5     sing N N 44  
A1IK9 CBI   H7     sing N N 45  
A1IK9 CBI   H8     sing N N 46  
A1IK9 CBJ   H9     sing N N 47  
A1IK9 CBJ   H10    sing N N 48  
A1IK9 CBE   H11    sing N N 49  
A1IK9 CAD   H12    sing N N 50  
A1IK9 CAD   H13    sing N N 51  
A1IK9 CAE   H14    sing N N 52  
A1IK9 CAE   H15    sing N N 53  
A1IK9 OAF   H16    sing N N 54  
A1IK9 CAZ   H17    sing N N 55  
A1IK9 OAW   H18    sing N N 56  
A1IK9 CBC   H19    sing N N 57  
A1IK9 CBB   H20    sing N N 58  
A1IK9 NAI   H21    sing N N 59  
A1IK9 CAN   H22    sing N N 60  
A1IK9 CAO   H23    sing N N 61  
A1IK9 OAQ   H24    sing N N 62  
A1IK9 CAU   H25    sing N N 63  
A1IK9 CAU   H26    sing N N 64  
A1IK9 CAT   H27    sing N N 65  
A1IK9 CAT   H28    sing N N 66  
A1IK9 CAT   H29    sing N N 67  
ALA   N     CA     sing N N 68  
ALA   N     H      sing N N 69  
ALA   N     H2     sing N N 70  
ALA   CA    C      sing N N 71  
ALA   CA    CB     sing N N 72  
ALA   CA    HA     sing N N 73  
ALA   C     O      doub N N 74  
ALA   C     OXT    sing N N 75  
ALA   CB    HB1    sing N N 76  
ALA   CB    HB2    sing N N 77  
ALA   CB    HB3    sing N N 78  
ALA   OXT   HXT    sing N N 79  
ARG   N     CA     sing N N 80  
ARG   N     H      sing N N 81  
ARG   N     H2     sing N N 82  
ARG   CA    C      sing N N 83  
ARG   CA    CB     sing N N 84  
ARG   CA    HA     sing N N 85  
ARG   C     O      doub N N 86  
ARG   C     OXT    sing N N 87  
ARG   CB    CG     sing N N 88  
ARG   CB    HB2    sing N N 89  
ARG   CB    HB3    sing N N 90  
ARG   CG    CD     sing N N 91  
ARG   CG    HG2    sing N N 92  
ARG   CG    HG3    sing N N 93  
ARG   CD    NE     sing N N 94  
ARG   CD    HD2    sing N N 95  
ARG   CD    HD3    sing N N 96  
ARG   NE    CZ     sing N N 97  
ARG   NE    HE     sing N N 98  
ARG   CZ    NH1    sing N N 99  
ARG   CZ    NH2    doub N N 100 
ARG   NH1   HH11   sing N N 101 
ARG   NH1   HH12   sing N N 102 
ARG   NH2   HH21   sing N N 103 
ARG   NH2   HH22   sing N N 104 
ARG   OXT   HXT    sing N N 105 
ASN   N     CA     sing N N 106 
ASN   N     H      sing N N 107 
ASN   N     H2     sing N N 108 
ASN   CA    C      sing N N 109 
ASN   CA    CB     sing N N 110 
ASN   CA    HA     sing N N 111 
ASN   C     O      doub N N 112 
ASN   C     OXT    sing N N 113 
ASN   CB    CG     sing N N 114 
ASN   CB    HB2    sing N N 115 
ASN   CB    HB3    sing N N 116 
ASN   CG    OD1    doub N N 117 
ASN   CG    ND2    sing N N 118 
ASN   ND2   HD21   sing N N 119 
ASN   ND2   HD22   sing N N 120 
ASN   OXT   HXT    sing N N 121 
ASP   N     CA     sing N N 122 
ASP   N     H      sing N N 123 
ASP   N     H2     sing N N 124 
ASP   CA    C      sing N N 125 
ASP   CA    CB     sing N N 126 
ASP   CA    HA     sing N N 127 
ASP   C     O      doub N N 128 
ASP   C     OXT    sing N N 129 
ASP   CB    CG     sing N N 130 
ASP   CB    HB2    sing N N 131 
ASP   CB    HB3    sing N N 132 
ASP   CG    OD1    doub N N 133 
ASP   CG    OD2    sing N N 134 
ASP   OD2   HD2    sing N N 135 
ASP   OXT   HXT    sing N N 136 
CYS   N     CA     sing N N 137 
CYS   N     H      sing N N 138 
CYS   N     H2     sing N N 139 
CYS   CA    C      sing N N 140 
CYS   CA    CB     sing N N 141 
CYS   CA    HA     sing N N 142 
CYS   C     O      doub N N 143 
CYS   C     OXT    sing N N 144 
CYS   CB    SG     sing N N 145 
CYS   CB    HB2    sing N N 146 
CYS   CB    HB3    sing N N 147 
CYS   SG    HG     sing N N 148 
CYS   OXT   HXT    sing N N 149 
EDO   C1    O1     sing N N 150 
EDO   C1    C2     sing N N 151 
EDO   C1    H11    sing N N 152 
EDO   C1    H12    sing N N 153 
EDO   O1    HO1    sing N N 154 
EDO   C2    O2     sing N N 155 
EDO   C2    H21    sing N N 156 
EDO   C2    H22    sing N N 157 
EDO   O2    HO2    sing N N 158 
GDP   PB    O1B    doub N N 159 
GDP   PB    O2B    sing N N 160 
GDP   PB    O3B    sing N N 161 
GDP   PB    O3A    sing N N 162 
GDP   O2B   HOB2   sing N N 163 
GDP   O3B   HOB3   sing N N 164 
GDP   O3A   PA     sing N N 165 
GDP   PA    O1A    doub N N 166 
GDP   PA    O2A    sing N N 167 
GDP   PA    "O5'"  sing N N 168 
GDP   O2A   HOA2   sing N N 169 
GDP   "O5'" "C5'"  sing N N 170 
GDP   "C5'" "C4'"  sing N N 171 
GDP   "C5'" "H5'"  sing N N 172 
GDP   "C5'" "H5''" sing N N 173 
GDP   "C4'" "O4'"  sing N N 174 
GDP   "C4'" "C3'"  sing N N 175 
GDP   "C4'" "H4'"  sing N N 176 
GDP   "O4'" "C1'"  sing N N 177 
GDP   "C3'" "O3'"  sing N N 178 
GDP   "C3'" "C2'"  sing N N 179 
GDP   "C3'" "H3'"  sing N N 180 
GDP   "O3'" "HO3'" sing N N 181 
GDP   "C2'" "O2'"  sing N N 182 
GDP   "C2'" "C1'"  sing N N 183 
GDP   "C2'" "H2'"  sing N N 184 
GDP   "O2'" "HO2'" sing N N 185 
GDP   "C1'" N9     sing N N 186 
GDP   "C1'" "H1'"  sing N N 187 
GDP   N9    C8     sing Y N 188 
GDP   N9    C4     sing Y N 189 
GDP   C8    N7     doub Y N 190 
GDP   C8    H8     sing N N 191 
GDP   N7    C5     sing Y N 192 
GDP   C5    C6     sing N N 193 
GDP   C5    C4     doub Y N 194 
GDP   C6    O6     doub N N 195 
GDP   C6    N1     sing N N 196 
GDP   N1    C2     sing N N 197 
GDP   N1    HN1    sing N N 198 
GDP   C2    N2     sing N N 199 
GDP   C2    N3     doub N N 200 
GDP   N2    HN21   sing N N 201 
GDP   N2    HN22   sing N N 202 
GDP   N3    C4     sing N N 203 
GLN   N     CA     sing N N 204 
GLN   N     H      sing N N 205 
GLN   N     H2     sing N N 206 
GLN   CA    C      sing N N 207 
GLN   CA    CB     sing N N 208 
GLN   CA    HA     sing N N 209 
GLN   C     O      doub N N 210 
GLN   C     OXT    sing N N 211 
GLN   CB    CG     sing N N 212 
GLN   CB    HB2    sing N N 213 
GLN   CB    HB3    sing N N 214 
GLN   CG    CD     sing N N 215 
GLN   CG    HG2    sing N N 216 
GLN   CG    HG3    sing N N 217 
GLN   CD    OE1    doub N N 218 
GLN   CD    NE2    sing N N 219 
GLN   NE2   HE21   sing N N 220 
GLN   NE2   HE22   sing N N 221 
GLN   OXT   HXT    sing N N 222 
GLU   N     CA     sing N N 223 
GLU   N     H      sing N N 224 
GLU   N     H2     sing N N 225 
GLU   CA    C      sing N N 226 
GLU   CA    CB     sing N N 227 
GLU   CA    HA     sing N N 228 
GLU   C     O      doub N N 229 
GLU   C     OXT    sing N N 230 
GLU   CB    CG     sing N N 231 
GLU   CB    HB2    sing N N 232 
GLU   CB    HB3    sing N N 233 
GLU   CG    CD     sing N N 234 
GLU   CG    HG2    sing N N 235 
GLU   CG    HG3    sing N N 236 
GLU   CD    OE1    doub N N 237 
GLU   CD    OE2    sing N N 238 
GLU   OE2   HE2    sing N N 239 
GLU   OXT   HXT    sing N N 240 
GLY   N     CA     sing N N 241 
GLY   N     H      sing N N 242 
GLY   N     H2     sing N N 243 
GLY   CA    C      sing N N 244 
GLY   CA    HA2    sing N N 245 
GLY   CA    HA3    sing N N 246 
GLY   C     O      doub N N 247 
GLY   C     OXT    sing N N 248 
GLY   OXT   HXT    sing N N 249 
HIS   N     CA     sing N N 250 
HIS   N     H      sing N N 251 
HIS   N     H2     sing N N 252 
HIS   CA    C      sing N N 253 
HIS   CA    CB     sing N N 254 
HIS   CA    HA     sing N N 255 
HIS   C     O      doub N N 256 
HIS   C     OXT    sing N N 257 
HIS   CB    CG     sing N N 258 
HIS   CB    HB2    sing N N 259 
HIS   CB    HB3    sing N N 260 
HIS   CG    ND1    sing Y N 261 
HIS   CG    CD2    doub Y N 262 
HIS   ND1   CE1    doub Y N 263 
HIS   ND1   HD1    sing N N 264 
HIS   CD2   NE2    sing Y N 265 
HIS   CD2   HD2    sing N N 266 
HIS   CE1   NE2    sing Y N 267 
HIS   CE1   HE1    sing N N 268 
HIS   NE2   HE2    sing N N 269 
HIS   OXT   HXT    sing N N 270 
HOH   O     H1     sing N N 271 
HOH   O     H2     sing N N 272 
ILE   N     CA     sing N N 273 
ILE   N     H      sing N N 274 
ILE   N     H2     sing N N 275 
ILE   CA    C      sing N N 276 
ILE   CA    CB     sing N N 277 
ILE   CA    HA     sing N N 278 
ILE   C     O      doub N N 279 
ILE   C     OXT    sing N N 280 
ILE   CB    CG1    sing N N 281 
ILE   CB    CG2    sing N N 282 
ILE   CB    HB     sing N N 283 
ILE   CG1   CD1    sing N N 284 
ILE   CG1   HG12   sing N N 285 
ILE   CG1   HG13   sing N N 286 
ILE   CG2   HG21   sing N N 287 
ILE   CG2   HG22   sing N N 288 
ILE   CG2   HG23   sing N N 289 
ILE   CD1   HD11   sing N N 290 
ILE   CD1   HD12   sing N N 291 
ILE   CD1   HD13   sing N N 292 
ILE   OXT   HXT    sing N N 293 
LEU   N     CA     sing N N 294 
LEU   N     H      sing N N 295 
LEU   N     H2     sing N N 296 
LEU   CA    C      sing N N 297 
LEU   CA    CB     sing N N 298 
LEU   CA    HA     sing N N 299 
LEU   C     O      doub N N 300 
LEU   C     OXT    sing N N 301 
LEU   CB    CG     sing N N 302 
LEU   CB    HB2    sing N N 303 
LEU   CB    HB3    sing N N 304 
LEU   CG    CD1    sing N N 305 
LEU   CG    CD2    sing N N 306 
LEU   CG    HG     sing N N 307 
LEU   CD1   HD11   sing N N 308 
LEU   CD1   HD12   sing N N 309 
LEU   CD1   HD13   sing N N 310 
LEU   CD2   HD21   sing N N 311 
LEU   CD2   HD22   sing N N 312 
LEU   CD2   HD23   sing N N 313 
LEU   OXT   HXT    sing N N 314 
LYS   N     CA     sing N N 315 
LYS   N     H      sing N N 316 
LYS   N     H2     sing N N 317 
LYS   CA    C      sing N N 318 
LYS   CA    CB     sing N N 319 
LYS   CA    HA     sing N N 320 
LYS   C     O      doub N N 321 
LYS   C     OXT    sing N N 322 
LYS   CB    CG     sing N N 323 
LYS   CB    HB2    sing N N 324 
LYS   CB    HB3    sing N N 325 
LYS   CG    CD     sing N N 326 
LYS   CG    HG2    sing N N 327 
LYS   CG    HG3    sing N N 328 
LYS   CD    CE     sing N N 329 
LYS   CD    HD2    sing N N 330 
LYS   CD    HD3    sing N N 331 
LYS   CE    NZ     sing N N 332 
LYS   CE    HE2    sing N N 333 
LYS   CE    HE3    sing N N 334 
LYS   NZ    HZ1    sing N N 335 
LYS   NZ    HZ2    sing N N 336 
LYS   NZ    HZ3    sing N N 337 
LYS   OXT   HXT    sing N N 338 
MET   N     CA     sing N N 339 
MET   N     H      sing N N 340 
MET   N     H2     sing N N 341 
MET   CA    C      sing N N 342 
MET   CA    CB     sing N N 343 
MET   CA    HA     sing N N 344 
MET   C     O      doub N N 345 
MET   C     OXT    sing N N 346 
MET   CB    CG     sing N N 347 
MET   CB    HB2    sing N N 348 
MET   CB    HB3    sing N N 349 
MET   CG    SD     sing N N 350 
MET   CG    HG2    sing N N 351 
MET   CG    HG3    sing N N 352 
MET   SD    CE     sing N N 353 
MET   CE    HE1    sing N N 354 
MET   CE    HE2    sing N N 355 
MET   CE    HE3    sing N N 356 
MET   OXT   HXT    sing N N 357 
PHE   N     CA     sing N N 358 
PHE   N     H      sing N N 359 
PHE   N     H2     sing N N 360 
PHE   CA    C      sing N N 361 
PHE   CA    CB     sing N N 362 
PHE   CA    HA     sing N N 363 
PHE   C     O      doub N N 364 
PHE   C     OXT    sing N N 365 
PHE   CB    CG     sing N N 366 
PHE   CB    HB2    sing N N 367 
PHE   CB    HB3    sing N N 368 
PHE   CG    CD1    doub Y N 369 
PHE   CG    CD2    sing Y N 370 
PHE   CD1   CE1    sing Y N 371 
PHE   CD1   HD1    sing N N 372 
PHE   CD2   CE2    doub Y N 373 
PHE   CD2   HD2    sing N N 374 
PHE   CE1   CZ     doub Y N 375 
PHE   CE1   HE1    sing N N 376 
PHE   CE2   CZ     sing Y N 377 
PHE   CE2   HE2    sing N N 378 
PHE   CZ    HZ     sing N N 379 
PHE   OXT   HXT    sing N N 380 
PRO   N     CA     sing N N 381 
PRO   N     CD     sing N N 382 
PRO   N     H      sing N N 383 
PRO   CA    C      sing N N 384 
PRO   CA    CB     sing N N 385 
PRO   CA    HA     sing N N 386 
PRO   C     O      doub N N 387 
PRO   C     OXT    sing N N 388 
PRO   CB    CG     sing N N 389 
PRO   CB    HB2    sing N N 390 
PRO   CB    HB3    sing N N 391 
PRO   CG    CD     sing N N 392 
PRO   CG    HG2    sing N N 393 
PRO   CG    HG3    sing N N 394 
PRO   CD    HD2    sing N N 395 
PRO   CD    HD3    sing N N 396 
PRO   OXT   HXT    sing N N 397 
SER   N     CA     sing N N 398 
SER   N     H      sing N N 399 
SER   N     H2     sing N N 400 
SER   CA    C      sing N N 401 
SER   CA    CB     sing N N 402 
SER   CA    HA     sing N N 403 
SER   C     O      doub N N 404 
SER   C     OXT    sing N N 405 
SER   CB    OG     sing N N 406 
SER   CB    HB2    sing N N 407 
SER   CB    HB3    sing N N 408 
SER   OG    HG     sing N N 409 
SER   OXT   HXT    sing N N 410 
THR   N     CA     sing N N 411 
THR   N     H      sing N N 412 
THR   N     H2     sing N N 413 
THR   CA    C      sing N N 414 
THR   CA    CB     sing N N 415 
THR   CA    HA     sing N N 416 
THR   C     O      doub N N 417 
THR   C     OXT    sing N N 418 
THR   CB    OG1    sing N N 419 
THR   CB    CG2    sing N N 420 
THR   CB    HB     sing N N 421 
THR   OG1   HG1    sing N N 422 
THR   CG2   HG21   sing N N 423 
THR   CG2   HG22   sing N N 424 
THR   CG2   HG23   sing N N 425 
THR   OXT   HXT    sing N N 426 
TYR   N     CA     sing N N 427 
TYR   N     H      sing N N 428 
TYR   N     H2     sing N N 429 
TYR   CA    C      sing N N 430 
TYR   CA    CB     sing N N 431 
TYR   CA    HA     sing N N 432 
TYR   C     O      doub N N 433 
TYR   C     OXT    sing N N 434 
TYR   CB    CG     sing N N 435 
TYR   CB    HB2    sing N N 436 
TYR   CB    HB3    sing N N 437 
TYR   CG    CD1    doub Y N 438 
TYR   CG    CD2    sing Y N 439 
TYR   CD1   CE1    sing Y N 440 
TYR   CD1   HD1    sing N N 441 
TYR   CD2   CE2    doub Y N 442 
TYR   CD2   HD2    sing N N 443 
TYR   CE1   CZ     doub Y N 444 
TYR   CE1   HE1    sing N N 445 
TYR   CE2   CZ     sing Y N 446 
TYR   CE2   HE2    sing N N 447 
TYR   CZ    OH     sing N N 448 
TYR   OH    HH     sing N N 449 
TYR   OXT   HXT    sing N N 450 
VAL   N     CA     sing N N 451 
VAL   N     H      sing N N 452 
VAL   N     H2     sing N N 453 
VAL   CA    C      sing N N 454 
VAL   CA    CB     sing N N 455 
VAL   CA    HA     sing N N 456 
VAL   C     O      doub N N 457 
VAL   C     OXT    sing N N 458 
VAL   CB    CG1    sing N N 459 
VAL   CB    CG2    sing N N 460 
VAL   CB    HB     sing N N 461 
VAL   CG1   HG11   sing N N 462 
VAL   CG1   HG12   sing N N 463 
VAL   CG1   HG13   sing N N 464 
VAL   CG2   HG21   sing N N 465 
VAL   CG2   HG22   sing N N 466 
VAL   CG2   HG23   sing N N 467 
VAL   OXT   HXT    sing N N 468 
# 
_pdbx_audit_support.funding_organization   'Cancer Research UK' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'unreleased crystal structure' 
# 
_atom_sites.entry_id                    9GGV 
_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]   0.027057 
_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]   0.024827 
_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]   0.009036 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . SER   A 1 3   ? -18.799 22.504 -7.275 1.00 39.78 ? 0   SER   A N     1 
ATOM   2    C  CA    . SER   A 1 3   ? -18.284 21.125 -7.028 1.00 34.30 ? 0   SER   A CA    1 
ATOM   3    C  C     . SER   A 1 3   ? -16.979 21.230 -6.232 1.00 32.33 ? 0   SER   A C     1 
ATOM   4    O  O     . SER   A 1 3   ? -15.933 21.290 -6.799 1.00 33.38 ? 0   SER   A O     1 
ATOM   5    C  CB    . SER   A 1 3   ? -18.145 20.280 -8.272 1.00 35.58 ? 0   SER   A CB    1 
ATOM   6    O  OG    . SER   A 1 3   ? -17.539 19.062 -7.938 1.00 38.88 ? 0   SER   A OG    1 
ATOM   7    N  N     . MET   A 1 4   ? -17.127 21.291 -4.926 1.00 29.93 ? 1   MET   A N     1 
ATOM   8    C  CA    . MET   A 1 4   ? -16.009 21.533 -4.008 1.00 26.71 ? 1   MET   A CA    1 
ATOM   9    C  C     . MET   A 1 4   ? -16.427 21.039 -2.621 1.00 23.08 ? 1   MET   A C     1 
ATOM   10   O  O     . MET   A 1 4   ? -17.565 21.227 -2.241 1.00 26.49 ? 1   MET   A O     1 
ATOM   11   C  CB    . MET   A 1 4   ? -15.930 23.047 -3.936 1.00 32.58 ? 1   MET   A CB    1 
ATOM   12   C  CG    . MET   A 1 4   ? -14.999 23.500 -2.968 1.00 30.77 ? 1   MET   A CG    1 
ATOM   13   S  SD    . MET   A 1 4   ? -13.710 24.239 -3.810 1.00 24.47 ? 1   MET   A SD    1 
ATOM   14   C  CE    . MET   A 1 4   ? -14.255 24.308 -5.513 1.00 26.40 ? 1   MET   A CE    1 
ATOM   15   N  N     . THR   A 1 5   ? -15.467 20.516 -1.870 1.00 19.75 ? 2   THR   A N     1 
ATOM   16   C  CA    . THR   A 1 5   ? -15.792 20.068 -0.507 1.00 19.57 ? 2   THR   A CA    1 
ATOM   17   C  C     . THR   A 1 5   ? -14.815 20.785 0.413  1.00 17.82 ? 2   THR   A C     1 
ATOM   18   O  O     . THR   A 1 5   ? -13.697 20.844 0.052  1.00 19.25 ? 2   THR   A O     1 
ATOM   19   C  CB    . THR   A 1 5   ? -15.613 18.559 -0.490 1.00 18.16 ? 2   THR   A CB    1 
ATOM   20   O  OG1   . THR   A 1 5   ? -16.564 18.004 -1.396 1.00 19.36 ? 2   THR   A OG1   1 
ATOM   21   C  CG2   . THR   A 1 5   ? -15.837 17.949 0.869  1.00 18.72 ? 2   THR   A CG2   1 
ATOM   22   N  N     . GLU   A 1 6   ? -15.278 21.242 1.566  1.00 14.63 ? 3   GLU   A N     1 
ATOM   23   C  CA    . GLU   A 1 6   ? -14.401 21.928 2.546  1.00 15.32 ? 3   GLU   A CA    1 
ATOM   24   C  C     . GLU   A 1 6   ? -13.895 20.934 3.609  1.00 13.16 ? 3   GLU   A C     1 
ATOM   25   O  O     . GLU   A 1 6   ? -14.610 20.056 4.001  1.00 16.59 ? 3   GLU   A O     1 
ATOM   26   C  CB    . GLU   A 1 6   ? -15.202 23.022 3.231  1.00 19.76 ? 3   GLU   A CB    1 
ATOM   27   C  CG    . GLU   A 1 6   ? -14.406 23.917 4.148  1.00 26.33 ? 3   GLU   A CG    1 
ATOM   28   C  CD    . GLU   A 1 6   ? -15.244 25.057 4.686  1.00 34.79 ? 3   GLU   A CD    1 
ATOM   29   O  OE1   . GLU   A 1 6   ? -14.725 25.794 5.508  1.00 43.64 ? 3   GLU   A OE1   1 
ATOM   30   O  OE2   . GLU   A 1 6   ? -16.427 25.171 4.266  1.00 41.31 ? 3   GLU   A OE2   1 
ATOM   31   N  N     . TYR   A 1 7   ? -12.665 21.153 4.056  1.00 11.50 ? 4   TYR   A N     1 
ATOM   32   C  CA    . TYR   A 1 7   ? -12.023 20.362 5.118  1.00 11.09 ? 4   TYR   A CA    1 
ATOM   33   C  C     . TYR   A 1 7   ? -11.317 21.307 6.079  1.00 12.25 ? 4   TYR   A C     1 
ATOM   34   O  O     . TYR   A 1 7   ? -10.413 22.015 5.673  1.00 12.75 ? 4   TYR   A O     1 
ATOM   35   C  CB    . TYR   A 1 7   ? -10.983 19.422 4.511  1.00 10.70 ? 4   TYR   A CB    1 
ATOM   36   C  CG    . TYR   A 1 7   ? -11.570 18.353 3.634  1.00 10.34 ? 4   TYR   A CG    1 
ATOM   37   C  CD1   . TYR   A 1 7   ? -11.794 18.570 2.281  1.00 11.49 ? 4   TYR   A CD1   1 
ATOM   38   C  CD2   . TYR   A 1 7   ? -11.940 17.150 4.162  1.00 12.33 ? 4   TYR   A CD2   1 
ATOM   39   C  CE1   . TYR   A 1 7   ? -12.368 17.583 1.479  1.00 10.73 ? 4   TYR   A CE1   1 
ATOM   40   C  CE2   . TYR   A 1 7   ? -12.490 16.153 3.381  1.00 12.17 ? 4   TYR   A CE2   1 
ATOM   41   C  CZ    . TYR   A 1 7   ? -12.737 16.378 2.046  1.00 11.65 ? 4   TYR   A CZ    1 
ATOM   42   O  OH    . TYR   A 1 7   ? -13.305 15.360 1.320  1.00 13.61 ? 4   TYR   A OH    1 
ATOM   43   N  N     . LYS   A 1 8   ? -11.758 21.320 7.325  1.00 10.75 ? 5   LYS   A N     1 
ATOM   44   C  CA    . LYS   A 1 8   ? -11.160 22.172 8.370  1.00 11.67 ? 5   LYS   A CA    1 
ATOM   45   C  C     . LYS   A 1 8   ? -10.092 21.398 9.105  1.00 10.07 ? 5   LYS   A C     1 
ATOM   46   O  O     . LYS   A 1 8   ? -10.414 20.451 9.803  1.00 11.22 ? 5   LYS   A O     1 
ATOM   47   C  CB    . LYS   A 1 8   ? -12.231 22.688 9.333  1.00 13.21 ? 5   LYS   A CB    1 
ATOM   48   C  CG    . LYS   A 1 8   ? -13.268 23.591 8.675  1.00 17.78 ? 5   LYS   A CG    1 
ATOM   49   C  CD    . LYS   A 1 8   ? -14.222 24.218 9.664  1.00 23.07 ? 5   LYS   A CD    1 
ATOM   50   C  CE    . LYS   A 1 8   ? -15.300 25.026 8.955  1.00 27.73 ? 5   LYS   A CE    1 
ATOM   51   N  NZ    . LYS   A 1 8   ? -16.413 24.161 8.497  1.00 39.22 ? 5   LYS   A NZ    1 
ATOM   52   N  N     . LEU   A 1 9   ? -8.844  21.808 8.919  1.00 9.50  ? 6   LEU   A N     1 
ATOM   53   C  CA    . LEU   A 1 9   ? -7.695  21.086 9.452  1.00 9.86  ? 6   LEU   A CA    1 
ATOM   54   C  C     . LEU   A 1 9   ? -7.051  21.930 10.531 1.00 10.63 ? 6   LEU   A C     1 
ATOM   55   O  O     . LEU   A 1 9   ? -7.003  23.174 10.417 1.00 12.68 ? 6   LEU   A O     1 
ATOM   56   C  CB    . LEU   A 1 9   ? -6.680  20.798 8.351  1.00 10.03 ? 6   LEU   A CB    1 
ATOM   57   C  CG    . LEU   A 1 9   ? -7.248  20.137 7.087  1.00 11.52 ? 6   LEU   A CG    1 
ATOM   58   C  CD1   . LEU   A 1 9   ? -6.119  19.809 6.127  1.00 12.25 ? 6   LEU   A CD1   1 
ATOM   59   C  CD2   . LEU   A 1 9   ? -8.092  18.897 7.357  1.00 11.87 ? 6   LEU   A CD2   1 
ATOM   60   N  N     . VAL   A 1 10  ? -6.517  21.277 11.554 1.00 9.64  ? 7   VAL   A N     1 
ATOM   61   C  CA    . VAL   A 1 10  ? -5.831  21.972 12.651 1.00 10.39 ? 7   VAL   A CA    1 
ATOM   62   C  C     . VAL   A 1 10  ? -4.473  21.324 12.847 1.00 9.39  ? 7   VAL   A C     1 
ATOM   63   O  O     . VAL   A 1 10  ? -4.393  20.088 13.008 1.00 10.24 ? 7   VAL   A O     1 
ATOM   64   C  CB    . VAL   A 1 10  ? -6.670  21.891 13.943 1.00 10.72 ? 7   VAL   A CB    1 
ATOM   65   C  CG1   . VAL   A 1 10  ? -6.001  22.659 15.074 1.00 11.61 ? 7   VAL   A CG1   1 
ATOM   66   C  CG2   . VAL   A 1 10  ? -8.076  22.462 13.727 1.00 12.23 ? 7   VAL   A CG2   1 
ATOM   67   N  N     . VAL   A 1 11  ? -3.415  22.128 12.879 1.00 9.15  ? 8   VAL   A N     1 
ATOM   68   C  CA    . VAL   A 1 11  ? -2.058  21.637 13.079 1.00 8.88  ? 8   VAL   A CA    1 
ATOM   69   C  C     . VAL   A 1 11  ? -1.648  21.920 14.517 1.00 9.41  ? 8   VAL   A C     1 
ATOM   70   O  O     . VAL   A 1 11  ? -1.627  23.106 14.906 1.00 9.77  ? 8   VAL   A O     1 
ATOM   71   C  CB    . VAL   A 1 11  ? -1.071  22.302 12.101 1.00 10.05 ? 8   VAL   A CB    1 
ATOM   72   C  CG1   . VAL   A 1 11  ? 0.306   21.673 12.218 1.00 10.38 ? 8   VAL   A CG1   1 
ATOM   73   C  CG2   . VAL   A 1 11  ? -1.566  22.229 10.660 1.00 10.15 ? 8   VAL   A CG2   1 
ATOM   74   N  N     . VAL   A 1 12  ? -1.386  20.869 15.290 1.00 9.36  ? 9   VAL   A N     1 
ATOM   75   C  CA    . VAL   A 1 12  ? -1.012  20.971 16.698 1.00 9.57  ? 9   VAL   A CA    1 
ATOM   76   C  C     . VAL   A 1 12  ? 0.323   20.276 16.938 1.00 9.35  ? 9   VAL   A C     1 
ATOM   77   O  O     . VAL   A 1 12  ? 0.777   19.468 16.097 1.00 10.15 ? 9   VAL   A O     1 
ATOM   78   C  CB    . VAL   A 1 12  ? -2.103  20.377 17.625 1.00 10.79 ? 9   VAL   A CB    1 
ATOM   79   C  CG1   . VAL   A 1 12  ? -3.444  21.042 17.371 1.00 11.82 ? 9   VAL   A CG1   1 
ATOM   80   C  CG2   . VAL   A 1 12  ? -2.257  18.870 17.467 1.00 11.77 ? 9   VAL   A CG2   1 
ATOM   81   N  N     . GLY   A 1 13  ? 0.918   20.544 18.105 1.00 9.58  ? 10  GLY   A N     1 
ATOM   82   C  CA    . GLY   A 1 13  ? 2.226   20.034 18.415 1.00 10.64 ? 10  GLY   A CA    1 
ATOM   83   C  C     . GLY   A 1 13  ? 3.016   21.014 19.230 1.00 11.36 ? 10  GLY   A C     1 
ATOM   84   O  O     . GLY   A 1 13  ? 2.702   22.217 19.227 1.00 11.32 ? 10  GLY   A O     1 
ATOM   85   N  N     . ALA   A 1 14  ? 4.048   20.500 19.900 1.00 10.73 ? 11  ALA   A N     1 
ATOM   86   C  CA    . ALA   A 1 14  ? 4.833   21.323 20.794 1.00 11.61 ? 11  ALA   A CA    1 
ATOM   87   C  C     . ALA   A 1 14  ? 5.492   22.473 20.032 1.00 12.39 ? 11  ALA   A C     1 
ATOM   88   O  O     . ALA   A 1 14  ? 5.757   22.402 18.843 1.00 12.39 ? 11  ALA   A O     1 
ATOM   89   C  CB    . ALA   A 1 14  ? 5.871   20.456 21.479 1.00 12.65 ? 11  ALA   A CB    1 
ATOM   90   N  N     . GLY   A 1 15  ? 5.779   23.545 20.766 1.00 13.16 ? 12  GLY   A N     1 
ATOM   91   C  CA    . GLY   A 1 15  ? 6.535   24.624 20.216 1.00 13.71 ? 12  GLY   A CA    1 
ATOM   92   C  C     . GLY   A 1 15  ? 7.819   24.133 19.581 1.00 14.14 ? 12  GLY   A C     1 
ATOM   93   O  O     . GLY   A 1 15  ? 8.548   23.313 20.144 1.00 15.83 ? 12  GLY   A O     1 
ATOM   94   N  N     . GLY   A 1 16  ? 8.071   24.617 18.378 1.00 13.66 ? 13  GLY   A N     1 
ATOM   95   C  CA    . GLY   A 1 16  ? 9.301   24.303 17.688 1.00 12.92 ? 13  GLY   A CA    1 
ATOM   96   C  C     . GLY   A 1 16  ? 9.319   23.043 16.832 1.00 12.88 ? 13  GLY   A C     1 
ATOM   97   O  O     . GLY   A 1 16  ? 10.342  22.756 16.222 1.00 14.00 ? 13  GLY   A O     1 
ATOM   98   N  N     . VAL   A 1 17  ? 8.224   22.291 16.758 1.00 11.45 ? 14  VAL   A N     1 
ATOM   99   C  CA    . VAL   A 1 17  ? 8.260   21.058 15.974 1.00 10.24 ? 14  VAL   A CA    1 
ATOM   100  C  C     . VAL   A 1 17  ? 8.183   21.267 14.464 1.00 10.12 ? 14  VAL   A C     1 
ATOM   101  O  O     . VAL   A 1 17  ? 8.540   20.354 13.711 1.00 10.34 ? 14  VAL   A O     1 
ATOM   102  C  CB    . VAL   A 1 17  ? 7.173   20.062 16.411 1.00 10.33 ? 14  VAL   A CB    1 
ATOM   103  C  CG1   . VAL   A 1 17  ? 7.381   19.623 17.869 1.00 10.38 ? 14  VAL   A CG1   1 
ATOM   104  C  CG2   . VAL   A 1 17  ? 5.756   20.579 16.130 1.00 10.28 ? 14  VAL   A CG2   1 
ATOM   105  N  N     . GLY   A 1 18  ? 7.661   22.422 14.049 1.00 11.23 ? 15  GLY   A N     1 
ATOM   106  C  CA    . GLY   A 1 18  ? 7.479   22.764 12.633 1.00 10.73 ? 15  GLY   A CA    1 
ATOM   107  C  C     . GLY   A 1 18  ? 6.062   22.912 12.140 1.00 10.74 ? 15  GLY   A C     1 
ATOM   108  O  O     . GLY   A 1 18  ? 5.824   22.771 10.943 1.00 11.58 ? 15  GLY   A O     1 
ATOM   109  N  N     . LYS   A 1 19  ? 5.118   23.245 13.012 1.00 10.92 ? 16  LYS   A N     1 
ATOM   110  C  CA    . LYS   A 1 19  ? 3.731   23.477 12.603 1.00 11.46 ? 16  LYS   A CA    1 
ATOM   111  C  C     . LYS   A 1 19  ? 3.624   24.568 11.543 1.00 11.13 ? 16  LYS   A C     1 
ATOM   112  O  O     . LYS   A 1 19  ? 3.022   24.364 10.480 1.00 12.35 ? 16  LYS   A O     1 
ATOM   113  C  CB    . LYS   A 1 19  ? 2.883   23.865 13.784 1.00 12.60 ? 16  LYS   A CB    1 
ATOM   114  C  CG    . LYS   A 1 19  ? 2.798   22.831 14.895 1.00 12.00 ? 16  LYS   A CG    1 
ATOM   115  C  CD    . LYS   A 1 19  ? 1.965   23.349 16.053 1.00 14.73 ? 16  LYS   A CD    1 
ATOM   116  C  CE    . LYS   A 1 19  ? 2.520   24.556 16.770 1.00 14.19 ? 16  LYS   A CE    1 
ATOM   117  N  NZ    . LYS   A 1 19  ? 3.781   24.230 17.484 1.00 13.79 ? 16  LYS   A NZ    1 
ATOM   118  N  N     . SER   A 1 20  ? 4.253   25.710 11.828 1.00 11.74 ? 17  SER   A N     1 
ATOM   119  C  CA    . SER   A 1 20  ? 4.238   26.813 10.894 1.00 12.57 ? 17  SER   A CA    1 
ATOM   120  C  C     . SER   A 1 20  ? 4.984   26.505 9.625  1.00 13.07 ? 17  SER   A C     1 
ATOM   121  O  O     . SER   A 1 20  ? 4.508   26.796 8.526  1.00 13.99 ? 17  SER   A O     1 
ATOM   122  C  CB    . SER   A 1 20  ? 4.792   28.088 11.530 1.00 13.92 ? 17  SER   A CB    1 
ATOM   123  O  OG    . SER   A 1 20  ? 3.955   28.498 12.601 1.00 14.23 ? 17  SER   A OG    1 
ATOM   124  N  N     . ALA   A 1 21  ? 6.175   25.925 9.752  1.00 11.77 ? 18  ALA   A N     1 
ATOM   125  C  CA    . ALA   A 1 21  ? 6.973   25.620 8.566  1.00 13.12 ? 18  ALA   A CA    1 
ATOM   126  C  C     . ALA   A 1 21  ? 6.249   24.649 7.633  1.00 12.30 ? 18  ALA   A C     1 
ATOM   127  O  O     . ALA   A 1 21  ? 6.325   24.775 6.411  1.00 14.76 ? 18  ALA   A O     1 
ATOM   128  C  CB    . ALA   A 1 21  ? 8.311   25.065 8.930  1.00 13.74 ? 18  ALA   A CB    1 
ATOM   129  N  N     . LEU   A 1 22  ? 5.581   23.622 8.204  1.00 12.22 ? 19  LEU   A N     1 
ATOM   130  C  CA    . LEU   A 1 22  ? 4.784   22.696 7.376  1.00 12.48 ? 19  LEU   A CA    1 
ATOM   131  C  C     . LEU   A 1 22  ? 3.649   23.391 6.663  1.00 11.34 ? 19  LEU   A C     1 
ATOM   132  O  O     . LEU   A 1 22  ? 3.437   23.186 5.456  1.00 13.29 ? 19  LEU   A O     1 
ATOM   133  C  CB    . LEU   A 1 22  ? 4.221   21.586 8.245  1.00 12.22 ? 19  LEU   A CB    1 
ATOM   134  C  CG    . LEU   A 1 22  ? 5.234   20.495 8.622  1.00 12.21 ? 19  LEU   A CG    1 
ATOM   135  C  CD1   . LEU   A 1 22  ? 4.671   19.631 9.725  1.00 12.12 ? 19  LEU   A CD1   1 
ATOM   136  C  CD2   . LEU   A 1 22  ? 5.655   19.635 7.444  1.00 12.95 ? 19  LEU   A CD2   1 
ATOM   137  N  N     . THR   A 1 23  ? 2.914   24.216 7.380  1.00 12.32 ? 20  THR   A N     1 
ATOM   138  C  CA    . THR   A 1 23  ? 1.730   24.901 6.818  1.00 13.71 ? 20  THR   A CA    1 
ATOM   139  C  C     . THR   A 1 23  ? 2.158   25.877 5.720  1.00 13.53 ? 20  THR   A C     1 
ATOM   140  O  O     . THR   A 1 23  ? 1.561   25.898 4.658  1.00 14.86 ? 20  THR   A O     1 
ATOM   141  C  CB    . THR   A 1 23  ? 0.930   25.612 7.912  1.00 13.64 ? 20  THR   A CB    1 
ATOM   142  O  OG1   . THR   A 1 23  ? 0.573   24.665 8.912  1.00 13.85 ? 20  THR   A OG1   1 
ATOM   143  C  CG2   . THR   A 1 23  ? -0.344  26.218 7.363  1.00 15.13 ? 20  THR   A CG2   1 
ATOM   144  N  N     . ILE   A 1 24  ? 3.182   26.651 6.012  1.00 14.81 ? 21  ILE   A N     1 
ATOM   145  C  CA    . ILE   A 1 24  ? 3.687   27.645 5.027  1.00 16.01 ? 21  ILE   A CA    1 
ATOM   146  C  C     . ILE   A 1 24  ? 4.264   26.909 3.814  1.00 15.20 ? 21  ILE   A C     1 
ATOM   147  O  O     . ILE   A 1 24  ? 4.062   27.381 2.724  1.00 18.46 ? 21  ILE   A O     1 
ATOM   148  C  CB    . ILE   A 1 24  ? 4.639   28.641 5.717  1.00 17.13 ? 21  ILE   A CB    1 
ATOM   149  C  CG1   . ILE   A 1 24  ? 3.857   29.481 6.730  1.00 19.19 ? 21  ILE   A CG1   1 
ATOM   150  C  CG2   . ILE   A 1 24  ? 5.336   29.494 4.673  1.00 17.77 ? 21  ILE   A CG2   1 
ATOM   151  C  CD1   . ILE   A 1 24  ? 4.729   30.201 7.740  1.00 20.97 ? 21  ILE   A CD1   1 
ATOM   152  N  N     . GLN   A 1 25  ? 4.965   25.794 4.005  1.00 15.57 ? 22  GLN   A N     1 
ATOM   153  C  CA    . GLN   A 1 25  ? 5.464   25.043 2.828  1.00 15.80 ? 22  GLN   A CA    1 
ATOM   154  C  C     . GLN   A 1 25  ? 4.300   24.588 1.958  1.00 16.10 ? 22  GLN   A C     1 
ATOM   155  O  O     . GLN   A 1 25  ? 4.363   24.710 0.773  1.00 17.89 ? 22  GLN   A O     1 
ATOM   156  C  CB    . GLN   A 1 25  ? 6.190   23.790 3.264  1.00 18.23 ? 22  GLN   A CB    1 
ATOM   157  C  CG    . GLN   A 1 25  ? 7.664   23.982 3.250  1.00 21.25 ? 22  GLN   A CG    1 
ATOM   158  C  CD    . GLN   A 1 25  ? 8.295   24.156 1.884  1.00 19.42 ? 22  GLN   A CD    1 
ATOM   159  O  OE1   . GLN   A 1 25  ? 7.686   24.457 0.861  1.00 21.74 ? 22  GLN   A OE1   1 
ATOM   160  N  NE2   . GLN   A 1 25  ? 9.575   23.931 1.891  1.00 18.65 ? 22  GLN   A NE2   1 
ATOM   161  N  N     . LEU   A 1 26  ? 3.290   24.061 2.599  1.00 15.87 ? 23  LEU   A N     1 
ATOM   162  C  CA    . LEU   A 1 26  ? 2.151   23.583 1.806  1.00 15.63 ? 23  LEU   A CA    1 
ATOM   163  C  C     . LEU   A 1 26  ? 1.545   24.745 1.005  1.00 16.94 ? 23  LEU   A C     1 
ATOM   164  O  O     . LEU   A 1 26  ? 1.358   24.604 -0.187 1.00 19.16 ? 23  LEU   A O     1 
ATOM   165  C  CB    . LEU   A 1 26  ? 1.114   23.001 2.756  1.00 14.82 ? 23  LEU   A CB    1 
ATOM   166  C  CG    . LEU   A 1 26  ? -0.128  22.518 2.020  1.00 16.65 ? 23  LEU   A CG    1 
ATOM   167  C  CD1   . LEU   A 1 26  ? 0.111   21.168 1.349  1.00 15.88 ? 23  LEU   A CD1   1 
ATOM   168  C  CD2   . LEU   A 1 26  ? -1.304  22.434 2.945  1.00 17.25 ? 23  LEU   A CD2   1 
ATOM   169  N  N     . ILE   A 1 27  ? 1.254   25.847 1.692  1.00 19.24 ? 24  ILE   A N     1 
ATOM   170  C  CA    . ILE   A 1 27  ? 0.469   26.971 1.101  1.00 21.47 ? 24  ILE   A CA    1 
ATOM   171  C  C     . ILE   A 1 27  ? 1.310   27.881 0.225  1.00 21.83 ? 24  ILE   A C     1 
ATOM   172  O  O     . ILE   A 1 27  ? 0.811   28.296 -0.810 1.00 23.98 ? 24  ILE   A O     1 
ATOM   173  C  CB    . ILE   A 1 27  ? -0.132  27.833 2.224  1.00 22.88 ? 24  ILE   A CB    1 
ATOM   174  C  CG1   . ILE   A 1 27  ? -1.054  27.019 3.115  1.00 23.70 ? 24  ILE   A CG1   1 
ATOM   175  C  CG2   . ILE   A 1 27  ? -0.869  29.037 1.640  1.00 25.83 ? 24  ILE   A CG2   1 
ATOM   176  C  CD1   . ILE   A 1 27  ? -2.232  26.457 2.412  1.00 24.78 ? 24  ILE   A CD1   1 
ATOM   177  N  N     . GLN   A 1 28  ? 2.523   28.142 0.635  1.00 21.30 ? 25  GLN   A N     1 
ATOM   178  C  CA    . GLN   A 1 28  ? 3.292   29.230 0.007  1.00 23.82 ? 25  GLN   A CA    1 
ATOM   179  C  C     . GLN   A 1 28  ? 4.567   28.703 -0.610 1.00 20.95 ? 25  GLN   A C     1 
ATOM   180  O  O     . GLN   A 1 28  ? 5.294   29.476 -1.182 1.00 25.72 ? 25  GLN   A O     1 
ATOM   181  C  CB    . GLN   A 1 28  ? 3.549   30.351 1.026  1.00 21.14 ? 25  GLN   A CB    1 
ATOM   182  C  CG    . GLN   A 1 28  ? 2.282   30.967 1.571  1.00 24.10 ? 25  GLN   A CG    1 
ATOM   183  C  CD    . GLN   A 1 28  ? 2.500   32.043 2.601  1.00 22.39 ? 25  GLN   A CD    1 
ATOM   184  O  OE1   . GLN   A 1 28  ? 3.600   32.433 2.895  1.00 26.21 ? 25  GLN   A OE1   1 
ATOM   185  N  NE2   . GLN   A 1 28  ? 1.406   32.567 3.100  1.00 29.53 ? 25  GLN   A NE2   1 
ATOM   186  N  N     . ASN   A 1 29  ? 4.815   27.401 -0.519 1.00 23.05 ? 26  ASN   A N     1 
ATOM   187  C  CA    . ASN   A 1 29  ? 5.985   26.800 -1.199 1.00 19.25 ? 26  ASN   A CA    1 
ATOM   188  C  C     . ASN   A 1 29  ? 7.325   27.449 -0.858 1.00 25.03 ? 26  ASN   A C     1 
ATOM   189  O  O     . ASN   A 1 29  ? 8.138   27.624 -1.745 1.00 30.11 ? 26  ASN   A O     1 
ATOM   190  C  CB    . ASN   A 1 29  ? 5.756   26.706 -2.714 1.00 23.03 ? 26  ASN   A CB    1 
ATOM   191  C  CG    . ASN   A 1 29  ? 6.785   25.893 -3.461 1.00 25.97 ? 26  ASN   A CG    1 
ATOM   192  O  OD1   . ASN   A 1 29  ? 7.396   24.970 -2.962 1.00 30.32 ? 26  ASN   A OD1   1 
ATOM   193  N  ND2   . ASN   A 1 29  ? 6.942   26.199 -4.736 1.00 32.03 ? 26  ASN   A ND2   1 
ATOM   194  N  N     . HIS   A 1 30  ? 7.518   27.752 0.409  1.00 21.46 ? 27  HIS   A N     1 
ATOM   195  C  CA    . HIS   A 1 30  ? 8.844   28.193 0.901  1.00 20.35 ? 27  HIS   A CA    1 
ATOM   196  C  C     . HIS   A 1 30  ? 9.024   27.659 2.325  1.00 21.31 ? 27  HIS   A C     1 
ATOM   197  O  O     . HIS   A 1 30  ? 8.051   27.392 2.992  1.00 18.88 ? 27  HIS   A O     1 
ATOM   198  C  CB    . HIS   A 1 30  ? 9.098   29.717 0.767  1.00 21.37 ? 27  HIS   A CB    1 
ATOM   199  C  CG    . HIS   A 1 30  ? 8.163   30.548 1.547  1.00 17.80 ? 27  HIS   A CG    1 
ATOM   200  N  ND1   . HIS   A 1 30  ? 8.530   31.137 2.696  1.00 19.94 ? 27  HIS   A ND1   1 
ATOM   201  C  CD2   . HIS   A 1 30  ? 6.875   30.828 1.363  1.00 20.84 ? 27  HIS   A CD2   1 
ATOM   202  C  CE1   . HIS   A 1 30  ? 7.496   31.773 3.183  1.00 21.81 ? 27  HIS   A CE1   1 
ATOM   203  N  NE2   . HIS   A 1 30  ? 6.475   31.610 2.388  1.00 24.87 ? 27  HIS   A NE2   1 
ATOM   204  N  N     . PHE   A 1 31  ? 10.268  27.575 2.734  1.00 22.49 ? 28  PHE   A N     1 
ATOM   205  C  CA    . PHE   A 1 31  ? 10.619  27.192 4.100  1.00 17.61 ? 28  PHE   A CA    1 
ATOM   206  C  C     . PHE   A 1 31  ? 10.990  28.383 4.979  1.00 23.20 ? 28  PHE   A C     1 
ATOM   207  O  O     . PHE   A 1 31  ? 11.887  29.158 4.622  1.00 25.61 ? 28  PHE   A O     1 
ATOM   208  C  CB    . PHE   A 1 31  ? 11.805  26.257 4.043  1.00 15.03 ? 28  PHE   A CB    1 
ATOM   209  C  CG    . PHE   A 1 31  ? 12.324  25.806 5.395  1.00 17.89 ? 28  PHE   A CG    1 
ATOM   210  C  CD1   . PHE   A 1 31  ? 11.515  25.083 6.278  1.00 18.73 ? 28  PHE   A CD1   1 
ATOM   211  C  CD2   . PHE   A 1 31  ? 13.655  26.024 5.764  1.00 19.95 ? 28  PHE   A CD2   1 
ATOM   212  C  CE1   . PHE   A 1 31  ? 11.996  24.640 7.506  1.00 19.71 ? 28  PHE   A CE1   1 
ATOM   213  C  CE2   . PHE   A 1 31  ? 14.130  25.589 6.992  1.00 19.88 ? 28  PHE   A CE2   1 
ATOM   214  C  CZ    . PHE   A 1 31  ? 13.306  24.879 7.855  1.00 19.76 ? 28  PHE   A CZ    1 
ATOM   215  N  N     . VAL   A 1 32  ? 10.334  28.506 6.122  1.00 20.04 ? 29  VAL   A N     1 
ATOM   216  C  CA    . VAL   A 1 32  ? 10.613  29.615 7.087  1.00 21.02 ? 29  VAL   A CA    1 
ATOM   217  C  C     . VAL   A 1 32  ? 11.564  29.114 8.174  1.00 25.60 ? 29  VAL   A C     1 
ATOM   218  O  O     . VAL   A 1 32  ? 11.267  28.124 8.807  1.00 27.79 ? 29  VAL   A O     1 
ATOM   219  C  CB    . VAL   A 1 32  ? 9.325   30.250 7.615  1.00 24.58 ? 29  VAL   A CB    1 
ATOM   220  C  CG1   . VAL   A 1 32  ? 8.665   31.024 6.501  1.00 26.82 ? 29  VAL   A CG1   1 
ATOM   221  C  CG2   . VAL   A 1 32  ? 8.368   29.236 8.214  1.00 24.79 ? 29  VAL   A CG2   1 
ATOM   222  N  N     . ASP   A 1 33  ? 12.708  29.797 8.282  1.00 32.98 ? 30  ASP   A N     1 
ATOM   223  C  CA    . ASP   A 1 33  ? 13.843  29.579 9.218  1.00 35.91 ? 30  ASP   A CA    1 
ATOM   224  C  C     . ASP   A 1 33  ? 13.502  29.928 10.662 1.00 38.55 ? 30  ASP   A C     1 
ATOM   225  O  O     . ASP   A 1 33  ? 14.109  29.330 11.534 1.00 50.44 ? 30  ASP   A O     1 
ATOM   226  C  CB    . ASP   A 1 33  ? 14.996  30.517 8.877  1.00 40.07 ? 30  ASP   A CB    1 
ATOM   227  C  CG    . ASP   A 1 33  ? 15.804  30.078 7.688  1.00 46.62 ? 30  ASP   A CG    1 
ATOM   228  O  OD1   . ASP   A 1 33  ? 15.748  28.895 7.392  1.00 60.62 ? 30  ASP   A OD1   1 
ATOM   229  O  OD2   . ASP   A 1 33  ? 16.497  30.927 7.083  1.00 59.34 ? 30  ASP   A OD2   1 
ATOM   230  N  N     . GLU   A 1 34  ? 12.693  30.944 10.911 1.00 36.37 ? 31  GLU   A N     1 
ATOM   231  C  CA    . GLU   A 1 34  ? 12.486  31.369 12.316 1.00 39.62 ? 31  GLU   A CA    1 
ATOM   232  C  C     . GLU   A 1 34  ? 11.184  32.152 12.466 1.00 36.20 ? 31  GLU   A C     1 
ATOM   233  O  O     . GLU   A 1 34  ? 11.188  33.329 12.812 1.00 41.65 ? 31  GLU   A O     1 
ATOM   234  C  CB    . GLU   A 1 34  ? 13.646  32.251 12.769 1.00 43.23 ? 31  GLU   A CB    1 
ATOM   235  C  CG    . GLU   A 1 34  ? 14.255  33.078 11.665 1.00 43.56 ? 31  GLU   A CG    1 
ATOM   236  C  CD    . GLU   A 1 34  ? 15.382  33.982 12.130 1.00 50.90 ? 31  GLU   A CD    1 
ATOM   237  O  OE1   . GLU   A 1 34  ? 15.180  34.655 13.136 1.00 57.54 ? 31  GLU   A OE1   1 
ATOM   238  O  OE2   . GLU   A 1 34  ? 16.434  34.006 11.481 1.00 61.79 ? 31  GLU   A OE2   1 
ATOM   239  N  N     . TYR   A 1 35  ? 10.093  31.451 12.292 1.00 25.09 ? 32  TYR   A N     1 
ATOM   240  C  CA    . TYR   A 1 35  ? 8.775   32.075 12.308 1.00 23.41 ? 32  TYR   A CA    1 
ATOM   241  C  C     . TYR   A 1 35  ? 8.322   32.270 13.748 1.00 21.01 ? 32  TYR   A C     1 
ATOM   242  O  O     . TYR   A 1 35  ? 8.429   31.336 14.521 1.00 22.02 ? 32  TYR   A O     1 
ATOM   243  C  CB    . TYR   A 1 35  ? 7.859   31.125 11.554 1.00 20.91 ? 32  TYR   A CB    1 
ATOM   244  C  CG    . TYR   A 1 35  ? 6.639   31.812 11.040 1.00 19.60 ? 32  TYR   A CG    1 
ATOM   245  C  CD1   . TYR   A 1 35  ? 6.752   32.699 9.996  1.00 23.28 ? 32  TYR   A CD1   1 
ATOM   246  C  CD2   . TYR   A 1 35  ? 5.404   31.622 11.608 1.00 19.72 ? 32  TYR   A CD2   1 
ATOM   247  C  CE1   . TYR   A 1 35  ? 5.650   33.364 9.517  1.00 23.47 ? 32  TYR   A CE1   1 
ATOM   248  C  CE2   . TYR   A 1 35  ? 4.293   32.288 11.150 1.00 21.59 ? 32  TYR   A CE2   1 
ATOM   249  C  CZ    . TYR   A 1 35  ? 4.420   33.145 10.078 1.00 22.41 ? 32  TYR   A CZ    1 
ATOM   250  O  OH    . TYR   A 1 35  ? 3.352   33.793 9.606  1.00 24.53 ? 32  TYR   A OH    1 
ATOM   251  N  N     . ASP   A 1 36  ? 7.867   33.497 14.025 1.00 22.51 ? 33  ASP   A N     1 
ATOM   252  C  CA    . ASP   A 1 36  ? 7.424   33.875 15.368 1.00 20.69 ? 33  ASP   A CA    1 
ATOM   253  C  C     . ASP   A 1 36  ? 6.502   32.784 15.925 1.00 20.16 ? 33  ASP   A C     1 
ATOM   254  O  O     . ASP   A 1 36  ? 5.451   32.503 15.322 1.00 20.75 ? 33  ASP   A O     1 
ATOM   255  C  CB    . ASP   A 1 36  ? 6.728   35.250 15.320 1.00 20.96 ? 33  ASP   A CB    1 
ATOM   256  C  CG    . ASP   A 1 36  ? 6.214   35.735 16.666 1.00 25.99 ? 33  ASP   A CG    1 
ATOM   257  O  OD1   . ASP   A 1 36  ? 6.075   34.951 17.628 1.00 24.57 ? 33  ASP   A OD1   1 
ATOM   258  O  OD2   . ASP   A 1 36  ? 5.909   36.952 16.744 1.00 28.96 ? 33  ASP   A OD2   1 
ATOM   259  N  N     . PRO   A 1 37  ? 6.887   32.164 17.058 1.00 19.82 ? 34  PRO   A N     1 
ATOM   260  C  CA    . PRO   A 1 37  ? 6.106   31.042 17.593 1.00 18.23 ? 34  PRO   A CA    1 
ATOM   261  C  C     . PRO   A 1 37  ? 4.731   31.390 18.129 1.00 17.60 ? 34  PRO   A C     1 
ATOM   262  O  O     . PRO   A 1 37  ? 3.944   30.476 18.381 1.00 20.14 ? 34  PRO   A O     1 
ATOM   263  C  CB    . PRO   A 1 37  ? 6.992   30.470 18.690 1.00 22.27 ? 34  PRO   A CB    1 
ATOM   264  C  CG    . PRO   A 1 37  ? 7.815   31.607 19.131 1.00 23.86 ? 34  PRO   A CG    1 
ATOM   265  C  CD    . PRO   A 1 37  ? 8.067   32.431 17.901 1.00 20.34 ? 34  PRO   A CD    1 
ATOM   266  N  N     . THR   A 1 38  ? 4.445   32.681 18.299 1.00 17.17 ? 35  THR   A N     1 
ATOM   267  C  CA    . THR   A 1 38  ? 3.157   33.122 18.822 1.00 17.47 ? 35  THR   A CA    1 
ATOM   268  C  C     . THR   A 1 38  ? 2.131   33.432 17.736 1.00 16.82 ? 35  THR   A C     1 
ATOM   269  O  O     . THR   A 1 38  ? 0.982   33.710 18.063 1.00 18.41 ? 35  THR   A O     1 
ATOM   270  C  CB    . THR   A 1 38  ? 3.307   34.386 19.714 1.00 20.79 ? 35  THR   A CB    1 
ATOM   271  O  OG1   . THR   A 1 38  ? 3.620   35.497 18.887 1.00 21.79 ? 35  THR   A OG1   1 
ATOM   272  C  CG2   . THR   A 1 38  ? 4.395   34.203 20.756 1.00 22.03 ? 35  THR   A CG2   1 
ATOM   273  N  N     . ILE   A 1 39  ? 2.524   33.367 16.459 1.00 15.76 ? 36  ILE   A N     1 
ATOM   274  C  CA    . ILE   A 1 39  ? 1.592   33.712 15.397 1.00 16.77 ? 36  ILE   A CA    1 
ATOM   275  C  C     . ILE   A 1 39  ? 0.654   32.533 15.114 1.00 15.09 ? 36  ILE   A C     1 
ATOM   276  O  O     . ILE   A 1 39  ? 1.123   31.427 14.799 1.00 14.81 ? 36  ILE   A O     1 
ATOM   277  C  CB    . ILE   A 1 39  ? 2.298   34.142 14.109 1.00 17.35 ? 36  ILE   A CB    1 
ATOM   278  C  CG1   . ILE   A 1 39  ? 3.135   35.408 14.339 1.00 16.06 ? 36  ILE   A CG1   1 
ATOM   279  C  CG2   . ILE   A 1 39  ? 1.270   34.365 12.997 1.00 19.77 ? 36  ILE   A CG2   1 
ATOM   280  C  CD1   . ILE   A 1 39  ? 3.921   35.837 13.121 1.00 18.46 ? 36  ILE   A CD1   1 
ATOM   281  N  N     . GLU   A 1 40  ? -0.651  32.774 15.233 1.00 15.97 ? 37  GLU   A N     1 
ATOM   282  C  CA    . GLU   A 1 40  ? -1.685  31.779 14.988 1.00 15.56 ? 37  GLU   A CA    1 
ATOM   283  C  C     . GLU   A 1 40  ? -2.539  32.337 13.862 1.00 16.23 ? 37  GLU   A C     1 
ATOM   284  O  O     . GLU   A 1 40  ? -3.096  33.410 13.981 1.00 18.55 ? 37  GLU   A O     1 
ATOM   285  C  CB    . GLU   A 1 40  ? -2.515  31.567 16.251 1.00 17.30 ? 37  GLU   A CB    1 
ATOM   286  C  CG    . GLU   A 1 40  ? -3.623  30.542 16.139 1.00 16.54 ? 37  GLU   A CG    1 
ATOM   287  C  CD    . GLU   A 1 40  ? -4.046  30.044 17.495 1.00 15.92 ? 37  GLU   A CD    1 
ATOM   288  O  OE1   . GLU   A 1 40  ? -3.293  29.246 18.087 1.00 17.36 ? 37  GLU   A OE1   1 
ATOM   289  O  OE2   . GLU   A 1 40  ? -5.100  30.486 18.007 1.00 19.50 ? 37  GLU   A OE2   1 
ATOM   290  N  N     . ASP   A 1 41  ? -2.610  31.630 12.753 1.00 17.22 ? 38  ASP   A N     1 
ATOM   291  C  CA    . ASP   A 1 41  ? -3.367  32.090 11.586 1.00 17.58 ? 38  ASP   A CA    1 
ATOM   292  C  C     . ASP   A 1 41  ? -3.991  30.913 10.868 1.00 15.87 ? 38  ASP   A C     1 
ATOM   293  O  O     . ASP   A 1 41  ? -3.546  29.762 11.046 1.00 15.86 ? 38  ASP   A O     1 
ATOM   294  C  CB    . ASP   A 1 41  ? -2.435  32.775 10.572 1.00 23.00 ? 38  ASP   A CB    1 
ATOM   295  C  CG    . ASP   A 1 41  ? -2.188  34.240 10.840 1.00 30.25 ? 38  ASP   A CG    1 
ATOM   296  O  OD1   . ASP   A 1 41  ? -3.138  35.008 11.111 1.00 31.36 ? 38  ASP   A OD1   1 
ATOM   297  O  OD2   . ASP   A 1 41  ? -1.009  34.637 10.713 1.00 33.25 ? 38  ASP   A OD2   1 
ATOM   298  N  N     . SER   A 1 42  ? -4.991  31.224 10.049 1.00 16.33 ? 39  SER   A N     1 
ATOM   299  C  CA    . SER   A 1 42  ? -5.576  30.245 9.144  1.00 14.90 ? 39  SER   A CA    1 
ATOM   300  C  C     . SER   A 1 42  ? -5.178  30.532 7.700  1.00 15.60 ? 39  SER   A C     1 
ATOM   301  O  O     . SER   A 1 42  ? -4.924  31.695 7.309  1.00 17.93 ? 39  SER   A O     1 
ATOM   302  C  CB    . SER   A 1 42  ? -7.087  30.170 9.302  1.00 17.35 ? 39  SER   A CB    1 
ATOM   303  O  OG    . SER   A 1 42  ? -7.712  31.347 8.854  1.00 21.10 ? 39  SER   A OG    1 
ATOM   304  N  N     . TYR   A 1 43  ? -5.128  29.452 6.907  1.00 15.21 ? 40  TYR   A N     1 
ATOM   305  C  CA    . TYR   A 1 43  ? -4.758  29.494 5.503  1.00 16.10 ? 40  TYR   A CA    1 
ATOM   306  C  C     . TYR   A 1 43  ? -5.755  28.651 4.722  1.00 15.38 ? 40  TYR   A C     1 
ATOM   307  O  O     . TYR   A 1 43  ? -6.129  27.568 5.146  1.00 15.96 ? 40  TYR   A O     1 
ATOM   308  C  CB    . TYR   A 1 43  ? -3.365  28.896 5.292  1.00 17.96 ? 40  TYR   A CB    1 
ATOM   309  C  CG    . TYR   A 1 43  ? -2.216  29.650 5.921  1.00 19.76 ? 40  TYR   A CG    1 
ATOM   310  C  CD1   . TYR   A 1 43  ? -1.922  29.513 7.268  1.00 18.93 ? 40  TYR   A CD1   1 
ATOM   311  C  CD2   . TYR   A 1 43  ? -1.421  30.491 5.151  1.00 25.39 ? 40  TYR   A CD2   1 
ATOM   312  C  CE1   . TYR   A 1 43  ? -0.861  30.205 7.842  1.00 21.71 ? 40  TYR   A CE1   1 
ATOM   313  C  CE2   . TYR   A 1 43  ? -0.371  31.189 5.715  1.00 25.85 ? 40  TYR   A CE2   1 
ATOM   314  C  CZ    . TYR   A 1 43  ? -0.096  31.041 7.063  1.00 24.13 ? 40  TYR   A CZ    1 
ATOM   315  O  OH    . TYR   A 1 43  ? 0.948   31.734 7.618  1.00 30.41 ? 40  TYR   A OH    1 
ATOM   316  N  N     . ARG   A 1 44  ? -6.170  29.141 3.567  1.00 16.86 ? 41  ARG   A N     1 
ATOM   317  C  CA    . ARG   A 1 44  ? -7.037  28.395 2.680  1.00 18.04 ? 41  ARG   A CA    1 
ATOM   318  C  C     . ARG   A 1 44  ? -6.416  28.161 1.347  1.00 21.86 ? 41  ARG   A C     1 
ATOM   319  O  O     . ARG   A 1 44  ? -5.685  28.995 0.800  1.00 26.21 ? 41  ARG   A O     1 
ATOM   320  C  CB    . ARG   A 1 44  ? -8.393  29.060 2.527  1.00 21.23 ? 41  ARG   A CB    1 
ATOM   321  C  CG    . ARG   A 1 44  ? -9.275  28.857 3.732  1.00 23.70 ? 41  ARG   A CG    1 
ATOM   322  C  CD    . ARG   A 1 44  ? -10.271 29.971 3.917  1.00 25.09 ? 41  ARG   A CD    1 
ATOM   323  N  NE    . ARG   A 1 44  ? -9.585  31.239 4.159  1.00 24.95 ? 41  ARG   A NE    1 
ATOM   324  C  CZ    . ARG   A 1 44  ? -8.934  31.568 5.273  1.00 24.73 ? 41  ARG   A CZ    1 
ATOM   325  N  NH1   . ARG   A 1 44  ? -8.870  30.732 6.303  1.00 24.46 ? 41  ARG   A NH1   1 
ATOM   326  N  NH2   . ARG   A 1 44  ? -8.338  32.757 5.372  1.00 27.13 ? 41  ARG   A NH2   1 
ATOM   327  N  N     . LYS   A 1 45  ? -6.743  27.015 0.780  1.00 18.45 ? 42  LYS   A N     1 
ATOM   328  C  CA    . LYS   A 1 45  ? -6.313  26.708 -0.558 1.00 18.61 ? 42  LYS   A CA    1 
ATOM   329  C  C     . LYS   A 1 45  ? -7.144  25.606 -1.134 1.00 17.29 ? 42  LYS   A C     1 
ATOM   330  O  O     . LYS   A 1 45  ? -7.449  24.640 -0.422 1.00 18.79 ? 42  LYS   A O     1 
ATOM   331  C  CB    . LYS   A 1 45  ? -4.886  26.209 -0.479 1.00 22.45 ? 42  LYS   A CB    1 
ATOM   332  C  CG    . LYS   A 1 45  ? -4.205  25.878 -1.787 1.00 25.55 ? 42  LYS   A CG    1 
ATOM   333  C  CD    . LYS   A 1 45  ? -3.012  24.988 -1.479 1.00 25.35 ? 42  LYS   A CD    1 
ATOM   334  C  CE    . LYS   A 1 45  ? -2.119  24.800 -2.675 1.00 30.94 ? 42  LYS   A CE    1 
ATOM   335  N  NZ    . LYS   A 1 45  ? -0.969  23.935 -2.303 1.00 33.90 ? 42  LYS   A NZ    1 
ATOM   336  N  N     . GLN   A 1 46  ? -7.475  25.749 -2.415 1.00 16.49 ? 43  GLN   A N     1 
ATOM   337  C  CA    . GLN   A 1 46  ? -8.080  24.696 -3.221 1.00 15.83 ? 43  GLN   A CA    1 
ATOM   338  C  C     . GLN   A 1 46  ? -7.056  23.725 -3.801 1.00 14.80 ? 43  GLN   A C     1 
ATOM   339  O  O     . GLN   A 1 46  ? -6.095  24.131 -4.458 1.00 16.02 ? 43  GLN   A O     1 
ATOM   340  C  CB    . GLN   A 1 46  ? -8.875  25.273 -4.390 1.00 21.22 ? 43  GLN   A CB    1 
ATOM   341  C  CG    . GLN   A 1 46  ? -10.307 25.671 -4.074 1.00 23.89 ? 43  GLN   A CG    1 
ATOM   342  C  CD    . GLN   A 1 46  ? -11.116 26.109 -5.310 1.00 25.74 ? 43  GLN   A CD    1 
ATOM   343  O  OE1   . GLN   A 1 46  ? -10.893 25.641 -6.423 1.00 23.62 ? 43  GLN   A OE1   1 
ATOM   344  N  NE2   . GLN   A 1 46  ? -12.074 27.008 -5.100 1.00 23.75 ? 43  GLN   A NE2   1 
ATOM   345  N  N     . VAL   A 1 47  ? -7.320  22.426 -3.642 1.00 13.45 ? 44  VAL   A N     1 
ATOM   346  C  CA    . VAL   A 1 47  ? -6.457  21.362 -4.181 1.00 14.52 ? 44  VAL   A CA    1 
ATOM   347  C  C     . VAL   A 1 47  ? -7.354  20.253 -4.738 1.00 13.17 ? 44  VAL   A C     1 
ATOM   348  O  O     . VAL   A 1 47  ? -8.515  20.187 -4.385 1.00 17.96 ? 44  VAL   A O     1 
ATOM   349  C  CB    . VAL   A 1 47  ? -5.509  20.772 -3.091 1.00 16.44 ? 44  VAL   A CB    1 
ATOM   350  C  CG1   . VAL   A 1 47  ? -4.565  21.823 -2.533 1.00 19.79 ? 44  VAL   A CG1   1 
ATOM   351  C  CG2   . VAL   A 1 47  ? -6.289  20.156 -1.951 1.00 18.39 ? 44  VAL   A CG2   1 
ATOM   352  N  N     . VAL   A 1 48  ? -6.806  19.375 -5.570 1.00 13.23 ? 45  VAL   A N     1 
ATOM   353  C  CA    . VAL   A 1 48  ? -7.543  18.202 -6.056 1.00 12.72 ? 45  VAL   A CA    1 
ATOM   354  C  C     . VAL   A 1 48  ? -6.935  16.956 -5.433 1.00 10.94 ? 45  VAL   A C     1 
ATOM   355  O  O     . VAL   A 1 48  ? -5.722  16.694 -5.563 1.00 12.46 ? 45  VAL   A O     1 
ATOM   356  C  CB    . VAL   A 1 48  ? -7.573  18.095 -7.594 1.00 14.55 ? 45  VAL   A CB    1 
ATOM   357  C  CG1   . VAL   A 1 48  ? -8.341  16.862 -8.006 1.00 15.19 ? 45  VAL   A CG1   1 
ATOM   358  C  CG2   . VAL   A 1 48  ? -8.237  19.330 -8.172 1.00 17.36 ? 45  VAL   A CG2   1 
ATOM   359  N  N     . ILE   A 1 49  ? -7.786  16.188 -4.755 1.00 10.30 ? 46  ILE   A N     1 
ATOM   360  C  CA    . ILE   A 1 49  ? -7.377  14.976 -4.076 1.00 10.40 ? 46  ILE   A CA    1 
ATOM   361  C  C     . ILE   A 1 49  ? -8.381  13.893 -4.438 1.00 9.75  ? 46  ILE   A C     1 
ATOM   362  O  O     . ILE   A 1 49  ? -9.564  14.028 -4.153 1.00 9.89  ? 46  ILE   A O     1 
ATOM   363  C  CB    . ILE   A 1 49  ? -7.360  15.170 -2.551 1.00 10.91 ? 46  ILE   A CB    1 
ATOM   364  C  CG1   . ILE   A 1 49  ? -6.454  16.338 -2.166 1.00 11.57 ? 46  ILE   A CG1   1 
ATOM   365  C  CG2   . ILE   A 1 49  ? -6.914  13.880 -1.867 1.00 12.31 ? 46  ILE   A CG2   1 
ATOM   366  C  CD1   . ILE   A 1 49  ? -6.598  16.794 -0.732 1.00 12.21 ? 46  ILE   A CD1   1 
ATOM   367  N  N     . ASP   A 1 50  ? -7.912  12.813 -5.045 1.00 9.50  ? 47  ASP   A N     1 
ATOM   368  C  CA    . ASP   A 1 50  ? -8.772  11.692 -5.443 1.00 10.00 ? 47  ASP   A CA    1 
ATOM   369  C  C     . ASP   A 1 50  ? -9.960  12.156 -6.305 1.00 9.11  ? 47  ASP   A C     1 
ATOM   370  O  O     . ASP   A 1 50  ? -11.089 11.656 -6.183 1.00 9.92  ? 47  ASP   A O     1 
ATOM   371  C  CB    . ASP   A 1 50  ? -9.265  10.885 -4.232 1.00 9.83  ? 47  ASP   A CB    1 
ATOM   372  C  CG    . ASP   A 1 50  ? -8.130  10.388 -3.365 1.00 10.53 ? 47  ASP   A CG    1 
ATOM   373  O  OD1   . ASP   A 1 50  ? -7.260  9.692  -3.920 1.00 12.24 ? 47  ASP   A OD1   1 
ATOM   374  O  OD2   . ASP   A 1 50  ? -8.113  10.681 -2.158 1.00 11.78 ? 47  ASP   A OD2   1 
ATOM   375  N  N     . GLY   A 1 51  ? -9.672  13.089 -7.215 1.00 10.09 ? 48  GLY   A N     1 
ATOM   376  C  CA    . GLY   A 1 51  ? -10.696 13.597 -8.154 1.00 10.90 ? 48  GLY   A CA    1 
ATOM   377  C  C     . GLY   A 1 51  ? -11.613 14.650 -7.567 1.00 10.41 ? 48  GLY   A C     1 
ATOM   378  O  O     . GLY   A 1 51  ? -12.392 15.208 -8.309 1.00 11.66 ? 48  GLY   A O     1 
ATOM   379  N  N     . GLU   A 1 52  ? -11.491 14.920 -6.272 1.00 10.38 ? 49  GLU   A N     1 
ATOM   380  C  CA    . GLU   A 1 52  ? -12.334 15.921 -5.592 1.00 10.86 ? 49  GLU   A CA    1 
ATOM   381  C  C     . GLU   A 1 52  ? -11.590 17.258 -5.479 1.00 10.87 ? 49  GLU   A C     1 
ATOM   382  O  O     . GLU   A 1 52  ? -10.468 17.286 -5.022 1.00 10.80 ? 49  GLU   A O     1 
ATOM   383  C  CB    . GLU   A 1 52  ? -12.681 15.436 -4.190 1.00 11.31 ? 49  GLU   A CB    1 
ATOM   384  C  CG    . GLU   A 1 52  ? -13.668 16.332 -3.445 1.00 12.37 ? 49  GLU   A CG    1 
ATOM   385  C  CD    . GLU   A 1 52  ? -14.090 15.722 -2.121 1.00 14.70 ? 49  GLU   A CD    1 
ATOM   386  O  OE1   . GLU   A 1 52  ? -13.222 15.332 -1.358 1.00 14.52 ? 49  GLU   A OE1   1 
ATOM   387  O  OE2   . GLU   A 1 52  ? -15.290 15.595 -1.901 1.00 18.87 ? 49  GLU   A OE2   1 
ATOM   388  N  N     . THR   A 1 53  ? -12.274 18.321 -5.890 1.00 12.01 ? 50  THR   A N     1 
ATOM   389  C  CA    . THR   A 1 53  ? -11.732 19.687 -5.663 1.00 12.63 ? 50  THR   A CA    1 
ATOM   390  C  C     . THR   A 1 53  ? -12.022 19.998 -4.200 1.00 12.54 ? 50  THR   A C     1 
ATOM   391  O  O     . THR   A 1 53  ? -13.133 19.999 -3.823 1.00 15.24 ? 50  THR   A O     1 
ATOM   392  C  CB    . THR   A 1 53  ? -12.372 20.697 -6.616 1.00 13.62 ? 50  THR   A CB    1 
ATOM   393  O  OG1   . THR   A 1 53  ? -11.984 20.306 -7.935 1.00 14.98 ? 50  THR   A OG1   1 
ATOM   394  C  CG2   . THR   A 1 53  ? -11.888 22.097 -6.291 1.00 15.62 ? 50  THR   A CG2   1 
ATOM   395  N  N     . CYS   A 1 54  ? -10.974 20.161 -3.410 1.00 13.04 ? 51  CYS   A N     1 
ATOM   396  C  CA    . CYS   A 1 54  ? -11.082 20.273 -1.927 1.00 13.98 ? 51  CYS   A CA    1 
ATOM   397  C  C     . CYS   A 1 54  ? -10.669 21.690 -1.499 1.00 15.21 ? 51  CYS   A C     1 
ATOM   398  O  O     . CYS   A 1 54  ? -9.669  22.125 -1.953 1.00 16.19 ? 51  CYS   A O     1 
ATOM   399  C  CB    . CYS   A 1 54  ? -10.134 19.265 -1.228 1.00 9.97  ? 51  CYS   A CB    1 
ATOM   400  S  SG    . CYS   A 1 54  ? -10.496 17.533 -1.576 1.00 14.10 ? 51  CYS   A SG    1 
ATOM   401  N  N     . LEU   A 1 55  ? -11.480 22.339 -0.678 1.00 13.01 ? 52  LEU   A N     1 
ATOM   402  C  CA    . LEU   A 1 55  ? -11.018 23.588 -0.042 1.00 14.00 ? 52  LEU   A CA    1 
ATOM   403  C  C     . LEU   A 1 55  ? -10.434 23.230 1.335  1.00 11.68 ? 52  LEU   A C     1 
ATOM   404  O  O     . LEU   A 1 55  ? -11.169 22.812 2.194  1.00 13.75 ? 52  LEU   A O     1 
ATOM   405  C  CB    . LEU   A 1 55  ? -12.183 24.575 0.069  1.00 15.37 ? 52  LEU   A CB    1 
ATOM   406  C  CG    . LEU   A 1 55  ? -11.851 25.863 0.815  1.00 19.18 ? 52  LEU   A CG    1 
ATOM   407  C  CD1   . LEU   A 1 55  ? -10.675 26.561 0.156  1.00 19.30 ? 52  LEU   A CD1   1 
ATOM   408  C  CD2   . LEU   A 1 55  ? -13.078 26.753 0.899  1.00 23.34 ? 52  LEU   A CD2   1 
ATOM   409  N  N     . LEU   A 1 56  ? -9.127  23.389 1.467  1.00 12.90 ? 53  LEU   A N     1 
ATOM   410  C  CA    . LEU   A 1 56  ? -8.451  23.155 2.768  1.00 12.53 ? 53  LEU   A CA    1 
ATOM   411  C  C     . LEU   A 1 56  ? -8.467  24.470 3.556  1.00 13.21 ? 53  LEU   A C     1 
ATOM   412  O  O     . LEU   A 1 56  ? -8.058  25.465 3.030  1.00 17.36 ? 53  LEU   A O     1 
ATOM   413  C  CB    . LEU   A 1 56  ? -6.999  22.742 2.551  1.00 13.52 ? 53  LEU   A CB    1 
ATOM   414  C  CG    . LEU   A 1 56  ? -6.768  21.577 1.591  1.00 15.69 ? 53  LEU   A CG    1 
ATOM   415  C  CD1   . LEU   A 1 56  ? -5.333  21.116 1.716  1.00 18.96 ? 53  LEU   A CD1   1 
ATOM   416  C  CD2   . LEU   A 1 56  ? -7.737  20.442 1.880  1.00 16.89 ? 53  LEU   A CD2   1 
ATOM   417  N  N     . ASP   A 1 57  ? -8.980  24.407 4.762  1.00 11.42 ? 54  ASP   A N     1 
ATOM   418  C  CA    . ASP   A 1 57  ? -9.019  25.577 5.683  1.00 12.80 ? 54  ASP   A CA    1 
ATOM   419  C  C     . ASP   A 1 57  ? -8.208  25.102 6.893  1.00 11.92 ? 54  ASP   A C     1 
ATOM   420  O  O     . ASP   A 1 57  ? -8.719  24.363 7.684  1.00 12.06 ? 54  ASP   A O     1 
ATOM   421  C  CB    . ASP   A 1 57  ? -10.456 25.980 5.986  1.00 15.68 ? 54  ASP   A CB    1 
ATOM   422  C  CG    . ASP   A 1 57  ? -10.577 27.340 6.649  1.00 17.24 ? 54  ASP   A CG    1 
ATOM   423  O  OD1   . ASP   A 1 57  ? -9.527  27.935 6.963  1.00 21.02 ? 54  ASP   A OD1   1 
ATOM   424  O  OD2   . ASP   A 1 57  ? -11.722 27.794 6.847  1.00 24.19 ? 54  ASP   A OD2   1 
ATOM   425  N  N     . ILE   A 1 58  ? -6.988  25.608 6.952  1.00 11.72 ? 55  ILE   A N     1 
ATOM   426  C  CA    . ILE   A 1 58  ? -5.985  25.086 7.921  1.00 11.89 ? 55  ILE   A CA    1 
ATOM   427  C  C     . ILE   A 1 58  ? -5.659  26.130 8.985  1.00 12.58 ? 55  ILE   A C     1 
ATOM   428  O  O     . ILE   A 1 58  ? -5.279  27.214 8.633  1.00 13.50 ? 55  ILE   A O     1 
ATOM   429  C  CB    . ILE   A 1 58  ? -4.696  24.749 7.166  1.00 12.69 ? 55  ILE   A CB    1 
ATOM   430  C  CG1   . ILE   A 1 58  ? -4.973  23.751 6.039  1.00 13.65 ? 55  ILE   A CG1   1 
ATOM   431  C  CG2   . ILE   A 1 58  ? -3.649  24.233 8.135  1.00 14.35 ? 55  ILE   A CG2   1 
ATOM   432  C  CD1   . ILE   A 1 58  ? -3.843  23.561 5.088  1.00 14.54 ? 55  ILE   A CD1   1 
ATOM   433  N  N     . LEU   A 1 59  ? -5.789  25.724 10.226 1.00 11.56 ? 56  LEU   A N     1 
ATOM   434  C  CA    . LEU   A 1 59  ? -5.393  26.584 11.370 1.00 11.92 ? 56  LEU   A CA    1 
ATOM   435  C  C     . LEU   A 1 59  ? -4.041  26.099 11.871 1.00 11.91 ? 56  LEU   A C     1 
ATOM   436  O  O     . LEU   A 1 59  ? -3.911  24.960 12.330 1.00 12.21 ? 56  LEU   A O     1 
ATOM   437  C  CB    . LEU   A 1 59  ? -6.434  26.544 12.477 1.00 12.93 ? 56  LEU   A CB    1 
ATOM   438  C  CG    . LEU   A 1 59  ? -6.204  27.464 13.669 1.00 13.89 ? 56  LEU   A CG    1 
ATOM   439  C  CD1   . LEU   A 1 59  ? -6.333  28.923 13.244 1.00 15.89 ? 56  LEU   A CD1   1 
ATOM   440  C  CD2   . LEU   A 1 59  ? -7.152  27.137 14.793 1.00 15.98 ? 56  LEU   A CD2   1 
ATOM   441  N  N     . ASP   A 1 60  ? -3.042  26.971 11.774 1.00 12.09 ? 57  ASP   A N     1 
ATOM   442  C  CA    . ASP   A 1 60  ? -1.702  26.752 12.278 1.00 12.19 ? 57  ASP   A CA    1 
ATOM   443  C  C     . ASP   A 1 60  ? -1.699  27.304 13.705 1.00 13.68 ? 57  ASP   A C     1 
ATOM   444  O  O     . ASP   A 1 60  ? -1.712  28.516 13.913 1.00 15.38 ? 57  ASP   A O     1 
ATOM   445  C  CB    . ASP   A 1 60  ? -0.687  27.508 11.420 1.00 14.55 ? 57  ASP   A CB    1 
ATOM   446  C  CG    . ASP   A 1 60  ? 0.696   27.467 11.981 1.00 14.73 ? 57  ASP   A CG    1 
ATOM   447  O  OD1   . ASP   A 1 60  ? 1.026   26.492 12.697 1.00 15.25 ? 57  ASP   A OD1   1 
ATOM   448  O  OD2   . ASP   A 1 60  ? 1.476   28.402 11.672 1.00 16.29 ? 57  ASP   A OD2   1 
ATOM   449  N  N     . THR   A 1 61  ? -1.728  26.410 14.676 1.00 12.03 ? 58  THR   A N     1 
ATOM   450  C  CA    . THR   A 1 61  ? -1.862  26.825 16.096 1.00 12.30 ? 58  THR   A CA    1 
ATOM   451  C  C     . THR   A 1 61  ? -0.545  27.291 16.700 1.00 12.56 ? 58  THR   A C     1 
ATOM   452  O  O     . THR   A 1 61  ? 0.466   26.759 16.401 1.00 13.31 ? 58  THR   A O     1 
ATOM   453  C  CB    . THR   A 1 61  ? -2.536  25.755 16.951 1.00 11.90 ? 58  THR   A CB    1 
ATOM   454  O  OG1   . THR   A 1 61  ? -1.668  24.646 17.159 1.00 12.10 ? 58  THR   A OG1   1 
ATOM   455  C  CG2   . THR   A 1 61  ? -3.868  25.331 16.371 1.00 12.25 ? 58  THR   A CG2   1 
ATOM   456  N  N     . ALA   A 1 62  ? -0.659  28.245 17.615 1.00 14.47 ? 59  ALA   A N     1 
ATOM   457  C  CA    . ALA   A 1 62  ? 0.546   28.804 18.264 1.00 15.38 ? 59  ALA   A CA    1 
ATOM   458  C  C     . ALA   A 1 62  ? 0.613   28.241 19.686 1.00 14.05 ? 59  ALA   A C     1 
ATOM   459  O  O     . ALA   A 1 62  ? 1.216   27.270 19.901 1.00 16.02 ? 59  ALA   A O     1 
ATOM   460  C  CB    . ALA   A 1 62  ? 0.485   30.327 18.251 1.00 17.08 ? 59  ALA   A CB    1 
ATOM   461  N  N     . GLY   A 1 63  ? -0.085  28.843 20.622 1.00 16.62 ? 60  GLY   A N     1 
ATOM   462  C  CA    . GLY   A 1 63  ? 0.008   28.328 21.993 1.00 16.75 ? 60  GLY   A CA    1 
ATOM   463  C  C     . GLY   A 1 63  ? -0.652  26.972 22.118 1.00 16.63 ? 60  GLY   A C     1 
ATOM   464  O  O     . GLY   A 1 63  ? -1.689  26.769 21.517 1.00 19.54 ? 60  GLY   A O     1 
ATOM   465  N  N     . GLN   A 1 64  ? -0.090  26.113 22.948 1.00 17.25 ? 61  GLN   A N     1 
ATOM   466  C  CA    . GLN   A 1 64  ? -0.653  24.762 23.114 1.00 17.33 ? 61  GLN   A CA    1 
ATOM   467  C  C     . GLN   A 1 64  ? -1.230  24.539 24.517 1.00 18.80 ? 61  GLN   A C     1 
ATOM   468  O  O     . GLN   A 1 64  ? -1.385  23.399 24.946 1.00 22.91 ? 61  GLN   A O     1 
ATOM   469  C  CB    . GLN   A 1 64  ? 0.391   23.688 22.759 1.00 17.25 ? 61  GLN   A CB    1 
ATOM   470  C  CG    . GLN   A 1 64  ? 1.067   23.882 21.409 1.00 16.45 ? 61  GLN   A CG    1 
ATOM   471  C  CD    . GLN   A 1 64  ? 0.130   23.672 20.241 1.00 13.93 ? 61  GLN   A CD    1 
ATOM   472  O  OE1   . GLN   A 1 64  ? -0.434  22.586 20.057 1.00 15.62 ? 61  GLN   A OE1   1 
ATOM   473  N  NE2   . GLN   A 1 64  ? -0.001  24.693 19.409 1.00 14.63 ? 61  GLN   A NE2   1 
ATOM   474  N  N     . GLU   A 1 65  ? -1.647  25.625 25.178 1.00 20.78 ? 62  GLU   A N     1 
ATOM   475  C  CA    . GLU   A 1 65  ? -2.113  25.613 26.574 1.00 22.72 ? 62  GLU   A CA    1 
ATOM   476  C  C     . GLU   A 1 65  ? -3.359  24.736 26.748 1.00 18.71 ? 62  GLU   A C     1 
ATOM   477  O  O     . GLU   A 1 65  ? -4.314  24.857 25.986 1.00 25.09 ? 62  GLU   A O     1 
ATOM   478  C  CB    . GLU   A 1 65  ? -2.465  27.036 27.059 1.00 26.36 ? 62  GLU   A CB    1 
ATOM   479  C  CG    . GLU   A 1 65  ? -1.456  28.160 26.792 1.00 30.41 ? 62  GLU   A CG    1 
ATOM   480  C  CD    . GLU   A 1 65  ? -1.624  28.920 25.445 1.00 37.78 ? 62  GLU   A CD    1 
ATOM   481  O  OE1   . GLU   A 1 65  ? -2.373  28.485 24.527 1.00 33.79 ? 62  GLU   A OE1   1 
ATOM   482  O  OE2   . GLU   A 1 65  ? -0.973  29.972 25.268 1.00 38.77 ? 62  GLU   A OE2   1 
ATOM   483  N  N     . GLU   A 1 66  ? -3.370  23.911 27.799 1.00 22.28 ? 63  GLU   A N     1 
ATOM   484  C  CA    . GLU   A 1 66  ? -4.534  23.140 28.248 1.00 26.88 ? 63  GLU   A CA    1 
ATOM   485  C  C     . GLU   A 1 66  ? -5.748  24.038 28.461 1.00 22.86 ? 63  GLU   A C     1 
ATOM   486  O  O     . GLU   A 1 66  ? -6.856  23.715 28.010 1.00 30.30 ? 63  GLU   A O     1 
ATOM   487  C  CB    . GLU   A 1 66  ? -4.186  22.459 29.580 1.00 32.02 ? 63  GLU   A CB    1 
ATOM   488  C  CG    . GLU   A 1 66  ? -5.323  21.718 30.287 1.00 35.79 ? 63  GLU   A CG    1 
ATOM   489  C  CD    . GLU   A 1 66  ? -5.529  20.302 29.796 1.00 40.88 ? 63  GLU   A CD    1 
ATOM   490  O  OE1   . GLU   A 1 66  ? -4.782  19.857 28.904 1.00 49.41 ? 63  GLU   A OE1   1 
ATOM   491  O  OE2   . GLU   A 1 66  ? -6.441  19.628 30.317 1.00 49.86 ? 63  GLU   A OE2   1 
ATOM   492  N  N     . TYR   A 1 67  ? -5.523  25.166 29.151 1.00 18.90 ? 64  TYR   A N     1 
ATOM   493  C  CA    . TYR   A 1 67  ? -6.594  26.065 29.560 1.00 17.19 ? 64  TYR   A CA    1 
ATOM   494  C  C     . TYR   A 1 67  ? -6.653  27.249 28.631 1.00 16.40 ? 64  TYR   A C     1 
ATOM   495  O  O     . TYR   A 1 67  ? -5.983  28.269 28.819 1.00 18.69 ? 64  TYR   A O     1 
ATOM   496  C  CB    . TYR   A 1 67  ? -6.482  26.505 31.039 1.00 16.37 ? 64  TYR   A CB    1 
ATOM   497  C  CG    . TYR   A 1 67  ? -6.464  25.317 31.945 1.00 15.55 ? 64  TYR   A CG    1 
ATOM   498  C  CD1   . TYR   A 1 67  ? -7.532  24.429 31.979 1.00 18.16 ? 64  TYR   A CD1   1 
ATOM   499  C  CD2   . TYR   A 1 67  ? -5.354  25.031 32.728 1.00 16.62 ? 64  TYR   A CD2   1 
ATOM   500  C  CE1   . TYR   A 1 67  ? -7.496  23.294 32.760 1.00 19.82 ? 64  TYR   A CE1   1 
ATOM   501  C  CE2   . TYR   A 1 67  ? -5.334  23.921 33.553 1.00 17.60 ? 64  TYR   A CE2   1 
ATOM   502  C  CZ    . TYR   A 1 67  ? -6.397  23.060 33.560 1.00 18.29 ? 64  TYR   A CZ    1 
ATOM   503  O  OH    . TYR   A 1 67  ? -6.360  21.950 34.341 1.00 21.44 ? 64  TYR   A OH    1 
ATOM   504  N  N     . SER   A 1 68  ? -7.480  27.081 27.609 1.00 15.34 ? 65  SER   A N     1 
ATOM   505  C  CA    . SER   A 1 68  ? -7.664  28.079 26.595 1.00 13.89 ? 65  SER   A CA    1 
ATOM   506  C  C     . SER   A 1 68  ? -9.029  27.932 25.961 1.00 14.13 ? 65  SER   A C     1 
ATOM   507  O  O     . SER   A 1 68  ? -9.313  26.946 25.280 1.00 15.84 ? 65  SER   A O     1 
ATOM   508  C  CB    . SER   A 1 68  ? -6.601  27.911 25.515 1.00 15.03 ? 65  SER   A CB    1 
ATOM   509  O  OG    . SER   A 1 68  ? -6.919  28.711 24.397 1.00 17.73 ? 65  SER   A OG    1 
ATOM   510  N  N     . ALA   A 1 69  ? -9.868  28.940 26.167 1.00 14.62 ? 66  ALA   A N     1 
ATOM   511  C  CA    . ALA   A 1 69  ? -11.174 28.925 25.528 1.00 15.51 ? 66  ALA   A CA    1 
ATOM   512  C  C     . ALA   A 1 69  ? -11.064 28.855 24.002 1.00 15.95 ? 66  ALA   A C     1 
ATOM   513  O  O     . ALA   A 1 69  ? -11.860 28.166 23.336 1.00 18.49 ? 66  ALA   A O     1 
ATOM   514  C  CB    . ALA   A 1 69  ? -11.980 30.134 25.935 1.00 18.02 ? 66  ALA   A CB    1 
ATOM   515  N  N     . MET   A 1 70  ? -10.099 29.559 23.444 1.00 16.05 ? 67  MET   A N     1 
ATOM   516  C  CA    . MET   A 1 70  ? -9.894  29.548 22.001 1.00 17.20 ? 67  MET   A CA    1 
ATOM   517  C  C     . MET   A 1 70  ? -9.500  28.169 21.493 1.00 15.41 ? 67  MET   A C     1 
ATOM   518  O  O     . MET   A 1 70  ? -10.008 27.746 20.456 1.00 16.30 ? 67  MET   A O     1 
ATOM   519  C  CB    . MET   A 1 70  ? -8.835  30.573 21.596 1.00 20.99 ? 67  MET   A CB    1 
ATOM   520  C  CG    . MET   A 1 70  ? -8.815  30.933 20.128 1.00 27.27 ? 67  MET   A CG    1 
ATOM   521  S  SD    . MET   A 1 70  ? -10.323 31.706 19.469 1.00 39.50 ? 67  MET   A SD    1 
ATOM   522  C  CE    . MET   A 1 70  ? -11.038 32.570 20.865 1.00 31.19 ? 67  MET   A CE    1 
ATOM   523  N  N     . ARG   A 1 71  ? -8.648  27.476 22.229 1.00 14.41 ? 68  ARG   A N     1 
ATOM   524  C  CA    . ARG   A 1 71  ? -8.238  26.111 21.815 1.00 14.77 ? 68  ARG   A CA    1 
ATOM   525  C  C     . ARG   A 1 71  ? -9.444  25.171 21.901 1.00 13.55 ? 68  ARG   A C     1 
ATOM   526  O  O     . ARG   A 1 71  ? -9.616  24.324 21.023 1.00 15.00 ? 68  ARG   A O     1 
ATOM   527  C  CB    . ARG   A 1 71  ? -7.067  25.668 22.690 1.00 16.25 ? 68  ARG   A CB    1 
ATOM   528  C  CG    . ARG   A 1 71  ? -6.507  24.310 22.313 1.00 19.12 ? 68  ARG   A CG    1 
ATOM   529  C  CD    . ARG   A 1 71  ? -5.071  24.424 22.747 1.00 24.14 ? 68  ARG   A CD    1 
ATOM   530  N  NE    . ARG   A 1 71  ? -4.505  23.127 22.696 1.00 25.18 ? 68  ARG   A NE    1 
ATOM   531  C  CZ    . ARG   A 1 71  ? -3.751  22.686 21.728 1.00 24.76 ? 68  ARG   A CZ    1 
ATOM   532  N  NH1   . ARG   A 1 71  ? -3.382  23.352 20.650 1.00 23.44 ? 68  ARG   A NH1   1 
ATOM   533  N  NH2   . ARG   A 1 71  ? -3.351  21.488 21.895 1.00 30.39 ? 68  ARG   A NH2   1 
ATOM   534  N  N     . ASP   A 1 72  ? -10.255 25.274 22.940 1.00 14.12 ? 69  ASP   A N     1 
ATOM   535  C  CA    . ASP   A 1 72  ? -11.465 24.459 23.000 1.00 16.31 ? 69  ASP   A CA    1 
ATOM   536  C  C     . ASP   A 1 72  ? -12.347 24.732 21.770 1.00 14.62 ? 69  ASP   A C     1 
ATOM   537  O  O     . ASP   A 1 72  ? -12.888 23.783 21.162 1.00 16.85 ? 69  ASP   A O     1 
ATOM   538  C  CB    . ASP   A 1 72  ? -12.255 24.719 24.277 1.00 18.65 ? 69  ASP   A CB    1 
ATOM   539  C  CG    . ASP   A 1 72  ? -11.576 24.166 25.522 1.00 24.06 ? 69  ASP   A CG    1 
ATOM   540  O  OD1   . ASP   A 1 72  ? -10.673 23.304 25.420 1.00 29.03 ? 69  ASP   A OD1   1 
ATOM   541  O  OD2   . ASP   A 1 72  ? -11.970 24.622 26.621 1.00 32.72 ? 69  ASP   A OD2   1 
ATOM   542  N  N     A GLN   A 1 73  ? -12.477 26.003 21.388 0.50 15.26 ? 70  GLN   A N     1 
ATOM   543  N  N     B GLN   A 1 73  ? -12.471 26.005 21.396 0.50 15.45 ? 70  GLN   A N     1 
ATOM   544  C  CA    A GLN   A 1 73  ? -13.321 26.362 20.261 0.50 16.24 ? 70  GLN   A CA    1 
ATOM   545  C  CA    B GLN   A 1 73  ? -13.295 26.393 20.267 0.50 16.40 ? 70  GLN   A CA    1 
ATOM   546  C  C     A GLN   A 1 73  ? -12.773 25.784 18.960 0.50 16.08 ? 70  GLN   A C     1 
ATOM   547  C  C     B GLN   A 1 73  ? -12.768 25.778 18.977 0.50 16.33 ? 70  GLN   A C     1 
ATOM   548  O  O     A GLN   A 1 73  ? -13.535 25.191 18.191 0.50 16.57 ? 70  GLN   A O     1 
ATOM   549  O  O     B GLN   A 1 73  ? -13.532 25.145 18.242 0.50 16.67 ? 70  GLN   A O     1 
ATOM   550  C  CB    A GLN   A 1 73  ? -13.498 27.872 20.139 0.50 17.80 ? 70  GLN   A CB    1 
ATOM   551  C  CB    B GLN   A 1 73  ? -13.373 27.913 20.148 0.50 18.33 ? 70  GLN   A CB    1 
ATOM   552  C  CG    A GLN   A 1 73  ? -14.442 28.273 19.018 0.50 20.94 ? 70  GLN   A CG    1 
ATOM   553  C  CG    B GLN   A 1 73  ? -14.208 28.412 18.988 0.50 20.38 ? 70  GLN   A CG    1 
ATOM   554  C  CD    A GLN   A 1 73  ? -15.775 27.562 19.098 0.50 21.76 ? 70  GLN   A CD    1 
ATOM   555  C  CD    B GLN   A 1 73  ? -14.568 29.874 19.142 0.50 22.80 ? 70  GLN   A CD    1 
ATOM   556  O  OE1   A GLN   A 1 73  ? -16.512 27.694 20.079 0.50 25.38 ? 70  GLN   A OE1   1 
ATOM   557  O  OE1   B GLN   A 1 73  ? -15.328 30.254 20.039 0.50 24.21 ? 70  GLN   A OE1   1 
ATOM   558  N  NE2   A GLN   A 1 73  ? -16.100 26.805 18.058 0.50 22.42 ? 70  GLN   A NE2   1 
ATOM   559  N  NE2   B GLN   A 1 73  ? -14.028 30.701 18.271 0.50 25.99 ? 70  GLN   A NE2   1 
ATOM   560  N  N     . TYR   A 1 74  ? -11.474 25.930 18.703 1.00 15.62 ? 71  TYR   A N     1 
ATOM   561  C  CA    . TYR   A 1 74  ? -10.943 25.386 17.455 1.00 15.89 ? 71  TYR   A CA    1 
ATOM   562  C  C     . TYR   A 1 74  ? -10.872 23.876 17.435 1.00 15.56 ? 71  TYR   A C     1 
ATOM   563  O  O     . TYR   A 1 74  ? -10.952 23.269 16.343 1.00 16.07 ? 71  TYR   A O     1 
ATOM   564  C  CB    . TYR   A 1 74  ? -9.681  26.077 17.010 1.00 16.76 ? 71  TYR   A CB    1 
ATOM   565  C  CG    . TYR   A 1 74  ? -8.402  25.924 17.773 1.00 17.46 ? 71  TYR   A CG    1 
ATOM   566  C  CD1   . TYR   A 1 74  ? -7.759  24.712 17.904 1.00 17.48 ? 71  TYR   A CD1   1 
ATOM   567  C  CD2   . TYR   A 1 74  ? -7.749  27.064 18.260 1.00 17.55 ? 71  TYR   A CD2   1 
ATOM   568  C  CE1   . TYR   A 1 74  ? -6.528  24.609 18.525 1.00 16.71 ? 71  TYR   A CE1   1 
ATOM   569  C  CE2   . TYR   A 1 74  ? -6.510  26.981 18.888 1.00 17.72 ? 71  TYR   A CE2   1 
ATOM   570  C  CZ    . TYR   A 1 74  ? -5.903  25.756 19.027 1.00 16.75 ? 71  TYR   A CZ    1 
ATOM   571  O  OH    . TYR   A 1 74  ? -4.687  25.650 19.643 1.00 17.82 ? 71  TYR   A OH    1 
ATOM   572  N  N     . MET   A 1 75  ? -10.780 23.227 18.575 1.00 13.81 ? 72  MET   A N     1 
ATOM   573  C  CA    . MET   A 1 75  ? -10.918 21.781 18.594 1.00 15.15 ? 72  MET   A CA    1 
ATOM   574  C  C     . MET   A 1 75  ? -12.355 21.344 18.318 1.00 15.39 ? 72  MET   A C     1 
ATOM   575  O  O     . MET   A 1 75  ? -12.558 20.319 17.665 1.00 17.61 ? 72  MET   A O     1 
ATOM   576  C  CB    . MET   A 1 75  ? -10.399 21.169 19.871 1.00 14.77 ? 72  MET   A CB    1 
ATOM   577  C  CG    . MET   A 1 75  ? -8.890  21.247 19.982 1.00 15.80 ? 72  MET   A CG    1 
ATOM   578  S  SD    . MET   A 1 75  ? -8.243  20.458 21.459 1.00 17.96 ? 72  MET   A SD    1 
ATOM   579  C  CE    . MET   A 1 75  ? -6.496  20.606 21.108 1.00 19.10 ? 72  MET   A CE    1 
ATOM   580  N  N     . ARG   A 1 76  ? -13.345 22.112 18.773 1.00 14.58 ? 73  ARG   A N     1 
ATOM   581  C  CA    . ARG   A 1 76  ? -14.735 21.823 18.405 1.00 15.35 ? 73  ARG   A CA    1 
ATOM   582  C  C     . ARG   A 1 76  ? -14.970 21.980 16.904 1.00 15.13 ? 73  ARG   A C     1 
ATOM   583  O  O     . ARG   A 1 76  ? -15.617 21.137 16.263 1.00 16.85 ? 73  ARG   A O     1 
ATOM   584  C  CB    . ARG   A 1 76  ? -15.721 22.692 19.188 1.00 17.39 ? 73  ARG   A CB    1 
ATOM   585  C  CG    . ARG   A 1 76  ? -15.892 22.271 20.637 1.00 19.75 ? 73  ARG   A CG    1 
ATOM   586  C  CD    . ARG   A 1 76  ? -17.055 23.002 21.277 1.00 23.21 ? 73  ARG   A CD    1 
ATOM   587  N  NE    . ARG   A 1 76  ? -16.806 24.432 21.435 1.00 28.03 ? 73  ARG   A NE    1 
ATOM   588  C  CZ    . ARG   A 1 76  ? -16.252 25.007 22.507 1.00 28.52 ? 73  ARG   A CZ    1 
ATOM   589  N  NH1   . ARG   A 1 76  ? -15.822 24.276 23.532 1.00 33.79 ? 73  ARG   A NH1   1 
ATOM   590  N  NH2   . ARG   A 1 76  ? -16.103 26.323 22.531 1.00 30.89 ? 73  ARG   A NH2   1 
ATOM   591  N  N     . THR   A 1 77  ? -14.430 23.042 16.331 1.00 13.38 ? 74  THR   A N     1 
ATOM   592  C  CA    . THR   A 1 77  ? -14.632 23.387 14.927 1.00 14.88 ? 74  THR   A CA    1 
ATOM   593  C  C     . THR   A 1 77  ? -13.803 22.507 13.974 1.00 13.84 ? 74  THR   A C     1 
ATOM   594  O  O     . THR   A 1 77  ? -14.235 22.194 12.856 1.00 15.24 ? 74  THR   A O     1 
ATOM   595  C  CB    . THR   A 1 77  ? -14.290 24.863 14.694 1.00 16.36 ? 74  THR   A CB    1 
ATOM   596  O  OG1   . THR   A 1 77  ? -15.168 25.666 15.507 1.00 19.58 ? 74  THR   A OG1   1 
ATOM   597  C  CG2   . THR   A 1 77  ? -14.441 25.230 13.231 1.00 18.62 ? 74  THR   A CG2   1 
ATOM   598  N  N     . GLY   A 1 78  ? -12.581 22.160 14.378 1.00 13.45 ? 75  GLY   A N     1 
ATOM   599  C  CA    . GLY   A 1 78  ? -11.696 21.381 13.525 1.00 12.15 ? 75  GLY   A CA    1 
ATOM   600  C  C     . GLY   A 1 78  ? -12.242 20.000 13.203 1.00 12.07 ? 75  GLY   A C     1 
ATOM   601  O  O     . GLY   A 1 78  ? -12.742 19.304 14.073 1.00 14.69 ? 75  GLY   A O     1 
ATOM   602  N  N     . GLU   A 1 79  ? -12.068 19.581 11.952 1.00 11.07 ? 76  GLU   A N     1 
ATOM   603  C  CA    . GLU   A 1 79  ? -12.534 18.270 11.503 1.00 10.28 ? 76  GLU   A CA    1 
ATOM   604  C  C     . GLU   A 1 79  ? -11.422 17.244 11.544 1.00 9.98  ? 76  GLU   A C     1 
ATOM   605  O  O     . GLU   A 1 79  ? -11.696 16.076 11.782 1.00 11.49 ? 76  GLU   A O     1 
ATOM   606  C  CB    . GLU   A 1 79  ? -13.115 18.355 10.109 1.00 11.00 ? 76  GLU   A CB    1 
ATOM   607  C  CG    . GLU   A 1 79  ? -14.417 19.142 10.069 1.00 14.13 ? 76  GLU   A CG    1 
ATOM   608  C  CD    . GLU   A 1 79  ? -14.881 19.298 8.654  1.00 17.50 ? 76  GLU   A CD    1 
ATOM   609  O  OE1   . GLU   A 1 79  ? -14.169 19.832 7.812  1.00 16.74 ? 76  GLU   A OE1   1 
ATOM   610  O  OE2   . GLU   A 1 79  ? -15.995 18.865 8.351  1.00 23.55 ? 76  GLU   A OE2   1 
ATOM   611  N  N     . GLY   A 1 80  ? -10.187 17.643 11.264 1.00 9.25  ? 77  GLY   A N     1 
ATOM   612  C  CA    . GLY   A 1 80  ? -9.055  16.727 11.392 1.00 8.67  ? 77  GLY   A CA    1 
ATOM   613  C  C     . GLY   A 1 80  ? -7.870  17.420 11.983 1.00 8.52  ? 77  GLY   A C     1 
ATOM   614  O  O     . GLY   A 1 80  ? -7.715  18.630 11.831 1.00 9.11  ? 77  GLY   A O     1 
ATOM   615  N  N     . PHE   A 1 81  ? -6.992  16.620 12.593 1.00 8.31  ? 78  PHE   A N     1 
ATOM   616  C  CA    . PHE   A 1 81  ? -5.860  17.136 13.376 1.00 8.73  ? 78  PHE   A CA    1 
ATOM   617  C  C     . PHE   A 1 81  ? -4.571  16.503 12.908 1.00 8.45  ? 78  PHE   A C     1 
ATOM   618  O  O     . PHE   A 1 81  ? -4.426  15.284 12.880 1.00 9.63  ? 78  PHE   A O     1 
ATOM   619  C  CB    . PHE   A 1 81  ? -6.094  16.881 14.866 1.00 9.75  ? 78  PHE   A CB    1 
ATOM   620  C  CG    . PHE   A 1 81  ? -7.349  17.548 15.349 1.00 9.94  ? 78  PHE   A CG    1 
ATOM   621  C  CD1   . PHE   A 1 81  ? -8.595  16.955 15.171 1.00 10.55 ? 78  PHE   A CD1   1 
ATOM   622  C  CD2   . PHE   A 1 81  ? -7.300  18.836 15.884 1.00 10.83 ? 78  PHE   A CD2   1 
ATOM   623  C  CE1   . PHE   A 1 81  ? -9.754  17.628 15.499 1.00 11.36 ? 78  PHE   A CE1   1 
ATOM   624  C  CE2   . PHE   A 1 81  ? -8.471  19.491 16.233 1.00 12.21 ? 78  PHE   A CE2   1 
ATOM   625  C  CZ    . PHE   A 1 81  ? -9.689  18.882 16.062 1.00 12.22 ? 78  PHE   A CZ    1 
ATOM   626  N  N     . LEU   A 1 82  ? -3.653  17.361 12.544 1.00 8.42  ? 79  LEU   A N     1 
ATOM   627  C  CA    . LEU   A 1 82  ? -2.278  16.939 12.210 1.00 8.72  ? 79  LEU   A CA    1 
ATOM   628  C  C     . LEU   A 1 82  ? -1.498  17.097 13.525 1.00 8.82  ? 79  LEU   A C     1 
ATOM   629  O  O     . LEU   A 1 82  ? -1.360  18.205 14.006 1.00 10.86 ? 79  LEU   A O     1 
ATOM   630  C  CB    . LEU   A 1 82  ? -1.748  17.890 11.128 1.00 12.80 ? 79  LEU   A CB    1 
ATOM   631  C  CG    . LEU   A 1 82  ? -0.773  17.279 10.135 1.00 14.97 ? 79  LEU   A CG    1 
ATOM   632  C  CD1   . LEU   A 1 82  ? -1.455  16.212 9.268  1.00 13.27 ? 79  LEU   A CD1   1 
ATOM   633  C  CD2   . LEU   A 1 82  ? -0.091  18.346 9.302  1.00 15.61 ? 79  LEU   A CD2   1 
ATOM   634  N  N     . CYS   A 1 83  ? -1.098  15.994 14.130 1.00 9.19  ? 80  CYS   A N     1 
ATOM   635  C  CA    . CYS   A 1 83  ? -0.378  15.971 15.425 1.00 9.11  ? 80  CYS   A CA    1 
ATOM   636  C  C     . CYS   A 1 83  ? 1.104   15.774 15.120 1.00 8.43  ? 80  CYS   A C     1 
ATOM   637  O  O     . CYS   A 1 83  ? 1.526   14.685 14.782 1.00 9.40  ? 80  CYS   A O     1 
ATOM   638  C  CB    . CYS   A 1 83  ? -0.932  14.872 16.314 1.00 11.14 ? 80  CYS   A CB    1 
ATOM   639  S  SG    . CYS   A 1 83  ? -2.681  15.118 16.743 1.00 15.85 ? 80  CYS   A SG    1 
ATOM   640  N  N     . VAL   A 1 84  ? 1.835   16.852 15.303 1.00 8.39  ? 81  VAL   A N     1 
ATOM   641  C  CA    . VAL   A 1 84  ? 3.242   16.918 14.839 1.00 8.16  ? 81  VAL   A CA    1 
ATOM   642  C  C     . VAL   A 1 84  ? 4.202   16.859 16.019 1.00 8.29  ? 81  VAL   A C     1 
ATOM   643  O  O     . VAL   A 1 84  ? 4.003   17.555 16.973 1.00 8.67  ? 81  VAL   A O     1 
ATOM   644  C  CB    . VAL   A 1 84  ? 3.475   18.247 14.087 1.00 8.75  ? 81  VAL   A CB    1 
ATOM   645  C  CG1   . VAL   A 1 84  ? 4.879   18.289 13.472 1.00 8.56  ? 81  VAL   A CG1   1 
ATOM   646  C  CG2   . VAL   A 1 84  ? 2.394   18.513 13.031 1.00 9.39  ? 81  VAL   A CG2   1 
ATOM   647  N  N     . PHE   A 1 85  ? 5.188   16.004 15.875 1.00 8.12  ? 82  PHE   A N     1 
ATOM   648  C  CA    . PHE   A 1 85  ? 6.363   15.997 16.784 1.00 8.32  ? 82  PHE   A CA    1 
ATOM   649  C  C     . PHE   A 1 85  ? 7.600   16.109 15.877 1.00 8.19  ? 82  PHE   A C     1 
ATOM   650  O  O     . PHE   A 1 85  ? 7.490   16.034 14.645 1.00 9.48  ? 82  PHE   A O     1 
ATOM   651  C  CB    . PHE   A 1 85  ? 6.427   14.735 17.648 1.00 9.15  ? 82  PHE   A CB    1 
ATOM   652  C  CG    . PHE   A 1 85  ? 6.729   13.461 16.899 1.00 8.88  ? 82  PHE   A CG    1 
ATOM   653  C  CD1   . PHE   A 1 85  ? 5.707   12.728 16.322 1.00 8.92  ? 82  PHE   A CD1   1 
ATOM   654  C  CD2   . PHE   A 1 85  ? 8.030   12.967 16.827 1.00 8.88  ? 82  PHE   A CD2   1 
ATOM   655  C  CE1   . PHE   A 1 85  ? 5.962   11.558 15.635 1.00 9.60  ? 82  PHE   A CE1   1 
ATOM   656  C  CE2   . PHE   A 1 85  ? 8.284   11.794 16.131 1.00 9.24  ? 82  PHE   A CE2   1 
ATOM   657  C  CZ    . PHE   A 1 85  ? 7.255   11.094 15.528 1.00 9.66  ? 82  PHE   A CZ    1 
ATOM   658  N  N     . ALA   A 1 86  ? 8.743   16.356 16.489 1.00 9.29  ? 83  ALA   A N     1 
ATOM   659  C  CA    . ALA   A 1 86  ? 9.994   16.399 15.737 1.00 9.45  ? 83  ALA   A CA    1 
ATOM   660  C  C     . ALA   A 1 86  ? 10.798  15.153 16.040 1.00 9.37  ? 83  ALA   A C     1 
ATOM   661  O  O     . ALA   A 1 86  ? 10.908  14.763 17.220 1.00 10.42 ? 83  ALA   A O     1 
ATOM   662  C  CB    . ALA   A 1 86  ? 10.789  17.635 16.092 1.00 10.68 ? 83  ALA   A CB    1 
ATOM   663  N  N     . ILE   A 1 87  ? 11.396  14.558 15.006 1.00 9.71  ? 84  ILE   A N     1 
ATOM   664  C  CA    . ILE   A 1 87  ? 12.062  13.288 15.204 1.00 10.03 ? 84  ILE   A CA    1 
ATOM   665  C  C     . ILE   A 1 87  ? 13.354  13.353 16.047 1.00 10.86 ? 84  ILE   A C     1 
ATOM   666  O  O     . ILE   A 1 87  ? 13.875  12.308 16.454 1.00 11.52 ? 84  ILE   A O     1 
ATOM   667  C  CB    . ILE   A 1 87  ? 12.374  12.557 13.877 1.00 10.78 ? 84  ILE   A CB    1 
ATOM   668  C  CG1   . ILE   A 1 87  ? 13.411  13.342 13.029 1.00 12.35 ? 84  ILE   A CG1   1 
ATOM   669  C  CG2   . ILE   A 1 87  ? 11.108  12.269 13.091 1.00 10.94 ? 84  ILE   A CG2   1 
ATOM   670  C  CD1   . ILE   A 1 87  ? 14.252  12.451 12.132 1.00 14.36 ? 84  ILE   A CD1   1 
ATOM   671  N  N     . ASN   A 1 88  ? 13.818  14.564 16.321 1.00 11.37 ? 85  ASN   A N     1 
ATOM   672  C  CA    . ASN   A 1 88  ? 15.003  14.801 17.197 1.00 12.61 ? 85  ASN   A CA    1 
ATOM   673  C  C     . ASN   A 1 88  ? 14.567  15.380 18.551 1.00 13.22 ? 85  ASN   A C     1 
ATOM   674  O  O     . ASN   A 1 88  ? 15.416  15.942 19.212 1.00 15.79 ? 85  ASN   A O     1 
ATOM   675  C  CB    . ASN   A 1 88  ? 15.983  15.752 16.514 1.00 12.60 ? 85  ASN   A CB    1 
ATOM   676  C  CG    . ASN   A 1 88  ? 15.441  17.154 16.345 1.00 13.25 ? 85  ASN   A CG    1 
ATOM   677  O  OD1   . ASN   A 1 88  ? 14.257  17.351 16.182 1.00 13.02 ? 85  ASN   A OD1   1 
ATOM   678  N  ND2   . ASN   A 1 88  ? 16.304  18.153 16.373 1.00 15.10 ? 85  ASN   A ND2   1 
ATOM   679  N  N     . ASN   A 1 89  ? 13.289  15.266 18.934 1.00 12.56 ? 86  ASN   A N     1 
ATOM   680  C  CA    . ASN   A 1 89  ? 12.796  15.831 20.232 1.00 13.08 ? 86  ASN   A CA    1 
ATOM   681  C  C     . ASN   A 1 89  ? 11.858  14.809 20.877 1.00 12.81 ? 86  ASN   A C     1 
ATOM   682  O  O     . ASN   A 1 89  ? 10.725  14.771 20.558 1.00 12.54 ? 86  ASN   A O     1 
ATOM   683  C  CB    . ASN   A 1 89  ? 12.162  17.211 20.009 1.00 14.83 ? 86  ASN   A CB    1 
ATOM   684  C  CG    . ASN   A 1 89  ? 11.538  17.901 21.220 1.00 19.31 ? 86  ASN   A CG    1 
ATOM   685  O  OD1   . ASN   A 1 89  ? 11.294  17.326 22.233 1.00 17.38 ? 86  ASN   A OD1   1 
ATOM   686  N  ND2   . ASN   A 1 89  ? 11.077  19.110 21.030 1.00 23.56 ? 86  ASN   A ND2   1 
ATOM   687  N  N     . THR   A 1 90  ? 12.382  13.996 21.784 1.00 13.58 ? 87  THR   A N     1 
ATOM   688  C  CA    . THR   A 1 90  ? 11.562  12.930 22.395 1.00 15.03 ? 87  THR   A CA    1 
ATOM   689  C  C     . THR   A 1 90  ? 10.398  13.534 23.201 1.00 13.92 ? 87  THR   A C     1 
ATOM   690  O  O     . THR   A 1 90  ? 9.334   12.990 23.197 1.00 13.93 ? 87  THR   A O     1 
ATOM   691  C  CB    . THR   A 1 90  ? 12.494  12.034 23.216 1.00 17.14 ? 87  THR   A CB    1 
ATOM   692  O  OG1   . THR   A 1 90  ? 13.408  11.418 22.313 1.00 20.45 ? 87  THR   A OG1   1 
ATOM   693  C  CG2   . THR   A 1 90  ? 11.732  10.987 23.986 1.00 19.44 ? 87  THR   A CG2   1 
ATOM   694  N  N     . LYS   A 1 91  ? 10.642  14.628 23.886 1.00 14.02 ? 88  LYS   A N     1 
ATOM   695  C  CA    . LYS   A 1 91  ? 9.581   15.289 24.647 1.00 15.34 ? 88  LYS   A CA    1 
ATOM   696  C  C     . LYS   A 1 91  ? 8.393   15.637 23.735 1.00 13.55 ? 88  LYS   A C     1 
ATOM   697  O  O     . LYS   A 1 91  ? 7.245   15.418 24.110 1.00 14.38 ? 88  LYS   A O     1 
ATOM   698  C  CB    . LYS   A 1 91  ? 10.107  16.553 25.320 1.00 17.25 ? 88  LYS   A CB    1 
ATOM   699  C  CG    . LYS   A 1 91  ? 9.087   17.408 26.062 1.00 24.53 ? 88  LYS   A CG    1 
ATOM   700  C  CD    . LYS   A 1 91  ? 8.605   16.780 27.353 1.00 30.93 ? 88  LYS   A CD    1 
ATOM   701  C  CE    . LYS   A 1 91  ? 7.892   17.795 28.248 1.00 34.57 ? 88  LYS   A CE    1 
ATOM   702  N  NZ    . LYS   A 1 91  ? 6.671   18.379 27.630 1.00 36.13 ? 88  LYS   A NZ    1 
ATOM   703  N  N     . SER   A 1 92  ? 8.658   16.136 22.535 1.00 12.48 ? 89  SER   A N     1 
ATOM   704  C  CA    . SER   A 1 92  ? 7.561   16.452 21.628 1.00 11.72 ? 89  SER   A CA    1 
ATOM   705  C  C     . SER   A 1 92  ? 6.767   15.201 21.228 1.00 11.37 ? 89  SER   A C     1 
ATOM   706  O  O     . SER   A 1 92  ? 5.567   15.285 21.011 1.00 11.93 ? 89  SER   A O     1 
ATOM   707  C  CB    . SER   A 1 92  ? 8.054   17.232 20.399 1.00 12.33 ? 89  SER   A CB    1 
ATOM   708  O  OG    . SER   A 1 92  ? 8.760   16.425 19.468 1.00 11.91 ? 89  SER   A OG    1 
ATOM   709  N  N     . PHE   A 1 93  ? 7.421   14.053 21.118 1.00 11.36 ? 90  PHE   A N     1 
ATOM   710  C  CA    . PHE   A 1 93  ? 6.746   12.781 20.830 1.00 11.62 ? 90  PHE   A CA    1 
ATOM   711  C  C     . PHE   A 1 93  ? 5.906   12.352 22.022 1.00 13.10 ? 90  PHE   A C     1 
ATOM   712  O  O     . PHE   A 1 93  ? 4.753   11.946 21.861 1.00 13.40 ? 90  PHE   A O     1 
ATOM   713  C  CB    . PHE   A 1 93  ? 7.805   11.712 20.483 1.00 11.40 ? 90  PHE   A CB    1 
ATOM   714  C  CG    . PHE   A 1 93  ? 7.269   10.340 20.221 1.00 11.92 ? 90  PHE   A CG    1 
ATOM   715  C  CD1   . PHE   A 1 93  ? 6.509   10.087 19.089 1.00 10.64 ? 90  PHE   A CD1   1 
ATOM   716  C  CD2   . PHE   A 1 93  ? 7.546   9.268  21.084 1.00 13.40 ? 90  PHE   A CD2   1 
ATOM   717  C  CE1   . PHE   A 1 93  ? 6.044   8.819  18.816 1.00 12.67 ? 90  PHE   A CE1   1 
ATOM   718  C  CE2   . PHE   A 1 93  ? 7.080   8.002  20.809 1.00 15.45 ? 90  PHE   A CE2   1 
ATOM   719  C  CZ    . PHE   A 1 93  ? 6.314   7.777  19.680 1.00 13.40 ? 90  PHE   A CZ    1 
ATOM   720  N  N     . GLU   A 1 94  ? 6.434   12.493 23.238 1.00 15.19 ? 91  GLU   A N     1 
ATOM   721  C  CA    . GLU   A 1 94  ? 5.615   12.267 24.462 1.00 17.27 ? 91  GLU   A CA    1 
ATOM   722  C  C     . GLU   A 1 94  ? 4.431   13.211 24.597 1.00 17.44 ? 91  GLU   A C     1 
ATOM   723  O  O     . GLU   A 1 94  ? 3.417   12.844 25.196 1.00 23.02 ? 91  GLU   A O     1 
ATOM   724  C  CB    . GLU   A 1 94  ? 6.484   12.409 25.683 1.00 18.76 ? 91  GLU   A CB    1 
ATOM   725  C  CG    . GLU   A 1 94  ? 7.467   11.292 25.733 1.00 18.87 ? 91  GLU   A CG    1 
ATOM   726  C  CD    . GLU   A 1 94  ? 8.210   11.241 27.042 1.00 23.53 ? 91  GLU   A CD    1 
ATOM   727  O  OE1   . GLU   A 1 94  ? 7.751   11.843 28.038 1.00 34.02 ? 91  GLU   A OE1   1 
ATOM   728  O  OE2   . GLU   A 1 94  ? 9.261   10.596 27.062 1.00 18.97 ? 91  GLU   A OE2   1 
ATOM   729  N  N     . ASP   A 1 95  ? 4.554   14.435 24.126 1.00 17.27 ? 92  ASP   A N     1 
ATOM   730  C  CA    . ASP   A 1 95  ? 3.419   15.379 24.231 1.00 18.25 ? 92  ASP   A CA    1 
ATOM   731  C  C     . ASP   A 1 95  ? 2.235   14.920 23.378 1.00 14.77 ? 92  ASP   A C     1 
ATOM   732  O  O     . ASP   A 1 95  ? 1.157   15.336 23.662 1.00 15.86 ? 92  ASP   A O     1 
ATOM   733  C  CB    . ASP   A 1 95  ? 3.797   16.794 23.790 1.00 20.35 ? 92  ASP   A CB    1 
ATOM   734  C  CG    . ASP   A 1 95  ? 4.780   17.515 24.707 1.00 26.20 ? 92  ASP   A CG    1 
ATOM   735  O  OD1   . ASP   A 1 95  ? 4.899   17.149 25.867 1.00 27.88 ? 92  ASP   A OD1   1 
ATOM   736  O  OD2   . ASP   A 1 95  ? 5.454   18.406 24.230 1.00 30.07 ? 92  ASP   A OD2   1 
ATOM   737  N  N     . ILE   A 1 96  ? 2.449   14.075 22.368 1.00 14.28 ? 93  ILE   A N     1 
ATOM   738  C  CA    . ILE   A 1 96  ? 1.362   13.698 21.425 1.00 14.40 ? 93  ILE   A CA    1 
ATOM   739  C  C     . ILE   A 1 96  ? 0.180   13.093 22.191 1.00 13.47 ? 93  ILE   A C     1 
ATOM   740  O  O     . ILE   A 1 96  ? -0.906  13.453 21.898 1.00 14.17 ? 93  ILE   A O     1 
ATOM   741  C  CB    . ILE   A 1 96  ? 1.909   12.708 20.373 1.00 13.25 ? 93  ILE   A CB    1 
ATOM   742  C  CG1   . ILE   A 1 96  ? 2.933   13.379 19.445 1.00 12.32 ? 93  ILE   A CG1   1 
ATOM   743  C  CG2   . ILE   A 1 96  ? 0.755   12.071 19.601 1.00 13.37 ? 93  ILE   A CG2   1 
ATOM   744  C  CD1   . ILE   A 1 96  ? 2.355   14.466 18.555 1.00 13.22 ? 93  ILE   A CD1   1 
ATOM   745  N  N     . HIS   A 1 97  ? 0.420   12.205 23.130 1.00 13.65 ? 94  HIS   A N     1 
ATOM   746  C  CA    . HIS   A 1 97  ? -0.692  11.577 23.884 1.00 14.36 ? 94  HIS   A CA    1 
ATOM   747  C  C     . HIS   A 1 97  ? -1.593  12.644 24.532 1.00 14.60 ? 94  HIS   A C     1 
ATOM   748  O  O     . HIS   A 1 97  ? -2.780  12.477 24.528 1.00 15.95 ? 94  HIS   A O     1 
ATOM   749  C  CB    . HIS   A 1 97  ? -0.060  10.616 24.899 1.00 19.54 ? 94  HIS   A CB    1 
ATOM   750  C  CG    . HIS   A 1 97  ? -1.036  9.858  25.724 1.00 27.96 ? 94  HIS   A CG    1 
ATOM   751  N  ND1   . HIS   A 1 97  ? -1.562  8.652  25.337 1.00 34.89 ? 94  HIS   A ND1   1 
ATOM   752  C  CD2   . HIS   A 1 97  ? -1.549  10.143 26.926 1.00 31.86 ? 94  HIS   A CD2   1 
ATOM   753  C  CE1   . HIS   A 1 97  ? -2.381  8.239  26.277 1.00 36.05 ? 94  HIS   A CE1   1 
ATOM   754  N  NE2   . HIS   A 1 97  ? -2.416  9.151  27.227 1.00 35.77 ? 94  HIS   A NE2   1 
ATOM   755  N  N     . HIS   A 1 98  ? -1.016  13.710 25.029 1.00 14.14 ? 95  HIS   A N     1 
ATOM   756  C  CA    . HIS   A 1 98  ? -1.826  14.746 25.708 1.00 15.32 ? 95  HIS   A CA    1 
ATOM   757  C  C     . HIS   A 1 98  ? -2.702  15.450 24.672 1.00 14.76 ? 95  HIS   A C     1 
ATOM   758  O  O     . HIS   A 1 98  ? -3.832  15.780 24.998 1.00 16.27 ? 95  HIS   A O     1 
ATOM   759  C  CB    . HIS   A 1 98  ? -0.910  15.762 26.390 1.00 18.94 ? 95  HIS   A CB    1 
ATOM   760  C  CG    . HIS   A 1 98  ? -0.184  15.147 27.526 1.00 22.93 ? 95  HIS   A CG    1 
ATOM   761  N  ND1   . HIS   A 1 98  ? -0.817  14.741 28.681 1.00 27.59 ? 95  HIS   A ND1   1 
ATOM   762  C  CD2   . HIS   A 1 98  ? 1.113   14.849 27.678 1.00 29.06 ? 95  HIS   A CD2   1 
ATOM   763  C  CE1   . HIS   A 1 98  ? 0.077   14.227 29.488 1.00 29.08 ? 95  HIS   A CE1   1 
ATOM   764  N  NE2   . HIS   A 1 98  ? 1.256   14.274 28.893 1.00 28.98 ? 95  HIS   A NE2   1 
ATOM   765  N  N     A TYR   A 1 99  ? -2.115  15.794 23.495 0.50 14.81 ? 96  TYR   A N     1 
ATOM   766  N  N     B TYR   A 1 99  ? -2.150  15.749 23.502 0.50 15.10 ? 96  TYR   A N     1 
ATOM   767  C  CA    A TYR   A 1 99  ? -2.900  16.497 22.445 0.50 15.74 ? 96  TYR   A CA    1 
ATOM   768  C  CA    B TYR   A 1 99  ? -2.979  16.415 22.473 0.50 15.88 ? 96  TYR   A CA    1 
ATOM   769  C  C     A TYR   A 1 99  ? -4.065  15.601 22.003 0.50 17.20 ? 96  TYR   A C     1 
ATOM   770  C  C     B TYR   A 1 99  ? -4.140  15.536 22.067 0.50 16.22 ? 96  TYR   A C     1 
ATOM   771  O  O     A TYR   A 1 99  ? -5.196  16.070 21.922 0.50 18.78 ? 96  TYR   A O     1 
ATOM   772  O  O     B TYR   A 1 99  ? -5.249  16.020 21.910 0.50 17.70 ? 96  TYR   A O     1 
ATOM   773  C  CB    A TYR   A 1 99  ? -1.982  16.963 21.303 0.50 14.83 ? 96  TYR   A CB    1 
ATOM   774  C  CB    B TYR   A 1 99  ? -2.171  16.415 21.192 0.50 15.88 ? 96  TYR   A CB    1 
ATOM   775  C  CG    A TYR   A 1 99  ? -0.867  17.902 21.704 0.50 15.21 ? 96  TYR   A CG    1 
ATOM   776  C  CG    B TYR   A 1 99  ? -1.209  17.535 21.283 0.50 17.46 ? 96  TYR   A CG    1 
ATOM   777  C  CD1   A TYR   A 1 99  ? -1.039  18.904 22.652 0.50 15.53 ? 96  TYR   A CD1   1 
ATOM   778  C  CD1   B TYR   A 1 99  ? -1.694  18.740 21.683 0.50 19.93 ? 96  TYR   A CD1   1 
ATOM   779  C  CD2   A TYR   A 1 99  ? 0.397   17.773 21.171 0.50 15.96 ? 96  TYR   A CD2   1 
ATOM   780  C  CD2   B TYR   A 1 99  ? 0.139   17.397 21.019 0.50 19.96 ? 96  TYR   A CD2   1 
ATOM   781  C  CE1   A TYR   A 1 99  ? -0.014  19.764 23.023 0.50 17.67 ? 96  TYR   A CE1   1 
ATOM   782  C  CE1   B TYR   A 1 99  ? -0.824  19.768 21.857 0.50 20.44 ? 96  TYR   A CE1   1 
ATOM   783  C  CE2   A TYR   A 1 99  ? 1.434   18.612 21.540 0.50 17.51 ? 96  TYR   A CE2   1 
ATOM   784  C  CE2   B TYR   A 1 99  ? 1.009   18.456 21.150 0.50 20.74 ? 96  TYR   A CE2   1 
ATOM   785  C  CZ    A TYR   A 1 99  ? 1.246   19.617 22.471 0.50 15.07 ? 96  TYR   A CZ    1 
ATOM   786  C  CZ    B TYR   A 1 99  ? 0.495   19.679 21.515 0.50 17.92 ? 96  TYR   A CZ    1 
ATOM   787  O  OH    A TYR   A 1 99  ? 2.278   20.454 22.831 0.50 16.62 ? 96  TYR   A OH    1 
ATOM   788  O  OH    B TYR   A 1 99  ? 1.243   20.805 21.639 0.50 18.75 ? 96  TYR   A OH    1 
ATOM   789  N  N     . ARG   A 1 100 ? -3.853  14.269 21.873 1.00 16.23 ? 97  ARG   A N     1 
ATOM   790  C  CA    . ARG   A 1 100 ? -4.921  13.352 21.466 1.00 16.54 ? 97  ARG   A CA    1 
ATOM   791  C  C     . ARG   A 1 100 ? -5.990  13.295 22.563 1.00 17.77 ? 97  ARG   A C     1 
ATOM   792  O  O     . ARG   A 1 100 ? -7.158  13.314 22.248 1.00 19.33 ? 97  ARG   A O     1 
ATOM   793  C  CB    . ARG   A 1 100 ? -4.350  11.985 21.133 1.00 17.86 ? 97  ARG   A CB    1 
ATOM   794  C  CG    . ARG   A 1 100 ? -5.432  11.009 20.732 1.00 18.53 ? 97  ARG   A CG    1 
ATOM   795  C  CD    . ARG   A 1 100 ? -4.856  9.767  20.119 1.00 19.06 ? 97  ARG   A CD    1 
ATOM   796  N  NE    . ARG   A 1 100 ? -5.837  8.732  20.041 1.00 21.11 ? 97  ARG   A NE    1 
ATOM   797  C  CZ    . ARG   A 1 100 ? -6.634  8.525  19.017 1.00 23.69 ? 97  ARG   A CZ    1 
ATOM   798  N  NH1   . ARG   A 1 100 ? -6.593  9.321  17.963 1.00 23.26 ? 97  ARG   A NH1   1 
ATOM   799  N  NH2   . ARG   A 1 100 ? -7.499  7.540  19.056 1.00 26.61 ? 97  ARG   A NH2   1 
ATOM   800  N  N     . GLU   A 1 101 ? -5.579  13.188 23.815 1.00 17.74 ? 98  GLU   A N     1 
ATOM   801  C  CA    . GLU   A 1 101 ? -6.532  13.180 24.929 1.00 19.12 ? 98  GLU   A CA    1 
ATOM   802  C  C     . GLU   A 1 101 ? -7.382  14.424 24.956 1.00 17.87 ? 98  GLU   A C     1 
ATOM   803  O  O     . GLU   A 1 101 ? -8.621  14.326 25.159 1.00 19.58 ? 98  GLU   A O     1 
ATOM   804  C  CB    . GLU   A 1 101 ? -5.797  13.024 26.256 1.00 21.82 ? 98  GLU   A CB    1 
ATOM   805  C  CG    . GLU   A 1 101 ? -5.246  11.635 26.458 1.00 27.43 ? 98  GLU   A CG    1 
ATOM   806  C  CD    . GLU   A 1 101 ? -6.303  10.562 26.418 1.00 31.60 ? 98  GLU   A CD    1 
ATOM   807  O  OE1   . GLU   A 1 101 ? -7.382  10.785 27.003 1.00 39.53 ? 98  GLU   A OE1   1 
ATOM   808  O  OE2   . GLU   A 1 101 ? -6.066  9.498  25.801 1.00 39.53 ? 98  GLU   A OE2   1 
ATOM   809  N  N     . GLN   A 1 102 ? -6.768  15.580 24.748 1.00 17.06 ? 99  GLN   A N     1 
ATOM   810  C  CA    . GLN   A 1 102 ? -7.503  16.878 24.763 1.00 18.51 ? 99  GLN   A CA    1 
ATOM   811  C  C     . GLN   A 1 102 ? -8.552  16.864 23.645 1.00 16.33 ? 99  GLN   A C     1 
ATOM   812  O  O     . GLN   A 1 102 ? -9.699  17.197 23.874 1.00 15.85 ? 99  GLN   A O     1 
ATOM   813  C  CB    . GLN   A 1 102 ? -6.594  18.072 24.479 1.00 19.98 ? 99  GLN   A CB    1 
ATOM   814  C  CG    . GLN   A 1 102 ? -5.602  18.455 25.566 1.00 26.69 ? 99  GLN   A CG    1 
ATOM   815  C  CD    . GLN   A 1 102 ? -4.645  19.567 25.184 1.00 29.15 ? 99  GLN   A CD    1 
ATOM   816  O  OE1   . GLN   A 1 102 ? -4.453  19.964 24.040 1.00 34.35 ? 99  GLN   A OE1   1 
ATOM   817  N  NE2   . GLN   A 1 102 ? -3.943  20.057 26.183 1.00 41.04 ? 99  GLN   A NE2   1 
ATOM   818  N  N     . ILE   A 1 103 ? -8.142  16.477 22.442 1.00 14.63 ? 100 ILE   A N     1 
ATOM   819  C  CA    . ILE   A 1 103 ? -9.034  16.477 21.292 1.00 14.70 ? 100 ILE   A CA    1 
ATOM   820  C  C     . ILE   A 1 103 ? -10.202 15.494 21.522 1.00 14.75 ? 100 ILE   A C     1 
ATOM   821  O  O     . ILE   A 1 103 ? -11.375 15.844 21.295 1.00 17.07 ? 100 ILE   A O     1 
ATOM   822  C  CB    . ILE   A 1 103 ? -8.273  16.143 19.992 1.00 14.25 ? 100 ILE   A CB    1 
ATOM   823  C  CG1   . ILE   A 1 103 ? -7.249  17.229 19.645 1.00 14.96 ? 100 ILE   A CG1   1 
ATOM   824  C  CG2   . ILE   A 1 103 ? -9.253  15.998 18.837 1.00 15.41 ? 100 ILE   A CG2   1 
ATOM   825  C  CD1   . ILE   A 1 103 ? -6.135  16.794 18.716 1.00 13.30 ? 100 ILE   A CD1   1 
ATOM   826  N  N     . LYS   A 1 104 ? -9.914  14.281 21.965 1.00 15.61 ? 101 LYS   A N     1 
ATOM   827  C  CA    . LYS   A 1 104 ? -10.977 13.303 22.238 1.00 17.03 ? 101 LYS   A CA    1 
ATOM   828  C  C     . LYS   A 1 104 ? -11.981 13.803 23.286 1.00 16.76 ? 101 LYS   A C     1 
ATOM   829  O  O     . LYS   A 1 104 ? -13.184 13.559 23.160 1.00 18.29 ? 101 LYS   A O     1 
ATOM   830  C  CB    . LYS   A 1 104 ? -10.382 11.998 22.726 1.00 19.35 ? 101 LYS   A CB    1 
ATOM   831  C  CG    . LYS   A 1 104 ? -9.646  11.219 21.651 1.00 22.62 ? 101 LYS   A CG    1 
ATOM   832  C  CD    . LYS   A 1 104 ? -9.386  9.776  22.053 1.00 29.44 ? 101 LYS   A CD    1 
ATOM   833  C  CE    . LYS   A 1 104 ? -8.633  9.648  23.366 1.00 32.91 ? 101 LYS   A CE    1 
ATOM   834  N  NZ    . LYS   A 1 104 ? -8.336  8.239  23.729 1.00 35.18 ? 101 LYS   A NZ    1 
ATOM   835  N  N     . ARG   A 1 105 ? -11.461 14.477 24.313 1.00 16.80 ? 102 ARG   A N     1 
ATOM   836  C  CA    . ARG   A 1 105 ? -12.293 15.076 25.353 1.00 17.82 ? 102 ARG   A CA    1 
ATOM   837  C  C     . ARG   A 1 105 ? -13.251 16.071 24.754 1.00 16.99 ? 102 ARG   A C     1 
ATOM   838  O  O     . ARG   A 1 105 ? -14.453 16.006 24.994 1.00 19.38 ? 102 ARG   A O     1 
ATOM   839  C  CB    . ARG   A 1 105 ? -11.432 15.743 26.452 1.00 19.94 ? 102 ARG   A CB    1 
ATOM   840  C  CG    . ARG   A 1 105 ? -12.180 16.607 27.462 1.00 24.72 ? 102 ARG   A CG    1 
ATOM   841  C  CD    . ARG   A 1 105 ? -11.251 17.266 28.481 1.00 32.26 ? 102 ARG   A CD    1 
ATOM   842  N  NE    . ARG   A 1 105 ? -10.526 18.435 27.953 1.00 38.51 ? 102 ARG   A NE    1 
ATOM   843  C  CZ    . ARG   A 1 105 ? -11.070 19.624 27.662 1.00 41.78 ? 102 ARG   A CZ    1 
ATOM   844  N  NH1   . ARG   A 1 105 ? -12.372 19.857 27.833 1.00 46.79 ? 102 ARG   A NH1   1 
ATOM   845  N  NH2   . ARG   A 1 105 ? -10.301 20.606 27.191 1.00 47.42 ? 102 ARG   A NH2   1 
ATOM   846  N  N     . VAL   A 1 106 ? -12.738 17.009 23.983 1.00 17.73 ? 103 VAL   A N     1 
ATOM   847  C  CA    . VAL   A 1 106 ? -13.554 18.045 23.330 1.00 17.47 ? 103 VAL   A CA    1 
ATOM   848  C  C     . VAL   A 1 106 ? -14.579 17.434 22.376 1.00 17.77 ? 103 VAL   A C     1 
ATOM   849  O  O     . VAL   A 1 106 ? -15.734 17.877 22.329 1.00 18.94 ? 103 VAL   A O     1 
ATOM   850  C  CB    . VAL   A 1 106 ? -12.681 19.082 22.588 1.00 20.38 ? 103 VAL   A CB    1 
ATOM   851  C  CG1   . VAL   A 1 106 ? -13.532 20.032 21.758 1.00 23.87 ? 103 VAL   A CG1   1 
ATOM   852  C  CG2   . VAL   A 1 106 ? -11.830 19.874 23.575 1.00 20.84 ? 103 VAL   A CG2   1 
ATOM   853  N  N     . LYS   A 1 107 ? -14.170 16.415 21.624 1.00 16.18 ? 104 LYS   A N     1 
ATOM   854  C  CA    . LYS   A 1 107 ? -15.070 15.766 20.674 1.00 17.14 ? 104 LYS   A CA    1 
ATOM   855  C  C     . LYS   A 1 107 ? -16.062 14.833 21.346 1.00 17.97 ? 104 LYS   A C     1 
ATOM   856  O  O     . LYS   A 1 107 ? -17.074 14.501 20.731 1.00 22.12 ? 104 LYS   A O     1 
ATOM   857  C  CB    . LYS   A 1 107 ? -14.273 14.989 19.621 1.00 17.07 ? 104 LYS   A CB    1 
ATOM   858  C  CG    . LYS   A 1 107 ? -13.464 15.860 18.690 1.00 16.89 ? 104 LYS   A CG    1 
ATOM   859  C  CD    . LYS   A 1 107 ? -14.294 16.879 17.949 1.00 15.72 ? 104 LYS   A CD    1 
ATOM   860  C  CE    . LYS   A 1 107 ? -13.492 17.440 16.810 1.00 14.10 ? 104 LYS   A CE    1 
ATOM   861  N  NZ    . LYS   A 1 107 ? -14.226 18.525 16.128 1.00 15.44 ? 104 LYS   A NZ    1 
ATOM   862  N  N     . ASP   A 1 108 ? -15.776 14.431 22.587 1.00 20.35 ? 105 ASP   A N     1 
ATOM   863  C  CA    . ASP   A 1 108 ? -16.582 13.386 23.256 1.00 22.82 ? 105 ASP   A CA    1 
ATOM   864  C  C     . ASP   A 1 108 ? -16.624 12.176 22.320 1.00 21.09 ? 105 ASP   A C     1 
ATOM   865  O  O     . ASP   A 1 108 ? -17.642 11.531 22.237 1.00 22.76 ? 105 ASP   A O     1 
ATOM   866  C  CB    . ASP   A 1 108 ? -17.960 13.912 23.717 1.00 24.42 ? 105 ASP   A CB    1 
ATOM   867  C  CG    . ASP   A 1 108 ? -18.837 12.878 24.405 1.00 25.62 ? 105 ASP   A CG    1 
ATOM   868  O  OD1   . ASP   A 1 108 ? -18.309 12.125 25.201 1.00 30.99 ? 105 ASP   A OD1   1 
ATOM   869  O  OD2   . ASP   A 1 108 ? -20.051 12.827 24.123 1.00 29.40 ? 105 ASP   A OD2   1 
ATOM   870  N  N     . SER   A 1 109 ? -15.523 11.893 21.627 1.00 22.05 ? 106 SER   A N     1 
ATOM   871  C  CA    . SER   A 1 109 ? -15.582 10.817 20.612 1.00 26.61 ? 106 SER   A CA    1 
ATOM   872  C  C     . SER   A 1 109 ? -14.259 10.071 20.480 1.00 29.73 ? 106 SER   A C     1 
ATOM   873  O  O     . SER   A 1 109 ? -13.223 10.648 20.772 1.00 29.73 ? 106 SER   A O     1 
ATOM   874  C  CB    . SER   A 1 109 ? -15.916 11.450 19.294 1.00 25.41 ? 106 SER   A CB    1 
ATOM   875  O  OG    . SER   A 1 109 ? -16.096 10.504 18.254 1.00 31.06 ? 106 SER   A OG    1 
ATOM   876  N  N     . GLU   A 1 110 ? -14.343 8.844  19.989 1.00 33.73 ? 107 GLU   A N     1 
ATOM   877  C  CA    . GLU   A 1 110 ? -13.140 8.060  19.602 1.00 33.53 ? 107 GLU   A CA    1 
ATOM   878  C  C     . GLU   A 1 110 ? -12.874 8.273  18.109 1.00 25.90 ? 107 GLU   A C     1 
ATOM   879  O  O     . GLU   A 1 110 ? -11.780 8.009  17.663 1.00 31.89 ? 107 GLU   A O     1 
ATOM   880  C  CB    . GLU   A 1 110 ? -13.437 6.567  19.743 1.00 36.53 ? 107 GLU   A CB    1 
ATOM   881  C  CG    . GLU   A 1 110 ? -13.517 6.090  21.172 1.00 39.44 ? 107 GLU   A CG    1 
ATOM   882  C  CD    . GLU   A 1 110 ? -12.249 6.440  21.897 1.00 44.58 ? 107 GLU   A CD    1 
ATOM   883  O  OE1   . GLU   A 1 110 ? -11.249 6.604  21.217 1.00 48.47 ? 107 GLU   A OE1   1 
ATOM   884  O  OE2   . GLU   A 1 110 ? -12.290 6.560  23.121 1.00 47.26 ? 107 GLU   A OE2   1 
ATOM   885  N  N     . ASP   A 1 111 ? -13.908 8.600  17.344 1.00 27.62 ? 108 ASP   A N     1 
ATOM   886  C  CA    . ASP   A 1 111 ? -13.755 8.793  15.908 1.00 26.40 ? 108 ASP   A CA    1 
ATOM   887  C  C     . ASP   A 1 111 ? -13.188 10.175 15.734 1.00 25.96 ? 108 ASP   A C     1 
ATOM   888  O  O     . ASP   A 1 111 ? -13.959 11.106 15.533 1.00 35.60 ? 108 ASP   A O     1 
ATOM   889  C  CB    . ASP   A 1 111 ? -15.120 8.740  15.171 1.00 27.24 ? 108 ASP   A CB    1 
ATOM   890  C  CG    . ASP   A 1 111 ? -15.749 7.365  15.151 1.00 27.87 ? 108 ASP   A CG    1 
ATOM   891  O  OD1   . ASP   A 1 111 ? -15.133 6.397  15.651 1.00 33.99 ? 108 ASP   A OD1   1 
ATOM   892  O  OD2   . ASP   A 1 111 ? -16.885 7.271  14.619 1.00 31.51 ? 108 ASP   A OD2   1 
ATOM   893  N  N     . VAL   A 1 112 ? -11.859 10.357 15.825 1.00 18.99 ? 109 VAL   A N     1 
ATOM   894  C  CA    . VAL   A 1 112 ? -11.332 11.654 15.436 1.00 15.10 ? 109 VAL   A CA    1 
ATOM   895  C  C     . VAL   A 1 112 ? -10.290 11.507 14.346 1.00 12.84 ? 109 VAL   A C     1 
ATOM   896  O  O     . VAL   A 1 112 ? -9.257  10.882 14.556 1.00 14.13 ? 109 VAL   A O     1 
ATOM   897  C  CB    . VAL   A 1 112 ? -10.805 12.497 16.591 1.00 18.43 ? 109 VAL   A CB    1 
ATOM   898  C  CG1   . VAL   A 1 112 ? -10.651 13.955 16.120 1.00 19.21 ? 109 VAL   A CG1   1 
ATOM   899  C  CG2   . VAL   A 1 112 ? -11.751 12.410 17.788 1.00 20.03 ? 109 VAL   A CG2   1 
ATOM   900  N  N     . PRO   A 1 113 ? -10.548 12.138 13.187 1.00 11.05 ? 110 PRO   A N     1 
ATOM   901  C  CA    . PRO   A 1 113 ? -9.543  12.088 12.114 1.00 10.49 ? 110 PRO   A CA    1 
ATOM   902  C  C     . PRO   A 1 113 ? -8.254  12.754 12.553 1.00 9.56  ? 110 PRO   A C     1 
ATOM   903  O  O     . PRO   A 1 113 ? -8.242  13.919 12.961 1.00 9.58  ? 110 PRO   A O     1 
ATOM   904  C  CB    . PRO   A 1 113 ? -10.204 12.859 10.975 1.00 10.23 ? 110 PRO   A CB    1 
ATOM   905  C  CG    . PRO   A 1 113 ? -11.679 12.810 11.287 1.00 11.41 ? 110 PRO   A CG    1 
ATOM   906  C  CD    . PRO   A 1 113 ? -11.747 12.892 12.775 1.00 11.47 ? 110 PRO   A CD    1 
ATOM   907  N  N     . MET   A 1 114 ? -7.161  12.011 12.469 1.00 10.28 ? 111 MET   A N     1 
ATOM   908  C  CA    . MET   A 1 114 ? -5.867  12.466 12.927 1.00 9.32  ? 111 MET   A CA    1 
ATOM   909  C  C     . MET   A 1 114 ? -4.785  11.764 12.144 1.00 8.68  ? 111 MET   A C     1 
ATOM   910  O  O     . MET   A 1 114 ? -4.937  10.613 11.749 1.00 9.83  ? 111 MET   A O     1 
ATOM   911  C  CB    . MET   A 1 114 ? -5.707  12.122 14.403 1.00 11.92 ? 111 MET   A CB    1 
ATOM   912  C  CG    . MET   A 1 114 ? -6.521  12.890 15.448 1.00 16.43 ? 111 MET   A CG    1 
ATOM   913  S  SD    . MET   A 1 114 ? -5.961  12.791 17.180 1.00 23.36 ? 111 MET   A SD    1 
ATOM   914  C  CE    . MET   A 1 114 ? -4.482  11.999 16.868 1.00 10.21 ? 111 MET   A CE    1 
ATOM   915  N  N     . VAL   A 1 115 ? -3.678  12.476 11.932 1.00 7.94  ? 112 VAL   A N     1 
ATOM   916  C  CA    . VAL   A 1 115 ? -2.465  11.885 11.349 1.00 7.56  ? 112 VAL   A CA    1 
ATOM   917  C  C     . VAL   A 1 115 ? -1.309  12.251 12.265 1.00 7.42  ? 112 VAL   A C     1 
ATOM   918  O  O     . VAL   A 1 115 ? -1.193  13.416 12.682 1.00 9.32  ? 112 VAL   A O     1 
ATOM   919  C  CB    . VAL   A 1 115 ? -2.221  12.396 9.914  1.00 9.06  ? 112 VAL   A CB    1 
ATOM   920  C  CG1   . VAL   A 1 115 ? -0.883  11.929 9.366  1.00 9.77  ? 112 VAL   A CG1   1 
ATOM   921  C  CG2   . VAL   A 1 115 ? -3.355  11.941 9.022  1.00 10.01 ? 112 VAL   A CG2   1 
ATOM   922  N  N     . LEU   A 1 116 ? -0.474  11.272 12.609 1.00 7.63  ? 113 LEU   A N     1 
ATOM   923  C  CA    . LEU   A 1 116 ? 0.743   11.494 13.374 1.00 7.84  ? 113 LEU   A CA    1 
ATOM   924  C  C     . LEU   A 1 116 ? 1.853   11.862 12.391 1.00 7.48  ? 113 LEU   A C     1 
ATOM   925  O  O     . LEU   A 1 116 ? 2.128   11.127 11.447 1.00 8.15  ? 113 LEU   A O     1 
ATOM   926  C  CB    . LEU   A 1 116 ? 1.108   10.220 14.128 1.00 8.21  ? 113 LEU   A CB    1 
ATOM   927  C  CG    . LEU   A 1 116 ? 2.339   10.337 15.021 1.00 9.48  ? 113 LEU   A CG    1 
ATOM   928  C  CD1   . LEU   A 1 116 ? 2.092   11.337 16.137 1.00 10.00 ? 113 LEU   A CD1   1 
ATOM   929  C  CD2   . LEU   A 1 116 ? 2.732   8.978  15.582 1.00 10.65 ? 113 LEU   A CD2   1 
ATOM   930  N  N     . VAL   A 1 117 ? 2.488   13.009 12.627 1.00 7.45  ? 114 VAL   A N     1 
ATOM   931  C  CA    . VAL   A 1 117 ? 3.548   13.508 11.758 1.00 7.56  ? 114 VAL   A CA    1 
ATOM   932  C  C     . VAL   A 1 117 ? 4.846   13.635 12.540 1.00 7.85  ? 114 VAL   A C     1 
ATOM   933  O  O     . VAL   A 1 117 ? 4.914   14.385 13.519 1.00 8.37  ? 114 VAL   A O     1 
ATOM   934  C  CB    . VAL   A 1 117 ? 3.163   14.865 11.146 1.00 8.74  ? 114 VAL   A CB    1 
ATOM   935  C  CG1   . VAL   A 1 117 ? 4.316   15.449 10.318 1.00 9.39  ? 114 VAL   A CG1   1 
ATOM   936  C  CG2   . VAL   A 1 117 ? 1.922   14.694 10.300 1.00 9.40  ? 114 VAL   A CG2   1 
ATOM   937  N  N     . GLY   A 1 118 ? 5.863   12.910 12.091 1.00 7.51  ? 115 GLY   A N     1 
ATOM   938  C  CA    . GLY   A 1 118 ? 7.219   13.096 12.616 1.00 7.96  ? 115 GLY   A CA    1 
ATOM   939  C  C     . GLY   A 1 118 ? 7.967   13.989 11.658 1.00 7.59  ? 115 GLY   A C     1 
ATOM   940  O  O     . GLY   A 1 118 ? 8.379   13.554 10.591 1.00 8.71  ? 115 GLY   A O     1 
ATOM   941  N  N     . ASN   A 1 119 ? 8.114   15.257 12.041 1.00 7.70  ? 116 ASN   A N     1 
ATOM   942  C  CA    . ASN   A 1 119 ? 8.737   16.263 11.187 1.00 8.03  ? 116 ASN   A CA    1 
ATOM   943  C  C     . ASN   A 1 119 ? 10.225  16.360 11.455 1.00 8.98  ? 116 ASN   A C     1 
ATOM   944  O  O     . ASN   A 1 119 ? 10.743  15.791 12.424 1.00 9.26  ? 116 ASN   A O     1 
ATOM   945  C  CB    . ASN   A 1 119 ? 8.036   17.604 11.395 1.00 8.55  ? 116 ASN   A CB    1 
ATOM   946  C  CG    . ASN   A 1 119 ? 8.455   18.663 10.393 1.00 9.03  ? 116 ASN   A CG    1 
ATOM   947  O  OD1   . ASN   A 1 119 ? 8.568   18.405 9.181  1.00 9.42  ? 116 ASN   A OD1   1 
ATOM   948  N  ND2   . ASN   A 1 119 ? 8.759   19.854 10.902 1.00 10.20 ? 116 ASN   A ND2   1 
ATOM   949  N  N     . LYS   A 1 120 ? 10.908  17.072 10.570 1.00 9.25  ? 117 LYS   A N     1 
ATOM   950  C  CA    . LYS   A 1 120 ? 12.362  17.278 10.595 1.00 9.61  ? 117 LYS   A CA    1 
ATOM   951  C  C     . LYS   A 1 120 ? 13.084  15.993 10.225 1.00 10.22 ? 117 LYS   A C     1 
ATOM   952  O  O     . LYS   A 1 120 ? 14.176  15.710 10.722 1.00 10.96 ? 117 LYS   A O     1 
ATOM   953  C  CB    . LYS   A 1 120 ? 12.903  17.885 11.900 1.00 9.94  ? 117 LYS   A CB    1 
ATOM   954  C  CG    . LYS   A 1 120 ? 12.038  19.002 12.459 1.00 9.91  ? 117 LYS   A CG    1 
ATOM   955  C  CD    . LYS   A 1 120 ? 12.788  19.862 13.470 1.00 11.04 ? 117 LYS   A CD    1 
ATOM   956  C  CE    . LYS   A 1 120 ? 11.920  20.955 14.052 1.00 11.66 ? 117 LYS   A CE    1 
ATOM   957  N  NZ    . LYS   A 1 120 ? 12.677  21.776 15.046 1.00 12.83 ? 117 LYS   A NZ    1 
ATOM   958  N  N     . SER   A 1 121 ? 12.525  15.266 9.253  1.00 9.81  ? 118 SER   A N     1 
ATOM   959  C  CA    . SER   A 1 121 ? 13.118  14.021 8.841  1.00 10.98 ? 118 SER   A CA    1 
ATOM   960  C  C     . SER   A 1 121 ? 14.484  14.182 8.159  1.00 11.83 ? 118 SER   A C     1 
ATOM   961  O  O     . SER   A 1 121 ? 15.213  13.209 8.023  1.00 14.11 ? 118 SER   A O     1 
ATOM   962  C  CB    . SER   A 1 121 ? 12.199  13.243 7.905  1.00 11.56 ? 118 SER   A CB    1 
ATOM   963  O  OG    . SER   A 1 121 ? 12.113  13.891 6.668  1.00 11.70 ? 118 SER   A OG    1 
ATOM   964  N  N     . ASP   A 1 122 ? 14.797  15.406 7.740  1.00 11.18 ? 119 ASP   A N     1 
ATOM   965  C  CA    . ASP   A 1 122 ? 16.100  15.749 7.166  1.00 12.53 ? 119 ASP   A CA    1 
ATOM   966  C  C     . ASP   A 1 122 ? 17.206  15.859 8.227  1.00 12.96 ? 119 ASP   A C     1 
ATOM   967  O  O     . ASP   A 1 122 ? 18.363  15.968 7.850  1.00 15.95 ? 119 ASP   A O     1 
ATOM   968  C  CB    . ASP   A 1 122 ? 16.010  17.071 6.428  1.00 14.42 ? 119 ASP   A CB    1 
ATOM   969  C  CG    . ASP   A 1 122 ? 15.581  18.227 7.338  1.00 14.05 ? 119 ASP   A CG    1 
ATOM   970  O  OD1   . ASP   A 1 122 ? 14.378  18.266 7.720  1.00 12.69 ? 119 ASP   A OD1   1 
ATOM   971  O  OD2   . ASP   A 1 122 ? 16.432  19.069 7.751  1.00 16.76 ? 119 ASP   A OD2   1 
ATOM   972  N  N     . LEU   A 1 123 ? 16.874  15.851 9.515  1.00 12.83 ? 120 LEU   A N     1 
ATOM   973  C  CA    . LEU   A 1 123 ? 17.908  15.978 10.531 1.00 12.84 ? 120 LEU   A CA    1 
ATOM   974  C  C     . LEU   A 1 123 ? 18.471  14.601 10.842 1.00 12.25 ? 120 LEU   A C     1 
ATOM   975  O  O     . LEU   A 1 123 ? 17.734  13.656 11.083 1.00 13.98 ? 120 LEU   A O     1 
ATOM   976  C  CB    . LEU   A 1 123 ? 17.366  16.613 11.803 1.00 13.78 ? 120 LEU   A CB    1 
ATOM   977  C  CG    . LEU   A 1 123 ? 16.953  18.067 11.643 1.00 14.73 ? 120 LEU   A CG    1 
ATOM   978  C  CD1   . LEU   A 1 123 ? 16.465  18.533 13.007 1.00 16.16 ? 120 LEU   A CD1   1 
ATOM   979  C  CD2   . LEU   A 1 123 ? 18.084  18.951 11.124 1.00 16.17 ? 120 LEU   A CD2   1 
ATOM   980  N  N     . PRO   A 1 124 ? 19.817  14.474 10.854 1.00 13.15 ? 121 PRO   A N     1 
ATOM   981  C  CA    . PRO   A 1 124 ? 20.408  13.150 10.989 1.00 12.86 ? 121 PRO   A CA    1 
ATOM   982  C  C     . PRO   A 1 124 ? 20.419  12.575 12.410 1.00 14.14 ? 121 PRO   A C     1 
ATOM   983  O  O     . PRO   A 1 124 ? 20.404  11.391 12.545 1.00 16.02 ? 121 PRO   A O     1 
ATOM   984  C  CB    . PRO   A 1 124 ? 21.844  13.340 10.486 1.00 13.13 ? 121 PRO   A CB    1 
ATOM   985  C  CG    . PRO   A 1 124 ? 22.119  14.779 10.739 1.00 13.31 ? 121 PRO   A CG    1 
ATOM   986  C  CD    . PRO   A 1 124 ? 20.813  15.485 10.465 1.00 12.75 ? 121 PRO   A CD    1 
ATOM   987  N  N     . SER   A 1 125 ? 20.403  13.400 13.458 1.00 13.50 ? 122 SER   A N     1 
ATOM   988  C  CA    . SER   A 1 125 ? 20.488  12.886 14.826 1.00 13.67 ? 122 SER   A CA    1 
ATOM   989  C  C     . SER   A 1 125 ? 19.077  12.627 15.407 1.00 13.82 ? 122 SER   A C     1 
ATOM   990  O  O     . SER   A 1 125 ? 18.582  13.305 16.308 1.00 15.47 ? 122 SER   A O     1 
ATOM   991  C  CB    . SER   A 1 125 ? 21.309  13.822 15.706 1.00 14.45 ? 122 SER   A CB    1 
ATOM   992  O  OG    . SER   A 1 125 ? 22.695  13.821 15.342 1.00 16.96 ? 122 SER   A OG    1 
ATOM   993  N  N     . ARG   A 1 126 ? 18.476  11.564 14.898 1.00 13.64 ? 123 ARG   A N     1 
ATOM   994  C  CA    . ARG   A 1 126 ? 17.159  11.104 15.327 1.00 13.43 ? 123 ARG   A CA    1 
ATOM   995  C  C     . ARG   A 1 126 ? 17.202  10.682 16.788 1.00 14.15 ? 123 ARG   A C     1 
ATOM   996  O  O     . ARG   A 1 126 ? 18.165  10.050 17.218 1.00 15.85 ? 123 ARG   A O     1 
ATOM   997  C  CB    . ARG   A 1 126 ? 16.822  9.881  14.475 1.00 14.68 ? 123 ARG   A CB    1 
ATOM   998  C  CG    . ARG   A 1 126 ? 15.515  9.212  14.803 1.00 14.04 ? 123 ARG   A CG    1 
ATOM   999  C  CD    . ARG   A 1 126 ? 15.330  8.030  13.895 1.00 14.36 ? 123 ARG   A CD    1 
ATOM   1000 N  NE    . ARG   A 1 126 ? 15.048  8.407  12.518 1.00 13.98 ? 123 ARG   A NE    1 
ATOM   1001 C  CZ    . ARG   A 1 126 ? 13.843  8.704  12.049 1.00 13.66 ? 123 ARG   A CZ    1 
ATOM   1002 N  NH1   . ARG   A 1 126 ? 12.787  8.709  12.865 1.00 14.28 ? 123 ARG   A NH1   1 
ATOM   1003 N  NH2   . ARG   A 1 126 ? 13.684  8.990  10.771 1.00 14.17 ? 123 ARG   A NH2   1 
ATOM   1004 N  N     . THR   A 1 127 ? 16.146  11.009 17.529 1.00 13.17 ? 124 THR   A N     1 
ATOM   1005 C  CA    . THR   A 1 127 ? 15.934  10.483 18.882 1.00 14.13 ? 124 THR   A CA    1 
ATOM   1006 C  C     . THR   A 1 127 ? 14.659  9.658  19.010 1.00 13.48 ? 124 THR   A C     1 
ATOM   1007 O  O     . THR   A 1 127 ? 14.540  8.915  19.969 1.00 16.09 ? 124 THR   A O     1 
ATOM   1008 C  CB    . THR   A 1 127 ? 15.920  11.616 19.934 1.00 15.60 ? 124 THR   A CB    1 
ATOM   1009 O  OG1   . THR   A 1 127 ? 14.761  12.420 19.772 1.00 15.43 ? 124 THR   A OG1   1 
ATOM   1010 C  CG2   . THR   A 1 127 ? 17.149  12.497 19.844 1.00 18.49 ? 124 THR   A CG2   1 
ATOM   1011 N  N     . VAL   A 1 128 ? 13.724  9.773  18.070 1.00 12.76 ? 125 VAL   A N     1 
ATOM   1012 C  CA    . VAL   A 1 128 ? 12.506  8.965  18.089 1.00 12.42 ? 125 VAL   A CA    1 
ATOM   1013 C  C     . VAL   A 1 128 ? 12.597  7.936  16.970 1.00 12.53 ? 125 VAL   A C     1 
ATOM   1014 O  O     . VAL   A 1 128 ? 12.543  8.290  15.772 1.00 13.33 ? 125 VAL   A O     1 
ATOM   1015 C  CB    . VAL   A 1 128 ? 11.259  9.856  17.911 1.00 12.18 ? 125 VAL   A CB    1 
ATOM   1016 C  CG1   . VAL   A 1 128 ? 9.992   9.008  17.962 1.00 11.77 ? 125 VAL   A CG1   1 
ATOM   1017 C  CG2   . VAL   A 1 128 ? 11.226  10.935 18.971 1.00 14.04 ? 125 VAL   A CG2   1 
ATOM   1018 N  N     . ASP   A 1 129 ? 12.697  6.687  17.340 1.00 14.13 ? 126 ASP   A N     1 
ATOM   1019 C  CA    . ASP   A 1 129 ? 12.785  5.602  16.351 1.00 14.87 ? 126 ASP   A CA    1 
ATOM   1020 C  C     . ASP   A 1 129 ? 11.472  5.545  15.579 1.00 15.24 ? 126 ASP   A C     1 
ATOM   1021 O  O     . ASP   A 1 129 ? 10.414  5.575  16.180 1.00 14.38 ? 126 ASP   A O     1 
ATOM   1022 C  CB    . ASP   A 1 129 ? 13.044  4.275  17.064 1.00 19.29 ? 126 ASP   A CB    1 
ATOM   1023 C  CG    . ASP   A 1 129 ? 13.502  3.125  16.188 1.00 28.92 ? 126 ASP   A CG    1 
ATOM   1024 O  OD1   . ASP   A 1 129 ? 13.015  2.945  15.082 1.00 30.67 ? 126 ASP   A OD1   1 
ATOM   1025 O  OD2   . ASP   A 1 129 ? 14.388  2.414  16.650 1.00 44.86 ? 126 ASP   A OD2   1 
ATOM   1026 N  N     . THR   A 1 130 ? 11.575  5.292  14.274 1.00 16.55 ? 127 THR   A N     1 
ATOM   1027 C  CA    . THR   A 1 130 ? 10.370  5.168  13.415 1.00 18.59 ? 127 THR   A CA    1 
ATOM   1028 C  C     . THR   A 1 130 ? 9.496   4.017  13.907 1.00 17.24 ? 127 THR   A C     1 
ATOM   1029 O  O     . THR   A 1 130 ? 8.304   4.146  13.859 1.00 19.38 ? 127 THR   A O     1 
ATOM   1030 C  CB    . THR   A 1 130 ? 10.755  4.915  11.958 1.00 21.38 ? 127 THR   A CB    1 
ATOM   1031 O  OG1   . THR   A 1 130 ? 11.496  6.033  11.507 1.00 26.68 ? 127 THR   A OG1   1 
ATOM   1032 C  CG2   . THR   A 1 130 ? 9.551   4.770  11.073 1.00 26.10 ? 127 THR   A CG2   1 
ATOM   1033 N  N     . LYS   A 1 131 ? 10.073  2.916  14.359 1.00 17.87 ? 128 LYS   A N     1 
ATOM   1034 C  CA    . LYS   A 1 131 ? 9.289   1.769  14.867 1.00 21.33 ? 128 LYS   A CA    1 
ATOM   1035 C  C     . LYS   A 1 131 ? 8.390   2.169  16.046 1.00 16.99 ? 128 LYS   A C     1 
ATOM   1036 O  O     . LYS   A 1 131 ? 7.311   1.645  16.160 1.00 17.88 ? 128 LYS   A O     1 
ATOM   1037 C  CB    . LYS   A 1 131 ? 10.188  0.567  15.172 1.00 25.03 ? 128 LYS   A CB    1 
ATOM   1038 C  CG    . LYS   A 1 131 ? 11.135  0.659  16.350 1.00 30.61 ? 128 LYS   A CG    1 
ATOM   1039 C  CD    . LYS   A 1 131 ? 11.866  -0.679 16.626 1.00 37.30 ? 128 LYS   A CD    1 
ATOM   1040 C  CE    . LYS   A 1 131 ? 13.388  -0.634 16.604 1.00 41.89 ? 128 LYS   A CE    1 
ATOM   1041 N  NZ    . LYS   A 1 131 ? 13.897  0.002  15.373 1.00 44.11 ? 128 LYS   A NZ    1 
ATOM   1042 N  N     . GLN   A 1 132 ? 8.901   2.986  16.936 1.00 15.52 ? 129 GLN   A N     1 
ATOM   1043 C  CA    . GLN   A 1 132 ? 8.128   3.443  18.084 1.00 13.58 ? 129 GLN   A CA    1 
ATOM   1044 C  C     . GLN   A 1 132 ? 6.975   4.333  17.633 1.00 12.43 ? 129 GLN   A C     1 
ATOM   1045 O  O     . GLN   A 1 132 ? 5.848   4.187  18.135 1.00 12.30 ? 129 GLN   A O     1 
ATOM   1046 C  CB    . GLN   A 1 132 ? 8.997   4.220  19.070 1.00 17.95 ? 129 GLN   A CB    1 
ATOM   1047 C  CG    . GLN   A 1 132 ? 9.997   3.346  19.816 1.00 22.21 ? 129 GLN   A CG    1 
ATOM   1048 C  CD    . GLN   A 1 132 ? 10.565  4.041  21.046 1.00 29.56 ? 129 GLN   A CD    1 
ATOM   1049 O  OE1   . GLN   A 1 132 ? 10.231  5.187  21.333 1.00 36.61 ? 129 GLN   A OE1   1 
ATOM   1050 N  NE2   . GLN   A 1 132 ? 11.392  3.343  21.787 1.00 32.98 ? 129 GLN   A NE2   1 
ATOM   1051 N  N     . ALA   A 1 133 ? 7.255   5.237  16.694 1.00 11.40 ? 130 ALA   A N     1 
ATOM   1052 C  CA    . ALA   A 1 133 ? 6.199   6.121  16.199 1.00 11.01 ? 130 ALA   A CA    1 
ATOM   1053 C  C     . ALA   A 1 133 ? 5.159   5.319  15.437 1.00 10.16 ? 130 ALA   A C     1 
ATOM   1054 O  O     . ALA   A 1 133 ? 3.936   5.573  15.575 1.00 10.56 ? 130 ALA   A O     1 
ATOM   1055 C  CB    . ALA   A 1 133 ? 6.807   7.231  15.361 1.00 11.94 ? 130 ALA   A CB    1 
ATOM   1056 N  N     . GLN   A 1 134 ? 5.587   4.320  14.650 1.00 10.55 ? 131 GLN   A N     1 
ATOM   1057 C  CA    . GLN   A 1 134 ? 4.608   3.445  13.975 1.00 10.86 ? 131 GLN   A CA    1 
ATOM   1058 C  C     . GLN   A 1 134 ? 3.756   2.689  14.997 1.00 11.10 ? 131 GLN   A C     1 
ATOM   1059 O  O     . GLN   A 1 134 ? 2.557   2.529  14.808 1.00 12.30 ? 131 GLN   A O     1 
ATOM   1060 C  CB    . GLN   A 1 134 ? 5.310   2.459  13.055 1.00 11.98 ? 131 GLN   A CB    1 
ATOM   1061 C  CG    . GLN   A 1 134 ? 5.917   3.114  11.819 1.00 12.02 ? 131 GLN   A CG    1 
ATOM   1062 C  CD    . GLN   A 1 134 ? 6.559   2.105  10.891 1.00 13.02 ? 131 GLN   A CD    1 
ATOM   1063 O  OE1   . GLN   A 1 134 ? 7.000   1.048  11.336 1.00 15.97 ? 131 GLN   A OE1   1 
ATOM   1064 N  NE2   . GLN   A 1 134 ? 6.604   2.401  9.604  1.00 13.46 ? 131 GLN   A NE2   1 
ATOM   1065 N  N     . ASP   A 1 135 ? 4.387   2.194  16.061 1.00 12.32 ? 132 ASP   A N     1 
ATOM   1066 C  CA    . ASP   A 1 135 ? 3.645   1.509  17.118 1.00 12.79 ? 132 ASP   A CA    1 
ATOM   1067 C  C     . ASP   A 1 135 ? 2.612   2.419  17.767 1.00 11.69 ? 132 ASP   A C     1 
ATOM   1068 O  O     . ASP   A 1 135 ? 1.485   2.012  17.967 1.00 12.77 ? 132 ASP   A O     1 
ATOM   1069 C  CB    . ASP   A 1 135 ? 4.596   0.944  18.157 1.00 13.96 ? 132 ASP   A CB    1 
ATOM   1070 C  CG    . ASP   A 1 135 ? 3.876   0.272  19.305 1.00 15.89 ? 132 ASP   A CG    1 
ATOM   1071 O  OD1   . ASP   A 1 135 ? 3.046   -0.640 19.084 1.00 20.23 ? 132 ASP   A OD1   1 
ATOM   1072 O  OD2   . ASP   A 1 135 ? 4.113   0.701  20.446 1.00 20.43 ? 132 ASP   A OD2   1 
ATOM   1073 N  N     . LEU   A 1 136 ? 2.993   3.666  18.057 1.00 11.02 ? 133 LEU   A N     1 
ATOM   1074 C  CA    . LEU   A 1 136 ? 2.052   4.613  18.662 1.00 11.04 ? 133 LEU   A CA    1 
ATOM   1075 C  C     . LEU   A 1 136 ? 0.884   4.864  17.740 1.00 10.39 ? 133 LEU   A C     1 
ATOM   1076 O  O     . LEU   A 1 136 ? -0.271  4.808  18.155 1.00 10.96 ? 133 LEU   A O     1 
ATOM   1077 C  CB    . LEU   A 1 136 ? 2.759   5.924  19.011 1.00 11.89 ? 133 LEU   A CB    1 
ATOM   1078 C  CG    . LEU   A 1 136 ? 1.906   6.943  19.757 1.00 12.89 ? 133 LEU   A CG    1 
ATOM   1079 C  CD1   . LEU   A 1 136 ? 1.620   6.479  21.175 1.00 14.08 ? 133 LEU   A CD1   1 
ATOM   1080 C  CD2   . LEU   A 1 136 ? 2.551   8.323  19.775 1.00 14.80 ? 133 LEU   A CD2   1 
ATOM   1081 N  N     . ALA   A 1 137 ? 1.189   5.129  16.469 1.00 9.52  ? 134 ALA   A N     1 
ATOM   1082 C  CA    . ALA   A 1 137 ? 0.123   5.351  15.507 1.00 10.06 ? 134 ALA   A CA    1 
ATOM   1083 C  C     . ALA   A 1 137 ? -0.800  4.138  15.387 1.00 9.99  ? 134 ALA   A C     1 
ATOM   1084 O  O     . ALA   A 1 137 ? -2.007  4.281  15.323 1.00 11.67 ? 134 ALA   A O     1 
ATOM   1085 C  CB    . ALA   A 1 137 ? 0.695   5.770  14.150 1.00 10.44 ? 134 ALA   A CB    1 
ATOM   1086 N  N     . ARG   A 1 138 ? -0.226  2.936  15.384 1.00 11.23 ? 135 ARG   A N     1 
ATOM   1087 C  CA    . ARG   A 1 138 ? -1.043  1.721  15.336 1.00 12.65 ? 135 ARG   A CA    1 
ATOM   1088 C  C     . ARG   A 1 138 ? -1.939  1.598  16.554 1.00 12.27 ? 135 ARG   A C     1 
ATOM   1089 O  O     . ARG   A 1 138 ? -3.099  1.243  16.436 1.00 13.74 ? 135 ARG   A O     1 
ATOM   1090 C  CB    . ARG   A 1 138 ? -0.122  0.520  15.228 1.00 13.75 ? 135 ARG   A CB    1 
ATOM   1091 C  CG    . ARG   A 1 138 ? -0.810  -0.803 15.019 1.00 16.58 ? 135 ARG   A CG    1 
ATOM   1092 C  CD    . ARG   A 1 138 ? 0.207   -1.904 14.796 1.00 18.22 ? 135 ARG   A CD    1 
ATOM   1093 N  NE    . ARG   A 1 138 ? 1.028   -1.645 13.605 1.00 22.30 ? 135 ARG   A NE    1 
ATOM   1094 C  CZ    . ARG   A 1 138 ? 2.339   -1.334 13.575 1.00 25.01 ? 135 ARG   A CZ    1 
ATOM   1095 N  NH1   . ARG   A 1 138 ? 3.087   -1.275 14.665 1.00 26.74 ? 135 ARG   A NH1   1 
ATOM   1096 N  NH2   . ARG   A 1 138 ? 2.920   -1.101 12.408 1.00 31.02 ? 135 ARG   A NH2   1 
ATOM   1097 N  N     . SER   A 1 139 ? -1.412  1.958  17.719 1.00 12.45 ? 136 SER   A N     1 
ATOM   1098 C  CA    . SER   A 1 139 ? -2.218  1.927  18.947 1.00 13.86 ? 136 SER   A CA    1 
ATOM   1099 C  C     . SER   A 1 139 ? -3.406  2.890  18.901 1.00 13.24 ? 136 SER   A C     1 
ATOM   1100 O  O     . SER   A 1 139 ? -4.421  2.644  19.547 1.00 16.30 ? 136 SER   A O     1 
ATOM   1101 C  CB    . SER   A 1 139 ? -1.353  2.191  20.181 1.00 14.92 ? 136 SER   A CB    1 
ATOM   1102 O  OG    . SER   A 1 139 ? -1.117  3.559  20.393 1.00 18.37 ? 136 SER   A OG    1 
ATOM   1103 N  N     . TYR   A 1 140 ? -3.261  4.008  18.172 1.00 12.56 ? 137 TYR   A N     1 
ATOM   1104 C  CA    . TYR   A 1 140 ? -4.323  4.989  18.024 1.00 13.99 ? 137 TYR   A CA    1 
ATOM   1105 C  C     . TYR   A 1 140 ? -5.225  4.728  16.842 1.00 13.57 ? 137 TYR   A C     1 
ATOM   1106 O  O     . TYR   A 1 140 ? -6.253  5.358  16.728 1.00 15.59 ? 137 TYR   A O     1 
ATOM   1107 C  CB    . TYR   A 1 140 ? -3.752  6.384  17.860 1.00 14.39 ? 137 TYR   A CB    1 
ATOM   1108 C  CG    . TYR   A 1 140 ? -2.984  6.953  19.012 1.00 14.58 ? 137 TYR   A CG    1 
ATOM   1109 C  CD1   . TYR   A 1 140 ? -3.138  6.498  20.327 1.00 16.36 ? 137 TYR   A CD1   1 
ATOM   1110 C  CD2   . TYR   A 1 140 ? -2.104  8.010  18.792 1.00 16.45 ? 137 TYR   A CD2   1 
ATOM   1111 C  CE1   . TYR   A 1 140 ? -2.427  7.088  21.372 1.00 18.61 ? 137 TYR   A CE1   1 
ATOM   1112 C  CE2   . TYR   A 1 140 ? -1.391  8.588  19.820 1.00 18.37 ? 137 TYR   A CE2   1 
ATOM   1113 C  CZ    . TYR   A 1 140 ? -1.551  8.126  21.110 1.00 17.81 ? 137 TYR   A CZ    1 
ATOM   1114 O  OH    . TYR   A 1 140 ? -0.856  8.720  22.139 1.00 22.04 ? 137 TYR   A OH    1 
ATOM   1115 N  N     . GLY   A 1 141 ? -4.830  3.826  15.942 1.00 12.51 ? 138 GLY   A N     1 
ATOM   1116 C  CA    . GLY   A 1 141 ? -5.525  3.579  14.696 1.00 13.11 ? 138 GLY   A CA    1 
ATOM   1117 C  C     . GLY   A 1 141 ? -5.458  4.737  13.723 1.00 12.02 ? 138 GLY   A C     1 
ATOM   1118 O  O     . GLY   A 1 141 ? -6.422  4.999  13.020 1.00 13.33 ? 138 GLY   A O     1 
ATOM   1119 N  N     . ILE   A 1 142 ? -4.284  5.380  13.636 1.00 11.04 ? 139 ILE   A N     1 
ATOM   1120 C  CA    . ILE   A 1 142 ? -4.108  6.528  12.746 1.00 9.96  ? 139 ILE   A CA    1 
ATOM   1121 C  C     . ILE   A 1 142 ? -2.902  6.342  11.850 1.00 9.40  ? 139 ILE   A C     1 
ATOM   1122 O  O     . ILE   A 1 142 ? -1.972  5.612  12.214 1.00 10.30 ? 139 ILE   A O     1 
ATOM   1123 C  CB    . ILE   A 1 142 ? -3.991  7.852  13.540 1.00 10.56 ? 139 ILE   A CB    1 
ATOM   1124 C  CG1   . ILE   A 1 142 ? -2.713  7.952  14.367 1.00 10.65 ? 139 ILE   A CG1   1 
ATOM   1125 C  CG2   . ILE   A 1 142 ? -5.222  8.028  14.421 1.00 11.85 ? 139 ILE   A CG2   1 
ATOM   1126 C  CD1   . ILE   A 1 142 ? -2.567  9.263  15.121 1.00 11.73 ? 139 ILE   A CD1   1 
ATOM   1127 N  N     . PRO   A 1 143 ? -2.871  7.043  10.714 1.00 9.47  ? 140 PRO   A N     1 
ATOM   1128 C  CA    . PRO   A 1 143 ? -1.646  7.010  9.897  1.00 8.92  ? 140 PRO   A CA    1 
ATOM   1129 C  C     . PRO   A 1 143 ? -0.472  7.707  10.561 1.00 8.56  ? 140 PRO   A C     1 
ATOM   1130 O  O     . PRO   A 1 143 ? -0.670  8.640  11.352 1.00 9.22  ? 140 PRO   A O     1 
ATOM   1131 C  CB    . PRO   A 1 143 ? -2.056  7.759  8.617  1.00 9.79  ? 140 PRO   A CB    1 
ATOM   1132 C  CG    . PRO   A 1 143 ? -3.555  7.716  8.596  1.00 10.41 ? 140 PRO   A CG    1 
ATOM   1133 C  CD    . PRO   A 1 143 ? -3.971  7.740  10.038 1.00 9.60  ? 140 PRO   A CD    1 
ATOM   1134 N  N     . PHE   A 1 144 ? 0.717   7.308  10.128 1.00 8.27  ? 141 PHE   A N     1 
ATOM   1135 C  CA    . PHE   A 1 144 ? 1.985   7.920  10.561 1.00 8.18  ? 141 PHE   A CA    1 
ATOM   1136 C  C     . PHE   A 1 144 ? 2.784   8.256  9.301  1.00 7.88  ? 141 PHE   A C     1 
ATOM   1137 O  O     . PHE   A 1 144 ? 3.003   7.416  8.463  1.00 8.91  ? 141 PHE   A O     1 
ATOM   1138 C  CB    . PHE   A 1 144 ? 2.812   6.979  11.438 1.00 9.51  ? 141 PHE   A CB    1 
ATOM   1139 C  CG    . PHE   A 1 144 ? 4.204   7.515  11.705 1.00 8.85  ? 141 PHE   A CG    1 
ATOM   1140 C  CD1   . PHE   A 1 144 ? 4.391   8.772  12.266 1.00 9.65  ? 141 PHE   A CD1   1 
ATOM   1141 C  CD2   . PHE   A 1 144 ? 5.327   6.763  11.380 1.00 10.66 ? 141 PHE   A CD2   1 
ATOM   1142 C  CE1   . PHE   A 1 144 ? 5.674   9.260  12.491 1.00 10.81 ? 141 PHE   A CE1   1 
ATOM   1143 C  CE2   . PHE   A 1 144 ? 6.594   7.261  11.616 1.00 11.27 ? 141 PHE   A CE2   1 
ATOM   1144 C  CZ    . PHE   A 1 144 ? 6.772   8.489  12.196 1.00 11.20 ? 141 PHE   A CZ    1 
ATOM   1145 N  N     . ILE   A 1 145 ? 3.223   9.504  9.228  1.00 7.92  ? 142 ILE   A N     1 
ATOM   1146 C  CA    . ILE   A 1 145 ? 4.042   10.017 8.091  1.00 8.01  ? 142 ILE   A CA    1 
ATOM   1147 C  C     . ILE   A 1 145 ? 5.231   10.809 8.647  1.00 7.63  ? 142 ILE   A C     1 
ATOM   1148 O  O     . ILE   A 1 145 ? 5.023   11.595 9.559  1.00 9.08  ? 142 ILE   A O     1 
ATOM   1149 C  CB    . ILE   A 1 145 ? 3.138   10.903 7.210  1.00 8.45  ? 142 ILE   A CB    1 
ATOM   1150 C  CG1   . ILE   A 1 145 ? 2.065   10.045 6.536  1.00 9.96  ? 142 ILE   A CG1   1 
ATOM   1151 C  CG2   . ILE   A 1 145 ? 3.955   11.662 6.175  1.00 8.95  ? 142 ILE   A CG2   1 
ATOM   1152 C  CD1   . ILE   A 1 145 ? 1.087   10.835 5.730  1.00 10.69 ? 142 ILE   A CD1   1 
ATOM   1153 N  N     . GLU   A 1 146 ? 6.429   10.570 8.113  1.00 7.93  ? 143 GLU   A N     1 
ATOM   1154 C  CA    . GLU   A 1 146 ? 7.567   11.474 8.450  1.00 8.18  ? 143 GLU   A CA    1 
ATOM   1155 C  C     . GLU   A 1 146 ? 7.707   12.490 7.312  1.00 8.10  ? 143 GLU   A C     1 
ATOM   1156 O  O     . GLU   A 1 146 ? 7.679   12.128 6.157  1.00 8.81  ? 143 GLU   A O     1 
ATOM   1157 C  CB    . GLU   A 1 146 ? 8.879   10.722 8.655  1.00 9.20  ? 143 GLU   A CB    1 
ATOM   1158 C  CG    . GLU   A 1 146 ? 8.880   9.921  9.956  1.00 10.36 ? 143 GLU   A CG    1 
ATOM   1159 C  CD    . GLU   A 1 146 ? 10.225  9.390  10.431 1.00 12.31 ? 143 GLU   A CD    1 
ATOM   1160 O  OE1   . GLU   A 1 146 ? 11.186  9.607  9.727  1.00 17.67 ? 143 GLU   A OE1   1 
ATOM   1161 O  OE2   . GLU   A 1 146 ? 10.287  8.854  11.521 1.00 13.46 ? 143 GLU   A OE2   1 
ATOM   1162 N  N     . THR   A 1 147 ? 7.871   13.737 7.716  1.00 7.93  ? 144 THR   A N     1 
ATOM   1163 C  CA    . THR   A 1 147 ? 7.968   14.869 6.779  1.00 8.32  ? 144 THR   A CA    1 
ATOM   1164 C  C     . THR   A 1 147 ? 9.233   15.689 7.016  1.00 8.77  ? 144 THR   A C     1 
ATOM   1165 O  O     . THR   A 1 147 ? 9.859   15.597 8.076  1.00 9.21  ? 144 THR   A O     1 
ATOM   1166 C  CB    . THR   A 1 147 ? 6.818   15.859 7.039  1.00 8.58  ? 144 THR   A CB    1 
ATOM   1167 O  OG1   . THR   A 1 147 ? 6.844   16.347 8.400  1.00 8.67  ? 144 THR   A OG1   1 
ATOM   1168 C  CG2   . THR   A 1 147 ? 5.453   15.242 6.805  1.00 9.12  ? 144 THR   A CG2   1 
ATOM   1169 N  N     . SER   A 1 148 ? 9.580   16.460 6.002  1.00 8.81  ? 145 SER   A N     1 
ATOM   1170 C  CA    . SER   A 1 148 ? 10.568  17.542 6.165  1.00 9.99  ? 145 SER   A CA    1 
ATOM   1171 C  C     . SER   A 1 148 ? 9.987   18.830 5.585  1.00 10.69 ? 145 SER   A C     1 
ATOM   1172 O  O     . SER   A 1 148 ? 9.785   18.914 4.374  1.00 11.60 ? 145 SER   A O     1 
ATOM   1173 C  CB    . SER   A 1 148 ? 11.883  17.207 5.534  1.00 10.75 ? 145 SER   A CB    1 
ATOM   1174 O  OG    . SER   A 1 148 ? 12.714  18.368 5.605  1.00 12.89 ? 145 SER   A OG    1 
ATOM   1175 N  N     . ALA   A 1 149 ? 9.635   19.771 6.447  1.00 11.40 ? 146 ALA   A N     1 
ATOM   1176 C  CA    . ALA   A 1 149 ? 9.232   21.103 5.956  1.00 12.88 ? 146 ALA   A CA    1 
ATOM   1177 C  C     . ALA   A 1 149 ? 10.364  21.820 5.228  1.00 14.85 ? 146 ALA   A C     1 
ATOM   1178 O  O     . ALA   A 1 149 ? 10.129  22.675 4.383  1.00 16.92 ? 146 ALA   A O     1 
ATOM   1179 C  CB    . ALA   A 1 149 ? 8.732   21.972 7.089  1.00 13.50 ? 146 ALA   A CB    1 
ATOM   1180 N  N     . LYS   A 1 150 ? 11.595  21.431 5.515  1.00 14.01 ? 147 LYS   A N     1 
ATOM   1181 C  CA    . LYS   A 1 150 ? 12.758  22.053 4.890  1.00 16.20 ? 147 LYS   A CA    1 
ATOM   1182 C  C     . LYS   A 1 150 ? 12.868  21.610 3.440  1.00 16.20 ? 147 LYS   A C     1 
ATOM   1183 O  O     . LYS   A 1 150 ? 13.076  22.447 2.551  1.00 19.93 ? 147 LYS   A O     1 
ATOM   1184 C  CB    . LYS   A 1 150 ? 14.023  21.721 5.660  1.00 17.61 ? 147 LYS   A CB    1 
ATOM   1185 C  CG    . LYS   A 1 150 ? 15.262  22.424 5.139  1.00 20.18 ? 147 LYS   A CG    1 
ATOM   1186 C  CD    . LYS   A 1 150 ? 16.425  22.321 6.111  1.00 23.22 ? 147 LYS   A CD    1 
ATOM   1187 C  CE    . LYS   A 1 150 ? 17.647  23.050 5.588  1.00 27.23 ? 147 LYS   A CE    1 
ATOM   1188 N  NZ    . LYS   A 1 150 ? 18.825  22.702 6.404  1.00 32.15 ? 147 LYS   A NZ    1 
ATOM   1189 N  N     . THR   A 1 151 ? 12.746  20.308 3.194  1.00 15.60 ? 148 THR   A N     1 
ATOM   1190 C  CA    . THR   A 1 151 ? 12.931  19.803 1.806  1.00 16.14 ? 148 THR   A CA    1 
ATOM   1191 C  C     . THR   A 1 151 ? 11.605  19.546 1.107  1.00 14.82 ? 148 THR   A C     1 
ATOM   1192 O  O     . THR   A 1 151 ? 11.693  19.203 -0.032 1.00 17.49 ? 148 THR   A O     1 
ATOM   1193 C  CB    . THR   A 1 151 ? 13.638  18.457 1.788  1.00 17.38 ? 148 THR   A CB    1 
ATOM   1194 O  OG1   . THR   A 1 151 ? 12.748  17.485 2.352  1.00 17.08 ? 148 THR   A OG1   1 
ATOM   1195 C  CG2   . THR   A 1 151 ? 14.968  18.485 2.501  1.00 18.48 ? 148 THR   A CG2   1 
ATOM   1196 N  N     . ARG   A 1 152 ? 10.473  19.690 1.808  1.00 14.43 ? 149 ARG   A N     1 
ATOM   1197 C  CA    . ARG   A 1 152 ? 9.068   19.456 1.353  1.00 15.15 ? 149 ARG   A CA    1 
ATOM   1198 C  C     . ARG   A 1 152 ? 8.737   17.968 1.313  1.00 13.68 ? 149 ARG   A C     1 
ATOM   1199 O  O     . ARG   A 1 152 ? 7.613   17.648 0.918  1.00 15.04 ? 149 ARG   A O     1 
ATOM   1200 C  CB    . ARG   A 1 152 ? 8.666   20.052 -0.001 1.00 19.33 ? 149 ARG   A CB    1 
ATOM   1201 C  CG    . ARG   A 1 152 ? 8.931   21.524 -0.113 1.00 26.29 ? 149 ARG   A CG    1 
ATOM   1202 C  CD    . ARG   A 1 152 ? 8.327   22.084 -1.380 1.00 28.86 ? 149 ARG   A CD    1 
ATOM   1203 N  NE    . ARG   A 1 152 ? 7.129   21.469 -1.868 1.00 30.49 ? 149 ARG   A NE    1 
ATOM   1204 C  CZ    . ARG   A 1 152 ? 5.917   21.869 -1.588 1.00 28.94 ? 149 ARG   A CZ    1 
ATOM   1205 N  NH1   . ARG   A 1 152 ? 5.737   22.885 -0.800 1.00 24.82 ? 149 ARG   A NH1   1 
ATOM   1206 N  NH2   . ARG   A 1 152 ? 4.896   21.235 -2.100 1.00 31.32 ? 149 ARG   A NH2   1 
ATOM   1207 N  N     . GLN   A 1 153 ? 9.600   17.112 1.829  1.00 11.12 ? 150 GLN   A N     1 
ATOM   1208 C  CA    . GLN   A 1 153 ? 9.301   15.664 1.763  1.00 11.00 ? 150 GLN   A CA    1 
ATOM   1209 C  C     . GLN   A 1 153 ? 8.015   15.335 2.523  1.00 9.43  ? 150 GLN   A C     1 
ATOM   1210 O  O     . GLN   A 1 153 ? 7.909   15.623 3.717  1.00 9.42  ? 150 GLN   A O     1 
ATOM   1211 C  CB    . GLN   A 1 153 ? 10.429  14.852 2.380  1.00 11.27 ? 150 GLN   A CB    1 
ATOM   1212 C  CG    . GLN   A 1 153 ? 10.489  13.437 1.818  1.00 14.31 ? 150 GLN   A CG    1 
ATOM   1213 C  CD    . GLN   A 1 153 ? 11.129  13.413 0.444  1.00 15.49 ? 150 GLN   A CD    1 
ATOM   1214 O  OE1   . GLN   A 1 153 ? 12.275  13.800 0.314  1.00 18.18 ? 150 GLN   A OE1   1 
ATOM   1215 N  NE2   . GLN   A 1 153 ? 10.379  12.990 -0.551 1.00 17.20 ? 150 GLN   A NE2   1 
ATOM   1216 N  N     . ARG   A 1 154 ? 7.076   14.766 1.766  1.00 8.80  ? 151 ARG   A N     1 
ATOM   1217 C  CA    . ARG   A 1 154 ? 5.786   14.312 2.272  1.00 8.71  ? 151 ARG   A CA    1 
ATOM   1218 C  C     . ARG   A 1 154 ? 4.894   15.376 2.892  1.00 8.61  ? 151 ARG   A C     1 
ATOM   1219 O  O     . ARG   A 1 154 ? 3.960   15.048 3.606  1.00 8.85  ? 151 ARG   A O     1 
ATOM   1220 C  CB    . ARG   A 1 154 ? 5.916   13.087 3.196  1.00 9.28  ? 151 ARG   A CB    1 
ATOM   1221 C  CG    . ARG   A 1 154 ? 6.609   11.923 2.512  1.00 10.49 ? 151 ARG   A CG    1 
ATOM   1222 C  CD    . ARG   A 1 154 ? 6.314   10.613 3.189  1.00 10.93 ? 151 ARG   A CD    1 
ATOM   1223 N  NE    . ARG   A 1 154 ? 4.963   10.139 2.909  1.00 12.09 ? 151 ARG   A NE    1 
ATOM   1224 C  CZ    . ARG   A 1 154 ? 4.398   9.076  3.480  1.00 11.62 ? 151 ARG   A CZ    1 
ATOM   1225 N  NH1   . ARG   A 1 154 ? 3.174   8.713  3.135  1.00 14.08 ? 151 ARG   A NH1   1 
ATOM   1226 N  NH2   . ARG   A 1 154 ? 5.029   8.410  4.418  1.00 11.38 ? 151 ARG   A NH2   1 
ATOM   1227 N  N     . VAL   A 1 155 ? 5.129   16.644 2.565  1.00 9.07  ? 152 VAL   A N     1 
ATOM   1228 C  CA    . VAL   A 1 155 ? 4.310   17.699 3.131  1.00 10.51 ? 152 VAL   A CA    1 
ATOM   1229 C  C     . VAL   A 1 155 ? 2.874   17.626 2.591  1.00 9.50  ? 152 VAL   A C     1 
ATOM   1230 O  O     . VAL   A 1 155 ? 1.914   17.606 3.356  1.00 9.75  ? 152 VAL   A O     1 
ATOM   1231 C  CB    . VAL   A 1 155 ? 4.941   19.095 2.938  1.00 12.36 ? 152 VAL   A CB    1 
ATOM   1232 C  CG1   . VAL   A 1 155 ? 3.978   20.192 3.361  1.00 14.57 ? 152 VAL   A CG1   1 
ATOM   1233 C  CG2   . VAL   A 1 155 ? 6.230   19.183 3.760  1.00 13.93 ? 152 VAL   A CG2   1 
ATOM   1234 N  N     . GLU   A 1 156 ? 2.723   17.565 1.266  1.00 10.42 ? 153 GLU   A N     1 
ATOM   1235 C  CA    . GLU   A 1 156 ? 1.362   17.446 0.704  1.00 11.33 ? 153 GLU   A CA    1 
ATOM   1236 C  C     . GLU   A 1 156 ? 0.763   16.109 1.165  1.00 10.23 ? 153 GLU   A C     1 
ATOM   1237 O  O     . GLU   A 1 156 ? -0.356  16.072 1.549  1.00 11.09 ? 153 GLU   A O     1 
ATOM   1238 C  CB    . GLU   A 1 156 ? 1.476   17.528 -0.816 1.00 13.42 ? 153 GLU   A CB    1 
ATOM   1239 C  CG    . GLU   A 1 156 ? 1.877   18.934 -1.318 1.00 16.86 ? 153 GLU   A CG    1 
ATOM   1240 C  CD    . GLU   A 1 156 ? 1.872   19.110 -2.833 1.00 22.86 ? 153 GLU   A CD    1 
ATOM   1241 O  OE1   . GLU   A 1 156 ? 2.125   18.114 -3.539 1.00 31.07 ? 153 GLU   A OE1   1 
ATOM   1242 O  OE2   . GLU   A 1 156 ? 1.613   20.238 -3.297 1.00 30.13 ? 153 GLU   A OE2   1 
ATOM   1243 N  N     . ASP   A 1 157 ? 1.569   15.067 1.180  1.00 10.05 ? 154 ASP   A N     1 
ATOM   1244 C  CA    . ASP   A 1 157 ? 1.063   13.745 1.609  1.00 9.68  ? 154 ASP   A CA    1 
ATOM   1245 C  C     . ASP   A 1 157 ? 0.465   13.800 3.033  1.00 8.83  ? 154 ASP   A C     1 
ATOM   1246 O  O     . ASP   A 1 157 ? -0.570  13.235 3.273  1.00 9.38  ? 154 ASP   A O     1 
ATOM   1247 C  CB    . ASP   A 1 157 ? 2.292   12.858 1.635  1.00 12.38 ? 154 ASP   A CB    1 
ATOM   1248 C  CG    . ASP   A 1 157 ? 2.044   11.408 1.464  1.00 17.60 ? 154 ASP   A CG    1 
ATOM   1249 O  OD1   . ASP   A 1 157 ? 0.958   10.958 1.822  1.00 22.22 ? 154 ASP   A OD1   1 
ATOM   1250 O  OD2   . ASP   A 1 157 ? 2.999   10.781 0.974  1.00 23.82 ? 154 ASP   A OD2   1 
ATOM   1251 N  N     . ALA   A 1 158 ? 1.130   14.499 3.945  1.00 8.25  ? 155 ALA   A N     1 
ATOM   1252 C  CA    . ALA   A 1 158 ? 0.609   14.555 5.333  1.00 8.24  ? 155 ALA   A CA    1 
ATOM   1253 C  C     . ALA   A 1 158 ? -0.777  15.225 5.349  1.00 7.75  ? 155 ALA   A C     1 
ATOM   1254 O  O     . ALA   A 1 158 ? -1.679  14.677 5.914  1.00 8.63  ? 155 ALA   A O     1 
ATOM   1255 C  CB    . ALA   A 1 158 ? 1.593   15.293 6.209  1.00 9.25  ? 155 ALA   A CB    1 
ATOM   1256 N  N     . PHE   A 1 159 ? -0.908  16.387 4.702  1.00 8.36  ? 156 PHE   A N     1 
ATOM   1257 C  CA    . PHE   A 1 159 ? -2.187  17.079 4.717  1.00 8.72  ? 156 PHE   A CA    1 
ATOM   1258 C  C     . PHE   A 1 159 ? -3.259  16.317 3.930  1.00 8.57  ? 156 PHE   A C     1 
ATOM   1259 O  O     . PHE   A 1 159 ? -4.425  16.246 4.346  1.00 9.09  ? 156 PHE   A O     1 
ATOM   1260 C  CB    . PHE   A 1 159 ? -2.004  18.502 4.169  1.00 9.69  ? 156 PHE   A CB    1 
ATOM   1261 C  CG    . PHE   A 1 159 ? -1.333  19.441 5.130  1.00 9.77  ? 156 PHE   A CG    1 
ATOM   1262 C  CD1   . PHE   A 1 159 ? -2.068  20.108 6.077  1.00 10.85 ? 156 PHE   A CD1   1 
ATOM   1263 C  CD2   . PHE   A 1 159 ? 0.018   19.659 5.082  1.00 9.98  ? 156 PHE   A CD2   1 
ATOM   1264 C  CE1   . PHE   A 1 159 ? -1.465  20.995 6.952  1.00 11.65 ? 156 PHE   A CE1   1 
ATOM   1265 C  CE2   . PHE   A 1 159 ? 0.639   20.558 5.960  1.00 11.34 ? 156 PHE   A CE2   1 
ATOM   1266 C  CZ    . PHE   A 1 159 ? -0.119  21.223 6.888  1.00 11.29 ? 156 PHE   A CZ    1 
ATOM   1267 N  N     . TYR   A 1 160 ? -2.878  15.741 2.773  1.00 8.14  ? 157 TYR   A N     1 
ATOM   1268 C  CA    . TYR   A 1 160 ? -3.866  15.050 1.934  1.00 8.13  ? 157 TYR   A CA    1 
ATOM   1269 C  C     . TYR   A 1 160 ? -4.306  13.742 2.577  1.00 7.93  ? 157 TYR   A C     1 
ATOM   1270 O  O     . TYR   A 1 160 ? -5.469  13.332 2.452  1.00 8.98  ? 157 TYR   A O     1 
ATOM   1271 C  CB    . TYR   A 1 160 ? -3.300  14.775 0.560  1.00 9.38  ? 157 TYR   A CB    1 
ATOM   1272 C  CG    . TYR   A 1 160 ? -2.994  15.982 -0.304 1.00 10.94 ? 157 TYR   A CG    1 
ATOM   1273 C  CD1   . TYR   A 1 160 ? -3.077  17.311 0.153  1.00 12.53 ? 157 TYR   A CD1   1 
ATOM   1274 C  CD2   . TYR   A 1 160 ? -2.571  15.775 -1.599 1.00 13.76 ? 157 TYR   A CD2   1 
ATOM   1275 C  CE1   . TYR   A 1 160 ? -2.760  18.381 -0.689 1.00 15.80 ? 157 TYR   A CE1   1 
ATOM   1276 C  CE2   . TYR   A 1 160 ? -2.279  16.830 -2.438 1.00 17.70 ? 157 TYR   A CE2   1 
ATOM   1277 C  CZ    . TYR   A 1 160 ? -2.363  18.119 -1.983 1.00 19.08 ? 157 TYR   A CZ    1 
ATOM   1278 O  OH    . TYR   A 1 160 ? -2.067  19.151 -2.864 1.00 23.44 ? 157 TYR   A OH    1 
ATOM   1279 N  N     . THR   A 1 161 ? -3.406  13.113 3.319  1.00 8.10  ? 158 THR   A N     1 
ATOM   1280 C  CA    . THR   A 1 161 ? -3.776  11.920 4.074  1.00 7.91  ? 158 THR   A CA    1 
ATOM   1281 C  C     . THR   A 1 161 ? -4.802  12.256 5.131  1.00 8.06  ? 158 THR   A C     1 
ATOM   1282 O  O     . THR   A 1 161 ? -5.752  11.503 5.361  1.00 8.98  ? 158 THR   A O     1 
ATOM   1283 C  CB    . THR   A 1 161 ? -2.530  11.265 4.692  1.00 8.53  ? 158 THR   A CB    1 
ATOM   1284 O  OG1   . THR   A 1 161 ? -1.696  10.779 3.638  1.00 9.06  ? 158 THR   A OG1   1 
ATOM   1285 C  CG2   . THR   A 1 161 ? -2.891  10.117 5.601  1.00 9.53  ? 158 THR   A CG2   1 
ATOM   1286 N  N     . LEU   A 1 162 ? -4.660  13.406 5.791  1.00 8.02  ? 159 LEU   A N     1 
ATOM   1287 C  CA    . LEU   A 1 162 ? -5.646  13.847 6.757  1.00 8.12  ? 159 LEU   A CA    1 
ATOM   1288 C  C     . LEU   A 1 162 ? -7.022  14.098 6.111  1.00 8.36  ? 159 LEU   A C     1 
ATOM   1289 O  O     . LEU   A 1 162 ? -8.052  13.743 6.670  1.00 9.10  ? 159 LEU   A O     1 
ATOM   1290 C  CB    . LEU   A 1 162 ? -5.156  15.081 7.512  1.00 8.08  ? 159 LEU   A CB    1 
ATOM   1291 C  CG    . LEU   A 1 162 ? -6.051  15.583 8.630  1.00 8.51  ? 159 LEU   A CG    1 
ATOM   1292 C  CD1   . LEU   A 1 162 ? -6.354  14.525 9.666  1.00 9.12  ? 159 LEU   A CD1   1 
ATOM   1293 C  CD2   . LEU   A 1 162 ? -5.405  16.802 9.281  1.00 9.41  ? 159 LEU   A CD2   1 
ATOM   1294 N  N     . VAL   A 1 163 ? -7.031  14.724 4.939  1.00 8.60  ? 160 VAL   A N     1 
ATOM   1295 C  CA    . VAL   A 1 163 ? -8.272  14.890 4.170  1.00 9.14  ? 160 VAL   A CA    1 
ATOM   1296 C  C     . VAL   A 1 163 ? -8.931  13.519 3.942  1.00 8.64  ? 160 VAL   A C     1 
ATOM   1297 O  O     . VAL   A 1 163 ? -10.148 13.346 4.147  1.00 10.36 ? 160 VAL   A O     1 
ATOM   1298 C  CB    . VAL   A 1 163 ? -7.996  15.627 2.845  1.00 9.54  ? 160 VAL   A CB    1 
ATOM   1299 C  CG1   . VAL   A 1 163 ? -9.186  15.572 1.905  1.00 11.42 ? 160 VAL   A CG1   1 
ATOM   1300 C  CG2   . VAL   A 1 163 ? -7.620  17.081 3.116  1.00 10.78 ? 160 VAL   A CG2   1 
ATOM   1301 N  N     . ARG   A 1 164 ? -8.137  12.551 3.502  1.00 9.07  ? 161 ARG   A N     1 
ATOM   1302 C  CA    . ARG   A 1 164 ? -8.665  11.203 3.251  1.00 9.43  ? 161 ARG   A CA    1 
ATOM   1303 C  C     . ARG   A 1 164 ? -9.275  10.607 4.523  1.00 10.24 ? 161 ARG   A C     1 
ATOM   1304 O  O     . ARG   A 1 164 ? -10.325 9.954  4.470  1.00 11.07 ? 161 ARG   A O     1 
ATOM   1305 C  CB    . ARG   A 1 164 ? -7.576  10.297 2.658  1.00 9.10  ? 161 ARG   A CB    1 
ATOM   1306 C  CG    . ARG   A 1 164 ? -7.215  10.655 1.229  1.00 9.37  ? 161 ARG   A CG    1 
ATOM   1307 C  CD    . ARG   A 1 164 ? -5.956  9.956  0.773  1.00 10.22 ? 161 ARG   A CD    1 
ATOM   1308 N  NE    . ARG   A 1 164 ? -5.815  9.967  -0.680 1.00 11.60 ? 161 ARG   A NE    1 
ATOM   1309 C  CZ    . ARG   A 1 164 ? -4.768  9.505  -1.354 1.00 14.23 ? 161 ARG   A CZ    1 
ATOM   1310 N  NH1   . ARG   A 1 164 ? -3.662  9.140  -0.711 1.00 15.65 ? 161 ARG   A NH1   1 
ATOM   1311 N  NH2   . ARG   A 1 164 ? -4.804  9.435  -2.687 1.00 18.09 ? 161 ARG   A NH2   1 
ATOM   1312 N  N     . GLU   A 1 165 ? -8.620  10.802 5.675  1.00 9.89  ? 162 GLU   A N     1 
ATOM   1313 C  CA    . GLU   A 1 165 ? -9.170  10.318 6.939  1.00 9.36  ? 162 GLU   A CA    1 
ATOM   1314 C  C     . GLU   A 1 165 ? -10.525 10.960 7.234  1.00 10.09 ? 162 GLU   A C     1 
ATOM   1315 O  O     . GLU   A 1 165 ? -11.482 10.265 7.613  1.00 12.27 ? 162 GLU   A O     1 
ATOM   1316 C  CB    . GLU   A 1 165 ? -8.212  10.562 8.109  1.00 10.21 ? 162 GLU   A CB    1 
ATOM   1317 C  CG    . GLU   A 1 165 ? -6.898  9.761  8.052  1.00 10.81 ? 162 GLU   A CG    1 
ATOM   1318 C  CD    . GLU   A 1 165 ? -7.168  8.272  8.178  1.00 12.88 ? 162 GLU   A CD    1 
ATOM   1319 O  OE1   . GLU   A 1 165 ? -7.656  7.843  9.232  1.00 15.09 ? 162 GLU   A OE1   1 
ATOM   1320 O  OE2   . GLU   A 1 165 ? -6.874  7.509  7.241  1.00 15.64 ? 162 GLU   A OE2   1 
ATOM   1321 N  N     . ILE   A 1 166 ? -10.607 12.269 7.065  1.00 9.69  ? 163 ILE   A N     1 
ATOM   1322 C  CA    . ILE   A 1 166 ? -11.886 12.956 7.287  1.00 10.55 ? 163 ILE   A CA    1 
ATOM   1323 C  C     . ILE   A 1 166 ? -12.968 12.429 6.350  1.00 11.16 ? 163 ILE   A C     1 
ATOM   1324 O  O     . ILE   A 1 166 ? -14.098 12.086 6.790  1.00 12.60 ? 163 ILE   A O     1 
ATOM   1325 C  CB    . ILE   A 1 166 ? -11.762 14.464 7.075  1.00 10.78 ? 163 ILE   A CB    1 
ATOM   1326 C  CG1   . ILE   A 1 166 ? -10.870 15.101 8.146  1.00 10.86 ? 163 ILE   A CG1   1 
ATOM   1327 C  CG2   . ILE   A 1 166 ? -13.139 15.129 7.058  1.00 12.28 ? 163 ILE   A CG2   1 
ATOM   1328 C  CD1   . ILE   A 1 166 ? -10.367 16.468 7.761  1.00 11.83 ? 163 ILE   A CD1   1 
ATOM   1329 N  N     . ARG   A 1 167 ? -12.637 12.343 5.059  1.00 11.55 ? 164 ARG   A N     1 
ATOM   1330 C  CA    . ARG   A 1 167 ? -13.608 11.943 4.053  1.00 11.99 ? 164 ARG   A CA    1 
ATOM   1331 C  C     . ARG   A 1 167 ? -14.155 10.583 4.444  1.00 12.06 ? 164 ARG   A C     1 
ATOM   1332 O  O     . ARG   A 1 167 ? -15.370 10.334 4.321  1.00 15.34 ? 164 ARG   A O     1 
ATOM   1333 C  CB    . ARG   A 1 167 ? -12.967 11.959 2.659  1.00 11.68 ? 164 ARG   A CB    1 
ATOM   1334 C  CG    . ARG   A 1 167 ? -13.934 11.695 1.537  1.00 14.40 ? 164 ARG   A CG    1 
ATOM   1335 C  CD    . ARG   A 1 167 ? -13.147 11.393 0.309  1.00 14.96 ? 164 ARG   A CD    1 
ATOM   1336 N  NE    . ARG   A 1 167 ? -12.472 12.535 -0.276 1.00 13.66 ? 164 ARG   A NE    1 
ATOM   1337 C  CZ    . ARG   A 1 167 ? -11.243 12.532 -0.818 1.00 11.69 ? 164 ARG   A CZ    1 
ATOM   1338 N  NH1   . ARG   A 1 167 ? -10.828 13.615 -1.455 1.00 12.65 ? 164 ARG   A NH1   1 
ATOM   1339 N  NH2   . ARG   A 1 167 ? -10.411 11.493 -0.722 1.00 12.14 ? 164 ARG   A NH2   1 
ATOM   1340 N  N     . GLN   A 1 168 ? -13.291 9.669  4.876  1.00 12.37 ? 165 GLN   A N     1 
ATOM   1341 C  CA    . GLN   A 1 168 ? -13.699 8.338  5.281  1.00 15.29 ? 165 GLN   A CA    1 
ATOM   1342 C  C     . GLN   A 1 168 ? -14.573 8.324  6.530  1.00 12.42 ? 165 GLN   A C     1 
ATOM   1343 O  O     . GLN   A 1 168 ? -15.597 7.629  6.555  1.00 15.96 ? 165 GLN   A O     1 
ATOM   1344 C  CB    . GLN   A 1 168 ? -12.507 7.433  5.515  1.00 17.18 ? 165 GLN   A CB    1 
ATOM   1345 C  CG    . GLN   A 1 168 ? -11.819 7.019  4.238  1.00 18.86 ? 165 GLN   A CG    1 
ATOM   1346 C  CD    . GLN   A 1 168 ? -10.400 6.539  4.470  1.00 21.62 ? 165 GLN   A CD    1 
ATOM   1347 O  OE1   . GLN   A 1 168 ? -10.136 5.782  5.407  1.00 27.20 ? 165 GLN   A OE1   1 
ATOM   1348 N  NE2   . GLN   A 1 168 ? -9.470  6.977  3.625  1.00 24.11 ? 165 GLN   A NE2   1 
ATOM   1349 N  N     . TYR   A 1 169 ? -14.174 9.081  7.548  1.00 13.04 ? 166 TYR   A N     1 
ATOM   1350 C  CA    . TYR   A 1 169 ? -14.981 9.153  8.765  1.00 13.75 ? 166 TYR   A CA    1 
ATOM   1351 C  C     . TYR   A 1 169 ? -16.387 9.703  8.473  1.00 12.79 ? 166 TYR   A C     1 
ATOM   1352 O  O     . TYR   A 1 169 ? -17.338 9.363  9.209  1.00 15.39 ? 166 TYR   A O     1 
ATOM   1353 C  CB    . TYR   A 1 169 ? -14.280 9.963  9.846  1.00 14.18 ? 166 TYR   A CB    1 
ATOM   1354 C  CG    . TYR   A 1 169 ? -13.399 9.144  10.747 1.00 14.79 ? 166 TYR   A CG    1 
ATOM   1355 C  CD1   . TYR   A 1 169 ? -13.953 8.267  11.690 1.00 21.92 ? 166 TYR   A CD1   1 
ATOM   1356 C  CD2   . TYR   A 1 169 ? -12.015 9.188  10.650 1.00 16.64 ? 166 TYR   A CD2   1 
ATOM   1357 C  CE1   . TYR   A 1 169 ? -13.151 7.512  12.536 1.00 21.78 ? 166 TYR   A CE1   1 
ATOM   1358 C  CE2   . TYR   A 1 169 ? -11.201 8.444  11.502 1.00 17.72 ? 166 TYR   A CE2   1 
ATOM   1359 C  CZ    . TYR   A 1 169 ? -11.765 7.613  12.437 1.00 21.70 ? 166 TYR   A CZ    1 
ATOM   1360 O  OH    . TYR   A 1 169 ? -10.984 6.869  13.285 1.00 25.51 ? 166 TYR   A OH    1 
ATOM   1361 N  N     . ARG   A 1 170 ? -16.534 10.569 7.464  1.00 14.01 ? 167 ARG   A N     1 
ATOM   1362 C  CA    . ARG   A 1 170 ? -17.872 11.090 7.084  1.00 14.01 ? 167 ARG   A CA    1 
ATOM   1363 C  C     . ARG   A 1 170 ? -18.811 9.986  6.608  1.00 14.92 ? 167 ARG   A C     1 
ATOM   1364 O  O     . ARG   A 1 170 ? -20.035 10.136 6.691  1.00 14.73 ? 167 ARG   A O     1 
ATOM   1365 C  CB    . ARG   A 1 170 ? -17.771 12.200 6.032  1.00 15.25 ? 167 ARG   A CB    1 
ATOM   1366 C  CG    . ARG   A 1 170 ? -17.187 13.495 6.546  1.00 15.62 ? 167 ARG   A CG    1 
ATOM   1367 C  CD    . ARG   A 1 170 ? -17.127 14.543 5.455  1.00 14.99 ? 167 ARG   A CD    1 
ATOM   1368 N  NE    . ARG   A 1 170 ? -16.614 15.854 5.895  1.00 16.71 ? 167 ARG   A NE    1 
ATOM   1369 C  CZ    . ARG   A 1 170 ? -15.880 16.685 5.159  1.00 17.05 ? 167 ARG   A CZ    1 
ATOM   1370 N  NH1   . ARG   A 1 170 ? -15.557 16.381 3.909  1.00 18.93 ? 167 ARG   A NH1   1 
ATOM   1371 N  NH2   . ARG   A 1 170 ? -15.453 17.834 5.673  1.00 22.03 ? 167 ARG   A NH2   1 
ATOM   1372 N  N     . LEU   A 1 171 ? -18.245 8.868  6.174  1.00 16.69 ? 168 LEU   A N     1 
ATOM   1373 C  CA    . LEU   A 1 171 ? -19.086 7.764  5.647  1.00 17.48 ? 168 LEU   A CA    1 
ATOM   1374 C  C     . LEU   A 1 171 ? -19.326 6.712  6.725  1.00 19.42 ? 168 LEU   A C     1 
ATOM   1375 O  O     . LEU   A 1 171 ? -19.984 5.732  6.378  1.00 24.35 ? 168 LEU   A O     1 
ATOM   1376 C  CB    . LEU   A 1 171 ? -18.427 7.158  4.395  1.00 19.81 ? 168 LEU   A CB    1 
ATOM   1377 C  CG    . LEU   A 1 171 ? -18.258 8.113  3.218  1.00 22.19 ? 168 LEU   A CG    1 
ATOM   1378 C  CD1   . LEU   A 1 171 ? -17.384 7.452  2.179  1.00 24.21 ? 168 LEU   A CD1   1 
ATOM   1379 C  CD2   . LEU   A 1 171 ? -19.604 8.458  2.602  1.00 24.49 ? 168 LEU   A CD2   1 
ATOM   1380 N  N     . LYS   A 1 172 ? -18.928 6.958  7.983  1.00 23.21 ? 169 LYS   A N     1 
ATOM   1381 C  CA    . LYS   A 1 172 ? -19.111 6.015  9.120  1.00 24.32 ? 169 LYS   A CA    1 
ATOM   1382 C  C     . LYS   A 1 172 ? -19.910 6.651  10.283 1.00 25.26 ? 169 LYS   A C     1 
ATOM   1383 O  O     . LYS   A 1 172 ? -20.475 5.919  11.016 1.00 28.95 ? 169 LYS   A O     1 
ATOM   1384 C  CB    . LYS   A 1 172 ? -17.778 5.540  9.695  1.00 31.84 ? 169 LYS   A CB    1 
ATOM   1385 C  CG    . LYS   A 1 172 ? -17.875 4.585  10.884 1.00 36.49 ? 169 LYS   A CG    1 
ATOM   1386 C  CD    . LYS   A 1 172 ? -16.812 4.853  11.945 1.00 39.14 ? 169 LYS   A CD    1 
ATOM   1387 C  CE    . LYS   A 1 172 ? -16.909 4.004  13.202 1.00 44.14 ? 169 LYS   A CE    1 
ATOM   1388 N  NZ    . LYS   A 1 172 ? -15.722 4.149  14.073 1.00 50.28 ? 169 LYS   A NZ    1 
ATOM   1389 O  OXT   . LYS   A 1 172 ? -19.888 7.857  10.432 1.00 18.10 ? 169 LYS   A OXT   1 
HETATM 1390 P  PB    . GDP   B 2 .   ? 6.266   25.717 15.385 1.00 12.68 ? 201 GDP   A PB    1 
HETATM 1391 O  O1B   . GDP   B 2 .   ? 5.388   26.507 14.478 1.00 12.70 ? 201 GDP   A O1B   1 
HETATM 1392 O  O2B   . GDP   B 2 .   ? 5.842   24.265 15.588 1.00 11.96 ? 201 GDP   A O2B   1 
HETATM 1393 O  O3B   . GDP   B 2 .   ? 6.576   26.379 16.687 1.00 13.41 ? 201 GDP   A O3B   1 
HETATM 1394 O  O3A   . GDP   B 2 .   ? 7.685   25.576 14.650 1.00 12.58 ? 201 GDP   A O3A   1 
HETATM 1395 P  PA    . GDP   B 2 .   ? 8.261   26.377 13.397 1.00 13.82 ? 201 GDP   A PA    1 
HETATM 1396 O  O1A   . GDP   B 2 .   ? 7.552   26.029 12.161 1.00 14.52 ? 201 GDP   A O1A   1 
HETATM 1397 O  O2A   . GDP   B 2 .   ? 8.373   27.822 13.782 1.00 16.38 ? 201 GDP   A O2A   1 
HETATM 1398 O  "O5'" . GDP   B 2 .   ? 9.700   25.746 13.305 1.00 12.98 ? 201 GDP   A "O5'" 1 
HETATM 1399 C  "C5'" . GDP   B 2 .   ? 10.608  25.796 14.414 1.00 13.84 ? 201 GDP   A "C5'" 1 
HETATM 1400 C  "C4'" . GDP   B 2 .   ? 12.067  25.712 13.979 1.00 15.51 ? 201 GDP   A "C4'" 1 
HETATM 1401 O  "O4'" . GDP   B 2 .   ? 12.351  24.433 13.349 1.00 13.91 ? 201 GDP   A "O4'" 1 
HETATM 1402 C  "C3'" . GDP   B 2 .   ? 12.413  26.749 12.922 1.00 15.61 ? 201 GDP   A "C3'" 1 
HETATM 1403 O  "O3'" . GDP   B 2 .   ? 13.768  27.198 13.110 1.00 17.59 ? 201 GDP   A "O3'" 1 
HETATM 1404 C  "C2'" . GDP   B 2 .   ? 12.254  26.014 11.592 1.00 15.10 ? 201 GDP   A "C2'" 1 
HETATM 1405 O  "O2'" . GDP   B 2 .   ? 13.016  26.579 10.530 1.00 19.40 ? 201 GDP   A "O2'" 1 
HETATM 1406 C  "C1'" . GDP   B 2 .   ? 12.730  24.619 12.005 1.00 13.84 ? 201 GDP   A "C1'" 1 
HETATM 1407 N  N9    . GDP   B 2 .   ? 12.098  23.547 11.228 1.00 12.89 ? 201 GDP   A N9    1 
HETATM 1408 C  C8    . GDP   B 2 .   ? 10.781  23.361 11.040 1.00 12.06 ? 201 GDP   A C8    1 
HETATM 1409 N  N7    . GDP   B 2 .   ? 10.555  22.285 10.255 1.00 12.06 ? 201 GDP   A N7    1 
HETATM 1410 C  C5    . GDP   B 2 .   ? 11.758  21.775 9.997  1.00 10.87 ? 201 GDP   A C5    1 
HETATM 1411 C  C6    . GDP   B 2 .   ? 12.235  20.647 9.213  1.00 11.39 ? 201 GDP   A C6    1 
HETATM 1412 O  O6    . GDP   B 2 .   ? 11.463  19.854 8.630  1.00 12.08 ? 201 GDP   A O6    1 
HETATM 1413 N  N1    . GDP   B 2 .   ? 13.554  20.471 9.192  1.00 11.75 ? 201 GDP   A N1    1 
HETATM 1414 C  C2    . GDP   B 2 .   ? 14.454  21.302 9.795  1.00 13.17 ? 201 GDP   A C2    1 
HETATM 1415 N  N2    . GDP   B 2 .   ? 15.744  21.003 9.688  1.00 15.34 ? 201 GDP   A N2    1 
HETATM 1416 N  N3    . GDP   B 2 .   ? 14.079  22.345 10.527 1.00 12.59 ? 201 GDP   A N3    1 
HETATM 1417 C  C4    . GDP   B 2 .   ? 12.765  22.609 10.627 1.00 11.79 ? 201 GDP   A C4    1 
HETATM 1418 MG MG    . MG    C 3 .   ? 4.353   28.360 14.663 1.00 12.36 2 202 MG    A MG    1 
HETATM 1419 C  C1    . EDO   D 4 .   ? -0.327  7.134  5.157  1.00 30.34 ? 203 EDO   A C1    1 
HETATM 1420 O  O1    . EDO   D 4 .   ? -0.507  5.867  5.667  1.00 29.19 ? 203 EDO   A O1    1 
HETATM 1421 C  C2    . EDO   D 4 .   ? 0.408   7.054  3.832  1.00 29.57 ? 203 EDO   A C2    1 
HETATM 1422 O  O2    . EDO   D 4 .   ? 1.634   6.371  3.937  1.00 27.36 ? 203 EDO   A O2    1 
HETATM 1423 C  C1    . EDO   E 4 .   ? -4.443  11.475 -6.121 1.00 22.15 ? 204 EDO   A C1    1 
HETATM 1424 O  O1    . EDO   E 4 .   ? -5.151  12.577 -5.544 1.00 19.50 ? 204 EDO   A O1    1 
HETATM 1425 C  C2    . EDO   E 4 .   ? -5.360  10.403 -6.550 1.00 20.47 ? 204 EDO   A C2    1 
HETATM 1426 O  O2    . EDO   E 4 .   ? -6.254  11.076 -7.394 1.00 23.11 ? 204 EDO   A O2    1 
HETATM 1427 C  CBF   . A1IK9 F 5 .   ? -6.366  36.211 13.367 1.00 29.68 ? 205 A1IK9 A CBF   1 
HETATM 1428 C  CBG   . A1IK9 F 5 .   ? -5.853  37.640 13.347 1.00 28.81 ? 205 A1IK9 A CBG   1 
HETATM 1429 N  NBH   . A1IK9 F 5 .   ? -4.673  37.796 14.185 1.00 30.03 ? 205 A1IK9 A NBH   1 
HETATM 1430 C  CBI   . A1IK9 F 5 .   ? -4.842  37.295 15.563 1.00 26.91 ? 205 A1IK9 A CBI   1 
HETATM 1431 C  CBJ   . A1IK9 F 5 .   ? -5.412  35.882 15.554 1.00 25.61 ? 205 A1IK9 A CBJ   1 
HETATM 1432 C  CBE   . A1IK9 F 5 .   ? -6.706  35.800 14.787 1.00 25.99 ? 205 A1IK9 A CBE   1 
HETATM 1433 N  NAC   . A1IK9 F 5 .   ? -7.233  34.423 14.925 1.00 24.97 ? 205 A1IK9 A NAC   1 
HETATM 1434 C  CAD   . A1IK9 F 5 .   ? -6.568  33.402 14.091 1.00 26.63 ? 205 A1IK9 A CAD   1 
HETATM 1435 C  CAE   . A1IK9 F 5 .   ? -7.485  32.727 13.100 1.00 29.69 ? 205 A1IK9 A CAE   1 
HETATM 1436 O  OAF   . A1IK9 F 5 .   ? -7.806  33.638 12.077 1.00 38.58 ? 205 A1IK9 A OAF   1 
HETATM 1437 C  CAB   . A1IK9 F 5 .   ? -8.169  34.157 15.802 1.00 24.89 ? 205 A1IK9 A CAB   1 
HETATM 1438 O  OAA   . A1IK9 F 5 .   ? -8.644  35.013 16.520 1.00 30.08 ? 205 A1IK9 A OAA   1 
HETATM 1439 C  CAY   . A1IK9 F 5 .   ? -8.606  32.836 16.002 1.00 22.96 ? 205 A1IK9 A CAY   1 
HETATM 1440 C  CAZ   . A1IK9 F 5 .   ? -9.890  32.433 15.698 1.00 22.85 ? 205 A1IK9 A CAZ   1 
HETATM 1441 C  CAX   . A1IK9 F 5 .   ? -7.753  31.918 16.574 1.00 21.65 ? 205 A1IK9 A CAX   1 
HETATM 1442 O  OAW   . A1IK9 F 5 .   ? -6.537  32.328 16.906 1.00 23.76 ? 205 A1IK9 A OAW   1 
HETATM 1443 C  CBC   . A1IK9 F 5 .   ? -8.142  30.622 16.835 1.00 21.97 ? 205 A1IK9 A CBC   1 
HETATM 1444 C  CBB   . A1IK9 F 5 .   ? -9.430  30.241 16.508 1.00 22.98 ? 205 A1IK9 A CBB   1 
HETATM 1445 C  CBA   . A1IK9 F 5 .   ? -10.312 31.135 15.933 1.00 22.16 ? 205 A1IK9 A CBA   1 
HETATM 1446 S  SAH   . A1IK9 F 5 .   ? -11.924 30.646 15.483 1.00 22.17 ? 205 A1IK9 A SAH   1 
HETATM 1447 O  OAG   . A1IK9 F 5 .   ? -12.279 29.546 16.220 1.00 22.69 ? 205 A1IK9 A OAG   1 
HETATM 1448 O  OBD   . A1IK9 F 5 .   ? -12.822 31.777 15.904 1.00 27.51 ? 205 A1IK9 A OBD   1 
HETATM 1449 N  NAI   . A1IK9 F 5 .   ? -11.972 30.473 13.921 1.00 22.07 ? 205 A1IK9 A NAI   1 
HETATM 1450 C  CAJ   . A1IK9 F 5 .   ? -11.487 29.393 13.313 1.00 20.69 ? 205 A1IK9 A CAJ   1 
HETATM 1451 S  SAK   . A1IK9 F 5 .   ? -11.366 27.881 13.993 1.00 19.20 ? 205 A1IK9 A SAK   1 
HETATM 1452 C  CAL   . A1IK9 F 5 .   ? -10.729 27.214 12.539 1.00 17.66 ? 205 A1IK9 A CAL   1 
HETATM 1453 C  CAM   . A1IK9 F 5 .   ? -10.344 25.937 12.275 1.00 16.88 ? 205 A1IK9 A CAM   1 
HETATM 1454 CL CLAR  . A1IK9 F 5 .   ? -10.544 24.796 13.451 1.00 16.67 ? 205 A1IK9 A CLAR  1 
HETATM 1455 C  CAN   . A1IK9 F 5 .   ? -9.838  25.657 11.019 1.00 16.24 ? 205 A1IK9 A CAN   1 
HETATM 1456 C  CAO   . A1IK9 F 5 .   ? -9.703  26.610 10.064 1.00 18.39 ? 205 A1IK9 A CAO   1 
HETATM 1457 C  CAP   . A1IK9 F 5 .   ? -10.154 27.873 10.394 1.00 19.59 ? 205 A1IK9 A CAP   1 
HETATM 1458 O  OAQ   . A1IK9 F 5 .   ? -10.033 28.775 9.469  1.00 22.89 ? 205 A1IK9 A OAQ   1 
HETATM 1459 C  CAS   . A1IK9 F 5 .   ? -10.641 28.188 11.611 1.00 20.05 ? 205 A1IK9 A CAS   1 
HETATM 1460 N  NAV   . A1IK9 F 5 .   ? -11.088 29.418 12.068 1.00 22.95 ? 205 A1IK9 A NAV   1 
HETATM 1461 C  CAU   . A1IK9 F 5 .   ? -11.156 30.636 11.330 1.00 24.52 ? 205 A1IK9 A CAU   1 
HETATM 1462 C  CAT   . A1IK9 F 5 .   ? -9.930  31.399 11.475 1.00 28.52 ? 205 A1IK9 A CAT   1 
HETATM 1463 O  O     . HOH   G 6 .   ? -16.109 13.867 -0.294 1.00 32.24 ? 301 HOH   A O     1 
HETATM 1464 O  O     . HOH   G 6 .   ? 10.183  8.609  25.782 1.00 32.34 ? 302 HOH   A O     1 
HETATM 1465 O  O     . HOH   G 6 .   ? -8.431  7.151  13.074 1.00 21.27 ? 303 HOH   A O     1 
HETATM 1466 O  O     . HOH   G 6 .   ? 23.442  15.878 13.966 1.00 15.42 ? 304 HOH   A O     1 
HETATM 1467 O  O     . HOH   G 6 .   ? -3.710  27.964 20.321 1.00 18.11 ? 305 HOH   A O     1 
HETATM 1468 O  O     . HOH   G 6 .   ? 1.045   32.669 10.050 1.00 23.45 ? 306 HOH   A O     1 
HETATM 1469 O  O     . HOH   G 6 .   ? 6.287   29.241 14.441 1.00 15.42 ? 307 HOH   A O     1 
HETATM 1470 O  O     . HOH   G 6 .   ? 3.053   -2.344 17.048 1.00 33.68 ? 308 HOH   A O     1 
HETATM 1471 O  O     . HOH   G 6 .   ? -17.997 19.699 6.873  1.00 27.33 ? 309 HOH   A O     1 
HETATM 1472 O  O     . HOH   G 6 .   ? -7.611  5.075  6.549  1.00 32.52 ? 310 HOH   A O     1 
HETATM 1473 O  O     . HOH   G 6 .   ? 2.424   27.543 14.678 1.00 14.14 ? 311 HOH   A O     1 
HETATM 1474 O  O     . HOH   G 6 .   ? 4.744   15.140 27.586 1.00 35.75 ? 312 HOH   A O     1 
HETATM 1475 O  O     . HOH   G 6 .   ? -8.452  6.160  15.486 1.00 27.81 ? 313 HOH   A O     1 
HETATM 1476 O  O     . HOH   G 6 .   ? 8.577   11.529 30.541 1.00 31.83 ? 314 HOH   A O     1 
HETATM 1477 O  O     . HOH   G 6 .   ? -9.228  24.386 -8.070 1.00 40.49 ? 315 HOH   A O     1 
HETATM 1478 O  O     . HOH   G 6 .   ? -6.980  13.527 -8.128 1.00 17.06 ? 316 HOH   A O     1 
HETATM 1479 O  O     . HOH   G 6 .   ? -8.505  8.784  16.009 1.00 24.38 ? 317 HOH   A O     1 
HETATM 1480 O  O     . HOH   G 6 .   ? -7.350  9.138  11.537 1.00 11.85 ? 318 HOH   A O     1 
HETATM 1481 O  O     . HOH   G 6 .   ? -6.883  6.629  3.078  1.00 26.18 ? 319 HOH   A O     1 
HETATM 1482 O  O     . HOH   G 6 .   ? -1.073  3.132  11.798 1.00 21.66 ? 320 HOH   A O     1 
HETATM 1483 O  O     . HOH   G 6 .   ? -16.446 14.521 2.197  1.00 30.63 ? 321 HOH   A O     1 
HETATM 1484 O  O     . HOH   G 6 .   ? 10.212  29.391 15.062 1.00 35.62 ? 322 HOH   A O     1 
HETATM 1485 O  O     . HOH   G 6 .   ? -5.729  8.428  4.982  1.00 21.31 ? 323 HOH   A O     1 
HETATM 1486 O  O     . HOH   G 6 .   ? -7.348  5.317  10.146 1.00 40.49 ? 324 HOH   A O     1 
HETATM 1487 O  O     . HOH   G 6 .   ? -5.482  34.108 10.088 1.00 30.59 ? 325 HOH   A O     1 
HETATM 1488 O  O     . HOH   G 6 .   ? 2.838   10.544 23.178 1.00 21.82 ? 326 HOH   A O     1 
HETATM 1489 O  O     . HOH   G 6 .   ? 7.325   20.258 24.895 1.00 36.24 ? 327 HOH   A O     1 
HETATM 1490 O  O     . HOH   G 6 .   ? 7.953   26.854 5.774  1.00 19.06 ? 328 HOH   A O     1 
HETATM 1491 O  O     . HOH   G 6 .   ? 17.359  15.998 21.111 1.00 31.86 ? 329 HOH   A O     1 
HETATM 1492 O  O     . HOH   G 6 .   ? -5.809  7.558  22.493 1.00 37.14 ? 330 HOH   A O     1 
HETATM 1493 O  O     . HOH   G 6 .   ? -2.828  8.885  2.040  1.00 19.39 ? 331 HOH   A O     1 
HETATM 1494 O  O     . HOH   G 6 .   ? 19.247  15.201 18.152 1.00 18.32 ? 332 HOH   A O     1 
HETATM 1495 O  O     . HOH   G 6 .   ? -17.568 20.400 14.504 1.00 24.10 ? 333 HOH   A O     1 
HETATM 1496 O  O     . HOH   G 6 .   ? 0.436   30.903 12.001 1.00 19.05 ? 334 HOH   A O     1 
HETATM 1497 O  O     . HOH   G 6 .   ? 5.759   -1.089 12.493 1.00 22.20 ? 335 HOH   A O     1 
HETATM 1498 O  O     . HOH   G 6 .   ? -16.098 21.687 24.373 1.00 50.26 ? 336 HOH   A O     1 
HETATM 1499 O  O     . HOH   G 6 .   ? 10.027  28.850 11.432 1.00 29.30 ? 337 HOH   A O     1 
HETATM 1500 O  O     . HOH   G 6 .   ? 21.422  21.829 6.339  1.00 28.86 ? 338 HOH   A O     1 
HETATM 1501 O  O     . HOH   G 6 .   ? -4.714  29.056 22.805 1.00 29.74 ? 339 HOH   A O     1 
HETATM 1502 O  O     . HOH   G 6 .   ? 4.477   28.144 16.714 1.00 16.32 ? 340 HOH   A O     1 
HETATM 1503 O  O     . HOH   G 6 .   ? 13.404  19.823 17.015 1.00 14.40 ? 341 HOH   A O     1 
HETATM 1504 O  O     . HOH   G 6 .   ? 1.500   2.349  12.281 1.00 19.00 ? 342 HOH   A O     1 
HETATM 1505 O  O     . HOH   G 6 .   ? -0.445  34.399 3.972  1.00 39.75 ? 343 HOH   A O     1 
HETATM 1506 O  O     . HOH   G 6 .   ? -21.514 10.513 23.901 1.00 36.99 ? 344 HOH   A O     1 
HETATM 1507 O  O     . HOH   G 6 .   ? 8.846   27.835 17.209 1.00 21.23 ? 345 HOH   A O     1 
HETATM 1508 O  O     . HOH   G 6 .   ? -14.465 27.692 24.260 1.00 31.80 ? 346 HOH   A O     1 
HETATM 1509 O  O     . HOH   G 6 .   ? 3.644   30.343 14.940 1.00 16.45 ? 347 HOH   A O     1 
HETATM 1510 O  O     . HOH   G 6 .   ? -10.313 22.018 -9.290 1.00 22.49 ? 348 HOH   A O     1 
HETATM 1511 O  O     . HOH   G 6 .   ? -8.264  7.468  -5.189 1.00 11.99 ? 349 HOH   A O     1 
HETATM 1512 O  O     . HOH   G 6 .   ? 14.179  13.915 4.850  1.00 19.25 ? 350 HOH   A O     1 
HETATM 1513 O  O     . HOH   G 6 .   ? 3.766   26.441 19.276 1.00 20.63 ? 351 HOH   A O     1 
HETATM 1514 O  O     . HOH   G 6 .   ? -17.417 8.782  12.378 1.00 18.69 ? 352 HOH   A O     1 
HETATM 1515 O  O     . HOH   G 6 .   ? 3.575   6.523  5.886  1.00 13.38 ? 353 HOH   A O     1 
HETATM 1516 O  O     . HOH   G 6 .   ? -4.356  0.255  14.187 1.00 22.79 ? 354 HOH   A O     1 
HETATM 1517 O  O     . HOH   G 6 .   ? -0.983  32.475 1.716  1.00 41.77 ? 355 HOH   A O     1 
HETATM 1518 O  O     . HOH   G 6 .   ? -14.903 28.414 15.372 1.00 29.80 ? 356 HOH   A O     1 
HETATM 1519 O  O     . HOH   G 6 .   ? -3.150  25.818 30.410 1.00 30.35 ? 357 HOH   A O     1 
HETATM 1520 O  O     . HOH   G 6 .   ? -21.433 10.688 9.011  1.00 13.98 ? 358 HOH   A O     1 
HETATM 1521 O  O     . HOH   G 6 .   ? 12.686  6.275  20.074 1.00 42.38 ? 359 HOH   A O     1 
HETATM 1522 O  O     . HOH   G 6 .   ? -16.890 21.892 12.145 1.00 28.81 ? 360 HOH   A O     1 
HETATM 1523 O  O     . HOH   G 6 .   ? 13.875  14.953 2.257  1.00 17.40 ? 361 HOH   A O     1 
HETATM 1524 O  O     . HOH   G 6 .   ? 9.515   19.950 23.159 1.00 28.88 ? 362 HOH   A O     1 
HETATM 1525 O  O     . HOH   G 6 .   ? 3.762   13.099 29.057 1.00 40.41 ? 363 HOH   A O     1 
HETATM 1526 O  O     . HOH   G 6 .   ? -14.436 20.462 -9.222 1.00 23.90 ? 364 HOH   A O     1 
HETATM 1527 O  O     . HOH   G 6 .   ? -22.274 5.498  4.826  1.00 20.49 ? 365 HOH   A O     1 
HETATM 1528 O  O     . HOH   G 6 .   ? 1.268   8.630  0.336  1.00 25.84 ? 366 HOH   A O     1 
HETATM 1529 O  O     . HOH   G 6 .   ? 3.056   -2.816 20.815 1.00 36.25 ? 367 HOH   A O     1 
HETATM 1530 O  O     . HOH   G 6 .   ? -15.829 14.395 26.804 1.00 33.79 ? 368 HOH   A O     1 
HETATM 1531 O  O     . HOH   G 6 .   ? 4.555   30.940 -3.437 1.00 40.09 ? 369 HOH   A O     1 
HETATM 1532 O  O     . HOH   G 6 .   ? 11.162  31.759 3.411  1.00 31.32 ? 370 HOH   A O     1 
HETATM 1533 O  O     . HOH   G 6 .   ? 2.119   0.812  22.413 1.00 47.92 ? 371 HOH   A O     1 
HETATM 1534 O  O     . HOH   G 6 .   ? -4.751  31.121 20.721 1.00 33.16 ? 372 HOH   A O     1 
HETATM 1535 O  O     . HOH   G 6 .   ? 5.173   17.543 -0.470 1.00 15.65 ? 373 HOH   A O     1 
HETATM 1536 O  O     . HOH   G 6 .   ? -4.166  9.603  23.734 1.00 35.86 ? 374 HOH   A O     1 
HETATM 1537 O  O     . HOH   G 6 .   ? 4.403   17.586 19.755 1.00 11.64 ? 375 HOH   A O     1 
HETATM 1538 O  O     . HOH   G 6 .   ? -21.719 14.348 22.430 1.00 23.65 ? 376 HOH   A O     1 
HETATM 1539 O  O     . HOH   G 6 .   ? -3.570  14.157 28.921 1.00 41.91 ? 377 HOH   A O     1 
HETATM 1540 O  O     . HOH   G 6 .   ? 6.452   37.978 19.320 1.00 34.72 ? 378 HOH   A O     1 
HETATM 1541 O  O     . HOH   G 6 .   ? -16.870 17.883 -4.203 1.00 37.68 ? 379 HOH   A O     1 
HETATM 1542 O  O     . HOH   G 6 .   ? 8.032   35.517 12.054 1.00 25.67 ? 380 HOH   A O     1 
HETATM 1543 O  O     . HOH   G 6 .   ? 12.593  8.258  21.912 1.00 38.22 ? 381 HOH   A O     1 
HETATM 1544 O  O     . HOH   G 6 .   ? 7.231   14.486 -1.048 1.00 17.39 ? 382 HOH   A O     1 
HETATM 1545 O  O     . HOH   G 6 .   ? -21.381 11.706 4.752  1.00 18.91 ? 383 HOH   A O     1 
HETATM 1546 O  O     . HOH   G 6 .   ? 17.453  10.833 10.990 1.00 13.41 ? 384 HOH   A O     1 
HETATM 1547 O  O     . HOH   G 6 .   ? 15.746  25.428 14.131 1.00 32.67 ? 385 HOH   A O     1 
HETATM 1548 O  O     . HOH   G 6 .   ? -15.115 15.984 -8.585 1.00 14.87 ? 386 HOH   A O     1 
HETATM 1549 O  O     . HOH   G 6 .   ? 10.899  20.334 18.461 1.00 33.16 ? 387 HOH   A O     1 
HETATM 1550 O  O     . HOH   G 6 .   ? 16.067  8.246  22.289 1.00 30.24 ? 388 HOH   A O     1 
HETATM 1551 O  O     . HOH   G 6 .   ? 8.872   23.285 22.987 1.00 37.27 ? 389 HOH   A O     1 
HETATM 1552 O  O     . HOH   G 6 .   ? 6.357   39.331 15.215 1.00 25.64 ? 390 HOH   A O     1 
HETATM 1553 O  O     . HOH   G 6 .   ? -3.895  29.572 -1.364 1.00 34.00 ? 391 HOH   A O     1 
HETATM 1554 O  O     . HOH   G 6 .   ? -15.003 18.059 -6.731 1.00 18.77 ? 392 HOH   A O     1 
HETATM 1555 O  O     . HOH   G 6 .   ? -5.851  34.372 18.812 1.00 40.04 ? 393 HOH   A O     1 
HETATM 1556 O  O     . HOH   G 6 .   ? -9.860  25.352 28.437 1.00 46.03 ? 394 HOH   A O     1 
HETATM 1557 O  O     . HOH   G 6 .   ? -4.208  20.175 -6.537 1.00 30.68 ? 395 HOH   A O     1 
HETATM 1558 O  O     . HOH   G 6 .   ? -2.257  36.307 13.535 1.00 30.36 ? 396 HOH   A O     1 
HETATM 1559 O  O     . HOH   G 6 .   ? 3.523   29.859 21.173 1.00 30.59 ? 397 HOH   A O     1 
HETATM 1560 O  O     . HOH   G 6 .   ? 19.114  17.426 16.509 1.00 27.96 ? 398 HOH   A O     1 
HETATM 1561 O  O     . HOH   G 6 .   ? 11.912  24.390 0.215  1.00 56.56 ? 399 HOH   A O     1 
HETATM 1562 O  O     . HOH   G 6 .   ? 12.436  28.231 0.875  1.00 46.13 ? 400 HOH   A O     1 
HETATM 1563 O  O     . HOH   G 6 .   ? -18.104 21.045 2.323  1.00 31.44 ? 401 HOH   A O     1 
HETATM 1564 O  O     . HOH   G 6 .   ? 9.790   9.000  14.415 1.00 17.32 ? 402 HOH   A O     1 
HETATM 1565 O  O     . HOH   G 6 .   ? 4.013   36.612 9.093  1.00 40.59 ? 403 HOH   A O     1 
HETATM 1566 O  O     . HOH   G 6 .   ? 15.111  22.615 13.621 1.00 23.39 ? 404 HOH   A O     1 
HETATM 1567 O  O     . HOH   G 6 .   ? 0.142   -0.846 18.625 1.00 32.91 ? 405 HOH   A O     1 
HETATM 1568 O  O     . HOH   G 6 .   ? 0.711   5.027  8.258  1.00 16.21 ? 406 HOH   A O     1 
HETATM 1569 O  O     . HOH   G 6 .   ? -10.134 6.474  8.397  1.00 41.33 ? 407 HOH   A O     1 
HETATM 1570 O  O     . HOH   G 6 .   ? 4.839   11.979 -1.001 1.00 25.67 ? 408 HOH   A O     1 
HETATM 1571 O  O     . HOH   G 6 .   ? -17.141 11.856 2.501  1.00 19.37 ? 409 HOH   A O     1 
HETATM 1572 O  O     . HOH   G 6 .   ? -16.931 19.256 18.146 1.00 56.87 ? 410 HOH   A O     1 
HETATM 1573 O  O     . HOH   G 6 .   ? 14.282  5.091  13.068 1.00 22.43 ? 411 HOH   A O     1 
HETATM 1574 O  O     . HOH   G 6 .   ? -1.457  35.505 16.152 1.00 23.42 ? 412 HOH   A O     1 
HETATM 1575 O  O     . HOH   G 6 .   ? 4.764   23.729 23.580 1.00 29.10 ? 413 HOH   A O     1 
HETATM 1576 O  O     . HOH   G 6 .   ? 16.620  21.008 15.499 1.00 22.09 ? 414 HOH   A O     1 
HETATM 1577 O  O     . HOH   G 6 .   ? -1.857  31.259 20.847 1.00 23.43 ? 415 HOH   A O     1 
HETATM 1578 O  O     . HOH   G 6 .   ? -19.560 17.089 -8.987 1.00 27.62 ? 416 HOH   A O     1 
HETATM 1579 O  O     . HOH   G 6 .   ? 10.073  7.614  23.146 1.00 38.23 ? 417 HOH   A O     1 
HETATM 1580 O  O     . HOH   G 6 .   ? 13.209  23.811 17.249 1.00 32.82 ? 418 HOH   A O     1 
HETATM 1581 O  O     . HOH   G 6 .   ? -19.306 17.859 -0.027 1.00 31.92 ? 419 HOH   A O     1 
HETATM 1582 O  O     . HOH   G 6 .   ? -1.423  8.049  -2.511 1.00 21.77 ? 420 HOH   A O     1 
HETATM 1583 O  O     . HOH   G 6 .   ? 13.421  15.844 24.434 1.00 24.70 ? 421 HOH   A O     1 
HETATM 1584 O  O     . HOH   G 6 .   ? 7.778   11.351 -0.968 1.00 11.80 ? 422 HOH   A O     1 
HETATM 1585 O  O     . HOH   G 6 .   ? 4.076   14.864 -0.655 1.00 14.17 ? 423 HOH   A O     1 
HETATM 1586 O  O     . HOH   G 6 .   ? 10.077  34.927 10.363 1.00 37.06 ? 424 HOH   A O     1 
HETATM 1587 O  O     . HOH   G 6 .   ? -17.843 19.024 3.985  1.00 36.49 ? 425 HOH   A O     1 
HETATM 1588 O  O     . HOH   G 6 .   ? 16.448  4.477  14.838 1.00 44.70 ? 426 HOH   A O     1 
HETATM 1589 O  O     . HOH   G 6 .   ? -4.747  4.161  10.101 1.00 33.24 ? 427 HOH   A O     1 
HETATM 1590 O  O     . HOH   G 6 .   ? 3.150   2.002  10.256 1.00 23.72 ? 428 HOH   A O     1 
HETATM 1591 O  O     . HOH   G 6 .   ? -2.909  28.539 30.631 1.00 31.51 ? 429 HOH   A O     1 
HETATM 1592 O  O     . HOH   G 6 .   ? 1.780   31.662 22.532 1.00 42.51 ? 430 HOH   A O     1 
HETATM 1593 O  O     . HOH   G 6 .   ? 4.720   27.393 21.635 1.00 45.20 ? 431 HOH   A O     1 
HETATM 1594 O  O     . HOH   G 6 .   ? -2.022  5.558  -1.486 1.00 28.93 ? 432 HOH   A O     1 
HETATM 1595 O  O     . HOH   G 6 .   ? 12.329  26.323 17.681 1.00 42.73 ? 433 HOH   A O     1 
HETATM 1596 O  O     . HOH   G 6 .   ? -3.137  1.101  12.051 1.00 31.41 ? 434 HOH   A O     1 
HETATM 1597 O  O     . HOH   G 6 .   ? 6.200   37.007 10.654 1.00 30.43 ? 435 HOH   A O     1 
HETATM 1598 O  O     . HOH   G 6 .   ? -3.267  35.016 18.378 1.00 31.10 ? 436 HOH   A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . SER   A 3   ? 0.4376 0.5414 0.5323 0.0469  -0.2364 0.1337  0   SER   A N     
2    C  CA    . SER   A 3   ? 0.4040 0.5001 0.3989 0.0558  -0.1235 0.0634  0   SER   A CA    
3    C  C     . SER   A 3   ? 0.3718 0.4960 0.3603 0.0787  -0.0800 0.0318  0   SER   A C     
4    O  O     . SER   A 3   ? 0.4191 0.5492 0.3000 0.0542  -0.1061 0.0068  0   SER   A O     
5    C  CB    . SER   A 3   ? 0.4128 0.4593 0.4795 0.0563  -0.0694 0.0409  0   SER   A CB    
6    O  OG    . SER   A 3   ? 0.3973 0.4309 0.6489 0.0352  -0.0423 0.0426  0   SER   A OG    
7    N  N     . MET   A 4   ? 0.3050 0.4776 0.3544 0.0712  -0.0886 0.0346  1   MET   A N     
8    C  CA    . MET   A 4   ? 0.3359 0.3745 0.3041 0.0822  -0.0868 0.0867  1   MET   A CA    
9    C  C     . MET   A 4   ? 0.2378 0.3372 0.3018 0.0886  -0.0417 0.0075  1   MET   A C     
10   O  O     . MET   A 4   ? 0.2794 0.3919 0.3349 0.0441  0.0638  0.0111  1   MET   A O     
11   C  CB    . MET   A 4   ? 0.5110 0.3913 0.3353 -0.0250 -0.0319 0.0820  1   MET   A CB    
12   C  CG    . MET   A 4   ? 0.5287 0.4182 0.2220 -0.0883 0.0366  0.0979  1   MET   A CG    
13   S  SD    . MET   A 4   ? 0.3371 0.2982 0.2942 -0.0004 0.0054  -0.0063 1   MET   A SD    
14   C  CE    . MET   A 4   ? 0.4347 0.3110 0.2573 -0.0203 0.0341  0.0539  1   MET   A CE    
15   N  N     . THR   A 5   ? 0.2744 0.2405 0.2352 0.0426  -0.0542 0.0214  2   THR   A N     
16   C  CA    . THR   A 5   ? 0.2703 0.2451 0.2278 -0.0025 -0.0732 0.0422  2   THR   A CA    
17   C  C     . THR   A 5   ? 0.2443 0.2356 0.1971 0.0142  -0.0271 0.0181  2   THR   A C     
18   O  O     . THR   A 5   ? 0.2921 0.2719 0.1673 -0.0536 -0.0016 -0.0324 2   THR   A O     
19   C  CB    . THR   A 5   ? 0.2397 0.2368 0.2136 -0.0041 -0.0646 -0.0086 2   THR   A CB    
20   O  OG1   . THR   A 5   ? 0.2411 0.2693 0.2250 -0.0256 -0.0656 0.0158  2   THR   A OG1   
21   C  CG2   . THR   A 5   ? 0.2251 0.2552 0.2310 0.0446  -0.0331 0.0207  2   THR   A CG2   
22   N  N     . GLU   A 6   ? 0.1431 0.2212 0.1913 0.0265  -0.0345 0.0194  3   GLU   A N     
23   C  CA    . GLU   A 6   ? 0.2007 0.2223 0.1591 0.0432  -0.0419 0.0084  3   GLU   A CA    
24   C  C     . GLU   A 6   ? 0.1361 0.2075 0.1563 0.0150  -0.0313 0.0220  3   GLU   A C     
25   O  O     . GLU   A 6   ? 0.1635 0.2477 0.2189 -0.0086 -0.0463 0.0449  3   GLU   A O     
26   C  CB    . GLU   A 6   ? 0.2687 0.2664 0.2154 0.1029  -0.0336 0.0161  3   GLU   A CB    
27   C  CG    . GLU   A 6   ? 0.3317 0.3003 0.3684 0.0447  -0.0460 -0.0077 3   GLU   A CG    
28   C  CD    . GLU   A 6   ? 0.4601 0.3825 0.4791 0.0904  -0.0328 -0.1024 3   GLU   A CD    
29   O  OE1   . GLU   A 6   ? 0.6292 0.4720 0.5567 -0.0584 -0.0056 -0.1318 3   GLU   A OE1   
30   O  OE2   . GLU   A 6   ? 0.5393 0.4499 0.5802 0.2162  -0.0912 -0.0481 3   GLU   A OE2   
31   N  N     . TYR   A 7   ? 0.1426 0.1594 0.1349 0.0447  -0.0393 -0.0157 4   TYR   A N     
32   C  CA    . TYR   A 7   ? 0.1497 0.1353 0.1363 0.0256  -0.0329 -0.0063 4   TYR   A CA    
33   C  C     . TYR   A 7   ? 0.1586 0.1670 0.1397 0.0215  -0.0201 -0.0273 4   TYR   A C     
34   O  O     . TYR   A 7   ? 0.2016 0.1557 0.1270 -0.0038 -0.0203 -0.0180 4   TYR   A O     
35   C  CB    . TYR   A 7   ? 0.1469 0.1304 0.1293 0.0287  -0.0445 -0.0145 4   TYR   A CB    
36   C  CG    . TYR   A 7   ? 0.1186 0.1546 0.1196 0.0165  -0.0331 -0.0199 4   TYR   A CG    
37   C  CD1   . TYR   A 7   ? 0.1542 0.1605 0.1217 0.0111  -0.0359 -0.0103 4   TYR   A CD1   
38   C  CD2   . TYR   A 7   ? 0.1784 0.1572 0.1327 0.0187  -0.0326 -0.0097 4   TYR   A CD2   
39   C  CE1   . TYR   A 7   ? 0.1569 0.1650 0.0854 0.0129  -0.0309 -0.0051 4   TYR   A CE1   
40   C  CE2   . TYR   A 7   ? 0.1815 0.1604 0.1203 0.0143  -0.0253 -0.0152 4   TYR   A CE2   
41   C  CZ    . TYR   A 7   ? 0.1436 0.1717 0.1270 -0.0107 -0.0376 -0.0079 4   TYR   A CZ    
42   O  OH    . TYR   A 7   ? 0.1958 0.1779 0.1433 -0.0085 -0.0239 -0.0344 4   TYR   A OH    
43   N  N     . LYS   A 8   ? 0.1343 0.1387 0.1354 0.0224  -0.0304 -0.0351 5   LYS   A N     
44   C  CA    . LYS   A 8   ? 0.1518 0.1532 0.1384 0.0295  -0.0405 -0.0365 5   LYS   A CA    
45   C  C     . LYS   A 8   ? 0.1288 0.1277 0.1259 0.0159  -0.0241 -0.0352 5   LYS   A C     
46   O  O     . LYS   A 8   ? 0.1250 0.1486 0.1524 0.0051  -0.0159 -0.0178 5   LYS   A O     
47   C  CB    . LYS   A 8   ? 0.1655 0.1844 0.1518 0.0368  -0.0375 -0.0423 5   LYS   A CB    
48   C  CG    . LYS   A 8   ? 0.2263 0.2354 0.2138 0.0868  -0.0527 -0.0393 5   LYS   A CG    
49   C  CD    . LYS   A 8   ? 0.2703 0.3574 0.2486 0.0931  0.0021  -0.0320 5   LYS   A CD    
50   C  CE    . LYS   A 8   ? 0.2946 0.4247 0.3340 0.1397  -0.0145 -0.0565 5   LYS   A CE    
51   N  NZ    . LYS   A 8   ? 0.4195 0.5393 0.5312 0.0288  -0.0174 -0.0648 5   LYS   A NZ    
52   N  N     . LEU   A 9   ? 0.1349 0.1263 0.0996 0.0126  -0.0285 -0.0318 6   LEU   A N     
53   C  CA    . LEU   A 9   ? 0.1422 0.1245 0.1077 0.0115  -0.0361 -0.0201 6   LEU   A CA    
54   C  C     . LEU   A 9   ? 0.1558 0.1325 0.1152 0.0166  -0.0415 -0.0272 6   LEU   A C     
55   O  O     . LEU   A 9   ? 0.1997 0.1310 0.1508 0.0071  -0.0741 -0.0195 6   LEU   A O     
56   C  CB    . LEU   A 9   ? 0.1402 0.1283 0.1123 0.0209  -0.0382 -0.0280 6   LEU   A CB    
57   C  CG    . LEU   A 9   ? 0.1723 0.1405 0.1247 0.0270  -0.0408 -0.0461 6   LEU   A CG    
58   C  CD1   . LEU   A 9   ? 0.1662 0.1501 0.1491 0.0013  -0.0313 -0.0595 6   LEU   A CD1   
59   C  CD2   . LEU   A 9   ? 0.1451 0.1513 0.1545 0.0156  -0.0348 -0.0608 6   LEU   A CD2   
60   N  N     . VAL   A 10  ? 0.1271 0.1215 0.1176 0.0102  -0.0378 -0.0243 7   VAL   A N     
61   C  CA    . VAL   A 10  ? 0.1370 0.1447 0.1131 0.0169  -0.0361 -0.0335 7   VAL   A CA    
62   C  C     . VAL   A 10  ? 0.1355 0.1186 0.1025 0.0058  -0.0302 -0.0300 7   VAL   A C     
63   O  O     . VAL   A 10  ? 0.1246 0.1139 0.1505 0.0033  -0.0296 -0.0184 7   VAL   A O     
64   C  CB    . VAL   A 10  ? 0.1286 0.1554 0.1231 0.0212  -0.0361 -0.0371 7   VAL   A CB    
65   C  CG1   . VAL   A 10  ? 0.1365 0.1745 0.1297 0.0168  -0.0223 -0.0579 7   VAL   A CG1   
66   C  CG2   . VAL   A 10  ? 0.1139 0.1973 0.1533 0.0147  -0.0124 -0.0294 7   VAL   A CG2   
67   N  N     . VAL   A 11  ? 0.1316 0.1035 0.1124 0.0124  -0.0263 -0.0308 8   VAL   A N     
68   C  CA    . VAL   A 11  ? 0.1281 0.0970 0.1122 0.0029  -0.0259 -0.0373 8   VAL   A CA    
69   C  C     . VAL   A 11  ? 0.1272 0.1240 0.1060 0.0200  -0.0148 -0.0322 8   VAL   A C     
70   O  O     . VAL   A 11  ? 0.1507 0.1247 0.0958 0.0062  -0.0307 -0.0349 8   VAL   A O     
71   C  CB    . VAL   A 11  ? 0.1391 0.1283 0.1143 0.0014  -0.0202 -0.0268 8   VAL   A CB    
72   C  CG1   . VAL   A 11  ? 0.1257 0.1514 0.1173 -0.0091 -0.0155 -0.0262 8   VAL   A CG1   
73   C  CG2   . VAL   A 11  ? 0.1473 0.1286 0.1098 0.0146  -0.0162 -0.0186 8   VAL   A CG2   
74   N  N     . VAL   A 12  ? 0.1246 0.1191 0.1116 0.0019  -0.0279 -0.0374 9   VAL   A N     
75   C  CA    . VAL   A 12  ? 0.1126 0.1469 0.1040 0.0177  -0.0181 -0.0411 9   VAL   A CA    
76   C  C     . VAL   A 12  ? 0.1187 0.1548 0.0816 0.0161  -0.0248 -0.0385 9   VAL   A C     
77   O  O     . VAL   A 12  ? 0.1216 0.1641 0.0999 0.0207  -0.0422 -0.0572 9   VAL   A O     
78   C  CB    . VAL   A 12  ? 0.1213 0.1781 0.1105 0.0054  -0.0186 -0.0313 9   VAL   A CB    
79   C  CG1   . VAL   A 12  ? 0.1291 0.1892 0.1306 0.0228  -0.0036 -0.0180 9   VAL   A CG1   
80   C  CG2   . VAL   A 12  ? 0.1356 0.1787 0.1328 0.0152  -0.0278 -0.0095 9   VAL   A CG2   
81   N  N     . GLY   A 13  ? 0.1225 0.1674 0.0739 0.0258  -0.0229 -0.0377 10  GLY   A N     
82   C  CA    . GLY   A 13  ? 0.1202 0.1805 0.1034 0.0241  -0.0355 -0.0452 10  GLY   A CA    
83   C  C     . GLY   A 13  ? 0.1237 0.1942 0.1135 0.0070  -0.0378 -0.0430 10  GLY   A C     
84   O  O     . GLY   A 13  ? 0.1330 0.1822 0.1147 -0.0055 -0.0142 -0.0465 10  GLY   A O     
85   N  N     . ALA   A 14  ? 0.1171 0.1983 0.0920 0.0187  -0.0086 -0.0562 11  ALA   A N     
86   C  CA    . ALA   A 14  ? 0.1305 0.2187 0.0919 0.0147  -0.0228 -0.0575 11  ALA   A CA    
87   C  C     . ALA   A 14  ? 0.1303 0.2343 0.1061 -0.0025 -0.0426 -0.0663 11  ALA   A C     
88   O  O     . ALA   A 14  ? 0.1492 0.2173 0.1043 0.0175  -0.0327 -0.0658 11  ALA   A O     
89   C  CB    . ALA   A 14  ? 0.1285 0.2430 0.1090 0.0097  -0.0232 -0.0343 11  ALA   A CB    
90   N  N     . GLY   A 15  ? 0.1612 0.2428 0.0959 -0.0346 0.0056  -0.0707 12  GLY   A N     
91   C  CA    . GLY   A 15  ? 0.1621 0.2346 0.1240 -0.0472 -0.0197 -0.0724 12  GLY   A CA    
92   C  C     . GLY   A 15  ? 0.1783 0.2129 0.1458 -0.0287 -0.0054 -0.0532 12  GLY   A C     
93   O  O     . GLY   A 15  ? 0.1920 0.2526 0.1567 -0.0297 -0.0256 -0.0437 12  GLY   A O     
94   N  N     . GLY   A 16  ? 0.1454 0.2346 0.1388 -0.0354 -0.0232 -0.0612 13  GLY   A N     
95   C  CA    . GLY   A 16  ? 0.1460 0.1916 0.1531 -0.0282 -0.0160 -0.0575 13  GLY   A CA    
96   C  C     . GLY   A 16  ? 0.1636 0.1987 0.1271 -0.0330 -0.0133 -0.0524 13  GLY   A C     
97   O  O     . GLY   A 16  ? 0.1663 0.2187 0.1467 -0.0216 -0.0015 -0.0520 13  GLY   A O     
98   N  N     . VAL   A 17  ? 0.1487 0.1712 0.1150 -0.0112 -0.0080 -0.0482 14  VAL   A N     
99   C  CA    . VAL   A 17  ? 0.1346 0.1614 0.0929 -0.0060 0.0051  -0.0378 14  VAL   A CA    
100  C  C     . VAL   A 17  ? 0.1272 0.1593 0.0978 -0.0211 -0.0174 -0.0392 14  VAL   A C     
101  O  O     . VAL   A 17  ? 0.1506 0.1502 0.0922 -0.0174 0.0024  -0.0258 14  VAL   A O     
102  C  CB    . VAL   A 17  ? 0.1344 0.1699 0.0882 -0.0158 -0.0108 -0.0277 14  VAL   A CB    
103  C  CG1   . VAL   A 17  ? 0.1386 0.1616 0.0942 0.0113  -0.0090 -0.0272 14  VAL   A CG1   
104  C  CG2   . VAL   A 17  ? 0.1309 0.1553 0.1042 -0.0235 -0.0398 -0.0128 14  VAL   A CG2   
105  N  N     . GLY   A 18  ? 0.1572 0.1632 0.1062 -0.0054 -0.0115 -0.0488 15  GLY   A N     
106  C  CA    . GLY   A 18  ? 0.1657 0.1246 0.1171 -0.0208 -0.0108 -0.0350 15  GLY   A CA    
107  C  C     . GLY   A 18  ? 0.1637 0.1264 0.1179 -0.0284 -0.0231 -0.0321 15  GLY   A C     
108  O  O     . GLY   A 18  ? 0.2047 0.1324 0.1027 -0.0215 -0.0210 -0.0206 15  GLY   A O     
109  N  N     . LYS   A 19  ? 0.1734 0.1309 0.1104 -0.0290 -0.0140 -0.0226 16  LYS   A N     
110  C  CA    . LYS   A 19  ? 0.1809 0.1272 0.1272 -0.0275 -0.0328 -0.0161 16  LYS   A CA    
111  C  C     . LYS   A 19  ? 0.1695 0.1236 0.1298 -0.0107 -0.0340 -0.0228 16  LYS   A C     
112  O  O     . LYS   A 19  ? 0.2122 0.1228 0.1340 -0.0218 -0.0527 -0.0076 16  LYS   A O     
113  C  CB    . LYS   A 19  ? 0.1811 0.1622 0.1353 -0.0068 -0.0412 -0.0302 16  LYS   A CB    
114  C  CG    . LYS   A 19  ? 0.1383 0.1851 0.1324 -0.0396 -0.0424 -0.0244 16  LYS   A CG    
115  C  CD    . LYS   A 19  ? 0.1714 0.2392 0.1490 -0.0059 -0.0141 0.0028  16  LYS   A CD    
116  C  CE    . LYS   A 19  ? 0.1873 0.2193 0.1323 0.0233  -0.0069 -0.0079 16  LYS   A CE    
117  N  NZ    . LYS   A 19  ? 0.1723 0.2021 0.1495 -0.0028 -0.0104 -0.0142 16  LYS   A NZ    
118  N  N     . SER   A 20  ? 0.1892 0.1248 0.1319 -0.0228 -0.0281 -0.0241 17  SER   A N     
119  C  CA    . SER   A 20  ? 0.2114 0.1232 0.1428 -0.0243 -0.0378 -0.0194 17  SER   A CA    
120  C  C     . SER   A 20  ? 0.2282 0.1134 0.1550 -0.0298 -0.0356 -0.0419 17  SER   A C     
121  O  O     . SER   A 20  ? 0.2583 0.1138 0.1595 -0.0313 -0.0371 -0.0192 17  SER   A O     
122  C  CB    . SER   A 20  ? 0.2231 0.1141 0.1915 -0.0326 -0.0094 -0.0362 17  SER   A CB    
123  O  OG    . SER   A 20  ? 0.2378 0.1380 0.1648 -0.0235 -0.0101 -0.0436 17  SER   A OG    
124  N  N     . ALA   A 21  ? 0.2104 0.1283 0.1083 -0.0341 -0.0316 -0.0200 18  ALA   A N     
125  C  CA    . ALA   A 21  ? 0.2451 0.1130 0.1401 -0.0047 -0.0138 -0.0340 18  ALA   A CA    
126  C  C     . ALA   A 21  ? 0.2279 0.1093 0.1302 -0.0229 0.0046  -0.0227 18  ALA   A C     
127  O  O     . ALA   A 21  ? 0.2999 0.1291 0.1318 -0.0487 0.0044  -0.0195 18  ALA   A O     
128  C  CB    . ALA   A 21  ? 0.2224 0.1404 0.1591 -0.0154 0.0169  -0.0625 18  ALA   A CB    
129  N  N     . LEU   A 22  ? 0.2226 0.1049 0.1367 -0.0170 -0.0164 -0.0091 19  LEU   A N     
130  C  CA    . LEU   A 22  ? 0.2245 0.1022 0.1472 -0.0210 -0.0276 -0.0046 19  LEU   A CA    
131  C  C     . LEU   A 22  ? 0.2142 0.0958 0.1208 -0.0043 0.0061  0.0185  19  LEU   A C     
132  O  O     . LEU   A 22  ? 0.2716 0.1140 0.1193 -0.0281 -0.0122 -0.0054 19  LEU   A O     
133  C  CB    . LEU   A 22  ? 0.2136 0.1159 0.1346 -0.0239 -0.0295 -0.0022 19  LEU   A CB    
134  C  CG    . LEU   A 22  ? 0.2064 0.1304 0.1271 -0.0298 -0.0374 -0.0037 19  LEU   A CG    
135  C  CD1   . LEU   A 22  ? 0.1974 0.1445 0.1184 -0.0164 -0.0466 0.0132  19  LEU   A CD1   
136  C  CD2   . LEU   A 22  ? 0.2054 0.1398 0.1466 0.0132  -0.0499 -0.0092 19  LEU   A CD2   
137  N  N     . THR   A 23  ? 0.2206 0.1119 0.1355 -0.0151 -0.0198 -0.0227 20  THR   A N     
138  C  CA    . THR   A 23  ? 0.2509 0.1087 0.1612 -0.0061 -0.0485 0.0067  20  THR   A CA    
139  C  C     . THR   A 23  ? 0.2870 0.0916 0.1355 -0.0047 -0.0422 -0.0244 20  THR   A C     
140  O  O     . THR   A 23  ? 0.3247 0.1137 0.1263 -0.0099 -0.0476 -0.0130 20  THR   A O     
141  C  CB    . THR   A 23  ? 0.2358 0.1042 0.1780 -0.0081 -0.0434 -0.0052 20  THR   A CB    
142  O  OG1   . THR   A 23  ? 0.2160 0.1498 0.1601 -0.0107 -0.0462 -0.0003 20  THR   A OG1   
143  C  CG2   . THR   A 23  ? 0.2334 0.1678 0.1736 0.0064  -0.0429 0.0084  20  THR   A CG2   
144  N  N     . ILE   A 24  ? 0.3094 0.1117 0.1415 -0.0357 -0.0430 0.0001  21  ILE   A N     
145  C  CA    . ILE   A 24  ? 0.3392 0.1113 0.1577 -0.0262 -0.0305 0.0095  21  ILE   A CA    
146  C  C     . ILE   A 24  ? 0.3243 0.1244 0.1288 -0.0545 -0.0174 0.0218  21  ILE   A C     
147  O  O     . ILE   A 24  ? 0.4029 0.1253 0.1730 -0.0387 -0.0517 0.0528  21  ILE   A O     
148  C  CB    . ILE   A 24  ? 0.3306 0.1317 0.1886 -0.0258 -0.0392 0.0109  21  ILE   A CB    
149  C  CG1   . ILE   A 24  ? 0.3970 0.1601 0.1718 -0.0649 -0.0100 -0.0209 21  ILE   A CG1   
150  C  CG2   . ILE   A 24  ? 0.3808 0.1139 0.1804 -0.0566 -0.0434 0.0022  21  ILE   A CG2   
151  C  CD1   . ILE   A 24  ? 0.4279 0.1779 0.1908 -0.0636 -0.0398 -0.0216 21  ILE   A CD1   
152  N  N     . GLN   A 25  ? 0.3542 0.1128 0.1246 -0.0529 -0.0412 0.0114  22  GLN   A N     
153  C  CA    . GLN   A 25  ? 0.3156 0.1066 0.1778 -0.0603 0.0036  0.0155  22  GLN   A CA    
154  C  C     . GLN   A 25  ? 0.3371 0.1428 0.1315 -0.0615 0.0060  -0.0216 22  GLN   A C     
155  O  O     . GLN   A 25  ? 0.3951 0.1465 0.1381 -0.0648 -0.0021 0.0092  22  GLN   A O     
156  C  CB    . GLN   A 25  ? 0.3385 0.1565 0.1975 -0.0344 -0.0090 0.0322  22  GLN   A CB    
157  C  CG    . GLN   A 25  ? 0.3635 0.2378 0.2059 -0.0470 0.0296  0.0485  22  GLN   A CG    
158  C  CD    . GLN   A 25  ? 0.3440 0.2173 0.1765 -0.0650 -0.0071 0.1138  22  GLN   A CD    
159  O  OE1   . GLN   A 25  ? 0.3265 0.2770 0.2223 -0.0895 -0.0306 0.0966  22  GLN   A OE1   
160  N  NE2   . GLN   A 25  ? 0.3114 0.2513 0.1459 -0.1023 -0.0030 0.0299  22  GLN   A NE2   
161  N  N     . LEU   A 26  ? 0.3258 0.1319 0.1452 -0.0615 -0.0184 0.0162  23  LEU   A N     
162  C  CA    . LEU   A 26  ? 0.3279 0.1148 0.1510 -0.0357 -0.0314 0.0021  23  LEU   A CA    
163  C  C     . LEU   A 26  ? 0.3819 0.1216 0.1398 -0.0241 -0.0384 -0.0038 23  LEU   A C     
164  O  O     . LEU   A 26  ? 0.4353 0.1525 0.1402 -0.0307 -0.0489 0.0024  23  LEU   A O     
165  C  CB    . LEU   A 26  ? 0.3085 0.1214 0.1329 -0.0077 -0.0201 -0.0086 23  LEU   A CB    
166  C  CG    . LEU   A 26  ? 0.3114 0.1632 0.1578 0.0020  -0.0352 -0.0168 23  LEU   A CG    
167  C  CD1   . LEU   A 26  ? 0.2794 0.1713 0.1524 -0.0133 -0.0279 -0.0293 23  LEU   A CD1   
168  C  CD2   . LEU   A 26  ? 0.2920 0.1811 0.1820 -0.0090 -0.0284 -0.0161 23  LEU   A CD2   
169  N  N     . ILE   A 27  ? 0.4864 0.1143 0.1303 -0.0069 -0.0516 0.0073  24  ILE   A N     
170  C  CA    . ILE   A 27  ? 0.4740 0.1981 0.1436 0.0276  -0.0656 0.0107  24  ILE   A CA    
171  C  C     . ILE   A 27  ? 0.5090 0.2185 0.1019 -0.0114 -0.0624 -0.0267 24  ILE   A C     
172  O  O     . ILE   A 27  ? 0.5473 0.1976 0.1661 -0.0092 -0.1002 0.0112  24  ILE   A O     
173  C  CB    . ILE   A 27  ? 0.5182 0.1837 0.1673 0.0514  -0.0900 -0.0138 24  ILE   A CB    
174  C  CG1   . ILE   A 27  ? 0.5192 0.1923 0.1889 0.0781  -0.0828 0.0409  24  ILE   A CG1   
175  C  CG2   . ILE   A 27  ? 0.5864 0.2041 0.1909 0.0591  -0.1111 0.0118  24  ILE   A CG2   
176  C  CD1   . ILE   A 27  ? 0.5654 0.2312 0.1447 0.0495  -0.0681 -0.0122 24  ILE   A CD1   
177  N  N     . GLN   A 28  ? 0.4698 0.1674 0.1720 -0.0015 -0.0792 0.0339  25  GLN   A N     
178  C  CA    . GLN   A 28  ? 0.4882 0.1638 0.2531 -0.0315 -0.0688 0.0386  25  GLN   A CA    
179  C  C     . GLN   A 28  ? 0.4621 0.1522 0.1816 -0.0869 -0.0556 0.0708  25  GLN   A C     
180  O  O     . GLN   A 28  ? 0.5237 0.2125 0.2408 -0.1090 -0.0337 0.0699  25  GLN   A O     
181  C  CB    . GLN   A 28  ? 0.3858 0.1832 0.2340 0.0246  -0.0356 0.0427  25  GLN   A CB    
182  C  CG    . GLN   A 28  ? 0.3958 0.1775 0.3422 0.0069  -0.0208 0.0039  25  GLN   A CG    
183  C  CD    . GLN   A 28  ? 0.2782 0.1572 0.4151 -0.0086 0.0209  -0.0206 25  GLN   A CD    
184  O  OE1   . GLN   A 28  ? 0.3606 0.2563 0.3789 -0.0798 -0.0808 -0.0349 25  GLN   A OE1   
185  N  NE2   . GLN   A 28  ? 0.3750 0.2769 0.4700 0.0182  0.1224  -0.0324 25  GLN   A NE2   
186  N  N     . ASN   A 29  ? 0.5101 0.1660 0.1995 -0.0651 0.0010  0.0178  26  ASN   A N     
187  C  CA    . ASN   A 29  ? 0.4151 0.1557 0.1604 -0.0971 -0.0199 0.0633  26  ASN   A CA    
188  C  C     . ASN   A 29  ? 0.4567 0.2976 0.1967 -0.1181 -0.0531 0.0546  26  ASN   A C     
189  O  O     . ASN   A 29  ? 0.5230 0.3691 0.2517 -0.2355 -0.0540 0.0373  26  ASN   A O     
190  C  CB    . ASN   A 29  ? 0.4427 0.2654 0.1668 -0.0875 -0.0594 0.0725  26  ASN   A CB    
191  C  CG    . ASN   A 29  ? 0.4339 0.3488 0.2038 -0.1323 0.0170  0.0542  26  ASN   A CG    
192  O  OD1   . ASN   A 29  ? 0.5055 0.4365 0.2099 -0.0910 0.0177  0.0473  26  ASN   A OD1   
193  N  ND2   . ASN   A 29  ? 0.5629 0.4626 0.1916 -0.1969 -0.0360 0.0732  26  ASN   A ND2   
194  N  N     . HIS   A 30  ? 0.3564 0.2590 0.1999 -0.0995 -0.0263 0.0310  27  HIS   A N     
195  C  CA    . HIS   A 30  ? 0.3280 0.2335 0.2116 -0.1162 0.0108  0.0444  27  HIS   A CA    
196  C  C     . HIS   A 30  ? 0.3371 0.3225 0.1500 -0.1003 0.0141  -0.0296 27  HIS   A C     
197  O  O     . HIS   A 30  ? 0.3437 0.1884 0.1851 -0.0876 -0.0064 0.0041  27  HIS   A O     
198  C  CB    . HIS   A 30  ? 0.3944 0.2307 0.1867 -0.1178 0.0685  0.0613  27  HIS   A CB    
199  C  CG    . HIS   A 30  ? 0.2469 0.1887 0.2406 -0.0924 -0.0372 0.0792  27  HIS   A CG    
200  N  ND1   . HIS   A 30  ? 0.3748 0.1354 0.2472 -0.0637 0.0622  0.0255  27  HIS   A ND1   
201  C  CD2   . HIS   A 30  ? 0.2779 0.2015 0.3121 -0.0823 -0.0279 0.0073  27  HIS   A CD2   
202  C  CE1   . HIS   A 30  ? 0.3800 0.1714 0.2769 -0.0494 0.0060  -0.0496 27  HIS   A CE1   
203  N  NE2   . HIS   A 30  ? 0.4872 0.2360 0.2214 -0.1827 -0.0157 0.0154  27  HIS   A NE2   
204  N  N     . PHE   A 31  ? 0.3523 0.3011 0.2008 -0.1331 0.0217  0.0732  28  PHE   A N     
205  C  CA    . PHE   A 31  ? 0.2473 0.2544 0.1673 -0.0729 0.0210  -0.0192 28  PHE   A CA    
206  C  C     . PHE   A 31  ? 0.3136 0.2695 0.2981 -0.1567 0.0293  -0.0520 28  PHE   A C     
207  O  O     . PHE   A 31  ? 0.3886 0.3052 0.2793 -0.1871 0.0355  0.0192  28  PHE   A O     
208  C  CB    . PHE   A 31  ? 0.2221 0.1871 0.1616 -0.0963 0.0337  -0.0099 28  PHE   A CB    
209  C  CG    . PHE   A 31  ? 0.3081 0.2195 0.1520 -0.1088 0.0207  -0.0258 28  PHE   A CG    
210  C  CD1   . PHE   A 31  ? 0.3014 0.2414 0.1688 -0.1067 0.0307  -0.0212 28  PHE   A CD1   
211  C  CD2   . PHE   A 31  ? 0.2917 0.3006 0.1655 -0.1299 0.0676  0.0094  28  PHE   A CD2   
212  C  CE1   . PHE   A 31  ? 0.3558 0.1856 0.2074 -0.0959 0.0170  -0.0353 28  PHE   A CE1   
213  C  CE2   . PHE   A 31  ? 0.3098 0.2625 0.1829 -0.1325 0.0265  -0.0541 28  PHE   A CE2   
214  C  CZ    . PHE   A 31  ? 0.3517 0.2511 0.1478 -0.0968 0.0324  -0.0271 28  PHE   A CZ    
215  N  N     . VAL   A 32  ? 0.3484 0.1843 0.2286 -0.1002 -0.0233 -0.0111 29  VAL   A N     
216  C  CA    . VAL   A 32  ? 0.3703 0.1704 0.2578 -0.1227 -0.0427 -0.0096 29  VAL   A CA    
217  C  C     . VAL   A 32  ? 0.4346 0.2256 0.3125 -0.1223 -0.0892 0.0211  29  VAL   A C     
218  O  O     . VAL   A 32  ? 0.5649 0.2229 0.2681 -0.1600 -0.1143 0.0132  29  VAL   A O     
219  C  CB    . VAL   A 32  ? 0.3841 0.2279 0.3217 -0.1006 -0.0953 -0.0424 29  VAL   A CB    
220  C  CG1   . VAL   A 32  ? 0.4430 0.2231 0.3526 -0.0877 -0.1033 -0.0255 29  VAL   A CG1   
221  C  CG2   . VAL   A 32  ? 0.4474 0.2229 0.2715 -0.0908 -0.0380 -0.0637 29  VAL   A CG2   
222  N  N     . ASP   A 33  ? 0.5282 0.2873 0.4374 -0.1981 -0.1706 -0.0261 30  ASP   A N     
223  C  CA    . ASP   A 33  ? 0.4297 0.3149 0.6198 -0.2178 -0.1278 0.1411  30  ASP   A CA    
224  C  C     . ASP   A 33  ? 0.4638 0.3514 0.6494 -0.2230 -0.0345 0.1336  30  ASP   A C     
225  O  O     . ASP   A 33  ? 0.5558 0.3921 0.9686 -0.4527 -0.1277 -0.0036 30  ASP   A O     
226  C  CB    . ASP   A 33  ? 0.4591 0.4208 0.6423 -0.2693 -0.0582 0.0651  30  ASP   A CB    
227  C  CG    . ASP   A 33  ? 0.5012 0.4377 0.8323 -0.2118 0.0037  -0.0367 30  ASP   A CG    
228  O  OD1   . ASP   A 33  ? 0.7975 0.4722 1.0335 -0.1874 -0.0731 -0.1187 30  ASP   A OD1   
229  O  OD2   . ASP   A 33  ? 0.6864 0.4838 1.0845 -0.2865 0.0014  0.0806  30  ASP   A OD2   
230  N  N     . GLU   A 34  ? 0.3230 0.4440 0.6149 -0.2486 -0.0454 0.1132  31  GLU   A N     
231  C  CA    . GLU   A 34  ? 0.3580 0.4956 0.6514 -0.1292 0.0168  0.0722  31  GLU   A CA    
232  C  C     . GLU   A 34  ? 0.3629 0.4356 0.5769 -0.1444 0.0084  0.0043  31  GLU   A C     
233  O  O     . GLU   A 34  ? 0.5647 0.5034 0.5145 -0.1902 -0.0124 -0.1092 31  GLU   A O     
234  C  CB    . GLU   A 34  ? 0.4894 0.5324 0.6204 -0.1704 -0.0121 -0.0295 31  GLU   A CB    
235  C  CG    . GLU   A 34  ? 0.6818 0.4293 0.5439 -0.1864 -0.0294 -0.0851 31  GLU   A CG    
236  C  CD    . GLU   A 34  ? 0.6292 0.6244 0.6803 -0.2204 -0.0391 -0.1137 31  GLU   A CD    
237  O  OE1   . GLU   A 34  ? 0.7007 0.6611 0.8244 -0.2616 0.0030  -0.2244 31  GLU   A OE1   
238  O  OE2   . GLU   A 34  ? 0.7286 0.7317 0.8871 -0.2111 0.0914  -0.0664 31  GLU   A OE2   
239  N  N     . TYR   A 35  ? 0.3888 0.3102 0.2542 -0.1294 0.0374  -0.0624 32  TYR   A N     
240  C  CA    . TYR   A 35  ? 0.3875 0.2534 0.2482 -0.1086 -0.0003 -0.0691 32  TYR   A CA    
241  C  C     . TYR   A 35  ? 0.3189 0.2504 0.2288 -0.0805 -0.0413 -0.0807 32  TYR   A C     
242  O  O     . TYR   A 35  ? 0.3374 0.2711 0.2280 -0.1236 0.0194  -0.0706 32  TYR   A O     
243  C  CB    . TYR   A 35  ? 0.3380 0.2047 0.2518 -0.0766 -0.0093 -0.0512 32  TYR   A CB    
244  C  CG    . TYR   A 35  ? 0.3471 0.1710 0.2263 -0.0656 -0.0117 -0.0314 32  TYR   A CG    
245  C  CD1   . TYR   A 35  ? 0.3670 0.2398 0.2776 -0.1171 -0.0545 0.0142  32  TYR   A CD1   
246  C  CD2   . TYR   A 35  ? 0.3405 0.1821 0.2267 -0.1065 -0.0272 -0.0500 32  TYR   A CD2   
247  C  CE1   . TYR   A 35  ? 0.4075 0.2376 0.2467 -0.0539 -0.0294 0.0018  32  TYR   A CE1   
248  C  CE2   . TYR   A 35  ? 0.3861 0.2102 0.2240 -0.0546 0.0048  -0.0287 32  TYR   A CE2   
249  C  CZ    . TYR   A 35  ? 0.3983 0.1930 0.2602 -0.0656 -0.0324 -0.0154 32  TYR   A CZ    
250  O  OH    . TYR   A 35  ? 0.3879 0.2857 0.2584 -0.0794 -0.0935 -0.0144 32  TYR   A OH    
251  N  N     . ASP   A 36  ? 0.3452 0.2319 0.2781 -0.1219 -0.0126 -0.0777 33  ASP   A N     
252  C  CA    . ASP   A 36  ? 0.2834 0.2683 0.2343 -0.1054 -0.0408 -0.0568 33  ASP   A CA    
253  C  C     . ASP   A 36  ? 0.2562 0.2912 0.2184 -0.0852 0.0004  -0.0514 33  ASP   A C     
254  O  O     . ASP   A 36  ? 0.2922 0.2681 0.2281 -0.1070 -0.0245 -0.0595 33  ASP   A O     
255  C  CB    . ASP   A 36  ? 0.3017 0.2458 0.2488 -0.1102 -0.0063 -0.0356 33  ASP   A CB    
256  C  CG    . ASP   A 36  ? 0.4447 0.2765 0.2660 -0.0507 -0.0061 -0.0553 33  ASP   A CG    
257  O  OD1   . ASP   A 36  ? 0.4241 0.2706 0.2385 -0.0636 0.0312  -0.0876 33  ASP   A OD1   
258  O  OD2   . ASP   A 36  ? 0.5486 0.2913 0.2605 -0.0221 0.0400  -0.0402 33  ASP   A OD2   
259  N  N     . PRO   A 37  ? 0.2934 0.2563 0.2030 -0.0488 -0.0212 -0.0901 34  PRO   A N     
260  C  CA    . PRO   A 37  ? 0.2478 0.2499 0.1946 -0.0284 0.0025  -0.0896 34  PRO   A CA    
261  C  C     . PRO   A 37  ? 0.2410 0.2414 0.1860 -0.0215 -0.0166 -0.0658 34  PRO   A C     
262  O  O     . PRO   A 37  ? 0.3229 0.2373 0.2049 -0.0549 0.0022  -0.0726 34  PRO   A O     
263  C  CB    . PRO   A 37  ? 0.2645 0.3189 0.2626 -0.0027 -0.0092 -0.0638 34  PRO   A CB    
264  C  CG    . PRO   A 37  ? 0.2970 0.3643 0.2451 -0.0356 -0.0736 -0.0410 34  PRO   A CG    
265  C  CD    . PRO   A 37  ? 0.2656 0.3011 0.2059 -0.0146 -0.0200 -0.0972 34  PRO   A CD    
266  N  N     . THR   A 38  ? 0.2351 0.2287 0.1884 -0.0367 -0.0284 -0.0857 35  THR   A N     
267  C  CA    . THR   A 38  ? 0.2399 0.2358 0.1881 -0.0338 -0.0169 -0.0728 35  THR   A CA    
268  C  C     . THR   A 38  ? 0.2500 0.2103 0.1786 -0.0486 -0.0161 -0.0776 35  THR   A C     
269  O  O     . THR   A 38  ? 0.2784 0.2210 0.2000 -0.0035 -0.0152 -0.0560 35  THR   A O     
270  C  CB    . THR   A 38  ? 0.3380 0.2554 0.1965 -0.0462 -0.0164 -0.0864 35  THR   A CB    
271  O  OG1   . THR   A 38  ? 0.3636 0.2130 0.2511 -0.0565 -0.0548 -0.0890 35  THR   A OG1   
272  C  CG2   . THR   A 38  ? 0.3394 0.2782 0.2195 -0.0571 -0.0184 -0.0932 35  THR   A CG2   
273  N  N     . ILE   A 39  ? 0.2670 0.1494 0.1825 -0.0117 -0.0061 -0.0651 36  ILE   A N     
274  C  CA    . ILE   A 39  ? 0.2835 0.1350 0.2186 -0.0250 -0.0193 -0.0345 36  ILE   A CA    
275  C  C     . ILE   A 39  ? 0.2455 0.1391 0.1887 -0.0133 -0.0305 -0.0495 36  ILE   A C     
276  O  O     . ILE   A 39  ? 0.2555 0.1429 0.1640 -0.0087 -0.0103 -0.0417 36  ILE   A O     
277  C  CB    . ILE   A 39  ? 0.2911 0.1338 0.2342 -0.0142 -0.0010 -0.0366 36  ILE   A CB    
278  C  CG1   . ILE   A 39  ? 0.2368 0.1513 0.2221 -0.0072 -0.0090 -0.0383 36  ILE   A CG1   
279  C  CG2   . ILE   A 39  ? 0.3216 0.1846 0.2447 -0.0232 -0.0153 -0.0103 36  ILE   A CG2   
280  C  CD1   . ILE   A 39  ? 0.2943 0.1808 0.2261 -0.0127 0.0032  -0.0253 36  ILE   A CD1   
281  N  N     . GLU   A 40  ? 0.2459 0.1490 0.2116 -0.0115 -0.0435 -0.0522 37  GLU   A N     
282  C  CA    . GLU   A 40  ? 0.2583 0.1399 0.1928 -0.0127 -0.0572 -0.0511 37  GLU   A CA    
283  C  C     . GLU   A 40  ? 0.2543 0.1640 0.1981 0.0060  -0.0520 -0.0723 37  GLU   A C     
284  O  O     . GLU   A 40  ? 0.2982 0.1689 0.2376 0.0376  -0.0809 -0.0605 37  GLU   A O     
285  C  CB    . GLU   A 40  ? 0.2353 0.2094 0.2125 -0.0034 -0.0538 -0.0491 37  GLU   A CB    
286  C  CG    . GLU   A 40  ? 0.2125 0.2211 0.1948 0.0042  -0.0315 -0.0582 37  GLU   A CG    
287  C  CD    . GLU   A 40  ? 0.2168 0.1837 0.2043 0.0227  -0.0148 -0.0561 37  GLU   A CD    
288  O  OE1   . GLU   A 40  ? 0.2530 0.2074 0.1991 0.0568  -0.0351 -0.0795 37  GLU   A OE1   
289  O  OE2   . GLU   A 40  ? 0.2305 0.2601 0.2502 0.0641  -0.0100 -0.0565 37  GLU   A OE2   
290  N  N     . ASP   A 41  ? 0.2999 0.1404 0.2138 0.0193  -0.0912 -0.0807 38  ASP   A N     
291  C  CA    . ASP   A 41  ? 0.2838 0.1511 0.2328 0.0390  -0.0899 -0.0721 38  ASP   A CA    
292  C  C     . ASP   A 41  ? 0.2502 0.1450 0.2076 0.0471  -0.0762 -0.0730 38  ASP   A C     
293  O  O     . ASP   A 41  ? 0.2531 0.1395 0.2098 0.0290  -0.0740 -0.0488 38  ASP   A O     
294  C  CB    . ASP   A 41  ? 0.3253 0.2871 0.2613 -0.0359 -0.0765 -0.0544 38  ASP   A CB    
295  C  CG    . ASP   A 41  ? 0.4632 0.2919 0.3942 -0.0057 -0.1048 -0.0559 38  ASP   A CG    
296  O  OD1   . ASP   A 41  ? 0.4719 0.3032 0.4161 0.0158  -0.1185 -0.0076 38  ASP   A OD1   
297  O  OD2   . ASP   A 41  ? 0.4899 0.3610 0.4121 -0.0055 -0.1301 0.0973  38  ASP   A OD2   
298  N  N     . SER   A 42  ? 0.2646 0.1681 0.1878 0.0251  -0.0702 -0.0489 39  SER   A N     
299  C  CA    . SER   A 42  ? 0.2420 0.1507 0.1735 0.0258  -0.0559 -0.0473 39  SER   A CA    
300  C  C     . SER   A 42  ? 0.2860 0.1257 0.1807 0.0239  -0.0440 -0.0398 39  SER   A C     
301  O  O     . SER   A 42  ? 0.3405 0.1277 0.2130 0.0019  -0.0608 -0.0360 39  SER   A O     
302  C  CB    . SER   A 42  ? 0.2574 0.2094 0.1922 0.0047  -0.0579 -0.0127 39  SER   A CB    
303  O  OG    . SER   A 42  ? 0.2952 0.2413 0.2651 0.0711  -0.0628 -0.0474 39  SER   A OG    
304  N  N     . TYR   A 43  ? 0.2795 0.1123 0.1861 0.0114  -0.0787 -0.0386 40  TYR   A N     
305  C  CA    . TYR   A 43  ? 0.3087 0.0982 0.2049 -0.0101 -0.0634 -0.0234 40  TYR   A CA    
306  C  C     . TYR   A 43  ? 0.3009 0.1182 0.1652 -0.0196 -0.0520 -0.0179 40  TYR   A C     
307  O  O     . TYR   A 43  ? 0.3120 0.1282 0.1659 -0.0215 -0.0714 0.0059  40  TYR   A O     
308  C  CB    . TYR   A 43  ? 0.3058 0.1594 0.2171 0.0027  -0.0743 -0.0492 40  TYR   A CB    
309  C  CG    . TYR   A 43  ? 0.3273 0.1706 0.2528 -0.0297 -0.0733 -0.0278 40  TYR   A CG    
310  C  CD1   . TYR   A 43  ? 0.2779 0.2012 0.2398 -0.0185 -0.0176 -0.0322 40  TYR   A CD1   
311  C  CD2   . TYR   A 43  ? 0.4137 0.2826 0.2681 -0.1126 -0.0348 -0.0467 40  TYR   A CD2   
312  C  CE1   . TYR   A 43  ? 0.3013 0.2860 0.2373 -0.0522 -0.0452 -0.0102 40  TYR   A CE1   
313  C  CE2   . TYR   A 43  ? 0.3692 0.3560 0.2567 -0.1158 -0.0427 -0.0055 40  TYR   A CE2   
314  C  CZ    . TYR   A 43  ? 0.3936 0.2928 0.2301 -0.1375 -0.0331 -0.0666 40  TYR   A CZ    
315  O  OH    . TYR   A 43  ? 0.3831 0.4712 0.3009 -0.1929 -0.0262 -0.1062 40  TYR   A OH    
316  N  N     . ARG   A 44  ? 0.3736 0.0938 0.1732 -0.0356 -0.0637 0.0004  41  ARG   A N     
317  C  CA    . ARG   A 44  ? 0.3606 0.1171 0.2077 -0.0351 -0.0910 0.0064  41  ARG   A CA    
318  C  C     . ARG   A 44  ? 0.4498 0.1654 0.2153 -0.0990 -0.0517 0.0164  41  ARG   A C     
319  O  O     . ARG   A 44  ? 0.5757 0.2481 0.1719 -0.2087 -0.0641 0.0093  41  ARG   A O     
320  C  CB    . ARG   A 44  ? 0.3960 0.1185 0.2922 -0.0120 -0.0969 0.0416  41  ARG   A CB    
321  C  CG    . ARG   A 44  ? 0.3880 0.2419 0.2704 0.0048  -0.1183 0.0606  41  ARG   A CG    
322  C  CD    . ARG   A 44  ? 0.4156 0.2489 0.2885 0.0055  -0.0714 0.0787  41  ARG   A CD    
323  N  NE    . ARG   A 44  ? 0.4236 0.2291 0.2950 0.0239  -0.0726 0.0958  41  ARG   A NE    
324  C  CZ    . ARG   A 44  ? 0.4479 0.2286 0.2630 -0.0103 -0.0080 0.0293  41  ARG   A CZ    
325  N  NH1   . ARG   A 44  ? 0.4494 0.2314 0.2483 0.0001  -0.0646 0.0299  41  ARG   A NH1   
326  N  NH2   . ARG   A 44  ? 0.4357 0.2178 0.3770 -0.0051 -0.0048 0.0175  41  ARG   A NH2   
327  N  N     . LYS   A 45  ? 0.3334 0.1812 0.1862 -0.0910 -0.0084 -0.0052 42  LYS   A N     
328  C  CA    . LYS   A 45  ? 0.2985 0.2334 0.1749 -0.0935 -0.0170 0.0228  42  LYS   A CA    
329  C  C     . LYS   A 45  ? 0.2998 0.2196 0.1374 -0.1022 0.0217  0.0097  42  LYS   A C     
330  O  O     . LYS   A 45  ? 0.3691 0.1940 0.1505 -0.0881 -0.0100 0.0229  42  LYS   A O     
331  C  CB    . LYS   A 45  ? 0.2640 0.3442 0.2447 -0.0932 -0.0433 -0.0215 42  LYS   A CB    
332  C  CG    . LYS   A 45  ? 0.2725 0.3956 0.3027 -0.0257 -0.0216 -0.0265 42  LYS   A CG    
333  C  CD    . LYS   A 45  ? 0.3272 0.3299 0.3057 0.0043  -0.0597 -0.0910 42  LYS   A CD    
334  C  CE    . LYS   A 45  ? 0.3818 0.3852 0.4082 0.0739  -0.0089 -0.0946 42  LYS   A CE    
335  N  NZ    . LYS   A 45  ? 0.3839 0.4678 0.4362 0.1181  -0.0623 -0.1279 42  LYS   A NZ    
336  N  N     . GLN   A 46  ? 0.3094 0.1559 0.1611 -0.0499 -0.0078 0.0184  43  GLN   A N     
337  C  CA    . GLN   A 46  ? 0.2540 0.1529 0.1945 -0.0526 -0.0155 0.0165  43  GLN   A CA    
338  C  C     . GLN   A 46  ? 0.2340 0.1582 0.1699 -0.0340 -0.0370 0.0528  43  GLN   A C     
339  O  O     . GLN   A 46  ? 0.2444 0.1646 0.1995 -0.0554 -0.0204 0.0196  43  GLN   A O     
340  C  CB    . GLN   A 46  ? 0.3139 0.2275 0.2649 0.0668  0.0016  0.0762  43  GLN   A CB    
341  C  CG    . GLN   A 46  ? 0.3280 0.3070 0.2726 0.0527  0.0086  0.0269  43  GLN   A CG    
342  C  CD    . GLN   A 46  ? 0.3016 0.3700 0.3063 0.0361  -0.0817 -0.0400 43  GLN   A CD    
343  O  OE1   . GLN   A 46  ? 0.3890 0.2570 0.2512 0.0034  -0.0436 0.0475  43  GLN   A OE1   
344  N  NE2   . GLN   A 46  ? 0.2805 0.3269 0.2948 0.0000  0.0043  0.0594  43  GLN   A NE2   
345  N  N     . VAL   A 47  ? 0.1996 0.1456 0.1656 -0.0297 -0.0430 0.0259  44  VAL   A N     
346  C  CA    . VAL   A 47  ? 0.1921 0.1725 0.1868 -0.0312 -0.0529 0.0133  44  VAL   A CA    
347  C  C     . VAL   A 47  ? 0.1747 0.1891 0.1364 -0.0127 -0.0495 -0.0239 44  VAL   A C     
348  O  O     . VAL   A 47  ? 0.2205 0.2242 0.2378 -0.0588 0.0235  -0.0796 44  VAL   A O     
349  C  CB    . VAL   A 47  ? 0.2044 0.1653 0.2548 0.0023  -0.0894 -0.0107 44  VAL   A CB    
350  C  CG1   . VAL   A 47  ? 0.2169 0.2165 0.3183 -0.0314 -0.0792 -0.0126 44  VAL   A CG1   
351  C  CG2   . VAL   A 47  ? 0.2988 0.2021 0.1975 0.0212  -0.0781 -0.0212 44  VAL   A CG2   
352  N  N     . VAL   A 48  ? 0.1790 0.1577 0.1659 -0.0309 0.0057  -0.0021 45  VAL   A N     
353  C  CA    . VAL   A 48  ? 0.1973 0.1541 0.1318 -0.0147 -0.0328 0.0039  45  VAL   A CA    
354  C  C     . VAL   A 48  ? 0.1424 0.1411 0.1320 -0.0164 -0.0300 -0.0193 45  VAL   A C     
355  O  O     . VAL   A 48  ? 0.1448 0.1735 0.1550 -0.0143 -0.0140 0.0011  45  VAL   A O     
356  C  CB    . VAL   A 48  ? 0.2393 0.1872 0.1262 0.0013  -0.0100 0.0163  45  VAL   A CB    
357  C  CG1   . VAL   A 48  ? 0.2610 0.2037 0.1121 -0.0038 -0.0263 0.0165  45  VAL   A CG1   
358  C  CG2   . VAL   A 48  ? 0.2800 0.2350 0.1443 0.0280  -0.0259 0.0391  45  VAL   A CG2   
359  N  N     . ILE   A 49  ? 0.1136 0.1488 0.1289 -0.0019 -0.0386 -0.0061 46  ILE   A N     
360  C  CA    . ILE   A 49  ? 0.1213 0.1593 0.1144 0.0026  -0.0390 -0.0042 46  ILE   A CA    
361  C  C     . ILE   A 49  ? 0.1209 0.1405 0.1090 0.0094  -0.0371 -0.0016 46  ILE   A C     
362  O  O     . ILE   A 49  ? 0.1285 0.1256 0.1215 0.0083  -0.0174 -0.0057 46  ILE   A O     
363  C  CB    . ILE   A 49  ? 0.1380 0.1591 0.1173 -0.0088 -0.0457 0.0029  46  ILE   A CB    
364  C  CG1   . ILE   A 49  ? 0.1456 0.1607 0.1329 -0.0040 -0.0650 -0.0041 46  ILE   A CG1   
365  C  CG2   . ILE   A 49  ? 0.1517 0.1637 0.1522 -0.0075 -0.0461 0.0072  46  ILE   A CG2   
366  C  CD1   . ILE   A 49  ? 0.1570 0.1615 0.1454 -0.0160 -0.0518 -0.0196 46  ILE   A CD1   
367  N  N     . ASP   A 50  ? 0.1142 0.1436 0.1031 0.0055  -0.0259 -0.0020 47  ASP   A N     
368  C  CA    . ASP   A 50  ? 0.1323 0.1477 0.0999 0.0034  -0.0198 -0.0209 47  ASP   A CA    
369  C  C     . ASP   A 50  ? 0.1270 0.1261 0.0931 0.0061  -0.0182 -0.0268 47  ASP   A C     
370  O  O     . ASP   A 50  ? 0.1325 0.1218 0.1225 0.0025  -0.0238 -0.0182 47  ASP   A O     
371  C  CB    . ASP   A 50  ? 0.1442 0.1339 0.0952 0.0052  -0.0196 -0.0275 47  ASP   A CB    
372  C  CG    . ASP   A 50  ? 0.1602 0.1376 0.1023 0.0243  -0.0130 -0.0128 47  ASP   A CG    
373  O  OD1   . ASP   A 50  ? 0.1633 0.1708 0.1308 0.0345  -0.0078 -0.0199 47  ASP   A OD1   
374  O  OD2   . ASP   A 50  ? 0.1606 0.1830 0.1038 0.0068  -0.0102 -0.0136 47  ASP   A OD2   
375  N  N     . GLY   A 51  ? 0.1406 0.1482 0.0944 -0.0026 -0.0303 -0.0056 48  GLY   A N     
376  C  CA    . GLY   A 51  ? 0.1534 0.1407 0.1201 0.0099  -0.0368 -0.0019 48  GLY   A CA    
377  C  C     . GLY   A 51  ? 0.1357 0.1282 0.1317 -0.0030 -0.0450 -0.0075 48  GLY   A C     
378  O  O     . GLY   A 51  ? 0.1540 0.1373 0.1516 0.0032  -0.0577 -0.0052 48  GLY   A O     
379  N  N     . GLU   A 52  ? 0.1466 0.1165 0.1311 0.0080  -0.0425 -0.0069 49  GLU   A N     
380  C  CA    . GLU   A 52  ? 0.1429 0.1247 0.1451 0.0050  -0.0405 -0.0056 49  GLU   A CA    
381  C  C     . GLU   A 52  ? 0.1492 0.1241 0.1396 -0.0012 -0.0519 0.0042  49  GLU   A C     
382  O  O     . GLU   A 52  ? 0.1367 0.1238 0.1497 -0.0072 -0.0494 -0.0062 49  GLU   A O     
383  C  CB    . GLU   A 52  ? 0.1430 0.1420 0.1445 -0.0099 -0.0134 -0.0359 49  GLU   A CB    
384  C  CG    . GLU   A 52  ? 0.1341 0.1712 0.1644 0.0028  -0.0286 -0.0540 49  GLU   A CG    
385  C  CD    . GLU   A 52  ? 0.1453 0.2235 0.1895 0.0442  0.0165  -0.0291 49  GLU   A CD    
386  O  OE1   . GLU   A 52  ? 0.1910 0.2128 0.1476 0.0184  -0.0019 -0.0136 49  GLU   A OE1   
387  O  OE2   . GLU   A 52  ? 0.1599 0.2755 0.2812 0.0050  0.0284  -0.0140 49  GLU   A OE2   
388  N  N     . THR   A 53  ? 0.1789 0.1227 0.1547 0.0049  -0.0755 -0.0111 50  THR   A N     
389  C  CA    . THR   A 53  ? 0.1879 0.1355 0.1563 -0.0129 -0.0660 -0.0072 50  THR   A CA    
390  C  C     . THR   A 53  ? 0.1469 0.1523 0.1771 0.0215  -0.0301 -0.0091 50  THR   A C     
391  O  O     . THR   A 53  ? 0.1768 0.1751 0.2270 -0.0009 -0.0415 -0.0427 50  THR   A O     
392  C  CB    . THR   A 53  ? 0.2350 0.1351 0.1472 -0.0165 -0.0573 0.0116  50  THR   A CB    
393  O  OG1   . THR   A 53  ? 0.2849 0.1487 0.1352 0.0036  -0.0801 0.0075  50  THR   A OG1   
394  C  CG2   . THR   A 53  ? 0.2818 0.1231 0.1884 -0.0097 -0.0770 0.0176  50  THR   A CG2   
395  N  N     . CYS   A 54  ? 0.1899 0.1551 0.1504 -0.0185 -0.0360 -0.0225 51  CYS   A N     
396  C  CA    . CYS   A 54  ? 0.2180 0.1616 0.1515 0.0335  -0.0563 -0.0211 51  CYS   A CA    
397  C  C     . CYS   A 54  ? 0.2040 0.1931 0.1805 -0.0354 -0.0128 -0.0152 51  CYS   A C     
398  O  O     . CYS   A 54  ? 0.2621 0.1470 0.2060 -0.0503 0.0364  -0.0637 51  CYS   A O     
399  C  CB    . CYS   A 54  ? 0.1081 0.1635 0.1071 0.0052  -0.0342 -0.0349 51  CYS   A CB    
400  S  SG    . CYS   A 54  ? 0.1926 0.1817 0.1613 0.0048  -0.0327 -0.0164 51  CYS   A SG    
401  N  N     . LEU   A 55  ? 0.2029 0.1384 0.1530 -0.0112 -0.0484 -0.0021 52  LEU   A N     
402  C  CA    . LEU   A 55  ? 0.2500 0.1328 0.1491 0.0105  -0.0666 -0.0006 52  LEU   A CA    
403  C  C     . LEU   A 55  ? 0.1951 0.1208 0.1277 -0.0021 -0.0337 -0.0072 52  LEU   A C     
404  O  O     . LEU   A 55  ? 0.2241 0.1626 0.1354 -0.0075 -0.0188 0.0049  52  LEU   A O     
405  C  CB    . LEU   A 55  ? 0.2705 0.1476 0.1658 0.0253  -0.0454 0.0195  52  LEU   A CB    
406  C  CG    . LEU   A 55  ? 0.3742 0.1527 0.2019 0.0380  -0.0585 0.0187  52  LEU   A CG    
407  C  CD1   . LEU   A 55  ? 0.3672 0.1115 0.2544 0.0271  -0.0705 -0.0052 52  LEU   A CD1   
408  C  CD2   . LEU   A 55  ? 0.4278 0.1564 0.3024 0.0712  -0.0091 -0.0014 52  LEU   A CD2   
409  N  N     . LEU   A 56  ? 0.2098 0.1295 0.1509 -0.0112 -0.0454 -0.0037 53  LEU   A N     
410  C  CA    . LEU   A 56  ? 0.2312 0.1113 0.1335 -0.0108 -0.0418 -0.0100 53  LEU   A CA    
411  C  C     . LEU   A 56  ? 0.2485 0.1088 0.1445 -0.0081 -0.0255 -0.0067 53  LEU   A C     
412  O  O     . LEU   A 56  ? 0.3795 0.1251 0.1546 -0.0449 -0.0132 -0.0038 53  LEU   A O     
413  C  CB    . LEU   A 56  ? 0.2229 0.1339 0.1567 -0.0076 -0.0555 -0.0105 53  LEU   A CB    
414  C  CG    . LEU   A 56  ? 0.2473 0.1629 0.1859 0.0096  -0.0535 -0.0339 53  LEU   A CG    
415  C  CD1   . LEU   A 56  ? 0.2730 0.2168 0.2304 0.0369  -0.0754 -0.0806 53  LEU   A CD1   
416  C  CD2   . LEU   A 56  ? 0.2980 0.1254 0.2183 0.0366  -0.0113 -0.0081 53  LEU   A CD2   
417  N  N     . ASP   A 57  ? 0.1950 0.1205 0.1184 -0.0024 -0.0481 -0.0076 54  ASP   A N     
418  C  CA    . ASP   A 57  ? 0.2053 0.1417 0.1393 0.0092  -0.0426 -0.0238 54  ASP   A CA    
419  C  C     . ASP   A 57  ? 0.1978 0.1262 0.1289 0.0126  -0.0405 -0.0314 54  ASP   A C     
420  O  O     . ASP   A 57  ? 0.1911 0.1349 0.1323 0.0198  -0.0495 -0.0249 54  ASP   A O     
421  C  CB    . ASP   A 57  ? 0.2296 0.2024 0.1636 0.0588  -0.0399 -0.0127 54  ASP   A CB    
422  C  CG    . ASP   A 57  ? 0.3045 0.1919 0.1587 0.0693  0.0027  0.0067  54  ASP   A CG    
423  O  OD1   . ASP   A 57  ? 0.3537 0.1988 0.2461 0.0588  -0.0173 -0.0590 54  ASP   A OD1   
424  O  OD2   . ASP   A 57  ? 0.3229 0.3126 0.2833 0.1167  -0.0057 0.0004  54  ASP   A OD2   
425  N  N     . ILE   A 58  ? 0.1990 0.1013 0.1450 0.0198  -0.0417 -0.0277 55  ILE   A N     
426  C  CA    . ILE   A 58  ? 0.2141 0.1093 0.1283 0.0160  -0.0479 -0.0160 55  ILE   A CA    
427  C  C     . ILE   A 58  ? 0.2110 0.1098 0.1570 0.0125  -0.0439 -0.0273 55  ILE   A C     
428  O  O     . ILE   A 58  ? 0.2673 0.1135 0.1318 0.0036  -0.0457 -0.0205 55  ILE   A O     
429  C  CB    . ILE   A 58  ? 0.2322 0.1051 0.1447 0.0289  -0.0493 -0.0236 55  ILE   A CB    
430  C  CG1   . ILE   A 58  ? 0.2614 0.1161 0.1411 0.0016  -0.0273 -0.0261 55  ILE   A CG1   
431  C  CG2   . ILE   A 58  ? 0.2343 0.1286 0.1822 0.0337  -0.0645 -0.0225 55  ILE   A CG2   
432  C  CD1   . ILE   A 58  ? 0.2560 0.1427 0.1534 0.0140  -0.0384 -0.0273 55  ILE   A CD1   
433  N  N     . LEU   A 59  ? 0.1909 0.1055 0.1425 0.0133  -0.0624 -0.0226 56  LEU   A N     
434  C  CA    . LEU   A 59  ? 0.1917 0.1163 0.1447 0.0083  -0.0463 -0.0357 56  LEU   A CA    
435  C  C     . LEU   A 59  ? 0.1930 0.1215 0.1380 0.0180  -0.0399 -0.0613 56  LEU   A C     
436  O  O     . LEU   A 59  ? 0.1836 0.1192 0.1608 0.0101  -0.0395 -0.0513 56  LEU   A O     
437  C  CB    . LEU   A 59  ? 0.1908 0.1452 0.1552 0.0148  -0.0478 -0.0321 56  LEU   A CB    
438  C  CG    . LEU   A 59  ? 0.2015 0.1524 0.1735 0.0284  -0.0425 -0.0473 56  LEU   A CG    
439  C  CD1   . LEU   A 59  ? 0.2531 0.1468 0.2038 0.0376  -0.0077 -0.0566 56  LEU   A CD1   
440  C  CD2   . LEU   A 59  ? 0.2120 0.2258 0.1693 0.0358  -0.0318 -0.0676 56  LEU   A CD2   
441  N  N     . ASP   A 60  ? 0.1983 0.1182 0.1427 0.0151  -0.0560 -0.0341 57  ASP   A N     
442  C  CA    . ASP   A 60  ? 0.1842 0.1206 0.1583 0.0017  -0.0431 -0.0537 57  ASP   A CA    
443  C  C     . ASP   A 60  ? 0.2311 0.1382 0.1502 -0.0035 -0.0240 -0.0341 57  ASP   A C     
444  O  O     . ASP   A 60  ? 0.2957 0.1442 0.1443 -0.0002 -0.0490 -0.0551 57  ASP   A O     
445  C  CB    . ASP   A 60  ? 0.2285 0.1592 0.1651 -0.0195 -0.0292 -0.0468 57  ASP   A CB    
446  C  CG    . ASP   A 60  ? 0.2166 0.1618 0.1812 -0.0115 -0.0155 -0.0403 57  ASP   A CG    
447  O  OD1   . ASP   A 60  ? 0.2323 0.1678 0.1793 -0.0173 -0.0579 -0.0407 57  ASP   A OD1   
448  O  OD2   . ASP   A 60  ? 0.2494 0.1838 0.1858 -0.0396 -0.0317 -0.0536 57  ASP   A OD2   
449  N  N     . THR   A 61  ? 0.2017 0.1181 0.1370 -0.0040 -0.0328 -0.0465 58  THR   A N     
450  C  CA    . THR   A 61  ? 0.1771 0.1479 0.1422 0.0197  -0.0302 -0.0485 58  THR   A CA    
451  C  C     . THR   A 61  ? 0.1612 0.1724 0.1435 0.0012  -0.0097 -0.0399 58  THR   A C     
452  O  O     . THR   A 61  ? 0.1546 0.2004 0.1507 -0.0009 -0.0271 -0.0274 58  THR   A O     
453  C  CB    . THR   A 61  ? 0.1663 0.1618 0.1237 0.0111  -0.0298 -0.0659 58  THR   A CB    
454  O  OG1   . THR   A 61  ? 0.1833 0.1631 0.1132 0.0169  -0.0293 -0.0477 58  THR   A OG1   
455  C  CG2   . THR   A 61  ? 0.1589 0.1560 0.1505 0.0131  -0.0313 -0.0724 58  THR   A CG2   
456  N  N     . ALA   A 62  ? 0.2180 0.1831 0.1485 0.0003  -0.0357 -0.0549 59  ALA   A N     
457  C  CA    . ALA   A 62  ? 0.2170 0.1947 0.1727 -0.0239 -0.0294 -0.0418 59  ALA   A CA    
458  C  C     . ALA   A 62  ? 0.1935 0.1702 0.1699 -0.0073 -0.0207 -0.0441 59  ALA   A C     
459  O  O     . ALA   A 62  ? 0.2469 0.1807 0.1810 0.0185  -0.0126 -0.0265 59  ALA   A O     
460  C  CB    . ALA   A 62  ? 0.2798 0.2088 0.1601 0.0035  -0.0379 -0.0280 59  ALA   A CB    
461  N  N     . GLY   A 63  ? 0.2369 0.2248 0.1698 0.0363  -0.0210 -0.0398 60  GLY   A N     
462  C  CA    . GLY   A 63  ? 0.2340 0.2575 0.1448 0.0281  0.0165  -0.0587 60  GLY   A CA    
463  C  C     . GLY   A 63  ? 0.2207 0.2329 0.1779 0.0488  0.0142  -0.0525 60  GLY   A C     
464  O  O     . GLY   A 63  ? 0.2152 0.2448 0.2825 0.0433  -0.0141 -0.0325 60  GLY   A O     
465  N  N     . GLN   A 64  ? 0.2403 0.2593 0.1556 0.0424  0.0105  -0.0379 61  GLN   A N     
466  C  CA    . GLN   A 64  ? 0.2347 0.2560 0.1677 0.0453  0.0339  -0.0317 61  GLN   A CA    
467  C  C     . GLN   A 64  ? 0.3021 0.2478 0.1643 0.0560  0.0472  -0.0183 61  GLN   A C     
468  O  O     . GLN   A 64  ? 0.4069 0.2608 0.2027 0.0586  0.0810  -0.0010 61  GLN   A O     
469  C  CB    . GLN   A 64  ? 0.2533 0.2734 0.1286 0.0571  0.0066  -0.0663 61  GLN   A CB    
470  C  CG    . GLN   A 64  ? 0.2223 0.2823 0.1204 0.0571  -0.0003 -0.0659 61  GLN   A CG    
471  C  CD    . GLN   A 64  ? 0.1829 0.2130 0.1334 0.0318  -0.0001 -0.0414 61  GLN   A CD    
472  O  OE1   . GLN   A 64  ? 0.1987 0.1933 0.2013 0.0430  0.0306  -0.0163 61  GLN   A OE1   
473  N  NE2   . GLN   A 64  ? 0.1935 0.2005 0.1618 0.0393  -0.0152 -0.0428 61  GLN   A NE2   
474  N  N     . GLU   A 65  ? 0.3439 0.2499 0.1956 0.0709  0.0727  -0.0060 62  GLU   A N     
475  C  CA    . GLU   A 65  ? 0.3506 0.3140 0.1987 0.0349  0.0658  -0.0477 62  GLU   A CA    
476  C  C     . GLU   A 65  ? 0.2923 0.2593 0.1593 0.0722  0.0213  -0.0420 62  GLU   A C     
477  O  O     . GLU   A 65  ? 0.3261 0.4376 0.1895 0.0839  0.0015  -0.0264 62  GLU   A O     
478  C  CB    . GLU   A 65  ? 0.4370 0.3355 0.2288 0.0347  0.1267  -0.0620 62  GLU   A CB    
479  C  CG    . GLU   A 65  ? 0.4033 0.4430 0.3090 -0.0106 0.1567  -0.1185 62  GLU   A CG    
480  C  CD    . GLU   A 65  ? 0.6450 0.5194 0.2710 -0.0848 -0.0027 -0.1499 62  GLU   A CD    
481  O  OE1   . GLU   A 65  ? 0.4734 0.5201 0.2901 -0.1092 -0.0525 0.0912  62  GLU   A OE1   
482  O  OE2   . GLU   A 65  ? 0.5707 0.4727 0.4298 -0.0177 -0.0846 -0.1001 62  GLU   A OE2   
483  N  N     . GLU   A 66  ? 0.3239 0.2974 0.2250 0.0756  0.0649  0.0094  63  GLU   A N     
484  C  CA    . GLU   A 66  ? 0.3632 0.3475 0.3104 0.0550  0.0890  -0.0371 63  GLU   A CA    
485  C  C     . GLU   A 66  ? 0.2959 0.3183 0.2542 0.0200  0.0577  -0.0499 63  GLU   A C     
486  O  O     . GLU   A 66  ? 0.3470 0.3826 0.4215 -0.0666 0.0571  -0.1036 63  GLU   A O     
487  C  CB    . GLU   A 66  ? 0.4820 0.3605 0.3742 0.0856  0.0931  0.0157  63  GLU   A CB    
488  C  CG    . GLU   A 66  ? 0.5561 0.3528 0.4509 0.0577  0.1628  -0.0396 63  GLU   A CG    
489  C  CD    . GLU   A 66  ? 0.6836 0.4158 0.4537 0.0195  0.1224  -0.1077 63  GLU   A CD    
490  O  OE1   . GLU   A 66  ? 0.7806 0.5280 0.5688 0.1392  0.1761  -0.0889 63  GLU   A OE1   
491  O  OE2   . GLU   A 66  ? 0.6715 0.6464 0.5764 -0.0528 0.0703  0.0036  63  GLU   A OE2   
492  N  N     . TYR   A 67  ? 0.2404 0.2884 0.1890 0.0466  0.0142  -0.0074 64  TYR   A N     
493  C  CA    . TYR   A 67  ? 0.2660 0.2660 0.1210 0.0482  0.0087  -0.0090 64  TYR   A CA    
494  C  C     . TYR   A 67  ? 0.2450 0.2550 0.1231 0.0261  -0.0311 -0.0073 64  TYR   A C     
495  O  O     . TYR   A 67  ? 0.2879 0.2577 0.1645 0.0216  -0.0675 -0.0267 64  TYR   A O     
496  C  CB    . TYR   A 67  ? 0.2225 0.2734 0.1258 0.0196  -0.0005 -0.0202 64  TYR   A CB    
497  C  CG    . TYR   A 67  ? 0.1884 0.2796 0.1227 0.0375  -0.0020 -0.0206 64  TYR   A CG    
498  C  CD1   . TYR   A 67  ? 0.2292 0.3161 0.1445 0.0095  -0.0038 0.0159  64  TYR   A CD1   
499  C  CD2   . TYR   A 67  ? 0.2331 0.2796 0.1185 0.0123  -0.0396 -0.0159 64  TYR   A CD2   
500  C  CE1   . TYR   A 67  ? 0.2397 0.3297 0.1834 -0.0115 -0.0239 0.0313  64  TYR   A CE1   
501  C  CE2   . TYR   A 67  ? 0.2477 0.2690 0.1517 0.0185  -0.0162 -0.0011 64  TYR   A CE2   
502  C  CZ    . TYR   A 67  ? 0.2604 0.2980 0.1364 0.0153  -0.0138 -0.0006 64  TYR   A CZ    
503  O  OH    . TYR   A 67  ? 0.3369 0.3202 0.1572 0.0599  -0.0111 0.0276  64  TYR   A OH    
504  N  N     . SER   A 68  ? 0.2235 0.2340 0.1251 0.0343  -0.0269 -0.0236 65  SER   A N     
505  C  CA    . SER   A 68  ? 0.1971 0.2199 0.1106 0.0169  -0.0180 -0.0325 65  SER   A CA    
506  C  C     . SER   A 68  ? 0.1998 0.2023 0.1348 0.0206  -0.0262 -0.0444 65  SER   A C     
507  O  O     . SER   A 68  ? 0.2357 0.2123 0.1535 0.0271  -0.0402 -0.0554 65  SER   A O     
508  C  CB    . SER   A 68  ? 0.2290 0.2336 0.1085 0.0501  -0.0096 -0.0367 65  SER   A CB    
509  O  OG    . SER   A 68  ? 0.3037 0.2304 0.1393 0.0177  -0.0465 -0.0204 65  SER   A OG    
510  N  N     . ALA   A 69  ? 0.2085 0.2172 0.1298 0.0227  -0.0200 -0.0578 66  ALA   A N     
511  C  CA    . ALA   A 69  ? 0.1972 0.2413 0.1507 0.0083  -0.0159 -0.0805 66  ALA   A CA    
512  C  C     . ALA   A 69  ? 0.2544 0.1956 0.1560 0.0288  -0.0150 -0.1039 66  ALA   A C     
513  O  O     . ALA   A 69  ? 0.2257 0.2882 0.1885 0.0531  -0.0628 -0.1302 66  ALA   A O     
514  C  CB    . ALA   A 69  ? 0.2482 0.2855 0.1508 0.0497  -0.0287 -0.1147 66  ALA   A CB    
515  N  N     . MET   A 70  ? 0.2606 0.2111 0.1378 0.0390  -0.0419 -0.0529 67  MET   A N     
516  C  CA    . MET   A 70  ? 0.2764 0.2434 0.1337 0.0585  -0.0519 -0.0710 67  MET   A CA    
517  C  C     . MET   A 70  ? 0.2216 0.2413 0.1225 0.0486  -0.0459 -0.0704 67  MET   A C     
518  O  O     . MET   A 70  ? 0.2309 0.2584 0.1298 0.0356  -0.0535 -0.0781 67  MET   A O     
519  C  CB    . MET   A 70  ? 0.3407 0.2344 0.2223 0.0466  -0.0367 -0.0642 67  MET   A CB    
520  C  CG    . MET   A 70  ? 0.4840 0.3444 0.2075 0.0572  -0.0336 -0.0911 67  MET   A CG    
521  S  SD    . MET   A 70  ? 0.6566 0.5462 0.2980 0.2321  -0.0324 -0.0283 67  MET   A SD    
522  C  CE    . MET   A 70  ? 0.5128 0.3935 0.2788 0.1556  -0.0425 -0.0142 67  MET   A CE    
523  N  N     . ARG   A 71  ? 0.2017 0.2102 0.1354 0.0315  -0.0472 -0.0791 68  ARG   A N     
524  C  CA    . ARG   A 71  ? 0.1815 0.2238 0.1560 0.0362  -0.0132 -0.0868 68  ARG   A CA    
525  C  C     . ARG   A 71  ? 0.1652 0.2356 0.1142 0.0475  -0.0254 -0.0798 68  ARG   A C     
526  O  O     . ARG   A 71  ? 0.1693 0.2450 0.1553 0.0365  -0.0125 -0.0964 68  ARG   A O     
527  C  CB    . ARG   A 71  ? 0.1877 0.2418 0.1877 0.0239  -0.0359 -0.1090 68  ARG   A CB    
528  C  CG    . ARG   A 71  ? 0.2462 0.2431 0.2368 0.0362  -0.0391 -0.1012 68  ARG   A CG    
529  C  CD    . ARG   A 71  ? 0.2724 0.3157 0.3291 0.0421  -0.0665 -0.0811 68  ARG   A CD    
530  N  NE    . ARG   A 71  ? 0.2745 0.3427 0.3392 0.0329  -0.0638 -0.0592 68  ARG   A NE    
531  C  CZ    . ARG   A 71  ? 0.3030 0.2438 0.3937 0.0514  -0.0735 -0.0588 68  ARG   A CZ    
532  N  NH1   . ARG   A 71  ? 0.2138 0.2522 0.4245 0.0041  -0.0543 -0.0548 68  ARG   A NH1   
533  N  NH2   . ARG   A 71  ? 0.4789 0.2399 0.4359 0.0332  -0.0845 -0.0299 68  ARG   A NH2   
534  N  N     . ASP   A 72  ? 0.1758 0.2414 0.1190 0.0343  -0.0166 -0.0887 69  ASP   A N     
535  C  CA    . ASP   A 72  ? 0.1886 0.2620 0.1689 0.0216  -0.0070 -0.0663 69  ASP   A CA    
536  C  C     . ASP   A 72  ? 0.1435 0.2268 0.1852 0.0224  -0.0062 -0.0758 69  ASP   A C     
537  O  O     . ASP   A 72  ? 0.1799 0.2889 0.1714 0.0060  -0.0236 -0.1028 69  ASP   A O     
538  C  CB    . ASP   A 72  ? 0.2525 0.2747 0.1814 0.0279  0.0207  -0.0566 69  ASP   A CB    
539  C  CG    . ASP   A 72  ? 0.3744 0.3394 0.2004 0.0097  -0.0100 -0.0257 69  ASP   A CG    
540  O  OD1   . ASP   A 72  ? 0.3861 0.4855 0.2313 0.0704  -0.0020 -0.0339 69  ASP   A OD1   
541  O  OD2   . ASP   A 72  ? 0.4613 0.5476 0.2340 0.0335  0.0602  -0.0479 69  ASP   A OD2   
542  N  N     A GLN   A 73  ? 0.2035 0.2252 0.1510 0.0347  -0.0384 -0.0958 70  GLN   A N     
543  N  N     B GLN   A 73  ? 0.2057 0.2231 0.1582 0.0357  -0.0370 -0.0956 70  GLN   A N     
544  C  CA    A GLN   A 73  ? 0.1675 0.2707 0.1789 0.0347  -0.0542 -0.1081 70  GLN   A CA    
545  C  CA    B GLN   A 73  ? 0.1794 0.2578 0.1856 0.0399  -0.0542 -0.1047 70  GLN   A CA    
546  C  C     A GLN   A 73  ? 0.1773 0.2740 0.1597 0.0368  -0.0591 -0.0955 70  GLN   A C     
547  C  C     B GLN   A 73  ? 0.1787 0.2703 0.1713 0.0410  -0.0524 -0.0930 70  GLN   A C     
548  O  O     A GLN   A 73  ? 0.1927 0.2832 0.1536 0.0183  -0.0508 -0.0993 70  GLN   A O     
549  O  O     B GLN   A 73  ? 0.1773 0.2657 0.1904 0.0313  -0.0373 -0.1108 70  GLN   A O     
550  C  CB    A GLN   A 73  ? 0.2159 0.2751 0.1853 0.0551  -0.0565 -0.1116 70  GLN   A CB    
551  C  CB    B GLN   A 73  ? 0.2389 0.2600 0.1974 0.0615  -0.0584 -0.1011 70  GLN   A CB    
552  C  CG    A GLN   A 73  ? 0.2423 0.3452 0.2081 0.0722  -0.0696 -0.1035 70  GLN   A CG    
553  C  CG    B GLN   A 73  ? 0.2539 0.2913 0.2291 0.0847  -0.0689 -0.0959 70  GLN   A CG    
554  C  CD    A GLN   A 73  ? 0.1951 0.4032 0.2284 0.0989  -0.0528 -0.1012 70  GLN   A CD    
555  C  CD    B GLN   A 73  ? 0.3116 0.3000 0.2547 0.1105  -0.0097 -0.0955 70  GLN   A CD    
556  O  OE1   A GLN   A 73  ? 0.2338 0.4846 0.2458 0.1025  -0.0354 -0.1159 70  GLN   A OE1   
557  O  OE1   B GLN   A 73  ? 0.2978 0.3316 0.2903 0.1032  0.0340  -0.0456 70  GLN   A OE1   
558  N  NE2   A GLN   A 73  ? 0.2188 0.3853 0.2476 0.0877  -0.0257 -0.1138 70  GLN   A NE2   
559  N  NE2   B GLN   A 73  ? 0.3349 0.3165 0.3360 0.0526  0.0122  -0.0905 70  GLN   A NE2   
560  N  N     . TYR   A 74  ? 0.1998 0.2543 0.1393 0.0189  -0.0356 -0.1004 71  TYR   A N     
561  C  CA    . TYR   A 74  ? 0.1873 0.2708 0.1453 0.0083  -0.0212 -0.0988 71  TYR   A CA    
562  C  C     . TYR   A 74  ? 0.1770 0.2648 0.1492 0.0052  -0.0046 -0.0911 71  TYR   A C     
563  O  O     . TYR   A 74  ? 0.1684 0.2736 0.1686 0.0061  -0.0060 -0.1183 71  TYR   A O     
564  C  CB    . TYR   A 74  ? 0.2215 0.2548 0.1606 -0.0114 0.0021  -0.1051 71  TYR   A CB    
565  C  CG    . TYR   A 74  ? 0.2293 0.2802 0.1539 -0.0178 0.0000  -0.1015 71  TYR   A CG    
566  C  CD1   . TYR   A 74  ? 0.2120 0.2697 0.1825 -0.0236 -0.0232 -0.1249 71  TYR   A CD1   
567  C  CD2   . TYR   A 74  ? 0.2045 0.2707 0.1915 -0.0145 0.0136  -0.1122 71  TYR   A CD2   
568  C  CE1   . TYR   A 74  ? 0.1878 0.2437 0.2033 0.0001  -0.0013 -0.1319 71  TYR   A CE1   
569  C  CE2   . TYR   A 74  ? 0.2224 0.2703 0.1805 -0.0237 -0.0024 -0.1072 71  TYR   A CE2   
570  C  CZ    . TYR   A 74  ? 0.1624 0.2774 0.1964 -0.0217 -0.0139 -0.1274 71  TYR   A CZ    
571  O  OH    . TYR   A 74  ? 0.1849 0.2643 0.2278 -0.0054 -0.0318 -0.0852 71  TYR   A OH    
572  N  N     . MET   A 75  ? 0.1381 0.2370 0.1493 0.0116  -0.0195 -0.0959 72  MET   A N     
573  C  CA    . MET   A 75  ? 0.1494 0.2334 0.1927 0.0404  -0.0204 -0.0953 72  MET   A CA    
574  C  C     . MET   A 75  ? 0.1533 0.2440 0.1873 0.0361  -0.0150 -0.1077 72  MET   A C     
575  O  O     . MET   A 75  ? 0.1742 0.2560 0.2386 0.0552  -0.0495 -0.1349 72  MET   A O     
576  C  CB    . MET   A 75  ? 0.1318 0.2608 0.1685 0.0365  0.0010  -0.0865 72  MET   A CB    
577  C  CG    . MET   A 75  ? 0.1353 0.2642 0.2006 0.0114  -0.0003 -0.0774 72  MET   A CG    
578  S  SD    . MET   A 75  ? 0.1760 0.3005 0.2056 0.0363  -0.0323 -0.0984 72  MET   A SD    
579  C  CE    . MET   A 75  ? 0.1924 0.2622 0.2708 0.0147  -0.0324 -0.0798 72  MET   A CE    
580  N  N     . ARG   A 76  ? 0.1386 0.2411 0.1740 0.0191  -0.0071 -0.1061 73  ARG   A N     
581  C  CA    . ARG   A 76  ? 0.1352 0.2533 0.1945 0.0181  -0.0072 -0.0960 73  ARG   A CA    
582  C  C     . ARG   A 76  ? 0.1604 0.2087 0.2056 0.0420  -0.0150 -0.0989 73  ARG   A C     
583  O  O     . ARG   A 76  ? 0.1623 0.2765 0.2011 0.0101  -0.0386 -0.0963 73  ARG   A O     
584  C  CB    . ARG   A 76  ? 0.1643 0.2939 0.2022 0.0427  -0.0058 -0.1044 73  ARG   A CB    
585  C  CG    . ARG   A 76  ? 0.1903 0.3567 0.2035 0.0343  -0.0093 -0.0937 73  ARG   A CG    
586  C  CD    . ARG   A 76  ? 0.2063 0.4397 0.2359 0.0538  0.0153  -0.1067 73  ARG   A CD    
587  N  NE    . ARG   A 76  ? 0.2668 0.4802 0.3180 -0.0275 0.0417  -0.0902 73  ARG   A NE    
588  C  CZ    . ARG   A 76  ? 0.2938 0.4901 0.2996 -0.0334 0.0919  -0.1236 73  ARG   A CZ    
589  N  NH1   . ARG   A 76  ? 0.3796 0.5761 0.3281 0.0285  0.0995  -0.1136 73  ARG   A NH1   
590  N  NH2   . ARG   A 76  ? 0.2722 0.4889 0.4125 -0.0602 0.0389  -0.1765 73  ARG   A NH2   
591  N  N     . THR   A 77  ? 0.1417 0.2170 0.1494 0.0242  -0.0112 -0.0931 74  THR   A N     
592  C  CA    . THR   A 77  ? 0.1686 0.2369 0.1599 0.0496  -0.0406 -0.1072 74  THR   A CA    
593  C  C     . THR   A 77  ? 0.1657 0.2210 0.1392 0.0508  -0.0315 -0.0756 74  THR   A C     
594  O  O     . THR   A 77  ? 0.1639 0.2421 0.1728 0.0536  -0.0458 -0.1139 74  THR   A O     
595  C  CB    . THR   A 77  ? 0.1839 0.2453 0.1924 0.0484  -0.0262 -0.0973 74  THR   A CB    
596  O  OG1   . THR   A 77  ? 0.2231 0.2879 0.2328 0.0850  -0.0036 -0.1046 74  THR   A OG1   
597  C  CG2   . THR   A 77  ? 0.2606 0.2329 0.2139 0.0458  -0.0429 -0.0635 74  THR   A CG2   
598  N  N     . GLY   A 78  ? 0.1482 0.2115 0.1509 0.0392  -0.0248 -0.0967 75  GLY   A N     
599  C  CA    . GLY   A 78  ? 0.1262 0.1886 0.1467 0.0268  -0.0082 -0.0656 75  GLY   A CA    
600  C  C     . GLY   A 78  ? 0.1231 0.2009 0.1346 0.0106  -0.0187 -0.0618 75  GLY   A C     
601  O  O     . GLY   A 78  ? 0.1778 0.2382 0.1419 -0.0044 0.0098  -0.0778 75  GLY   A O     
602  N  N     . GLU   A 79  ? 0.1123 0.1732 0.1352 0.0166  -0.0268 -0.0561 76  GLU   A N     
603  C  CA    . GLU   A 79  ? 0.1045 0.1601 0.1260 0.0235  -0.0141 -0.0557 76  GLU   A CA    
604  C  C     . GLU   A 79  ? 0.1072 0.1461 0.1257 0.0201  -0.0082 -0.0558 76  GLU   A C     
605  O  O     . GLU   A 79  ? 0.1040 0.1621 0.1704 0.0061  0.0082  -0.0269 76  GLU   A O     
606  C  CB    . GLU   A 79  ? 0.1182 0.1601 0.1396 0.0099  -0.0362 -0.0526 76  GLU   A CB    
607  C  CG    . GLU   A 79  ? 0.1398 0.2157 0.1812 0.0336  -0.0197 -0.0605 76  GLU   A CG    
608  C  CD    . GLU   A 79  ? 0.1723 0.2883 0.2043 0.0291  -0.0388 -0.0021 76  GLU   A CD    
609  O  OE1   . GLU   A 79  ? 0.1663 0.2685 0.2011 -0.0308 -0.0644 -0.0016 76  GLU   A OE1   
610  O  OE2   . GLU   A 79  ? 0.2073 0.4852 0.2020 -0.0631 -0.0374 -0.0044 76  GLU   A OE2   
611  N  N     . GLY   A 80  ? 0.1063 0.1396 0.1053 0.0195  -0.0235 -0.0306 77  GLY   A N     
612  C  CA    . GLY   A 80  ? 0.0963 0.1398 0.0932 0.0119  -0.0112 -0.0185 77  GLY   A CA    
613  C  C     . GLY   A 80  ? 0.1007 0.1286 0.0942 0.0173  -0.0139 -0.0271 77  GLY   A C     
614  O  O     . GLY   A 80  ? 0.1070 0.1272 0.1116 0.0159  -0.0300 -0.0205 77  GLY   A O     
615  N  N     . PHE   A 81  ? 0.0995 0.1260 0.0901 0.0209  -0.0149 -0.0397 78  PHE   A N     
616  C  CA    . PHE   A 81  ? 0.1065 0.1298 0.0951 0.0143  -0.0215 -0.0360 78  PHE   A CA    
617  C  C     . PHE   A 81  ? 0.0947 0.1295 0.0967 0.0022  -0.0202 -0.0241 78  PHE   A C     
618  O  O     . PHE   A 81  ? 0.1025 0.1313 0.1319 0.0062  -0.0036 -0.0137 78  PHE   A O     
619  C  CB    . PHE   A 81  ? 0.1143 0.1628 0.0934 0.0179  -0.0307 -0.0264 78  PHE   A CB    
620  C  CG    . PHE   A 81  ? 0.1190 0.1704 0.0882 0.0113  -0.0100 -0.0307 78  PHE   A CG    
621  C  CD1   . PHE   A 81  ? 0.1305 0.1655 0.1047 0.0050  -0.0038 -0.0347 78  PHE   A CD1   
622  C  CD2   . PHE   A 81  ? 0.1201 0.1911 0.1000 0.0063  -0.0159 -0.0514 78  PHE   A CD2   
623  C  CE1   . PHE   A 81  ? 0.1330 0.1862 0.1123 0.0051  0.0025  -0.0372 78  PHE   A CE1   
624  C  CE2   . PHE   A 81  ? 0.1616 0.1814 0.1210 0.0392  -0.0135 -0.0496 78  PHE   A CE2   
625  C  CZ    . PHE   A 81  ? 0.1487 0.1958 0.1197 0.0430  -0.0027 -0.0567 78  PHE   A CZ    
626  N  N     . LEU   A 82  ? 0.1071 0.1186 0.0939 0.0038  -0.0141 -0.0183 79  LEU   A N     
627  C  CA    . LEU   A 82  ? 0.1180 0.1112 0.1020 -0.0007 -0.0082 -0.0277 79  LEU   A CA    
628  C  C     . LEU   A 82  ? 0.1109 0.1128 0.1113 0.0068  -0.0136 -0.0305 79  LEU   A C     
629  O  O     . LEU   A 82  ? 0.1356 0.1242 0.1528 0.0071  -0.0430 -0.0440 79  LEU   A O     
630  C  CB    . LEU   A 82  ? 0.2057 0.1554 0.1250 -0.0490 0.0226  -0.0249 79  LEU   A CB    
631  C  CG    . LEU   A 82  ? 0.2891 0.1465 0.1330 -0.0224 0.0379  -0.0241 79  LEU   A CG    
632  C  CD1   . LEU   A 82  ? 0.2707 0.1421 0.0914 0.0456  -0.0090 -0.0435 79  LEU   A CD1   
633  C  CD2   . LEU   A 82  ? 0.2666 0.1496 0.1766 -0.0141 0.0774  -0.0295 79  LEU   A CD2   
634  N  N     . CYS   A 83  ? 0.0976 0.1337 0.1176 0.0109  -0.0071 -0.0205 80  CYS   A N     
635  C  CA    . CYS   A 83  ? 0.0997 0.1343 0.1119 0.0163  -0.0006 -0.0136 80  CYS   A CA    
636  C  C     . CYS   A 83  ? 0.0914 0.1266 0.1023 0.0040  -0.0022 -0.0107 80  CYS   A C     
637  O  O     . CYS   A 83  ? 0.1147 0.1344 0.1078 0.0071  -0.0004 -0.0306 80  CYS   A O     
638  C  CB    . CYS   A 83  ? 0.1084 0.1911 0.1238 -0.0040 0.0045  0.0047  80  CYS   A CB    
639  S  SG    . CYS   A 83  ? 0.1312 0.2502 0.2209 0.0036  0.0376  -0.0005 80  CYS   A SG    
640  N  N     . VAL   A 84  ? 0.0899 0.1329 0.0960 0.0050  -0.0205 -0.0222 81  VAL   A N     
641  C  CA    . VAL   A 84  ? 0.0851 0.1275 0.0973 0.0173  -0.0119 -0.0268 81  VAL   A CA    
642  C  C     . VAL   A 84  ? 0.0922 0.1428 0.0798 -0.0004 -0.0052 -0.0335 81  VAL   A C     
643  O  O     . VAL   A 84  ? 0.1063 0.1495 0.0733 0.0050  -0.0132 -0.0257 81  VAL   A O     
644  C  CB    . VAL   A 84  ? 0.1032 0.1323 0.0967 0.0004  -0.0220 -0.0328 81  VAL   A CB    
645  C  CG1   . VAL   A 84  ? 0.1022 0.1332 0.0899 0.0037  -0.0213 -0.0195 81  VAL   A CG1   
646  C  CG2   . VAL   A 84  ? 0.1168 0.1313 0.1084 -0.0052 -0.0240 -0.0031 81  VAL   A CG2   
647  N  N     . PHE   A 85  ? 0.0902 0.1453 0.0729 0.0061  -0.0081 -0.0265 82  PHE   A N     
648  C  CA    . PHE   A 85  ? 0.0905 0.1522 0.0733 -0.0019 -0.0102 -0.0238 82  PHE   A CA    
649  C  C     . PHE   A 85  ? 0.0961 0.1414 0.0736 0.0003  -0.0080 -0.0154 82  PHE   A C     
650  O  O     . PHE   A 85  ? 0.1000 0.1813 0.0786 -0.0027 -0.0071 -0.0198 82  PHE   A O     
651  C  CB    . PHE   A 85  ? 0.0869 0.1716 0.0890 0.0000  -0.0104 0.0003  82  PHE   A CB    
652  C  CG    . PHE   A 85  ? 0.0915 0.1615 0.0845 0.0006  0.0002  0.0160  82  PHE   A CG    
653  C  CD1   . PHE   A 85  ? 0.0873 0.1513 0.1000 0.0017  0.0086  0.0155  82  PHE   A CD1   
654  C  CD2   . PHE   A 85  ? 0.0886 0.1628 0.0859 0.0005  0.0059  0.0058  82  PHE   A CD2   
655  C  CE1   . PHE   A 85  ? 0.1146 0.1520 0.0981 -0.0091 0.0120  0.0134  82  PHE   A CE1   
656  C  CE2   . PHE   A 85  ? 0.1041 0.1623 0.0845 0.0103  0.0071  0.0194  82  PHE   A CE2   
657  C  CZ    . PHE   A 85  ? 0.1241 0.1585 0.0842 0.0123  0.0041  0.0113  82  PHE   A CZ    
658  N  N     . ALA   A 86  ? 0.1022 0.1728 0.0777 -0.0121 -0.0136 -0.0086 83  ALA   A N     
659  C  CA    . ALA   A 86  ? 0.1037 0.1740 0.0812 -0.0085 -0.0100 0.0015  83  ALA   A CA    
660  C  C     . ALA   A 86  ? 0.0837 0.1867 0.0853 0.0002  -0.0005 -0.0081 83  ALA   A C     
661  O  O     . ALA   A 86  ? 0.0975 0.2150 0.0833 0.0078  -0.0041 -0.0071 83  ALA   A O     
662  C  CB    . ALA   A 86  ? 0.1225 0.1778 0.1054 -0.0184 0.0084  -0.0144 83  ALA   A CB    
663  N  N     . ILE   A 87  ? 0.0892 0.1840 0.0958 0.0001  0.0105  -0.0033 84  ILE   A N     
664  C  CA    . ILE   A 87  ? 0.1056 0.1909 0.0845 0.0060  0.0052  0.0012  84  ILE   A CA    
665  C  C     . ILE   A 87  ? 0.1170 0.2056 0.0899 0.0085  -0.0001 0.0084  84  ILE   A C     
666  O  O     . ILE   A 87  ? 0.1140 0.2123 0.1111 0.0033  -0.0062 0.0238  84  ILE   A O     
667  C  CB    . ILE   A 87  ? 0.1188 0.1947 0.0958 0.0218  0.0067  -0.0002 84  ILE   A CB    
668  C  CG1   . ILE   A 87  ? 0.1202 0.2485 0.1005 0.0062  0.0178  0.0036  84  ILE   A CG1   
669  C  CG2   . ILE   A 87  ? 0.1395 0.1724 0.1037 0.0031  -0.0034 -0.0057 84  ILE   A CG2   
670  C  CD1   . ILE   A 87  ? 0.1638 0.2546 0.1271 0.0310  0.0327  0.0114  84  ILE   A CD1   
671  N  N     . ASN   A 88  ? 0.1050 0.2218 0.1050 -0.0031 0.0006  0.0018  85  ASN   A N     
672  C  CA    . ASN   A 88  ? 0.1094 0.2397 0.1300 -0.0077 -0.0109 -0.0049 85  ASN   A CA    
673  C  C     . ASN   A 88  ? 0.1167 0.2660 0.1197 -0.0029 -0.0310 -0.0100 85  ASN   A C     
674  O  O     . ASN   A 88  ? 0.1473 0.2994 0.1533 -0.0268 -0.0400 -0.0229 85  ASN   A O     
675  C  CB    . ASN   A 88  ? 0.0920 0.2440 0.1426 -0.0098 -0.0011 -0.0180 85  ASN   A CB    
676  C  CG    . ASN   A 88  ? 0.1244 0.2436 0.1353 -0.0202 -0.0393 -0.0435 85  ASN   A CG    
677  O  OD1   . ASN   A 88  ? 0.1147 0.2417 0.1381 -0.0152 -0.0238 -0.0113 85  ASN   A OD1   
678  N  ND2   . ASN   A 88  ? 0.1393 0.2466 0.1878 -0.0253 -0.0061 -0.0303 85  ASN   A ND2   
679  N  N     . ASN   A 89  ? 0.1200 0.2458 0.1112 -0.0086 -0.0251 -0.0103 86  ASN   A N     
680  C  CA    . ASN   A 89  ? 0.1607 0.2382 0.0980 -0.0198 -0.0350 -0.0220 86  ASN   A CA    
681  C  C     . ASN   A 89  ? 0.1375 0.2554 0.0935 0.0008  -0.0219 0.0064  86  ASN   A C     
682  O  O     . ASN   A 89  ? 0.1399 0.2445 0.0918 0.0145  -0.0164 -0.0017 86  ASN   A O     
683  C  CB    . ASN   A 89  ? 0.2454 0.2312 0.0867 -0.0271 -0.0181 -0.0122 86  ASN   A CB    
684  C  CG    . ASN   A 89  ? 0.2993 0.2580 0.1761 -0.0233 0.0304  -0.0423 86  ASN   A CG    
685  O  OD1   . ASN   A 89  ? 0.2128 0.3287 0.1186 -0.0479 0.0151  -0.0580 86  ASN   A OD1   
686  N  ND2   . ASN   A 89  ? 0.2869 0.2882 0.3200 -0.0069 -0.0094 0.0000  86  ASN   A ND2   
687  N  N     . THR   A 90  ? 0.1493 0.2674 0.0991 -0.0120 -0.0484 0.0040  87  THR   A N     
688  C  CA    . THR   A 90  ? 0.1699 0.2839 0.1170 -0.0155 -0.0261 0.0181  87  THR   A CA    
689  C  C     . THR   A 90  ? 0.1724 0.2907 0.0656 -0.0429 -0.0204 0.0180  87  THR   A C     
690  O  O     . THR   A 90  ? 0.1515 0.2580 0.1196 -0.0084 -0.0264 0.0423  87  THR   A O     
691  C  CB    . THR   A 90  ? 0.1761 0.3126 0.1625 0.0247  -0.0053 0.0364  87  THR   A CB    
692  O  OG1   . THR   A 90  ? 0.2007 0.3876 0.1886 0.0761  0.0007  0.0415  87  THR   A OG1   
693  C  CG2   . THR   A 90  ? 0.1991 0.3167 0.2224 -0.0024 0.0180  0.0273  87  THR   A CG2   
694  N  N     . LYS   A 91  ? 0.1459 0.2931 0.0935 -0.0135 -0.0321 0.0008  88  LYS   A N     
695  C  CA    . LYS   A 91  ? 0.1610 0.3388 0.0827 -0.0075 -0.0174 0.0049  88  LYS   A CA    
696  C  C     . LYS   A 91  ? 0.1613 0.2955 0.0581 -0.0207 -0.0194 -0.0043 88  LYS   A C     
697  O  O     . LYS   A 91  ? 0.1683 0.2954 0.0827 -0.0059 -0.0007 -0.0115 88  LYS   A O     
698  C  CB    . LYS   A 91  ? 0.1696 0.3897 0.0957 -0.0048 -0.0350 -0.0295 88  LYS   A CB    
699  C  CG    . LYS   A 91  ? 0.2547 0.4658 0.2114 0.0357  -0.0064 -0.0772 88  LYS   A CG    
700  C  CD    . LYS   A 91  ? 0.3876 0.5254 0.2621 0.0356  0.0262  -0.0464 88  LYS   A CD    
701  C  CE    . LYS   A 91  ? 0.4333 0.5673 0.3129 0.0404  0.0167  -0.1251 88  LYS   A CE    
702  N  NZ    . LYS   A 91  ? 0.4398 0.5731 0.3597 0.0380  0.0260  -0.1372 88  LYS   A NZ    
703  N  N     . SER   A 92  ? 0.1521 0.2550 0.0669 0.0063  -0.0134 -0.0005 89  SER   A N     
704  C  CA    . SER   A 92  ? 0.1422 0.2387 0.0643 0.0248  -0.0032 -0.0137 89  SER   A CA    
705  C  C     . SER   A 92  ? 0.1448 0.2214 0.0656 0.0152  -0.0183 -0.0036 89  SER   A C     
706  O  O     . SER   A 92  ? 0.1331 0.2321 0.0879 0.0162  0.0031  -0.0160 89  SER   A O     
707  C  CB    . SER   A 92  ? 0.1617 0.2353 0.0715 0.0072  -0.0064 -0.0160 89  SER   A CB    
708  O  OG    . SER   A 92  ? 0.1349 0.2455 0.0719 -0.0148 -0.0003 -0.0242 89  SER   A OG    
709  N  N     . PHE   A 93  ? 0.1214 0.2158 0.0941 0.0066  -0.0050 0.0131  90  PHE   A N     
710  C  CA    . PHE   A 93  ? 0.1226 0.2213 0.0975 -0.0010 -0.0077 0.0317  90  PHE   A CA    
711  C  C     . PHE   A 93  ? 0.1281 0.2801 0.0895 0.0075  -0.0024 0.0281  90  PHE   A C     
712  O  O     . PHE   A 93  ? 0.1183 0.2811 0.1094 0.0033  0.0101  0.0267  90  PHE   A O     
713  C  CB    . PHE   A 93  ? 0.1347 0.2107 0.0877 0.0146  -0.0151 0.0488  90  PHE   A CB    
714  C  CG    . PHE   A 93  ? 0.1399 0.2077 0.1051 0.0108  -0.0066 0.0329  90  PHE   A CG    
715  C  CD1   . PHE   A 93  ? 0.1174 0.1984 0.0884 0.0219  0.0036  0.0433  90  PHE   A CD1   
716  C  CD2   . PHE   A 93  ? 0.1771 0.2260 0.1059 -0.0026 -0.0391 0.0478  90  PHE   A CD2   
717  C  CE1   . PHE   A 93  ? 0.1497 0.2118 0.1198 -0.0157 0.0030  0.0368  90  PHE   A CE1   
718  C  CE2   . PHE   A 93  ? 0.2354 0.2259 0.1257 -0.0085 -0.0270 0.0426  90  PHE   A CE2   
719  C  CZ    . PHE   A 93  ? 0.1767 0.2021 0.1302 -0.0147 -0.0094 0.0300  90  PHE   A CZ    
720  N  N     . GLU   A 94  ? 0.1670 0.3140 0.0960 -0.0203 -0.0137 0.0508  91  GLU   A N     
721  C  CA    . GLU   A 94  ? 0.2044 0.3530 0.0984 -0.0233 -0.0104 0.0731  91  GLU   A CA    
722  C  C     . GLU   A 94  ? 0.1873 0.3561 0.1191 -0.0259 0.0324  0.0261  91  GLU   A C     
723  O  O     . GLU   A 94  ? 0.2544 0.4448 0.1750 -0.0338 0.1025  0.0358  91  GLU   A O     
724  C  CB    . GLU   A 94  ? 0.2376 0.3666 0.1083 0.0004  -0.0296 0.0630  91  GLU   A CB    
725  C  CG    . GLU   A 94  ? 0.2273 0.3279 0.1616 -0.0173 0.0085  0.0831  91  GLU   A CG    
726  C  CD    . GLU   A 94  ? 0.2879 0.3854 0.2205 0.0534  -0.0511 0.1145  91  GLU   A CD    
727  O  OE1   . GLU   A 94  ? 0.5121 0.5106 0.2699 0.0772  -0.0517 0.0340  91  GLU   A OE1   
728  O  OE2   . GLU   A 94  ? 0.2527 0.2900 0.1778 0.0089  -0.0288 0.1036  91  GLU   A OE2   
729  N  N     . ASP   A 95  ? 0.2079 0.3449 0.1034 -0.0406 0.0289  -0.0262 92  ASP   A N     
730  C  CA    . ASP   A 95  ? 0.2034 0.3590 0.1310 -0.0273 0.0533  -0.0327 92  ASP   A CA    
731  C  C     . ASP   A 95  ? 0.1739 0.2846 0.1023 0.0022  0.0575  -0.0320 92  ASP   A C     
732  O  O     . ASP   A 95  ? 0.1957 0.2903 0.1166 0.0139  0.0544  -0.0121 92  ASP   A O     
733  C  CB    . ASP   A 95  ? 0.2462 0.3285 0.1984 0.0046  0.1044  -0.0527 92  ASP   A CB    
734  C  CG    . ASP   A 95  ? 0.3758 0.3938 0.2256 -0.0660 0.0876  -0.0879 92  ASP   A CG    
735  O  OD1   . ASP   A 95  ? 0.3994 0.4544 0.2053 -0.0311 0.1006  -0.1091 92  ASP   A OD1   
736  O  OD2   . ASP   A 95  ? 0.5194 0.3459 0.2770 -0.0574 0.0852  -0.0360 92  ASP   A OD2   
737  N  N     . ILE   A 96  ? 0.1493 0.2849 0.1083 0.0009  0.0344  -0.0323 93  ILE   A N     
738  C  CA    . ILE   A 96  ? 0.1542 0.2733 0.1195 0.0028  0.0276  -0.0286 93  ILE   A CA    
739  C  C     . ILE   A 96  ? 0.1380 0.2860 0.0877 0.0375  0.0142  0.0067  93  ILE   A C     
740  O  O     . ILE   A 96  ? 0.1421 0.2807 0.1153 0.0407  0.0167  -0.0018 93  ILE   A O     
741  C  CB    . ILE   A 96  ? 0.1494 0.2685 0.0852 0.0160  0.0254  -0.0052 93  ILE   A CB    
742  C  CG1   . ILE   A 96  ? 0.1474 0.2363 0.0843 0.0021  0.0106  -0.0206 93  ILE   A CG1   
743  C  CG2   . ILE   A 96  ? 0.1421 0.2429 0.1228 -0.0011 0.0314  0.0171  93  ILE   A CG2   
744  C  CD1   . ILE   A 96  ? 0.1459 0.2390 0.1172 -0.0127 0.0129  0.0058  93  ILE   A CD1   
745  N  N     . HIS   A 97  ? 0.1313 0.2850 0.1020 0.0376  0.0191  0.0094  94  HIS   A N     
746  C  CA    . HIS   A 97  ? 0.1275 0.2791 0.1390 0.0269  0.0100  0.0174  94  HIS   A CA    
747  C  C     . HIS   A 97  ? 0.1419 0.3019 0.1107 0.0322  0.0420  0.0303  94  HIS   A C     
748  O  O     . HIS   A 97  ? 0.1515 0.3256 0.1289 0.0353  0.0248  0.0187  94  HIS   A O     
749  C  CB    . HIS   A 97  ? 0.2189 0.3222 0.2011 0.0683  0.0002  0.0620  94  HIS   A CB    
750  C  CG    . HIS   A 97  ? 0.2696 0.4260 0.3665 0.0513  0.0296  0.1320  94  HIS   A CG    
751  N  ND1   . HIS   A 97  ? 0.3448 0.4795 0.5013 -0.0130 0.0391  0.1468  94  HIS   A ND1   
752  C  CD2   . HIS   A 97  ? 0.4124 0.4497 0.3482 0.0673  0.0295  0.1644  94  HIS   A CD2   
753  C  CE1   . HIS   A 97  ? 0.3896 0.5035 0.4765 -0.0783 0.0046  0.2044  94  HIS   A CE1   
754  N  NE2   . HIS   A 97  ? 0.3800 0.5789 0.4002 0.0094  0.0430  0.2171  94  HIS   A NE2   
755  N  N     . HIS   A 98  ? 0.1645 0.2721 0.1006 0.0377  0.0085  0.0319  95  HIS   A N     
756  C  CA    . HIS   A 98  ? 0.1750 0.3148 0.0920 0.0333  0.0196  0.0059  95  HIS   A CA    
757  C  C     . HIS   A 98  ? 0.1627 0.3090 0.0891 0.0382  0.0151  -0.0150 95  HIS   A C     
758  O  O     . HIS   A 98  ? 0.1621 0.3251 0.1309 0.0433  0.0375  0.0100  95  HIS   A O     
759  C  CB    . HIS   A 98  ? 0.2209 0.3543 0.1444 0.0229  0.0132  -0.0290 95  HIS   A CB    
760  C  CG    . HIS   A 98  ? 0.3085 0.4225 0.1400 0.0519  0.0214  -0.0162 95  HIS   A CG    
761  N  ND1   . HIS   A 98  ? 0.3126 0.5794 0.1561 0.0472  0.0037  0.0438  95  HIS   A ND1   
762  C  CD2   . HIS   A 98  ? 0.3301 0.5689 0.2050 0.0575  0.0247  0.0302  95  HIS   A CD2   
763  C  CE1   . HIS   A 98  ? 0.3006 0.6182 0.1857 0.0260  -0.0153 0.0632  95  HIS   A CE1   
764  N  NE2   . HIS   A 98  ? 0.2738 0.6310 0.1960 0.0613  -0.0382 0.0287  95  HIS   A NE2   
765  N  N     A TYR   A 99  ? 0.1474 0.3038 0.1115 0.0529  0.0206  0.0062  96  TYR   A N     
766  N  N     B TYR   A 99  ? 0.1630 0.2996 0.1110 0.0448  0.0303  -0.0044 96  TYR   A N     
767  C  CA    A TYR   A 99  ? 0.1575 0.3196 0.1207 0.0789  0.0122  0.0009  96  TYR   A CA    
768  C  CA    B TYR   A 99  ? 0.1926 0.3056 0.1049 0.0622  0.0244  -0.0065 96  TYR   A CA    
769  C  C     A TYR   A 99  ? 0.1677 0.3387 0.1470 0.0692  0.0093  0.0024  96  TYR   A C     
770  C  C     B TYR   A 99  ? 0.1843 0.3351 0.0967 0.0665  0.0163  -0.0033 96  TYR   A C     
771  O  O     A TYR   A 99  ? 0.1942 0.3879 0.1312 0.1141  -0.0118 0.0021  96  TYR   A O     
772  O  O     B TYR   A 99  ? 0.1642 0.4042 0.1039 0.0692  0.0228  -0.0076 96  TYR   A O     
773  C  CB    A TYR   A 99  ? 0.1470 0.2866 0.1299 0.0720  0.0088  0.0053  96  TYR   A CB    
774  C  CB    B TYR   A 99  ? 0.2223 0.2694 0.1114 0.0379  0.0383  0.0045  96  TYR   A CB    
775  C  CG    A TYR   A 99  ? 0.1880 0.2536 0.1361 0.0542  0.0259  0.0120  96  TYR   A CG    
776  C  CG    B TYR   A 99  ? 0.2744 0.2383 0.1506 0.0215  0.0441  0.0065  96  TYR   A CG    
777  C  CD1   A TYR   A 99  ? 0.1979 0.2318 0.1600 0.0129  -0.0191 0.0044  96  TYR   A CD1   
778  C  CD1   B TYR   A 99  ? 0.2755 0.2751 0.2064 0.0224  0.0458  -0.0513 96  TYR   A CD1   
779  C  CD2   A TYR   A 99  ? 0.1823 0.3008 0.1234 0.0461  0.0201  -0.0205 96  TYR   A CD2   
780  C  CD2   B TYR   A 99  ? 0.2612 0.2560 0.2409 -0.0085 0.0572  -0.0095 96  TYR   A CD2   
781  C  CE1   A TYR   A 99  ? 0.2070 0.2631 0.2012 0.0097  0.0131  -0.0277 96  TYR   A CE1   
782  C  CE1   B TYR   A 99  ? 0.2955 0.2150 0.2660 0.0268  0.0999  -0.0062 96  TYR   A CE1   
783  C  CE2   A TYR   A 99  ? 0.2154 0.2795 0.1703 0.0409  -0.0008 0.0044  96  TYR   A CE2   
784  C  CE2   B TYR   A 99  ? 0.2996 0.2163 0.2722 -0.0035 0.0431  -0.0290 96  TYR   A CE2   
785  C  CZ    A TYR   A 99  ? 0.1555 0.2615 0.1556 -0.0149 -0.0440 0.0212  96  TYR   A CZ    
786  C  CZ    B TYR   A 99  ? 0.2744 0.2199 0.1863 -0.0169 0.0769  -0.0080 96  TYR   A CZ    
787  O  OH    A TYR   A 99  ? 0.1986 0.1964 0.2364 -0.0371 0.0225  0.0192  96  TYR   A OH    
788  O  OH    B TYR   A 99  ? 0.2642 0.1699 0.2783 0.0115  0.0781  0.0044  96  TYR   A OH    
789  N  N     . ARG   A 100 ? 0.1767 0.3377 0.1020 0.0639  0.0068  0.0091  97  ARG   A N     
790  C  CA    . ARG   A 100 ? 0.1911 0.3423 0.0950 0.0541  0.0076  -0.0099 97  ARG   A CA    
791  C  C     . ARG   A 100 ? 0.1749 0.3913 0.1088 0.0807  0.0037  -0.0277 97  ARG   A C     
792  O  O     . ARG   A 100 ? 0.1627 0.4096 0.1622 0.0535  -0.0160 -0.0344 97  ARG   A O     
793  C  CB    . ARG   A 100 ? 0.1755 0.3360 0.1667 0.0513  0.0410  0.0132  97  ARG   A CB    
794  C  CG    . ARG   A 100 ? 0.2017 0.3270 0.1753 0.0484  0.0536  -0.0008 97  ARG   A CG    
795  C  CD    . ARG   A 100 ? 0.2355 0.2980 0.1905 0.0659  0.0401  0.0075  97  ARG   A CD    
796  N  NE    . ARG   A 100 ? 0.2598 0.2960 0.2461 0.0419  0.0499  0.0114  97  ARG   A NE    
797  C  CZ    . ARG   A 100 ? 0.3155 0.3315 0.2529 0.0411  0.0304  0.0138  97  ARG   A CZ    
798  N  NH1   . ARG   A 100 ? 0.3468 0.2932 0.2435 0.0194  0.0373  -0.0177 97  ARG   A NH1   
799  N  NH2   . ARG   A 100 ? 0.3997 0.3478 0.2633 0.0001  0.0177  0.0127  97  ARG   A NH2   
800  N  N     . GLU   A 101 ? 0.1469 0.4078 0.1192 0.0617  0.0026  0.0208  98  GLU   A N     
801  C  CA    . GLU   A 101 ? 0.1758 0.4220 0.1285 0.0480  0.0228  0.0205  98  GLU   A CA    
802  C  C     . GLU   A 101 ? 0.1596 0.4091 0.1101 0.0390  -0.0155 -0.0242 98  GLU   A C     
803  O  O     . GLU   A 101 ? 0.1567 0.4342 0.1529 0.0595  0.0045  -0.0186 98  GLU   A O     
804  C  CB    . GLU   A 101 ? 0.1809 0.5059 0.1421 0.0316  0.0168  0.0430  98  GLU   A CB    
805  C  CG    . GLU   A 101 ? 0.2750 0.5338 0.2334 0.0836  0.0583  0.0593  98  GLU   A CG    
806  C  CD    . GLU   A 101 ? 0.3023 0.5101 0.3881 0.1115  0.0560  0.0558  98  GLU   A CD    
807  O  OE1   . GLU   A 101 ? 0.2902 0.7194 0.4921 0.0298  0.1258  0.0944  98  GLU   A OE1   
808  O  OE2   . GLU   A 101 ? 0.4611 0.5542 0.4865 0.1884  0.0307  0.0013  98  GLU   A OE2   
809  N  N     . GLN   A 102 ? 0.1534 0.3897 0.1051 0.0527  -0.0053 -0.0446 99  GLN   A N     
810  C  CA    . GLN   A 102 ? 0.1658 0.3895 0.1479 0.0532  -0.0084 -0.0602 99  GLN   A CA    
811  C  C     . GLN   A 102 ? 0.1376 0.3436 0.1390 0.0542  0.0114  -0.0660 99  GLN   A C     
812  O  O     . GLN   A 102 ? 0.1416 0.3335 0.1268 0.0525  0.0051  -0.0653 99  GLN   A O     
813  C  CB    . GLN   A 102 ? 0.1956 0.3609 0.2026 0.0652  0.0039  -0.0899 99  GLN   A CB    
814  C  CG    . GLN   A 102 ? 0.2808 0.5122 0.2210 0.0395  -0.0226 -0.1062 99  GLN   A CG    
815  C  CD    . GLN   A 102 ? 0.3884 0.4722 0.2469 -0.0080 -0.0299 -0.1555 99  GLN   A CD    
816  O  OE1   . GLN   A 102 ? 0.4398 0.5898 0.2754 0.0003  -0.0043 -0.1069 99  GLN   A OE1   
817  N  NE2   . GLN   A 102 ? 0.5824 0.5768 0.4000 -0.0239 -0.1465 -0.2531 99  GLN   A NE2   
818  N  N     . ILE   A 103 ? 0.1404 0.2949 0.1206 0.0466  -0.0081 -0.0596 100 ILE   A N     
819  C  CA    . ILE   A 103 ? 0.1421 0.2890 0.1273 0.0285  -0.0117 -0.0445 100 ILE   A CA    
820  C  C     . ILE   A 103 ? 0.1522 0.2981 0.1100 0.0249  0.0075  -0.0458 100 ILE   A C     
821  O  O     . ILE   A 103 ? 0.1462 0.3566 0.1457 0.0334  0.0078  -0.0337 100 ILE   A O     
822  C  CB    . ILE   A 103 ? 0.1468 0.2629 0.1315 0.0262  -0.0061 -0.0417 100 ILE   A CB    
823  C  CG1   . ILE   A 103 ? 0.1608 0.2452 0.1623 0.0389  0.0012  -0.0154 100 ILE   A CG1   
824  C  CG2   . ILE   A 103 ? 0.1622 0.2848 0.1382 0.0065  -0.0163 -0.0247 100 ILE   A CG2   
825  C  CD1   . ILE   A 103 ? 0.1424 0.2272 0.1356 0.0208  -0.0054 0.0017  100 ILE   A CD1   
826  N  N     . LYS   A 104 ? 0.1379 0.3165 0.1386 0.0177  0.0168  -0.0139 101 LYS   A N     
827  C  CA    . LYS   A 104 ? 0.1782 0.3303 0.1385 -0.0017 0.0324  -0.0214 101 LYS   A CA    
828  C  C     . LYS   A 104 ? 0.1612 0.3294 0.1459 -0.0026 0.0234  -0.0091 101 LYS   A C     
829  O  O     . LYS   A 104 ? 0.1562 0.3692 0.1693 0.0118  0.0181  -0.0054 101 LYS   A O     
830  C  CB    . LYS   A 104 ? 0.2233 0.3276 0.1842 -0.0094 0.0700  0.0074  101 LYS   A CB    
831  C  CG    . LYS   A 104 ? 0.2691 0.3304 0.2599 0.0028  0.0523  -0.0519 101 LYS   A CG    
832  C  CD    . LYS   A 104 ? 0.3920 0.3560 0.3705 0.0432  0.0444  -0.0221 101 LYS   A CD    
833  C  CE    . LYS   A 104 ? 0.4410 0.4118 0.3973 0.0630  0.0405  0.0279  101 LYS   A CE    
834  N  NZ    . LYS   A 104 ? 0.3840 0.4163 0.5363 0.0413  0.1675  0.0820  101 LYS   A NZ    
835  N  N     . ARG   A 105 ? 0.1645 0.3392 0.1346 0.0260  0.0136  -0.0117 102 ARG   A N     
836  C  CA    . ARG   A 105 ? 0.1873 0.3552 0.1346 0.0133  0.0343  -0.0095 102 ARG   A CA    
837  C  C     . ARG   A 105 ? 0.1445 0.3459 0.1551 0.0223  0.0209  -0.0634 102 ARG   A C     
838  O  O     . ARG   A 105 ? 0.1417 0.4042 0.1903 0.0125  0.0217  -0.0591 102 ARG   A O     
839  C  CB    . ARG   A 105 ? 0.2109 0.4087 0.1380 0.0166  0.0188  -0.0091 102 ARG   A CB    
840  C  CG    . ARG   A 105 ? 0.2781 0.4760 0.1850 0.0662  0.0121  -0.0455 102 ARG   A CG    
841  C  CD    . ARG   A 105 ? 0.4397 0.5798 0.2060 -0.0028 0.0052  -0.1168 102 ARG   A CD    
842  N  NE    . ARG   A 105 ? 0.5175 0.5811 0.3646 -0.0535 0.0509  -0.1624 102 ARG   A NE    
843  C  CZ    . ARG   A 105 ? 0.4905 0.6072 0.4898 -0.0070 0.0832  -0.1720 102 ARG   A CZ    
844  N  NH1   . ARG   A 105 ? 0.4726 0.6875 0.6177 -0.0045 0.0461  -0.1236 102 ARG   A NH1   
845  N  NH2   . ARG   A 105 ? 0.5400 0.6641 0.5973 -0.0547 0.0313  -0.1109 102 ARG   A NH2   
846  N  N     . VAL   A 106 ? 0.1347 0.3599 0.1790 0.0424  0.0214  -0.0364 103 VAL   A N     
847  C  CA    . VAL   A 106 ? 0.1612 0.3391 0.1634 0.0423  0.0201  -0.0462 103 VAL   A CA    
848  C  C     . VAL   A 106 ? 0.1542 0.3280 0.1930 0.0534  -0.0047 -0.0264 103 VAL   A C     
849  O  O     . VAL   A 106 ? 0.1375 0.3548 0.2271 0.0465  -0.0084 -0.0326 103 VAL   A O     
850  C  CB    . VAL   A 106 ? 0.1802 0.3504 0.2438 0.0337  0.0087  -0.0297 103 VAL   A CB    
851  C  CG1   . VAL   A 106 ? 0.2288 0.3807 0.2972 0.0598  -0.0236 -0.0271 103 VAL   A CG1   
852  C  CG2   . VAL   A 106 ? 0.1954 0.3428 0.2534 0.0719  0.0153  -0.0759 103 VAL   A CG2   
853  N  N     . LYS   A 107 ? 0.1098 0.3434 0.1613 0.0202  -0.0048 -0.0371 104 LYS   A N     
854  C  CA    . LYS   A 107 ? 0.1379 0.3639 0.1493 0.0055  -0.0187 -0.0116 104 LYS   A CA    
855  C  C     . LYS   A 107 ? 0.1471 0.3728 0.1628 0.0045  0.0107  -0.0268 104 LYS   A C     
856  O  O     . LYS   A 107 ? 0.1626 0.4691 0.2086 -0.0118 -0.0218 -0.0330 104 LYS   A O     
857  C  CB    . LYS   A 107 ? 0.1398 0.3439 0.1647 0.0016  -0.0292 -0.0250 104 LYS   A CB    
858  C  CG    . LYS   A 107 ? 0.1601 0.3219 0.1597 0.0069  0.0010  -0.0453 104 LYS   A CG    
859  C  CD    . LYS   A 107 ? 0.1354 0.3041 0.1575 -0.0230 -0.0094 -0.0506 104 LYS   A CD    
860  C  CE    . LYS   A 107 ? 0.1484 0.2285 0.1585 -0.0061 0.0013  -0.0464 104 LYS   A CE    
861  N  NZ    . LYS   A 107 ? 0.1686 0.2271 0.1907 -0.0069 -0.0226 -0.0591 104 LYS   A NZ    
862  N  N     . ASP   A 108 ? 0.1721 0.4355 0.1653 0.0034  -0.0001 -0.0242 105 ASP   A N     
863  C  CA    . ASP   A 108 ? 0.1819 0.4905 0.1944 -0.0363 0.0220  -0.0391 105 ASP   A CA    
864  C  C     . ASP   A 108 ? 0.1480 0.4286 0.2245 -0.0467 0.0569  -0.0026 105 ASP   A C     
865  O  O     . ASP   A 108 ? 0.1763 0.4772 0.2111 -0.0756 0.0364  0.0055  105 ASP   A O     
866  C  CB    . ASP   A 108 ? 0.2037 0.5068 0.2170 0.0002  0.0367  -0.0344 105 ASP   A CB    
867  C  CG    . ASP   A 108 ? 0.2355 0.5510 0.1867 0.0378  0.0192  0.0603  105 ASP   A CG    
868  O  OD1   . ASP   A 108 ? 0.2956 0.6686 0.2130 0.0853  -0.0389 0.0963  105 ASP   A OD1   
869  O  OD2   . ASP   A 108 ? 0.2533 0.6002 0.2632 0.0683  0.0199  0.1139  105 ASP   A OD2   
870  N  N     . SER   A 109 ? 0.1693 0.4345 0.2337 -0.0081 0.0515  -0.0174 106 SER   A N     
871  C  CA    . SER   A 109 ? 0.2562 0.4714 0.2832 -0.0411 0.1071  -0.0707 106 SER   A CA    
872  C  C     . SER   A 109 ? 0.2968 0.4847 0.3479 0.0051  0.0565  -0.0336 106 SER   A C     
873  O  O     . SER   A 109 ? 0.2179 0.5601 0.3513 0.0713  0.0372  -0.0399 106 SER   A O     
874  C  CB    . SER   A 109 ? 0.1917 0.5072 0.2666 -0.0321 0.0517  -0.1249 106 SER   A CB    
875  O  OG    . SER   A 109 ? 0.3221 0.5320 0.3259 -0.0432 0.0972  -0.1583 106 SER   A OG    
876  N  N     . GLU   A 110 ? 0.3143 0.4622 0.5049 -0.0701 0.1175  -0.0291 107 GLU   A N     
877  C  CA    . GLU   A 110 ? 0.3904 0.4201 0.4633 0.0227  0.0310  -0.0055 107 GLU   A CA    
878  C  C     . GLU   A 110 ? 0.2354 0.2940 0.4546 -0.0311 0.0366  -0.0065 107 GLU   A C     
879  O  O     . GLU   A 110 ? 0.3414 0.3983 0.4717 0.0277  0.1030  -0.0062 107 GLU   A O     
880  C  CB    . GLU   A 110 ? 0.4711 0.4598 0.4570 -0.0131 0.1032  0.0612  107 GLU   A CB    
881  C  CG    . GLU   A 110 ? 0.5704 0.4645 0.4636 0.0278  0.0287  0.1089  107 GLU   A CG    
882  C  CD    . GLU   A 110 ? 0.6001 0.5468 0.5470 -0.0047 0.0182  0.0386  107 GLU   A CD    
883  O  OE1   . GLU   A 110 ? 0.7144 0.6476 0.4796 0.0281  0.0768  -0.0057 107 GLU   A OE1   
884  O  OE2   . GLU   A 110 ? 0.6109 0.6422 0.5423 0.0315  0.0609  0.1027  107 GLU   A OE2   
885  N  N     . ASP   A 111 ? 0.2204 0.4753 0.3537 -0.0112 0.0989  0.0142  108 ASP   A N     
886  C  CA    . ASP   A 111 ? 0.2224 0.4284 0.3520 -0.0430 0.0963  -0.0137 108 ASP   A CA    
887  C  C     . ASP   A 111 ? 0.2243 0.3890 0.3732 -0.0544 0.1176  -0.1070 108 ASP   A C     
888  O  O     . ASP   A 111 ? 0.2406 0.5339 0.5779 -0.0309 0.0123  -0.0555 108 ASP   A O     
889  C  CB    . ASP   A 111 ? 0.2370 0.3859 0.4119 -0.0091 0.0596  -0.0151 108 ASP   A CB    
890  C  CG    . ASP   A 111 ? 0.2312 0.3868 0.4407 -0.0131 -0.0003 0.0427  108 ASP   A CG    
891  O  OD1   . ASP   A 111 ? 0.3652 0.4324 0.4939 0.0562  -0.0006 0.0956  108 ASP   A OD1   
892  O  OD2   . ASP   A 111 ? 0.2890 0.4303 0.4776 -0.0702 -0.0634 0.0197  108 ASP   A OD2   
893  N  N     . VAL   A 112 ? 0.2397 0.2673 0.2144 -0.0487 0.0779  -0.0255 109 VAL   A N     
894  C  CA    . VAL   A 112 ? 0.1916 0.2468 0.1354 -0.0122 0.0411  -0.0168 109 VAL   A CA    
895  C  C     . VAL   A 112 ? 0.1485 0.2099 0.1291 -0.0106 0.0204  0.0044  109 VAL   A C     
896  O  O     . VAL   A 112 ? 0.1525 0.2018 0.1823 -0.0143 -0.0019 0.0201  109 VAL   A O     
897  C  CB    . VAL   A 112 ? 0.2621 0.2852 0.1529 -0.0740 0.0485  -0.0260 109 VAL   A CB    
898  C  CG1   . VAL   A 112 ? 0.2677 0.2823 0.1798 -0.0310 0.0429  -0.0279 109 VAL   A CG1   
899  C  CG2   . VAL   A 112 ? 0.2922 0.3315 0.1372 -0.0544 0.0560  -0.0497 109 VAL   A CG2   
900  N  N     . PRO   A 113 ? 0.1144 0.1798 0.1255 -0.0048 0.0153  -0.0138 110 PRO   A N     
901  C  CA    . PRO   A 113 ? 0.1049 0.1550 0.1384 -0.0163 0.0170  -0.0247 110 PRO   A CA    
902  C  C     . PRO   A 113 ? 0.1033 0.1415 0.1181 -0.0081 0.0123  -0.0077 110 PRO   A C     
903  O  O     . PRO   A 113 ? 0.1101 0.1359 0.1178 0.0050  -0.0025 -0.0046 110 PRO   A O     
904  C  CB    . PRO   A 113 ? 0.0995 0.1620 0.1270 -0.0044 -0.0005 -0.0356 110 PRO   A CB    
905  C  CG    . PRO   A 113 ? 0.1056 0.1814 0.1462 -0.0044 0.0167  -0.0357 110 PRO   A CG    
906  C  CD    . PRO   A 113 ? 0.0875 0.1994 0.1488 -0.0038 0.0415  -0.0278 110 PRO   A CD    
907  N  N     . MET   A 114 ? 0.1037 0.1316 0.1550 -0.0083 0.0047  -0.0110 111 MET   A N     
908  C  CA    . MET   A 114 ? 0.1114 0.1311 0.1115 0.0019  -0.0005 -0.0035 111 MET   A CA    
909  C  C     . MET   A 114 ? 0.1051 0.1195 0.1050 -0.0041 -0.0134 -0.0085 111 MET   A C     
910  O  O     . MET   A 114 ? 0.1045 0.1206 0.1484 -0.0062 -0.0039 -0.0163 111 MET   A O     
911  C  CB    . MET   A 114 ? 0.1520 0.1779 0.1229 -0.0044 0.0025  -0.0014 111 MET   A CB    
912  C  CG    . MET   A 114 ? 0.1794 0.2545 0.1903 0.0231  0.0270  -0.0118 111 MET   A CG    
913  S  SD    . MET   A 114 ? 0.2544 0.4381 0.1949 0.0288  0.0017  -0.0083 111 MET   A SD    
914  C  CE    . MET   A 114 ? 0.2140 0.1629 0.0110 -0.0170 -0.0122 -0.0238 111 MET   A CE    
915  N  N     . VAL   A 115 ? 0.0960 0.1045 0.1012 0.0046  -0.0055 -0.0130 112 VAL   A N     
916  C  CA    . VAL   A 115 ? 0.1016 0.1048 0.0808 0.0079  -0.0089 -0.0151 112 VAL   A CA    
917  C  C     . VAL   A 115 ? 0.0976 0.1136 0.0707 -0.0001 -0.0027 0.0024  112 VAL   A C     
918  O  O     . VAL   A 115 ? 0.1112 0.1252 0.1174 -0.0053 0.0005  -0.0179 112 VAL   A O     
919  C  CB    . VAL   A 115 ? 0.1336 0.1242 0.0863 -0.0036 -0.0058 -0.0115 112 VAL   A CB    
920  C  CG1   . VAL   A 115 ? 0.1400 0.1505 0.0806 -0.0040 0.0015  -0.0139 112 VAL   A CG1   
921  C  CG2   . VAL   A 115 ? 0.1469 0.1421 0.0912 0.0092  -0.0145 -0.0152 112 VAL   A CG2   
922  N  N     . LEU   A 116 ? 0.0880 0.1149 0.0867 0.0033  0.0022  -0.0114 113 LEU   A N     
923  C  CA    . LEU   A 116 ? 0.0893 0.1270 0.0814 0.0012  0.0039  -0.0099 113 LEU   A CA    
924  C  C     . LEU   A 116 ? 0.0991 0.1034 0.0816 0.0141  0.0100  -0.0018 113 LEU   A C     
925  O  O     . LEU   A 116 ? 0.1032 0.1143 0.0921 0.0051  0.0097  -0.0148 113 LEU   A O     
926  C  CB    . LEU   A 116 ? 0.1024 0.1315 0.0781 0.0010  0.0072  -0.0003 113 LEU   A CB    
927  C  CG    . LEU   A 116 ? 0.1168 0.1579 0.0855 0.0015  -0.0090 -0.0008 113 LEU   A CG    
928  C  CD1   . LEU   A 116 ? 0.1282 0.1650 0.0866 -0.0119 -0.0188 -0.0106 113 LEU   A CD1   
929  C  CD2   . LEU   A 116 ? 0.1412 0.1640 0.0993 -0.0044 -0.0261 0.0065  113 LEU   A CD2   
930  N  N     . VAL   A 117 ? 0.0965 0.1063 0.0802 0.0104  0.0062  -0.0002 114 VAL   A N     
931  C  CA    . VAL   A 117 ? 0.0975 0.1167 0.0729 0.0006  -0.0024 -0.0058 114 VAL   A CA    
932  C  C     . VAL   A 117 ? 0.0954 0.1090 0.0935 -0.0005 -0.0041 -0.0058 114 VAL   A C     
933  O  O     . VAL   A 117 ? 0.1004 0.1303 0.0873 0.0061  -0.0132 -0.0095 114 VAL   A O     
934  C  CB    . VAL   A 117 ? 0.1088 0.1280 0.0951 0.0050  -0.0154 0.0028  114 VAL   A CB    
935  C  CG1   . VAL   A 117 ? 0.1282 0.1226 0.1057 -0.0151 -0.0156 0.0004  114 VAL   A CG1   
936  C  CG2   . VAL   A 117 ? 0.1179 0.1334 0.1058 0.0063  -0.0214 0.0095  114 VAL   A CG2   
937  N  N     . GLY   A 118 ? 0.1013 0.1093 0.0747 0.0000  -0.0091 0.0041  115 GLY   A N     
938  C  CA    . GLY   A 118 ? 0.1013 0.1257 0.0754 -0.0052 -0.0068 0.0059  115 GLY   A CA    
939  C  C     . GLY   A 118 ? 0.0948 0.1178 0.0756 -0.0027 0.0012  -0.0017 115 GLY   A C     
940  O  O     . GLY   A 118 ? 0.1109 0.1386 0.0812 -0.0024 -0.0052 -0.0239 115 GLY   A O     
941  N  N     . ASN   A 119 ? 0.1027 0.1185 0.0714 -0.0067 -0.0012 0.0005  116 ASN   A N     
942  C  CA    . ASN   A 119 ? 0.1133 0.1227 0.0689 -0.0165 -0.0059 -0.0036 116 ASN   A CA    
943  C  C     . ASN   A 119 ? 0.1131 0.1489 0.0790 -0.0076 0.0014  -0.0046 116 ASN   A C     
944  O  O     . ASN   A 119 ? 0.1068 0.1477 0.0972 -0.0072 -0.0078 -0.0008 116 ASN   A O     
945  C  CB    . ASN   A 119 ? 0.1176 0.1313 0.0758 -0.0125 -0.0071 -0.0077 116 ASN   A CB    
946  C  CG    . ASN   A 119 ? 0.1318 0.1295 0.0815 -0.0249 -0.0118 -0.0080 116 ASN   A CG    
947  O  OD1   . ASN   A 119 ? 0.1408 0.1325 0.0845 -0.0269 -0.0022 -0.0097 116 ASN   A OD1   
948  N  ND2   . ASN   A 119 ? 0.1416 0.1306 0.1151 -0.0253 -0.0088 -0.0135 116 ASN   A ND2   
949  N  N     . LYS   A 120 ? 0.1151 0.1510 0.0853 -0.0179 0.0013  -0.0021 117 LYS   A N     
950  C  CA    . LYS   A 120 ? 0.1143 0.1645 0.0861 -0.0233 0.0033  -0.0150 117 LYS   A CA    
951  C  C     . LYS   A 120 ? 0.1230 0.1677 0.0974 -0.0279 -0.0076 -0.0194 117 LYS   A C     
952  O  O     . LYS   A 120 ? 0.1206 0.1988 0.0970 -0.0120 0.0038  -0.0270 117 LYS   A O     
953  C  CB    . LYS   A 120 ? 0.1102 0.1685 0.0990 -0.0305 -0.0059 -0.0145 117 LYS   A CB    
954  C  CG    . LYS   A 120 ? 0.1116 0.1642 0.1005 -0.0325 0.0039  -0.0155 117 LYS   A CG    
955  C  CD    . LYS   A 120 ? 0.1233 0.1781 0.1178 -0.0437 0.0005  -0.0213 117 LYS   A CD    
956  C  CE    . LYS   A 120 ? 0.1299 0.1945 0.1185 -0.0346 -0.0157 -0.0405 117 LYS   A CE    
957  N  NZ    . LYS   A 120 ? 0.1487 0.2045 0.1339 -0.0245 -0.0260 -0.0640 117 LYS   A NZ    
958  N  N     . SER   A 121 ? 0.1158 0.1629 0.0940 -0.0215 -0.0036 -0.0239 118 SER   A N     
959  C  CA    . SER   A 121 ? 0.1195 0.1824 0.1150 0.0003  -0.0148 -0.0202 118 SER   A CA    
960  C  C     . SER   A 121 ? 0.1363 0.2111 0.1017 -0.0094 -0.0040 -0.0451 118 SER   A C     
961  O  O     . SER   A 121 ? 0.1391 0.2475 0.1493 0.0050  0.0046  -0.0720 118 SER   A O     
962  C  CB    . SER   A 121 ? 0.1344 0.1712 0.1335 -0.0281 -0.0073 -0.0128 118 SER   A CB    
963  O  OG    . SER   A 121 ? 0.1519 0.1899 0.1025 -0.0311 0.0051  -0.0265 118 SER   A OG    
964  N  N     . ASP   A 122 ? 0.1128 0.2048 0.1070 -0.0089 -0.0006 -0.0467 119 ASP   A N     
965  C  CA    . ASP   A 122 ? 0.1271 0.2311 0.1177 -0.0086 0.0179  -0.0450 119 ASP   A CA    
966  C  C     . ASP   A 122 ? 0.1172 0.2361 0.1392 0.0028  0.0123  -0.0432 119 ASP   A C     
967  O  O     . ASP   A 122 ? 0.1278 0.3348 0.1430 -0.0302 0.0260  -0.0505 119 ASP   A O     
968  C  CB    . ASP   A 122 ? 0.1543 0.2501 0.1432 -0.0286 0.0365  -0.0224 119 ASP   A CB    
969  C  CG    . ASP   A 122 ? 0.1301 0.2586 0.1451 -0.0149 0.0036  -0.0319 119 ASP   A CG    
970  O  OD1   . ASP   A 122 ? 0.1404 0.2152 0.1264 -0.0322 0.0123  -0.0393 119 ASP   A OD1   
971  O  OD2   . ASP   A 122 ? 0.1492 0.2655 0.2220 -0.0328 0.0306  -0.0383 119 ASP   A OD2   
972  N  N     . LEU   A 123 ? 0.1106 0.2510 0.1259 -0.0071 -0.0021 -0.0655 120 LEU   A N     
973  C  CA    . LEU   A 123 ? 0.1193 0.2339 0.1346 -0.0232 -0.0095 -0.0414 120 LEU   A CA    
974  C  C     . LEU   A 123 ? 0.1016 0.2249 0.1386 -0.0217 0.0036  -0.0369 120 LEU   A C     
975  O  O     . LEU   A 123 ? 0.1089 0.2419 0.1803 -0.0378 0.0018  -0.0155 120 LEU   A O     
976  C  CB    . LEU   A 123 ? 0.1172 0.2746 0.1316 -0.0255 -0.0181 -0.0634 120 LEU   A CB    
977  C  CG    . LEU   A 123 ? 0.1198 0.2742 0.1655 -0.0201 -0.0194 -0.0844 120 LEU   A CG    
978  C  CD1   . LEU   A 123 ? 0.1184 0.3220 0.1732 -0.0206 -0.0160 -0.1022 120 LEU   A CD1   
979  C  CD2   . LEU   A 123 ? 0.1713 0.2635 0.1795 -0.0340 -0.0153 -0.0617 120 LEU   A CD2   
980  N  N     . PRO   A 124 ? 0.1039 0.2300 0.1655 -0.0189 0.0099  -0.0391 121 PRO   A N     
981  C  CA    . PRO   A 124 ? 0.1059 0.2280 0.1545 -0.0233 0.0121  -0.0402 121 PRO   A CA    
982  C  C     . PRO   A 124 ? 0.1251 0.2452 0.1667 -0.0078 0.0078  -0.0331 121 PRO   A C     
983  O  O     . PRO   A 124 ? 0.1691 0.2351 0.2042 -0.0020 0.0302  -0.0575 121 PRO   A O     
984  C  CB    . PRO   A 124 ? 0.1192 0.2327 0.1468 -0.0149 0.0257  -0.0398 121 PRO   A CB    
985  C  CG    . PRO   A 124 ? 0.1085 0.2335 0.1636 -0.0188 0.0025  -0.0449 121 PRO   A CG    
986  C  CD    . PRO   A 124 ? 0.1014 0.2434 0.1396 -0.0209 0.0055  -0.0367 121 PRO   A CD    
987  N  N     . SER   A 125 ? 0.1254 0.2330 0.1544 0.0033  0.0144  -0.0266 122 SER   A N     
988  C  CA    . SER   A 125 ? 0.0982 0.2529 0.1682 0.0050  0.0000  -0.0255 122 SER   A CA    
989  C  C     . SER   A 125 ? 0.1010 0.2402 0.1837 0.0206  0.0069  -0.0127 122 SER   A C     
990  O  O     . SER   A 125 ? 0.1471 0.2859 0.1546 0.0146  0.0121  -0.0271 122 SER   A O     
991  C  CB    . SER   A 125 ? 0.1100 0.2845 0.1546 -0.0051 0.0044  -0.0399 122 SER   A CB    
992  O  OG    . SER   A 125 ? 0.1049 0.3373 0.2023 -0.0220 -0.0043 -0.0278 122 SER   A OG    
993  N  N     . ARG   A 126 ? 0.1148 0.2425 0.1608 0.0051  0.0232  0.0031  123 ARG   A N     
994  C  CA    . ARG   A 126 ? 0.1013 0.2500 0.1588 -0.0072 0.0016  0.0093  123 ARG   A CA    
995  C  C     . ARG   A 126 ? 0.1012 0.2718 0.1643 0.0179  -0.0012 0.0023  123 ARG   A C     
996  O  O     . ARG   A 126 ? 0.1143 0.3180 0.1699 0.0339  0.0127  0.0192  123 ARG   A O     
997  C  CB    . ARG   A 126 ? 0.1607 0.2506 0.1463 -0.0213 -0.0061 0.0138  123 ARG   A CB    
998  C  CG    . ARG   A 126 ? 0.1595 0.2174 0.1562 0.0000  0.0092  0.0172  123 ARG   A CG    
999  C  CD    . ARG   A 126 ? 0.1502 0.2330 0.1624 0.0107  0.0010  0.0089  123 ARG   A CD    
1000 N  NE    . ARG   A 126 ? 0.1281 0.2516 0.1515 0.0077  0.0173  -0.0080 123 ARG   A NE    
1001 C  CZ    . ARG   A 126 ? 0.1402 0.2402 0.1385 0.0212  0.0188  0.0167  123 ARG   A CZ    
1002 N  NH1   . ARG   A 126 ? 0.1338 0.2762 0.1324 0.0194  0.0183  0.0286  123 ARG   A NH1   
1003 N  NH2   . ARG   A 126 ? 0.1451 0.2586 0.1344 0.0006  0.0272  0.0033  123 ARG   A NH2   
1004 N  N     . THR   A 127 ? 0.1042 0.2720 0.1240 0.0191  -0.0088 0.0206  124 THR   A N     
1005 C  CA    . THR   A 127 ? 0.1237 0.2806 0.1325 0.0125  -0.0193 0.0249  124 THR   A CA    
1006 C  C     . THR   A 127 ? 0.1159 0.2717 0.1245 0.0238  -0.0016 0.0372  124 THR   A C     
1007 O  O     . THR   A 127 ? 0.1451 0.3069 0.1591 -0.0078 -0.0339 0.0722  124 THR   A O     
1008 C  CB    . THR   A 127 ? 0.1339 0.3291 0.1295 0.0156  0.0052  -0.0079 124 THR   A CB    
1009 O  OG1   . THR   A 127 ? 0.1456 0.3093 0.1314 0.0233  -0.0032 -0.0030 124 THR   A OG1   
1010 C  CG2   . THR   A 127 ? 0.1850 0.3688 0.1486 -0.0314 -0.0384 -0.0228 124 THR   A CG2   
1011 N  N     . VAL   A 128 ? 0.1222 0.2453 0.1173 0.0053  -0.0074 0.0279  125 VAL   A N     
1012 C  CA    . VAL   A 128 ? 0.1140 0.2397 0.1182 0.0232  -0.0049 0.0328  125 VAL   A CA    
1013 C  C     . VAL   A 128 ? 0.1212 0.2349 0.1198 0.0102  0.0043  0.0304  125 VAL   A C     
1014 O  O     . VAL   A 128 ? 0.1430 0.2494 0.1139 0.0142  0.0162  0.0300  125 VAL   A O     
1015 C  CB    . VAL   A 128 ? 0.1143 0.2239 0.1244 0.0175  0.0019  0.0264  125 VAL   A CB    
1016 C  CG1   . VAL   A 128 ? 0.1100 0.2296 0.1073 0.0228  0.0093  0.0272  125 VAL   A CG1   
1017 C  CG2   . VAL   A 128 ? 0.1176 0.2653 0.1504 0.0202  -0.0105 -0.0057 125 VAL   A CG2   
1018 N  N     . ASP   A 129 ? 0.1549 0.2500 0.1319 0.0350  0.0094  0.0343  126 ASP   A N     
1019 C  CA    . ASP   A 129 ? 0.1486 0.2618 0.1542 0.0122  0.0247  0.0143  126 ASP   A CA    
1020 C  C     . ASP   A 129 ? 0.1541 0.2683 0.1566 0.0438  0.0162  0.0221  126 ASP   A C     
1021 O  O     . ASP   A 129 ? 0.1527 0.2492 0.1445 0.0350  0.0113  0.0200  126 ASP   A O     
1022 C  CB    . ASP   A 129 ? 0.1952 0.3026 0.2350 0.0436  -0.0292 0.0537  126 ASP   A CB    
1023 C  CG    . ASP   A 129 ? 0.3801 0.3417 0.3770 0.0581  -0.0434 -0.0130 126 ASP   A CG    
1024 O  OD1   . ASP   A 129 ? 0.3384 0.4299 0.3968 0.0673  -0.0460 0.0377  126 ASP   A OD1   
1025 O  OD2   . ASP   A 129 ? 0.4186 0.5584 0.7274 0.1522  -0.0968 0.0122  126 ASP   A OD2   
1026 N  N     . THR   A 130 ? 0.1551 0.3080 0.1657 0.0580  0.0148  -0.0124 127 THR   A N     
1027 C  CA    . THR   A 130 ? 0.1856 0.3488 0.1717 0.0824  -0.0103 -0.0040 127 THR   A CA    
1028 C  C     . THR   A 130 ? 0.1617 0.3409 0.1522 0.0751  -0.0070 -0.0519 127 THR   A C     
1029 O  O     . THR   A 130 ? 0.1589 0.4148 0.1625 0.0824  -0.0148 -0.0768 127 THR   A O     
1030 C  CB    . THR   A 130 ? 0.2815 0.3677 0.1629 0.0955  0.0018  0.0473  127 THR   A CB    
1031 O  OG1   . THR   A 130 ? 0.3633 0.3743 0.2761 0.0822  0.0218  0.0374  127 THR   A OG1   
1032 C  CG2   . THR   A 130 ? 0.2792 0.4685 0.2438 0.0903  -0.0135 0.0226  127 THR   A CG2   
1033 N  N     . LYS   A 131 ? 0.1760 0.2862 0.2168 0.0600  0.0133  -0.0608 128 LYS   A N     
1034 C  CA    . LYS   A 131 ? 0.2762 0.2702 0.2640 0.0371  0.0334  -0.0540 128 LYS   A CA    
1035 C  C     . LYS   A 131 ? 0.2148 0.2185 0.2120 0.0088  0.0042  -0.0085 128 LYS   A C     
1036 O  O     . LYS   A 131 ? 0.2050 0.2264 0.2478 0.0246  0.0114  -0.0215 128 LYS   A O     
1037 C  CB    . LYS   A 131 ? 0.2722 0.2397 0.4390 0.0189  0.0751  -0.0098 128 LYS   A CB    
1038 C  CG    . LYS   A 131 ? 0.4136 0.2979 0.4512 0.0372  0.0452  -0.0284 128 LYS   A CG    
1039 C  CD    . LYS   A 131 ? 0.4773 0.3878 0.5522 0.1183  0.0292  0.0135  128 LYS   A CD    
1040 C  CE    . LYS   A 131 ? 0.4853 0.5000 0.6061 0.1410  0.0289  0.0154  128 LYS   A CE    
1041 N  NZ    . LYS   A 131 ? 0.4969 0.4998 0.6792 0.1630  0.0945  0.0165  128 LYS   A NZ    
1042 N  N     . GLN   A 132 ? 0.1696 0.2380 0.1821 0.0387  0.0001  -0.0055 129 GLN   A N     
1043 C  CA    . GLN   A 132 ? 0.1921 0.1879 0.1359 0.0237  -0.0042 0.0292  129 GLN   A CA    
1044 C  C     . GLN   A 132 ? 0.1645 0.1872 0.1203 0.0129  0.0170  0.0296  129 GLN   A C     
1045 O  O     . GLN   A 132 ? 0.1540 0.1899 0.1233 0.0182  0.0077  0.0329  129 GLN   A O     
1046 C  CB    . GLN   A 132 ? 0.2507 0.2547 0.1766 0.0122  -0.0535 0.0259  129 GLN   A CB    
1047 C  CG    . GLN   A 132 ? 0.2807 0.3205 0.2424 0.0537  -0.0456 0.0571  129 GLN   A CG    
1048 C  CD    . GLN   A 132 ? 0.3774 0.4212 0.3244 -0.0191 -0.1020 0.0185  129 GLN   A CD    
1049 O  OE1   . GLN   A 132 ? 0.5406 0.4539 0.3964 -0.0631 -0.1196 -0.0471 129 GLN   A OE1   
1050 N  NE2   . GLN   A 132 ? 0.2857 0.5881 0.3790 0.0084  -0.0822 0.0222  129 GLN   A NE2   
1051 N  N     . ALA   A 133 ? 0.1266 0.1969 0.1094 0.0014  0.0068  0.0177  130 ALA   A N     
1052 C  CA    . ALA   A 133 ? 0.1420 0.1726 0.1034 0.0162  0.0196  0.0007  130 ALA   A CA    
1053 C  C     . ALA   A 133 ? 0.1445 0.1559 0.0854 0.0205  0.0038  0.0103  130 ALA   A C     
1054 O  O     . ALA   A 133 ? 0.1432 0.1493 0.1087 0.0184  0.0107  0.0058  130 ALA   A O     
1055 C  CB    . ALA   A 133 ? 0.1464 0.1822 0.1250 0.0094  0.0109  0.0132  130 ALA   A CB    
1056 N  N     . GLN   A 134 ? 0.1274 0.1588 0.1146 0.0145  0.0131  -0.0061 131 GLN   A N     
1057 C  CA    . GLN   A 134 ? 0.1379 0.1658 0.1087 0.0129  0.0083  0.0060  131 GLN   A CA    
1058 C  C     . GLN   A 134 ? 0.1574 0.1584 0.1060 0.0207  0.0149  0.0106  131 GLN   A C     
1059 O  O     . GLN   A 134 ? 0.1579 0.1782 0.1310 0.0196  0.0149  -0.0005 131 GLN   A O     
1060 C  CB    . GLN   A 134 ? 0.1607 0.1595 0.1348 0.0248  0.0243  -0.0002 131 GLN   A CB    
1061 C  CG    . GLN   A 134 ? 0.1743 0.1545 0.1278 0.0157  0.0198  -0.0103 131 GLN   A CG    
1062 C  CD    . GLN   A 134 ? 0.1881 0.1643 0.1419 0.0277  0.0491  0.0063  131 GLN   A CD    
1063 O  OE1   . GLN   A 134 ? 0.2308 0.1806 0.1951 0.0420  0.0749  0.0336  131 GLN   A OE1   
1064 N  NE2   . GLN   A 134 ? 0.2116 0.1468 0.1530 0.0131  0.0782  0.0052  131 GLN   A NE2   
1065 N  N     . ASP   A 135 ? 0.1706 0.1813 0.1159 0.0460  0.0168  0.0210  132 ASP   A N     
1066 C  CA    . ASP   A 135 ? 0.2011 0.1622 0.1227 0.0236  0.0144  0.0205  132 ASP   A CA    
1067 C  C     . ASP   A 135 ? 0.1780 0.1520 0.1140 0.0121  -0.0035 0.0201  132 ASP   A C     
1068 O  O     . ASP   A 135 ? 0.1906 0.1548 0.1396 0.0073  0.0283  0.0209  132 ASP   A O     
1069 C  CB    . ASP   A 135 ? 0.2223 0.1636 0.1442 0.0303  0.0029  0.0234  132 ASP   A CB    
1070 C  CG    . ASP   A 135 ? 0.2800 0.1801 0.1435 -0.0085 0.0019  0.0182  132 ASP   A CG    
1071 O  OD1   . ASP   A 135 ? 0.3716 0.2041 0.1926 -0.0641 0.0082  0.0280  132 ASP   A OD1   
1072 O  OD2   . ASP   A 135 ? 0.3509 0.2670 0.1582 -0.0372 0.0194  -0.0310 132 ASP   A OD2   
1073 N  N     . LEU   A 136 ? 0.1626 0.1587 0.0972 0.0054  0.0172  0.0061  133 LEU   A N     
1074 C  CA    . LEU   A 136 ? 0.1597 0.1585 0.1011 0.0155  0.0247  0.0235  133 LEU   A CA    
1075 C  C     . LEU   A 136 ? 0.1501 0.1469 0.0975 -0.0042 0.0232  0.0080  133 LEU   A C     
1076 O  O     . LEU   A 136 ? 0.1547 0.1571 0.1045 0.0011  0.0330  0.0210  133 LEU   A O     
1077 C  CB    . LEU   A 136 ? 0.1611 0.1693 0.1211 0.0174  0.0100  0.0166  133 LEU   A CB    
1078 C  CG    . LEU   A 136 ? 0.1886 0.1894 0.1117 0.0136  0.0091  -0.0052 133 LEU   A CG    
1079 C  CD1   . LEU   A 136 ? 0.2154 0.2146 0.1048 0.0171  0.0180  -0.0144 133 LEU   A CD1   
1080 C  CD2   . LEU   A 136 ? 0.2208 0.1794 0.1620 0.0177  0.0313  -0.0315 133 LEU   A CD2   
1081 N  N     . ALA   A 137 ? 0.1316 0.1356 0.0945 -0.0027 0.0158  0.0139  134 ALA   A N     
1082 C  CA    . ALA   A 137 ? 0.1292 0.1482 0.1047 -0.0018 0.0077  0.0183  134 ALA   A CA    
1083 C  C     . ALA   A 137 ? 0.1340 0.1489 0.0966 -0.0037 0.0173  0.0213  134 ALA   A C     
1084 O  O     . ALA   A 137 ? 0.1336 0.1641 0.1454 -0.0128 0.0284  0.0435  134 ALA   A O     
1085 C  CB    . ALA   A 137 ? 0.1366 0.1477 0.1121 -0.0146 0.0072  0.0209  134 ALA   A CB    
1086 N  N     . ARG   A 138 ? 0.1410 0.1446 0.1410 -0.0056 0.0416  0.0115  135 ARG   A N     
1087 C  CA    . ARG   A 138 ? 0.1775 0.1474 0.1556 -0.0065 0.0443  0.0058  135 ARG   A CA    
1088 C  C     . ARG   A 138 ? 0.1612 0.1496 0.1553 -0.0107 0.0376  0.0020  135 ARG   A C     
1089 O  O     . ARG   A 138 ? 0.1758 0.1617 0.1842 -0.0261 0.0328  0.0055  135 ARG   A O     
1090 C  CB    . ARG   A 138 ? 0.1608 0.1814 0.1799 0.0100  0.0311  -0.0200 135 ARG   A CB    
1091 C  CG    . ARG   A 138 ? 0.2016 0.1927 0.2357 -0.0150 0.0262  -0.0015 135 ARG   A CG    
1092 C  CD    . ARG   A 138 ? 0.2284 0.1838 0.2798 -0.0023 0.0086  -0.0104 135 ARG   A CD    
1093 N  NE    . ARG   A 138 ? 0.2562 0.2279 0.3629 0.0123  0.0753  0.0224  135 ARG   A NE    
1094 C  CZ    . ARG   A 138 ? 0.2653 0.2674 0.4175 0.0363  0.0561  -0.0556 135 ARG   A CZ    
1095 N  NH1   . ARG   A 138 ? 0.4021 0.1698 0.4440 0.0532  -0.0267 -0.0954 135 ARG   A NH1   
1096 N  NH2   . ARG   A 138 ? 0.3946 0.2932 0.4906 0.0310  0.1245  0.0202  135 ARG   A NH2   
1097 N  N     . SER   A 139 ? 0.1784 0.1570 0.1375 -0.0036 0.0281  0.0295  136 SER   A N     
1098 C  CA    . SER   A 139 ? 0.2131 0.1774 0.1361 -0.0146 0.0383  0.0381  136 SER   A CA    
1099 C  C     . SER   A 139 ? 0.1892 0.1737 0.1400 -0.0195 0.0456  0.0248  136 SER   A C     
1100 O  O     . SER   A 139 ? 0.2086 0.2145 0.1961 0.0100  0.0775  0.0651  136 SER   A O     
1101 C  CB    . SER   A 139 ? 0.2210 0.2221 0.1235 -0.0028 0.0433  0.0465  136 SER   A CB    
1102 O  OG    . SER   A 139 ? 0.2686 0.2553 0.1740 -0.0184 0.0142  0.0307  136 SER   A OG    
1103 N  N     . TYR   A 140 ? 0.1705 0.1769 0.1298 0.0053  0.0641  0.0266  137 TYR   A N     
1104 C  CA    . TYR   A 140 ? 0.1860 0.1938 0.1514 0.0151  0.0534  0.0000  137 TYR   A CA    
1105 C  C     . TYR   A 140 ? 0.1906 0.1837 0.1410 0.0063  0.0433  0.0271  137 TYR   A C     
1106 O  O     . TYR   A 140 ? 0.1775 0.2070 0.2078 0.0092  0.0308  0.0162  137 TYR   A O     
1107 C  CB    . TYR   A 140 ? 0.2023 0.1894 0.1547 0.0150  0.0444  0.0079  137 TYR   A CB    
1108 C  CG    . TYR   A 140 ? 0.1822 0.2189 0.1528 0.0320  0.0458  -0.0027 137 TYR   A CG    
1109 C  CD1   . TYR   A 140 ? 0.2718 0.1963 0.1535 0.0257  0.0275  -0.0024 137 TYR   A CD1   
1110 C  CD2   . TYR   A 140 ? 0.2158 0.2198 0.1892 0.0210  0.0344  0.0045  137 TYR   A CD2   
1111 C  CE1   . TYR   A 140 ? 0.3039 0.2599 0.1431 0.0351  0.0026  -0.0057 137 TYR   A CE1   
1112 C  CE2   . TYR   A 140 ? 0.2073 0.2643 0.2262 0.0059  0.0401  -0.0337 137 TYR   A CE2   
1113 C  CZ    . TYR   A 140 ? 0.2436 0.2398 0.1931 0.0609  -0.0158 -0.0391 137 TYR   A CZ    
1114 O  OH    . TYR   A 140 ? 0.2709 0.3253 0.2409 0.0652  -0.0474 -0.0795 137 TYR   A OH    
1115 N  N     . GLY   A 141 ? 0.1574 0.1591 0.1584 -0.0171 0.0495  0.0194  138 GLY   A N     
1116 C  CA    . GLY   A 141 ? 0.1521 0.1724 0.1734 -0.0187 0.0337  0.0276  138 GLY   A CA    
1117 C  C     . GLY   A 141 ? 0.1279 0.1751 0.1537 -0.0183 0.0227  0.0229  138 GLY   A C     
1118 O  O     . GLY   A 141 ? 0.1374 0.1857 0.1831 -0.0234 0.0000  0.0329  138 GLY   A O     
1119 N  N     . ILE   A 142 ? 0.1222 0.1502 0.1469 -0.0076 0.0451  0.0283  139 ILE   A N     
1120 C  CA    . ILE   A 142 ? 0.1153 0.1420 0.1210 -0.0090 0.0320  0.0159  139 ILE   A CA    
1121 C  C     . ILE   A 142 ? 0.1074 0.1237 0.1261 -0.0110 0.0272  0.0090  139 ILE   A C     
1122 O  O     . ILE   A 142 ? 0.1191 0.1367 0.1354 0.0023  0.0162  0.0118  139 ILE   A O     
1123 C  CB    . ILE   A 142 ? 0.1495 0.1390 0.1124 -0.0018 0.0282  0.0149  139 ILE   A CB    
1124 C  CG1   . ILE   A 142 ? 0.1619 0.1533 0.0893 -0.0138 0.0309  0.0009  139 ILE   A CG1   
1125 C  CG2   . ILE   A 142 ? 0.1397 0.1765 0.1338 0.0017  0.0285  0.0099  139 ILE   A CG2   
1126 C  CD1   . ILE   A 142 ? 0.1789 0.1615 0.1051 -0.0191 0.0412  -0.0070 139 ILE   A CD1   
1127 N  N     . PRO   A 143 ? 0.1101 0.1298 0.1197 -0.0096 0.0243  0.0061  140 PRO   A N     
1128 C  CA    . PRO   A 143 ? 0.1095 0.1175 0.1119 -0.0103 0.0209  -0.0005 140 PRO   A CA    
1129 C  C     . PRO   A 143 ? 0.1048 0.1239 0.0965 0.0026  0.0176  -0.0017 140 PRO   A C     
1130 O  O     . PRO   A 143 ? 0.1067 0.1316 0.1120 -0.0077 0.0207  -0.0131 140 PRO   A O     
1131 C  CB    . PRO   A 143 ? 0.1318 0.1339 0.1063 -0.0141 0.0076  -0.0055 140 PRO   A CB    
1132 C  CG    . PRO   A 143 ? 0.1347 0.1418 0.1188 -0.0101 0.0155  0.0115  140 PRO   A CG    
1133 C  CD    . PRO   A 143 ? 0.1159 0.1312 0.1177 -0.0110 0.0098  -0.0007 140 PRO   A CD    
1134 N  N     . PHE   A 144 ? 0.1046 0.1083 0.1012 -0.0007 0.0209  -0.0066 141 PHE   A N     
1135 C  CA    . PHE   A 144 ? 0.1063 0.1221 0.0822 0.0026  0.0166  -0.0068 141 PHE   A CA    
1136 C  C     . PHE   A 144 ? 0.1049 0.1097 0.0846 0.0138  0.0157  -0.0091 141 PHE   A C     
1137 O  O     . PHE   A 144 ? 0.1324 0.1141 0.0921 0.0010  0.0250  -0.0168 141 PHE   A O     
1138 C  CB    . PHE   A 144 ? 0.1153 0.1466 0.0993 0.0048  0.0101  0.0089  141 PHE   A CB    
1139 C  CG    . PHE   A 144 ? 0.1101 0.1445 0.0813 0.0156  0.0069  0.0152  141 PHE   A CG    
1140 C  CD1   . PHE   A 144 ? 0.1182 0.1527 0.0956 0.0167  0.0034  0.0100  141 PHE   A CD1   
1141 C  CD2   . PHE   A 144 ? 0.1294 0.1433 0.1319 0.0171  0.0201  0.0066  141 PHE   A CD2   
1142 C  CE1   . PHE   A 144 ? 0.1397 0.1548 0.1160 -0.0003 -0.0149 0.0091  141 PHE   A CE1   
1143 C  CE2   . PHE   A 144 ? 0.1250 0.1932 0.1100 0.0219  0.0049  0.0098  141 PHE   A CE2   
1144 C  CZ    . PHE   A 144 ? 0.1258 0.1973 0.1025 -0.0020 -0.0023 0.0107  141 PHE   A CZ    
1145 N  N     . ILE   A 145 ? 0.1015 0.1189 0.0805 -0.0014 0.0125  -0.0094 142 ILE   A N     
1146 C  CA    . ILE   A 145 ? 0.0944 0.1224 0.0873 0.0000  0.0082  -0.0070 142 ILE   A CA    
1147 C  C     . ILE   A 145 ? 0.0971 0.1185 0.0742 0.0050  0.0038  -0.0081 142 ILE   A C     
1148 O  O     . ILE   A 145 ? 0.1162 0.1408 0.0880 0.0025  0.0167  -0.0192 142 ILE   A O     
1149 C  CB    . ILE   A 145 ? 0.1157 0.1185 0.0868 0.0067  0.0067  0.0041  142 ILE   A CB    
1150 C  CG1   . ILE   A 145 ? 0.1170 0.1522 0.1090 -0.0035 -0.0013 -0.0032 142 ILE   A CG1   
1151 C  CG2   . ILE   A 145 ? 0.1186 0.1209 0.1002 0.0065  0.0056  0.0058  142 ILE   A CG2   
1152 C  CD1   . ILE   A 145 ? 0.1360 0.1479 0.1221 0.0082  -0.0078 -0.0019 142 ILE   A CD1   
1153 N  N     . GLU   A 146 ? 0.0965 0.1114 0.0931 -0.0044 0.0175  -0.0100 143 GLU   A N     
1154 C  CA    . GLU   A 146 ? 0.1035 0.1246 0.0825 -0.0108 0.0041  -0.0039 143 GLU   A CA    
1155 C  C     . GLU   A 146 ? 0.1013 0.1333 0.0731 -0.0033 0.0015  -0.0103 143 GLU   A C     
1156 O  O     . GLU   A 146 ? 0.1272 0.1281 0.0794 -0.0232 0.0163  -0.0145 143 GLU   A O     
1157 C  CB    . GLU   A 146 ? 0.1116 0.1428 0.0951 -0.0029 -0.0002 0.0019  143 GLU   A CB    
1158 C  CG    . GLU   A 146 ? 0.1217 0.1686 0.1031 -0.0026 -0.0002 0.0133  143 GLU   A CG    
1159 C  CD    . GLU   A 146 ? 0.1248 0.2119 0.1309 0.0062  0.0008  0.0348  143 GLU   A CD    
1160 O  OE1   . GLU   A 146 ? 0.1290 0.3750 0.1670 0.0482  0.0199  0.0718  143 GLU   A OE1   
1161 O  OE2   . GLU   A 146 ? 0.1329 0.2510 0.1273 0.0174  -0.0104 0.0383  143 GLU   A OE2   
1162 N  N     . THR   A 147 ? 0.1018 0.1233 0.0762 0.0012  -0.0001 -0.0095 144 THR   A N     
1163 C  CA    . THR   A 147 ? 0.1182 0.1383 0.0595 -0.0166 0.0046  -0.0082 144 THR   A CA    
1164 C  C     . THR   A 147 ? 0.1216 0.1391 0.0723 -0.0194 -0.0049 -0.0159 144 THR   A C     
1165 O  O     . THR   A 147 ? 0.1085 0.1649 0.0761 -0.0194 0.0004  -0.0045 144 THR   A O     
1166 C  CB    . THR   A 147 ? 0.1294 0.1249 0.0716 -0.0230 -0.0025 -0.0073 144 THR   A CB    
1167 O  OG1   . THR   A 147 ? 0.1311 0.1334 0.0648 -0.0142 -0.0088 -0.0021 144 THR   A OG1   
1168 C  CG2   . THR   A 147 ? 0.1350 0.1232 0.0883 -0.0235 -0.0165 -0.0059 144 THR   A CG2   
1169 N  N     . SER   A 148 ? 0.1240 0.1348 0.0759 -0.0295 -0.0058 -0.0113 145 SER   A N     
1170 C  CA    . SER   A 148 ? 0.1224 0.1585 0.0987 -0.0375 -0.0059 -0.0244 145 SER   A CA    
1171 C  C     . SER   A 148 ? 0.1644 0.1495 0.0921 -0.0567 0.0039  -0.0046 145 SER   A C     
1172 O  O     . SER   A 148 ? 0.1819 0.1740 0.0848 -0.0566 0.0072  -0.0044 145 SER   A O     
1173 C  CB    . SER   A 148 ? 0.1190 0.1752 0.1141 -0.0381 0.0060  -0.0167 145 SER   A CB    
1174 O  OG    . SER   A 148 ? 0.1502 0.1996 0.1399 -0.0668 0.0235  -0.0127 145 SER   A OG    
1175 N  N     . ALA   A 149 ? 0.1910 0.1536 0.0886 -0.0267 -0.0139 -0.0100 146 ALA   A N     
1176 C  CA    . ALA   A 149 ? 0.2076 0.1507 0.1307 -0.0269 -0.0269 -0.0079 146 ALA   A CA    
1177 C  C     . ALA   A 149 ? 0.2475 0.1777 0.1389 -0.0502 -0.0230 -0.0092 146 ALA   A C     
1178 O  O     . ALA   A 149 ? 0.2858 0.1804 0.1766 -0.0378 -0.0136 0.0186  146 ALA   A O     
1179 C  CB    . ALA   A 149 ? 0.2385 0.1548 0.1193 -0.0446 -0.0237 -0.0169 146 ALA   A CB    
1180 N  N     . LYS   A 150 ? 0.2109 0.1690 0.1525 -0.0578 0.0026  -0.0037 147 LYS   A N     
1181 C  CA    . LYS   A 150 ? 0.2506 0.1867 0.1783 -0.0584 0.0333  0.0257  147 LYS   A CA    
1182 C  C     . LYS   A 150 ? 0.2277 0.2226 0.1652 -0.0353 0.0556  0.0264  147 LYS   A C     
1183 O  O     . LYS   A 150 ? 0.3372 0.2483 0.1718 -0.0406 0.0325  0.0500  147 LYS   A O     
1184 C  CB    . LYS   A 150 ? 0.2172 0.2176 0.2343 -0.0671 0.0302  0.0094  147 LYS   A CB    
1185 C  CG    . LYS   A 150 ? 0.2549 0.2322 0.2796 -0.0793 0.0486  0.0270  147 LYS   A CG    
1186 C  CD    . LYS   A 150 ? 0.2337 0.2882 0.3602 -0.0593 0.0250  0.0361  147 LYS   A CD    
1187 C  CE    . LYS   A 150 ? 0.2913 0.3267 0.4164 -0.0804 0.0553  0.0642  147 LYS   A CE    
1188 N  NZ    . LYS   A 150 ? 0.3648 0.4052 0.4513 -0.0730 -0.0231 0.0104  147 LYS   A NZ    
1189 N  N     . THR   A 151 ? 0.2294 0.2163 0.1470 -0.0476 0.0402  0.0289  148 THR   A N     
1190 C  CA    . THR   A 151 ? 0.2074 0.2583 0.1474 -0.0365 0.0350  0.0200  148 THR   A CA    
1191 C  C     . THR   A 151 ? 0.2156 0.2056 0.1416 -0.0148 0.0178  0.0076  148 THR   A C     
1192 O  O     . THR   A 151 ? 0.2465 0.2718 0.1462 -0.0505 0.0455  0.0026  148 THR   A O     
1193 C  CB    . THR   A 151 ? 0.2230 0.2802 0.1571 -0.0158 0.0579  0.0328  148 THR   A CB    
1194 O  OG1   . THR   A 151 ? 0.2440 0.2449 0.1599 -0.0204 0.0612  0.0007  148 THR   A OG1   
1195 C  CG2   . THR   A 151 ? 0.2073 0.2990 0.1956 -0.0173 0.0526  -0.0193 148 THR   A CG2   
1196 N  N     . ARG   A 152 ? 0.2061 0.1988 0.1433 -0.0040 0.0174  0.0450  149 ARG   A N     
1197 C  CA    . ARG   A 152 ? 0.2236 0.2207 0.1313 -0.0049 0.0160  0.0277  149 ARG   A CA    
1198 C  C     . ARG   A 152 ? 0.1730 0.2256 0.1210 0.0029  -0.0224 -0.0188 149 ARG   A C     
1199 O  O     . ARG   A 152 ? 0.1806 0.2371 0.1534 0.0126  -0.0352 0.0019  149 ARG   A O     
1200 C  CB    . ARG   A 152 ? 0.2749 0.3151 0.1443 0.0322  0.0250  0.0467  149 ARG   A CB    
1201 C  CG    . ARG   A 152 ? 0.3617 0.3514 0.2856 -0.0217 0.0139  0.0237  149 ARG   A CG    
1202 C  CD    . ARG   A 152 ? 0.4719 0.3320 0.2924 -0.0251 -0.0189 0.0390  149 ARG   A CD    
1203 N  NE    . ARG   A 152 ? 0.3853 0.3189 0.4543 -0.0401 0.0356  0.1555  149 ARG   A NE    
1204 C  CZ    . ARG   A 152 ? 0.4299 0.3931 0.2764 -0.0327 0.0551  0.0856  149 ARG   A CZ    
1205 N  NH1   . ARG   A 152 ? 0.3852 0.3756 0.1819 -0.0579 -0.0070 0.0738  149 ARG   A NH1   
1206 N  NH2   . ARG   A 152 ? 0.4091 0.4516 0.3292 -0.0897 0.0411  0.1294  149 ARG   A NH2   
1207 N  N     . GLN   A 153 ? 0.1228 0.1847 0.1150 -0.0335 -0.0061 -0.0117 150 GLN   A N     
1208 C  CA    . GLN   A 153 ? 0.1318 0.1912 0.0950 -0.0117 0.0278  -0.0158 150 GLN   A CA    
1209 C  C     . GLN   A 153 ? 0.1120 0.1586 0.0876 -0.0155 0.0041  -0.0001 150 GLN   A C     
1210 O  O     . GLN   A 153 ? 0.1195 0.1523 0.0859 -0.0229 0.0085  -0.0005 150 GLN   A O     
1211 C  CB    . GLN   A 153 ? 0.1148 0.1973 0.1158 -0.0185 0.0157  -0.0113 150 GLN   A CB    
1212 C  CG    . GLN   A 153 ? 0.1559 0.1956 0.1920 0.0028  0.0140  -0.0064 150 GLN   A CG    
1213 C  CD    . GLN   A 153 ? 0.1910 0.2037 0.1937 0.0251  0.0225  -0.0278 150 GLN   A CD    
1214 O  OE1   . GLN   A 153 ? 0.2082 0.2747 0.2078 -0.0194 0.0558  -0.0058 150 GLN   A OE1   
1215 N  NE2   . GLN   A 153 ? 0.2332 0.2045 0.2156 0.0382  0.0156  -0.0474 150 GLN   A NE2   
1216 N  N     . ARG   A 154 ? 0.1146 0.1466 0.0731 -0.0132 0.0111  -0.0039 151 ARG   A N     
1217 C  CA    . ARG   A 154 ? 0.1070 0.1371 0.0868 -0.0171 -0.0079 -0.0038 151 ARG   A CA    
1218 C  C     . ARG   A 154 ? 0.0949 0.1395 0.0927 -0.0178 -0.0101 -0.0052 151 ARG   A C     
1219 O  O     . ARG   A 154 ? 0.1092 0.1317 0.0954 -0.0130 -0.0025 0.0015  151 ARG   A O     
1220 C  CB    . ARG   A 154 ? 0.1207 0.1393 0.0923 -0.0079 -0.0017 -0.0020 151 ARG   A CB    
1221 C  CG    . ARG   A 154 ? 0.1445 0.1563 0.0975 0.0146  0.0020  -0.0012 151 ARG   A CG    
1222 C  CD    . ARG   A 154 ? 0.1546 0.1563 0.1041 0.0364  0.0051  0.0064  151 ARG   A CD    
1223 N  NE    . ARG   A 154 ? 0.1847 0.1348 0.1399 0.0093  -0.0119 -0.0033 151 ARG   A NE    
1224 C  CZ    . ARG   A 154 ? 0.1724 0.1197 0.1494 0.0202  0.0198  -0.0296 151 ARG   A CZ    
1225 N  NH1   . ARG   A 154 ? 0.1926 0.1489 0.1932 -0.0096 0.0025  -0.0166 151 ARG   A NH1   
1226 N  NH2   . ARG   A 154 ? 0.1563 0.1290 0.1467 0.0075  0.0197  -0.0216 151 ARG   A NH2   
1227 N  N     . VAL   A 155 ? 0.1177 0.1402 0.0866 -0.0175 0.0148  -0.0074 152 VAL   A N     
1228 C  CA    . VAL   A 155 ? 0.1384 0.1391 0.1215 -0.0084 0.0020  -0.0161 152 VAL   A CA    
1229 C  C     . VAL   A 155 ? 0.1381 0.1135 0.1092 0.0032  -0.0033 -0.0072 152 VAL   A C     
1230 O  O     . VAL   A 155 ? 0.1377 0.1220 0.1108 0.0009  -0.0049 -0.0029 152 VAL   A O     
1231 C  CB    . VAL   A 155 ? 0.1769 0.1430 0.1496 -0.0227 -0.0083 -0.0098 152 VAL   A CB    
1232 C  CG1   . VAL   A 155 ? 0.2179 0.1377 0.1977 -0.0249 0.0134  -0.0237 152 VAL   A CG1   
1233 C  CG2   . VAL   A 155 ? 0.1728 0.1686 0.1879 -0.0254 -0.0089 -0.0160 152 VAL   A CG2   
1234 N  N     . GLU   A 156 ? 0.1496 0.1348 0.1113 -0.0042 0.0085  -0.0101 153 GLU   A N     
1235 C  CA    . GLU   A 156 ? 0.1537 0.1735 0.1033 0.0000  -0.0019 0.0009  153 GLU   A CA    
1236 C  C     . GLU   A 156 ? 0.1329 0.1724 0.0832 -0.0008 -0.0175 0.0038  153 GLU   A C     
1237 O  O     . GLU   A 156 ? 0.1343 0.1881 0.0987 0.0002  -0.0078 0.0044  153 GLU   A O     
1238 C  CB    . GLU   A 156 ? 0.1962 0.2093 0.1041 0.0275  -0.0001 0.0280  153 GLU   A CB    
1239 C  CG    . GLU   A 156 ? 0.2812 0.1998 0.1593 0.0186  -0.0193 0.0412  153 GLU   A CG    
1240 C  CD    . GLU   A 156 ? 0.3447 0.3504 0.1735 -0.0143 -0.0179 0.0565  153 GLU   A CD    
1241 O  OE1   . GLU   A 156 ? 0.4930 0.4867 0.2007 0.0363  0.0411  -0.0069 153 GLU   A OE1   
1242 O  OE2   . GLU   A 156 ? 0.5391 0.3584 0.2472 -0.0696 -0.0599 0.0743  153 GLU   A OE2   
1243 N  N     . ASP   A 157 ? 0.1305 0.1649 0.0864 -0.0270 -0.0178 -0.0012 154 ASP   A N     
1244 C  CA    . ASP   A 157 ? 0.1284 0.1441 0.0949 -0.0098 -0.0132 -0.0281 154 ASP   A CA    
1245 C  C     . ASP   A 157 ? 0.1091 0.1182 0.1080 -0.0080 -0.0037 -0.0249 154 ASP   A C     
1246 O  O     . ASP   A 157 ? 0.1078 0.1255 0.1228 -0.0061 -0.0108 -0.0264 154 ASP   A O     
1247 C  CB    . ASP   A 157 ? 0.1575 0.1965 0.1162 0.0287  -0.0030 -0.0551 154 ASP   A CB    
1248 C  CG    . ASP   A 157 ? 0.1671 0.2242 0.2773 0.0185  -0.0608 -0.0375 154 ASP   A CG    
1249 O  OD1   . ASP   A 157 ? 0.2207 0.2771 0.3463 -0.0078 0.0052  -0.0186 154 ASP   A OD1   
1250 O  OD2   . ASP   A 157 ? 0.2935 0.3158 0.2955 0.1546  -0.1588 -0.1689 154 ASP   A OD2   
1251 N  N     . ALA   A 158 ? 0.1053 0.1165 0.0913 -0.0147 -0.0030 -0.0060 155 ALA   A N     
1252 C  CA    . ALA   A 158 ? 0.1146 0.1072 0.0913 -0.0066 -0.0018 -0.0023 155 ALA   A CA    
1253 C  C     . ALA   A 158 ? 0.1209 0.1112 0.0622 -0.0062 -0.0045 -0.0107 155 ALA   A C     
1254 O  O     . ALA   A 158 ? 0.1217 0.1066 0.0994 -0.0009 -0.0088 -0.0101 155 ALA   A O     
1255 C  CB    . ALA   A 158 ? 0.1294 0.1333 0.0885 0.0013  -0.0242 -0.0036 155 ALA   A CB    
1256 N  N     . PHE   A 159 ? 0.1211 0.1108 0.0857 -0.0077 -0.0077 -0.0087 156 PHE   A N     
1257 C  CA    . PHE   A 159 ? 0.1211 0.1252 0.0847 -0.0017 -0.0120 -0.0144 156 PHE   A CA    
1258 C  C     . PHE   A 159 ? 0.1226 0.1165 0.0862 0.0021  -0.0095 -0.0121 156 PHE   A C     
1259 O  O     . PHE   A 159 ? 0.1277 0.1194 0.0981 0.0100  -0.0083 -0.0058 156 PHE   A O     
1260 C  CB    . PHE   A 159 ? 0.1404 0.1268 0.1008 -0.0008 -0.0296 -0.0074 156 PHE   A CB    
1261 C  CG    . PHE   A 159 ? 0.1517 0.1068 0.1127 0.0092  -0.0250 -0.0134 156 PHE   A CG    
1262 C  CD1   . PHE   A 159 ? 0.1538 0.1106 0.1479 0.0084  -0.0115 -0.0238 156 PHE   A CD1   
1263 C  CD2   . PHE   A 159 ? 0.1534 0.1112 0.1143 0.0028  -0.0217 -0.0152 156 PHE   A CD2   
1264 C  CE1   . PHE   A 159 ? 0.1818 0.1226 0.1381 0.0211  -0.0116 -0.0382 156 PHE   A CE1   
1265 C  CE2   . PHE   A 159 ? 0.1703 0.1297 0.1309 -0.0072 -0.0203 -0.0278 156 PHE   A CE2   
1266 C  CZ    . PHE   A 159 ? 0.1884 0.1055 0.1349 0.0080  -0.0259 -0.0308 156 PHE   A CZ    
1267 N  N     . TYR   A 160 ? 0.1163 0.1076 0.0853 -0.0005 -0.0180 -0.0200 157 TYR   A N     
1268 C  CA    . TYR   A 160 ? 0.1069 0.1308 0.0709 0.0032  -0.0221 -0.0124 157 TYR   A CA    
1269 C  C     . TYR   A 160 ? 0.1136 0.1114 0.0760 0.0042  -0.0144 -0.0232 157 TYR   A C     
1270 O  O     . TYR   A 160 ? 0.1132 0.1302 0.0977 -0.0029 -0.0203 -0.0203 157 TYR   A O     
1271 C  CB    . TYR   A 160 ? 0.1181 0.1609 0.0772 -0.0166 -0.0085 -0.0100 157 TYR   A CB    
1272 C  CG    . TYR   A 160 ? 0.1290 0.1862 0.1005 0.0033  -0.0307 0.0277  157 TYR   A CG    
1273 C  CD1   . TYR   A 160 ? 0.1725 0.1936 0.1100 0.0057  -0.0239 0.0323  157 TYR   A CD1   
1274 C  CD2   . TYR   A 160 ? 0.1847 0.2250 0.1128 0.0313  0.0063  0.0459  157 TYR   A CD2   
1275 C  CE1   . TYR   A 160 ? 0.2281 0.1894 0.1828 0.0129  -0.0337 0.0630  157 TYR   A CE1   
1276 C  CE2   . TYR   A 160 ? 0.2784 0.2530 0.1407 0.0191  0.0362  0.0769  157 TYR   A CE2   
1277 C  CZ    . TYR   A 160 ? 0.2991 0.2337 0.1919 -0.0211 0.0238  0.0767  157 TYR   A CZ    
1278 O  OH    . TYR   A 160 ? 0.3721 0.2672 0.2510 0.0066  0.0447  0.1261  157 TYR   A OH    
1279 N  N     . THR   A 161 ? 0.1105 0.1082 0.0888 -0.0026 -0.0101 -0.0099 158 THR   A N     
1280 C  CA    . THR   A 161 ? 0.1178 0.1066 0.0761 -0.0042 -0.0134 -0.0175 158 THR   A CA    
1281 C  C     . THR   A 161 ? 0.1062 0.1122 0.0876 0.0022  -0.0231 -0.0228 158 THR   A C     
1282 O  O     . THR   A 161 ? 0.1121 0.1197 0.1092 -0.0116 -0.0046 -0.0224 158 THR   A O     
1283 C  CB    . THR   A 161 ? 0.1166 0.1142 0.0932 0.0015  -0.0102 -0.0165 158 THR   A CB    
1284 O  OG1   . THR   A 161 ? 0.1259 0.1211 0.0971 0.0152  -0.0052 -0.0175 158 THR   A OG1   
1285 C  CG2   . THR   A 161 ? 0.1217 0.1291 0.1110 0.0058  0.0090  -0.0042 158 THR   A CG2   
1286 N  N     . LEU   A 162 ? 0.1055 0.1117 0.0874 -0.0003 -0.0039 -0.0254 159 LEU   A N     
1287 C  CA    . LEU   A 162 ? 0.1046 0.1175 0.0861 0.0026  -0.0029 -0.0197 159 LEU   A CA    
1288 C  C     . LEU   A 162 ? 0.1096 0.1286 0.0793 0.0085  -0.0019 -0.0182 159 LEU   A C     
1289 O  O     . LEU   A 162 ? 0.1092 0.1340 0.1022 -0.0003 -0.0027 -0.0335 159 LEU   A O     
1290 C  CB    . LEU   A 162 ? 0.1090 0.1117 0.0863 0.0058  -0.0144 -0.0159 159 LEU   A CB    
1291 C  CG    . LEU   A 162 ? 0.1111 0.1253 0.0868 0.0051  -0.0101 -0.0194 159 LEU   A CG    
1292 C  CD1   . LEU   A 162 ? 0.1241 0.1280 0.0943 0.0084  -0.0131 -0.0139 159 LEU   A CD1   
1293 C  CD2   . LEU   A 162 ? 0.1208 0.1139 0.1228 0.0063  -0.0128 -0.0241 159 LEU   A CD2   
1294 N  N     . VAL   A 163 ? 0.1110 0.1230 0.0927 0.0173  -0.0156 -0.0146 160 VAL   A N     
1295 C  CA    . VAL   A 163 ? 0.1089 0.1311 0.1070 0.0191  -0.0225 -0.0312 160 VAL   A CA    
1296 C  C     . VAL   A 163 ? 0.1046 0.1432 0.0803 0.0074  -0.0308 -0.0257 160 VAL   A C     
1297 O  O     . VAL   A 163 ? 0.1026 0.1887 0.1021 0.0136  -0.0153 -0.0459 160 VAL   A O     
1298 C  CB    . VAL   A 163 ? 0.1232 0.1410 0.0981 0.0319  -0.0218 -0.0284 160 VAL   A CB    
1299 C  CG1   . VAL   A 163 ? 0.1455 0.1828 0.1053 0.0236  -0.0360 -0.0098 160 VAL   A CG1   
1300 C  CG2   . VAL   A 163 ? 0.1490 0.1421 0.1185 0.0260  -0.0304 -0.0221 160 VAL   A CG2   
1301 N  N     . ARG   A 164 ? 0.0992 0.1421 0.1030 -0.0020 -0.0069 -0.0290 161 ARG   A N     
1302 C  CA    . ARG   A 164 ? 0.0894 0.1551 0.1137 -0.0014 -0.0117 -0.0390 161 ARG   A CA    
1303 C  C     . ARG   A 164 ? 0.0977 0.1588 0.1325 -0.0066 -0.0047 -0.0270 161 ARG   A C     
1304 O  O     . ARG   A 164 ? 0.1100 0.1677 0.1428 -0.0193 0.0084  -0.0463 161 ARG   A O     
1305 C  CB    . ARG   A 164 ? 0.1113 0.1411 0.0934 0.0017  -0.0043 -0.0330 161 ARG   A CB    
1306 C  CG    . ARG   A 164 ? 0.1070 0.1423 0.1067 -0.0084 0.0064  -0.0278 161 ARG   A CG    
1307 C  CD    . ARG   A 164 ? 0.1186 0.1524 0.1171 0.0035  0.0081  -0.0235 161 ARG   A CD    
1308 N  NE    . ARG   A 164 ? 0.1194 0.2062 0.1148 0.0262  0.0109  -0.0084 161 ARG   A NE    
1309 C  CZ    . ARG   A 164 ? 0.1475 0.2701 0.1229 0.0316  0.0197  -0.0455 161 ARG   A CZ    
1310 N  NH1   . ARG   A 164 ? 0.1417 0.3168 0.1361 0.0296  0.0127  -0.0477 161 ARG   A NH1   
1311 N  NH2   . ARG   A 164 ? 0.1888 0.3679 0.1303 0.0661  0.0266  -0.0648 161 ARG   A NH2   
1312 N  N     . GLU   A 165 ? 0.0936 0.1628 0.1190 -0.0178 0.0088  -0.0155 162 GLU   A N     
1313 C  CA    . GLU   A 165 ? 0.1089 0.1298 0.1168 -0.0228 0.0055  -0.0208 162 GLU   A CA    
1314 C  C     . GLU   A 165 ? 0.1124 0.1634 0.1075 -0.0116 0.0058  -0.0258 162 GLU   A C     
1315 O  O     . GLU   A 165 ? 0.1317 0.1734 0.1608 -0.0261 0.0271  -0.0433 162 GLU   A O     
1316 C  CB    . GLU   A 165 ? 0.1186 0.1550 0.1143 -0.0138 -0.0018 -0.0175 162 GLU   A CB    
1317 C  CG    . GLU   A 165 ? 0.1230 0.1680 0.1195 -0.0106 0.0061  -0.0189 162 GLU   A CG    
1318 C  CD    . GLU   A 165 ? 0.1560 0.1667 0.1667 -0.0048 0.0261  -0.0053 162 GLU   A CD    
1319 O  OE1   . GLU   A 165 ? 0.2200 0.1956 0.1577 -0.0514 0.0313  -0.0306 162 GLU   A OE1   
1320 O  OE2   . GLU   A 165 ? 0.2241 0.1876 0.1824 0.0083  0.0223  -0.0128 162 GLU   A OE2   
1321 N  N     . ILE   A 166 ? 0.0971 0.1731 0.0978 -0.0033 0.0058  -0.0237 163 ILE   A N     
1322 C  CA    . ILE   A 166 ? 0.0921 0.2076 0.1011 0.0014  0.0071  -0.0393 163 ILE   A CA    
1323 C  C     . ILE   A 166 ? 0.0991 0.2216 0.1032 0.0149  0.0070  -0.0556 163 ILE   A C     
1324 O  O     . ILE   A 166 ? 0.0984 0.2533 0.1269 0.0040  0.0127  -0.0695 163 ILE   A O     
1325 C  CB    . ILE   A 166 ? 0.1232 0.2078 0.0786 0.0245  -0.0063 -0.0099 163 ILE   A CB    
1326 C  CG1   . ILE   A 166 ? 0.1301 0.1974 0.0850 0.0330  -0.0057 -0.0274 163 ILE   A CG1   
1327 C  CG2   . ILE   A 166 ? 0.1318 0.2304 0.1041 0.0402  0.0015  -0.0344 163 ILE   A CG2   
1328 C  CD1   . ILE   A 166 ? 0.1493 0.1915 0.1085 0.0255  -0.0120 -0.0337 163 ILE   A CD1   
1329 N  N     . ARG   A 167 ? 0.1126 0.2292 0.0969 0.0086  -0.0028 -0.0500 164 ARG   A N     
1330 C  CA    . ARG   A 167 ? 0.1166 0.2390 0.0999 0.0141  0.0058  -0.0704 164 ARG   A CA    
1331 C  C     . ARG   A 167 ? 0.1329 0.2312 0.0940 -0.0072 0.0111  -0.0631 164 ARG   A C     
1332 O  O     . ARG   A 167 ? 0.1285 0.2835 0.1708 -0.0143 0.0215  -0.0831 164 ARG   A O     
1333 C  CB    . ARG   A 167 ? 0.1240 0.2119 0.1076 -0.0103 0.0074  -0.0400 164 ARG   A CB    
1334 C  CG    . ARG   A 167 ? 0.1713 0.2395 0.1360 -0.0300 -0.0099 -0.0426 164 ARG   A CG    
1335 C  CD    . ARG   A 167 ? 0.2027 0.2335 0.1318 -0.0295 0.0164  -0.0105 164 ARG   A CD    
1336 N  NE    . ARG   A 167 ? 0.1745 0.1989 0.1453 0.0139  0.0294  -0.0104 164 ARG   A NE    
1337 C  CZ    . ARG   A 167 ? 0.1566 0.1950 0.0926 0.0007  0.0045  -0.0145 164 ARG   A CZ    
1338 N  NH1   . ARG   A 167 ? 0.1606 0.1876 0.1323 0.0115  0.0070  0.0044  164 ARG   A NH1   
1339 N  NH2   . ARG   A 167 ? 0.1284 0.2019 0.1306 -0.0082 -0.0124 -0.0087 164 ARG   A NH2   
1340 N  N     . GLN   A 168 ? 0.1297 0.2255 0.1147 -0.0143 0.0147  -0.0559 165 GLN   A N     
1341 C  CA    . GLN   A 168 ? 0.1906 0.2425 0.1477 -0.0068 0.0417  -0.0519 165 GLN   A CA    
1342 C  C     . GLN   A 168 ? 0.1397 0.1925 0.1395 -0.0232 0.0248  -0.0412 165 GLN   A C     
1343 O  O     . GLN   A 168 ? 0.1587 0.2405 0.2071 -0.0556 0.0508  -0.0862 165 GLN   A O     
1344 C  CB    . GLN   A 168 ? 0.1950 0.2340 0.2234 -0.0183 0.0025  -0.0707 165 GLN   A CB    
1345 C  CG    . GLN   A 168 ? 0.2349 0.2579 0.2238 -0.0374 0.0368  -0.0358 165 GLN   A CG    
1346 C  CD    . GLN   A 168 ? 0.2805 0.2919 0.2487 0.0293  0.0509  -0.0137 165 GLN   A CD    
1347 O  OE1   . GLN   A 168 ? 0.3809 0.3741 0.2785 0.1090  0.0711  0.0357  165 GLN   A OE1   
1348 N  NE2   . GLN   A 168 ? 0.3437 0.2789 0.2933 -0.0235 0.0843  -0.0101 165 GLN   A NE2   
1349 N  N     . TYR   A 169 ? 0.1214 0.1990 0.1748 -0.0197 0.0366  -0.0718 166 TYR   A N     
1350 C  CA    . TYR   A 169 ? 0.1312 0.2262 0.1650 -0.0250 0.0257  -0.0577 166 TYR   A CA    
1351 C  C     . TYR   A 169 ? 0.1089 0.2158 0.1613 -0.0340 0.0268  -0.0541 166 TYR   A C     
1352 O  O     . TYR   A 169 ? 0.1460 0.2771 0.1615 -0.0353 0.0463  -0.0397 166 TYR   A O     
1353 C  CB    . TYR   A 169 ? 0.1261 0.2443 0.1681 -0.0128 0.0139  -0.0620 166 TYR   A CB    
1354 C  CG    . TYR   A 169 ? 0.1664 0.2392 0.1564 -0.0135 0.0196  -0.0433 166 TYR   A CG    
1355 C  CD1   . TYR   A 169 ? 0.2113 0.3859 0.2356 0.0042  0.0372  0.0771  166 TYR   A CD1   
1356 C  CD2   . TYR   A 169 ? 0.1642 0.2566 0.2114 -0.0126 0.0042  -0.0127 166 TYR   A CD2   
1357 C  CE1   . TYR   A 169 ? 0.1754 0.3935 0.2586 -0.0354 0.0084  0.0702  166 TYR   A CE1   
1358 C  CE2   . TYR   A 169 ? 0.1649 0.2724 0.2357 -0.0333 -0.0005 0.0221  166 TYR   A CE2   
1359 C  CZ    . TYR   A 169 ? 0.1805 0.4117 0.2323 -0.0400 0.0001  0.0728  166 TYR   A CZ    
1360 O  OH    . TYR   A 169 ? 0.2012 0.4886 0.2794 -0.0171 0.0003  0.1018  166 TYR   A OH    
1361 N  N     . ARG   A 170 ? 0.1109 0.2640 0.1574 -0.0116 0.0176  -0.0549 167 ARG   A N     
1362 C  CA    . ARG   A 170 ? 0.1039 0.2902 0.1381 -0.0134 0.0241  -0.0529 167 ARG   A CA    
1363 C  C     . ARG   A 170 ? 0.1252 0.2849 0.1564 -0.0184 0.0415  -0.0644 167 ARG   A C     
1364 O  O     . ARG   A 170 ? 0.1254 0.2869 0.1471 -0.0026 0.0345  -0.0574 167 ARG   A O     
1365 C  CB    . ARG   A 170 ? 0.1411 0.2741 0.1639 -0.0009 0.0157  -0.0472 167 ARG   A CB    
1366 C  CG    . ARG   A 170 ? 0.1563 0.2564 0.1807 0.0219  -0.0003 -0.0371 167 ARG   A CG    
1367 C  CD    . ARG   A 170 ? 0.1638 0.2404 0.1651 0.0278  0.0192  -0.0514 167 ARG   A CD    
1368 N  NE    . ARG   A 170 ? 0.1852 0.2366 0.2131 0.0064  0.0009  -0.0074 167 ARG   A NE    
1369 C  CZ    . ARG   A 170 ? 0.2203 0.2675 0.1599 0.0260  -0.0194 0.0298  167 ARG   A CZ    
1370 N  NH1   . ARG   A 170 ? 0.2093 0.3252 0.1846 0.0121  0.0096  0.0000  167 ARG   A NH1   
1371 N  NH2   . ARG   A 170 ? 0.2905 0.3223 0.2241 0.0306  -0.0797 -0.0282 167 ARG   A NH2   
1372 N  N     . LEU   A 171 ? 0.1294 0.3069 0.1976 -0.0280 0.0249  -0.1239 168 LEU   A N     
1373 C  CA    . LEU   A 171 ? 0.1494 0.2980 0.2166 -0.0143 -0.0312 -0.1064 168 LEU   A CA    
1374 C  C     . LEU   A 171 ? 0.1851 0.2642 0.2884 -0.0549 0.0085  -0.0884 168 LEU   A C     
1375 O  O     . LEU   A 171 ? 0.2092 0.2707 0.4452 -0.0542 -0.0422 -0.0811 168 LEU   A O     
1376 C  CB    . LEU   A 171 ? 0.1843 0.3317 0.2366 0.0077  -0.0234 -0.1141 168 LEU   A CB    
1377 C  CG    . LEU   A 171 ? 0.2569 0.3634 0.2226 -0.0254 -0.0134 -0.1140 168 LEU   A CG    
1378 C  CD1   . LEU   A 171 ? 0.3498 0.4206 0.1492 -0.0397 0.0516  -0.0558 168 LEU   A CD1   
1379 C  CD2   . LEU   A 171 ? 0.2709 0.3562 0.3032 0.0094  -0.0198 -0.0839 168 LEU   A CD2   
1380 N  N     . LYS   A 172 ? 0.2833 0.3176 0.2806 -0.0659 0.0236  -0.0801 169 LYS   A N     
1381 C  CA    . LYS   A 172 ? 0.3444 0.2388 0.3407 -0.0099 0.0253  -0.0647 169 LYS   A CA    
1382 C  C     . LYS   A 172 ? 0.2664 0.2739 0.4192 -0.0130 0.0891  -0.0246 169 LYS   A C     
1383 O  O     . LYS   A 172 ? 0.4379 0.2823 0.3797 0.0348  0.2073  -0.0441 169 LYS   A O     
1384 C  CB    . LYS   A 172 ? 0.3960 0.3494 0.4641 0.0420  0.0380  0.0214  169 LYS   A CB    
1385 C  CG    . LYS   A 172 ? 0.4773 0.4385 0.4706 0.0388  0.0309  0.0601  169 LYS   A CG    
1386 C  CD    . LYS   A 172 ? 0.5597 0.4764 0.4509 0.0619  0.0263  0.0150  169 LYS   A CD    
1387 C  CE    . LYS   A 172 ? 0.6195 0.5618 0.4958 0.1213  0.0480  0.0861  169 LYS   A CE    
1388 N  NZ    . LYS   A 172 ? 0.6242 0.7216 0.5645 0.0232  0.0564  0.0612  169 LYS   A NZ    
1389 O  OXT   . LYS   A 172 ? 0.1481 0.2712 0.2682 -0.0017 0.0431  -0.0658 169 LYS   A OXT   
1390 P  PB    . GDP   B .   ? 0.1709 0.1691 0.1417 -0.0388 -0.0192 -0.0477 201 GDP   A PB    
1391 O  O1B   . GDP   B .   ? 0.1914 0.1486 0.1424 -0.0332 -0.0115 -0.0380 201 GDP   A O1B   
1392 O  O2B   . GDP   B .   ? 0.1351 0.1791 0.1402 -0.0339 -0.0102 -0.0188 201 GDP   A O2B   
1393 O  O3B   . GDP   B .   ? 0.1886 0.1829 0.1380 -0.0233 -0.0200 -0.0534 201 GDP   A O3B   
1394 O  O3A   . GDP   B .   ? 0.1471 0.1706 0.1602 -0.0179 -0.0282 -0.0557 201 GDP   A O3A   
1395 P  PA    . GDP   B .   ? 0.1923 0.1720 0.1608 -0.0420 -0.0022 -0.0393 201 GDP   A PA    
1396 O  O1A   . GDP   B .   ? 0.2144 0.1930 0.1441 -0.0341 -0.0160 -0.0098 201 GDP   A O1A   
1397 O  O2A   . GDP   B .   ? 0.2067 0.1677 0.2479 -0.0494 0.0262  -0.0396 201 GDP   A O2A   
1398 O  "O5'" . GDP   B .   ? 0.2162 0.1686 0.1083 -0.0709 -0.0086 -0.0359 201 GDP   A "O5'" 
1399 C  "C5'" . GDP   B .   ? 0.2061 0.1807 0.1391 -0.0463 -0.0214 -0.0628 201 GDP   A "C5'" 
1400 C  "C4'" . GDP   B .   ? 0.2083 0.2066 0.1742 -0.0576 -0.0135 -0.0630 201 GDP   A "C4'" 
1401 O  "O4'" . GDP   B .   ? 0.1800 0.1943 0.1542 -0.0575 -0.0158 -0.0397 201 GDP   A "O4'" 
1402 C  "C3'" . GDP   B .   ? 0.1957 0.2031 0.1941 -0.0534 -0.0276 -0.0483 201 GDP   A "C3'" 
1403 O  "O3'" . GDP   B .   ? 0.1884 0.2495 0.2301 -0.0611 -0.0084 -0.0816 201 GDP   A "O3'" 
1404 C  "C2'" . GDP   B .   ? 0.2027 0.1952 0.1755 -0.0758 0.0028  -0.0371 201 GDP   A "C2'" 
1405 O  "O2'" . GDP   B .   ? 0.2933 0.2253 0.2183 -0.1134 0.0186  -0.0192 201 GDP   A "O2'" 
1406 C  "C1'" . GDP   B .   ? 0.1742 0.2024 0.1492 -0.0616 -0.0097 -0.0498 201 GDP   A "C1'" 
1407 N  N9    . GDP   B .   ? 0.1604 0.1723 0.1568 -0.0556 0.0104  -0.0421 201 GDP   A N9    
1408 C  C8    . GDP   B .   ? 0.1535 0.1593 0.1454 -0.0442 0.0150  -0.0249 201 GDP   A C8    
1409 N  N7    . GDP   B .   ? 0.1632 0.1647 0.1302 -0.0392 0.0124  -0.0217 201 GDP   A N7    
1410 C  C5    . GDP   B .   ? 0.1516 0.1354 0.1257 -0.0410 -0.0013 -0.0077 201 GDP   A C5    
1411 C  C6    . GDP   B .   ? 0.1403 0.1648 0.1275 -0.0385 0.0196  -0.0126 201 GDP   A C6    
1412 O  O6    . GDP   B .   ? 0.1697 0.1759 0.1130 -0.0364 -0.0083 -0.0126 201 GDP   A O6    
1413 N  N1    . GDP   B .   ? 0.1363 0.1744 0.1355 -0.0323 0.0104  -0.0261 201 GDP   A N1    
1414 C  C2    . GDP   B .   ? 0.1584 0.1831 0.1587 -0.0494 0.0406  -0.0373 201 GDP   A C2    
1415 N  N2    . GDP   B .   ? 0.1582 0.2080 0.2164 -0.0391 0.0061  -0.0511 201 GDP   A N2    
1416 N  N3    . GDP   B .   ? 0.1458 0.1847 0.1477 -0.0324 0.0114  -0.0334 201 GDP   A N3    
1417 C  C4    . GDP   B .   ? 0.1317 0.1625 0.1536 -0.0475 0.0014  -0.0023 201 GDP   A C4    
1418 MG MG    . MG    C .   ? 0.1863 0.1354 0.1476 -0.0266 -0.0205 -0.0423 202 MG    A MG    
1419 C  C1    . EDO   D .   ? 0.4324 0.3546 0.3657 -0.1054 0.0473  -0.0628 203 EDO   A C1    
1420 O  O1    . EDO   D .   ? 0.4113 0.3797 0.3180 -0.1238 0.0627  -0.0972 203 EDO   A O1    
1421 C  C2    . EDO   D .   ? 0.4292 0.3767 0.3176 -0.0770 0.0077  0.0302  203 EDO   A C2    
1422 O  O2    . EDO   D .   ? 0.3885 0.3607 0.2903 -0.1057 0.0111  -0.0393 203 EDO   A O2    
1423 C  C1    . EDO   E .   ? 0.2095 0.3053 0.3266 0.0055  0.0516  -0.0888 204 EDO   A C1    
1424 O  O1    . EDO   E .   ? 0.1338 0.3185 0.2884 0.0043  -0.0049 -0.0988 204 EDO   A O1    
1425 C  C2    . EDO   E .   ? 0.2317 0.2194 0.3263 0.0442  0.0171  -0.0571 204 EDO   A C2    
1426 O  O2    . EDO   E .   ? 0.3173 0.3521 0.2083 0.0083  0.0051  -0.0459 204 EDO   A O2    
1427 C  CBF   . A1IK9 F .   ? 0.4569 0.2808 0.3897 -0.0272 -0.0431 0.0181  205 A1IK9 A CBF   
1428 C  CBG   . A1IK9 F .   ? 0.4196 0.2708 0.4041 -0.0211 -0.0287 0.0061  205 A1IK9 A CBG   
1429 N  NBH   . A1IK9 F .   ? 0.4529 0.2887 0.3991 -0.0315 -0.0481 0.0219  205 A1IK9 A NBH   
1430 C  CBI   . A1IK9 F .   ? 0.3803 0.2832 0.3586 -0.0460 -0.0607 -0.0396 205 A1IK9 A CBI   
1431 C  CBJ   . A1IK9 F .   ? 0.3542 0.2741 0.3448 -0.0359 -0.0571 -0.0370 205 A1IK9 A CBJ   
1432 C  CBE   . A1IK9 F .   ? 0.3497 0.2863 0.3515 -0.0406 -0.0584 -0.0411 205 A1IK9 A CBE   
1433 N  NAC   . A1IK9 F .   ? 0.3374 0.2371 0.3742 0.0289  -0.0039 -0.0478 205 A1IK9 A NAC   
1434 C  CAD   . A1IK9 F .   ? 0.3767 0.2276 0.4075 0.0125  -0.0303 -0.0941 205 A1IK9 A CAD   
1435 C  CAE   . A1IK9 F .   ? 0.4362 0.3188 0.3731 0.0218  -0.0671 -0.0733 205 A1IK9 A CAE   
1436 O  OAF   . A1IK9 F .   ? 0.5188 0.4299 0.5168 0.0575  -0.0129 0.0771  205 A1IK9 A OAF   
1437 C  CAB   . A1IK9 F .   ? 0.3114 0.2752 0.3591 0.0145  -0.0176 -0.0995 205 A1IK9 A CAB   
1438 O  OAA   . A1IK9 F .   ? 0.3532 0.3080 0.4815 0.0715  -0.0377 -0.1482 205 A1IK9 A OAA   
1439 C  CAY   . A1IK9 F .   ? 0.2687 0.2444 0.3591 0.0375  -0.0392 -0.1242 205 A1IK9 A CAY   
1440 C  CAZ   . A1IK9 F .   ? 0.2891 0.2534 0.3254 0.0102  -0.0793 -0.1032 205 A1IK9 A CAZ   
1441 C  CAX   . A1IK9 F .   ? 0.2951 0.2478 0.2797 0.0160  -0.0352 -0.0874 205 A1IK9 A CAX   
1442 O  OAW   . A1IK9 F .   ? 0.3026 0.2537 0.3462 0.0039  -0.0235 -0.0840 205 A1IK9 A OAW   
1443 C  CBC   . A1IK9 F .   ? 0.2785 0.2335 0.3225 0.0419  0.0021  -0.1004 205 A1IK9 A CBC   
1444 C  CBB   . A1IK9 F .   ? 0.3092 0.2374 0.3264 0.0546  -0.0431 -0.1410 205 A1IK9 A CBB   
1445 C  CBA   . A1IK9 F .   ? 0.2668 0.2386 0.3364 0.0473  0.0030  -0.1259 205 A1IK9 A CBA   
1446 S  SAH   . A1IK9 F .   ? 0.2803 0.2808 0.2809 0.0563  -0.0242 -0.1242 205 A1IK9 A SAH   
1447 O  OAG   . A1IK9 F .   ? 0.2792 0.3402 0.2426 0.0470  0.0174  -0.0980 205 A1IK9 A OAG   
1448 O  OBD   . A1IK9 F .   ? 0.2990 0.3394 0.4068 0.0921  -0.0434 -0.1839 205 A1IK9 A OBD   
1449 N  NAI   . A1IK9 F .   ? 0.2895 0.2747 0.2744 0.0564  -0.0501 -0.1716 205 A1IK9 A NAI   
1450 C  CAJ   . A1IK9 F .   ? 0.3265 0.2038 0.2557 0.0497  -0.0475 -0.1248 205 A1IK9 A CAJ   
1451 S  SAK   . A1IK9 F .   ? 0.2503 0.2417 0.2375 0.0681  -0.0441 -0.1147 205 A1IK9 A SAK   
1452 C  CAL   . A1IK9 F .   ? 0.2444 0.2192 0.2071 0.0516  -0.0723 -0.1020 205 A1IK9 A CAL   
1453 C  CAM   . A1IK9 F .   ? 0.2290 0.2012 0.2111 0.0422  -0.0470 -0.0781 205 A1IK9 A CAM   
1454 CL CLAR  . A1IK9 F .   ? 0.2019 0.2168 0.2144 0.0599  -0.0513 -0.0843 205 A1IK9 A CLAR  
1455 C  CAN   . A1IK9 F .   ? 0.1694 0.2335 0.2141 0.0507  -0.0492 -0.0883 205 A1IK9 A CAN   
1456 C  CAO   . A1IK9 F .   ? 0.2795 0.2221 0.1972 0.0440  -0.0685 -0.0957 205 A1IK9 A CAO   
1457 C  CAP   . A1IK9 F .   ? 0.2769 0.2059 0.2614 0.0479  -0.0464 -0.0511 205 A1IK9 A CAP   
1458 O  OAQ   . A1IK9 F .   ? 0.3832 0.2104 0.2760 0.0471  0.0038  -0.0943 205 A1IK9 A OAQ   
1459 C  CAS   . A1IK9 F .   ? 0.2998 0.1801 0.2818 0.0402  -0.0411 -0.0913 205 A1IK9 A CAS   
1460 N  NAV   . A1IK9 F .   ? 0.3897 0.2133 0.2690 0.1096  -0.0262 -0.0651 205 A1IK9 A NAV   
1461 C  CAU   . A1IK9 F .   ? 0.4190 0.2478 0.2645 0.0655  0.0052  -0.0604 205 A1IK9 A CAU   
1462 C  CAT   . A1IK9 F .   ? 0.4633 0.3079 0.3123 0.0325  0.0240  -0.0919 205 A1IK9 A CAT   
1463 O  O     . HOH   G .   ? 0.6604 0.3744 0.1900 -0.1016 -0.0338 -0.0730 301 HOH   A O     
1464 O  O     . HOH   G .   ? 0.3534 0.6405 0.2347 -0.0219 -0.0398 0.1049  302 HOH   A O     
1465 O  O     . HOH   G .   ? 0.2320 0.2627 0.3134 -0.0182 0.0531  0.0695  303 HOH   A O     
1466 O  O     . HOH   G .   ? 0.1685 0.2472 0.1700 0.0052  0.0001  -0.0527 304 HOH   A O     
1467 O  O     . HOH   G .   ? 0.1956 0.2499 0.2425 -0.0092 -0.0427 -0.0780 305 HOH   A O     
1468 O  O     . HOH   G .   ? 0.4049 0.2315 0.2543 -0.0580 -0.0473 -0.0443 306 HOH   A O     
1469 O  O     . HOH   G .   ? 0.2509 0.1478 0.1872 -0.0527 -0.0059 -0.0234 307 HOH   A O     
1470 O  O     . HOH   G .   ? 0.5540 0.3076 0.4179 0.0060  -0.0821 -0.1697 308 HOH   A O     
1471 O  O     . HOH   G .   ? 0.1922 0.4472 0.3990 -0.0476 0.0197  -0.0088 309 HOH   A O     
1472 O  O     . HOH   G .   ? 0.3937 0.2973 0.5447 -0.0103 0.0125  -0.0483 310 HOH   A O     
1473 O  O     . HOH   G .   ? 0.1937 0.1853 0.1582 -0.0306 -0.0264 -0.0385 311 HOH   A O     
1474 O  O     . HOH   G .   ? 0.4895 0.5343 0.3345 0.0207  0.0742  0.0090  312 HOH   A O     
1475 O  O     . HOH   G .   ? 0.3173 0.4564 0.2828 0.0688  0.0205  -0.0015 313 HOH   A O     
1476 O  O     . HOH   G .   ? 0.5917 0.3163 0.3012 0.0899  -0.1080 0.0030  314 HOH   A O     
1477 O  O     . HOH   G .   ? 0.4871 0.7144 0.3369 -0.2529 -0.0257 -0.0525 315 HOH   A O     
1478 O  O     . HOH   G .   ? 0.1755 0.2958 0.1769 -0.0274 -0.0195 0.0081  316 HOH   A O     
1479 O  O     . HOH   G .   ? 0.3011 0.3626 0.2625 0.0655  0.0425  0.0373  317 HOH   A O     
1480 O  O     . HOH   G .   ? 0.1457 0.1504 0.1540 -0.0127 0.0176  -0.0096 318 HOH   A O     
1481 O  O     . HOH   G .   ? 0.4263 0.3372 0.2311 0.0891  0.0127  -0.0129 319 HOH   A O     
1482 O  O     . HOH   G .   ? 0.3007 0.2340 0.2883 0.0773  -0.0709 -0.0733 320 HOH   A O     
1483 O  O     . HOH   G .   ? 0.6273 0.2821 0.2543 0.0834  -0.0007 -0.0032 321 HOH   A O     
1484 O  O     . HOH   G .   ? 0.7717 0.2670 0.3144 0.0671  -0.0915 -0.0802 322 HOH   A O     
1485 O  O     . HOH   G .   ? 0.2802 0.3235 0.2057 -0.0594 0.0032  -0.0051 323 HOH   A O     
1486 O  O     . HOH   G .   ? 0.9196 0.3286 0.2900 -0.0889 -0.0201 0.0049  324 HOH   A O     
1487 O  O     . HOH   G .   ? 0.6088 0.2012 0.3523 0.0380  -0.0340 -0.0146 325 HOH   A O     
1488 O  O     . HOH   G .   ? 0.1673 0.4747 0.1868 0.0260  -0.0013 0.1025  326 HOH   A O     
1489 O  O     . HOH   G .   ? 0.3708 0.7043 0.3017 -0.0364 -0.0758 0.0611  327 HOH   A O     
1490 O  O     . HOH   G .   ? 0.3721 0.1811 0.1710 -0.1032 -0.0496 0.0278  328 HOH   A O     
1491 O  O     . HOH   G .   ? 0.3102 0.5475 0.3526 0.0384  -0.0142 -0.0743 329 HOH   A O     
1492 O  O     . HOH   G .   ? 0.4625 0.5919 0.3567 0.1704  0.0788  0.1307  330 HOH   A O     
1493 O  O     . HOH   G .   ? 0.2909 0.2593 0.1863 -0.0151 -0.0608 -0.0435 331 HOH   A O     
1494 O  O     . HOH   G .   ? 0.1505 0.3419 0.2034 -0.0027 -0.0113 -0.0585 332 HOH   A O     
1495 O  O     . HOH   G .   ? 0.2575 0.3801 0.2778 -0.0882 -0.1051 0.0164  333 HOH   A O     
1496 O  O     . HOH   G .   ? 0.2885 0.1872 0.2480 0.0156  -0.0284 -0.0230 334 HOH   A O     
1497 O  O     . HOH   G .   ? 0.4050 0.1721 0.2661 -0.0402 0.0835  -0.0153 335 HOH   A O     
1498 O  O     . HOH   G .   ? 0.4219 1.0643 0.4234 0.3624  0.0471  0.0340  336 HOH   A O     
1499 O  O     . HOH   G .   ? 0.3184 0.4041 0.3908 -0.0674 0.0379  0.0407  337 HOH   A O     
1500 O  O     . HOH   G .   ? 0.3381 0.3869 0.3713 0.0974  -0.0613 -0.0462 338 HOH   A O     
1501 O  O     . HOH   G .   ? 0.4643 0.3017 0.3638 -0.0470 0.1082  -0.0275 339 HOH   A O     
1502 O  O     . HOH   G .   ? 0.2416 0.1928 0.1856 -0.0310 -0.0243 -0.0612 340 HOH   A O     
1503 O  O     . HOH   G .   ? 0.1487 0.2699 0.1284 -0.0283 -0.0066 -0.0543 341 HOH   A O     
1504 O  O     . HOH   G .   ? 0.2476 0.2862 0.1880 0.0335  0.0045  -0.0254 342 HOH   A O     
1505 O  O     . HOH   G .   ? 0.3839 0.5688 0.5576 -0.0603 0.0227  0.1667  343 HOH   A O     
1506 O  O     . HOH   G .   ? 0.2942 0.7209 0.3902 -0.0391 0.0836  -0.0263 344 HOH   A O     
1507 O  O     . HOH   G .   ? 0.2569 0.2677 0.2819 -0.0831 0.0119  -0.1307 345 HOH   A O     
1508 O  O     . HOH   G .   ? 0.3048 0.5485 0.3549 0.1167  -0.0407 -0.2246 346 HOH   A O     
1509 O  O     . HOH   G .   ? 0.2826 0.1787 0.1636 -0.0008 -0.0103 -0.0626 347 HOH   A O     
1510 O  O     . HOH   G .   ? 0.3823 0.2244 0.2477 -0.0232 -0.0359 0.0378  348 HOH   A O     
1511 O  O     . HOH   G .   ? 0.1480 0.1968 0.1108 0.0316  -0.0131 -0.0421 349 HOH   A O     
1512 O  O     . HOH   G .   ? 0.2078 0.3840 0.1393 -0.0415 0.0010  -0.0053 350 HOH   A O     
1513 O  O     . HOH   G .   ? 0.2150 0.2672 0.3014 -0.0075 0.0107  -0.1554 351 HOH   A O     
1514 O  O     . HOH   G .   ? 0.1432 0.3233 0.2435 -0.0023 0.0382  -0.0583 352 HOH   A O     
1515 O  O     . HOH   G .   ? 0.2478 0.1318 0.1288 0.0034  0.0388  -0.0199 353 HOH   A O     
1516 O  O     . HOH   G .   ? 0.3016 0.2179 0.3461 -0.0239 -0.0282 -0.0425 354 HOH   A O     
1517 O  O     . HOH   G .   ? 0.8942 0.3221 0.3705 0.2066  0.0411  0.0208  355 HOH   A O     
1518 O  O     . HOH   G .   ? 0.3485 0.3304 0.4533 -0.0062 0.0542  -0.1453 356 HOH   A O     
1519 O  O     . HOH   G .   ? 0.2957 0.6705 0.1870 0.0401  0.0014  0.0458  357 HOH   A O     
1520 O  O     . HOH   G .   ? 0.1548 0.2560 0.1202 -0.0117 0.0313  -0.0431 358 HOH   A O     
1521 O  O     . HOH   G .   ? 0.6646 0.4929 0.4526 0.1255  0.0707  -0.0972 359 HOH   A O     
1522 O  O     . HOH   G .   ? 0.2987 0.4151 0.3808 -0.0645 -0.1399 -0.0236 360 HOH   A O     
1523 O  O     . HOH   G .   ? 0.2076 0.2677 0.1858 -0.0145 0.0059  -0.0009 361 HOH   A O     
1524 O  O     . HOH   G .   ? 0.3278 0.4440 0.3252 -0.0076 -0.0108 -0.0280 362 HOH   A O     
1525 O  O     . HOH   G .   ? 0.3565 0.6255 0.5534 0.1260  0.0016  -0.0194 363 HOH   A O     
1526 O  O     . HOH   G .   ? 0.3047 0.3201 0.2833 -0.0275 -0.0934 -0.0028 364 HOH   A O     
1527 O  O     . HOH   G .   ? 0.2038 0.2617 0.3130 -0.0072 0.0467  -0.0579 365 HOH   A O     
1528 O  O     . HOH   G .   ? 0.4393 0.2815 0.2609 0.0343  -0.0671 0.0157  366 HOH   A O     
1529 O  O     . HOH   G .   ? 0.7047 0.2968 0.3756 0.0637  0.0441  -0.0296 367 HOH   A O     
1530 O  O     . HOH   G .   ? 0.3380 0.6906 0.2553 -0.0311 0.0952  0.0085  368 HOH   A O     
1531 O  O     . HOH   G .   ? 0.4070 0.6308 0.4852 -0.0338 -0.0421 0.1321  369 HOH   A O     
1532 O  O     . HOH   G .   ? 0.3060 0.2743 0.6095 -0.0576 0.0880  -0.0848 370 HOH   A O     
1533 O  O     . HOH   G .   ? 0.5230 0.7467 0.5508 -0.2280 0.0567  -0.1886 371 HOH   A O     
1534 O  O     . HOH   G .   ? 0.4272 0.4980 0.3347 0.0520  0.0000  -0.1496 372 HOH   A O     
1535 O  O     . HOH   G .   ? 0.2338 0.2173 0.1433 -0.0092 0.0188  0.0268  373 HOH   A O     
1536 O  O     . HOH   G .   ? 0.4427 0.5229 0.3966 0.0679  -0.0138 0.1440  374 HOH   A O     
1537 O  O     . HOH   G .   ? 0.1438 0.1939 0.1043 0.0134  -0.0218 -0.0420 375 HOH   A O     
1538 O  O     . HOH   G .   ? 0.1291 0.4895 0.2798 0.0178  0.0090  0.1216  376 HOH   A O     
1539 O  O     . HOH   G .   ? 0.6663 0.6189 0.3069 -0.1367 -0.0004 0.0063  377 HOH   A O     
1540 O  O     . HOH   G .   ? 0.4817 0.3720 0.4652 -0.0112 -0.0295 -0.1438 378 HOH   A O     
1541 O  O     . HOH   G .   ? 0.3882 0.3440 0.6994 0.0495  -0.0335 -0.1075 379 HOH   A O     
1542 O  O     . HOH   G .   ? 0.3874 0.3259 0.2621 -0.0863 -0.0040 -0.0137 380 HOH   A O     
1543 O  O     . HOH   G .   ? 0.5325 0.6313 0.2882 0.0806  0.1646  0.0289  381 HOH   A O     
1544 O  O     . HOH   G .   ? 0.2345 0.2958 0.1303 0.0218  -0.0085 -0.0235 382 HOH   A O     
1545 O  O     . HOH   G .   ? 0.1822 0.3593 0.1769 -0.0464 -0.0212 -0.0263 383 HOH   A O     
1546 O  O     . HOH   G .   ? 0.1175 0.2402 0.1518 -0.0152 0.0060  -0.0370 384 HOH   A O     
1547 O  O     . HOH   G .   ? 0.3940 0.3420 0.5051 -0.1063 -0.1419 -0.0445 385 HOH   A O     
1548 O  O     . HOH   G .   ? 0.1747 0.1774 0.2127 -0.0178 -0.0608 0.0105  386 HOH   A O     
1549 O  O     . HOH   G .   ? 0.2820 0.4868 0.4910 -0.0344 -0.0981 0.0599  387 HOH   A O     
1550 O  O     . HOH   G .   ? 0.2761 0.5665 0.3064 0.0297  -0.0312 0.1022  388 HOH   A O     
1551 O  O     . HOH   G .   ? 0.4075 0.7652 0.2433 -0.0397 -0.1099 0.0930  389 HOH   A O     
1552 O  O     . HOH   G .   ? 0.4428 0.2971 0.2341 -0.0470 0.0384  -0.0296 390 HOH   A O     
1553 O  O     . HOH   G .   ? 0.5280 0.3154 0.4483 -0.0520 0.0100  0.0594  391 HOH   A O     
1554 O  O     . HOH   G .   ? 0.2031 0.1852 0.3248 0.0210  -0.1133 -0.0344 392 HOH   A O     
1555 O  O     . HOH   G .   ? 0.6060 0.4264 0.4887 -0.1365 0.0561  -0.0586 393 HOH   A O     
1556 O  O     . HOH   G .   ? 0.5495 0.5234 0.6759 -0.2048 -0.2969 0.1276  394 HOH   A O     
1557 O  O     . HOH   G .   ? 0.3071 0.4121 0.4464 -0.0911 0.1151  -0.0790 395 HOH   A O     
1558 O  O     . HOH   G .   ? 0.4183 0.2874 0.4479 0.0277  -0.0707 -0.1254 396 HOH   A O     
1559 O  O     . HOH   G .   ? 0.5391 0.3623 0.2607 0.1071  -0.0340 -0.0752 397 HOH   A O     
1560 O  O     . HOH   G .   ? 0.1888 0.3752 0.4982 -0.0137 -0.0855 0.0703  398 HOH   A O     
1561 O  O     . HOH   G .   ? 0.8542 0.6450 0.6496 -0.2790 0.2591  -0.2023 399 HOH   A O     
1562 O  O     . HOH   G .   ? 0.4712 0.9138 0.3675 -0.2248 -0.0099 0.0631  400 HOH   A O     
1563 O  O     . HOH   G .   ? 0.2767 0.4997 0.4181 0.1483  -0.0516 -0.0367 401 HOH   A O     
1564 O  O     . HOH   G .   ? 0.1986 0.3072 0.1523 0.0218  0.0190  0.0354  402 HOH   A O     
1565 O  O     . HOH   G .   ? 0.8203 0.2585 0.4631 -0.1621 -0.0165 -0.0241 403 HOH   A O     
1566 O  O     . HOH   G .   ? 0.2060 0.2722 0.4103 -0.0763 0.0385  -0.0142 404 HOH   A O     
1567 O  O     . HOH   G .   ? 0.4955 0.4514 0.3033 0.1240  0.0556  0.0304  405 HOH   A O     
1568 O  O     . HOH   G .   ? 0.1542 0.1905 0.2710 -0.0025 0.0470  -0.0906 406 HOH   A O     
1569 O  O     . HOH   G .   ? 0.4194 0.6176 0.5332 -0.1795 0.0123  -0.1948 407 HOH   A O     
1570 O  O     . HOH   G .   ? 0.3570 0.2745 0.3438 0.0314  -0.0508 -0.0271 408 HOH   A O     
1571 O  O     . HOH   G .   ? 0.2206 0.3048 0.2104 0.0273  -0.0208 -0.0355 409 HOH   A O     
1572 O  O     . HOH   G .   ? 0.7094 0.7706 0.6808 -0.0428 -0.0839 0.2173  410 HOH   A O     
1573 O  O     . HOH   G .   ? 0.1930 0.3384 0.3208 0.0179  0.0599  -0.0401 411 HOH   A O     
1574 O  O     . HOH   G .   ? 0.3317 0.1874 0.3707 0.0358  -0.0263 -0.0702 412 HOH   A O     
1575 O  O     . HOH   G .   ? 0.4769 0.4202 0.2084 0.0228  -0.0085 -0.1052 413 HOH   A O     
1576 O  O     . HOH   G .   ? 0.2788 0.2879 0.2724 -0.0811 0.0059  -0.0750 414 HOH   A O     
1577 O  O     . HOH   G .   ? 0.3017 0.2538 0.3347 0.0334  -0.0141 -0.0598 415 HOH   A O     
1578 O  O     . HOH   G .   ? 0.4333 0.3180 0.2979 0.0535  -0.0348 0.0335  416 HOH   A O     
1579 O  O     . HOH   G .   ? 0.3404 0.5789 0.5331 0.0005  -0.2048 0.0566  417 HOH   A O     
1580 O  O     . HOH   G .   ? 0.3936 0.4886 0.3646 -0.0379 -0.0831 -0.1501 418 HOH   A O     
1581 O  O     . HOH   G .   ? 0.3448 0.5108 0.3570 0.0267  -0.0855 0.0621  419 HOH   A O     
1582 O  O     . HOH   G .   ? 0.2525 0.3800 0.1945 0.0720  -0.0202 -0.0725 420 HOH   A O     
1583 O  O     . HOH   G .   ? 0.2312 0.5353 0.1718 -0.0453 -0.0173 -0.0867 421 HOH   A O     
1584 O  O     . HOH   G .   ? 0.1302 0.1969 0.1210 0.0081  0.0330  0.0197  422 HOH   A O     
1585 O  O     . HOH   G .   ? 0.1346 0.1929 0.2107 -0.0248 -0.0514 0.0461  423 HOH   A O     
1586 O  O     . HOH   G .   ? 0.5225 0.5945 0.2908 -0.0839 -0.0415 0.1110  424 HOH   A O     
1587 O  O     . HOH   G .   ? 0.5018 0.5734 0.3111 0.2278  -0.0568 -0.0346 425 HOH   A O     
1588 O  O     . HOH   G .   ? 0.3291 0.6234 0.7456 -0.0762 -0.1062 0.3299  426 HOH   A O     
1589 O  O     . HOH   G .   ? 0.5991 0.3195 0.3442 -0.2179 -0.0545 0.0081  427 HOH   A O     
1590 O  O     . HOH   G .   ? 0.3009 0.3509 0.2493 0.0293  0.0662  0.0388  428 HOH   A O     
1591 O  O     . HOH   G .   ? 0.4614 0.3878 0.3480 -0.1360 0.1410  -0.1520 429 HOH   A O     
1592 O  O     . HOH   G .   ? 0.6564 0.4647 0.4939 0.0204  0.1234  -0.1871 430 HOH   A O     
1593 O  O     . HOH   G .   ? 0.5941 0.7286 0.3946 0.0152  -0.1371 -0.3696 431 HOH   A O     
1594 O  O     . HOH   G .   ? 0.2740 0.5507 0.2743 -0.0222 0.0065  -0.0050 432 HOH   A O     
1595 O  O     . HOH   G .   ? 0.6908 0.5859 0.3467 -0.1352 -0.1166 -0.0950 433 HOH   A O     
1596 O  O     . HOH   G .   ? 0.5353 0.3784 0.2796 -0.1340 -0.0077 -0.0142 434 HOH   A O     
1597 O  O     . HOH   G .   ? 0.4239 0.2818 0.4503 -0.0610 0.1565  -0.0710 435 HOH   A O     
1598 O  O     . HOH   G .   ? 0.3536 0.4415 0.3863 -0.0012 0.0169  -0.0076 436 HOH   A O     
# 
